CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 2404121838403870988

Job options:

ID        	=	 2404121838403870988
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   3      26.244   2.633 -18.736  1.00 59.04           N  
ANISOU    1  N   PRO A   3     7219   7880   7330    155   -165    373       N  
ATOM      2  CA  PRO A   3      26.062   3.272 -17.428  1.00 58.90           C  
ANISOU    2  CA  PRO A   3     7209   7809   7361    140   -145    371       C  
ATOM      3  C   PRO A   3      26.649   2.426 -16.307  1.00 55.91           C  
ANISOU    3  C   PRO A   3     6852   7407   6984    122   -135    332       C  
ATOM      4  O   PRO A   3      26.680   1.190 -16.410  1.00 57.88           O  
ANISOU    4  O   PRO A   3     7107   7674   7210    120   -146    299       O  
ATOM      5  CB  PRO A   3      24.544   3.293 -17.259  1.00 55.60           C  
ANISOU    5  CB  PRO A   3     6776   7378   6970    143   -154    363       C  
ATOM      6  CG  PRO A   3      24.116   2.060 -17.972  1.00 57.98           C  
ANISOU    6  CG  PRO A   3     7073   7717   7239    150   -177    335       C  
ATOM      7  CD  PRO A   3      24.990   2.033 -19.213  1.00 59.84           C  
ANISOU    7  CD  PRO A   3     7307   8001   7428    163   -187    356       C  
ATOM      8  N   LYS A   4      27.091   3.110 -15.250  1.00 50.29           N  
ANISOU    8  N   LYS A   4     6150   6654   6301    109   -115    335       N  
ATOM      9  CA  LYS A   4      27.602   2.518 -13.998  1.00 44.45           C  
ANISOU    9  CA  LYS A   4     5432   5887   5569     91   -103    303       C  
ATOM     10  C   LYS A   4      26.688   1.442 -13.378  1.00 39.73           C  
ANISOU   10  C   LYS A   4     4838   5279   4977     86   -108    264       C  
ATOM     11  O   LYS A   4      25.498   1.600 -13.403  1.00 42.03           O  
ANISOU   11  O   LYS A   4     5118   5563   5289     90   -111    264       O  
ATOM     12  CB  LYS A   4      27.682   3.652 -12.999  1.00 42.43           C  
ANISOU   12  CB  LYS A   4     5181   5588   5353     82    -83    314       C  
ATOM     13  CG  LYS A   4      28.908   3.632 -12.103  1.00 45.17           C  
ANISOU   13  CG  LYS A   4     5547   5916   5699     67    -71    302       C  
ATOM     14  CD  LYS A   4      29.010   4.968 -11.370  1.00 43.52           C  
ANISOU   14  CD  LYS A   4     5337   5668   5527     60    -53    318       C  
ATOM     15  CE  LYS A   4      28.797   6.163 -12.305  1.00 46.09           C  
ANISOU   15  CE  LYS A   4     5643   6000   5869     72    -51    361       C  
ATOM     16  NZ  LYS A   4      29.193   7.580 -11.885  1.00 42.52           N  
ANISOU   16  NZ  LYS A   4     5186   5513   5455     67    -33    384       N  
ATOM     17  N   ALA A   5      27.239   0.386 -12.792  1.00 36.23           N  
ANISOU   17  N   ALA A   5     4411   4833   4519     76   -106    234       N  
ATOM     18  CA  ALA A   5      26.478  -0.562 -11.913  1.00 35.60           C  
ANISOU   18  CA  ALA A   5     4338   4733   4453     68   -104    199       C  
ATOM     19  C   ALA A   5      25.610   0.160 -10.835  1.00 32.45           C  
ANISOU   19  C   ALA A   5     3942   4292   4095     61    -87    199       C  
ATOM     20  O   ALA A   5      26.019   1.198 -10.331  1.00 32.06           O  
ANISOU   20  O   ALA A   5     3897   4221   4061     56    -74    215       O  
ATOM     21  CB  ALA A   5      27.429  -1.587 -11.254  1.00 31.31           C  
ANISOU   21  CB  ALA A   5     3815   4187   3893     57   -100    174       C  
ATOM     22  N   LYS A   6      24.391  -0.345 -10.594  1.00 30.73           N  
ANISOU   22  N   LYS A   6     3716   4064   3894     61    -89    182       N  
ATOM     23  CA  LYS A   6      23.545   0.081  -9.488  1.00 28.39           C  
ANISOU   23  CA  LYS A   6     3423   3728   3635     54    -70    175       C  
ATOM     24  C   LYS A   6      23.421  -1.104  -8.556  1.00 27.87           C  
ANISOU   24  C   LYS A   6     3372   3648   3568     44    -63    142       C  
ATOM     25  O   LYS A   6      22.997  -2.154  -8.955  1.00 28.87           O  
ANISOU   25  O   LYS A   6     3491   3789   3686     47    -74    125       O  
ATOM     26  CB  LYS A   6      22.166   0.552  -9.984  1.00 28.44           C  
ANISOU   26  CB  LYS A   6     3405   3732   3668     63    -76    186       C  
ATOM     27  CG  LYS A   6      21.068   0.660  -8.908  1.00 26.40           C  
ANISOU   27  CG  LYS A   6     3147   3435   3449     57    -57    172       C  
ATOM     28  CD  LYS A   6      19.745   1.174  -9.473  1.00 28.02           C  
ANISOU   28  CD  LYS A   6     3324   3638   3682     68    -63    185       C  
ATOM     29  CE  LYS A   6      18.828   1.725  -8.375  1.00 28.51           C  
ANISOU   29  CE  LYS A   6     3387   3657   3788     62    -39    180       C  
ATOM     30  NZ  LYS A   6      17.546   2.185  -8.937  1.00 30.30           N  
ANISOU   30  NZ  LYS A   6     3584   3881   4045     72    -46    193       N  
ATOM     31  N   ILE A   7      23.868  -0.944  -7.331  1.00 27.44           N  
ANISOU   31  N   ILE A   7     3339   3567   3520     33    -44    134       N  
ATOM     32  CA  ILE A   7      23.865  -2.002  -6.404  1.00 25.94           C  
ANISOU   32  CA  ILE A   7     3164   3364   3327     24    -35    108       C  
ATOM     33  C   ILE A   7      22.807  -1.635  -5.360  1.00 25.44           C  
ANISOU   33  C   ILE A   7     3103   3264   3296     19    -14    101       C  
ATOM     34  O   ILE A   7      22.945  -0.614  -4.677  1.00 24.72           O  
ANISOU   34  O   ILE A   7     3021   3152   3219     15      0    109       O  
ATOM     35  CB  ILE A   7      25.232  -2.028  -5.759  1.00 26.98           C  
ANISOU   35  CB  ILE A   7     3319   3493   3438     16    -30    106       C  
ATOM     36  CG1 ILE A   7      26.209  -2.636  -6.732  1.00 28.13           C  
ANISOU   36  CG1 ILE A   7     3461   3672   3551     20    -49    108       C  
ATOM     37  CG2 ILE A   7      25.268  -2.869  -4.485  1.00 26.97           C  
ANISOU   37  CG2 ILE A   7     3338   3472   3435      6    -16     83       C  
ATOM     38  CD1 ILE A   7      27.595  -2.024  -6.647  1.00 27.16           C  
ANISOU   38  CD1 ILE A   7     3351   3555   3414     16    -49    121       C  
ATOM     39  N   VAL A   8      21.801  -2.482  -5.178  1.00 23.26           N  
ANISOU   39  N   VAL A   8     2820   2981   3035     20    -11     84       N  
ATOM     40  CA  VAL A   8      20.856  -2.296  -4.047  1.00 21.79           C  
ANISOU   40  CA  VAL A   8     2639   2760   2879     14     13     75       C  
ATOM     41  C   VAL A   8      21.130  -3.114  -2.777  1.00 21.35           C  
ANISOU   41  C   VAL A   8     2608   2687   2816      5     31     56       C  
ATOM     42  O   VAL A   8      21.137  -4.417  -2.759  1.00 20.71           O  
ANISOU   42  O   VAL A   8     2529   2613   2726      4     27     41       O  
ATOM     43  CB  VAL A   8      19.378  -2.532  -4.513  1.00 22.01           C  
ANISOU   43  CB  VAL A   8     2640   2783   2937     21     10     71       C  
ATOM     44  CG1 VAL A   8      18.378  -2.181  -3.455  1.00 19.94           C  
ANISOU   44  CG1 VAL A   8     2379   2485   2709     17     37     65       C  
ATOM     45  CG2 VAL A   8      19.044  -1.681  -5.758  1.00 21.55           C  
ANISOU   45  CG2 VAL A   8     2557   2744   2886     32     -8     93       C  
ATOM     46  N   LEU A   9      21.238  -2.406  -1.683  1.00 20.78           N  
ANISOU   46  N   LEU A   9     2554   2591   2751     -1     52     55       N  
ATOM     47  CA  LEU A   9      21.363  -3.106  -0.397  1.00 21.93           C  
ANISOU   47  CA  LEU A   9     2723   2720   2889     -8     71     40       C  
ATOM     48  C   LEU A   9      20.025  -3.248   0.347  1.00 24.00           C  
ANISOU   48  C   LEU A   9     2981   2955   3182     -9     96     30       C  
ATOM     49  O   LEU A   9      19.526  -2.276   0.929  1.00 23.54           O  
ANISOU   49  O   LEU A   9     2924   2874   3143    -10    115     33       O  
ATOM     50  CB  LEU A   9      22.419  -2.431   0.443  1.00 21.35           C  
ANISOU   50  CB  LEU A   9     2674   2640   2796    -15     79     41       C  
ATOM     51  CG  LEU A   9      23.685  -2.103  -0.381  1.00 21.77           C  
ANISOU   51  CG  LEU A   9     2726   2718   2826    -14     56     53       C  
ATOM     52  CD1 LEU A   9      24.609  -1.241   0.405  1.00 22.07           C  
ANISOU   52  CD1 LEU A   9     2784   2746   2855    -21     63     53       C  
ATOM     53  CD2 LEU A   9      24.434  -3.360  -0.746  1.00 21.81           C  
ANISOU   53  CD2 LEU A   9     2736   2746   2805    -14     40     47       C  
ATOM     54  N   VAL A  10      19.408  -4.451   0.288  1.00 24.37           N  
ANISOU   54  N   VAL A  10     3020   3001   3237     -8     97     20       N  
ATOM     55  CA  VAL A  10      18.120  -4.669   0.977  1.00 24.12           C  
ANISOU   55  CA  VAL A  10     2983   2943   3238     -9    122     12       C  
ATOM     56  C   VAL A  10      18.416  -5.010   2.442  1.00 24.10           C  
ANISOU   56  C   VAL A  10     3010   2922   3221    -15    149      4       C  
ATOM     57  O   VAL A  10      18.711  -6.173   2.746  1.00 22.85           O  
ANISOU   57  O   VAL A  10     2861   2768   3050    -17    150     -2       O  
ATOM     58  CB  VAL A  10      17.278  -5.763   0.305  1.00 24.55           C  
ANISOU   58  CB  VAL A  10     3013   3002   3312     -5    113      4       C  
ATOM     59  CG1 VAL A  10      15.975  -6.019   1.070  1.00 24.09           C  
ANISOU   59  CG1 VAL A  10     2948   2913   3291     -6    142     -3       C  
ATOM     60  CG2 VAL A  10      16.944  -5.342  -1.144  1.00 24.48           C  
ANISOU   60  CG2 VAL A  10     2974   3014   3313      2     85     12       C  
ATOM     61  N   GLY A  11      18.332  -4.000   3.322  1.00 24.18           N  
ANISOU   61  N   GLY A  11     3036   2915   3236    -18    170      5       N  
ATOM     62  CA  GLY A  11      18.712  -4.173   4.743  1.00 26.42           C  
ANISOU   62  CA  GLY A  11     3351   3186   3500    -24    194     -2       C  
ATOM     63  C   GLY A  11      19.851  -3.184   4.946  1.00 28.22           C  
ANISOU   63  C   GLY A  11     3597   3422   3703    -28    185      0       C  
ATOM     64  O   GLY A  11      20.942  -3.402   4.392  1.00 30.42           O  
ANISOU   64  O   GLY A  11     3878   3723   3956    -28    160      4       O  
ATOM     65  N   SER A  12      19.590  -2.074   5.649  1.00 25.76           N  
ANISOU   65  N   SER A  12     3293   3091   3401    -30    205     -3       N  
ATOM     66  CA  SER A  12      20.622  -1.061   5.876  1.00 25.66           C  
ANISOU   66  CA  SER A  12     3295   3083   3372    -35    197     -3       C  
ATOM     67  C   SER A  12      21.116  -1.126   7.372  1.00 24.88           C  
ANISOU   67  C   SER A  12     3231   2977   3245    -41    216    -17       C  
ATOM     68  O   SER A  12      21.319  -0.064   8.000  1.00 25.57           O  
ANISOU   68  O   SER A  12     3329   3052   3332    -45    227    -26       O  
ATOM     69  CB  SER A  12      20.067   0.322   5.577  1.00 24.65           C  
ANISOU   69  CB  SER A  12     3151   2938   3275    -33    204      0       C  
ATOM     70  OG  SER A  12      19.504   0.359   4.220  1.00 27.29           O  
ANISOU   70  OG  SER A  12     3452   3280   3634    -26    186     15       O  
ATOM     71  N   GLY A  13      21.294  -2.314   7.911  1.00 22.77           N  
ANISOU   71  N   GLY A  13     2978   2716   2955    -41    220    -20       N  
ATOM     72  CA  GLY A  13      21.849  -2.434   9.297  1.00 25.95           C  
ANISOU   72  CA  GLY A  13     3415   3118   3325    -45    235    -31       C  
ATOM     73  C   GLY A  13      23.366  -2.458   9.161  1.00 26.22           C  
ANISOU   73  C   GLY A  13     3462   3174   3327    -49    207    -29       C  
ATOM     74  O   GLY A  13      23.870  -2.064   8.104  1.00 26.95           O  
ANISOU   74  O   GLY A  13     3536   3276   3425    -49    183    -21       O  
ATOM     75  N   MET A  14      24.078  -2.980  10.142  1.00 25.78           N  
ANISOU   75  N   MET A  14     3433   3126   3236    -51    208    -34       N  
ATOM     76  CA  MET A  14      25.516  -2.819  10.231  1.00 28.51           C  
ANISOU   76  CA  MET A  14     3791   3489   3551    -55    184    -36       C  
ATOM     77  C   MET A  14      26.303  -3.365   9.035  1.00 29.09           C  
ANISOU   77  C   MET A  14     3847   3582   3622    -54    154    -23       C  
ATOM     78  O   MET A  14      27.225  -2.703   8.539  1.00 31.46           O  
ANISOU   78  O   MET A  14     4142   3892   3918    -57    133    -21       O  
ATOM     79  CB  MET A  14      26.006  -3.490  11.517  1.00 31.03           C  
ANISOU   79  CB  MET A  14     4142   3815   3833    -56    192    -41       C  
ATOM     80  CG  MET A  14      25.271  -3.053  12.788  1.00 32.30           C  
ANISOU   80  CG  MET A  14     4323   3960   3989    -57    224    -55       C  
ATOM     81  SD  MET A  14      25.147  -1.245  12.786  1.00 48.48           S  
ANISOU   81  SD  MET A  14     6367   5994   6060    -62    229    -71       S  
ATOM     82  CE  MET A  14      26.810  -0.750  13.172  1.00 36.92           C  
ANISOU   82  CE  MET A  14     4919   4546   4560    -70    200    -80       C  
ATOM     83  N   ILE A  15      25.985  -4.579   8.611  1.00 26.48           N  
ANISOU   83  N   ILE A  15     3508   3257   3294    -49    152    -15       N  
ATOM     84  CA  ILE A  15      26.628  -5.156   7.444  1.00 27.53           C  
ANISOU   84  CA  ILE A  15     3624   3409   3426    -46    126     -6       C  
ATOM     85  C   ILE A  15      26.357  -4.268   6.275  1.00 27.48           C  
ANISOU   85  C   ILE A  15     3592   3403   3443    -45    115     -1       C  
ATOM     86  O   ILE A  15      27.236  -4.031   5.446  1.00 29.74           O  
ANISOU   86  O   ILE A  15     3869   3706   3723    -45     93      5       O  
ATOM     87  CB  ILE A  15      26.095  -6.581   7.121  1.00 26.29           C  
ANISOU   87  CB  ILE A  15     3458   3254   3276    -41    129     -2       C  
ATOM     88  CG1 ILE A  15      26.228  -7.459   8.380  1.00 23.84           C  
ANISOU   88  CG1 ILE A  15     3172   2939   2945    -41    144     -3       C  
ATOM     89  CG2 ILE A  15      26.753  -7.141   5.847  1.00 23.98           C  
ANISOU   89  CG2 ILE A  15     3146   2981   2981    -38    102      3       C  
ATOM     90  CD1 ILE A  15      25.812  -8.943   8.257  1.00 22.75           C  
ANISOU   90  CD1 ILE A  15     3027   2799   2815    -37    150      0       C  
ATOM     91  N   GLY A  16      25.132  -3.768   6.201  1.00 26.96           N  
ANISOU   91  N   GLY A  16     3515   3321   3406    -43    132     -2       N  
ATOM     92  CA  GLY A  16      24.733  -2.950   5.036  1.00 24.67           C  
ANISOU   92  CA  GLY A  16     3199   3032   3142    -40    123      5       C  
ATOM     93  C   GLY A  16      25.581  -1.676   5.032  1.00 23.35           C  
ANISOU   93  C   GLY A  16     3036   2865   2971    -45    115      7       C  
ATOM     94  O   GLY A  16      26.037  -1.205   3.980  1.00 22.70           O  
ANISOU   94  O   GLY A  16     2936   2794   2893    -43     96     19       O  
ATOM     95  N   GLY A  17      25.836  -1.134   6.205  1.00 22.97           N  
ANISOU   95  N   GLY A  17     3010   2804   2913    -51    128     -3       N  
ATOM     96  CA  GLY A  17      26.563   0.118   6.251  1.00 22.90           C  
ANISOU   96  CA  GLY A  17     3002   2792   2907    -56    122     -5       C  
ATOM     97  C   GLY A  17      27.999  -0.130   5.774  1.00 22.16           C  
ANISOU   97  C   GLY A  17     2909   2720   2790    -58     95      1       C  
ATOM     98  O   GLY A  17      28.606   0.757   5.269  1.00 21.65           O  
ANISOU   98  O   GLY A  17     2835   2657   2734    -60     85      7       O  
ATOM     99  N   VAL A  18      28.537  -1.335   5.952  1.00 22.09           N  
ANISOU   99  N   VAL A  18     2910   2726   2754    -57     86      0       N  
ATOM    100  CA  VAL A  18      29.983  -1.516   5.756  1.00 23.55           C  
ANISOU  100  CA  VAL A  18     3100   2930   2917    -60     64      4       C  
ATOM    101  C   VAL A  18      30.138  -1.804   4.303  1.00 23.33           C  
ANISOU  101  C   VAL A  18     3048   2919   2896    -54     47     19       C  
ATOM    102  O   VAL A  18      30.992  -1.221   3.655  1.00 24.08           O  
ANISOU  102  O   VAL A  18     3133   3022   2992    -55     33     28       O  
ATOM    103  CB  VAL A  18      30.648  -2.496   6.749  1.00 24.62           C  
ANISOU  103  CB  VAL A  18     3259   3073   3020    -62     61     -3       C  
ATOM    104  CG1 VAL A  18      32.133  -2.759   6.425  1.00 25.18           C  
ANISOU  104  CG1 VAL A  18     3329   3163   3072    -63     36      1       C  
ATOM    105  CG2 VAL A  18      30.516  -1.947   8.175  1.00 23.27           C  
ANISOU  105  CG2 VAL A  18     3112   2887   2840    -67     77    -19       C  
ATOM    106  N   MET A  19      29.166  -2.500   3.756  1.00 23.52           N  
ANISOU  106  N   MET A  19     3060   2944   2931    -47     52     23       N  
ATOM    107  CA  MET A  19      29.051  -2.611   2.273  1.00 24.24           C  
ANISOU  107  CA  MET A  19     3126   3051   3031    -41     37     36       C  
ATOM    108  C   MET A  19      29.084  -1.344   1.472  1.00 23.57           C  
ANISOU  108  C   MET A  19     3025   2967   2964    -39     33     49       C  
ATOM    109  O   MET A  19      29.791  -1.267   0.471  1.00 26.06           O  
ANISOU  109  O   MET A  19     3327   3301   3273    -36     16     61       O  
ATOM    110  CB  MET A  19      27.839  -3.426   1.892  1.00 23.55           C  
ANISOU  110  CB  MET A  19     3027   2963   2957    -34     44     34       C  
ATOM    111  CG  MET A  19      28.192  -4.911   1.935  1.00 23.78           C  
ANISOU  111  CG  MET A  19     3061   3003   2968    -33     37     28       C  
ATOM    112  SD  MET A  19      26.824  -6.022   1.724  1.00 27.50           S  
ANISOU  112  SD  MET A  19     3520   3468   3457    -28     47     21       S  
ATOM    113  CE  MET A  19      25.373  -5.182   2.370  1.00 26.15           C  
ANISOU  113  CE  MET A  19     3347   3269   3316    -29     72     18       C  
ATOM    114  N   ALA A  20      28.233  -0.390   1.854  1.00 22.77           N  
ANISOU  114  N   ALA A  20     2920   2842   2886    -41     49     48       N  
ATOM    115  CA  ALA A  20      28.177   0.930   1.237  1.00 19.95           C  
ANISOU  115  CA  ALA A  20     2548   2480   2552    -39     48     61       C  
ATOM    116  C   ALA A  20      29.512   1.543   1.238  1.00 19.66           C  
ANISOU  116  C   ALA A  20     2515   2447   2506    -45     38     66       C  
ATOM    117  O   ALA A  20      29.982   1.995   0.209  1.00 18.99           O  
ANISOU  117  O   ALA A  20     2414   2375   2426    -41     27     84       O  
ATOM    118  CB  ALA A  20      27.255   1.844   1.988  1.00 20.23           C  
ANISOU  118  CB  ALA A  20     2585   2485   2613    -42     70     54       C  
ATOM    119  N   THR A  21      30.111   1.653   2.426  1.00 17.94           N  
ANISOU  119  N   THR A  21     2318   2219   2276    -54     43     50       N  
ATOM    120  CA  THR A  21      31.451   2.108   2.525  1.00 18.07           C  
ANISOU  120  CA  THR A  21     2340   2241   2285    -60     31     51       C  
ATOM    121  C   THR A  21      32.519   1.539   1.576  1.00 17.90           C  
ANISOU  121  C   THR A  21     2309   2246   2246    -57     11     64       C  
ATOM    122  O   THR A  21      33.379   2.295   1.058  1.00 17.58           O  
ANISOU  122  O   THR A  21     2258   2208   2213    -59      3     76       O  
ATOM    123  CB  THR A  21      31.930   1.870   3.999  1.00 18.20           C  
ANISOU  123  CB  THR A  21     2384   2249   2282    -68     35     28       C  
ATOM    124  OG1 THR A  21      31.067   2.590   4.885  1.00 18.57           O  
ANISOU  124  OG1 THR A  21     2438   2271   2344    -72     56     14       O  
ATOM    125  CG2 THR A  21      33.289   2.388   4.167  1.00 18.41           C  
ANISOU  125  CG2 THR A  21     2412   2279   2302    -76     22     26       C  
ATOM    126  N   LEU A  22      32.532   0.198   1.414  1.00 17.82           N  
ANISOU  126  N   LEU A  22     2303   2253   2213    -53      4     61       N  
ATOM    127  CA  LEU A  22      33.532  -0.516   0.662  1.00 18.01           C  
ANISOU  127  CA  LEU A  22     2321   2301   2219    -50    -12     70       C  
ATOM    128  C   LEU A  22      33.219  -0.364  -0.832  1.00 18.84           C  
ANISOU  128  C   LEU A  22     2403   2423   2333    -40    -18     89       C  
ATOM    129  O   LEU A  22      34.168  -0.209  -1.632  1.00 19.14           O  
ANISOU  129  O   LEU A  22     2430   2477   2365    -38    -29    102       O  
ATOM    130  CB  LEU A  22      33.457  -2.041   1.082  1.00 18.46           C  
ANISOU  130  CB  LEU A  22     2390   2367   2254    -47    -15     58       C  
ATOM    131  CG  LEU A  22      33.909  -2.285   2.556  1.00 19.22           C  
ANISOU  131  CG  LEU A  22     2511   2452   2336    -55    -11     42       C  
ATOM    132  CD1 LEU A  22      33.716  -3.763   2.821  1.00 20.58           C  
ANISOU  132  CD1 LEU A  22     2693   2633   2493    -51    -11     36       C  
ATOM    133  CD2 LEU A  22      35.432  -1.995   2.693  1.00 19.49           C  
ANISOU  133  CD2 LEU A  22     2549   2495   2359    -61    -26     44       C  
ATOM    134  N   ILE A  23      31.913  -0.299  -1.187  1.00 18.94           N  
ANISOU  134  N   ILE A  23     2405   2430   2360    -34    -10     91       N  
ATOM    135  CA  ILE A  23      31.523  -0.006  -2.571  1.00 20.22           C  
ANISOU  135  CA  ILE A  23     2543   2607   2529    -25    -17    110       C  
ATOM    136  C   ILE A  23      32.063   1.347  -3.056  1.00 21.18           C  
ANISOU  136  C   ILE A  23     2654   2726   2666    -25    -17    131       C  
ATOM    137  O   ILE A  23      32.577   1.451  -4.165  1.00 20.70           O  
ANISOU  137  O   ILE A  23     2579   2686   2599    -19    -27    149       O  
ATOM    138  CB  ILE A  23      30.005  -0.030  -2.679  1.00 21.14           C  
ANISOU  138  CB  ILE A  23     2652   2715   2664    -19     -8    108       C  
ATOM    139  CG1 ILE A  23      29.527  -1.476  -2.402  1.00 23.68           C  
ANISOU  139  CG1 ILE A  23     2981   3043   2973    -18     -9     90       C  
ATOM    140  CG2 ILE A  23      29.608   0.205  -4.107  1.00 23.01           C  
ANISOU  140  CG2 ILE A  23     2865   2972   2905     -8    -18    128       C  
ATOM    141  CD1 ILE A  23      28.040  -1.708  -2.136  1.00 23.06           C  
ANISOU  141  CD1 ILE A  23     2898   2949   2915    -16      1     82       C  
ATOM    142  N   VAL A  24      31.925   2.386  -2.223  1.00 21.55           N  
ANISOU  142  N   VAL A  24     2706   2745   2734    -32     -5    127       N  
ATOM    143  CA  VAL A  24      32.476   3.701  -2.533  1.00 21.95           C  
ANISOU  143  CA  VAL A  24     2746   2787   2806    -34     -2    145       C  
ATOM    144  C   VAL A  24      34.013   3.665  -2.434  1.00 23.12           C  
ANISOU  144  C   VAL A  24     2899   2943   2940    -41    -12    145       C  
ATOM    145  O   VAL A  24      34.672   4.200  -3.298  1.00 21.47           O  
ANISOU  145  O   VAL A  24     2676   2744   2737    -38    -16    166       O  
ATOM    146  CB  VAL A  24      31.955   4.833  -1.639  1.00 21.47           C  
ANISOU  146  CB  VAL A  24     2689   2691   2776    -41     13    137       C  
ATOM    147  CG1 VAL A  24      32.569   6.156  -2.121  1.00 23.19           C  
ANISOU  147  CG1 VAL A  24     2891   2899   3019    -42     15    158       C  
ATOM    148  CG2 VAL A  24      30.440   5.002  -1.703  1.00 21.32           C  
ANISOU  148  CG2 VAL A  24     2662   2660   2777    -35     25    139       C  
ATOM    149  N   GLN A  25      34.606   3.090  -1.367  1.00 23.48           N  
ANISOU  149  N   GLN A  25     2966   2985   2971    -49    -15    122       N  
ATOM    150  CA  GLN A  25      36.087   2.912  -1.477  1.00 25.06           C  
ANISOU  150  CA  GLN A  25     3165   3197   3156    -54    -27    125       C  
ATOM    151  C   GLN A  25      36.526   2.275  -2.870  1.00 26.96           C  
ANISOU  151  C   GLN A  25     3392   3470   3382    -43    -37    145       C  
ATOM    152  O   GLN A  25      37.501   2.685  -3.485  1.00 28.41           O  
ANISOU  152  O   GLN A  25     3564   3662   3567    -43    -42    161       O  
ATOM    153  CB  GLN A  25      36.672   2.093  -0.349  1.00 24.50           C  
ANISOU  153  CB  GLN A  25     3117   3126   3065    -61    -33    102       C  
ATOM    154  CG  GLN A  25      36.493   2.692   1.069  1.00 24.57           C  
ANISOU  154  CG  GLN A  25     3143   3109   3082    -71    -24     81       C  
ATOM    155  CD  GLN A  25      37.344   3.940   1.223  1.00 25.15           C  
ANISOU  155  CD  GLN A  25     3210   3168   3178    -80    -26     83       C  
ATOM    156  OE1 GLN A  25      38.595   3.884   1.090  1.00 25.59           O  
ANISOU  156  OE1 GLN A  25     3261   3233   3228    -84    -38     86       O  
ATOM    157  NE2 GLN A  25      36.697   5.073   1.481  1.00 24.28           N  
ANISOU  157  NE2 GLN A  25     3095   3033   3095    -83    -12     81       N  
ATOM    158  N   LYS A  26      35.819   1.284  -3.356  1.00 26.70           N  
ANISOU  158  N   LYS A  26     3358   3453   3332    -35    -40    142       N  
ATOM    159  CA  LYS A  26      36.329   0.562  -4.501  1.00 27.79           C  
ANISOU  159  CA  LYS A  26     3485   3622   3451    -26    -50    153       C  
ATOM    160  C   LYS A  26      35.733   1.136  -5.785  1.00 27.42           C  
ANISOU  160  C   LYS A  26     3418   3588   3411    -15    -49    177       C  
ATOM    161  O   LYS A  26      35.955   0.628  -6.855  1.00 27.84           O  
ANISOU  161  O   LYS A  26     3461   3669   3447     -6    -57    187       O  
ATOM    162  CB  LYS A  26      35.972  -0.905  -4.328  1.00 27.31           C  
ANISOU  162  CB  LYS A  26     3433   3572   3369    -23    -55    135       C  
ATOM    163  CG  LYS A  26      36.792  -1.583  -3.233  1.00 28.98           C  
ANISOU  163  CG  LYS A  26     3664   3778   3570    -32    -59    117       C  
ATOM    164  CD  LYS A  26      36.317  -3.015  -3.068  1.00 27.81           C  
ANISOU  164  CD  LYS A  26     3522   3636   3406    -28    -61    101       C  
ATOM    165  CE  LYS A  26      37.383  -3.849  -2.370  1.00 33.08           C  
ANISOU  165  CE  LYS A  26     4203   4307   4059    -33    -68     91       C  
ATOM    166  NZ  LYS A  26      38.650  -3.619  -3.140  1.00 34.37           N  
ANISOU  166  NZ  LYS A  26     4355   4486   4217    -31    -77    104       N  
ATOM    167  N   ASN A  27      34.967   2.211  -5.654  1.00 26.47           N  
ANISOU  167  N   ASN A  27     3292   3449   3317    -16    -40    187       N  
ATOM    168  CA  ASN A  27      34.253   2.817  -6.769  1.00 29.36           C  
ANISOU  168  CA  ASN A  27     3638   3824   3692     -4    -39    211       C  
ATOM    169  C   ASN A  27      33.418   1.829  -7.521  1.00 30.77           C  
ANISOU  169  C   ASN A  27     3811   4027   3852      5    -47    207       C  
ATOM    170  O   ASN A  27      33.428   1.868  -8.732  1.00 30.21           O  
ANISOU  170  O   ASN A  27     3725   3982   3769     16    -54    227       O  
ATOM    171  CB  ASN A  27      35.226   3.527  -7.780  1.00 29.76           C  
ANISOU  171  CB  ASN A  27     3673   3889   3742      0    -40    242       C  
ATOM    172  CG  ASN A  27      34.546   4.640  -8.565  1.00 29.90           C  
ANISOU  172  CG  ASN A  27     3672   3905   3781      8    -34    272       C  
ATOM    173  OD1 ASN A  27      33.577   5.269  -8.102  1.00 28.94           O  
ANISOU  173  OD1 ASN A  27     3549   3759   3686      7    -26    271       O  
ATOM    174  ND2 ASN A  27      35.023   4.874  -9.790  1.00 32.73           N  
ANISOU  174  ND2 ASN A  27     4016   4290   4130     19    -37    301       N  
ATOM    175  N   LEU A  28      32.673   0.948  -6.828  1.00 30.00           N  
ANISOU  175  N   LEU A  28     3724   3921   3750      2    -47    182       N  
ATOM    176  CA  LEU A  28      32.078  -0.190  -7.527  1.00 29.88           C  
ANISOU  176  CA  LEU A  28     3704   3931   3717     11    -57    173       C  
ATOM    177  C   LEU A  28      30.724   0.040  -8.279  1.00 30.75           C  
ANISOU  177  C   LEU A  28     3797   4047   3838     22    -60    182       C  
ATOM    178  O   LEU A  28      30.385  -0.741  -9.144  1.00 29.03           O  
ANISOU  178  O   LEU A  28     3570   3855   3604     30    -72    178       O  
ATOM    179  CB  LEU A  28      31.863  -1.310  -6.557  1.00 30.46           C  
ANISOU  179  CB  LEU A  28     3793   3993   3785      4    -55    144       C  
ATOM    180  CG  LEU A  28      33.020  -2.224  -6.418  1.00 33.44           C  
ANISOU  180  CG  LEU A  28     4180   4383   4140      1    -62    134       C  
ATOM    181  CD1 LEU A  28      32.494  -3.366  -5.569  1.00 35.88           C  
ANISOU  181  CD1 LEU A  28     4503   4682   4448     -2    -59    109       C  
ATOM    182  CD2 LEU A  28      33.462  -2.737  -7.785  1.00 32.97           C  
ANISOU  182  CD2 LEU A  28     4108   4359   4060     11    -74    142       C  
ATOM    183  N   GLY A  29      29.969   1.083  -7.886  1.00 27.99           N  
ANISOU  183  N   GLY A  29     3443   3673   3518     20    -49    192       N  
ATOM    184  CA  GLY A  29      28.707   1.420  -8.458  1.00 26.62           C  
ANISOU  184  CA  GLY A  29     3252   3500   3359     30    -51    202       C  
ATOM    185  C   GLY A  29      27.870   2.359  -7.587  1.00 25.59           C  
ANISOU  185  C   GLY A  29     3122   3333   3266     25    -35    202       C  
ATOM    186  O   GLY A  29      28.204   2.648  -6.413  1.00 23.42           O  
ANISOU  186  O   GLY A  29     2863   3031   3002     13    -21    190       O  
ATOM    187  N   ASP A  30      26.747   2.802  -8.142  1.00 25.05           N  
ANISOU  187  N   ASP A  30     3035   3265   3216     34    -36    216       N  
ATOM    188  CA  ASP A  30      25.811   3.518  -7.335  1.00 26.68           C  
ANISOU  188  CA  ASP A  30     3241   3437   3459     30    -20    213       C  
ATOM    189  C   ASP A  30      25.185   2.565  -6.323  1.00 26.59           C  
ANISOU  189  C   ASP A  30     3243   3410   3449     23    -12    180       C  
ATOM    190  O   ASP A  30      25.167   1.355  -6.537  1.00 28.43           O  
ANISOU  190  O   ASP A  30     3478   3661   3660     24    -23    165       O  
ATOM    191  CB  ASP A  30      24.798   4.178  -8.204  1.00 28.36           C  
ANISOU  191  CB  ASP A  30     3428   3653   3692     43    -25    236       C  
ATOM    192  CG  ASP A  30      25.409   5.362  -9.013  1.00 33.23           C  
ANISOU  192  CG  ASP A  30     4032   4277   4314     50    -27    273       C  
ATOM    193  OD1 ASP A  30      26.486   5.930  -8.589  1.00 30.73           O  
ANISOU  193  OD1 ASP A  30     3726   3948   3999     42    -17    278       O  
ATOM    194  OD2 ASP A  30      24.802   5.695 -10.093  1.00 29.99           O  
ANISOU  194  OD2 ASP A  30     3600   3885   3907     64    -37    298       O  
ATOM    195  N   VAL A  31      24.682   3.109  -5.228  1.00 24.95           N  
ANISOU  195  N   VAL A  31     3042   3167   3268     16      6    171       N  
ATOM    196  CA  VAL A  31      24.275   2.309  -4.059  1.00 23.08           C  
ANISOU  196  CA  VAL A  31     2823   2912   3031      7     19    142       C  
ATOM    197  C   VAL A  31      23.005   2.849  -3.462  1.00 21.85           C  
ANISOU  197  C   VAL A  31     2662   2727   2912      8     38    138       C  
ATOM    198  O   VAL A  31      22.901   4.046  -3.230  1.00 21.45           O  
ANISOU  198  O   VAL A  31     2606   2655   2886      7     49    148       O  
ATOM    199  CB  VAL A  31      25.325   2.491  -2.923  1.00 22.88           C  
ANISOU  199  CB  VAL A  31     2824   2873   2995     -4     30    129       C  
ATOM    200  CG1 VAL A  31      24.822   1.872  -1.586  1.00 22.85           C  
ANISOU  200  CG1 VAL A  31     2839   2847   2992    -11     47    103       C  
ATOM    201  CG2 VAL A  31      26.620   1.871  -3.374  1.00 23.50           C  
ANISOU  201  CG2 VAL A  31     2909   2978   3039     -5     13    131       C  
ATOM    202  N   VAL A  32      22.103   1.957  -3.088  1.00 21.48           N  
ANISOU  202  N   VAL A  32     2615   2675   2870      7     43    120       N  
ATOM    203  CA  VAL A  32      20.871   2.323  -2.473  1.00 20.82           C  
ANISOU  203  CA  VAL A  32     2525   2562   2821      8     63    114       C  
ATOM    204  C   VAL A  32      20.868   1.553  -1.235  1.00 20.68           C  
ANISOU  204  C   VAL A  32     2531   2530   2794      0     80     89       C  
ATOM    205  O   VAL A  32      21.027   0.327  -1.251  1.00 20.67           O  
ANISOU  205  O   VAL A  32     2537   2544   2773     -1     73     78       O  
ATOM    206  CB  VAL A  32      19.673   1.842  -3.321  1.00 21.58           C  
ANISOU  206  CB  VAL A  32     2596   2669   2935     17     53    118       C  
ATOM    207  CG1 VAL A  32      18.323   2.163  -2.646  1.00 20.40           C  
ANISOU  207  CG1 VAL A  32     2438   2487   2825     18     75    111       C  
ATOM    208  CG2 VAL A  32      19.772   2.424  -4.727  1.00 21.05           C  
ANISOU  208  CG2 VAL A  32     2506   2626   2866     29     30    145       C  
ATOM    209  N   LEU A  33      20.684   2.243  -0.151  1.00 20.95           N  
ANISOU  209  N   LEU A  33     2579   2536   2845     -6    104     81       N  
ATOM    210  CA  LEU A  33      20.572   1.579   1.100  1.00 22.12           C  
ANISOU  210  CA  LEU A  33     2750   2670   2984    -14    123     59       C  
ATOM    211  C   LEU A  33      19.118   1.491   1.355  1.00 23.61           C  
ANISOU  211  C   LEU A  33     2925   2838   3205    -10    142     54       C  
ATOM    212  O   LEU A  33      18.436   2.531   1.549  1.00 23.62           O  
ANISOU  212  O   LEU A  33     2917   2817   3239     -9    157     58       O  
ATOM    213  CB  LEU A  33      21.229   2.321   2.231  1.00 21.85           C  
ANISOU  213  CB  LEU A  33     2739   2618   2942    -22    140     49       C  
ATOM    214  CG  LEU A  33      22.751   2.118   2.189  1.00 21.92           C  
ANISOU  214  CG  LEU A  33     2765   2648   2915    -27    122     49       C  
ATOM    215  CD1 LEU A  33      23.378   3.467   2.445  1.00 21.93           C  
ANISOU  215  CD1 LEU A  33     2770   2636   2927    -32    126     52       C  
ATOM    216  CD2 LEU A  33      23.178   1.091   3.207  1.00 21.46           C  
ANISOU  216  CD2 LEU A  33     2732   2591   2827    -33    128     32       C  
ATOM    217  N   PHE A  34      18.627   0.262   1.343  1.00 23.30           N  
ANISOU  217  N   PHE A  34     2883   2805   3162     -9    141     45       N  
ATOM    218  CA  PHE A  34      17.190   0.111   1.550  1.00 25.43           C  
ANISOU  218  CA  PHE A  34     3138   3055   3468     -6    159     41       C  
ATOM    219  C   PHE A  34      16.857  -0.503   2.903  1.00 25.35           C  
ANISOU  219  C   PHE A  34     3150   3026   3456    -12    188     23       C  
ATOM    220  O   PHE A  34      17.544  -1.388   3.400  1.00 27.43           O  
ANISOU  220  O   PHE A  34     3433   3298   3688    -16    188     15       O  
ATOM    221  CB  PHE A  34      16.452  -0.577   0.389  1.00 24.59           C  
ANISOU  221  CB  PHE A  34     3002   2965   3376      1    138     46       C  
ATOM    222  CG  PHE A  34      15.102  -1.108   0.795  1.00 26.04           C  
ANISOU  222  CG  PHE A  34     3173   3128   3593      2    158     36       C  
ATOM    223  CD1 PHE A  34      14.994  -2.276   1.584  1.00 26.02           C  
ANISOU  223  CD1 PHE A  34     3185   3119   3583     -2    173     20       C  
ATOM    224  CD2 PHE A  34      13.917  -0.458   0.394  1.00 25.85           C  
ANISOU  224  CD2 PHE A  34     3120   3089   3611      9    162     43       C  
ATOM    225  CE1 PHE A  34      13.736  -2.726   2.040  1.00 26.42           C  
ANISOU  225  CE1 PHE A  34     3223   3146   3668     -2    195     12       C  
ATOM    226  CE2 PHE A  34      12.663  -0.931   0.813  1.00 26.88           C  
ANISOU  226  CE2 PHE A  34     3236   3198   3776      9    182     34       C  
ATOM    227  CZ  PHE A  34      12.562  -2.074   1.612  1.00 26.57           C  
ANISOU  227  CZ  PHE A  34     3212   3151   3730      3    199     18       C  
ATOM    228  N   ASP A  35      15.825   0.022   3.512  1.00 26.06           N  
ANISOU  228  N   ASP A  35     3234   3087   3578    -11    216     19       N  
ATOM    229  CA  ASP A  35      15.267  -0.566   4.693  1.00 26.48           C  
ANISOU  229  CA  ASP A  35     3302   3121   3635    -15    247      5       C  
ATOM    230  C   ASP A  35      13.834  -0.141   4.873  1.00 27.20           C  
ANISOU  230  C   ASP A  35     3374   3186   3774    -11    271      4       C  
ATOM    231  O   ASP A  35      13.476   0.985   4.536  1.00 26.47           O  
ANISOU  231  O   ASP A  35     3265   3082   3707     -7    272     11       O  
ATOM    232  CB  ASP A  35      16.025  -0.142   5.926  1.00 27.35           C  
ANISOU  232  CB  ASP A  35     3448   3224   3718    -22    266     -5       C  
ATOM    233  CG  ASP A  35      16.129  -1.267   6.894  1.00 29.85           C  
ANISOU  233  CG  ASP A  35     3788   3541   4012    -25    282    -15       C  
ATOM    234  OD1 ASP A  35      15.134  -1.468   7.657  1.00 32.09           O  
ANISOU  234  OD1 ASP A  35     4072   3803   4315    -24    314    -21       O  
ATOM    235  OD2 ASP A  35      17.168  -1.996   6.826  1.00 30.26           O  
ANISOU  235  OD2 ASP A  35     3854   3614   4027    -27    263    -14       O  
ATOM    236  N   ILE A  36      13.040  -0.986   5.511  1.00 27.29           N  
ANISOU  236  N   ILE A  36     3386   3183   3797    -12    295     -4       N  
ATOM    237  CA  ILE A  36      11.694  -0.521   5.952  1.00 30.04           C  
ANISOU  237  CA  ILE A  36     3718   3501   4191     -9    326     -7       C  
ATOM    238  C   ILE A  36      11.719   0.492   7.067  1.00 29.64           C  
ANISOU  238  C   ILE A  36     3690   3429   4141    -12    358    -16       C  
ATOM    239  O   ILE A  36      10.736   1.206   7.226  1.00 30.24           O  
ANISOU  239  O   ILE A  36     3749   3480   4258     -8    380    -16       O  
ATOM    240  CB  ILE A  36      10.770  -1.686   6.433  1.00 29.50           C  
ANISOU  240  CB  ILE A  36     3645   3420   4142     -9    349    -14       C  
ATOM    241  CG1 ILE A  36      11.348  -2.373   7.663  1.00 28.69           C  
ANISOU  241  CG1 ILE A  36     3579   3317   4002    -14    371    -23       C  
ATOM    242  CG2 ILE A  36      10.565  -2.719   5.320  1.00 28.19           C  
ANISOU  242  CG2 ILE A  36     3453   3272   3985     -6    319    -10       C  
ATOM    243  CD1 ILE A  36      10.391  -3.405   8.232  1.00 31.94           C  
ANISOU  243  CD1 ILE A  36     3986   3711   4437    -14    400    -26       C  
ATOM    244  N   VAL A  37      12.806   0.507   7.869  1.00 30.16           N  
ANISOU  244  N   VAL A  37     3791   3504   4163    -18    361    -24       N  
ATOM    245  CA  VAL A  37      12.915   1.401   9.022  1.00 31.69           C  
ANISOU  245  CA  VAL A  37     4009   3679   4350    -21    391    -37       C  
ATOM    246  C   VAL A  37      13.121   2.746   8.386  1.00 34.28           C  
ANISOU  246  C   VAL A  37     4323   4003   4699    -20    377    -31       C  
ATOM    247  O   VAL A  37      13.907   2.884   7.461  1.00 37.57           O  
ANISOU  247  O   VAL A  37     4731   4439   5102    -20    343    -19       O  
ATOM    248  CB  VAL A  37      14.119   1.032   9.950  1.00 32.39           C  
ANISOU  248  CB  VAL A  37     4138   3783   4384    -28    391    -47       C  
ATOM    249  CG1 VAL A  37      14.378   2.114  10.960  1.00 30.08           C  
ANISOU  249  CG1 VAL A  37     3868   3477   4083    -31    413    -63       C  
ATOM    250  CG2 VAL A  37      13.900  -0.325  10.638  1.00 31.37           C  
ANISOU  250  CG2 VAL A  37     4024   3658   4237    -28    408    -50       C  
ATOM    251  N   LYS A  38      12.374   3.737   8.813  1.00 37.94           N  
ANISOU  251  N   LYS A  38     4778   4438   5196    -18    404    -37       N  
ATOM    252  CA  LYS A  38      12.279   5.000   8.094  1.00 40.41           C  
ANISOU  252  CA  LYS A  38     5069   4742   5543    -15    394    -27       C  
ATOM    253  C   LYS A  38      13.431   5.936   8.492  1.00 39.68           C  
ANISOU  253  C   LYS A  38     4999   4650   5427    -21    390    -36       C  
ATOM    254  O   LYS A  38      13.920   5.876   9.630  1.00 39.51           O  
ANISOU  254  O   LYS A  38     5009   4626   5375    -27    407    -56       O  
ATOM    255  CB  LYS A  38      10.912   5.623   8.425  1.00 46.02           C  
ANISOU  255  CB  LYS A  38     5761   5418   6306    -10    428    -31       C  
ATOM    256  CG  LYS A  38      10.075   5.906   7.201  1.00 48.57           C  
ANISOU  256  CG  LYS A  38     6040   5737   6675     -1    411    -10       C  
ATOM    257  CD  LYS A  38       8.817   5.062   7.088  1.00 50.05           C  
ANISOU  257  CD  LYS A  38     6206   5917   6893      3    422     -7       C  
ATOM    258  CE  LYS A  38       8.610   4.718   5.606  1.00 51.69           C  
ANISOU  258  CE  LYS A  38     6380   6145   7114     10    382     13       C  
ATOM    259  NZ  LYS A  38       7.211   4.842   5.113  1.00 50.25           N  
ANISOU  259  NZ  LYS A  38     6158   5946   6988     18    388     22       N  
ATOM    260  N   ASN A  39      13.860   6.791   7.567  1.00 40.22           N  
ANISOU  260  N   ASN A  39     5050   4722   5510    -19    366    -21       N  
ATOM    261  CA  ASN A  39      14.889   7.841   7.834  1.00 42.88           C  
ANISOU  261  CA  ASN A  39     5400   5054   5836    -25    362    -28       C  
ATOM    262  C   ASN A  39      16.336   7.353   7.957  1.00 41.03           C  
ANISOU  262  C   ASN A  39     5192   4848   5550    -32    339    -32       C  
ATOM    263  O   ASN A  39      17.249   7.908   7.342  1.00 37.62           O  
ANISOU  263  O   ASN A  39     4755   4425   5113    -34    316    -22       O  
ATOM    264  CB  ASN A  39      14.561   8.667   9.093  1.00 45.34           C  
ANISOU  264  CB  ASN A  39     5728   5336   6163    -29    400    -53       C  
ATOM    265  CG  ASN A  39      13.187   9.281   9.032  1.00 48.91           C  
ANISOU  265  CG  ASN A  39     6154   5756   6671    -22    426    -50       C  
ATOM    266  OD1 ASN A  39      12.736   9.666   7.955  1.00 51.59           O  
ANISOU  266  OD1 ASN A  39     6461   6093   7047    -15    412    -26       O  
ATOM    267  ND2 ASN A  39      12.503   9.362  10.180  1.00 48.87           N  
ANISOU  267  ND2 ASN A  39     6163   5730   6674    -23    466    -73       N  
ATOM    268  N   MET A  40      16.515   6.336   8.792  1.00 40.93           N  
ANISOU  268  N   MET A  40     5205   4845   5499    -36    347    -47       N  
ATOM    269  CA  MET A  40      17.796   5.703   9.025  1.00 40.22           C  
ANISOU  269  CA  MET A  40     5140   4781   5358    -42    327    -51       C  
ATOM    270  C   MET A  40      18.644   5.375   7.763  1.00 37.14           C  
ANISOU  270  C   MET A  40     4736   4418   4955    -41    287    -30       C  
ATOM    271  O   MET A  40      19.823   5.716   7.756  1.00 36.88           O  
ANISOU  271  O   MET A  40     4715   4397   4901    -46    270    -31       O  
ATOM    272  CB  MET A  40      17.607   4.498   9.934  1.00 41.03           C  
ANISOU  272  CB  MET A  40     5267   4892   5431    -43    342    -62       C  
ATOM    273  CG  MET A  40      18.913   3.814  10.285  1.00 40.08           C  
ANISOU  273  CG  MET A  40     5173   4797   5258    -49    322    -67       C  
ATOM    274  SD  MET A  40      19.376   2.741   8.914  1.00 43.03           S  
ANISOU  274  SD  MET A  40     5527   5199   5620    -45    284    -43       S  
ATOM    275  CE  MET A  40      18.380   1.273   9.242  1.00 35.63           C  
ANISOU  275  CE  MET A  40     4591   4262   4682    -40    302    -43       C  
ATOM    276  N   PRO A  41      18.066   4.759   6.694  1.00 36.83           N  
ANISOU  276  N   PRO A  41     4672   4391   4930    -33    273    -11       N  
ATOM    277  CA  PRO A  41      18.953   4.562   5.517  1.00 34.13           C  
ANISOU  277  CA  PRO A  41     4319   4076   4573    -31    237      7       C  
ATOM    278  C   PRO A  41      19.400   5.864   4.892  1.00 33.39           C  
ANISOU  278  C   PRO A  41     4210   3976   4498    -31    227     20       C  
ATOM    279  O   PRO A  41      20.528   5.946   4.368  1.00 33.55           O  
ANISOU  279  O   PRO A  41     4233   4015   4498    -33    203     29       O  
ATOM    280  CB  PRO A  41      18.081   3.779   4.527  1.00 34.32           C  
ANISOU  280  CB  PRO A  41     4317   4111   4611    -23    225     21       C  
ATOM    281  CG  PRO A  41      16.702   3.826   5.074  1.00 34.84           C  
ANISOU  281  CG  PRO A  41     4375   4151   4712    -20    255     13       C  
ATOM    282  CD  PRO A  41      16.856   3.933   6.564  1.00 34.91           C  
ANISOU  282  CD  PRO A  41     4415   4143   4706    -27    284     -8       C  
ATOM    283  N   HIS A  42      18.537   6.883   4.943  1.00 31.45           N  
ANISOU  283  N   HIS A  42     3949   3704   4296    -28    245     22       N  
ATOM    284  CA  HIS A  42      18.916   8.220   4.522  1.00 28.88           C  
ANISOU  284  CA  HIS A  42     3611   3366   3996    -27    242     34       C  
ATOM    285  C   HIS A  42      20.067   8.807   5.301  1.00 26.35           C  
ANISOU  285  C   HIS A  42     3314   3040   3658    -38    244     17       C  
ATOM    286  O   HIS A  42      20.918   9.387   4.720  1.00 26.12           O  
ANISOU  286  O   HIS A  42     3277   3016   3629    -39    227     30       O  
ATOM    287  CB  HIS A  42      17.698   9.108   4.522  1.00 30.86           C  
ANISOU  287  CB  HIS A  42     3839   3585   4298    -21    264     38       C  
ATOM    288  CG  HIS A  42      16.618   8.638   3.574  1.00 34.03           C  
ANISOU  288  CG  HIS A  42     4213   3995   4722    -10    255     58       C  
ATOM    289  ND1 HIS A  42      16.689   8.822   2.223  1.00 33.80           N  
ANISOU  289  ND1 HIS A  42     4157   3982   4700     -2    229     87       N  
ATOM    290  CD2 HIS A  42      15.402   7.978   3.819  1.00 35.87           C  
ANISOU  290  CD2 HIS A  42     4439   4220   4971     -6    270     51       C  
ATOM    291  CE1 HIS A  42      15.577   8.325   1.640  1.00 34.24           C  
ANISOU  291  CE1 HIS A  42     4190   4043   4775      6    225     97       C  
ATOM    292  NE2 HIS A  42      14.799   7.794   2.609  1.00 35.76           N  
ANISOU  292  NE2 HIS A  42     4393   4219   4974      3    250     74       N  
ATOM    293  N   GLY A  43      20.090   8.690   6.633  1.00 25.50           N  
ANISOU  293  N   GLY A  43     3233   2921   3535    -45    265    -12       N  
ATOM    294  CA  GLY A  43      21.205   9.184   7.444  1.00 23.97           C  
ANISOU  294  CA  GLY A  43     3061   2723   3320    -56    264    -32       C  
ATOM    295  C   GLY A  43      22.538   8.546   7.136  1.00 22.97           C  
ANISOU  295  C   GLY A  43     2947   2628   3152    -60    235    -26       C  
ATOM    296  O   GLY A  43      23.533   9.242   6.964  1.00 21.98           O  
ANISOU  296  O   GLY A  43     2820   2502   3028    -65    222    -25       O  
ATOM    297  N   LYS A  44      22.562   7.210   7.097  1.00 22.64           N  
ANISOU  297  N   LYS A  44     2915   2610   3077    -57    226    -24       N  
ATOM    298  CA  LYS A  44      23.676   6.466   6.540  1.00 22.90           C  
ANISOU  298  CA  LYS A  44     2951   2672   3075    -59    197    -13       C  
ATOM    299  C   LYS A  44      24.039   6.769   5.085  1.00 22.65           C  
ANISOU  299  C   LYS A  44     2893   2654   3058    -53    174     14       C  
ATOM    300  O   LYS A  44      25.207   6.857   4.795  1.00 25.09           O  
ANISOU  300  O   LYS A  44     3205   2977   3350    -57    155     19       O  
ATOM    301  CB  LYS A  44      23.461   4.926   6.700  1.00 24.23           C  
ANISOU  301  CB  LYS A  44     3132   2861   3213    -56    193    -15       C  
ATOM    302  CG  LYS A  44      23.321   4.478   8.155  1.00 25.35           C  
ANISOU  302  CG  LYS A  44     3303   2996   3332    -60    214    -39       C  
ATOM    303  CD  LYS A  44      23.231   2.947   8.262  1.00 28.28           C  
ANISOU  303  CD  LYS A  44     3684   3385   3675    -57    211    -37       C  
ATOM    304  CE  LYS A  44      23.039   2.497   9.728  1.00 32.22           C  
ANISOU  304  CE  LYS A  44     4213   3878   4150    -60    234    -57       C  
ATOM    305  NZ  LYS A  44      23.262   0.998   9.834  1.00 33.01           N  
ANISOU  305  NZ  LYS A  44     4324   3998   4220    -58    227    -51       N  
ATOM    306  N   ALA A  45      23.121   6.877   4.161  1.00 21.51           N  
ANISOU  306  N   ALA A  45     2723   2508   2941    -44    173     34       N  
ATOM    307  CA  ALA A  45      23.531   7.153   2.783  1.00 22.00           C  
ANISOU  307  CA  ALA A  45     2762   2587   3009    -38    151     62       C  
ATOM    308  C   ALA A  45      24.280   8.517   2.677  1.00 23.38           C  
ANISOU  308  C   ALA A  45     2931   2747   3206    -42    151     69       C  
ATOM    309  O   ALA A  45      25.362   8.626   2.110  1.00 23.82           O  
ANISOU  309  O   ALA A  45     2983   2818   3248    -44    133     82       O  
ATOM    310  CB  ALA A  45      22.294   7.189   1.898  1.00 21.60           C  
ANISOU  310  CB  ALA A  45     2684   2535   2988    -27    152     81       C  
ATOM    311  N   LEU A  46      23.682   9.563   3.232  1.00 24.05           N  
ANISOU  311  N   LEU A  46     3011   2799   3326    -44    173     61       N  
ATOM    312  CA  LEU A  46      24.301  10.875   3.249  1.00 24.58           C  
ANISOU  312  CA  LEU A  46     3071   2846   3420    -49    176     64       C  
ATOM    313  C   LEU A  46      25.717  10.896   3.876  1.00 24.59           C  
ANISOU  313  C   LEU A  46     3093   2853   3395    -61    167     47       C  
ATOM    314  O   LEU A  46      26.668  11.410   3.277  1.00 25.01           O  
ANISOU  314  O   LEU A  46     3137   2912   3454    -63    153     62       O  
ATOM    315  CB  LEU A  46      23.395  11.841   4.057  1.00 25.90           C  
ANISOU  315  CB  LEU A  46     3237   2975   3629    -51    206     48       C  
ATOM    316  CG  LEU A  46      23.765  13.342   3.943  1.00 27.24           C  
ANISOU  316  CG  LEU A  46     3391   3116   3841    -54    213     54       C  
ATOM    317  CD1 LEU A  46      23.677  13.679   2.449  1.00 26.04           C  
ANISOU  317  CD1 LEU A  46     3208   2974   3710    -42    199     98       C  
ATOM    318  CD2 LEU A  46      22.864  14.295   4.814  1.00 28.19           C  
ANISOU  318  CD2 LEU A  46     3510   3195   4004    -56    244     33       C  
ATOM    319  N   ASP A  47      25.847  10.368   5.079  1.00 23.62           N  
ANISOU  319  N   ASP A  47     2998   2730   3245    -68    174     15       N  
ATOM    320  CA  ASP A  47      27.132  10.270   5.693  1.00 24.46           C  
ANISOU  320  CA  ASP A  47     3124   2845   3323    -79    162     -1       C  
ATOM    321  C   ASP A  47      28.139   9.556   4.761  1.00 25.29           C  
ANISOU  321  C   ASP A  47     3224   2983   3402    -77    135     19       C  
ATOM    322  O   ASP A  47      29.249  10.045   4.467  1.00 25.83           O  
ANISOU  322  O   ASP A  47     3287   3054   3472    -82    121     25       O  
ATOM    323  CB  ASP A  47      26.961   9.514   7.045  1.00 24.32           C  
ANISOU  323  CB  ASP A  47     3138   2830   3272    -84    173    -33       C  
ATOM    324  CG  ASP A  47      28.290   9.306   7.821  1.00 25.38           C  
ANISOU  324  CG  ASP A  47     3294   2976   3371    -94    158    -54       C  
ATOM    325  OD1 ASP A  47      29.238  10.116   7.659  1.00 23.91           O  
ANISOU  325  OD1 ASP A  47     3101   2784   3198   -101    148    -54       O  
ATOM    326  OD2 ASP A  47      28.373   8.318   8.628  1.00 25.57           O  
ANISOU  326  OD2 ASP A  47     3344   3015   3356    -95    158    -69       O  
ATOM    327  N   THR A  48      27.755   8.378   4.305  1.00 24.72           N  
ANISOU  327  N   THR A  48     3152   2933   3305    -69    127     29       N  
ATOM    328  CA  THR A  48      28.632   7.619   3.520  1.00 25.12           C  
ANISOU  328  CA  THR A  48     3199   3014   3329    -67    103     45       C  
ATOM    329  C   THR A  48      28.957   8.286   2.119  1.00 25.74           C  
ANISOU  329  C   THR A  48     3250   3100   3429    -61     92     78       C  
ATOM    330  O   THR A  48      30.081   8.130   1.566  1.00 24.21           O  
ANISOU  330  O   THR A  48     3053   2925   3220    -62     75     90       O  
ATOM    331  CB  THR A  48      27.927   6.255   3.290  1.00 25.12           C  
ANISOU  331  CB  THR A  48     3203   3034   3306    -60    101     47       C  
ATOM    332  OG1 THR A  48      27.768   5.590   4.557  1.00 24.49           O  
ANISOU  332  OG1 THR A  48     3150   2950   3205    -65    111     21       O  
ATOM    333  CG2 THR A  48      28.699   5.412   2.284  1.00 25.33           C  
ANISOU  333  CG2 THR A  48     3222   3092   3307    -55     77     64       C  
ATOM    334  N   SER A  49      27.977   8.973   1.527  1.00 24.96           N  
ANISOU  334  N   SER A  49     3131   2988   3365    -53    102     95       N  
ATOM    335  CA  SER A  49      28.222   9.687   0.231  1.00 24.77           C  
ANISOU  335  CA  SER A  49     3079   2968   3361    -46     94    130       C  
ATOM    336  C   SER A  49      29.412  10.682   0.224  1.00 25.25           C  
ANISOU  336  C   SER A  49     3137   3019   3438    -54     91    136       C  
ATOM    337  O   SER A  49      29.970  11.004  -0.862  1.00 23.33           O  
ANISOU  337  O   SER A  49     2875   2789   3200    -48     81    166       O  
ATOM    338  CB  SER A  49      27.015  10.515  -0.175  1.00 25.13           C  
ANISOU  338  CB  SER A  49     3104   2995   3448    -37    107    147       C  
ATOM    339  OG  SER A  49      26.779  11.591   0.771  1.00 23.26           O  
ANISOU  339  OG  SER A  49     2871   2720   3247    -45    129    129       O  
ATOM    340  N   HIS A  50      29.790  11.175   1.417  1.00 24.69           N  
ANISOU  340  N   HIS A  50     3081   2924   3375    -66    101    107       N  
ATOM    341  CA  HIS A  50      30.777  12.283   1.472  1.00 24.57           C  
ANISOU  341  CA  HIS A  50     3058   2891   3385    -74    101    109       C  
ATOM    342  C   HIS A  50      32.123  11.666   1.310  1.00 23.87           C  
ANISOU  342  C   HIS A  50     2977   2828   3265    -79     81    109       C  
ATOM    343  O   HIS A  50      33.035  12.374   0.907  1.00 24.16           O  
ANISOU  343  O   HIS A  50     2999   2859   3319    -83     77    123       O  
ATOM    344  CB  HIS A  50      30.795  13.057   2.780  1.00 23.66           C  
ANISOU  344  CB  HIS A  50     2956   2743   3290    -86    116     74       C  
ATOM    345  CG  HIS A  50      29.489  13.637   3.140  1.00 24.67           C  
ANISOU  345  CG  HIS A  50     3078   2843   3449    -83    139     67       C  
ATOM    346  ND1 HIS A  50      28.966  13.560   4.405  1.00 24.24           N  
ANISOU  346  ND1 HIS A  50     3046   2774   3390    -89    154     31       N  
ATOM    347  CD2 HIS A  50      28.565  14.299   2.353  1.00 24.27           C  
ANISOU  347  CD2 HIS A  50     3004   2779   3438    -72    150     94       C  
ATOM    348  CE1 HIS A  50      27.775  14.200   4.402  1.00 25.70           C  
ANISOU  348  CE1 HIS A  50     3219   2933   3612    -83    175     34       C  
ATOM    349  NE2 HIS A  50      27.517  14.614   3.134  1.00 25.04           N  
ANISOU  349  NE2 HIS A  50     3107   2851   3556    -73    171     74       N  
ATOM    350  N   THR A  51      32.216  10.350   1.547  1.00 22.44           N  
ANISOU  350  N   THR A  51     2813   2673   3039    -78     70     98       N  
ATOM    351  CA  THR A  51      33.494   9.633   1.416  1.00 22.11           C  
ANISOU  351  CA  THR A  51     2778   2655   2965    -82     51     98       C  
ATOM    352  C   THR A  51      33.927   9.565   0.004  1.00 22.38           C  
ANISOU  352  C   THR A  51     2792   2712   3000    -73     41    133       C  
ATOM    353  O   THR A  51      35.102   9.311  -0.241  1.00 21.52           O  
ANISOU  353  O   THR A  51     2682   2617   2876    -76     28    137       O  
ATOM    354  CB  THR A  51      33.468   8.187   1.969  1.00 22.47           C  
ANISOU  354  CB  THR A  51     2846   2723   2966    -82     43     79       C  
ATOM    355  OG1 THR A  51      32.550   7.423   1.207  1.00 21.40           O  
ANISOU  355  OG1 THR A  51     2705   2605   2821    -70     43     94       O  
ATOM    356  CG2 THR A  51      33.092   8.182   3.557  1.00 21.76           C  
ANISOU  356  CG2 THR A  51     2782   2615   2870    -90     54     42       C  
ATOM    357  N   ASN A  52      33.005   9.773  -0.954  1.00 22.57           N  
ANISOU  357  N   ASN A  52     2797   2738   3037    -61     46    159       N  
ATOM    358  CA  ASN A  52      33.502   9.937  -2.312  1.00 24.49           C  
ANISOU  358  CA  ASN A  52     3020   3001   3282    -52     38    195       C  
ATOM    359  C   ASN A  52      34.677  10.868  -2.496  1.00 24.39           C  
ANISOU  359  C   ASN A  52     2996   2978   3291    -59     38    207       C  
ATOM    360  O   ASN A  52      35.435  10.665  -3.449  1.00 23.90           O  
ANISOU  360  O   ASN A  52     2923   2939   3217    -54     29    231       O  
ATOM    361  CB  ASN A  52      32.441  10.412  -3.274  1.00 25.67           C  
ANISOU  361  CB  ASN A  52     3149   3151   3452    -39     44    224       C  
ATOM    362  CG  ASN A  52      31.506   9.324  -3.606  1.00 28.43           C  
ANISOU  362  CG  ASN A  52     3502   3523   3775    -30     38    221       C  
ATOM    363  OD1 ASN A  52      31.769   8.521  -4.558  1.00 30.33           O  
ANISOU  363  OD1 ASN A  52     3738   3799   3987    -21     24    235       O  
ATOM    364  ND2 ASN A  52      30.397   9.244  -2.820  1.00 26.06           N  
ANISOU  364  ND2 ASN A  52     3210   3205   3486    -31     49    201       N  
ATOM    365  N   VAL A  53      34.783  11.911  -1.648  1.00 25.55           N  
ANISOU  365  N   VAL A  53     3144   3090   3473    -70     49    192       N  
ATOM    366  CA  VAL A  53      35.746  13.023  -1.875  1.00 25.13           C  
ANISOU  366  CA  VAL A  53     3074   3019   3455    -76     53    206       C  
ATOM    367  C   VAL A  53      37.098  12.426  -1.475  1.00 26.12           C  
ANISOU  367  C   VAL A  53     3210   3158   3555    -86     38    189       C  
ATOM    368  O   VAL A  53      37.994  12.441  -2.269  1.00 25.02           O  
ANISOU  368  O   VAL A  53     3057   3033   3414    -83     31    213       O  
ATOM    369  CB  VAL A  53      35.463  14.275  -0.998  1.00 24.51           C  
ANISOU  369  CB  VAL A  53     2993   2896   3424    -86     69    188       C  
ATOM    370  CG1 VAL A  53      36.682  15.159  -0.962  1.00 24.27           C  
ANISOU  370  CG1 VAL A  53     2949   2847   3423    -96     69    191       C  
ATOM    371  CG2 VAL A  53      34.215  15.028  -1.434  1.00 23.97           C  
ANISOU  371  CG2 VAL A  53     2907   2808   3389    -76     86    208       C  
ATOM    372  N   MET A  54      37.185  11.907  -0.236  1.00 26.87           N  
ANISOU  372  N   MET A  54     3330   3250   3630    -95     32    150       N  
ATOM    373  CA  MET A  54      38.345  11.154   0.283  1.00 29.06           C  
ANISOU  373  CA  MET A  54     3620   3543   3877   -104     15    131       C  
ATOM    374  C   MET A  54      38.769   9.895  -0.523  1.00 28.96           C  
ANISOU  374  C   MET A  54     3609   3569   3824    -95      1    147       C  
ATOM    375  O   MET A  54      39.977   9.574  -0.572  1.00 27.31           O  
ANISOU  375  O   MET A  54     3398   3372   3604    -99    -10    147       O  
ATOM    376  CB  MET A  54      38.150  10.746   1.755  1.00 28.66           C  
ANISOU  376  CB  MET A  54     3597   3484   3806   -113     13     89       C  
ATOM    377  CG  MET A  54      38.051  11.892   2.735  1.00 31.72           C  
ANISOU  377  CG  MET A  54     3986   3836   4227   -124     24     63       C  
ATOM    378  SD  MET A  54      36.337  12.408   2.834  1.00 38.74           S  
ANISOU  378  SD  MET A  54     4875   4704   5139   -117     48     63       S  
ATOM    379  CE  MET A  54      35.982  12.491   4.583  1.00 35.18           C  
ANISOU  379  CE  MET A  54     4453   4234   4679   -128     55     12       C  
ATOM    380  N   ALA A  55      37.817   9.236  -1.208  1.00 27.81           N  
ANISOU  380  N   ALA A  55     3463   3442   3661    -82      4    162       N  
ATOM    381  CA  ALA A  55      38.152   7.999  -1.957  1.00 26.28           C  
ANISOU  381  CA  ALA A  55     3270   3285   3430    -73     -8    172       C  
ATOM    382  C   ALA A  55      38.440   8.342  -3.392  1.00 27.47           C  
ANISOU  382  C   ALA A  55     3397   3450   3588    -64     -7    210       C  
ATOM    383  O   ALA A  55      38.766   7.494  -4.188  1.00 24.62           O  
ANISOU  383  O   ALA A  55     3034   3120   3200    -55    -15    222       O  
ATOM    384  CB  ALA A  55      37.052   6.991  -1.904  1.00 25.52           C  
ANISOU  384  CB  ALA A  55     3186   3202   3309    -66     -8    163       C  
ATOM    385  N   TYR A  56      38.394   9.615  -3.728  1.00 27.45           N  
ANISOU  385  N   TYR A  56     3377   3427   3624    -64      3    230       N  
ATOM    386  CA  TYR A  56      38.522   9.899  -5.126  1.00 32.33           C  
ANISOU  386  CA  TYR A  56     3973   4062   4245    -52      6    270       C  
ATOM    387  C   TYR A  56      37.510   9.089  -6.009  1.00 33.76           C  
ANISOU  387  C   TYR A  56     4154   4273   4398    -36      2    283       C  
ATOM    388  O   TYR A  56      37.806   8.794  -7.137  1.00 35.51           O  
ANISOU  388  O   TYR A  56     4365   4524   4603    -25     -1    308       O  
ATOM    389  CB  TYR A  56      39.979   9.699  -5.604  1.00 33.06           C  
ANISOU  389  CB  TYR A  56     4059   4172   4329    -54      0    281       C  
ATOM    390  CG  TYR A  56      40.332  10.822  -6.571  1.00 38.55           C  
ANISOU  390  CG  TYR A  56     4729   4861   5056    -49     11    321       C  
ATOM    391  CD1 TYR A  56      39.396  11.229  -7.549  1.00 37.57           C  
ANISOU  391  CD1 TYR A  56     4591   4744   4938    -34     19    354       C  
ATOM    392  CD2 TYR A  56      41.567  11.515  -6.504  1.00 38.91           C  
ANISOU  392  CD2 TYR A  56     4762   4892   5129    -58     14    329       C  
ATOM    393  CE1 TYR A  56      39.663  12.260  -8.420  1.00 37.17           C  
ANISOU  393  CE1 TYR A  56     4517   4688   4917    -28     31    394       C  
ATOM    394  CE2 TYR A  56      41.845  12.560  -7.401  1.00 36.59           C  
ANISOU  394  CE2 TYR A  56     4443   4589   4867    -53     27    369       C  
ATOM    395  CZ  TYR A  56      40.885  12.919  -8.352  1.00 37.98           C  
ANISOU  395  CZ  TYR A  56     4608   4774   5046    -37     36    402       C  
ATOM    396  OH  TYR A  56      41.067  13.979  -9.237  1.00 39.74           O  
ANISOU  396  OH  TYR A  56     4807   4990   5302    -30     51    446       O  
ATOM    397  N   SER A  57      36.333   8.744  -5.486  1.00 33.65           N  
ANISOU  397  N   SER A  57     4151   4253   4381    -35      4    264       N  
ATOM    398  CA  SER A  57      35.286   8.020  -6.237  1.00 32.62           C  
ANISOU  398  CA  SER A  57     4017   4146   4229    -21      0    272       C  
ATOM    399  C   SER A  57      34.163   8.865  -6.722  1.00 31.67           C  
ANISOU  399  C   SER A  57     3881   4014   4135    -12      8    294       C  
ATOM    400  O   SER A  57      34.085  10.026  -6.375  1.00 33.46           O  
ANISOU  400  O   SER A  57     4101   4211   4400    -17     20    301       O  
ATOM    401  CB  SER A  57      34.638   7.014  -5.310  1.00 35.51           C  
ANISOU  401  CB  SER A  57     4404   4511   4576    -25     -3    238       C  
ATOM    402  OG  SER A  57      35.551   5.942  -5.151  1.00 37.58           O  
ANISOU  402  OG  SER A  57     4679   4793   4807    -29    -15    223       O  
ATOM    403  N   ASN A  58      33.260   8.261  -7.486  1.00 31.53           N  
ANISOU  403  N   ASN A  58     3858   4021   4100      0      1    303       N  
ATOM    404  CA  ASN A  58      32.033   8.910  -7.952  1.00 30.70           C  
ANISOU  404  CA  ASN A  58     3737   3908   4018     10      7    322       C  
ATOM    405  C   ASN A  58      30.774   8.027  -7.952  1.00 29.87           C  
ANISOU  405  C   ASN A  58     3636   3814   3899     17      1    307       C  
ATOM    406  O   ASN A  58      30.162   7.709  -9.042  1.00 27.87           O  
ANISOU  406  O   ASN A  58     3369   3588   3632     31     -9    325       O  
ATOM    407  CB  ASN A  58      32.237   9.517  -9.328  1.00 29.15           C  
ANISOU  407  CB  ASN A  58     3519   3732   3824     24      5    366       C  
ATOM    408  CG  ASN A  58      31.153  10.520  -9.672  1.00 32.15           C  
ANISOU  408  CG  ASN A  58     3880   4095   4238     33     13    392       C  
ATOM    409  OD1 ASN A  58      30.520  11.088  -8.773  1.00 29.61           O  
ANISOU  409  OD1 ASN A  58     3561   3737   3950     26     25    377       O  
ATOM    410  ND2 ASN A  58      30.890  10.719 -11.005  1.00 33.52           N  
ANISOU  410  ND2 ASN A  58     4035   4296   4402     50      7    430       N  
ATOM    411  N   CYS A  59      30.389   7.620  -6.750  1.00 28.12           N  
ANISOU  411  N   CYS A  59     3432   3571   3681      6      6    273       N  
ATOM    412  CA  CYS A  59      29.245   6.738  -6.597  1.00 27.94           C  
ANISOU  412  CA  CYS A  59     3412   3554   3649     10      3    255       C  
ATOM    413  C   CYS A  59      28.145   7.399  -5.835  1.00 28.01           C  
ANISOU  413  C   CYS A  59     3420   3529   3694      8     19    247       C  
ATOM    414  O   CYS A  59      28.372   7.749  -4.677  1.00 26.08           O  
ANISOU  414  O   CYS A  59     3189   3255   3462     -3     32    226       O  
ATOM    415  CB  CYS A  59      29.615   5.458  -5.837  1.00 29.75           C  
ANISOU  415  CB  CYS A  59     3663   3790   3849      2     -1    222       C  
ATOM    416  SG  CYS A  59      30.892   4.412  -6.623  1.00 32.82           S  
ANISOU  416  SG  CYS A  59     4056   4219   4194      4    -18    224       S  
ATOM    417  N   LYS A  60      26.941   7.486  -6.421  1.00 28.12           N  
ANISOU  417  N   LYS A  60     3417   3546   3722     19     18    259       N  
ATOM    418  CA  LYS A  60      25.778   8.016  -5.687  1.00 29.57           C  
ANISOU  418  CA  LYS A  60     3597   3696   3942     17     34    250       C  
ATOM    419  C   LYS A  60      25.439   7.025  -4.663  1.00 28.74           C  
ANISOU  419  C   LYS A  60     3512   3584   3823      9     39    214       C  
ATOM    420  O   LYS A  60      25.471   5.816  -4.930  1.00 28.04           O  
ANISOU  420  O   LYS A  60     3429   3521   3704     11     26    204       O  
ATOM    421  CB  LYS A  60      24.523   8.129  -6.521  1.00 32.74           C  
ANISOU  421  CB  LYS A  60     3975   4104   4359     31     29    269       C  
ATOM    422  CG  LYS A  60      24.384   9.404  -7.299  1.00 40.13           C  
ANISOU  422  CG  LYS A  60     4888   5034   5325     41     31    307       C  
ATOM    423  CD  LYS A  60      23.285   9.222  -8.349  1.00 43.44           C  
ANISOU  423  CD  LYS A  60     5284   5474   5746     58     17    327       C  
ATOM    424  CE  LYS A  60      23.155  10.469  -9.234  1.00 44.78           C  
ANISOU  424  CE  LYS A  60     5430   5642   5943     70     18    371       C  
ATOM    425  NZ  LYS A  60      24.252  10.481 -10.252  1.00 45.53           N  
ANISOU  425  NZ  LYS A  60     5522   5770   6006     76      5    398       N  
ATOM    426  N   VAL A  61      25.123   7.533  -3.485  1.00 27.88           N  
ANISOU  426  N   VAL A  61     3414   3440   3737      0     59    196       N  
ATOM    427  CA  VAL A  61      24.635   6.711  -2.409  1.00 27.73           C  
ANISOU  427  CA  VAL A  61     3414   3411   3710     -5     69    164       C  
ATOM    428  C   VAL A  61      23.316   7.330  -1.933  1.00 29.06           C  
ANISOU  428  C   VAL A  61     3574   3549   3918     -3     89    160       C  
ATOM    429  O   VAL A  61      23.264   8.535  -1.640  1.00 30.11           O  
ANISOU  429  O   VAL A  61     3700   3654   4083     -5    103    166       O  
ATOM    430  CB  VAL A  61      25.602   6.720  -1.216  1.00 27.29           C  
ANISOU  430  CB  VAL A  61     3385   3343   3641    -19     77    141       C  
ATOM    431  CG1 VAL A  61      25.257   5.561  -0.291  1.00 25.41           C  
ANISOU  431  CG1 VAL A  61     3167   3105   3381    -24     83    113       C  
ATOM    432  CG2 VAL A  61      27.053   6.600  -1.721  1.00 28.53           C  
ANISOU  432  CG2 VAL A  61     3544   3522   3771    -22     60    150       C  
ATOM    433  N   SER A  62      22.257   6.542  -1.869  1.00 27.47           N  
ANISOU  433  N   SER A  62     3368   3349   3718      0     91    151       N  
ATOM    434  CA  SER A  62      21.016   7.095  -1.397  1.00 27.72           C  
ANISOU  434  CA  SER A  62     3390   3351   3789      2    112    146       C  
ATOM    435  C   SER A  62      20.330   6.125  -0.469  1.00 26.70           C  
ANISOU  435  C   SER A  62     3276   3214   3654     -1    125    119       C  
ATOM    436  O   SER A  62      20.627   4.914  -0.440  1.00 25.59           O  
ANISOU  436  O   SER A  62     3146   3093   3481     -3    115    108       O  
ATOM    437  CB  SER A  62      20.108   7.341  -2.589  1.00 27.80           C  
ANISOU  437  CB  SER A  62     3369   3371   3822     16    100    173       C  
ATOM    438  OG  SER A  62      19.957   6.116  -3.255  1.00 28.63           O  
ANISOU  438  OG  SER A  62     3470   3507   3900     21     80    171       O  
ATOM    439  N   GLY A  63      19.428   6.653   0.311  1.00 25.64           N  
ANISOU  439  N   GLY A  63     3141   3049   3552     -3    150    109       N  
ATOM    440  CA  GLY A  63      18.589   5.806   1.111  1.00 26.51           C  
ANISOU  440  CA  GLY A  63     3259   3148   3662     -5    167     88       C  
ATOM    441  C   GLY A  63      17.282   5.511   0.405  1.00 28.57           C  
ANISOU  441  C   GLY A  63     3492   3410   3951      4    164     98       C  
ATOM    442  O   GLY A  63      16.917   6.117  -0.656  1.00 28.93           O  
ANISOU  442  O   GLY A  63     3511   3461   4018     14    150    122       O  
ATOM    443  N   SER A  64      16.589   4.506   0.950  1.00 30.07           N  
ANISOU  443  N   SER A  64     3688   3596   4140      2    175     81       N  
ATOM    444  CA  SER A  64      15.315   4.133   0.415  1.00 29.24           C  
ANISOU  444  CA  SER A  64     3557   3490   4063     11    173     85       C  
ATOM    445  C   SER A  64      14.427   3.410   1.357  1.00 29.52           C  
ANISOU  445  C   SER A  64     3598   3505   4110      7    198     65       C  
ATOM    446  O   SER A  64      14.886   2.565   2.121  1.00 30.09           O  
ANISOU  446  O   SER A  64     3695   3580   4154      0    206     49       O  
ATOM    447  CB  SER A  64      15.449   3.324  -0.851  1.00 28.32           C  
ANISOU  447  CB  SER A  64     3423   3407   3928     17    139     96       C  
ATOM    448  OG  SER A  64      14.154   3.091  -1.325  1.00 27.09           O  
ANISOU  448  OG  SER A  64     3239   3247   3804     25    137     99       O  
ATOM    449  N   ASN A  65      13.135   3.707   1.232  1.00 29.63           N  
ANISOU  449  N   ASN A  65     3587   3500   4168     13    210     69       N  
ATOM    450  CA  ASN A  65      12.095   2.967   1.929  1.00 31.26           C  
ANISOU  450  CA  ASN A  65     3792   3689   4396     12    233     53       C  
ATOM    451  C   ASN A  65      11.076   2.292   0.989  1.00 30.49           C  
ANISOU  451  C   ASN A  65     3661   3601   4323     20    216     59       C  
ATOM    452  O   ASN A  65      10.072   1.809   1.439  1.00 31.55           O  
ANISOU  452  O   ASN A  65     3785   3717   4485     19    235     49       O  
ATOM    453  CB  ASN A  65      11.389   3.888   2.973  1.00 33.02           C  
ANISOU  453  CB  ASN A  65     4018   3874   4653     10    272     45       C  
ATOM    454  CG  ASN A  65      12.359   4.410   4.079  1.00 34.91           C  
ANISOU  454  CG  ASN A  65     4295   4104   4866      1    291     32       C  
ATOM    455  OD1 ASN A  65      12.206   5.546   4.564  1.00 39.22           O  
ANISOU  455  OD1 ASN A  65     4842   4626   5434      1    312     30       O  
ATOM    456  ND2 ASN A  65      13.376   3.606   4.455  1.00 31.91           N  
ANISOU  456  ND2 ASN A  65     3942   3743   4437     -4    283     23       N  
ATOM    457  N   THR A  66      11.338   2.254  -0.304  1.00 30.85           N  
ANISOU  457  N   THR A  66     3687   3674   4358     26    180     75       N  
ATOM    458  CA  THR A  66      10.457   1.601  -1.308  1.00 31.51           C  
ANISOU  458  CA  THR A  66     3737   3773   4461     34    157     78       C  
ATOM    459  C   THR A  66      11.201   0.583  -2.205  1.00 31.06           C  
ANISOU  459  C   THR A  66     3681   3754   4363     35    122     76       C  
ATOM    460  O   THR A  66      12.275   0.881  -2.762  1.00 29.48           O  
ANISOU  460  O   THR A  66     3492   3579   4130     36    103     87       O  
ATOM    461  CB  THR A  66       9.750   2.601  -2.243  1.00 33.47           C  
ANISOU  461  CB  THR A  66     3952   4021   4743     46    142    101       C  
ATOM    462  OG1 THR A  66       9.092   1.876  -3.296  1.00 33.49           O  
ANISOU  462  OG1 THR A  66     3925   4046   4753     53    113    102       O  
ATOM    463  CG2 THR A  66      10.792   3.613  -2.881  1.00 34.04           C  
ANISOU  463  CG2 THR A  66     4029   4110   4791     50    125    124       C  
ATOM    464  N   TYR A  67      10.625  -0.611  -2.327  1.00 30.44           N  
ANISOU  464  N   TYR A  67     3592   3681   4292     34    117     60       N  
ATOM    465  CA  TYR A  67      11.141  -1.633  -3.222  1.00 31.07           C  
ANISOU  465  CA  TYR A  67     3668   3794   4341     35     85     54       C  
ATOM    466  C   TYR A  67      11.073  -1.160  -4.691  1.00 30.54           C  
ANISOU  466  C   TYR A  67     3575   3758   4270     47     49     72       C  
ATOM    467  O   TYR A  67      11.623  -1.795  -5.578  1.00 29.06           O  
ANISOU  467  O   TYR A  67     3385   3604   4052     50     20     70       O  
ATOM    468  CB  TYR A  67      10.383  -2.972  -3.065  1.00 31.74           C  
ANISOU  468  CB  TYR A  67     3742   3873   4443     32     89     33       C  
ATOM    469  CG  TYR A  67      10.682  -3.704  -1.807  1.00 33.54           C  
ANISOU  469  CG  TYR A  67     3998   4082   4664     22    119     17       C  
ATOM    470  CD1 TYR A  67      11.978  -4.177  -1.554  1.00 35.84           C  
ANISOU  470  CD1 TYR A  67     4319   4388   4909     16    115     14       C  
ATOM    471  CD2 TYR A  67       9.683  -3.950  -0.854  1.00 35.32           C  
ANISOU  471  CD2 TYR A  67     4220   4273   4927     18    152      8       C  
ATOM    472  CE1 TYR A  67      12.300  -4.864  -0.363  1.00 35.74           C  
ANISOU  472  CE1 TYR A  67     4334   4359   4887      8    142      2       C  
ATOM    473  CE2 TYR A  67       9.985  -4.633   0.346  1.00 36.75           C  
ANISOU  473  CE2 TYR A  67     4429   4437   5096     10    182     -2       C  
ATOM    474  CZ  TYR A  67      11.307  -5.102   0.565  1.00 36.04           C  
ANISOU  474  CZ  TYR A  67     4369   4365   4958      5    175     -4       C  
ATOM    475  OH  TYR A  67      11.674  -5.759   1.702  1.00 39.71           O  
ANISOU  475  OH  TYR A  67     4862   4817   5409     -1    201    -12       O  
ATOM    476  N   ASP A  68      10.444  -0.017  -4.955  1.00 31.86           N  
ANISOU  476  N   ASP A  68     3723   3915   4466     55     50     92       N  
ATOM    477  CA  ASP A  68      10.457   0.523  -6.337  1.00 31.02           C  
ANISOU  477  CA  ASP A  68     3593   3839   4353     67     16    114       C  
ATOM    478  C   ASP A  68      11.898   0.887  -6.724  1.00 28.61           C  
ANISOU  478  C   ASP A  68     3310   3559   4001     67      4    128       C  
ATOM    479  O   ASP A  68      12.260   0.932  -7.915  1.00 28.29           O  
ANISOU  479  O   ASP A  68     3257   3554   3935     76    -26    142       O  
ATOM    480  CB  ASP A  68       9.586   1.771  -6.439  1.00 33.48           C  
ANISOU  480  CB  ASP A  68     3881   4131   4707     76     23    136       C  
ATOM    481  CG  ASP A  68       8.102   1.505  -6.139  1.00 36.69           C  
ANISOU  481  CG  ASP A  68     4262   4513   5166     77     34    125       C  
ATOM    482  OD1 ASP A  68       7.642   0.338  -6.042  1.00 40.73           O  
ANISOU  482  OD1 ASP A  68     4768   5026   5682     73     31    102       O  
ATOM    483  OD2 ASP A  68       7.363   2.495  -6.026  1.00 39.95           O  
ANISOU  483  OD2 ASP A  68     4657   4902   5618     83     46    141       O  
ATOM    484  N   ASP A  69      12.751   1.088  -5.721  1.00 26.91           N  
ANISOU  484  N   ASP A  69     3125   3326   3770     57     28    123       N  
ATOM    485  CA  ASP A  69      14.132   1.490  -6.023  1.00 26.95           C  
ANISOU  485  CA  ASP A  69     3150   3352   3737     56     18    136       C  
ATOM    486  C   ASP A  69      15.000   0.346  -6.592  1.00 27.48           C  
ANISOU  486  C   ASP A  69     3226   3454   3759     55     -3    124       C  
ATOM    487  O   ASP A  69      16.118   0.606  -7.124  1.00 27.25           O  
ANISOU  487  O   ASP A  69     3208   3449   3697     56    -16    137       O  
ATOM    488  CB  ASP A  69      14.750   2.189  -4.790  1.00 29.00           C  
ANISOU  488  CB  ASP A  69     3437   3582   3999     46     49    134       C  
ATOM    489  CG  ASP A  69      14.242   3.661  -4.657  1.00 33.48           C  
ANISOU  489  CG  ASP A  69     3992   4124   4605     51     64    154       C  
ATOM    490  OD1 ASP A  69      13.904   4.256  -5.721  1.00 34.25           O  
ANISOU  490  OD1 ASP A  69     4063   4235   4713     63     45    178       O  
ATOM    491  OD2 ASP A  69      14.091   4.199  -3.540  1.00 33.59           O  
ANISOU  491  OD2 ASP A  69     4019   4103   4639     44     94    145       O  
ATOM    492  N   LEU A  70      14.501  -0.902  -6.471  1.00 25.42           N  
ANISOU  492  N   LEU A  70     2962   3194   3500     52     -6    100       N  
ATOM    493  CA  LEU A  70      15.057  -2.030  -7.218  1.00 26.91           C  
ANISOU  493  CA  LEU A  70     3151   3417   3655     53    -30     87       C  
ATOM    494  C   LEU A  70      15.090  -1.868  -8.734  1.00 29.15           C  
ANISOU  494  C   LEU A  70     3413   3741   3921     65    -65    102       C  
ATOM    495  O   LEU A  70      15.782  -2.654  -9.379  1.00 30.68           O  
ANISOU  495  O   LEU A  70     3611   3965   4080     67    -84     92       O  
ATOM    496  CB  LEU A  70      14.339  -3.335  -6.916  1.00 24.74           C  
ANISOU  496  CB  LEU A  70     2870   3134   3395     48    -28     59       C  
ATOM    497  CG  LEU A  70      14.648  -3.799  -5.518  1.00 23.95           C  
ANISOU  497  CG  LEU A  70     2797   3005   3297     36      2     44       C  
ATOM    498  CD1 LEU A  70      13.598  -4.782  -4.983  1.00 24.49           C  
ANISOU  498  CD1 LEU A  70     2855   3052   3398     32     16     23       C  
ATOM    499  CD2 LEU A  70      16.021  -4.419  -5.528  1.00 22.77           C  
ANISOU  499  CD2 LEU A  70     2671   2875   3104     32     -4     39       C  
ATOM    500  N   ALA A  71      14.357  -0.908  -9.319  1.00 31.07           N  
ANISOU  500  N   ALA A  71     3633   3985   4186     76    -73    124       N  
ATOM    501  CA  ALA A  71      14.360  -0.798 -10.826  1.00 33.56           C  
ANISOU  501  CA  ALA A  71     3926   4343   4479     90   -108    139       C  
ATOM    502  C   ALA A  71      15.817  -0.534 -11.308  1.00 34.52           C  
ANISOU  502  C   ALA A  71     4068   4493   4555     92   -115    155       C  
ATOM    503  O   ALA A  71      16.467   0.327 -10.761  1.00 37.40           O  
ANISOU  503  O   ALA A  71     4448   4839   4920     87    -97    172       O  
ATOM    504  CB  ALA A  71      13.432   0.313 -11.299  1.00 31.84           C  
ANISOU  504  CB  ALA A  71     3682   4121   4292    102   -114    167       C  
ATOM    505  N   GLY A  72      16.312  -1.325 -12.265  1.00 36.24           N  
ANISOU  505  N   GLY A  72     4283   4750   4734     97   -140    146       N  
ATOM    506  CA  GLY A  72      17.638  -1.157 -12.902  1.00 32.09           C  
ANISOU  506  CA  GLY A  72     3771   4255   4164    100   -149    161       C  
ATOM    507  C   GLY A  72      18.787  -1.700 -12.055  1.00 31.82           C  
ANISOU  507  C   GLY A  72     3767   4210   4112     87   -131    145       C  
ATOM    508  O   GLY A  72      19.962  -1.539 -12.420  1.00 31.31           O  
ANISOU  508  O   GLY A  72     3715   4165   4015     88   -134    157       O  
ATOM    509  N   ALA A  73      18.493  -2.308 -10.907  1.00 30.31           N  
ANISOU  509  N   ALA A  73     3587   3986   3941     75   -113    121       N  
ATOM    510  CA  ALA A  73      19.554  -2.833 -10.062  1.00 29.55           C  
ANISOU  510  CA  ALA A  73     3519   3880   3828     63    -98    107       C  
ATOM    511  C   ALA A  73      20.401  -3.899 -10.860  1.00 31.26           C  
ANISOU  511  C   ALA A  73     3739   4133   4005     66   -117     93       C  
ATOM    512  O   ALA A  73      19.867  -4.648 -11.668  1.00 31.11           O  
ANISOU  512  O   ALA A  73     3703   4136   3981     72   -137     78       O  
ATOM    513  CB  ALA A  73      18.985  -3.412  -8.778  1.00 29.14           C  
ANISOU  513  CB  ALA A  73     3477   3791   3803     52    -75     85       C  
ATOM    514  N   ASP A  74      21.729  -3.874 -10.685  1.00 30.42           N  
ANISOU  514  N   ASP A  74     3653   4033   3871     61   -112     98       N  
ATOM    515  CA  ASP A  74      22.623  -4.794 -11.353  1.00 27.70           C  
ANISOU  515  CA  ASP A  74     3312   3718   3491     63   -126     86       C  
ATOM    516  C   ASP A  74      22.896  -5.944 -10.430  1.00 26.46           C  
ANISOU  516  C   ASP A  74     3171   3544   3338     53   -115     58       C  
ATOM    517  O   ASP A  74      23.049  -7.110 -10.871  1.00 23.99           O  
ANISOU  517  O   ASP A  74     2855   3248   3011     54   -126     35       O  
ATOM    518  CB  ASP A  74      23.879  -4.048 -11.781  1.00 29.85           C  
ANISOU  518  CB  ASP A  74     3593   4009   3736     66   -127    110       C  
ATOM    519  CG  ASP A  74      23.641  -3.288 -13.093  1.00 32.30           C  
ANISOU  519  CG  ASP A  74     3885   4352   4035     81   -144    136       C  
ATOM    520  OD1 ASP A  74      23.230  -3.969 -14.003  1.00 31.37           O  
ANISOU  520  OD1 ASP A  74     3753   4263   3903     89   -164    123       O  
ATOM    521  OD2 ASP A  74      23.740  -2.035 -13.206  1.00 33.63           O  
ANISOU  521  OD2 ASP A  74     4050   4516   4211     85   -139    167       O  
ATOM    522  N   VAL A  75      22.945  -5.590  -9.137  1.00 24.66           N  
ANISOU  522  N   VAL A  75     2960   3280   3127     43    -92     60       N  
ATOM    523  CA  VAL A  75      23.262  -6.508  -8.098  1.00 23.39           C  
ANISOU  523  CA  VAL A  75     2817   3099   2969     33    -78     40       C  
ATOM    524  C   VAL A  75      22.342  -6.156  -6.928  1.00 22.32           C  
ANISOU  524  C   VAL A  75     2687   2927   2867     26    -56     39       C  
ATOM    525  O   VAL A  75      22.156  -4.957  -6.644  1.00 21.58           O  
ANISOU  525  O   VAL A  75     2594   2819   2785     26    -47     57       O  
ATOM    526  CB  VAL A  75      24.703  -6.278  -7.642  1.00 23.64           C  
ANISOU  526  CB  VAL A  75     2871   3132   2977     27    -72     49       C  
ATOM    527  CG1 VAL A  75      24.981  -6.961  -6.298  1.00 22.46           C  
ANISOU  527  CG1 VAL A  75     2742   2956   2832     17    -55     35       C  
ATOM    528  CG2 VAL A  75      25.647  -6.757  -8.716  1.00 24.57           C  
ANISOU  528  CG2 VAL A  75     2985   3286   3063     33    -91     49       C  
ATOM    529  N   VAL A  76      21.742  -7.173  -6.284  1.00 21.06           N  
ANISOU  529  N   VAL A  76     2528   2748   2723     21    -46     18       N  
ATOM    530  CA  VAL A  76      20.946  -6.944  -5.048  1.00 19.97           C  
ANISOU  530  CA  VAL A  76     2397   2573   2614     15    -20     16       C  
ATOM    531  C   VAL A  76      21.507  -7.758  -3.882  1.00 19.02           C  
ANISOU  531  C   VAL A  76     2302   2436   2487      7     -3      5       C  
ATOM    532  O   VAL A  76      21.772  -8.959  -4.015  1.00 19.98           O  
ANISOU  532  O   VAL A  76     2423   2565   2601      6     -8     -9       O  
ATOM    533  CB  VAL A  76      19.451  -7.350  -5.288  1.00 20.26           C  
ANISOU  533  CB  VAL A  76     2410   2600   2686     18    -20      5       C  
ATOM    534  CG1 VAL A  76      18.589  -7.191  -4.061  1.00 19.48           C  
ANISOU  534  CG1 VAL A  76     2317   2464   2619     12      8      2       C  
ATOM    535  CG2 VAL A  76      18.880  -6.656  -6.516  1.00 20.18           C  
ANISOU  535  CG2 VAL A  76     2374   2611   2682     28    -41     16       C  
ATOM    536  N   ILE A  77      21.651  -7.168  -2.731  1.00 18.61           N  
ANISOU  536  N   ILE A  77     2270   2362   2437      1     18     11       N  
ATOM    537  CA  ILE A  77      22.246  -7.918  -1.625  1.00 18.51           C  
ANISOU  537  CA  ILE A  77     2281   2337   2413     -5     32      3       C  
ATOM    538  C   ILE A  77      21.265  -7.892  -0.509  1.00 18.24           C  
ANISOU  538  C   ILE A  77     2253   2272   2403     -9     60     -1       C  
ATOM    539  O   ILE A  77      20.871  -6.836  -0.081  1.00 17.72           O  
ANISOU  539  O   ILE A  77     2190   2192   2348    -10     73      6       O  
ATOM    540  CB  ILE A  77      23.581  -7.304  -1.138  1.00 18.88           C  
ANISOU  540  CB  ILE A  77     2352   2390   2432     -9     32     12       C  
ATOM    541  CG1 ILE A  77      24.643  -7.617  -2.200  1.00 19.39           C  
ANISOU  541  CG1 ILE A  77     2411   2484   2471     -5      7     15       C  
ATOM    542  CG2 ILE A  77      24.000  -7.900   0.245  1.00 18.71           C  
ANISOU  542  CG2 ILE A  77     2357   2351   2399    -16     50      6       C  
ATOM    543  CD1 ILE A  77      25.587  -6.494  -2.554  1.00 19.70           C  
ANISOU  543  CD1 ILE A  77     2454   2536   2493     -5     -1     31       C  
ATOM    544  N   VAL A  78      20.823  -9.076  -0.104  1.00 18.68           N  
ANISOU  544  N   VAL A  78     2308   2316   2470    -10     70    -12       N  
ATOM    545  CA  VAL A  78      19.828  -9.142   0.876  1.00 19.16           C  
ANISOU  545  CA  VAL A  78     2373   2349   2557    -13     98    -15       C  
ATOM    546  C   VAL A  78      20.406  -9.458   2.256  1.00 19.84           C  
ANISOU  546  C   VAL A  78     2490   2422   2625    -18    120    -14       C  
ATOM    547  O   VAL A  78      20.780 -10.571   2.551  1.00 19.58           O  
ANISOU  547  O   VAL A  78     2465   2389   2584    -19    122    -18       O  
ATOM    548  CB  VAL A  78      18.741 -10.095   0.439  1.00 19.31           C  
ANISOU  548  CB  VAL A  78     2367   2360   2608    -11     99    -27       C  
ATOM    549  CG1 VAL A  78      17.599  -9.956   1.422  1.00 19.70           C  
ANISOU  549  CG1 VAL A  78     2416   2378   2688    -13    131    -27       C  
ATOM    550  CG2 VAL A  78      18.242  -9.685  -0.962  1.00 18.98           C  
ANISOU  550  CG2 VAL A  78     2295   2336   2578     -5     73    -28       C  
ATOM    551  N   THR A  79      20.453  -8.478   3.132  1.00 21.34           N  
ANISOU  551  N   THR A  79     2698   2600   2809    -21    137     -9       N  
ATOM    552  CA  THR A  79      20.845  -8.785   4.543  1.00 22.10           C  
ANISOU  552  CA  THR A  79     2825   2684   2887    -25    159     -9       C  
ATOM    553  C   THR A  79      19.638  -8.723   5.500  1.00 24.21           C  
ANISOU  553  C   THR A  79     3095   2923   3179    -26    194    -12       C  
ATOM    554  O   THR A  79      19.741  -9.029   6.690  1.00 23.73           O  
ANISOU  554  O   THR A  79     3058   2852   3105    -27    216    -11       O  
ATOM    555  CB  THR A  79      21.940  -7.804   5.007  1.00 22.04           C  
ANISOU  555  CB  THR A  79     2841   2685   2848    -28    153     -5       C  
ATOM    556  OG1 THR A  79      21.490  -6.397   4.830  1.00 22.27           O  
ANISOU  556  OG1 THR A  79     2862   2707   2893    -28    157     -3       O  
ATOM    557  CG2 THR A  79      23.232  -8.044   4.174  1.00 22.12           C  
ANISOU  557  CG2 THR A  79     2849   2721   2833    -28    122     -1       C  
ATOM    558  N   ALA A  80      18.490  -8.259   5.024  1.00 26.58           N  
ANISOU  558  N   ALA A  80     3372   3213   3515    -23    199    -13       N  
ATOM    559  CA  ALA A  80      17.467  -7.890   6.028  1.00 27.94           C  
ANISOU  559  CA  ALA A  80     3548   3357   3708    -24    235    -15       C  
ATOM    560  C   ALA A  80      16.819  -9.172   6.500  1.00 28.53           C  
ANISOU  560  C   ALA A  80     3621   3417   3800    -24    255    -17       C  
ATOM    561  O   ALA A  80      16.792 -10.134   5.758  1.00 27.77           O  
ANISOU  561  O   ALA A  80     3507   3328   3714    -22    239    -20       O  
ATOM    562  CB  ALA A  80      16.430  -6.978   5.437  1.00 28.24           C  
ANISOU  562  CB  ALA A  80     3561   3385   3782    -21    236    -15       C  
ATOM    563  N   GLY A  81      16.351  -9.199   7.752  1.00 28.94           N  
ANISOU  563  N   GLY A  81     3691   3450   3854    -25    291    -17       N  
ATOM    564  CA  GLY A  81      15.508 -10.326   8.197  1.00 29.15           C  
ANISOU  564  CA  GLY A  81     3710   3457   3906    -24    316    -16       C  
ATOM    565  C   GLY A  81      15.540 -10.312   9.693  1.00 30.16           C  
ANISOU  565  C   GLY A  81     3870   3573   4015    -24    352    -12       C  
ATOM    566  O   GLY A  81      16.356  -9.615  10.240  1.00 29.20           O  
ANISOU  566  O   GLY A  81     3774   3462   3856    -26    350    -11       O  
ATOM    567  N   PHE A  82      14.645 -11.070  10.330  1.00 31.67           N  
ANISOU  567  N   PHE A  82     4058   3742   4231    -23    385     -8       N  
ATOM    568  CA  PHE A  82      14.702 -11.353  11.751  1.00 31.79           C  
ANISOU  568  CA  PHE A  82     4104   3749   4224    -22    421     -1       C  
ATOM    569  C   PHE A  82      15.899 -12.191  12.146  1.00 32.16           C  
ANISOU  569  C   PHE A  82     4175   3812   4229    -22    409      7       C  
ATOM    570  O   PHE A  82      16.324 -13.015  11.409  1.00 34.03           O  
ANISOU  570  O   PHE A  82     4399   4058   4472    -22    386      8       O  
ATOM    571  CB  PHE A  82      13.399 -12.018  12.154  1.00 31.82           C  
ANISOU  571  CB  PHE A  82     4093   3725   4272    -20    458      2       C  
ATOM    572  CG  PHE A  82      12.226 -11.113  11.953  1.00 32.67           C  
ANISOU  572  CG  PHE A  82     4179   3815   4419    -20    473     -5       C  
ATOM    573  CD1 PHE A  82      11.910 -10.149  12.927  1.00 31.37           C  
ANISOU  573  CD1 PHE A  82     4034   3640   4243    -20    504     -7       C  
ATOM    574  CD2 PHE A  82      11.537 -11.112  10.738  1.00 31.44           C  
ANISOU  574  CD2 PHE A  82     3984   3654   4308    -21    453    -12       C  
ATOM    575  CE1 PHE A  82      10.875  -9.259  12.733  1.00 31.35           C  
ANISOU  575  CE1 PHE A  82     4011   3620   4278    -19    518    -14       C  
ATOM    576  CE2 PHE A  82      10.511 -10.204  10.528  1.00 32.96           C  
ANISOU  576  CE2 PHE A  82     4154   3830   4535    -20    464    -17       C  
ATOM    577  CZ  PHE A  82      10.180  -9.272  11.526  1.00 31.54           C  
ANISOU  577  CZ  PHE A  82     3994   3638   4349    -19    497    -18       C  
ATOM    578  N   THR A  83      16.439 -11.970  13.316  1.00 32.42           N  
ANISOU  578  N   THR A  83     4243   3851   4222    -21    426     12       N  
ATOM    579  CA  THR A  83      17.588 -12.746  13.732  1.00 33.32           C  
ANISOU  579  CA  THR A  83     4380   3982   4297    -19    414     22       C  
ATOM    580  C   THR A  83      17.330 -13.230  15.152  1.00 36.20           C  
ANISOU  580  C   THR A  83     4772   4338   4645    -15    454     35       C  
ATOM    581  O   THR A  83      17.838 -14.269  15.530  1.00 39.09           O  
ANISOU  581  O   THR A  83     5148   4707   4995    -12    455     49       O  
ATOM    582  CB  THR A  83      18.939 -11.969  13.652  1.00 31.40           C  
ANISOU  582  CB  THR A  83     4156   3764   4008    -22    381     17       C  
ATOM    583  OG1 THR A  83      18.759 -10.659  14.194  1.00 31.47           O  
ANISOU  583  OG1 THR A  83     4180   3772   4004    -23    393      7       O  
ATOM    584  CG2 THR A  83      19.477 -11.797  12.189  1.00 28.93           C  
ANISOU  584  CG2 THR A  83     3819   3466   3706    -24    339     10       C  
ATOM    585  N   LYS A  84      16.507 -12.525  15.919  1.00 36.60           N  
ANISOU  585  N   LYS A  84     4831   4374   4699    -14    488     31       N  
ATOM    586  CA  LYS A  84      16.254 -12.897  17.330  1.00 36.62           C  
ANISOU  586  CA  LYS A  84     4862   4371   4679     -9    529     44       C  
ATOM    587  C   LYS A  84      14.749 -12.806  17.549  1.00 36.68           C  
ANISOU  587  C   LYS A  84     4853   4350   4733     -8    571     42       C  
ATOM    588  O   LYS A  84      14.006 -12.539  16.587  1.00 32.87           O  
ANISOU  588  O   LYS A  84     4337   3854   4298    -11    563     33       O  
ATOM    589  CB  LYS A  84      17.032 -11.987  18.299  1.00 34.71           C  
ANISOU  589  CB  LYS A  84     4658   4148   4379     -9    529     37       C  
ATOM    590  CG  LYS A  84      17.063 -10.496  17.878  1.00 35.28           C  
ANISOU  590  CG  LYS A  84     4727   4224   4454    -14    513     15       C  
ATOM    591  CD  LYS A  84      16.064  -9.613  18.643  1.00 36.69           C  
ANISOU  591  CD  LYS A  84     4913   4386   4642    -13    554      4       C  
ATOM    592  CE  LYS A  84      15.749  -8.300  17.933  1.00 34.21           C  
ANISOU  592  CE  LYS A  84     4580   4064   4353    -18    541    -14       C  
ATOM    593  NZ  LYS A  84      14.370  -7.701  18.097  1.00 31.04           N  
ANISOU  593  NZ  LYS A  84     4164   3636   3994    -17    579    -21       N  
ATOM    594  N   ALA A  85      14.309 -13.018  18.798  1.00 36.30           N  
ANISOU  594  N   ALA A  85     4828   4294   4670     -3    615     53       N  
ATOM    595  CA  ALA A  85      12.911 -12.780  19.175  1.00 39.11           C  
ANISOU  595  CA  ALA A  85     5171   4622   5065     -1    660     51       C  
ATOM    596  C   ALA A  85      12.589 -11.338  18.841  1.00 40.15           C  
ANISOU  596  C   ALA A  85     5296   4751   5206     -5    654     29       C  
ATOM    597  O   ALA A  85      13.293 -10.454  19.298  1.00 42.75           O  
ANISOU  597  O   ALA A  85     5652   5098   5492     -6    645     18       O  
ATOM    598  CB  ALA A  85      12.702 -13.019  20.670  1.00 39.76           C  
ANISOU  598  CB  ALA A  85     5288   4703   5116      4    708     65       C  
ATOM    599  N   PRO A  86      11.564 -11.100  18.018  1.00 37.31           N  
ANISOU  599  N   PRO A  86     4899   4371   4905     -8    656     22       N  
ATOM    600  CA  PRO A  86      11.244  -9.788  17.528  1.00 37.71           C  
ANISOU  600  CA  PRO A  86     4937   4417   4972    -11    646      3       C  
ATOM    601  C   PRO A  86      10.848  -8.794  18.597  1.00 38.84           C  
ANISOU  601  C   PRO A  86     5103   4553   5100     -9    684     -5       C  
ATOM    602  O   PRO A  86      11.169  -7.587  18.479  1.00 36.04           O  
ANISOU  602  O   PRO A  86     4754   4205   4733    -11    670    -21       O  
ATOM    603  CB  PRO A  86      10.072 -10.043  16.587  1.00 38.18           C  
ANISOU  603  CB  PRO A  86     4951   4454   5102    -11    649      3       C  
ATOM    604  CG  PRO A  86      10.329 -11.413  16.095  1.00 37.73           C  
ANISOU  604  CG  PRO A  86     4881   4400   5054    -12    632     15       C  
ATOM    605  CD  PRO A  86      10.863 -12.150  17.267  1.00 39.01           C  
ANISOU  605  CD  PRO A  86     5078   4568   5174     -8    656     30       C  
ATOM    606  N   GLY A  87      10.150  -9.294  19.623  1.00 38.53           N  
ANISOU  606  N   GLY A  87     5076   4500   5062     -4    733      3       N  
ATOM    607  CA  GLY A  87       9.723  -8.455  20.716  1.00 39.00           C  
ANISOU  607  CA  GLY A  87     5158   4552   5105     -1    774     -6       C  
ATOM    608  C   GLY A  87       9.890  -9.125  22.049  1.00 38.54           C  
ANISOU  608  C   GLY A  87     5137   4503   5004      4    810      7       C  
ATOM    609  O   GLY A  87      10.101 -10.352  22.132  1.00 39.72           O  
ANISOU  609  O   GLY A  87     5288   4655   5148      7    811     29       O  
ATOM    610  N   LYS A  88       9.835  -8.291  23.079  1.00 37.58           N  
ANISOU  610  N   LYS A  88     5045   4384   4848      7    839     -5       N  
ATOM    611  CA  LYS A  88       9.692  -8.730  24.473  1.00 40.76           C  
ANISOU  611  CA  LYS A  88     5482   4792   5212     15    886      5       C  
ATOM    612  C   LYS A  88       8.552  -9.785  24.650  1.00 41.79           C  
ANISOU  612  C   LYS A  88     5592   4896   5388     20    931     29       C  
ATOM    613  O   LYS A  88       8.708 -10.815  25.320  1.00 39.19           O  
ANISOU  613  O   LYS A  88     5281   4573   5036     26    951     53       O  
ATOM    614  CB  LYS A  88       9.374  -7.513  25.304  1.00 39.81           C  
ANISOU  614  CB  LYS A  88     5383   4670   5072     17    916    -17       C  
ATOM    615  CG  LYS A  88       9.002  -7.877  26.704  1.00 42.68           C  
ANISOU  615  CG  LYS A  88     5779   5036   5401     26    971     -7       C  
ATOM    616  CD  LYS A  88      10.136  -8.546  27.437  1.00 39.62           C  
ANISOU  616  CD  LYS A  88     5430   4682   4940     30    957      6       C  
ATOM    617  CE  LYS A  88       9.894  -8.302  28.909  1.00 39.57           C  
ANISOU  617  CE  LYS A  88     5463   4685   4885     39   1007      3       C  
ATOM    618  NZ  LYS A  88      10.401  -9.505  29.561  1.00 37.70           N  
ANISOU  618  NZ  LYS A  88     5250   4467   4605     47   1013     35       N  
ATOM    619  N   SER A  89       7.445  -9.530  23.959  1.00 43.46           N  
ANISOU  619  N   SER A  89     5764   5077   5669     17    942     23       N  
ATOM    620  CA  SER A  89       6.290 -10.396  23.998  1.00 47.48           C  
ANISOU  620  CA  SER A  89     6248   5558   6233     20    982     41       C  
ATOM    621  C   SER A  89       6.555 -11.803  23.460  1.00 49.37           C  
ANISOU  621  C   SER A  89     6471   5797   6490     19    963     64       C  
ATOM    622  O   SER A  89       5.915 -12.741  23.911  1.00 51.48           O  
ANISOU  622  O   SER A  89     6732   6047   6781     24   1002     85       O  
ATOM    623  CB  SER A  89       5.093  -9.728  23.307  1.00 49.93           C  
ANISOU  623  CB  SER A  89     6516   5838   6616     17    993     26       C  
ATOM    624  OG  SER A  89       5.328  -9.482  21.930  1.00 50.27           O  
ANISOU  624  OG  SER A  89     6527   5883   6690     10    939     17       O  
ATOM    625  N   ASP A  90       7.509 -11.983  22.550  1.00 46.71           N  
ANISOU  625  N   ASP A  90     6127   5478   6141     14    906     61       N  
ATOM    626  CA  ASP A  90       7.660 -13.298  21.964  1.00 48.62           C  
ANISOU  626  CA  ASP A  90     6348   5715   6408     13    889     79       C  
ATOM    627  C   ASP A  90       8.323 -14.265  22.930  1.00 52.57           C  
ANISOU  627  C   ASP A  90     6882   6229   6861     20    906    104       C  
ATOM    628  O   ASP A  90       9.543 -14.404  22.999  1.00 53.07           O  
ANISOU  628  O   ASP A  90     6971   6321   6872     20    873    107       O  
ATOM    629  CB  ASP A  90       8.278 -13.232  20.568  1.00 48.22           C  
ANISOU  629  CB  ASP A  90     6274   5676   6371      6    827     67       C  
ATOM    630  CG  ASP A  90       7.555 -12.243  19.685  1.00 49.27           C  
ANISOU  630  CG  ASP A  90     6374   5795   6549      2    814     45       C  
ATOM    631  OD1 ASP A  90       6.300 -12.231  19.629  1.00 48.59           O  
ANISOU  631  OD1 ASP A  90     6260   5681   6520      2    846     45       O  
ATOM    632  OD2 ASP A  90       8.234 -11.411  19.076  1.00 53.91           O  
ANISOU  632  OD2 ASP A  90     6964   6401   7116     -1    774     30       O  
ATOM    633  N   LYS A  91       7.440 -14.967  23.631  1.00 58.56           N  
ANISOU  633  N   LYS A  91     7638   6965   7645     25    959    124       N  
ATOM    634  CA  LYS A  91       7.675 -15.572  24.940  1.00 64.14           C  
ANISOU  634  CA  LYS A  91     8382   7682   8306     35    998    150       C  
ATOM    635  C   LYS A  91       8.805 -16.554  24.988  1.00 64.01           C  
ANISOU  635  C   LYS A  91     8381   7684   8252     37    970    171       C  
ATOM    636  O   LYS A  91       9.768 -16.374  25.719  1.00 64.77           O  
ANISOU  636  O   LYS A  91     8518   7811   8279     42    961    176       O  
ATOM    637  CB  LYS A  91       6.423 -16.322  25.428  1.00 68.58           C  
ANISOU  637  CB  LYS A  91     8926   8210   8920     39   1058    171       C  
ATOM    638  CG  LYS A  91       5.078 -15.652  25.198  1.00 72.14           C  
ANISOU  638  CG  LYS A  91     9347   8632   9432     36   1089    155       C  
ATOM    639  CD  LYS A  91       4.501 -15.131  26.506  1.00 73.03           C  
ANISOU  639  CD  LYS A  91     9488   8741   9516     44   1150    159       C  
ATOM    640  CE  LYS A  91       5.001 -13.737  26.848  1.00 70.27           C  
ANISOU  640  CE  LYS A  91     9169   8416   9111     44   1136    131       C  
ATOM    641  NZ  LYS A  91       5.515 -13.785  28.237  1.00 72.34           N  
ANISOU  641  NZ  LYS A  91     9484   8704   9298     54   1167    145       N  
ATOM    642  N   GLU A  92       8.654 -17.653  24.282  1.00 61.19           N  
ANISOU  642  N   GLU A  92     7993   7310   7945     35    960    184       N  
ATOM    643  CA  GLU A  92       9.675 -18.656  24.378  1.00 65.11           C  
ANISOU  643  CA  GLU A  92     8503   7822   8412     39    940    206       C  
ATOM    644  C   GLU A  92       9.860 -19.172  23.004  1.00 64.97           C  
ANISOU  644  C   GLU A  92     8448   7796   8442     31    895    196       C  
ATOM    645  O   GLU A  92       9.272 -20.154  22.561  1.00 72.77           O  
ANISOU  645  O   GLU A  92     9403   8756   9490     29    906    206       O  
ATOM    646  CB  GLU A  92       9.336 -19.743  25.380  1.00 73.96           C  
ANISOU  646  CB  GLU A  92     9635   8929   9534     48    990    244       C  
ATOM    647  CG  GLU A  92      10.135 -19.588  26.663  1.00 82.05           C  
ANISOU  647  CG  GLU A  92    10714   9987  10475     59   1003    261       C  
ATOM    648  CD  GLU A  92       9.509 -20.319  27.827  1.00 88.12           C  
ANISOU  648  CD  GLU A  92    11496  10742  11241     70   1067    297       C  
ATOM    649  OE1 GLU A  92       8.821 -21.338  27.591  1.00 95.32           O  
ANISOU  649  OE1 GLU A  92    12379  11622  12216     70   1092    318       O  
ATOM    650  OE2 GLU A  92       9.709 -19.875  28.978  1.00 89.60           O  
ANISOU  650  OE2 GLU A  92    11726  10952  11364     79   1092    305       O  
ATOM    651  N   TRP A  93      10.689 -18.449  22.314  1.00 56.21           N  
ANISOU  651  N   TRP A  93     7341   6709   7305     25    844    174       N  
ATOM    652  CA  TRP A  93      10.732 -18.564  20.913  1.00 56.39           C  
ANISOU  652  CA  TRP A  93     7327   6727   7371     17    802    156       C  
ATOM    653  C   TRP A  93      12.077 -19.199  20.631  1.00 49.96           C  
ANISOU  653  C   TRP A  93     6524   5935   6521     18    761    164       C  
ATOM    654  O   TRP A  93      12.955 -19.121  21.460  1.00 50.40           O  
ANISOU  654  O   TRP A  93     6617   6014   6516     23    760    176       O  
ATOM    655  CB  TRP A  93      10.504 -17.139  20.425  1.00 60.71           C  
ANISOU  655  CB  TRP A  93     7868   7280   7916     12    784    126       C  
ATOM    656  CG  TRP A  93      11.195 -16.786  19.181  1.00 66.59           C  
ANISOU  656  CG  TRP A  93     8596   8041   8661      5    726    107       C  
ATOM    657  CD1 TRP A  93      10.638 -16.558  17.916  1.00 67.76           C  
ANISOU  657  CD1 TRP A  93     8704   8178   8861      0    701     88       C  
ATOM    658  CD2 TRP A  93      12.632 -16.608  19.025  1.00 70.37           C  
ANISOU  658  CD2 TRP A  93     9098   8552   9084      5    683    104       C  
ATOM    659  NE1 TRP A  93      11.626 -16.254  16.993  1.00 68.36           N  
ANISOU  659  NE1 TRP A  93     8779   8279   8916     -4    648     75       N  
ATOM    660  CE2 TRP A  93      12.854 -16.286  17.596  1.00 70.76           C  
ANISOU  660  CE2 TRP A  93     9118   8607   9158     -1    636     84       C  
ATOM    661  CE3 TRP A  93      13.729 -16.687  19.890  1.00 68.57           C  
ANISOU  661  CE3 TRP A  93     8911   8349   8793      9    679    117       C  
ATOM    662  CZ2 TRP A  93      14.123 -16.061  17.095  1.00 70.19           C  
ANISOU  662  CZ2 TRP A  93     9057   8563   9047     -3    590     78       C  
ATOM    663  CZ3 TRP A  93      14.998 -16.457  19.367  1.00 72.05           C  
ANISOU  663  CZ3 TRP A  93     9360   8816   9198      7    630    109       C  
ATOM    664  CH2 TRP A  93      15.189 -16.153  18.002  1.00 72.82           C  
ANISOU  664  CH2 TRP A  93     9429   8918   9320      0    588     90       C  
ATOM    665  N   ASN A  94      12.256 -19.923  19.540  1.00 43.93           N  
ANISOU  665  N   ASN A  94     5730   5165   5796     14    730    159       N  
ATOM    666  CA  ASN A  94      13.614 -20.388  19.215  1.00 44.65           C  
ANISOU  666  CA  ASN A  94     5832   5279   5852     14    688    163       C  
ATOM    667  C   ASN A  94      13.950 -20.138  17.753  1.00 42.51           C  
ANISOU  667  C   ASN A  94     5533   5017   5601      7    638    137       C  
ATOM    668  O   ASN A  94      13.071 -19.756  16.984  1.00 41.20           O  
ANISOU  668  O   ASN A  94     5337   4836   5480      1    635    118       O  
ATOM    669  CB  ASN A  94      13.744 -21.871  19.505  1.00 44.25           C  
ANISOU  669  CB  ASN A  94     5776   5214   5820     19    705    190       C  
ATOM    670  CG  ASN A  94      12.632 -22.676  18.881  1.00 49.65           C  
ANISOU  670  CG  ASN A  94     6418   5862   6585     16    723    187       C  
ATOM    671  OD1 ASN A  94      12.124 -23.615  19.495  1.00 56.74           O  
ANISOU  671  OD1 ASN A  94     7311   6736   7510     20    762    212       O  
ATOM    672  ND2 ASN A  94      12.223 -22.310  17.658  1.00 49.91           N  
ANISOU  672  ND2 ASN A  94     6416   5890   6656      8    694    158       N  
ATOM    673  N   ARG A  95      15.185 -20.448  17.371  1.00 40.18           N  
ANISOU  673  N   ARG A  95     5246   4743   5276      7    599    138       N  
ATOM    674  CA  ARG A  95      15.713 -20.224  16.040  1.00 42.19           C  
ANISOU  674  CA  ARG A  95     5479   5011   5538      1    550    116       C  
ATOM    675  C   ARG A  95      14.729 -20.550  14.901  1.00 38.59           C  
ANISOU  675  C   ARG A  95     4978   4534   5150     -3    545     98       C  
ATOM    676  O   ARG A  95      14.525 -19.754  13.999  1.00 36.79           O  
ANISOU  676  O   ARG A  95     4733   4313   4931     -8    520     77       O  
ATOM    677  CB  ARG A  95      17.008 -21.032  15.881  1.00 49.70           C  
ANISOU  677  CB  ARG A  95     6440   5979   6464      4    522    126       C  
ATOM    678  CG  ARG A  95      16.869 -22.496  16.367  1.00 64.64           C  
ANISOU  678  CG  ARG A  95     8328   7850   8382      9    549    150       C  
ATOM    679  CD  ARG A  95      18.176 -23.290  16.382  1.00 71.64           C  
ANISOU  679  CD  ARG A  95     9226   8752   9242     13    525    164       C  
ATOM    680  NE  ARG A  95      18.696 -23.517  15.024  1.00 82.77           N  
ANISOU  680  NE  ARG A  95    10609  10168  10669      8    482    143       N  
ATOM    681  CZ  ARG A  95      19.613 -22.756  14.413  1.00 85.60           C  
ANISOU  681  CZ  ARG A  95    10974  10555  10993      5    442    127       C  
ATOM    682  NH1 ARG A  95      20.135 -21.694  15.030  1.00 92.89           N  
ANISOU  682  NH1 ARG A  95    11929  11501  11864      6    436    129       N  
ATOM    683  NH2 ARG A  95      20.006 -23.047  13.174  1.00 79.88           N  
ANISOU  683  NH2 ARG A  95    10225   9836  10288      2    408    109       N  
ATOM    684  N   ASP A  96      14.129 -21.733  14.960  1.00 36.75           N  
ANISOU  684  N   ASP A  96     4725   4274   4963     -2    568    109       N  
ATOM    685  CA  ASP A  96      13.182 -22.203  13.968  1.00 34.74           C  
ANISOU  685  CA  ASP A  96     4425   3997   4775     -7    564     92       C  
ATOM    686  C   ASP A  96      11.959 -21.289  13.820  1.00 34.23           C  
ANISOU  686  C   ASP A  96     4344   3920   4741    -10    579     78       C  
ATOM    687  O   ASP A  96      11.370 -21.170  12.735  1.00 31.67           O  
ANISOU  687  O   ASP A  96     3984   3590   4457    -15    558     56       O  
ATOM    688  CB  ASP A  96      12.732 -23.642  14.311  1.00 38.24           C  
ANISOU  688  CB  ASP A  96     4854   4410   5265     -5    595    108       C  
ATOM    689  CG  ASP A  96      13.789 -24.734  13.938  1.00 41.64           C  
ANISOU  689  CG  ASP A  96     5282   4846   5690     -3    571    113       C  
ATOM    690  OD1 ASP A  96      14.933 -24.429  13.501  1.00 44.79           O  
ANISOU  690  OD1 ASP A  96     5696   5275   6047     -3    532    106       O  
ATOM    691  OD2 ASP A  96      13.449 -25.941  14.085  1.00 45.28           O  
ANISOU  691  OD2 ASP A  96     5726   5280   6196     -2    592    125       O  
ATOM    692  N   ASP A  97      11.564 -20.617  14.885  1.00 33.43           N  
ANISOU  692  N   ASP A  97     4266   3814   4619     -7    615     90       N  
ATOM    693  CA  ASP A  97      10.404 -19.767  14.770  1.00 36.34           C  
ANISOU  693  CA  ASP A  97     4617   4169   5020    -10    631     77       C  
ATOM    694  C   ASP A  97      10.565 -18.648  13.742  1.00 40.83           C  
ANISOU  694  C   ASP A  97     5174   4757   5580    -14    590     53       C  
ATOM    695  O   ASP A  97       9.575 -18.042  13.310  1.00 43.58           O  
ANISOU  695  O   ASP A  97     5498   5093   5966    -16    593     41       O  
ATOM    696  CB  ASP A  97      10.145 -19.142  16.091  1.00 37.42           C  
ANISOU  696  CB  ASP A  97     4786   4303   5127     -5    674     91       C  
ATOM    697  CG  ASP A  97       9.498 -20.083  17.045  1.00 36.05           C  
ANISOU  697  CG  ASP A  97     4615   4104   4979     -1    725    115       C  
ATOM    698  OD1 ASP A  97       8.520 -20.698  16.626  1.00 36.01           O  
ANISOU  698  OD1 ASP A  97     4573   4069   5038     -4    739    112       O  
ATOM    699  OD2 ASP A  97       9.969 -20.201  18.185  1.00 36.26           O  
ANISOU  699  OD2 ASP A  97     4678   4138   4960      4    750    136       O  
ATOM    700  N   LEU A  98      11.812 -18.374  13.357  1.00 38.32           N  
ANISOU  700  N   LEU A  98     4874   4469   5214    -14    550     49       N  
ATOM    701  CA  LEU A  98      12.113 -17.235  12.538  1.00 38.38           C  
ANISOU  701  CA  LEU A  98     4878   4498   5206    -17    515     32       C  
ATOM    702  C   LEU A  98      11.902 -17.602  11.110  1.00 36.60           C  
ANISOU  702  C   LEU A  98     4614   4274   5018    -20    479     16       C  
ATOM    703  O   LEU A  98      11.761 -16.720  10.262  1.00 39.13           O  
ANISOU  703  O   LEU A  98     4920   4606   5342    -21    453      2       O  
ATOM    704  CB  LEU A  98      13.597 -16.889  12.696  1.00 43.19           C  
ANISOU  704  CB  LEU A  98     5520   5138   5751    -16    488     36       C  
ATOM    705  CG  LEU A  98      13.933 -16.264  14.043  1.00 41.92           C  
ANISOU  705  CG  LEU A  98     5400   4982   5543    -13    514     47       C  
ATOM    706  CD1 LEU A  98      15.407 -15.969  14.052  1.00 41.53           C  
ANISOU  706  CD1 LEU A  98     5378   4964   5438    -13    481     48       C  
ATOM    707  CD2 LEU A  98      13.130 -14.981  14.191  1.00 44.55           C  
ANISOU  707  CD2 LEU A  98     5731   5309   5886    -14    529     37       C  
ATOM    708  N   LEU A  99      11.925 -18.903  10.834  1.00 33.39           N  
ANISOU  708  N   LEU A  99     4190   3857   4637    -20    478     17       N  
ATOM    709  CA  LEU A  99      11.769 -19.384   9.486  1.00 32.87           C  
ANISOU  709  CA  LEU A  99     4089   3794   4605    -23    444     -1       C  
ATOM    710  C   LEU A  99      10.507 -18.862   8.720  1.00 34.37           C  
ANISOU  710  C   LEU A  99     4241   3973   4844    -25    439    -18       C  
ATOM    711  O   LEU A  99      10.625 -18.406   7.564  1.00 36.33           O  
ANISOU  711  O   LEU A  99     4471   4240   5092    -26    400    -34       O  
ATOM    712  CB  LEU A  99      11.862 -20.919   9.487  1.00 31.44           C  
ANISOU  712  CB  LEU A  99     3895   3597   4452    -23    451      1       C  
ATOM    713  CG  LEU A  99      13.288 -21.418   9.739  1.00 31.61           C  
ANISOU  713  CG  LEU A  99     3944   3637   4426    -21    437     12       C  
ATOM    714  CD1 LEU A  99      13.186 -22.874  10.041  1.00 30.18           C  
ANISOU  714  CD1 LEU A  99     3753   3432   4278    -20    457     21       C  
ATOM    715  CD2 LEU A  99      14.240 -21.217   8.566  1.00 30.05           C  
ANISOU  715  CD2 LEU A  99     3742   3471   4204    -22    387     -4       C  
ATOM    716  N   PRO A 100       9.293 -18.955   9.331  1.00 33.25           N  
ANISOU  716  N   PRO A 100     4085   3800   4746    -26    479    -13       N  
ATOM    717  CA  PRO A 100       8.137 -18.466   8.572  1.00 33.51           C  
ANISOU  717  CA  PRO A 100     4081   3823   4828    -27    472    -29       C  
ATOM    718  C   PRO A 100       8.196 -16.935   8.326  1.00 33.88           C  
ANISOU  718  C   PRO A 100     4136   3888   4848    -26    456    -32       C  
ATOM    719  O   PRO A 100       7.873 -16.480   7.205  1.00 33.12           O  
ANISOU  719  O   PRO A 100     4012   3802   4768    -26    423    -46       O  
ATOM    720  CB  PRO A 100       6.926 -18.835   9.471  1.00 36.37           C  
ANISOU  720  CB  PRO A 100     4431   4146   5238    -28    523    -19       C  
ATOM    721  CG  PRO A 100       7.503 -18.985  10.868  1.00 37.15           C  
ANISOU  721  CG  PRO A 100     4574   4243   5297    -24    561      3       C  
ATOM    722  CD  PRO A 100       8.914 -19.502  10.651  1.00 34.61           C  
ANISOU  722  CD  PRO A 100     4274   3946   4928    -24    531      6       C  
ATOM    723  N   LEU A 101       8.609 -16.159   9.334  1.00 30.80           N  
ANISOU  723  N   LEU A 101     3784   3503   4417    -24    478    -18       N  
ATOM    724  CA  LEU A 101       8.834 -14.719   9.157  1.00 32.21           C  
ANISOU  724  CA  LEU A 101     3972   3697   4567    -22    463    -21       C  
ATOM    725  C   LEU A 101       9.825 -14.320   8.049  1.00 29.90           C  
ANISOU  725  C   LEU A 101     3679   3437   4241    -23    412    -29       C  
ATOM    726  O   LEU A 101       9.534 -13.409   7.320  1.00 31.67           O  
ANISOU  726  O   LEU A 101     3888   3670   4475    -22    392    -35       O  
ATOM    727  CB  LEU A 101       9.331 -14.093  10.434  1.00 34.06           C  
ANISOU  727  CB  LEU A 101     4249   3933   4757    -21    492     -9       C  
ATOM    728  CG  LEU A 101       8.296 -13.956  11.535  1.00 38.56           C  
ANISOU  728  CG  LEU A 101     4823   4474   5352    -19    545     -2       C  
ATOM    729  CD1 LEU A 101       8.921 -13.249  12.739  1.00 38.31           C  
ANISOU  729  CD1 LEU A 101     4836   4450   5266    -17    568      5       C  
ATOM    730  CD2 LEU A 101       7.051 -13.234  11.008  1.00 38.09           C  
ANISOU  730  CD2 LEU A 101     4728   4397   5344    -19    549    -11       C  
ATOM    731  N   ASN A 102      10.953 -15.008   7.878  1.00 27.65           N  
ANISOU  731  N   ASN A 102     3409   3171   3923    -23    391    -28       N  
ATOM    732  CA  ASN A 102      11.888 -14.533   6.867  1.00 27.36           C  
ANISOU  732  CA  ASN A 102     3373   3167   3855    -23    346    -34       C  
ATOM    733  C   ASN A 102      11.434 -14.947   5.500  1.00 29.26           C  
ANISOU  733  C   ASN A 102     3574   3413   4128    -23    315    -49       C  
ATOM    734  O   ASN A 102      11.683 -14.268   4.535  1.00 29.56           O  
ANISOU  734  O   ASN A 102     3602   3474   4156    -21    282    -54       O  
ATOM    735  CB  ASN A 102      13.309 -14.953   7.170  1.00 25.99           C  
ANISOU  735  CB  ASN A 102     3230   3012   3631    -23    335    -27       C  
ATOM    736  CG  ASN A 102      13.873 -14.178   8.320  1.00 26.81           C  
ANISOU  736  CG  ASN A 102     3372   3119   3694    -23    354    -16       C  
ATOM    737  OD1 ASN A 102      13.562 -12.978   8.531  1.00 28.07           O  
ANISOU  737  OD1 ASN A 102     3537   3277   3851    -22    362    -16       O  
ATOM    738  ND2 ASN A 102      14.652 -14.807   9.078  1.00 27.42           N  
ANISOU  738  ND2 ASN A 102     3475   3198   3742    -22    363     -6       N  
ATOM    739  N   ASN A 103      10.755 -16.086   5.437  1.00 31.66           N  
ANISOU  739  N   ASN A 103     3856   3698   4475    -24    325    -56       N  
ATOM    740  CA  ASN A 103      10.188 -16.554   4.208  1.00 33.90           C  
ANISOU  740  CA  ASN A 103     4099   3985   4794    -25    297    -74       C  
ATOM    741  C   ASN A 103       9.232 -15.493   3.680  1.00 32.96           C  
ANISOU  741  C   ASN A 103     3956   3865   4699    -22    290    -78       C  
ATOM    742  O   ASN A 103       9.265 -15.149   2.512  1.00 34.04           O  
ANISOU  742  O   ASN A 103     4074   4024   4835    -20    252    -88       O  
ATOM    743  CB  ASN A 103       9.449 -17.911   4.376  1.00 34.17           C  
ANISOU  743  CB  ASN A 103     4111   3991   4880    -27    316    -82       C  
ATOM    744  CG  ASN A 103       8.889 -18.396   3.054  1.00 36.77           C  
ANISOU  744  CG  ASN A 103     4398   4327   5247    -28    283   -105       C  
ATOM    745  OD1 ASN A 103       9.488 -18.188   1.995  1.00 37.96           O  
ANISOU  745  OD1 ASN A 103     4543   4508   5371    -26    243   -116       O  
ATOM    746  ND2 ASN A 103       7.742 -19.011   3.093  1.00 40.34           N  
ANISOU  746  ND2 ASN A 103     4819   4750   5758    -31    300   -114       N  
ATOM    747  N   LYS A 104       8.394 -14.970   4.557  1.00 34.40           N  
ANISOU  747  N   LYS A 104     4141   4022   4905    -22    326    -69       N  
ATOM    748  CA  LYS A 104       7.461 -13.875   4.192  1.00 34.70           C  
ANISOU  748  CA  LYS A 104     4157   4055   4969    -20    323    -70       C  
ATOM    749  C   LYS A 104       8.177 -12.622   3.601  1.00 33.07           C  
ANISOU  749  C   LYS A 104     3963   3878   4722    -16    294    -65       C  
ATOM    750  O   LYS A 104       7.811 -12.079   2.530  1.00 32.90           O  
ANISOU  750  O   LYS A 104     3915   3871   4714    -13    263    -69       O  
ATOM    751  CB  LYS A 104       6.586 -13.570   5.396  1.00 36.65           C  
ANISOU  751  CB  LYS A 104     4411   4269   5243    -20    373    -60       C  
ATOM    752  CG  LYS A 104       6.041 -12.182   5.458  1.00 40.98           C  
ANISOU  752  CG  LYS A 104     4956   4814   5800    -17    380    -55       C  
ATOM    753  CD  LYS A 104       4.739 -12.243   6.246  1.00 44.94           C  
ANISOU  753  CD  LYS A 104     5442   5279   6354    -17    425    -53       C  
ATOM    754  CE  LYS A 104       4.046 -10.893   6.142  1.00 52.16           C  
ANISOU  754  CE  LYS A 104     6344   6186   7287    -13    430    -51       C  
ATOM    755  NZ  LYS A 104       2.553 -11.036   6.265  1.00 59.30           N  
ANISOU  755  NZ  LYS A 104     7213   7058   8260    -13    455    -54       N  
ATOM    756  N   ILE A 105       9.256 -12.220   4.234  1.00 31.40           N  
ANISOU  756  N   ILE A 105     3789   3678   4461    -17    300    -55       N  
ATOM    757  CA  ILE A 105      10.149 -11.227   3.629  1.00 30.51           C  
ANISOU  757  CA  ILE A 105     3689   3594   4309    -14    270    -50       C  
ATOM    758  C   ILE A 105      10.692 -11.590   2.244  1.00 29.67           C  
ANISOU  758  C   ILE A 105     3565   3518   4189    -12    223    -58       C  
ATOM    759  O   ILE A 105      10.751 -10.725   1.386  1.00 29.65           O  
ANISOU  759  O   ILE A 105     3551   3534   4180     -8    198    -55       O  
ATOM    760  CB  ILE A 105      11.307 -10.941   4.584  1.00 31.15           C  
ANISOU  760  CB  ILE A 105     3814   3682   4340    -17    283    -41       C  
ATOM    761  CG1 ILE A 105      10.740 -10.262   5.865  1.00 30.51           C  
ANISOU  761  CG1 ILE A 105     3749   3574   4267    -17    326    -34       C  
ATOM    762  CG2 ILE A 105      12.429 -10.175   3.856  1.00 31.40           C  
ANISOU  762  CG2 ILE A 105     3855   3744   4330    -15    248    -37       C  
ATOM    763  CD1 ILE A 105      11.752 -10.095   6.981  1.00 30.54           C  
ANISOU  763  CD1 ILE A 105     3797   3583   4224    -19    343    -28       C  
ATOM    764  N   MET A 106      11.068 -12.865   2.015  1.00 29.51           N  
ANISOU  764  N   MET A 106     3542   3503   4166    -14    214    -68       N  
ATOM    765  CA  MET A 106      11.631 -13.276   0.738  1.00 29.96           C  
ANISOU  765  CA  MET A 106     3584   3590   4207    -12    173    -79       C  
ATOM    766  C   MET A 106      10.583 -13.337  -0.374  1.00 30.07           C  
ANISOU  766  C   MET A 106     3556   3608   4260     -9    150    -92       C  
ATOM    767  O   MET A 106      10.909 -13.105  -1.542  1.00 29.72           O  
ANISOU  767  O   MET A 106     3499   3593   4198     -5    113    -97       O  
ATOM    768  CB  MET A 106      12.374 -14.639   0.829  1.00 32.56           C  
ANISOU  768  CB  MET A 106     3924   3922   4525    -15    171    -87       C  
ATOM    769  CG  MET A 106      13.497 -14.723   1.864  1.00 35.38           C  
ANISOU  769  CG  MET A 106     4321   4279   4843    -17    188    -74       C  
ATOM    770  SD  MET A 106      14.895 -13.578   1.640  1.00 36.74           S  
ANISOU  770  SD  MET A 106     4521   4483   4955    -15    166    -62       S  
ATOM    771  CE  MET A 106      15.315 -13.221   3.348  1.00 37.06           C  
ANISOU  771  CE  MET A 106     4602   4505   4973    -19    204    -46       C  
ATOM    772  N   ILE A 107       9.331 -13.670   0.000  1.00 30.57           N  
ANISOU  772  N   ILE A 107     3598   3642   4376    -11    172    -97       N  
ATOM    773  CA  ILE A 107       8.155 -13.634  -0.889  1.00 29.36           C  
ANISOU  773  CA  ILE A 107     3401   3487   4266     -8    154   -109       C  
ATOM    774  C   ILE A 107       8.013 -12.202  -1.356  1.00 28.48           C  
ANISOU  774  C   ILE A 107     3285   3389   4144     -2    139    -96       C  
ATOM    775  O   ILE A 107       7.930 -11.893  -2.557  1.00 30.30           O  
ANISOU  775  O   ILE A 107     3495   3647   4370      3    102   -100       O  
ATOM    776  CB  ILE A 107       6.902 -14.154  -0.099  1.00 30.71           C  
ANISOU  776  CB  ILE A 107     3554   3616   4496    -12    190   -113       C  
ATOM    777  CG1 ILE A 107       6.946 -15.685  -0.003  1.00 30.82           C  
ANISOU  777  CG1 ILE A 107     3561   3619   4530    -17    195   -129       C  
ATOM    778  CG2 ILE A 107       5.573 -13.714  -0.704  1.00 29.92           C  
ANISOU  778  CG2 ILE A 107     3412   3508   4445     -9    180   -119       C  
ATOM    779  CD1 ILE A 107       5.816 -16.243   0.865  1.00 33.75           C  
ANISOU  779  CD1 ILE A 107     3917   3948   4959    -21    236   -130       C  
ATOM    780  N   GLU A 108       8.061 -11.284  -0.424  1.00 28.67           N  
ANISOU  780  N   GLU A 108     3332   3398   4161     -2    168    -79       N  
ATOM    781  CA  GLU A 108       7.873  -9.903  -0.823  1.00 29.50           C  
ANISOU  781  CA  GLU A 108     3432   3513   4263      3    157    -66       C  
ATOM    782  C   GLU A 108       9.051  -9.366  -1.664  1.00 28.76           C  
ANISOU  782  C   GLU A 108     3351   3457   4119      7    123    -58       C  
ATOM    783  O   GLU A 108       8.847  -8.788  -2.735  1.00 28.34           O  
ANISOU  783  O   GLU A 108     3276   3424   4065     14     92    -54       O  
ATOM    784  CB  GLU A 108       7.616  -9.039   0.390  1.00 30.36           C  
ANISOU  784  CB  GLU A 108     3560   3594   4380      1    197    -53       C  
ATOM    785  CG  GLU A 108       7.701  -7.539   0.133  1.00 33.38           C  
ANISOU  785  CG  GLU A 108     3945   3984   4754      7    190    -37       C  
ATOM    786  CD  GLU A 108       7.107  -6.758   1.298  1.00 36.56           C  
ANISOU  786  CD  GLU A 108     4357   4353   5180      5    233    -30       C  
ATOM    787  OE1 GLU A 108       7.159  -7.312   2.407  1.00 43.82           O  
ANISOU  787  OE1 GLU A 108     5298   5253   6097      0    267    -34       O  
ATOM    788  OE2 GLU A 108       6.565  -5.617   1.129  1.00 40.63           O  
ANISOU  788  OE2 GLU A 108     4859   4860   5716     10    235    -20       O  
ATOM    789  N   ILE A 109      10.283  -9.584  -1.212  1.00 27.69           N  
ANISOU  789  N   ILE A 109     3249   3330   3939      3    127    -55       N  
ATOM    790  CA  ILE A 109      11.383  -9.121  -1.993  1.00 26.46           C  
ANISOU  790  CA  ILE A 109     3104   3208   3739      7     97    -48       C  
ATOM    791  C   ILE A 109      11.368  -9.799  -3.345  1.00 25.65           C  
ANISOU  791  C   ILE A 109     2977   3135   3634     11     59    -60       C  
ATOM    792  O   ILE A 109      11.627  -9.187  -4.356  1.00 25.46           O  
ANISOU  792  O   ILE A 109     2943   3139   3591     18     30    -53       O  
ATOM    793  CB  ILE A 109      12.694  -9.421  -1.268  1.00 27.00           C  
ANISOU  793  CB  ILE A 109     3210   3281   3766      1    108    -45       C  
ATOM    794  CG1 ILE A 109      12.757  -8.604   0.009  1.00 26.99           C  
ANISOU  794  CG1 ILE A 109     3236   3257   3762     -1    142    -34       C  
ATOM    795  CG2 ILE A 109      13.865  -9.119  -2.184  1.00 26.75           C  
ANISOU  795  CG2 ILE A 109     3186   3285   3691      5     76    -39       C  
ATOM    796  CD1 ILE A 109      13.920  -9.034   0.903  1.00 27.89           C  
ANISOU  796  CD1 ILE A 109     3385   3371   3838     -7    154    -33       C  
ATOM    797  N   GLY A 110      11.049 -11.088  -3.412  1.00 26.34           N  
ANISOU  797  N   GLY A 110     3051   3216   3739      8     58    -80       N  
ATOM    798  CA  GLY A 110      11.191 -11.731  -4.727  1.00 24.72           C  
ANISOU  798  CA  GLY A 110     2825   3043   3525     12     20    -97       C  
ATOM    799  C   GLY A 110      10.224 -11.264  -5.811  1.00 25.94           C  
ANISOU  799  C   GLY A 110     2942   3211   3701     19     -7    -99       C  
ATOM    800  O   GLY A 110      10.560 -11.248  -7.066  1.00 25.00           O  
ANISOU  800  O   GLY A 110     2812   3130   3557     26    -44   -103       O  
ATOM    801  N   GLY A 111       9.014 -10.879  -5.365  1.00 25.25           N  
ANISOU  801  N   GLY A 111     2837   3095   3660     19     10    -95       N  
ATOM    802  CA  GLY A 111       8.001 -10.393  -6.324  1.00 25.12           C  
ANISOU  802  CA  GLY A 111     2784   3091   3670     27    -15    -96       C  
ATOM    803  C   GLY A 111       8.530  -9.071  -6.859  1.00 25.57           C  
ANISOU  803  C   GLY A 111     2849   3172   3693     36    -31    -70       C  
ATOM    804  O   GLY A 111       8.356  -8.723  -8.060  1.00 26.62           O  
ANISOU  804  O   GLY A 111     2960   3337   3817     45    -66    -67       O  
ATOM    805  N   HIS A 112       9.183  -8.318  -6.009  1.00 25.17           N  
ANISOU  805  N   HIS A 112     2829   3109   3625     33     -5    -51       N  
ATOM    806  CA  HIS A 112       9.735  -7.037  -6.563  1.00 27.99           C  
ANISOU  806  CA  HIS A 112     3192   3488   3953     41    -20    -26       C  
ATOM    807  C   HIS A 112      10.954  -7.174  -7.405  1.00 26.74           C  
ANISOU  807  C   HIS A 112     3047   3369   3743     44    -47    -24       C  
ATOM    808  O   HIS A 112      11.161  -6.355  -8.278  1.00 26.29           O  
ANISOU  808  O   HIS A 112     2982   3337   3667     53    -69     -6       O  
ATOM    809  CB  HIS A 112       9.951  -5.959  -5.558  1.00 28.10           C  
ANISOU  809  CB  HIS A 112     3228   3476   3969     38     10     -6       C  
ATOM    810  CG  HIS A 112       8.701  -5.544  -4.868  1.00 29.88           C  
ANISOU  810  CG  HIS A 112     3438   3666   4247     38     36     -5       C  
ATOM    811  ND1 HIS A 112       7.772  -4.777  -5.467  1.00 29.98           N  
ANISOU  811  ND1 HIS A 112     3421   3678   4290     46     24      6       N  
ATOM    812  CD2 HIS A 112       8.259  -5.754  -3.550  1.00 30.05           C  
ANISOU  812  CD2 HIS A 112     3472   3649   4295     30     77    -11       C  
ATOM    813  CE1 HIS A 112       6.772  -4.528  -4.586  1.00 30.54           C  
ANISOU  813  CE1 HIS A 112     3483   3710   4407     44     56      5       C  
ATOM    814  NE2 HIS A 112       7.078  -5.114  -3.419  1.00 30.17           N  
ANISOU  814  NE2 HIS A 112     3463   3641   4356     34     89     -5       N  
ATOM    815  N   ILE A 113      11.705  -8.251  -7.226  1.00 26.55           N  
ANISOU  815  N   ILE A 113     3039   3350   3696     38    -46    -41       N  
ATOM    816  CA  ILE A 113      12.832  -8.474  -8.136  1.00 25.37           C  
ANISOU  816  CA  ILE A 113     2899   3241   3500     42    -73    -42       C  
ATOM    817  C   ILE A 113      12.246  -8.822  -9.500  1.00 26.41           C  
ANISOU  817  C   ILE A 113     2997   3403   3632     51   -110    -54       C  
ATOM    818  O   ILE A 113      12.682  -8.371 -10.572  1.00 25.63           O  
ANISOU  818  O   ILE A 113     2893   3342   3501     60   -137    -43       O  
ATOM    819  CB  ILE A 113      13.713  -9.555  -7.522  1.00 25.00           C  
ANISOU  819  CB  ILE A 113     2875   3187   3434     33    -60    -58       C  
ATOM    820  CG1 ILE A 113      14.385  -8.963  -6.257  1.00 25.43           C  
ANISOU  820  CG1 ILE A 113     2963   3219   3479     26    -29    -41       C  
ATOM    821  CG2 ILE A 113      14.682 -10.183  -8.502  1.00 25.10           C  
ANISOU  821  CG2 ILE A 113     2891   3239   3407     37    -87    -68       C  
ATOM    822  CD1 ILE A 113      15.381  -9.889  -5.578  1.00 26.37           C  
ANISOU  822  CD1 ILE A 113     3109   3333   3577     19    -16    -51       C  
ATOM    823  N   LYS A 114      11.189  -9.607  -9.436  1.00 27.39           N  
ANISOU  823  N   LYS A 114     3098   3512   3797     48   -110    -76       N  
ATOM    824  CA  LYS A 114      10.628 -10.195 -10.629  1.00 29.32           C  
ANISOU  824  CA  LYS A 114     3311   3783   4044     55   -146    -96       C  
ATOM    825  C   LYS A 114      10.053  -9.112 -11.500  1.00 28.45           C  
ANISOU  825  C   LYS A 114     3180   3695   3935     67   -169    -76       C  
ATOM    826  O   LYS A 114      10.202  -9.166 -12.717  1.00 29.35           O  
ANISOU  826  O   LYS A 114     3280   3850   4021     76   -204    -79       O  
ATOM    827  CB  LYS A 114       9.577 -11.201 -10.197  1.00 29.24           C  
ANISOU  827  CB  LYS A 114     3279   3744   4086     47   -136   -124       C  
ATOM    828  CG  LYS A 114       8.844 -11.815 -11.311  1.00 29.47           C  
ANISOU  828  CG  LYS A 114     3272   3795   4127     52   -172   -149       C  
ATOM    829  CD  LYS A 114       7.983 -12.919 -10.738  1.00 29.17           C  
ANISOU  829  CD  LYS A 114     3217   3723   4143     43   -157   -177       C  
ATOM    830  CE  LYS A 114       8.716 -14.227 -10.931  1.00 29.94           C  
ANISOU  830  CE  LYS A 114     3322   3829   4223     37   -163   -206       C  
ATOM    831  NZ  LYS A 114       7.797 -15.241 -10.370  1.00 32.12           N  
ANISOU  831  NZ  LYS A 114     3577   4068   4558     28   -146   -231       N  
ATOM    832  N   LYS A 115       9.391  -8.155 -10.844  1.00 29.23           N  
ANISOU  832  N   LYS A 115     3275   3765   4065     67   -148    -54       N  
ATOM    833  CA  LYS A 115       8.911  -6.895 -11.431  1.00 30.47           C  
ANISOU  833  CA  LYS A 115     3415   3934   4227     79   -162    -26       C  
ATOM    834  C   LYS A 115      10.031  -5.976 -11.872  1.00 30.77           C  
ANISOU  834  C   LYS A 115     3474   3999   4218     86   -169      2       C  
ATOM    835  O   LYS A 115      10.057  -5.569 -13.054  1.00 29.96           O  
ANISOU  835  O   LYS A 115     3355   3934   4091     98   -201     15       O  
ATOM    836  CB  LYS A 115       8.024  -6.091 -10.466  1.00 31.36           C  
ANISOU  836  CB  LYS A 115     3522   4003   4389     77   -132    -11       C  
ATOM    837  CG  LYS A 115       6.691  -5.685 -11.056  1.00 34.54           C  
ANISOU  837  CG  LYS A 115     3885   4406   4832     86   -150     -6       C  
ATOM    838  CD  LYS A 115       6.393  -4.212 -10.927  1.00 39.22           C  
ANISOU  838  CD  LYS A 115     4473   4987   5441     94   -140     28       C  
ATOM    839  CE  LYS A 115       6.059  -3.792  -9.502  1.00 39.59           C  
ANISOU  839  CE  LYS A 115     4533   4982   5525     85    -93     33       C  
ATOM    840  NZ  LYS A 115       6.804  -2.509  -9.405  1.00 38.45           N  
ANISOU  840  NZ  LYS A 115     4408   4839   5359     89    -84     64       N  
ATOM    841  N   ASN A 116      10.959  -5.645 -10.960  1.00 28.94           N  
ANISOU  841  N   ASN A 116     3276   3749   3971     78   -140     13       N  
ATOM    842  CA  ASN A 116      11.855  -4.494 -11.206  1.00 30.13           C  
ANISOU  842  CA  ASN A 116     3442   3914   4090     84   -141     45       C  
ATOM    843  C   ASN A 116      13.254  -4.782 -11.711  1.00 30.28           C  
ANISOU  843  C   ASN A 116     3483   3966   4055     84   -152     46       C  
ATOM    844  O   ASN A 116      13.900  -3.872 -12.250  1.00 31.55           O  
ANISOU  844  O   ASN A 116     3649   4147   4191     92   -160     73       O  
ATOM    845  CB  ASN A 116      11.990  -3.637  -9.950  1.00 30.99           C  
ANISOU  845  CB  ASN A 116     3571   3983   4219     76   -103     60       C  
ATOM    846  CG  ASN A 116      10.648  -3.168  -9.446  1.00 32.24           C  
ANISOU  846  CG  ASN A 116     3708   4107   4431     77    -88     63       C  
ATOM    847  OD1 ASN A 116      10.498  -2.859  -8.263  1.00 33.78           O  
ANISOU  847  OD1 ASN A 116     3918   4265   4650     69    -54     63       O  
ATOM    848  ND2 ASN A 116       9.655  -3.196 -10.316  1.00 30.56           N  
ANISOU  848  ND2 ASN A 116     3462   3909   4239     87   -113     63       N  
ATOM    849  N   CYS A 117      13.781  -5.978 -11.442  1.00 28.70           N  
ANISOU  849  N   CYS A 117     3296   3767   3840     76   -150     18       N  
ATOM    850  CA  CYS A 117      15.132  -6.271 -11.887  1.00 27.85           C  
ANISOU  850  CA  CYS A 117     3208   3689   3684     76   -159     18       C  
ATOM    851  C   CYS A 117      15.297  -7.783 -12.137  1.00 28.54           C  
ANISOU  851  C   CYS A 117     3294   3788   3762     72   -170    -16       C  
ATOM    852  O   CYS A 117      16.166  -8.473 -11.514  1.00 28.10           O  
ANISOU  852  O   CYS A 117     3260   3723   3692     64   -155    -28       O  
ATOM    853  CB  CYS A 117      16.174  -5.715 -10.933  1.00 27.06           C  
ANISOU  853  CB  CYS A 117     3139   3569   3571     69   -132     34       C  
ATOM    854  SG  CYS A 117      15.871  -6.115  -9.165  1.00 28.38           S  
ANISOU  854  SG  CYS A 117     3325   3683   3772     53    -93     19       S  
ATOM    855  N   PRO A 118      14.495  -8.300 -13.085  1.00 29.66           N  
ANISOU  855  N   PRO A 118     3407   3951   3910     79   -197    -34       N  
ATOM    856  CA  PRO A 118      14.583  -9.749 -13.360  1.00 28.94           C  
ANISOU  856  CA  PRO A 118     3311   3870   3815     75   -208    -72       C  
ATOM    857  C   PRO A 118      15.968 -10.133 -13.824  1.00 28.50           C  
ANISOU  857  C   PRO A 118     3274   3843   3709     77   -215    -75       C  
ATOM    858  O   PRO A 118      16.283 -11.348 -13.811  1.00 29.56           O  
ANISOU  858  O   PRO A 118     3411   3977   3841     71   -216   -105       O  
ATOM    859  CB  PRO A 118      13.575  -9.955 -14.520  1.00 29.59           C  
ANISOU  859  CB  PRO A 118     3358   3980   3905     85   -243    -86       C  
ATOM    860  CG  PRO A 118      13.497  -8.628 -15.197  1.00 28.60           C  
ANISOU  860  CG  PRO A 118     3226   3877   3762     98   -256    -51       C  
ATOM    861  CD  PRO A 118      13.624  -7.609 -14.074  1.00 28.62           C  
ANISOU  861  CD  PRO A 118     3247   3843   3784     92   -223    -21       C  
ATOM    862  N   ASN A 119      16.794  -9.176 -14.264  1.00 28.12           N  
ANISOU  862  N   ASN A 119     3239   3819   3626     84   -219    -45       N  
ATOM    863  CA  ASN A 119      18.164  -9.578 -14.650  1.00 29.83           C  
ANISOU  863  CA  ASN A 119     3474   4061   3798     84   -222    -49       C  
ATOM    864  C   ASN A 119      19.236  -9.346 -13.628  1.00 28.69           C  
ANISOU  864  C   ASN A 119     3359   3893   3646     75   -195    -35       C  
ATOM    865  O   ASN A 119      20.419  -9.554 -13.916  1.00 29.19           O  
ANISOU  865  O   ASN A 119     3438   3976   3675     76   -197    -34       O  
ATOM    866  CB  ASN A 119      18.648  -8.939 -15.926  1.00 34.19           C  
ANISOU  866  CB  ASN A 119     4022   4661   4308     98   -245    -29       C  
ATOM    867  CG  ASN A 119      17.759  -9.249 -17.096  1.00 39.90           C  
ANISOU  867  CG  ASN A 119     4716   5417   5027    109   -277    -45       C  
ATOM    868  OD1 ASN A 119      17.075 -10.269 -17.140  1.00 41.93           O  
ANISOU  868  OD1 ASN A 119     4958   5668   5304    106   -287    -81       O  
ATOM    869  ND2 ASN A 119      17.773  -8.369 -18.066  1.00 44.63           N  
ANISOU  869  ND2 ASN A 119     5307   6051   5599    123   -295    -19       N  
ATOM    870  N   ALA A 120      18.874  -8.897 -12.450  1.00 27.66           N  
ANISOU  870  N   ALA A 120     3239   3723   3547     67   -171    -25       N  
ATOM    871  CA  ALA A 120      19.922  -8.663 -11.428  1.00 25.71           C  
ANISOU  871  CA  ALA A 120     3021   3455   3290     58   -147    -13       C  
ATOM    872  C   ALA A 120      20.632  -9.910 -11.043  1.00 24.96           C  
ANISOU  872  C   ALA A 120     2939   3356   3187     51   -141    -37       C  
ATOM    873  O   ALA A 120      20.083 -11.020 -11.188  1.00 25.61           O  
ANISOU  873  O   ALA A 120     3008   3436   3284     50   -147    -65       O  
ATOM    874  CB  ALA A 120      19.334  -8.016 -10.214  1.00 26.17           C  
ANISOU  874  CB  ALA A 120     3087   3473   3382     51   -121     -2       C  
ATOM    875  N   PHE A 121      21.850  -9.736 -10.529  1.00 25.10           N  
ANISOU  875  N   PHE A 121     2980   3371   3183     47   -129    -26       N  
ATOM    876  CA  PHE A 121      22.564 -10.774  -9.836  1.00 25.85           C  
ANISOU  876  CA  PHE A 121     3092   3453   3275     39   -118    -42       C  
ATOM    877  C   PHE A 121      22.266 -10.663  -8.298  1.00 24.20           C  
ANISOU  877  C   PHE A 121     2900   3202   3092     29    -90    -38       C  
ATOM    878  O   PHE A 121      22.350  -9.577  -7.731  1.00 23.33           O  
ANISOU  878  O   PHE A 121     2800   3079   2983     27    -78    -17       O  
ATOM    879  CB  PHE A 121      24.090 -10.671 -10.146  1.00 26.38           C  
ANISOU  879  CB  PHE A 121     3176   3543   3305     40   -122    -32       C  
ATOM    880  CG  PHE A 121      24.907 -11.740  -9.482  1.00 27.79           C  
ANISOU  880  CG  PHE A 121     3369   3710   3479     34   -112    -47       C  
ATOM    881  CD1 PHE A 121      24.840 -13.046  -9.927  1.00 27.88           C  
ANISOU  881  CD1 PHE A 121     3370   3729   3492     35   -121    -75       C  
ATOM    882  CD2 PHE A 121      25.623 -11.464  -8.333  1.00 30.02           C  
ANISOU  882  CD2 PHE A 121     3674   3970   3759     26    -94    -35       C  
ATOM    883  CE1 PHE A 121      25.548 -14.030  -9.327  1.00 28.80           C  
ANISOU  883  CE1 PHE A 121     3499   3833   3610     30   -111    -86       C  
ATOM    884  CE2 PHE A 121      26.364 -12.452  -7.716  1.00 30.81           C  
ANISOU  884  CE2 PHE A 121     3788   4061   3857     21    -87    -46       C  
ATOM    885  CZ  PHE A 121      26.331 -13.743  -8.202  1.00 30.22           C  
ANISOU  885  CZ  PHE A 121     3702   3993   3785     23    -94    -70       C  
ATOM    886  N   ILE A 122      21.876 -11.758  -7.641  1.00 22.35           N  
ANISOU  886  N   ILE A 122     2666   2946   2878     23    -79    -58       N  
ATOM    887  CA  ILE A 122      21.357 -11.616  -6.272  1.00 21.22           C  
ANISOU  887  CA  ILE A 122     2536   2765   2761     16    -51    -53       C  
ATOM    888  C   ILE A 122      22.235 -12.350  -5.302  1.00 20.84           C  
ANISOU  888  C   ILE A 122     2510   2702   2702      9    -36    -56       C  
ATOM    889  O   ILE A 122      22.593 -13.520  -5.522  1.00 20.39           O  
ANISOU  889  O   ILE A 122     2452   2651   2644      9    -41    -73       O  
ATOM    890  CB  ILE A 122      19.941 -12.219  -6.124  1.00 22.39           C  
ANISOU  890  CB  ILE A 122     2664   2893   2950     14    -45    -69       C  
ATOM    891  CG1 ILE A 122      19.049 -11.871  -7.337  1.00 23.25           C  
ANISOU  891  CG1 ILE A 122     2743   3021   3068     22    -68    -74       C  
ATOM    892  CG2 ILE A 122      19.270 -11.849  -4.796  1.00 21.70           C  
ANISOU  892  CG2 ILE A 122     2587   2768   2888      8    -15    -61       C  
ATOM    893  CD1 ILE A 122      18.829 -10.345  -7.421  1.00 24.00           C  
ANISOU  893  CD1 ILE A 122     2838   3119   3161     26    -68    -48       C  
ATOM    894  N   ILE A 123      22.512 -11.739  -4.185  1.00 20.70           N  
ANISOU  894  N   ILE A 123     2515   2666   2682      4    -17    -42       N  
ATOM    895  CA  ILE A 123      23.374 -12.417  -3.176  1.00 20.32           C  
ANISOU  895  CA  ILE A 123     2491   2606   2623      0     -3    -42       C  
ATOM    896  C   ILE A 123      22.609 -12.366  -1.898  1.00 20.82           C  
ANISOU  896  C   ILE A 123     2564   2636   2707     -5     23    -40       C  
ATOM    897  O   ILE A 123      22.221 -11.273  -1.471  1.00 20.50           O  
ANISOU  897  O   ILE A 123     2530   2586   2672     -7     33    -29       O  
ATOM    898  CB  ILE A 123      24.668 -11.645  -2.950  1.00 19.70           C  
ANISOU  898  CB  ILE A 123     2433   2539   2513     -2     -7    -27       C  
ATOM    899  CG1 ILE A 123      25.538 -11.818  -4.187  1.00 19.91           C  
ANISOU  899  CG1 ILE A 123     2449   2597   2516      3    -31    -29       C  
ATOM    900  CG2 ILE A 123      25.406 -12.126  -1.684  1.00 18.99           C  
ANISOU  900  CG2 ILE A 123     2369   2434   2413     -7      7    -24       C  
ATOM    901  CD1 ILE A 123      26.453 -10.641  -4.500  1.00 20.38           C  
ANISOU  901  CD1 ILE A 123     2516   2674   2552      4    -39    -10       C  
ATOM    902  N   VAL A 124      22.345 -13.520  -1.284  1.00 21.60           N  
ANISOU  902  N   VAL A 124     2665   2717   2822     -8     37    -49       N  
ATOM    903  CA  VAL A 124      21.439 -13.506  -0.091  1.00 22.36           C  
ANISOU  903  CA  VAL A 124     2770   2782   2942    -12     67    -46       C  
ATOM    904  C   VAL A 124      22.305 -13.737   1.161  1.00 23.26           C  
ANISOU  904  C   VAL A 124     2914   2886   3034    -15     83    -37       C  
ATOM    905  O   VAL A 124      23.232 -14.539   1.109  1.00 23.50           O  
ANISOU  905  O   VAL A 124     2952   2926   3048    -15     75    -38       O  
ATOM    906  CB  VAL A 124      20.392 -14.599  -0.248  1.00 22.63           C  
ANISOU  906  CB  VAL A 124     2782   2800   3013    -11     74    -61       C  
ATOM    907  CG1 VAL A 124      19.555 -14.786   1.035  1.00 23.12           C  
ANISOU  907  CG1 VAL A 124     2853   2829   3099    -15    109    -56       C  
ATOM    908  CG2 VAL A 124      19.526 -14.357  -1.522  1.00 21.74           C  
ANISOU  908  CG2 VAL A 124     2638   2701   2921     -7     54    -72       C  
ATOM    909  N   VAL A 125      22.026 -13.076   2.273  1.00 24.27           N  
ANISOU  909  N   VAL A 125     3062   2998   3161    -18    106    -27       N  
ATOM    910  CA  VAL A 125      22.880 -13.213   3.461  1.00 26.57           C  
ANISOU  910  CA  VAL A 125     3384   3285   3427    -20    118    -19       C  
ATOM    911  C   VAL A 125      21.999 -13.612   4.621  1.00 30.13           C  
ANISOU  911  C   VAL A 125     3843   3708   3895    -22    151    -16       C  
ATOM    912  O   VAL A 125      22.474 -14.081   5.641  1.00 34.70           O  
ANISOU  912  O   VAL A 125     4445   4281   4458    -22    165     -9       O  
ATOM    913  CB  VAL A 125      23.535 -11.868   3.848  1.00 26.15           C  
ANISOU  913  CB  VAL A 125     3349   3239   3347    -23    115    -11       C  
ATOM    914  CG1 VAL A 125      24.297 -12.017   5.167  1.00 25.38           C  
ANISOU  914  CG1 VAL A 125     3282   3137   3223    -25    128     -4       C  
ATOM    915  CG2 VAL A 125      24.473 -11.402   2.752  1.00 27.19           C  
ANISOU  915  CG2 VAL A 125     3472   3396   3460    -21     86     -9       C  
ATOM    916  N   THR A 126      20.706 -13.343   4.510  1.00 33.17           N  
ANISOU  916  N   THR A 126     4212   4078   4314    -22    165    -21       N  
ATOM    917  CA  THR A 126      19.823 -13.525   5.642  1.00 34.42           C  
ANISOU  917  CA  THR A 126     4378   4209   4488    -23    200    -17       C  
ATOM    918  C   THR A 126      19.864 -15.005   6.077  1.00 37.76           C  
ANISOU  918  C   THR A 126     4803   4621   4921    -22    213    -15       C  
ATOM    919  O   THR A 126      19.719 -15.915   5.236  1.00 35.36           O  
ANISOU  919  O   THR A 126     4476   4319   4639    -21    200    -24       O  
ATOM    920  CB  THR A 126      18.368 -13.261   5.215  1.00 35.85           C  
ANISOU  920  CB  THR A 126     4533   4375   4714    -22    210    -24       C  
ATOM    921  OG1 THR A 126      18.239 -11.958   4.643  1.00 37.11           O  
ANISOU  921  OG1 THR A 126     4684   4543   4871    -21    197    -24       O  
ATOM    922  CG2 THR A 126      17.411 -13.396   6.409  1.00 34.98           C  
ANISOU  922  CG2 THR A 126     4431   4236   4624    -23    251    -20       C  
ATOM    923  N   ASN A 127      19.987 -15.232   7.385  1.00 39.48           N  
ANISOU  923  N   ASN A 127     5047   4828   5125    -22    239     -4       N  
ATOM    924  CA  ASN A 127      20.034 -16.585   7.958  1.00 39.59           C  
ANISOU  924  CA  ASN A 127     5065   4828   5147    -20    256      2       C  
ATOM    925  C   ASN A 127      18.750 -17.395   8.158  1.00 35.89           C  
ANISOU  925  C   ASN A 127     4577   4331   4726    -20    284      1       C  
ATOM    926  O   ASN A 127      17.722 -16.805   8.468  1.00 39.24           O  
ANISOU  926  O   ASN A 127     4997   4740   5170    -21    305      0       O  
ATOM    927  CB  ASN A 127      20.814 -16.495   9.248  1.00 41.80           C  
ANISOU  927  CB  ASN A 127     5381   5111   5387    -19    270     18       C  
ATOM    928  CG  ASN A 127      22.290 -16.557   8.964  1.00 45.97           C  
ANISOU  928  CG  ASN A 127     5921   5664   5879    -18    239     20       C  
ATOM    929  OD1 ASN A 127      22.751 -17.454   8.247  1.00 48.12           O  
ANISOU  929  OD1 ASN A 127     6179   5942   6160    -17    222     17       O  
ATOM    930  ND2 ASN A 127      23.031 -15.595   9.454  1.00 47.25           N  
ANISOU  930  ND2 ASN A 127     6107   5841   6004    -20    232     23       N  
ATOM    931  N   PRO A 128      18.792 -18.764   7.970  1.00 34.62           N  
ANISOU  931  N   PRO A 128     4404   4161   4588    -18    285      1       N  
ATOM    932  CA  PRO A 128      19.887 -19.654   7.518  1.00 30.92           C  
ANISOU  932  CA  PRO A 128     3935   3705   4106    -17    263      1       C  
ATOM    933  C   PRO A 128      19.984 -19.564   6.007  1.00 31.45           C  
ANISOU  933  C   PRO A 128     3975   3789   4184    -18    228    -19       C  
ATOM    934  O   PRO A 128      18.987 -19.746   5.298  1.00 28.77           O  
ANISOU  934  O   PRO A 128     3607   3441   3884    -19    226    -33       O  
ATOM    935  CB  PRO A 128      19.393 -21.035   7.925  1.00 31.21           C  
ANISOU  935  CB  PRO A 128     3962   3716   4181    -15    287      7       C  
ATOM    936  CG  PRO A 128      17.917 -20.934   7.792  1.00 31.77           C  
ANISOU  936  CG  PRO A 128     4009   3765   4298    -18    306     -1       C  
ATOM    937  CD  PRO A 128      17.577 -19.554   8.284  1.00 31.00           C  
ANISOU  937  CD  PRO A 128     3927   3672   4179    -19    316      2       C  
ATOM    938  N   VAL A 129      21.168 -19.250   5.511  1.00 30.56           N  
ANISOU  938  N   VAL A 129     3871   3703   4036    -17    199    -20       N  
ATOM    939  CA  VAL A 129      21.254 -18.656   4.190  1.00 28.80           C  
ANISOU  939  CA  VAL A 129     3630   3502   3811    -17    168    -35       C  
ATOM    940  C   VAL A 129      20.922 -19.663   3.128  1.00 27.93           C  
ANISOU  940  C   VAL A 129     3488   3391   3733    -17    155    -54       C  
ATOM    941  O   VAL A 129      20.343 -19.326   2.073  1.00 29.93           O  
ANISOU  941  O   VAL A 129     3717   3653   4000    -17    137    -70       O  
ATOM    942  CB  VAL A 129      22.627 -17.901   3.982  1.00 29.98           C  
ANISOU  942  CB  VAL A 129     3798   3680   3913    -17    144    -30       C  
ATOM    943  CG1 VAL A 129      23.765 -18.778   4.408  1.00 29.45           C  
ANISOU  943  CG1 VAL A 129     3746   3617   3827    -15    142    -21       C  
ATOM    944  CG2 VAL A 129      22.825 -17.430   2.525  1.00 32.61           C  
ANISOU  944  CG2 VAL A 129     4110   4037   4241    -16    113    -43       C  
ATOM    945  N   ASP A 130      21.260 -20.924   3.406  1.00 29.63           N  
ANISOU  945  N   ASP A 130     3703   3594   3961    -16    163    -54       N  
ATOM    946  CA  ASP A 130      21.100 -22.007   2.416  1.00 27.75           C  
ANISOU  946  CA  ASP A 130     3436   3354   3753    -15    149    -75       C  
ATOM    947  C   ASP A 130      19.613 -22.242   2.158  1.00 27.42           C  
ANISOU  947  C   ASP A 130     3366   3291   3761    -18    160    -89       C  
ATOM    948  O   ASP A 130      19.177 -22.467   1.014  1.00 28.14           O  
ANISOU  948  O   ASP A 130     3427   3389   3872    -18    140   -113       O  
ATOM    949  CB  ASP A 130      21.886 -23.247   2.836  1.00 27.89           C  
ANISOU  949  CB  ASP A 130     3461   3362   3775    -13    156    -69       C  
ATOM    950  CG  ASP A 130      23.433 -22.939   3.080  1.00 28.88           C  
ANISOU  950  CG  ASP A 130     3612   3509   3849    -10    142    -55       C  
ATOM    951  OD1 ASP A 130      24.222 -22.841   2.077  1.00 28.46           O  
ANISOU  951  OD1 ASP A 130     3552   3481   3778     -9    114    -67       O  
ATOM    952  OD2 ASP A 130      23.866 -22.793   4.289  1.00 28.43           O  
ANISOU  952  OD2 ASP A 130     3584   3447   3771     -9    159    -31       O  
ATOM    953  N   VAL A 131      18.833 -22.106   3.214  1.00 27.18           N  
ANISOU  953  N   VAL A 131     3343   3235   3748    -19    192    -75       N  
ATOM    954  CA  VAL A 131      17.361 -22.004   3.123  1.00 27.90           C  
ANISOU  954  CA  VAL A 131     3410   3306   3884    -22    206    -84       C  
ATOM    955  C   VAL A 131      16.876 -20.679   2.528  1.00 26.60           C  
ANISOU  955  C   VAL A 131     3238   3158   3709    -22    190    -89       C  
ATOM    956  O   VAL A 131      16.239 -20.616   1.403  1.00 26.50           O  
ANISOU  956  O   VAL A 131     3194   3153   3719    -22    168   -110       O  
ATOM    957  CB  VAL A 131      16.725 -22.199   4.520  1.00 28.03           C  
ANISOU  957  CB  VAL A 131     3440   3291   3919    -22    250    -63       C  
ATOM    958  CG1 VAL A 131      15.217 -21.983   4.430  1.00 30.33           C  
ANISOU  958  CG1 VAL A 131     3705   3561   4257    -25    265    -72       C  
ATOM    959  CG2 VAL A 131      17.007 -23.618   4.964  1.00 29.22           C  
ANISOU  959  CG2 VAL A 131     3590   3421   4090    -22    266    -58       C  
ATOM    960  N   MET A 132      17.202 -19.583   3.191  1.00 25.63           N  
ANISOU  960  N   MET A 132     3142   3042   3552    -21    198    -72       N  
ATOM    961  CA  MET A 132      16.746 -18.312   2.598  1.00 25.65           C  
ANISOU  961  CA  MET A 132     3136   3059   3549    -21    183    -75       C  
ATOM    962  C   MET A 132      17.085 -18.117   1.084  1.00 25.70           C  
ANISOU  962  C   MET A 132     3123   3096   3546    -18    142    -91       C  
ATOM    963  O   MET A 132      16.248 -17.616   0.374  1.00 25.22           O  
ANISOU  963  O   MET A 132     3038   3038   3503    -17    131   -100       O  
ATOM    964  CB  MET A 132      17.162 -17.145   3.448  1.00 27.45           C  
ANISOU  964  CB  MET A 132     3394   3291   3742    -20    195    -57       C  
ATOM    965  CG  MET A 132      16.683 -17.254   4.918  1.00 28.05           C  
ANISOU  965  CG  MET A 132     3489   3339   3826    -22    237    -42       C  
ATOM    966  SD  MET A 132      14.882 -17.201   4.815  1.00 32.44           S  
ANISOU  966  SD  MET A 132     4014   3868   4443    -23    258    -51       S  
ATOM    967  CE  MET A 132      14.462 -18.110   6.317  1.00 29.18           C  
ANISOU  967  CE  MET A 132     3616   3421   4048    -24    306    -36       C  
ATOM    968  N   VAL A 133      18.268 -18.524   0.592  1.00 25.28           N  
ANISOU  968  N   VAL A 133     3077   3065   3462    -17    121    -95       N  
ATOM    969  CA  VAL A 133      18.630 -18.270  -0.821  1.00 25.99           C  
ANISOU  969  CA  VAL A 133     3151   3187   3537    -13     85   -109       C  
ATOM    970  C   VAL A 133      17.713 -19.029  -1.764  1.00 25.54           C  
ANISOU  970  C   VAL A 133     3057   3126   3518    -13     72   -134       C  
ATOM    971  O   VAL A 133      17.369 -18.545  -2.827  1.00 25.98           O  
ANISOU  971  O   VAL A 133     3094   3204   3573    -10     47   -144       O  
ATOM    972  CB  VAL A 133      20.164 -18.513  -1.116  1.00 26.31           C  
ANISOU  972  CB  VAL A 133     3207   3251   3536    -11     67   -106       C  
ATOM    973  CG1 VAL A 133      20.496 -19.970  -1.047  1.00 26.30           C  
ANISOU  973  CG1 VAL A 133     3202   3239   3551    -12     71   -118       C  
ATOM    974  CG2 VAL A 133      20.575 -18.005  -2.498  1.00 27.84           C  
ANISOU  974  CG2 VAL A 133     3389   3481   3708     -7     34   -116       C  
ATOM    975  N   GLN A 134      17.343 -20.265  -1.383  1.00 26.24           N  
ANISOU  975  N   GLN A 134     3137   3191   3643    -16     88   -144       N  
ATOM    976  CA  GLN A 134      16.500 -21.070  -2.215  1.00 24.99           C  
ANISOU  976  CA  GLN A 134     2942   3026   3524    -16     76   -171       C  
ATOM    977  C   GLN A 134      15.070 -20.491  -2.250  1.00 25.14           C  
ANISOU  977  C   GLN A 134     2940   3032   3580    -17     82   -173       C  
ATOM    978  O   GLN A 134      14.440 -20.318  -3.342  1.00 24.44           O  
ANISOU  978  O   GLN A 134     2822   2958   3503    -15     56   -192       O  
ATOM    979  CB  GLN A 134      16.523 -22.564  -1.815  1.00 24.56           C  
ANISOU  979  CB  GLN A 134     2881   2946   3504    -20     93   -181       C  
ATOM    980  CG  GLN A 134      15.629 -23.336  -2.777  1.00 24.42           C  
ANISOU  980  CG  GLN A 134     2823   2923   3530    -21     77   -215       C  
ATOM    981  CD  GLN A 134      15.808 -24.822  -2.678  1.00 25.43           C  
ANISOU  981  CD  GLN A 134     2940   3029   3691    -24     86   -230       C  
ATOM    982  OE1 GLN A 134      16.106 -25.345  -1.602  1.00 24.39           O  
ANISOU  982  OE1 GLN A 134     2826   2872   3567    -25    116   -211       O  
ATOM    983  NE2 GLN A 134      15.666 -25.510  -3.790  1.00 24.54           N  
ANISOU  983  NE2 GLN A 134     2800   2927   3596    -23     61   -264       N  
ATOM    984  N   LEU A 135      14.558 -20.167  -1.071  1.00 25.43           N  
ANISOU  984  N   LEU A 135     2989   3041   3631    -20    116   -154       N  
ATOM    985  CA  LEU A 135      13.312 -19.384  -1.032  1.00 26.62           C  
ANISOU  985  CA  LEU A 135     3123   3180   3811    -20    123   -152       C  
ATOM    986  C   LEU A 135      13.335 -18.170  -2.008  1.00 26.88           C  
ANISOU  986  C   LEU A 135     3149   3245   3817    -15     92   -151       C  
ATOM    987  O   LEU A 135      12.385 -18.000  -2.842  1.00 25.41           O  
ANISOU  987  O   LEU A 135     2931   3064   3659    -13     74   -166       O  
ATOM    988  CB  LEU A 135      13.012 -18.887   0.379  1.00 27.04           C  
ANISOU  988  CB  LEU A 135     3199   3207   3867    -22    164   -128       C  
ATOM    989  CG  LEU A 135      12.715 -20.123   1.272  1.00 28.50           C  
ANISOU  989  CG  LEU A 135     3383   3357   4086    -26    196   -127       C  
ATOM    990  CD1 LEU A 135      12.618 -19.817   2.772  1.00 27.44           C  
ANISOU  990  CD1 LEU A 135     3277   3200   3946    -27    239   -102       C  
ATOM    991  CD2 LEU A 135      11.414 -20.783   0.809  1.00 30.14           C  
ANISOU  991  CD2 LEU A 135     3550   3544   4358    -28    198   -147       C  
ATOM    992  N   LEU A 136      14.406 -17.350  -1.945  1.00 24.89           N  
ANISOU  992  N   LEU A 136     2925   3016   3516    -13     85   -135       N  
ATOM    993  CA  LEU A 136      14.384 -16.160  -2.778  1.00 25.04           C  
ANISOU  993  CA  LEU A 136     2937   3060   3513     -8     60   -130       C  
ATOM    994  C   LEU A 136      14.549 -16.511  -4.263  1.00 25.91           C  
ANISOU  994  C   LEU A 136     3024   3203   3615     -3     21   -150       C  
ATOM    995  O   LEU A 136      14.017 -15.812  -5.119  1.00 26.56           O  
ANISOU  995  O   LEU A 136     3087   3303   3699      1      0   -151       O  
ATOM    996  CB  LEU A 136      15.438 -15.152  -2.367  1.00 24.55           C  
ANISOU  996  CB  LEU A 136     2909   3013   3406     -6     63   -108       C  
ATOM    997  CG  LEU A 136      15.335 -13.774  -3.034  1.00 24.25           C  
ANISOU  997  CG  LEU A 136     2865   2994   3353     -1     45    -96       C  
ATOM    998  CD1 LEU A 136      13.999 -13.061  -2.911  1.00 23.68           C  
ANISOU  998  CD1 LEU A 136     2774   2905   3319      0     55    -92       C  
ATOM    999  CD2 LEU A 136      16.452 -12.935  -2.476  1.00 23.90           C  
ANISOU  999  CD2 LEU A 136     2853   2958   3269     -2     51    -77       C  
ATOM   1000  N   HIS A 137      15.199 -17.647  -4.557  1.00 26.91           N  
ANISOU 1000  N   HIS A 137     3151   3337   3735     -4     12   -166       N  
ATOM   1001  CA  HIS A 137      15.323 -18.124  -5.939  1.00 28.07           C  
ANISOU 1001  CA  HIS A 137     3275   3513   3874      0    -22   -191       C  
ATOM   1002  C   HIS A 137      13.976 -18.550  -6.416  1.00 30.16           C  
ANISOU 1002  C   HIS A 137     3503   3768   4187     -1    -30   -213       C  
ATOM   1003  O   HIS A 137      13.632 -18.343  -7.560  1.00 32.01           O  
ANISOU 1003  O   HIS A 137     3715   4028   4417      4    -61   -227       O  
ATOM   1004  CB  HIS A 137      16.269 -19.329  -6.012  1.00 27.61           C  
ANISOU 1004  CB  HIS A 137     3225   3458   3806     -2    -24   -206       C  
ATOM   1005  CG  HIS A 137      16.363 -19.943  -7.380  1.00 27.92           C  
ANISOU 1005  CG  HIS A 137     3241   3526   3840      1    -57   -236       C  
ATOM   1006  ND1 HIS A 137      16.279 -21.268  -7.584  1.00 28.19           N  
ANISOU 1006  ND1 HIS A 137     3259   3549   3901     -1    -58   -264       N  
ATOM   1007  CD2 HIS A 137      16.555 -19.356  -8.635  1.00 29.65           C  
ANISOU 1007  CD2 HIS A 137     3451   3788   4027      9    -90   -242       C  
ATOM   1008  CE1 HIS A 137      16.410 -21.545  -8.919  1.00 30.74           C  
ANISOU 1008  CE1 HIS A 137     3563   3906   4209      3    -91   -291       C  
ATOM   1009  NE2 HIS A 137      16.581 -20.370  -9.570  1.00 30.72           N  
ANISOU 1009  NE2 HIS A 137     3565   3938   4168     10   -111   -276       N  
ATOM   1010  N   GLN A 138      13.219 -19.207  -5.554  1.00 32.36           N  
ANISOU 1010  N   GLN A 138     3774   4007   4511     -7     -2   -217       N  
ATOM   1011  CA  GLN A 138      11.887 -19.666  -5.941  1.00 35.08           C  
ANISOU 1011  CA  GLN A 138     4081   4337   4910     -8     -8   -239       C  
ATOM   1012  C   GLN A 138      10.941 -18.498  -6.111  1.00 34.21           C  
ANISOU 1012  C   GLN A 138     3957   4229   4811     -5    -13   -227       C  
ATOM   1013  O   GLN A 138      10.225 -18.393  -7.091  1.00 32.99           O  
ANISOU 1013  O   GLN A 138     3772   4091   4671     -1    -41   -243       O  
ATOM   1014  CB  GLN A 138      11.305 -20.649  -4.927  1.00 36.90           C  
ANISOU 1014  CB  GLN A 138     4306   4522   5191    -16     26   -243       C  
ATOM   1015  CG  GLN A 138      11.742 -22.075  -5.219  1.00 42.77           C  
ANISOU 1015  CG  GLN A 138     5041   5261   5948    -19     21   -269       C  
ATOM   1016  CD  GLN A 138      11.739 -22.953  -3.979  1.00 45.87           C  
ANISOU 1016  CD  GLN A 138     5444   5611   6371    -25     62   -259       C  
ATOM   1017  OE1 GLN A 138      11.107 -22.616  -2.959  1.00 51.39           O  
ANISOU 1017  OE1 GLN A 138     6150   6282   7093    -28     94   -238       O  
ATOM   1018  NE2 GLN A 138      12.464 -24.075  -4.048  1.00 44.68           N  
ANISOU 1018  NE2 GLN A 138     5296   5457   6221    -27     61   -272       N  
ATOM   1019  N   HIS A 139      10.931 -17.609  -5.155  1.00 32.92           N  
ANISOU 1019  N   HIS A 139     3816   4050   4641     -5     13   -198       N  
ATOM   1020  CA  HIS A 139      10.024 -16.469  -5.315  1.00 32.19           C  
ANISOU 1020  CA  HIS A 139     3708   3957   4563     -1      9   -186       C  
ATOM   1021  C   HIS A 139      10.441 -15.402  -6.343  1.00 32.00           C  
ANISOU 1021  C   HIS A 139     3685   3974   4498      6    -23   -176       C  
ATOM   1022  O   HIS A 139       9.559 -14.773  -6.900  1.00 33.74           O  
ANISOU 1022  O   HIS A 139     3880   4201   4737     11    -38   -175       O  
ATOM   1023  CB  HIS A 139       9.762 -15.849  -3.965  1.00 32.35           C  
ANISOU 1023  CB  HIS A 139     3749   3946   4595     -5     51   -162       C  
ATOM   1024  CG  HIS A 139       9.359 -16.840  -2.886  1.00 33.24           C  
ANISOU 1024  CG  HIS A 139     3864   4018   4745    -12     88   -166       C  
ATOM   1025  ND1 HIS A 139       8.390 -17.768  -3.062  1.00 33.68           N  
ANISOU 1025  ND1 HIS A 139     3886   4053   4854    -15     90   -187       N  
ATOM   1026  CD2 HIS A 139       9.798 -16.976  -1.555  1.00 34.27           C  
ANISOU 1026  CD2 HIS A 139     4026   4125   4866    -16    126   -149       C  
ATOM   1027  CE1 HIS A 139       8.243 -18.496  -1.937  1.00 35.43           C  
ANISOU 1027  CE1 HIS A 139     4119   4241   5102    -21    129   -182       C  
ATOM   1028  NE2 HIS A 139       9.067 -17.986  -0.991  1.00 34.59           N  
ANISOU 1028  NE2 HIS A 139     4053   4133   4956    -21    152   -158       N  
ATOM   1029  N   SER A 140      11.748 -15.191  -6.638  1.00 28.32           N  
ANISOU 1029  N   SER A 140     3244   3537   3979      9    -35   -168       N  
ATOM   1030  CA  SER A 140      12.141 -14.209  -7.662  1.00 26.94           C  
ANISOU 1030  CA  SER A 140     3067   3401   3766     18    -65   -157       C  
ATOM   1031  C   SER A 140      11.977 -14.640  -9.130  1.00 27.00           C  
ANISOU 1031  C   SER A 140     3047   3444   3765     25   -107   -179       C  
ATOM   1032  O   SER A 140      11.832 -13.792  -9.981  1.00 26.03           O  
ANISOU 1032  O   SER A 140     2914   3349   3625     34   -131   -169       O  
ATOM   1033  CB  SER A 140      13.590 -13.734  -7.491  1.00 26.60           C  
ANISOU 1033  CB  SER A 140     3060   3375   3670     19    -63   -138       C  
ATOM   1034  OG  SER A 140      14.479 -14.848  -7.533  1.00 25.22           O  
ANISOU 1034  OG  SER A 140     2896   3207   3478     16    -65   -155       O  
ATOM   1035  N   GLY A 141      12.038 -15.942  -9.411  1.00 27.00           N  
ANISOU 1035  N   GLY A 141     3037   3445   3776     21   -114   -210       N  
ATOM   1036  CA  GLY A 141      12.119 -16.467 -10.778  1.00 26.36           C  
ANISOU 1036  CA  GLY A 141     2935   3402   3678     27   -153   -237       C  
ATOM   1037  C   GLY A 141      13.474 -16.238 -11.460  1.00 27.90           C  
ANISOU 1037  C   GLY A 141     3152   3637   3812     33   -170   -230       C  
ATOM   1038  O   GLY A 141      13.579 -16.367 -12.674  1.00 28.29           O  
ANISOU 1038  O   GLY A 141     3186   3724   3837     41   -202   -245       O  
ATOM   1039  N   VAL A 142      14.534 -15.880 -10.723  1.00 27.12           N  
ANISOU 1039  N   VAL A 142     3086   3531   3685     31   -148   -206       N  
ATOM   1040  CA  VAL A 142      15.801 -15.630 -11.434  1.00 27.56           C  
ANISOU 1040  CA  VAL A 142     3158   3624   3686     37   -164   -199       C  
ATOM   1041  C   VAL A 142      16.520 -16.949 -11.807  1.00 27.85           C  
ANISOU 1041  C   VAL A 142     3197   3672   3713     35   -172   -230       C  
ATOM   1042  O   VAL A 142      16.330 -17.989 -11.152  1.00 25.52           O  
ANISOU 1042  O   VAL A 142     2899   3346   3450     27   -155   -248       O  
ATOM   1043  CB  VAL A 142      16.746 -14.654 -10.705  1.00 27.84           C  
ANISOU 1043  CB  VAL A 142     3227   3656   3694     36   -145   -164       C  
ATOM   1044  CG1 VAL A 142      16.045 -13.334 -10.395  1.00 26.45           C  
ANISOU 1044  CG1 VAL A 142     3048   3469   3530     38   -138   -137       C  
ATOM   1045  CG2 VAL A 142      17.298 -15.303  -9.452  1.00 27.44           C  
ANISOU 1045  CG2 VAL A 142     3199   3572   3652     26   -115   -164       C  
ATOM   1046  N   PRO A 143      17.360 -16.900 -12.861  1.00 28.96           N  
ANISOU 1046  N   PRO A 143     3340   3854   3808     42   -195   -234       N  
ATOM   1047  CA  PRO A 143      18.093 -18.106 -13.310  1.00 29.23           C  
ANISOU 1047  CA  PRO A 143     3374   3901   3831     42   -202   -264       C  
ATOM   1048  C   PRO A 143      19.018 -18.535 -12.193  1.00 29.13           C  
ANISOU 1048  C   PRO A 143     3388   3859   3819     34   -173   -254       C  
ATOM   1049  O   PRO A 143      19.349 -17.721 -11.331  1.00 24.78           O  
ANISOU 1049  O   PRO A 143     2858   3293   3261     32   -154   -222       O  
ATOM   1050  CB  PRO A 143      18.888 -17.622 -14.521  1.00 29.84           C  
ANISOU 1050  CB  PRO A 143     3455   4029   3854     53   -227   -260       C  
ATOM   1051  CG  PRO A 143      18.131 -16.380 -14.997  1.00 31.00           C  
ANISOU 1051  CG  PRO A 143     3589   4193   3993     61   -241   -237       C  
ATOM   1052  CD  PRO A 143      17.637 -15.729 -13.718  1.00 30.23           C  
ANISOU 1052  CD  PRO A 143     3502   4054   3928     53   -214   -211       C  
ATOM   1053  N   LYS A 144      19.296 -19.846 -12.158  1.00 29.55           N  
ANISOU 1053  N   LYS A 144     3436   3902   3888     30   -169   -283       N  
ATOM   1054  CA  LYS A 144      19.969 -20.475 -11.044  1.00 29.93           C  
ANISOU 1054  CA  LYS A 144     3505   3918   3948     23   -142   -276       C  
ATOM   1055  C   LYS A 144      21.414 -19.974 -10.981  1.00 28.81           C  
ANISOU 1055  C   LYS A 144     3391   3795   3759     26   -139   -253       C  
ATOM   1056  O   LYS A 144      22.074 -20.054  -9.922  1.00 26.59           O  
ANISOU 1056  O   LYS A 144     3132   3491   3478     21   -117   -234       O  
ATOM   1057  CB  LYS A 144      19.939 -22.018 -11.221  1.00 32.75           C  
ANISOU 1057  CB  LYS A 144     3846   4261   4333     19   -142   -313       C  
ATOM   1058  CG  LYS A 144      20.517 -22.515 -12.528  1.00 36.17           C  
ANISOU 1058  CG  LYS A 144     4269   4733   4739     26   -168   -342       C  
ATOM   1059  CD  LYS A 144      21.189 -23.888 -12.395  1.00 42.26           C  
ANISOU 1059  CD  LYS A 144     5040   5489   5527     23   -159   -367       C  
ATOM   1060  CE  LYS A 144      21.732 -24.304 -13.758  1.00 45.96           C  
ANISOU 1060  CE  LYS A 144     5497   5998   5965     30   -184   -399       C  
ATOM   1061  NZ  LYS A 144      20.573 -24.375 -14.714  1.00 47.18           N  
ANISOU 1061  NZ  LYS A 144     5621   6170   6133     33   -210   -430       N  
ATOM   1062  N   ASN A 145      21.915 -19.450 -12.105  1.00 26.81           N  
ANISOU 1062  N   ASN A 145     3136   3585   3466     34   -162   -252       N  
ATOM   1063  CA  ASN A 145      23.261 -18.967 -12.056  1.00 27.57           C  
ANISOU 1063  CA  ASN A 145     3255   3697   3522     37   -158   -230       C  
ATOM   1064  C   ASN A 145      23.287 -17.470 -11.802  1.00 27.14           C  
ANISOU 1064  C   ASN A 145     3213   3648   3449     39   -155   -193       C  
ATOM   1065  O   ASN A 145      24.325 -16.863 -11.965  1.00 26.39           O  
ANISOU 1065  O   ASN A 145     3134   3572   3320     42   -156   -174       O  
ATOM   1066  CB  ASN A 145      23.929 -19.235 -13.364  1.00 31.16           C  
ANISOU 1066  CB  ASN A 145     3702   4193   3941     45   -180   -248       C  
ATOM   1067  CG  ASN A 145      23.142 -18.649 -14.476  1.00 32.56           C  
ANISOU 1067  CG  ASN A 145     3860   4403   4106     54   -204   -253       C  
ATOM   1068  OD1 ASN A 145      21.930 -18.930 -14.590  1.00 35.07           O  
ANISOU 1068  OD1 ASN A 145     4156   4711   4455     52   -212   -272       O  
ATOM   1069  ND2 ASN A 145      23.764 -17.732 -15.227  1.00 33.04           N  
ANISOU 1069  ND2 ASN A 145     3928   4501   4124     62   -215   -233       N  
ATOM   1070  N   LYS A 146      22.174 -16.847 -11.408  1.00 25.30           N  
ANISOU 1070  N   LYS A 146     2973   3398   3241     37   -150   -183       N  
ATOM   1071  CA  LYS A 146      22.250 -15.419 -11.144  1.00 24.89           C  
ANISOU 1071  CA  LYS A 146     2934   3349   3175     38   -146   -149       C  
ATOM   1072  C   LYS A 146      21.909 -15.217  -9.668  1.00 24.77           C  
ANISOU 1072  C   LYS A 146     2933   3291   3187     29   -118   -135       C  
ATOM   1073  O   LYS A 146      21.698 -14.093  -9.207  1.00 25.99           O  
ANISOU 1073  O   LYS A 146     3095   3436   3341     29   -109   -110       O  
ATOM   1074  CB  LYS A 146      21.327 -14.639 -12.026  1.00 25.69           C  
ANISOU 1074  CB  LYS A 146     3014   3470   3275     46   -165   -144       C  
ATOM   1075  CG  LYS A 146      21.537 -14.802 -13.553  1.00 27.15           C  
ANISOU 1075  CG  LYS A 146     3183   3702   3428     57   -194   -158       C  
ATOM   1076  CD  LYS A 146      22.747 -14.021 -14.075  1.00 29.00           C  
ANISOU 1076  CD  LYS A 146     3432   3967   3617     63   -198   -134       C  
ATOM   1077  CE  LYS A 146      22.563 -12.516 -13.872  1.00 29.57           C  
ANISOU 1077  CE  LYS A 146     3510   4037   3687     66   -193    -96       C  
ATOM   1078  NZ  LYS A 146      21.389 -12.038 -14.669  1.00 30.70           N  
ANISOU 1078  NZ  LYS A 146     3629   4196   3837     74   -213    -95       N  
ATOM   1079  N   ILE A 147      21.913 -16.289  -8.886  1.00 24.96           N  
ANISOU 1079  N   ILE A 147     2961   3288   3233     23   -102   -149       N  
ATOM   1080  CA  ILE A 147      21.615 -16.127  -7.427  1.00 23.46           C  
ANISOU 1080  CA  ILE A 147     2788   3060   3066     15    -73   -134       C  
ATOM   1081  C   ILE A 147      22.380 -17.006  -6.531  1.00 23.97           C  
ANISOU 1081  C   ILE A 147     2870   3105   3131     10    -56   -136       C  
ATOM   1082  O   ILE A 147      22.439 -18.222  -6.817  1.00 25.52           O  
ANISOU 1082  O   ILE A 147     3056   3299   3340      9    -60   -158       O  
ATOM   1083  CB  ILE A 147      20.092 -16.299  -7.093  1.00 24.47           C  
ANISOU 1083  CB  ILE A 147     2897   3161   3239     12    -64   -143       C  
ATOM   1084  CG1 ILE A 147      19.890 -16.216  -5.564  1.00 23.20           C  
ANISOU 1084  CG1 ILE A 147     2756   2963   3096      5    -31   -128       C  
ATOM   1085  CG2 ILE A 147      19.533 -17.595  -7.774  1.00 24.98           C  
ANISOU 1085  CG2 ILE A 147     2936   3227   3329     12    -76   -177       C  
ATOM   1086  CD1 ILE A 147      18.501 -15.868  -5.036  1.00 22.74           C  
ANISOU 1086  CD1 ILE A 147     2685   2877   3077      3    -15   -126       C  
ATOM   1087  N   ILE A 148      22.904 -16.450  -5.404  1.00 23.02           N  
ANISOU 1087  N   ILE A 148     2776   2969   3000      6    -38   -113       N  
ATOM   1088  CA  ILE A 148      23.799 -17.193  -4.546  1.00 23.41           C  
ANISOU 1088  CA  ILE A 148     2845   3005   3042      2    -24   -109       C  
ATOM   1089  C   ILE A 148      23.729 -16.842  -3.084  1.00 23.37           C  
ANISOU 1089  C   ILE A 148     2863   2974   3043     -2      1    -91       C  
ATOM   1090  O   ILE A 148      23.290 -15.776  -2.687  1.00 22.56           O  
ANISOU 1090  O   ILE A 148     2767   2865   2939     -3      8    -78       O  
ATOM   1091  CB  ILE A 148      25.342 -17.084  -4.888  1.00 23.23           C  
ANISOU 1091  CB  ILE A 148     2836   3007   2981      5    -37   -102       C  
ATOM   1092  CG1 ILE A 148      25.832 -15.626  -5.005  1.00 22.32           C  
ANISOU 1092  CG1 ILE A 148     2733   2909   2839      6    -43    -81       C  
ATOM   1093  CG2 ILE A 148      25.701 -18.048  -6.028  1.00 23.34           C  
ANISOU 1093  CG2 ILE A 148     2833   3042   2993      9    -55   -125       C  
ATOM   1094  CD1 ILE A 148      27.369 -15.491  -5.200  1.00 22.82           C  
ANISOU 1094  CD1 ILE A 148     2808   2991   2868      7    -52    -72       C  
ATOM   1095  N   GLY A 149      24.262 -17.706  -2.267  1.00 23.99           N  
ANISOU 1095  N   GLY A 149     2955   3036   3122     -4     14    -89       N  
ATOM   1096  CA  GLY A 149      24.179 -17.392  -0.821  1.00 27.03           C  
ANISOU 1096  CA  GLY A 149     3363   3398   3507     -8     39    -71       C  
ATOM   1097  C   GLY A 149      25.565 -17.171  -0.259  1.00 31.22           C  
ANISOU 1097  C   GLY A 149     3920   3938   4003     -9     37    -56       C  
ATOM   1098  O   GLY A 149      26.534 -17.761  -0.736  1.00 29.76           O  
ANISOU 1098  O   GLY A 149     3733   3767   3804     -7     23    -61       O  
ATOM   1099  N   LEU A 150      25.641 -16.332   0.771  1.00 34.74           N  
ANISOU 1099  N   LEU A 150     4387   4375   4436    -12     51    -41       N  
ATOM   1100  CA  LEU A 150      26.870 -16.061   1.461  1.00 35.49           C  
ANISOU 1100  CA  LEU A 150     4507   4476   4499    -13     49    -28       C  
ATOM   1101  C   LEU A 150      27.152 -17.143   2.465  1.00 37.89           C  
ANISOU 1101  C   LEU A 150     4824   4764   4806    -13     64    -22       C  
ATOM   1102  O   LEU A 150      26.325 -17.422   3.362  1.00 37.00           O  
ANISOU 1102  O   LEU A 150     4718   4629   4710    -14     88    -18       O  
ATOM   1103  CB  LEU A 150      26.843 -14.713   2.189  1.00 33.44           C  
ANISOU 1103  CB  LEU A 150     4265   4214   4225    -16     57    -16       C  
ATOM   1104  CG  LEU A 150      28.063 -14.528   3.115  1.00 33.21           C  
ANISOU 1104  CG  LEU A 150     4262   4189   4165    -18     56     -5       C  
ATOM   1105  CD1 LEU A 150      29.351 -14.328   2.324  1.00 30.61           C  
ANISOU 1105  CD1 LEU A 150     3930   3885   3815    -17     31     -3       C  
ATOM   1106  CD2 LEU A 150      27.905 -13.372   4.115  1.00 32.71           C  
ANISOU 1106  CD2 LEU A 150     4219   4117   4090    -22     69      2       C  
ATOM   1107  N   GLY A 151      28.343 -17.733   2.320  1.00 36.98           N  
ANISOU 1107  N   GLY A 151     4713   4661   4675    -11     52    -20       N  
ATOM   1108  CA  GLY A 151      28.787 -18.780   3.209  1.00 32.29           C  
ANISOU 1108  CA  GLY A 151     4132   4054   4082     -9     63    -11       C  
ATOM   1109  C   GLY A 151      30.293 -18.934   3.259  1.00 31.97           C  
ANISOU 1109  C   GLY A 151     4102   4029   4015     -7     47     -4       C  
ATOM   1110  O   GLY A 151      30.960 -18.407   4.173  1.00 31.46           O  
ANISOU 1110  O   GLY A 151     4060   3968   3925     -9     48      9       O  
ATOM   1111  N   GLY A 152      30.831 -19.682   2.299  1.00 28.25           N  
ANISOU 1111  N   GLY A 152     3613   3568   3550     -4     33    -14       N  
ATOM   1112  CA  GLY A 152      32.217 -20.139   2.358  1.00 27.04           C  
ANISOU 1112  CA  GLY A 152     3467   3426   3381     -1     21     -7       C  
ATOM   1113  C   GLY A 152      33.264 -19.055   2.427  1.00 25.45           C  
ANISOU 1113  C   GLY A 152     3277   3243   3147     -3      6      1       C  
ATOM   1114  O   GLY A 152      34.246 -19.165   3.194  1.00 27.31           O  
ANISOU 1114  O   GLY A 152     3529   3481   3366     -2      2     14       O  
ATOM   1115  N   VAL A 153      33.000 -17.924   1.761  1.00 25.72           N  
ANISOU 1115  N   VAL A 153     3307   3291   3174     -6     -1     -3       N  
ATOM   1116  CA  VAL A 153      34.006 -16.863   1.750  1.00 21.80           C  
ANISOU 1116  CA  VAL A 153     2819   2811   2652     -8    -15      5       C  
ATOM   1117  C   VAL A 153      34.251 -16.468   3.166  1.00 23.17           C  
ANISOU 1117  C   VAL A 153     3017   2974   2810    -11     -7     18       C  
ATOM   1118  O   VAL A 153      35.408 -16.352   3.575  1.00 23.45           O  
ANISOU 1118  O   VAL A 153     3064   3018   2827    -12    -18     26       O  
ATOM   1119  CB  VAL A 153      33.672 -15.724   0.839  1.00 21.99           C  
ANISOU 1119  CB  VAL A 153     2832   2848   2673    -10    -23      1       C  
ATOM   1120  CG1 VAL A 153      34.800 -14.625   0.967  1.00 21.01           C  
ANISOU 1120  CG1 VAL A 153     2719   2737   2526    -13    -35     11       C  
ATOM   1121  CG2 VAL A 153      33.491 -16.294  -0.641  1.00 19.29           C  
ANISOU 1121  CG2 VAL A 153     2465   2520   2341     -5    -33    -13       C  
ATOM   1122  N   LEU A 154      33.182 -16.335   3.933  1.00 23.47           N  
ANISOU 1122  N   LEU A 154     3065   2996   2856    -13     10     19       N  
ATOM   1123  CA  LEU A 154      33.316 -15.790   5.257  1.00 23.76           C  
ANISOU 1123  CA  LEU A 154     3126   3025   2874    -16     19     28       C  
ATOM   1124  C   LEU A 154      33.877 -16.817   6.172  1.00 24.00           C  
ANISOU 1124  C   LEU A 154     3170   3050   2897    -13     23     39       C  
ATOM   1125  O   LEU A 154      34.891 -16.584   6.747  1.00 26.39           O  
ANISOU 1125  O   LEU A 154     3486   3361   3177    -13     12     47       O  
ATOM   1126  CB  LEU A 154      31.945 -15.225   5.726  1.00 24.59           C  
ANISOU 1126  CB  LEU A 154     3236   3115   2990    -19     40     25       C  
ATOM   1127  CG  LEU A 154      31.787 -14.981   7.242  1.00 26.00           C  
ANISOU 1127  CG  LEU A 154     3442   3282   3152    -20     57     33       C  
ATOM   1128  CD1 LEU A 154      32.797 -13.934   7.731  1.00 25.30           C  
ANISOU 1128  CD1 LEU A 154     3370   3206   3035    -24     43     35       C  
ATOM   1129  CD2 LEU A 154      30.317 -14.678   7.642  1.00 25.41           C  
ANISOU 1129  CD2 LEU A 154     3369   3190   3096    -22     83     30       C  
ATOM   1130  N   ASP A 155      33.224 -17.998   6.276  1.00 25.44           N  
ANISOU 1130  N   ASP A 155     3346   3217   3101     -9     38     40       N  
ATOM   1131  CA  ASP A 155      33.722 -19.080   7.071  1.00 25.91           C  
ANISOU 1131  CA  ASP A 155     3416   3270   3158     -4     43     53       C  
ATOM   1132  C   ASP A 155      35.189 -19.377   6.823  1.00 24.03           C  
ANISOU 1132  C   ASP A 155     3175   3047   2906     -1     21     58       C  
ATOM   1133  O   ASP A 155      35.977 -19.603   7.817  1.00 24.07           O  
ANISOU 1133  O   ASP A 155     3199   3055   2892      1     18     74       O  
ATOM   1134  CB  ASP A 155      32.871 -20.391   6.918  1.00 29.55           C  
ANISOU 1134  CB  ASP A 155     3862   3710   3653      0     61     52       C  
ATOM   1135  CG  ASP A 155      31.391 -20.203   7.340  1.00 33.97           C  
ANISOU 1135  CG  ASP A 155     4424   4252   4230     -2     87     50       C  
ATOM   1136  OD1 ASP A 155      31.110 -19.431   8.315  1.00 39.61           O  
ANISOU 1136  OD1 ASP A 155     5160   4965   4925     -4     98     58       O  
ATOM   1137  OD2 ASP A 155      30.503 -20.846   6.722  1.00 38.05           O  
ANISOU 1137  OD2 ASP A 155     4921   4756   4781     -1     97     40       O  
ATOM   1138  N   THR A 156      35.567 -19.441   5.565  1.00 22.02           N  
ANISOU 1138  N   THR A 156     2900   2804   2662     -1      6     47       N  
ATOM   1139  CA  THR A 156      36.965 -19.745   5.250  1.00 22.74           C  
ANISOU 1139  CA  THR A 156     2987   2909   2744      1    -12     50       C  
ATOM   1140  C   THR A 156      37.878 -18.594   5.555  1.00 21.17           C  
ANISOU 1140  C   THR A 156     2800   2726   2517     -2    -28     56       C  
ATOM   1141  O   THR A 156      39.047 -18.873   5.877  1.00 20.58           O  
ANISOU 1141  O   THR A 156     2728   2658   2430      0    -41     65       O  
ATOM   1142  CB  THR A 156      37.309 -20.127   3.759  1.00 23.05           C  
ANISOU 1142  CB  THR A 156     3001   2959   2798      3    -24     36       C  
ATOM   1143  OG1 THR A 156      37.037 -19.040   2.894  1.00 24.70           O  
ANISOU 1143  OG1 THR A 156     3202   3181   3002      0    -31     26       O  
ATOM   1144  CG2 THR A 156      36.617 -21.372   3.238  1.00 24.23           C  
ANISOU 1144  CG2 THR A 156     3132   3094   2978      8    -13     25       C  
ATOM   1145  N   SER A 157      37.391 -17.325   5.496  1.00 20.19           N  
ANISOU 1145  N   SER A 157     2680   2605   2384     -8    -27     50       N  
ATOM   1146  CA  SER A 157      38.330 -16.253   5.703  1.00 20.47           C  
ANISOU 1146  CA  SER A 157     2723   2653   2398    -13    -43     53       C  
ATOM   1147  C   SER A 157      38.786 -16.364   7.183  1.00 20.75           C  
ANISOU 1147  C   SER A 157     2783   2686   2413    -12    -43     64       C  
ATOM   1148  O   SER A 157      39.909 -15.964   7.532  1.00 20.11           O  
ANISOU 1148  O   SER A 157     2708   2615   2315    -14    -61     69       O  
ATOM   1149  CB  SER A 157      37.704 -14.909   5.486  1.00 21.50           C  
ANISOU 1149  CB  SER A 157     2855   2785   2527    -19    -40     46       C  
ATOM   1150  OG  SER A 157      36.691 -14.673   6.484  1.00 25.36           O  
ANISOU 1150  OG  SER A 157     3361   3259   3013    -21    -22     46       O  
ATOM   1151  N   ARG A 158      37.958 -16.964   8.034  1.00 20.78           N  
ANISOU 1151  N   ARG A 158     2800   2675   2418     -9    -24     70       N  
ATOM   1152  CA  ARG A 158      38.411 -17.070   9.473  1.00 21.91           C  
ANISOU 1152  CA  ARG A 158     2967   2819   2535     -8    -24     83       C  
ATOM   1153  C   ARG A 158      39.318 -18.291   9.625  1.00 24.12           C  
ANISOU 1153  C   ARG A 158     3244   3101   2817      0    -33     97       C  
ATOM   1154  O   ARG A 158      40.207 -18.365  10.509  1.00 25.80           O  
ANISOU 1154  O   ARG A 158     3471   3322   3008      2    -46    109       O  
ATOM   1155  CB  ARG A 158      37.186 -17.261  10.310  1.00 22.62           C  
ANISOU 1155  CB  ARG A 158     3073   2894   2626     -6      1     87       C  
ATOM   1156  CG  ARG A 158      36.318 -16.025  10.188  1.00 22.80           C  
ANISOU 1156  CG  ARG A 158     3098   2914   2650    -13     10     73       C  
ATOM   1157  CD  ARG A 158      34.893 -16.271  10.490  1.00 24.03           C  
ANISOU 1157  CD  ARG A 158     3256   3052   2820    -12     39     72       C  
ATOM   1158  NE  ARG A 158      34.201 -14.985  10.700  1.00 24.46           N  
ANISOU 1158  NE  ARG A 158     3319   3103   2870    -19     48     61       N  
ATOM   1159  CZ  ARG A 158      32.900 -14.978  10.880  1.00 25.32           C  
ANISOU 1159  CZ  ARG A 158     3428   3197   2995    -19     73     58       C  
ATOM   1160  NH1 ARG A 158      32.272 -16.164  10.830  1.00 24.24           N  
ANISOU 1160  NH1 ARG A 158     3283   3046   2878    -13     89     66       N  
ATOM   1161  NH2 ARG A 158      32.236 -13.842  11.129  1.00 25.82           N  
ANISOU 1161  NH2 ARG A 158     3498   3255   3056    -23     84     48       N  
ATOM   1162  N   LEU A 159      39.122 -19.303   8.779  1.00 23.16           N  
ANISOU 1162  N   LEU A 159     3103   2973   2724      4    -28     96       N  
ATOM   1163  CA  LEU A 159      39.998 -20.443   8.932  1.00 22.93           C  
ANISOU 1163  CA  LEU A 159     3069   2943   2699     11    -35    109       C  
ATOM   1164  C   LEU A 159      41.360 -20.050   8.336  1.00 23.88           C  
ANISOU 1164  C   LEU A 159     3178   3080   2812     10    -62    106       C  
ATOM   1165  O   LEU A 159      42.389 -20.277   8.932  1.00 23.71           O  
ANISOU 1165  O   LEU A 159     3163   3066   2778     13    -76    119       O  
ATOM   1166  CB  LEU A 159      39.460 -21.707   8.307  1.00 22.57           C  
ANISOU 1166  CB  LEU A 159     3005   2881   2688     17    -21    107       C  
ATOM   1167  CG  LEU A 159      40.331 -22.961   8.459  1.00 23.53           C  
ANISOU 1167  CG  LEU A 159     3120   2998   2821     26    -26    122       C  
ATOM   1168  CD1 LEU A 159      40.300 -23.451   9.920  1.00 24.07           C  
ANISOU 1168  CD1 LEU A 159     3210   3059   2874     32    -17    147       C  
ATOM   1169  CD2 LEU A 159      39.659 -23.990   7.558  1.00 24.46           C  
ANISOU 1169  CD2 LEU A 159     3215   3100   2977     28    -12    111       C  
ATOM   1170  N   LYS A 160      41.361 -19.432   7.169  1.00 23.30           N  
ANISOU 1170  N   LYS A 160     3088   3014   2748      5    -68     90       N  
ATOM   1171  CA  LYS A 160      42.631 -18.950   6.657  1.00 23.56           C  
ANISOU 1171  CA  LYS A 160     3112   3064   2774      4    -90     89       C  
ATOM   1172  C   LYS A 160      43.405 -18.081   7.648  1.00 24.20           C  
ANISOU 1172  C   LYS A 160     3210   3154   2829      0   -105     96       C  
ATOM   1173  O   LYS A 160      44.619 -18.197   7.783  1.00 24.41           O  
ANISOU 1173  O   LYS A 160     3233   3190   2850      1   -124    103       O  
ATOM   1174  CB  LYS A 160      42.371 -18.202   5.407  1.00 22.31           C  
ANISOU 1174  CB  LYS A 160     2938   2913   2625      0    -91     74       C  
ATOM   1175  CG  LYS A 160      41.713 -19.131   4.412  1.00 21.96           C  
ANISOU 1175  CG  LYS A 160     2876   2863   2605      4    -80     65       C  
ATOM   1176  CD  LYS A 160      41.089 -18.259   3.380  1.00 23.22           C  
ANISOU 1176  CD  LYS A 160     3024   3029   2767      0    -78     51       C  
ATOM   1177  CE  LYS A 160      40.735 -19.110   2.185  1.00 22.61           C  
ANISOU 1177  CE  LYS A 160     2926   2954   2710      4    -74     38       C  
ATOM   1178  NZ  LYS A 160      39.724 -18.429   1.412  1.00 24.07           N  
ANISOU 1178  NZ  LYS A 160     3103   3142   2898      1    -68     27       N  
ATOM   1179  N   TYR A 161      42.692 -17.224   8.338  1.00 23.81           N  
ANISOU 1179  N   TYR A 161     3179   3102   2765     -5    -98     93       N  
ATOM   1180  CA  TYR A 161      43.320 -16.249   9.119  1.00 23.87           C  
ANISOU 1180  CA  TYR A 161     3201   3119   2750    -10   -112     92       C  
ATOM   1181  C   TYR A 161      43.970 -16.866  10.364  1.00 24.38           C  
ANISOU 1181  C   TYR A 161     3281   3186   2794     -5   -121    108       C  
ATOM   1182  O   TYR A 161      45.110 -16.615  10.637  1.00 24.26           O  
ANISOU 1182  O   TYR A 161     3265   3183   2769     -6   -144    111       O  
ATOM   1183  CB  TYR A 161      42.321 -15.097   9.453  1.00 24.11           C  
ANISOU 1183  CB  TYR A 161     3244   3144   2771    -18   -100     81       C  
ATOM   1184  CG  TYR A 161      43.055 -14.038  10.211  1.00 26.33           C  
ANISOU 1184  CG  TYR A 161     3537   3434   3031    -24   -117     77       C  
ATOM   1185  CD1 TYR A 161      43.886 -13.078   9.526  1.00 25.43           C  
ANISOU 1185  CD1 TYR A 161     3409   3328   2924    -31   -134     69       C  
ATOM   1186  CD2 TYR A 161      43.012 -14.033  11.603  1.00 25.67           C  
ANISOU 1186  CD2 TYR A 161     3479   3352   2921    -23   -117     80       C  
ATOM   1187  CE1 TYR A 161      44.607 -12.130  10.212  1.00 25.06           C  
ANISOU 1187  CE1 TYR A 161     3371   3288   2862    -38   -151     63       C  
ATOM   1188  CE2 TYR A 161      43.736 -13.110  12.294  1.00 27.47           C  
ANISOU 1188  CE2 TYR A 161     3717   3589   3129    -29   -135     73       C  
ATOM   1189  CZ  TYR A 161      44.524 -12.166  11.613  1.00 27.33           C  
ANISOU 1189  CZ  TYR A 161     3684   3577   3122    -37   -152     63       C  
ATOM   1190  OH  TYR A 161      45.270 -11.321  12.406  1.00 29.44           O  
ANISOU 1190  OH  TYR A 161     3960   3852   3371    -43   -171     54       O  
ATOM   1191  N   TYR A 162      43.238 -17.697  11.087  1.00 25.50           N  
ANISOU 1191  N   TYR A 162     3437   3319   2933      1   -104    118       N  
ATOM   1192  CA  TYR A 162      43.732 -18.368  12.295  1.00 25.42           C  
ANISOU 1192  CA  TYR A 162     3443   3312   2902      8   -110    137       C  
ATOM   1193  C   TYR A 162      44.922 -19.278  11.928  1.00 25.58           C  
ANISOU 1193  C   TYR A 162     3446   3337   2936     15   -127    149       C  
ATOM   1194  O   TYR A 162      45.909 -19.348  12.668  1.00 22.68           O  
ANISOU 1194  O   TYR A 162     3086   2981   2550     18   -148    160       O  
ATOM   1195  CB  TYR A 162      42.641 -19.222  12.880  1.00 25.62           C  
ANISOU 1195  CB  TYR A 162     3480   3323   2930     15    -83    149       C  
ATOM   1196  CG  TYR A 162      41.456 -18.442  13.348  1.00 26.56           C  
ANISOU 1196  CG  TYR A 162     3616   3437   3038      9    -62    139       C  
ATOM   1197  CD1 TYR A 162      41.614 -17.169  13.932  1.00 27.88           C  
ANISOU 1197  CD1 TYR A 162     3800   3615   3178      2    -72    127       C  
ATOM   1198  CD2 TYR A 162      40.177 -18.993  13.293  1.00 26.57           C  
ANISOU 1198  CD2 TYR A 162     3617   3420   3057     12    -33    141       C  
ATOM   1199  CE1 TYR A 162      40.519 -16.425  14.363  1.00 27.28           C  
ANISOU 1199  CE1 TYR A 162     3738   3532   3093     -2    -52    116       C  
ATOM   1200  CE2 TYR A 162      39.083 -18.296  13.781  1.00 27.03           C  
ANISOU 1200  CE2 TYR A 162     3691   3472   3106      8    -12    133       C  
ATOM   1201  CZ  TYR A 162      39.262 -16.969  14.303  1.00 26.90           C  
ANISOU 1201  CZ  TYR A 162     3690   3468   3063      0    -22    120       C  
ATOM   1202  OH  TYR A 162      38.168 -16.235  14.771  1.00 25.20           O  
ANISOU 1202  OH  TYR A 162     3488   3244   2840     -3      0    110       O  
ATOM   1203  N   ILE A 163      44.860 -19.900  10.749  1.00 24.60           N  
ANISOU 1203  N   ILE A 163     3299   3205   2843     17   -121    145       N  
ATOM   1204  CA  ILE A 163      46.004 -20.728  10.314  1.00 25.51           C  
ANISOU 1204  CA  ILE A 163     3396   3324   2973     24   -136    154       C  
ATOM   1205  C   ILE A 163      47.187 -19.832   9.968  1.00 25.72           C  
ANISOU 1205  C   ILE A 163     3413   3366   2993     18   -162    146       C  
ATOM   1206  O   ILE A 163      48.354 -20.225  10.161  1.00 24.96           O  
ANISOU 1206  O   ILE A 163     3309   3276   2897     22   -181    157       O  
ATOM   1207  CB  ILE A 163      45.641 -21.734   9.201  1.00 26.84           C  
ANISOU 1207  CB  ILE A 163     3541   3479   3176     28   -122    149       C  
ATOM   1208  CG1 ILE A 163      44.782 -22.870   9.802  1.00 25.41           C  
ANISOU 1208  CG1 ILE A 163     3367   3279   3006     36    -99    162       C  
ATOM   1209  CG2 ILE A 163      46.878 -22.468   8.628  1.00 26.66           C  
ANISOU 1209  CG2 ILE A 163     3498   3460   3172     34   -136    154       C  
ATOM   1210  CD1 ILE A 163      44.081 -23.622   8.725  1.00 23.75           C  
ANISOU 1210  CD1 ILE A 163     3137   3055   2830     37    -82    150       C  
ATOM   1211  N   SER A 164      46.910 -18.586   9.578  1.00 26.23           N  
ANISOU 1211  N   SER A 164     3478   3436   3052      8   -163    130       N  
ATOM   1212  CA  SER A 164      47.995 -17.814   9.006  1.00 25.83           C  
ANISOU 1212  CA  SER A 164     3413   3397   3004      2   -183    123       C  
ATOM   1213  C   SER A 164      48.754 -17.289  10.164  1.00 26.63           C  
ANISOU 1213  C   SER A 164     3529   3508   3081      0   -204    128       C  
ATOM   1214  O   SER A 164      49.964 -17.107  10.089  1.00 25.59           O  
ANISOU 1214  O   SER A 164     3385   3385   2951      0   -226    131       O  
ATOM   1215  CB  SER A 164      47.524 -16.750   8.126  1.00 26.01           C  
ANISOU 1215  CB  SER A 164     3428   3420   3032     -6   -177    107       C  
ATOM   1216  OG  SER A 164      47.048 -15.652   8.867  1.00 29.89           O  
ANISOU 1216  OG  SER A 164     3938   3913   3505    -14   -177    100       O  
ATOM   1217  N   GLN A 165      48.050 -17.110  11.267  1.00 27.89           N  
ANISOU 1217  N   GLN A 165     3713   3665   3216      0   -198    130       N  
ATOM   1218  CA  GLN A 165      48.707 -16.598  12.468  1.00 29.88           C  
ANISOU 1218  CA  GLN A 165     3983   3930   3440     -1   -219    132       C  
ATOM   1219  C   GLN A 165      49.664 -17.601  13.033  1.00 28.71           C  
ANISOU 1219  C   GLN A 165     3832   3787   3287      8   -236    152       C  
ATOM   1220  O   GLN A 165      50.791 -17.290  13.189  1.00 32.27           O  
ANISOU 1220  O   GLN A 165     4275   4249   3735      6   -261    153       O  
ATOM   1221  CB  GLN A 165      47.683 -16.035  13.473  1.00 31.76           C  
ANISOU 1221  CB  GLN A 165     4249   4167   3652     -4   -205    126       C  
ATOM   1222  CG  GLN A 165      46.933 -14.806  12.945  1.00 32.63           C  
ANISOU 1222  CG  GLN A 165     4358   4270   3768    -16   -194    105       C  
ATOM   1223  CD  GLN A 165      47.840 -13.825  12.143  1.00 37.21           C  
ANISOU 1223  CD  GLN A 165     4919   4856   4363    -25   -212     92       C  
ATOM   1224  OE1 GLN A 165      47.925 -13.858  10.863  1.00 37.11           O  
ANISOU 1224  OE1 GLN A 165     4883   4840   4377    -26   -208     91       O  
ATOM   1225  NE2 GLN A 165      48.524 -12.944  12.880  1.00 34.63           N  
ANISOU 1225  NE2 GLN A 165     4599   4538   4019    -32   -233     83       N  
ATOM   1226  N   LYS A 166      49.242 -18.842  13.248  1.00 29.06           N  
ANISOU 1226  N   LYS A 166     3880   3823   3337     19   -221    170       N  
ATOM   1227  CA  LYS A 166      50.156 -19.908  13.654  1.00 27.88           C  
ANISOU 1227  CA  LYS A 166     3724   3677   3190     30   -235    193       C  
ATOM   1228  C   LYS A 166      51.368 -20.073  12.765  1.00 26.26           C  
ANISOU 1228  C   LYS A 166     3490   3474   3010     31   -253    192       C  
ATOM   1229  O   LYS A 166      52.471 -20.268  13.252  1.00 26.65           O  
ANISOU 1229  O   LYS A 166     3535   3534   3055     35   -278    204       O  
ATOM   1230  CB  LYS A 166      49.390 -21.253  13.813  1.00 29.57           C  
ANISOU 1230  CB  LYS A 166     3942   3876   3416     42   -210    212       C  
ATOM   1231  CG  LYS A 166      50.274 -22.416  14.225  1.00 31.18           C  
ANISOU 1231  CG  LYS A 166     4139   4080   3627     55   -222    238       C  
ATOM   1232  CD  LYS A 166      50.652 -22.294  15.721  1.00 32.83           C  
ANISOU 1232  CD  LYS A 166     4372   4305   3796     61   -240    256       C  
ATOM   1233  CE  LYS A 166      51.471 -23.481  16.246  1.00 32.81           C  
ANISOU 1233  CE  LYS A 166     4363   4303   3798     76   -252    287       C  
ATOM   1234  NZ  LYS A 166      52.030 -23.128  17.582  1.00 35.25           N  
ANISOU 1234  NZ  LYS A 166     4694   4634   4064     80   -278    300       N  
ATOM   1235  N   LEU A 167      51.197 -19.998  11.454  1.00 25.98           N  
ANISOU 1235  N   LEU A 167     3434   3432   3002     27   -241    179       N  
ATOM   1236  CA  LEU A 167      52.340 -20.224  10.528  1.00 26.84           C  
ANISOU 1236  CA  LEU A 167     3516   3544   3138     28   -254    178       C  
ATOM   1237  C   LEU A 167      53.067 -18.995   9.994  1.00 27.79           C  
ANISOU 1237  C   LEU A 167     3623   3674   3259     17   -270    163       C  
ATOM   1238  O   LEU A 167      53.966 -19.145   9.179  1.00 30.98           O  
ANISOU 1238  O   LEU A 167     4003   4080   3686     18   -278    163       O  
ATOM   1239  CB  LEU A 167      51.899 -21.058   9.346  1.00 27.53           C  
ANISOU 1239  CB  LEU A 167     3585   3619   3256     33   -233    174       C  
ATOM   1240  CG  LEU A 167      51.356 -22.439   9.779  1.00 26.79           C  
ANISOU 1240  CG  LEU A 167     3496   3511   3170     44   -217    191       C  
ATOM   1241  CD1 LEU A 167      50.717 -23.103   8.598  1.00 26.75           C  
ANISOU 1241  CD1 LEU A 167     3474   3493   3195     46   -194    179       C  
ATOM   1242  CD2 LEU A 167      52.489 -23.254  10.310  1.00 27.62           C  
ANISOU 1242  CD2 LEU A 167     3593   3618   3281     54   -235    212       C  
ATOM   1243  N   ASN A 168      52.651 -17.783  10.380  1.00 28.98           N  
ANISOU 1243  N   ASN A 168     3789   3829   3391      7   -273    150       N  
ATOM   1244  CA  ASN A 168      53.330 -16.545   9.995  1.00 28.01           C  
ANISOU 1244  CA  ASN A 168     3655   3714   3272     -3   -288    137       C  
ATOM   1245  C   ASN A 168      53.482 -16.334   8.549  1.00 27.93           C  
ANISOU 1245  C   ASN A 168     3620   3701   3288     -6   -278    129       C  
ATOM   1246  O   ASN A 168      54.604 -16.047   8.097  1.00 26.75           O  
ANISOU 1246  O   ASN A 168     3450   3557   3153     -8   -293    130       O  
ATOM   1247  CB  ASN A 168      54.739 -16.563  10.515  1.00 34.18           C  
ANISOU 1247  CB  ASN A 168     4427   4506   4054     -2   -318    144       C  
ATOM   1248  CG  ASN A 168      54.834 -15.938  11.827  1.00 40.60           C  
ANISOU 1248  CG  ASN A 168     5262   5327   4837     -6   -337    141       C  
ATOM   1249  OD1 ASN A 168      54.365 -16.491  12.820  1.00 42.54           O  
ANISOU 1249  OD1 ASN A 168     5529   5574   5058      0   -336    151       O  
ATOM   1250  ND2 ASN A 168      55.398 -14.722  11.850  1.00 45.55           N  
ANISOU 1250  ND2 ASN A 168     5883   5959   5465    -18   -354    126       N  
ATOM   1251  N   VAL A 169      52.393 -16.500   7.804  1.00 27.00           N  
ANISOU 1251  N   VAL A 169     3503   3577   3176     -5   -253    123       N  
ATOM   1252  CA  VAL A 169      52.350 -16.149   6.389  1.00 27.26           C  
ANISOU 1252  CA  VAL A 169     3517   3611   3229     -8   -242    115       C  
ATOM   1253  C   VAL A 169      51.204 -15.116   6.084  1.00 27.75           C  
ANISOU 1253  C   VAL A 169     3588   3670   3284    -16   -227    103       C  
ATOM   1254  O   VAL A 169      50.261 -14.927   6.892  1.00 26.91           O  
ANISOU 1254  O   VAL A 169     3504   3558   3162    -18   -220    100       O  
ATOM   1255  CB  VAL A 169      52.187 -17.448   5.486  1.00 28.25           C  
ANISOU 1255  CB  VAL A 169     3627   3732   3372      1   -227    118       C  
ATOM   1256  CG1 VAL A 169      53.382 -18.384   5.616  1.00 26.81           C  
ANISOU 1256  CG1 VAL A 169     3431   3551   3202     10   -240    130       C  
ATOM   1257  CG2 VAL A 169      50.898 -18.225   5.824  1.00 25.52           C  
ANISOU 1257  CG2 VAL A 169     3297   3375   3021      6   -208    118       C  
ATOM   1258  N   CYS A 170      51.288 -14.421   4.940  1.00 27.77           N  
ANISOU 1258  N   CYS A 170     3574   3677   3300    -20   -221     97       N  
ATOM   1259  CA  CYS A 170      50.138 -13.668   4.451  1.00 28.06           C  
ANISOU 1259  CA  CYS A 170     3615   3710   3334    -25   -205     89       C  
ATOM   1260  C   CYS A 170      48.839 -14.494   4.609  1.00 27.23           C  
ANISOU 1260  C   CYS A 170     3523   3597   3225    -19   -187     86       C  
ATOM   1261  O   CYS A 170      48.805 -15.637   4.164  1.00 22.76           O  
ANISOU 1261  O   CYS A 170     2948   3029   2667    -11   -181     89       O  
ATOM   1262  CB  CYS A 170      50.258 -13.361   2.965  1.00 29.53           C  
ANISOU 1262  CB  CYS A 170     3779   3903   3535    -24   -197     87       C  
ATOM   1263  SG  CYS A 170      49.332 -11.857   2.650  1.00 38.26           S  
ANISOU 1263  SG  CYS A 170     4890   5007   4640    -33   -187     81       S  
ATOM   1264  N   PRO A 171      47.807 -13.922   5.290  1.00 27.70           N  
ANISOU 1264  N   PRO A 171     3602   3649   3273    -24   -179     81       N  
ATOM   1265  CA  PRO A 171      46.518 -14.565   5.575  1.00 27.94           C  
ANISOU 1265  CA  PRO A 171     3644   3669   3300    -20   -161     80       C  
ATOM   1266  C   PRO A 171      45.908 -15.113   4.346  1.00 27.56           C  
ANISOU 1266  C   PRO A 171     3580   3621   3268    -15   -147     75       C  
ATOM   1267  O   PRO A 171      45.380 -16.228   4.395  1.00 27.16           O  
ANISOU 1267  O   PRO A 171     3530   3563   3223     -9   -137     76       O  
ATOM   1268  CB  PRO A 171      45.676 -13.421   6.161  1.00 28.90           C  
ANISOU 1268  CB  PRO A 171     3783   3786   3412    -28   -154     73       C  
ATOM   1269  CG  PRO A 171      46.721 -12.726   7.019  1.00 29.28           C  
ANISOU 1269  CG  PRO A 171     3838   3839   3448    -34   -174     73       C  
ATOM   1270  CD  PRO A 171      47.939 -12.677   6.067  1.00 28.44           C  
ANISOU 1270  CD  PRO A 171     3707   3741   3355    -34   -188     77       C  
ATOM   1271  N   ARG A 172      46.022 -14.397   3.230  1.00 26.81           N  
ANISOU 1271  N   ARG A 172     3469   3534   3180    -18   -148     71       N  
ATOM   1272  CA  ARG A 172      45.477 -14.923   2.006  1.00 26.86           C  
ANISOU 1272  CA  ARG A 172     3461   3545   3198    -12   -137     65       C  
ATOM   1273  C   ARG A 172      46.295 -16.036   1.312  1.00 27.29           C  
ANISOU 1273  C   ARG A 172     3499   3607   3263     -4   -140     65       C  
ATOM   1274  O   ARG A 172      45.910 -16.492   0.173  1.00 23.61           O  
ANISOU 1274  O   ARG A 172     3018   3147   2805      0   -132     56       O  
ATOM   1275  CB  ARG A 172      45.294 -13.836   0.980  1.00 27.48           C  
ANISOU 1275  CB  ARG A 172     3528   3633   3278    -16   -135     62       C  
ATOM   1276  CG  ARG A 172      43.963 -14.019   0.255  1.00 27.25           C  
ANISOU 1276  CG  ARG A 172     3495   3603   3254    -13   -121     54       C  
ATOM   1277  CD  ARG A 172      43.941 -13.082  -0.939  1.00 27.61           C  
ANISOU 1277  CD  ARG A 172     3526   3662   3301    -13   -121     55       C  
ATOM   1278  NE  ARG A 172      43.057 -13.554  -1.966  1.00 28.25           N  
ANISOU 1278  NE  ARG A 172     3596   3750   3386     -7   -113     46       N  
ATOM   1279  CZ  ARG A 172      41.730 -13.342  -2.079  1.00 31.65           C  
ANISOU 1279  CZ  ARG A 172     4029   4176   3821     -7   -105     41       C  
ATOM   1280  NH1 ARG A 172      41.035 -12.643  -1.152  1.00 27.75           N  
ANISOU 1280  NH1 ARG A 172     3549   3666   3326    -13   -100     43       N  
ATOM   1281  NH2 ARG A 172      41.071 -13.844  -3.177  1.00 29.65           N  
ANISOU 1281  NH2 ARG A 172     3762   3933   3570     -1   -101     31       N  
ATOM   1282  N   ASP A 173      47.473 -16.362   1.876  1.00 25.74           N  
ANISOU 1282  N   ASP A 173     3302   3411   3066     -3   -153     73       N  
ATOM   1283  CA  ASP A 173      48.276 -17.412   1.263  1.00 26.74           C  
ANISOU 1283  CA  ASP A 173     3412   3542   3205      4   -155     74       C  
ATOM   1284  C   ASP A 173      47.848 -18.741   1.798  1.00 25.46           C  
ANISOU 1284  C   ASP A 173     3255   3367   3050     10   -148     74       C  
ATOM   1285  O   ASP A 173      48.286 -19.787   1.350  1.00 26.39           O  
ANISOU 1285  O   ASP A 173     3359   3483   3182     18   -146     73       O  
ATOM   1286  CB  ASP A 173      49.769 -17.115   1.299  1.00 30.01           C  
ANISOU 1286  CB  ASP A 173     3816   3964   3621      3   -170     82       C  
ATOM   1287  CG  ASP A 173      50.198 -16.234   0.084  1.00 38.48           C  
ANISOU 1287  CG  ASP A 173     4871   5051   4696      0   -170     80       C  
ATOM   1288  OD1 ASP A 173      49.327 -15.935  -0.798  1.00 44.40           O  
ANISOU 1288  OD1 ASP A 173     5619   5807   5445      1   -158     72       O  
ATOM   1289  OD2 ASP A 173      51.355 -15.800   0.004  1.00 38.67           O  
ANISOU 1289  OD2 ASP A 173     4885   5081   4725     -1   -180     86       O  
ATOM   1290  N   VAL A 174      46.947 -18.702   2.766  1.00 25.02           N  
ANISOU 1290  N   VAL A 174     3219   3299   2986      8   -142     77       N  
ATOM   1291  CA  VAL A 174      46.264 -19.919   3.248  1.00 23.76           C  
ANISOU 1291  CA  VAL A 174     3065   3125   2836     14   -130     79       C  
ATOM   1292  C   VAL A 174      45.030 -20.103   2.399  1.00 25.76           C  
ANISOU 1292  C   VAL A 174     3311   3374   3100     14   -114     64       C  
ATOM   1293  O   VAL A 174      44.266 -19.148   2.129  1.00 26.54           O  
ANISOU 1293  O   VAL A 174     3414   3477   3192      8   -110     57       O  
ATOM   1294  CB  VAL A 174      45.901 -19.810   4.741  1.00 23.51           C  
ANISOU 1294  CB  VAL A 174     3057   3084   2789     12   -129     91       C  
ATOM   1295  CG1 VAL A 174      45.160 -21.076   5.219  1.00 21.77           C  
ANISOU 1295  CG1 VAL A 174     2842   2847   2583     19   -114     96       C  
ATOM   1296  CG2 VAL A 174      47.218 -19.554   5.538  1.00 21.59           C  
ANISOU 1296  CG2 VAL A 174     2820   2849   2534     12   -150    104       C  
ATOM   1297  N   ASN A 175      44.842 -21.314   1.919  1.00 25.29           N  
ANISOU 1297  N   ASN A 175     3239   3307   3061     21   -106     57       N  
ATOM   1298  CA  ASN A 175      43.657 -21.578   1.173  1.00 24.85           C  
ANISOU 1298  CA  ASN A 175     3176   3248   3018     21    -93     41       C  
ATOM   1299  C   ASN A 175      42.963 -22.757   1.836  1.00 22.71           C  
ANISOU 1299  C   ASN A 175     2908   2954   2765     25    -79     43       C  
ATOM   1300  O   ASN A 175      43.610 -23.708   2.142  1.00 21.63           O  
ANISOU 1300  O   ASN A 175     2768   2809   2640     31    -80     51       O  
ATOM   1301  CB  ASN A 175      44.014 -21.965  -0.264  1.00 26.08           C  
ANISOU 1301  CB  ASN A 175     3309   3416   3184     25    -94     24       C  
ATOM   1302  CG  ASN A 175      42.989 -21.476  -1.251  1.00 28.42           C  
ANISOU 1302  CG  ASN A 175     3598   3721   3479     23    -89      7       C  
ATOM   1303  OD1 ASN A 175      41.779 -21.139  -0.923  1.00 30.38           O  
ANISOU 1303  OD1 ASN A 175     3854   3960   3727     19    -82      5       O  
ATOM   1304  ND2 ASN A 175      43.471 -21.300  -2.457  1.00 32.61           N  
ANISOU 1304  ND2 ASN A 175     4113   4271   4006     26    -94     -2       N  
ATOM   1305  N   ALA A 176      41.640 -22.701   2.026  1.00 22.93           N  
ANISOU 1305  N   ALA A 176     2942   2971   2798     22    -65     37       N  
ATOM   1306  CA  ALA A 176      40.937 -23.799   2.715  1.00 22.38           C  
ANISOU 1306  CA  ALA A 176     2875   2877   2749     26    -49     42       C  
ATOM   1307  C   ALA A 176      39.569 -23.876   2.102  1.00 22.47           C  
ANISOU 1307  C   ALA A 176     2877   2881   2777     23    -37     24       C  
ATOM   1308  O   ALA A 176      39.083 -22.880   1.602  1.00 21.87           O  
ANISOU 1308  O   ALA A 176     2802   2818   2690     19    -40     15       O  
ATOM   1309  CB  ALA A 176      40.791 -23.491   4.209  1.00 21.10           C  
ANISOU 1309  CB  ALA A 176     2739   2707   2571     24    -45     64       C  
ATOM   1310  N   HIS A 177      38.910 -25.026   2.225  1.00 23.38           N  
ANISOU 1310  N   HIS A 177     2985   2976   2922     27    -22     20       N  
ATOM   1311  CA  HIS A 177      37.544 -25.134   1.751  1.00 25.56           C  
ANISOU 1311  CA  HIS A 177     3251   3242   3218     24    -10      2       C  
ATOM   1312  C   HIS A 177      36.626 -25.434   2.846  1.00 27.63           C  
ANISOU 1312  C   HIS A 177     3525   3480   3490     23      8     15       C  
ATOM   1313  O   HIS A 177      36.978 -26.209   3.740  1.00 30.72           O  
ANISOU 1313  O   HIS A 177     3924   3857   3890     28     17     34       O  
ATOM   1314  CB  HIS A 177      37.450 -26.201   0.732  1.00 24.21           C  
ANISOU 1314  CB  HIS A 177     3055   3066   3076     28     -9    -20       C  
ATOM   1315  CG  HIS A 177      38.118 -25.804  -0.504  1.00 25.16           C  
ANISOU 1315  CG  HIS A 177     3163   3212   3183     29    -26    -36       C  
ATOM   1316  ND1 HIS A 177      37.417 -25.544  -1.643  1.00 25.53           N  
ANISOU 1316  ND1 HIS A 177     3195   3271   3233     27    -30    -61       N  
ATOM   1317  CD2 HIS A 177      39.464 -25.465  -0.753  1.00 23.99           C  
ANISOU 1317  CD2 HIS A 177     3016   3083   3014     31    -40    -29       C  
ATOM   1318  CE1 HIS A 177      38.301 -25.116  -2.611  1.00 24.81           C  
ANISOU 1318  CE1 HIS A 177     3096   3206   3122     29    -44    -69       C  
ATOM   1319  NE2 HIS A 177      39.548 -25.081  -2.066  1.00 25.51           N  
ANISOU 1319  NE2 HIS A 177     3195   3298   3199     32    -49    -49       N  
ATOM   1320  N   ILE A 178      35.422 -24.845   2.768  1.00 26.58           N  
ANISOU 1320  N   ILE A 178     3393   3344   3362     18     17      7       N  
ATOM   1321  CA  ILE A 178      34.390 -25.188   3.707  1.00 25.65           C  
ANISOU 1321  CA  ILE A 178     3282   3202   3259     17     39     17       C  
ATOM   1322  C   ILE A 178      33.075 -25.178   2.939  1.00 25.44           C  
ANISOU 1322  C   ILE A 178     3237   3167   3258     14     47     -5       C  
ATOM   1323  O   ILE A 178      32.652 -24.135   2.483  1.00 24.61           O  
ANISOU 1323  O   ILE A 178     3132   3076   3139      9     39    -13       O  
ATOM   1324  CB  ILE A 178      34.259 -24.211   4.866  1.00 25.04           C  
ANISOU 1324  CB  ILE A 178     3233   3127   3153     14     45     36       C  
ATOM   1325  CG1 ILE A 178      35.381 -24.398   5.895  1.00 23.87           C  
ANISOU 1325  CG1 ILE A 178     3104   2982   2982     19     41     61       C  
ATOM   1326  CG2 ILE A 178      32.848 -24.370   5.448  1.00 25.04           C  
ANISOU 1326  CG2 ILE A 178     3235   3104   3174     12     71     38       C  
ATOM   1327  CD1 ILE A 178      35.610 -23.182   6.787  1.00 23.16           C  
ANISOU 1327  CD1 ILE A 178     3040   2905   2854     15     37     73       C  
ATOM   1328  N   VAL A 179      32.395 -26.330   2.921  1.00 25.05           N  
ANISOU 1328  N   VAL A 179     3173   3094   3248     15     62    -12       N  
ATOM   1329  CA  VAL A 179      31.289 -26.582   2.022  1.00 23.41           C  
ANISOU 1329  CA  VAL A 179     2941   2879   3072     13     65    -38       C  
ATOM   1330  C   VAL A 179      30.072 -27.104   2.758  1.00 24.71           C  
ANISOU 1330  C   VAL A 179     3104   3013   3271     11     91    -33       C  
ATOM   1331  O   VAL A 179      30.099 -27.383   4.012  1.00 23.10           O  
ANISOU 1331  O   VAL A 179     2918   2792   3066     13    111     -6       O  
ATOM   1332  CB  VAL A 179      31.697 -27.642   0.992  1.00 23.72           C  
ANISOU 1332  CB  VAL A 179     2956   2918   3136     16     56    -62       C  
ATOM   1333  CG1 VAL A 179      32.837 -27.144   0.093  1.00 24.00           C  
ANISOU 1333  CG1 VAL A 179     2990   2985   3140     18     31    -70       C  
ATOM   1334  CG2 VAL A 179      32.047 -28.940   1.662  1.00 22.73           C  
ANISOU 1334  CG2 VAL A 179     2830   2767   3039     20     71    -49       C  
ATOM   1335  N   GLY A 180      29.005 -27.247   1.979  1.00 23.85           N  
ANISOU 1335  N   GLY A 180     2972   2897   3191      8     92    -58       N  
ATOM   1336  CA  GLY A 180      27.782 -27.862   2.492  1.00 26.17           C  
ANISOU 1336  CA  GLY A 180     3256   3159   3527      6    118    -57       C  
ATOM   1337  C   GLY A 180      26.757 -26.852   2.988  1.00 28.82           C  
ANISOU 1337  C   GLY A 180     3601   3492   3855      1    129    -49       C  
ATOM   1338  O   GLY A 180      25.761 -26.578   2.297  1.00 30.06           O  
ANISOU 1338  O   GLY A 180     3739   3648   4032     -1    126    -70       O  
ATOM   1339  N   ALA A 181      26.998 -26.299   4.180  1.00 28.46           N  
ANISOU 1339  N   ALA A 181     3584   3445   3782      2    142    -21       N  
ATOM   1340  CA  ALA A 181      26.160 -25.231   4.721  1.00 28.30           C  
ANISOU 1340  CA  ALA A 181     3576   3424   3750      0    154    -14       C  
ATOM   1341  C   ALA A 181      26.975 -24.265   5.564  1.00 29.54           C  
ANISOU 1341  C   ALA A 181     3766   3599   3858      0    151      7       C  
ATOM   1342  O   ALA A 181      28.030 -24.641   6.077  1.00 29.32           O  
ANISOU 1342  O   ALA A 181     3753   3576   3810      3    147     23       O  
ATOM   1343  CB  ALA A 181      25.004 -25.816   5.538  1.00 28.29           C  
ANISOU 1343  CB  ALA A 181     3571   3390   3786     -1    188     -4       C  
ATOM   1344  N   HIS A 182      26.485 -23.030   5.656  1.00 29.16           N  
ANISOU 1344  N   HIS A 182     3726   3560   3793     -3    151      6       N  
ATOM   1345  CA  HIS A 182      26.941 -22.031   6.545  1.00 30.98           C  
ANISOU 1345  CA  HIS A 182     3985   3800   3983     -4    153     22       C  
ATOM   1346  C   HIS A 182      26.339 -22.364   7.893  1.00 33.26           C  
ANISOU 1346  C   HIS A 182     4291   4067   4277     -2    186     41       C  
ATOM   1347  O   HIS A 182      25.306 -22.979   7.943  1.00 38.01           O  
ANISOU 1347  O   HIS A 182     4878   4646   4916     -2    207     39       O  
ATOM   1348  CB  HIS A 182      26.475 -20.678   5.982  1.00 33.16           C  
ANISOU 1348  CB  HIS A 182     4258   4090   4250     -8    142     10       C  
ATOM   1349  CG  HIS A 182      26.966 -19.459   6.750  1.00 35.99           C  
ANISOU 1349  CG  HIS A 182     4643   4461   4569    -10    141     21       C  
ATOM   1350  ND1 HIS A 182      28.217 -19.357   7.239  1.00 34.02           N  
ANISOU 1350  ND1 HIS A 182     4414   4226   4286     -8    129     32       N  
ATOM   1351  CD2 HIS A 182      26.321 -18.235   7.052  1.00 37.21           C  
ANISOU 1351  CD2 HIS A 182     4806   4615   4717    -13    150     19       C  
ATOM   1352  CE1 HIS A 182      28.360 -18.158   7.855  1.00 35.44           C  
ANISOU 1352  CE1 HIS A 182     4614   4414   4438    -11    130     36       C  
ATOM   1353  NE2 HIS A 182      27.196 -17.476   7.734  1.00 33.80           N  
ANISOU 1353  NE2 HIS A 182     4398   4195   4246    -14    143     28       N  
ATOM   1354  N   GLY A 183      26.973 -22.047   9.016  1.00 33.20           N  
ANISOU 1354  N   GLY A 183     4313   4067   4234      0    192     61       N  
ATOM   1355  CA  GLY A 183      26.389 -22.433  10.322  1.00 32.61           C  
ANISOU 1355  CA  GLY A 183     4255   3973   4160      2    225     81       C  
ATOM   1356  C   GLY A 183      27.038 -23.640  10.968  1.00 33.36           C  
ANISOU 1356  C   GLY A 183     4358   4060   4255      9    233    103       C  
ATOM   1357  O   GLY A 183      28.010 -24.151  10.474  1.00 31.44           O  
ANISOU 1357  O   GLY A 183     4108   3826   4009     12    211    102       O  
ATOM   1358  N   ASN A 184      26.483 -24.079  12.087  1.00 33.71           N  
ANISOU 1358  N   ASN A 184     4417   4088   4304     13    265    124       N  
ATOM   1359  CA  ASN A 184      27.010 -25.144  12.855  1.00 36.02           C  
ANISOU 1359  CA  ASN A 184     4719   4372   4594     21    276    150       C  
ATOM   1360  C   ASN A 184      27.336 -26.412  12.118  1.00 34.06           C  
ANISOU 1360  C   ASN A 184     4445   4110   4384     24    269    148       C  
ATOM   1361  O   ASN A 184      28.203 -27.148  12.529  1.00 29.82           O  
ANISOU 1361  O   ASN A 184     3915   3575   3838     31    265    168       O  
ATOM   1362  CB  ASN A 184      26.078 -25.455  14.026  1.00 43.55           C  
ANISOU 1362  CB  ASN A 184     5686   5305   5554     25    318    173       C  
ATOM   1363  CG  ASN A 184      26.386 -24.568  15.222  1.00 51.96           C  
ANISOU 1363  CG  ASN A 184     6789   6390   6564     28    324    187       C  
ATOM   1364  OD1 ASN A 184      25.488 -24.019  15.895  1.00 51.64           O  
ANISOU 1364  OD1 ASN A 184     6761   6343   6518     27    351    190       O  
ATOM   1365  ND2 ASN A 184      27.681 -24.369  15.461  1.00 52.35           N  
ANISOU 1365  ND2 ASN A 184     6855   6463   6571     31    297    194       N  
ATOM   1366  N   LYS A 185      26.681 -26.668  11.006  1.00 32.79           N  
ANISOU 1366  N   LYS A 185     4253   3938   4266     19    265    123       N  
ATOM   1367  CA  LYS A 185      26.981 -27.918  10.410  1.00 33.51           C  
ANISOU 1367  CA  LYS A 185     4321   4015   4394     22    261    120       C  
ATOM   1368  C   LYS A 185      27.975 -27.852   9.265  1.00 31.04           C  
ANISOU 1368  C   LYS A 185     3996   3723   4074     20    224     99       C  
ATOM   1369  O   LYS A 185      28.200 -28.859   8.589  1.00 28.82           O  
ANISOU 1369  O   LYS A 185     3692   3431   3826     22    219     89       O  
ATOM   1370  CB  LYS A 185      25.680 -28.682  10.106  1.00 38.49           C  
ANISOU 1370  CB  LYS A 185     4925   4613   5086     19    286    110       C  
ATOM   1371  CG  LYS A 185      25.086 -29.269  11.403  1.00 39.36           C  
ANISOU 1371  CG  LYS A 185     5047   4697   5209     24    326    142       C  
ATOM   1372  CD  LYS A 185      24.055 -30.342  11.092  1.00 41.72           C  
ANISOU 1372  CD  LYS A 185     5315   4959   5577     22    350    136       C  
ATOM   1373  CE  LYS A 185      23.070 -30.508  12.239  1.00 42.86           C  
ANISOU 1373  CE  LYS A 185     5469   5079   5735     25    394    162       C  
ATOM   1374  NZ  LYS A 185      23.817 -30.770  13.513  1.00 48.11           N  
ANISOU 1374  NZ  LYS A 185     6166   5750   6363     35    408    203       N  
ATOM   1375  N   MET A 186      28.597 -26.680   9.105  1.00 27.80           N  
ANISOU 1375  N   MET A 186     3600   3342   3619     18    201     93       N  
ATOM   1376  CA  MET A 186      29.605 -26.426   8.051  1.00 28.19           C  
ANISOU 1376  CA  MET A 186     3640   3415   3654     16    167     75       C  
ATOM   1377  C   MET A 186      30.636 -27.541   7.903  1.00 27.65           C  
ANISOU 1377  C   MET A 186     3565   3344   3596     23    158     82       C  
ATOM   1378  O   MET A 186      31.101 -28.032   8.897  1.00 25.61           O  
ANISOU 1378  O   MET A 186     3322   3079   3329     29    168    109       O  
ATOM   1379  CB  MET A 186      30.320 -25.104   8.330  1.00 27.36           C  
ANISOU 1379  CB  MET A 186     3558   3338   3497     14    149     79       C  
ATOM   1380  CG  MET A 186      31.339 -25.093   9.439  1.00 27.71           C  
ANISOU 1380  CG  MET A 186     3629   3391   3505     20    146    105       C  
ATOM   1381  SD  MET A 186      32.118 -23.458   9.615  1.00 35.41           S  
ANISOU 1381  SD  MET A 186     4627   4398   4427     15    122    102       S  
ATOM   1382  CE  MET A 186      30.682 -22.390   9.610  1.00 29.26           C  
ANISOU 1382  CE  MET A 186     3849   3613   3654      8    139     89       C  
ATOM   1383  N   VAL A 187      31.004 -27.949   6.687  1.00 26.97           N  
ANISOU 1383  N   VAL A 187     3455   3263   3529     22    140     59       N  
ATOM   1384  CA  VAL A 187      32.027 -29.013   6.642  1.00 28.86           C  
ANISOU 1384  CA  VAL A 187     3687   3497   3778     29    134     67       C  
ATOM   1385  C   VAL A 187      33.434 -28.459   6.434  1.00 28.71           C  
ANISOU 1385  C   VAL A 187     3678   3507   3720     31    106     70       C  
ATOM   1386  O   VAL A 187      33.724 -27.960   5.380  1.00 29.70           O  
ANISOU 1386  O   VAL A 187     3793   3652   3838     27     86     47       O  
ATOM   1387  CB  VAL A 187      31.799 -30.044   5.514  1.00 30.20           C  
ANISOU 1387  CB  VAL A 187     3824   3653   3996     29    132     40       C  
ATOM   1388  CG1 VAL A 187      32.791 -31.176   5.712  1.00 30.42           C  
ANISOU 1388  CG1 VAL A 187     3847   3670   4039     37    132     53       C  
ATOM   1389  CG2 VAL A 187      30.376 -30.587   5.551  1.00 30.76           C  
ANISOU 1389  CG2 VAL A 187     3879   3694   4112     26    157     31       C  
ATOM   1390  N   LEU A 188      34.307 -28.563   7.439  1.00 30.16           N  
ANISOU 1390  N   LEU A 188     3883   3695   3881     36    105     98       N  
ATOM   1391  CA  LEU A 188      35.715 -28.120   7.337  1.00 30.16           C  
ANISOU 1391  CA  LEU A 188     3890   3720   3847     38     79    103       C  
ATOM   1392  C   LEU A 188      36.565 -29.299   6.718  1.00 29.01           C  
ANISOU 1392  C   LEU A 188     3724   3567   3730     45     71     99       C  
ATOM   1393  O   LEU A 188      36.667 -30.387   7.337  1.00 28.36           O  
ANISOU 1393  O   LEU A 188     3639   3463   3670     52     85    119       O  
ATOM   1394  CB  LEU A 188      36.270 -27.710   8.750  1.00 32.89           C  
ANISOU 1394  CB  LEU A 188     4267   4074   4154     42     78    135       C  
ATOM   1395  CG  LEU A 188      35.368 -26.744   9.594  1.00 38.42           C  
ANISOU 1395  CG  LEU A 188     4989   4776   4830     37     92    141       C  
ATOM   1396  CD1 LEU A 188      34.387 -27.475  10.517  1.00 37.25           C  
ANISOU 1396  CD1 LEU A 188     4848   4602   4701     41    125    160       C  
ATOM   1397  CD2 LEU A 188      36.185 -25.717  10.386  1.00 35.42           C  
ANISOU 1397  CD2 LEU A 188     4636   4420   4400     37     76    153       C  
ATOM   1398  N   LEU A 189      37.136 -29.071   5.530  1.00 25.76           N  
ANISOU 1398  N   LEU A 189     3297   3173   3318     43     52     75       N  
ATOM   1399  CA  LEU A 189      37.799 -30.105   4.738  1.00 25.83           C  
ANISOU 1399  CA  LEU A 189     3282   3175   3355     48     46     63       C  
ATOM   1400  C   LEU A 189      39.302 -30.022   5.016  1.00 27.07           C  
ANISOU 1400  C   LEU A 189     3446   3347   3489     53     28     81       C  
ATOM   1401  O   LEU A 189      40.061 -29.414   4.260  1.00 26.90           O  
ANISOU 1401  O   LEU A 189     3421   3350   3450     51      9     68       O  
ATOM   1402  CB  LEU A 189      37.510 -29.879   3.244  1.00 24.25           C  
ANISOU 1402  CB  LEU A 189     3061   2987   3165     43     37     26       C  
ATOM   1403  CG  LEU A 189      36.080 -30.239   2.822  1.00 23.47           C  
ANISOU 1403  CG  LEU A 189     2946   2870   3098     39     52      4       C  
ATOM   1404  CD1 LEU A 189      35.789 -29.771   1.388  1.00 22.86           C  
ANISOU 1404  CD1 LEU A 189     2852   2813   3020     35     38    -30       C  
ATOM   1405  CD2 LEU A 189      35.839 -31.781   2.949  1.00 24.03           C  
ANISOU 1405  CD2 LEU A 189     3001   2908   3221     44     70      4       C  
ATOM   1406  N   LYS A 190      39.739 -30.577   6.134  1.00 29.13           N  
ANISOU 1406  N   LYS A 190     3719   3597   3749     60     34    112       N  
ATOM   1407  CA  LYS A 190      41.182 -30.670   6.445  1.00 32.92           C  
ANISOU 1407  CA  LYS A 190     4203   4089   4214     67     16    130       C  
ATOM   1408  C   LYS A 190      42.109 -31.084   5.267  1.00 32.51           C  
ANISOU 1408  C   LYS A 190     4127   4045   4180     69      3    110       C  
ATOM   1409  O   LYS A 190      43.196 -30.540   5.115  1.00 33.66           O  
ANISOU 1409  O   LYS A 190     4275   4211   4302     70    -16    113       O  
ATOM   1410  CB  LYS A 190      41.394 -31.637   7.598  1.00 36.16           C  
ANISOU 1410  CB  LYS A 190     4622   4481   4637     76     28    165       C  
ATOM   1411  CG  LYS A 190      42.867 -31.941   7.841  1.00 41.90           C  
ANISOU 1411  CG  LYS A 190     5346   5216   5356     85      9    183       C  
ATOM   1412  CD  LYS A 190      43.049 -32.656   9.178  1.00 42.99           C  
ANISOU 1412  CD  LYS A 190     5498   5340   5495     95     18    224       C  
ATOM   1413  CE  LYS A 190      44.524 -32.822   9.502  1.00 46.45           C  
ANISOU 1413  CE  LYS A 190     5934   5790   5921    103     -3    245       C  
ATOM   1414  NZ  LYS A 190      44.671 -32.843  10.989  1.00 46.00           N  
ANISOU 1414  NZ  LYS A 190     5903   5737   5838    111     -3    285       N  
ATOM   1415  N   ARG A 191      41.674 -32.014   4.433  1.00 30.37           N  
ANISOU 1415  N   ARG A 191     3833   3756   3950     71     15     88       N  
ATOM   1416  CA  ARG A 191      42.469 -32.414   3.276  1.00 31.78           C  
ANISOU 1416  CA  ARG A 191     3988   3941   4144     73      5     65       C  
ATOM   1417  C   ARG A 191      42.667 -31.347   2.223  1.00 31.86           C  
ANISOU 1417  C   ARG A 191     3995   3981   4127     67    -10     40       C  
ATOM   1418  O   ARG A 191      43.484 -31.495   1.340  1.00 34.68           O  
ANISOU 1418  O   ARG A 191     4338   4351   4489     70    -19     24       O  
ATOM   1419  CB  ARG A 191      41.813 -33.598   2.552  1.00 31.97           C  
ANISOU 1419  CB  ARG A 191     3988   3940   4218     75     21     40       C  
ATOM   1420  CG  ARG A 191      41.826 -34.941   3.266  1.00 31.54           C  
ANISOU 1420  CG  ARG A 191     3926   3851   4205     83     39     60       C  
ATOM   1421  CD  ARG A 191      41.661 -36.026   2.166  1.00 30.66           C  
ANISOU 1421  CD  ARG A 191     3783   3721   4143     85     47     25       C  
ATOM   1422  NE  ARG A 191      40.381 -35.843   1.469  1.00 31.21           N  
ANISOU 1422  NE  ARG A 191     3845   3789   4223     77     54     -6       N  
ATOM   1423  CZ  ARG A 191      40.182 -36.001   0.140  1.00 29.91           C  
ANISOU 1423  CZ  ARG A 191     3658   3631   4071     74     50    -50       C  
ATOM   1424  NH1 ARG A 191      41.166 -36.367  -0.653  1.00 28.43           N  
ANISOU 1424  NH1 ARG A 191     3457   3454   3891     79     41    -67       N  
ATOM   1425  NH2 ARG A 191      38.998 -35.803  -0.392  1.00 29.66           N  
ANISOU 1425  NH2 ARG A 191     3620   3600   4048     67     53    -76       N  
ATOM   1426  N   TYR A 192      41.903 -30.280   2.247  1.00 31.60           N  
ANISOU 1426  N   TYR A 192     3976   3962   4069     59    -12     35       N  
ATOM   1427  CA  TYR A 192      41.951 -29.355   1.131  1.00 30.56           C  
ANISOU 1427  CA  TYR A 192     3837   3856   3916     54    -24     12       C  
ATOM   1428  C   TYR A 192      42.447 -27.992   1.637  1.00 31.81           C  
ANISOU 1428  C   TYR A 192     4017   4037   4033     49    -39     29       C  
ATOM   1429  O   TYR A 192      41.904 -26.940   1.267  1.00 36.92           O  
ANISOU 1429  O   TYR A 192     4668   4698   4659     43    -42     19       O  
ATOM   1430  CB  TYR A 192      40.529 -29.151   0.614  1.00 30.27           C  
ANISOU 1430  CB  TYR A 192     3796   3816   3888     48    -15     -9       C  
ATOM   1431  CG  TYR A 192      40.022 -30.196  -0.290  1.00 28.99           C  
ANISOU 1431  CG  TYR A 192     3610   3640   3763     50     -7    -38       C  
ATOM   1432  CD1 TYR A 192      39.393 -31.363   0.233  1.00 28.58           C  
ANISOU 1432  CD1 TYR A 192     3551   3555   3751     53     11    -36       C  
ATOM   1433  CD2 TYR A 192      40.112 -30.023  -1.665  1.00 27.44           C  
ANISOU 1433  CD2 TYR A 192     3397   3465   3563     50    -16    -69       C  
ATOM   1434  CE1 TYR A 192      38.893 -32.320  -0.599  1.00 29.15           C  
ANISOU 1434  CE1 TYR A 192     3599   3613   3861     54     18    -66       C  
ATOM   1435  CE2 TYR A 192      39.600 -30.967  -2.520  1.00 28.13           C  
ANISOU 1435  CE2 TYR A 192     3461   3541   3682     52    -10   -100       C  
ATOM   1436  CZ  TYR A 192      39.005 -32.116  -1.995  1.00 29.29           C  
ANISOU 1436  CZ  TYR A 192     3601   3654   3872     53      6   -101       C  
ATOM   1437  OH  TYR A 192      38.562 -33.100  -2.833  1.00 30.21           O  
ANISOU 1437  OH  TYR A 192     3693   3758   4025     54     12   -134       O  
ATOM   1438  N   ILE A 193      43.369 -28.018   2.588  1.00 27.22           N  
ANISOU 1438  N   ILE A 193     3447   3454   3440     53    -46     55       N  
ATOM   1439  CA  ILE A 193      43.961 -26.837   3.070  1.00 24.46           C  
ANISOU 1439  CA  ILE A 193     3113   3123   3055     49    -61     68       C  
ATOM   1440  C   ILE A 193      45.364 -26.773   2.484  1.00 24.50           C  
ANISOU 1440  C   ILE A 193     3106   3144   3057     52    -77     67       C  
ATOM   1441  O   ILE A 193      46.005 -27.797   2.289  1.00 23.77           O  
ANISOU 1441  O   ILE A 193     2999   3043   2987     59    -76     68       O  
ATOM   1442  CB  ILE A 193      44.055 -26.848   4.628  1.00 23.53           C  
ANISOU 1442  CB  ILE A 193     3019   2998   2923     50    -60     98       C  
ATOM   1443  CG1 ILE A 193      42.664 -26.827   5.233  1.00 22.77           C  
ANISOU 1443  CG1 ILE A 193     2936   2887   2828     47    -41    100       C  
ATOM   1444  CG2 ILE A 193      44.685 -25.556   5.100  1.00 23.73           C  
ANISOU 1444  CG2 ILE A 193     3060   3043   2912     45    -78    107       C  
ATOM   1445  CD1 ILE A 193      42.666 -26.891   6.764  1.00 22.23           C  
ANISOU 1445  CD1 ILE A 193     2891   2811   2743     50    -37    130       C  
ATOM   1446  N   THR A 194      45.850 -25.558   2.223  1.00 23.76           N  
ANISOU 1446  N   THR A 194     3017   3073   2938     46    -91     66       N  
ATOM   1447  CA  THR A 194      47.137 -25.395   1.674  1.00 23.59           C  
ANISOU 1447  CA  THR A 194     2982   3065   2913     48   -104     66       C  
ATOM   1448  C   THR A 194      47.647 -24.111   2.141  1.00 23.02           C  
ANISOU 1448  C   THR A 194     2923   3008   2813     42   -119     77       C  
ATOM   1449  O   THR A 194      46.870 -23.192   2.488  1.00 21.45           O  
ANISOU 1449  O   THR A 194     2739   2812   2596     35   -117     76       O  
ATOM   1450  CB  THR A 194      47.134 -25.234   0.070  1.00 25.14           C  
ANISOU 1450  CB  THR A 194     3159   3277   3115     48   -102     40       C  
ATOM   1451  OG1 THR A 194      46.183 -24.266  -0.314  1.00 26.87           O  
ANISOU 1451  OG1 THR A 194     3385   3506   3318     41    -99     30       O  
ATOM   1452  CG2 THR A 194      46.769 -26.573  -0.704  1.00 24.44           C  
ANISOU 1452  CG2 THR A 194     3051   3176   3057     55    -89     20       C  
ATOM   1453  N   VAL A 195      48.976 -23.994   2.018  1.00 22.98           N  
ANISOU 1453  N   VAL A 195     2909   3014   2808     44   -133     84       N  
ATOM   1454  CA  VAL A 195      49.660 -22.805   2.426  1.00 24.88           C  
ANISOU 1454  CA  VAL A 195     3158   3268   3027     38   -149     93       C  
ATOM   1455  C   VAL A 195      50.598 -22.481   1.304  1.00 26.54           C  
ANISOU 1455  C   VAL A 195     3348   3493   3242     38   -155     85       C  
ATOM   1456  O   VAL A 195      51.450 -23.295   0.954  1.00 30.34           O  
ANISOU 1456  O   VAL A 195     3813   3973   3742     45   -156     86       O  
ATOM   1457  CB  VAL A 195      50.473 -23.041   3.743  1.00 23.01           C  
ANISOU 1457  CB  VAL A 195     2931   3026   2783     41   -164    115       C  
ATOM   1458  CG1 VAL A 195      51.157 -21.764   4.219  1.00 24.43           C  
ANISOU 1458  CG1 VAL A 195     3119   3220   2943     33   -182    121       C  
ATOM   1459  CG2 VAL A 195      49.602 -23.636   4.792  1.00 22.95           C  
ANISOU 1459  CG2 VAL A 195     2941   3003   2773     43   -154    126       C  
ATOM   1460  N   GLY A 196      50.475 -21.287   0.751  1.00 27.97           N  
ANISOU 1460  N   GLY A 196     3529   3688   3410     31   -157     79       N  
ATOM   1461  CA  GLY A 196      51.181 -20.993  -0.504  1.00 28.01           C  
ANISOU 1461  CA  GLY A 196     3514   3708   3420     32   -156     71       C  
ATOM   1462  C   GLY A 196      51.123 -22.152  -1.501  1.00 29.91           C  
ANISOU 1462  C   GLY A 196     3737   3948   3678     41   -144     56       C  
ATOM   1463  O   GLY A 196      52.083 -22.368  -2.255  1.00 30.42           O  
ANISOU 1463  O   GLY A 196     3784   4022   3752     46   -144     54       O  
ATOM   1464  N   GLY A 197      50.014 -22.905  -1.538  1.00 29.23           N  
ANISOU 1464  N   GLY A 197     3654   3850   3599     44   -132     45       N  
ATOM   1465  CA  GLY A 197      49.785 -23.870  -2.645  1.00 26.48           C  
ANISOU 1465  CA  GLY A 197     3289   3503   3267     51   -120     24       C  
ATOM   1466  C   GLY A 197      50.342 -25.211  -2.244  1.00 27.04           C  
ANISOU 1466  C   GLY A 197     3352   3557   3364     59   -117     28       C  
ATOM   1467  O   GLY A 197      50.224 -26.154  -2.974  1.00 28.28           O  
ANISOU 1467  O   GLY A 197     3495   3710   3540     65   -107     10       O  
ATOM   1468  N   ILE A 198      50.913 -25.289  -1.039  1.00 26.25           N  
ANISOU 1468  N   ILE A 198     3261   3446   3264     59   -127     50       N  
ATOM   1469  CA  ILE A 198      51.498 -26.489  -0.463  1.00 24.54           C  
ANISOU 1469  CA  ILE A 198     3038   3212   3072     67   -127     61       C  
ATOM   1470  C   ILE A 198      50.526 -27.112   0.525  1.00 25.07           C  
ANISOU 1470  C   ILE A 198     3120   3258   3145     68   -120     70       C  
ATOM   1471  O   ILE A 198      49.986 -26.362   1.325  1.00 25.39           O  
ANISOU 1471  O   ILE A 198     3181   3301   3165     62   -124     80       O  
ATOM   1472  CB  ILE A 198      52.778 -26.108   0.330  1.00 24.49           C  
ANISOU 1472  CB  ILE A 198     3034   3211   3061     68   -145     84       C  
ATOM   1473  CG1 ILE A 198      53.665 -25.162  -0.510  1.00 24.96           C  
ANISOU 1473  CG1 ILE A 198     3081   3291   3111     64   -153     79       C  
ATOM   1474  CG2 ILE A 198      53.599 -27.364   0.664  1.00 24.09           C  
ANISOU 1474  CG2 ILE A 198     2969   3144   3038     78   -146     95       C  
ATOM   1475  CD1 ILE A 198      54.839 -24.510   0.193  1.00 25.40           C  
ANISOU 1475  CD1 ILE A 198     3137   3353   3160     62   -173     99       C  
ATOM   1476  N   PRO A 199      50.324 -28.492   0.513  1.00 25.12           N  
ANISOU 1476  N   PRO A 199     3117   3244   3184     76   -107     66       N  
ATOM   1477  CA  PRO A 199      49.368 -29.095   1.391  1.00 23.43           C  
ANISOU 1477  CA  PRO A 199     2915   3009   2979     77    -97     76       C  
ATOM   1478  C   PRO A 199      49.686 -28.805   2.848  1.00 25.42           C  
ANISOU 1478  C   PRO A 199     3186   3258   3213     77   -108    108       C  
ATOM   1479  O   PRO A 199      50.829 -28.901   3.302  1.00 23.69           O  
ANISOU 1479  O   PRO A 199     2965   3043   2994     82   -122    125       O  
ATOM   1480  CB  PRO A 199      49.503 -30.621   1.121  1.00 24.25           C  
ANISOU 1480  CB  PRO A 199     2999   3090   3124     87    -84     70       C  
ATOM   1481  CG  PRO A 199      49.975 -30.755  -0.264  1.00 24.68           C  
ANISOU 1481  CG  PRO A 199     3031   3155   3189     89    -82     42       C  
ATOM   1482  CD  PRO A 199      50.800 -29.444  -0.529  1.00 25.22           C  
ANISOU 1482  CD  PRO A 199     3104   3253   3225     83    -99     47       C  
ATOM   1483  N   LEU A 200      48.668 -28.425   3.607  1.00 26.48           N  
ANISOU 1483  N   LEU A 200     3341   3388   3331     72   -102    114       N  
ATOM   1484  CA  LEU A 200      48.897 -28.244   5.038  1.00 29.17           C  
ANISOU 1484  CA  LEU A 200     3703   3727   3653     74   -111    144       C  
ATOM   1485  C   LEU A 200      49.711 -29.413   5.637  1.00 29.81           C  
ANISOU 1485  C   LEU A 200     3776   3794   3756     86   -113    167       C  
ATOM   1486  O   LEU A 200      50.555 -29.182   6.450  1.00 34.12           O  
ANISOU 1486  O   LEU A 200     4329   4348   4285     89   -131    189       O  
ATOM   1487  CB  LEU A 200      47.549 -28.122   5.734  1.00 27.67           C  
ANISOU 1487  CB  LEU A 200     3533   3527   3453     70    -96    148       C  
ATOM   1488  CG  LEU A 200      47.740 -27.734   7.172  1.00 29.63           C  
ANISOU 1488  CG  LEU A 200     3806   3780   3673     71   -105    175       C  
ATOM   1489  CD1 LEU A 200      48.243 -26.297   7.088  1.00 29.75           C  
ANISOU 1489  CD1 LEU A 200     3828   3819   3656     62   -124    167       C  
ATOM   1490  CD2 LEU A 200      46.424 -27.849   7.955  1.00 28.18           C  
ANISOU 1490  CD2 LEU A 200     3640   3582   3483     70    -85    182       C  
ATOM   1491  N   GLN A 201      49.420 -30.678   5.279  1.00 31.69           N  
ANISOU 1491  N   GLN A 201     3998   4009   4031     93    -96    163       N  
ATOM   1492  CA  GLN A 201      50.094 -31.851   5.881  1.00 31.59           C  
ANISOU 1492  CA  GLN A 201     3977   3979   4044    105    -96    188       C  
ATOM   1493  C   GLN A 201      51.633 -31.769   5.953  1.00 33.92           C  
ANISOU 1493  C   GLN A 201     4262   4287   4338    111   -118    201       C  
ATOM   1494  O   GLN A 201      52.254 -32.253   6.935  1.00 30.74           O  
ANISOU 1494  O   GLN A 201     3863   3879   3937    120   -127    232       O  
ATOM   1495  CB  GLN A 201      49.651 -33.158   5.215  1.00 32.32           C  
ANISOU 1495  CB  GLN A 201     4048   4045   4185    111    -74    174       C  
ATOM   1496  CG  GLN A 201      50.113 -34.452   5.917  1.00 31.97           C  
ANISOU 1496  CG  GLN A 201     3995   3976   4174    125    -68    203       C  
ATOM   1497  CD  GLN A 201      49.463 -34.645   7.258  1.00 33.58           C  
ANISOU 1497  CD  GLN A 201     4221   4169   4367    128    -60    236       C  
ATOM   1498  OE1 GLN A 201      48.252 -34.580   7.358  1.00 37.07           O  
ANISOU 1498  OE1 GLN A 201     4673   4602   4807    122    -43    229       O  
ATOM   1499  NE2 GLN A 201      50.248 -34.914   8.294  1.00 32.54           N  
ANISOU 1499  NE2 GLN A 201     4097   4038   4227    138    -72    273       N  
ATOM   1500  N   GLU A 202      52.262 -31.147   4.943  1.00 33.51           N  
ANISOU 1500  N   GLU A 202     4196   4252   4282    106   -127    179       N  
ATOM   1501  CA  GLU A 202      53.711 -30.956   5.008  1.00 31.18           C  
ANISOU 1501  CA  GLU A 202     3891   3969   3986    110   -148    191       C  
ATOM   1502  C   GLU A 202      54.159 -30.115   6.220  1.00 31.46           C  
ANISOU 1502  C   GLU A 202     3947   4020   3986    107   -171    215       C  
ATOM   1503  O   GLU A 202      55.223 -30.362   6.800  1.00 31.01           O  
ANISOU 1503  O   GLU A 202     3884   3965   3932    115   -189    237       O  
ATOM   1504  CB  GLU A 202      54.214 -30.346   3.735  1.00 32.01           C  
ANISOU 1504  CB  GLU A 202     3979   4090   4091    104   -151    164       C  
ATOM   1505  CG  GLU A 202      53.850 -31.108   2.480  1.00 32.18           C  
ANISOU 1505  CG  GLU A 202     3980   4101   4142    107   -130    136       C  
ATOM   1506  CD  GLU A 202      54.860 -30.911   1.336  1.00 36.10           C  
ANISOU 1506  CD  GLU A 202     4455   4612   4648    108   -133    119       C  
ATOM   1507  OE1 GLU A 202      55.930 -30.300   1.613  1.00 39.37           O  
ANISOU 1507  OE1 GLU A 202     4866   5040   5051    108   -152    133       O  
ATOM   1508  OE2 GLU A 202      54.609 -31.342   0.157  1.00 35.26           O  
ANISOU 1508  OE2 GLU A 202     4332   4505   4559    110   -118     91       O  
ATOM   1509  N   PHE A 203      53.352 -29.122   6.608  1.00 30.48           N  
ANISOU 1509  N   PHE A 203     3846   3907   3828     97   -172    211       N  
ATOM   1510  CA  PHE A 203      53.657 -28.306   7.800  1.00 29.97           C  
ANISOU 1510  CA  PHE A 203     3803   3857   3727     95   -193    230       C  
ATOM   1511  C   PHE A 203      53.387 -29.002   9.099  1.00 30.40           C  
ANISOU 1511  C   PHE A 203     3873   3900   3774    103   -192    259       C  
ATOM   1512  O   PHE A 203      53.996 -28.685  10.125  1.00 31.57           O  
ANISOU 1512  O   PHE A 203     4034   4061   3898    106   -213    280       O  
ATOM   1513  CB  PHE A 203      52.913 -26.970   7.795  1.00 26.97           C  
ANISOU 1513  CB  PHE A 203     3442   3491   3315     81   -193    213       C  
ATOM   1514  CG  PHE A 203      53.263 -26.103   6.621  1.00 26.35           C  
ANISOU 1514  CG  PHE A 203     3349   3425   3237     73   -197    189       C  
ATOM   1515  CD1 PHE A 203      52.674 -26.338   5.368  1.00 25.44           C  
ANISOU 1515  CD1 PHE A 203     3219   3304   3140     71   -178    167       C  
ATOM   1516  CD2 PHE A 203      54.135 -24.987   6.775  1.00 25.17           C  
ANISOU 1516  CD2 PHE A 203     3200   3294   3069     66   -220    189       C  
ATOM   1517  CE1 PHE A 203      52.985 -25.525   4.278  1.00 24.36           C  
ANISOU 1517  CE1 PHE A 203     3071   3182   3002     64   -180    147       C  
ATOM   1518  CE2 PHE A 203      54.466 -24.196   5.678  1.00 24.28           C  
ANISOU 1518  CE2 PHE A 203     3073   3191   2960     58   -221    171       C  
ATOM   1519  CZ  PHE A 203      53.873 -24.458   4.431  1.00 23.66           C  
ANISOU 1519  CZ  PHE A 203     2982   3110   2898     58   -200    151       C  
ATOM   1520  N   ILE A 204      52.411 -29.894   9.061  1.00 31.87           N  
ANISOU 1520  N   ILE A 204     4061   4066   3981    108   -166    261       N  
ATOM   1521  CA  ILE A 204      52.116 -30.743  10.207  1.00 31.63           C  
ANISOU 1521  CA  ILE A 204     4044   4023   3951    118   -159    293       C  
ATOM   1522  C   ILE A 204      53.269 -31.714  10.305  1.00 33.96           C  
ANISOU 1522  C   ILE A 204     4319   4310   4274    131   -169    314       C  
ATOM   1523  O   ILE A 204      53.745 -32.006  11.418  1.00 32.95           O  
ANISOU 1523  O   ILE A 204     4201   4185   4133    141   -182    347       O  
ATOM   1524  CB  ILE A 204      50.795 -31.527  10.064  1.00 30.61           C  
ANISOU 1524  CB  ILE A 204     3916   3868   3845    120   -126    289       C  
ATOM   1525  CG1 ILE A 204      49.650 -30.505  10.120  1.00 29.98           C  
ANISOU 1525  CG1 ILE A 204     3857   3797   3736    107   -118    272       C  
ATOM   1526  CG2 ILE A 204      50.662 -32.568  11.225  1.00 30.68           C  
ANISOU 1526  CG2 ILE A 204     3933   3860   3861    133   -117    328       C  
ATOM   1527  CD1 ILE A 204      48.266 -31.128   9.990  1.00 28.61           C  
ANISOU 1527  CD1 ILE A 204     3684   3600   3585    107    -86    266       C  
ATOM   1528  N   ASN A 205      53.747 -32.225   9.169  1.00 32.62           N  
ANISOU 1528  N   ASN A 205     4121   4131   4142    133   -164    296       N  
ATOM   1529  CA  ASN A 205      54.969 -33.089   9.282  1.00 36.32           C  
ANISOU 1529  CA  ASN A 205     4569   4592   4639    146   -176    317       C  
ATOM   1530  C   ASN A 205      56.218 -32.412   9.907  1.00 37.43           C  
ANISOU 1530  C   ASN A 205     4710   4755   4753    147   -210    334       C  
ATOM   1531  O   ASN A 205      57.005 -33.100  10.568  1.00 35.56           O  
ANISOU 1531  O   ASN A 205     4467   4514   4529    160   -223    364       O  
ATOM   1532  CB  ASN A 205      55.342 -33.775   7.964  1.00 36.58           C  
ANISOU 1532  CB  ASN A 205     4570   4611   4718    149   -164    294       C  
ATOM   1533  CG  ASN A 205      54.233 -34.674   7.445  1.00 37.34           C  
ANISOU 1533  CG  ASN A 205     4660   4681   4846    150   -132    279       C  
ATOM   1534  OD1 ASN A 205      53.340 -35.118   8.195  1.00 33.83           O  
ANISOU 1534  OD1 ASN A 205     4229   4221   4401    153   -118    296       O  
ATOM   1535  ND2 ASN A 205      54.246 -34.900   6.148  1.00 35.65           N  
ANISOU 1535  ND2 ASN A 205     4424   4461   4658    147   -121    246       N  
ATOM   1536  N   ASN A 206      56.408 -31.093   9.673  1.00 36.35           N  
ANISOU 1536  N   ASN A 206     4582   4642   4586    135   -226    314       N  
ATOM   1537  CA  ASN A 206      57.574 -30.387  10.162  1.00 35.31           C  
ANISOU 1537  CA  ASN A 206     4449   4532   4435    134   -259    324       C  
ATOM   1538  C   ASN A 206      57.279 -29.916  11.539  1.00 36.59           C  
ANISOU 1538  C   ASN A 206     4641   4707   4554    134   -273    344       C  
ATOM   1539  O   ASN A 206      58.106 -29.235  12.153  1.00 37.58           O  
ANISOU 1539  O   ASN A 206     4770   4852   4655    132   -303    352       O  
ATOM   1540  CB  ASN A 206      57.964 -29.176   9.319  1.00 35.18           C  
ANISOU 1540  CB  ASN A 206     4425   4532   4408    120   -269    296       C  
ATOM   1541  CG  ASN A 206      58.320 -29.546   7.895  1.00 38.36           C  
ANISOU 1541  CG  ASN A 206     4799   4927   4848    121   -255    274       C  
ATOM   1542  OD1 ASN A 206      58.793 -30.623   7.626  1.00 41.61           O  
ANISOU 1542  OD1 ASN A 206     5190   5323   5295    132   -248    283       O  
ATOM   1543  ND2 ASN A 206      58.091 -28.653   6.986  1.00 37.63           N  
ANISOU 1543  ND2 ASN A 206     4703   4844   4747    109   -249    248       N  
ATOM   1544  N   LYS A 207      56.099 -30.262  12.035  1.00 36.54           N  
ANISOU 1544  N   LYS A 207     4655   4690   4538    135   -252    352       N  
ATOM   1545  CA  LYS A 207      55.734 -29.940  13.392  1.00 36.78           C  
ANISOU 1545  CA  LYS A 207     4715   4732   4525    137   -261    373       C  
ATOM   1546  C   LYS A 207      55.633 -28.430  13.543  1.00 35.60           C  
ANISOU 1546  C   LYS A 207     4584   4607   4336    123   -276    351       C  
ATOM   1547  O   LYS A 207      55.934 -27.869  14.593  1.00 34.21           O  
ANISOU 1547  O   LYS A 207     4426   4449   4122    123   -298    362       O  
ATOM   1548  CB  LYS A 207      56.759 -30.490  14.362  1.00 43.10           C  
ANISOU 1548  CB  LYS A 207     5514   5540   5322    152   -285    408       C  
ATOM   1549  CG  LYS A 207      56.868 -32.007  14.403  1.00 47.32           C  
ANISOU 1549  CG  LYS A 207     6032   6050   5897    168   -270    437       C  
ATOM   1550  CD  LYS A 207      58.028 -32.285  15.376  1.00 50.89           C  
ANISOU 1550  CD  LYS A 207     6482   6515   6338    181   -303    471       C  
ATOM   1551  CE  LYS A 207      57.688 -33.307  16.453  1.00 52.76           C  
ANISOU 1551  CE  LYS A 207     6732   6742   6571    198   -293    515       C  
ATOM   1552  NZ  LYS A 207      58.358 -34.625  16.236  1.00 54.06           N  
ANISOU 1552  NZ  LYS A 207     6868   6883   6787    214   -289    540       N  
ATOM   1553  N   LEU A 208      55.146 -27.776  12.504  1.00 33.54           N  
ANISOU 1553  N   LEU A 208     4317   4344   4082    110   -263    319       N  
ATOM   1554  CA  LEU A 208      54.982 -26.312  12.565  1.00 33.59           C  
ANISOU 1554  CA  LEU A 208     4337   4369   4056     95   -274    297       C  
ATOM   1555  C   LEU A 208      53.574 -26.012  13.073  1.00 33.05           C  
ANISOU 1555  C   LEU A 208     4296   4297   3962     91   -253    294       C  
ATOM   1556  O   LEU A 208      53.258 -24.901  13.423  1.00 32.50           O  
ANISOU 1556  O   LEU A 208     4244   4240   3862     81   -259    280       O  
ATOM   1557  CB  LEU A 208      55.198 -25.711  11.172  1.00 32.50           C  
ANISOU 1557  CB  LEU A 208     4177   4231   3938     85   -271    268       C  
ATOM   1558  CG  LEU A 208      56.592 -25.945  10.605  1.00 32.12           C  
ANISOU 1558  CG  LEU A 208     4100   4185   3915     89   -289    271       C  
ATOM   1559  CD1 LEU A 208      56.803 -25.243   9.277  1.00 30.72           C  
ANISOU 1559  CD1 LEU A 208     3905   4013   3754     79   -284    244       C  
ATOM   1560  CD2 LEU A 208      57.518 -25.388  11.659  1.00 32.28           C  
ANISOU 1560  CD2 LEU A 208     4129   4224   3911     89   -323    284       C  
ATOM   1561  N   ILE A 209      52.735 -27.037  13.092  1.00 32.79           N  
ANISOU 1561  N   ILE A 209     4266   4245   3948     99   -227    305       N  
ATOM   1562  CA  ILE A 209      51.376 -26.921  13.575  1.00 32.88           C  
ANISOU 1562  CA  ILE A 209     4301   4250   3942     96   -203    304       C  
ATOM   1563  C   ILE A 209      50.971 -28.368  13.754  1.00 34.30           C  
ANISOU 1563  C   ILE A 209     4475   4406   4150    109   -181    328       C  
ATOM   1564  O   ILE A 209      51.435 -29.220  13.008  1.00 38.57           O  
ANISOU 1564  O   ILE A 209     4991   4934   4729    115   -178    329       O  
ATOM   1565  CB  ILE A 209      50.442 -26.156  12.598  1.00 34.17           C  
ANISOU 1565  CB  ILE A 209     4462   4409   4111     83   -186    272       C  
ATOM   1566  CG1 ILE A 209      49.013 -26.216  13.146  1.00 35.15           C  
ANISOU 1566  CG1 ILE A 209     4608   4523   4224     82   -159    274       C  
ATOM   1567  CG2 ILE A 209      50.518 -26.746  11.180  1.00 30.36           C  
ANISOU 1567  CG2 ILE A 209     3950   3914   3672     83   -175    256       C  
ATOM   1568  CD1 ILE A 209      48.184 -24.974  12.967  1.00 34.74           C  
ANISOU 1568  CD1 ILE A 209     4568   4478   4152     69   -152    250       C  
ATOM   1569  N   SER A 210      50.152 -28.666  14.757  1.00 31.93           N  
ANISOU 1569  N   SER A 210     4198   4101   3832    114   -165    348       N  
ATOM   1570  CA  SER A 210      49.835 -30.034  15.113  1.00 30.66           C  
ANISOU 1570  CA  SER A 210     4033   3919   3697    128   -144    377       C  
ATOM   1571  C   SER A 210      48.350 -30.332  14.801  1.00 30.40           C  
ANISOU 1571  C   SER A 210     4003   3863   3683    124   -107    366       C  
ATOM   1572  O   SER A 210      47.535 -29.413  14.715  1.00 30.40           O  
ANISOU 1572  O   SER A 210     4016   3869   3663    113    -99    345       O  
ATOM   1573  CB  SER A 210      50.081 -30.153  16.632  1.00 31.46           C  
ANISOU 1573  CB  SER A 210     4160   4034   3760    139   -154    413       C  
ATOM   1574  OG  SER A 210      48.960 -29.599  17.307  1.00 31.04           O  
ANISOU 1574  OG  SER A 210     4134   3984   3674    134   -136    411       O  
ATOM   1575  N   ASP A 211      47.978 -31.604  14.653  1.00 32.04           N  
ANISOU 1575  N   ASP A 211     4198   4044   3933    133    -84    381       N  
ATOM   1576  CA  ASP A 211      46.564 -32.010  14.549  1.00 34.30           C  
ANISOU 1576  CA  ASP A 211     4485   4306   4239    130    -48    377       C  
ATOM   1577  C   ASP A 211      45.606 -31.419  15.528  1.00 33.17           C  
ANISOU 1577  C   ASP A 211     4374   4171   4059    128    -34    385       C  
ATOM   1578  O   ASP A 211      44.470 -31.073  15.114  1.00 33.08           O  
ANISOU 1578  O   ASP A 211     4363   4149   4056    118    -13    363       O  
ATOM   1579  CB  ASP A 211      46.413 -33.524  14.654  1.00 41.00           C  
ANISOU 1579  CB  ASP A 211     5319   5124   5134    143    -27    402       C  
ATOM   1580  CG  ASP A 211      47.068 -34.260  13.481  1.00 48.68           C  
ANISOU 1580  CG  ASP A 211     6257   6081   6156    145    -31    386       C  
ATOM   1581  OD1 ASP A 211      47.397 -33.598  12.454  1.00 50.44           O  
ANISOU 1581  OD1 ASP A 211     6468   6317   6378    135    -45    351       O  
ATOM   1582  OD2 ASP A 211      47.241 -35.505  13.587  1.00 54.05           O  
ANISOU 1582  OD2 ASP A 211     6922   6737   6876    157    -19    408       O  
ATOM   1583  N   ALA A 212      46.032 -31.314  16.812  1.00 31.33           N  
ANISOU 1583  N   ALA A 212     4163   3954   3785    137    -45    417       N  
ATOM   1584  CA  ALA A 212      45.174 -30.840  17.864  1.00 31.54           C  
ANISOU 1584  CA  ALA A 212     4221   3988   3773    136    -29    428       C  
ATOM   1585  C   ALA A 212      45.023 -29.314  17.833  1.00 31.46           C  
ANISOU 1585  C   ALA A 212     4227   4002   3722    122    -44    397       C  
ATOM   1586  O   ALA A 212      43.964 -28.787  18.168  1.00 31.88           O  
ANISOU 1586  O   ALA A 212     4298   4055   3759    117    -23    389       O  
ATOM   1587  CB  ALA A 212      45.704 -31.283  19.227  1.00 31.42           C  
ANISOU 1587  CB  ALA A 212     4226   3986   3726    152    -37    473       C  
ATOM   1588  N   GLU A 213      46.083 -28.606  17.463  1.00 33.10           N  
ANISOU 1588  N   GLU A 213     4429   4231   3916    117    -78    381       N  
ATOM   1589  CA  GLU A 213      46.004 -27.150  17.305  1.00 32.91           C  
ANISOU 1589  CA  GLU A 213     4415   4226   3861    103    -91    350       C  
ATOM   1590  C   GLU A 213      45.096 -26.930  16.053  1.00 33.14           C  
ANISOU 1590  C   GLU A 213     4427   4237   3925     92    -71    318       C  
ATOM   1591  O   GLU A 213      44.321 -26.008  16.028  1.00 30.93           O  
ANISOU 1591  O   GLU A 213     4159   3962   3630     82    -63    299       O  
ATOM   1592  CB  GLU A 213      47.393 -26.536  17.073  1.00 35.15           C  
ANISOU 1592  CB  GLU A 213     4691   4532   4132    100   -131    340       C  
ATOM   1593  CG  GLU A 213      48.289 -26.275  18.278  1.00 39.86           C  
ANISOU 1593  CG  GLU A 213     5306   5153   4685    107   -158    360       C  
ATOM   1594  CD  GLU A 213      49.800 -26.312  17.950  1.00 45.92           C  
ANISOU 1594  CD  GLU A 213     6053   5932   5461    109   -195    361       C  
ATOM   1595  OE1 GLU A 213      50.210 -26.708  16.809  1.00 45.36           O  
ANISOU 1595  OE1 GLU A 213     5953   5849   5432    107   -195    352       O  
ATOM   1596  OE2 GLU A 213      50.603 -25.966  18.862  1.00 48.96           O  
ANISOU 1596  OE2 GLU A 213     6451   6341   5810    113   -223    373       O  
ATOM   1597  N   LEU A 214      45.178 -27.786  15.027  1.00 31.80           N  
ANISOU 1597  N   LEU A 214     4230   4049   3802     94    -65    313       N  
ATOM   1598  CA  LEU A 214      44.303 -27.558  13.900  1.00 33.37           C  
ANISOU 1598  CA  LEU A 214     4413   4235   4028     84    -49    283       C  
ATOM   1599  C   LEU A 214      42.848 -27.807  14.307  1.00 35.15           C  
ANISOU 1599  C   LEU A 214     4650   4443   4260     84    -15    287       C  
ATOM   1600  O   LEU A 214      41.978 -27.018  13.990  1.00 34.26           O  
ANISOU 1600  O   LEU A 214     4542   4330   4143     74     -5    265       O  
ATOM   1601  CB  LEU A 214      44.693 -28.397  12.700  1.00 32.34           C  
ANISOU 1601  CB  LEU A 214     4251   4091   3943     86    -49    272       C  
ATOM   1602  CG  LEU A 214      43.728 -28.224  11.540  1.00 33.46           C  
ANISOU 1602  CG  LEU A 214     4378   4221   4111     77    -34    241       C  
ATOM   1603  CD1 LEU A 214      43.888 -26.820  10.929  1.00 34.77           C  
ANISOU 1603  CD1 LEU A 214     4546   4410   4255     65    -51    215       C  
ATOM   1604  CD2 LEU A 214      44.028 -29.287  10.503  1.00 33.19           C  
ANISOU 1604  CD2 LEU A 214     4314   4172   4123     81    -30    232       C  
ATOM   1605  N   GLU A 215      42.614 -28.880  15.059  1.00 36.41           N  
ANISOU 1605  N   GLU A 215     4814   4587   4431     95      3    318       N  
ATOM   1606  CA  GLU A 215      41.290 -29.164  15.556  1.00 37.78           C  
ANISOU 1606  CA  GLU A 215     4998   4741   4612     96     37    326       C  
ATOM   1607  C   GLU A 215      40.757 -28.024  16.396  1.00 35.14           C  
ANISOU 1607  C   GLU A 215     4694   4425   4232     90     40    323       C  
ATOM   1608  O   GLU A 215      39.625 -27.625  16.235  1.00 34.08           O  
ANISOU 1608  O   GLU A 215     4562   4281   4104     83     62    308       O  
ATOM   1609  CB  GLU A 215      41.218 -30.489  16.338  1.00 40.60           C  
ANISOU 1609  CB  GLU A 215     5357   5081   4988    110     57    365       C  
ATOM   1610  CG  GLU A 215      41.262 -31.731  15.472  1.00 44.99           C  
ANISOU 1610  CG  GLU A 215     5880   5607   5603    114     66    364       C  
ATOM   1611  CD  GLU A 215      40.145 -31.752  14.428  1.00 50.11           C  
ANISOU 1611  CD  GLU A 215     6511   6237   6292    104     86    332       C  
ATOM   1612  OE1 GLU A 215      38.992 -31.350  14.778  1.00 55.31           O  
ANISOU 1612  OE1 GLU A 215     7181   6889   6943     99    108    328       O  
ATOM   1613  OE2 GLU A 215      40.419 -32.153  13.258  1.00 48.76           O  
ANISOU 1613  OE2 GLU A 215     6312   6057   6157    101     79    308       O  
ATOM   1614  N   ALA A 216      41.575 -27.488  17.277  1.00 34.45           N  
ANISOU 1614  N   ALA A 216     4627   4363   4098     94     19    336       N  
ATOM   1615  CA  ALA A 216      41.152 -26.325  18.027  1.00 33.48           C  
ANISOU 1615  CA  ALA A 216     4532   4258   3930     88     20    327       C  
ATOM   1616  C   ALA A 216      40.854 -25.114  17.125  1.00 32.19           C  
ANISOU 1616  C   ALA A 216     4362   4099   3768     73     12    287       C  
ATOM   1617  O   ALA A 216      39.907 -24.352  17.391  1.00 32.06           O  
ANISOU 1617  O   ALA A 216     4359   4082   3738     66     29    275       O  
ATOM   1618  CB  ALA A 216      42.119 -25.999  19.153  1.00 31.58           C  
ANISOU 1618  CB  ALA A 216     4315   4044   3639     95     -4    345       C  
ATOM   1619  N   ILE A 217      41.583 -24.950  16.022  1.00 32.48           N  
ANISOU 1619  N   ILE A 217     4376   4140   3825     67     -9    269       N  
ATOM   1620  CA  ILE A 217      41.280 -23.843  15.086  1.00 30.09           C  
ANISOU 1620  CA  ILE A 217     4064   3841   3527     54    -15    235       C  
ATOM   1621  C   ILE A 217      39.926 -24.036  14.351  1.00 30.94           C  
ANISOU 1621  C   ILE A 217     4159   3927   3669     49     12    221       C  
ATOM   1622  O   ILE A 217      39.199 -23.046  14.036  1.00 30.28           O  
ANISOU 1622  O   ILE A 217     4077   3844   3581     40     18    199       O  
ATOM   1623  CB  ILE A 217      42.408 -23.644  14.072  1.00 29.02           C  
ANISOU 1623  CB  ILE A 217     3907   3716   3403     50    -44    222       C  
ATOM   1624  CG1 ILE A 217      43.421 -22.649  14.652  1.00 28.00           C  
ANISOU 1624  CG1 ILE A 217     3792   3612   3235     47    -73    219       C  
ATOM   1625  CG2 ILE A 217      41.850 -23.173  12.729  1.00 25.38           C  
ANISOU 1625  CG2 ILE A 217     3426   3249   2968     41    -39    193       C  
ATOM   1626  CD1 ILE A 217      44.868 -22.816  14.252  1.00 27.64           C  
ANISOU 1626  CD1 ILE A 217     3730   3577   3194     49   -103    222       C  
ATOM   1627  N   PHE A 218      39.645 -25.306  14.075  1.00 31.24           N  
ANISOU 1627  N   PHE A 218     4181   3944   3743     56     28    232       N  
ATOM   1628  CA  PHE A 218      38.412 -25.826  13.456  1.00 32.17           C  
ANISOU 1628  CA  PHE A 218     4283   4038   3901     54     56    222       C  
ATOM   1629  C   PHE A 218      37.207 -25.474  14.370  1.00 31.37           C  
ANISOU 1629  C   PHE A 218     4203   3928   3786     53     84    229       C  
ATOM   1630  O   PHE A 218      36.152 -24.979  13.899  1.00 29.70           O  
ANISOU 1630  O   PHE A 218     3986   3708   3589     46     98    209       O  
ATOM   1631  CB  PHE A 218      38.561 -27.358  13.312  1.00 33.86           C  
ANISOU 1631  CB  PHE A 218     4480   4230   4153     64     66    239       C  
ATOM   1632  CG  PHE A 218      39.182 -27.813  12.008  1.00 37.51           C  
ANISOU 1632  CG  PHE A 218     4913   4690   4646     63     50    221       C  
ATOM   1633  CD1 PHE A 218      39.887 -26.952  11.198  1.00 38.07           C  
ANISOU 1633  CD1 PHE A 218     4977   4783   4705     56     24    199       C  
ATOM   1634  CD2 PHE A 218      39.080 -29.138  11.605  1.00 39.41           C  
ANISOU 1634  CD2 PHE A 218     5133   4908   4933     69     63    226       C  
ATOM   1635  CE1 PHE A 218      40.424 -27.383   9.988  1.00 40.07           C  
ANISOU 1635  CE1 PHE A 218     5204   5034   4984     56     13    182       C  
ATOM   1636  CE2 PHE A 218      39.624 -29.583  10.402  1.00 40.73           C  
ANISOU 1636  CE2 PHE A 218     5273   5074   5129     68     50    206       C  
ATOM   1637  CZ  PHE A 218      40.321 -28.705   9.596  1.00 40.11           C  
ANISOU 1637  CZ  PHE A 218     5189   5018   5032     62     25    185       C  
ATOM   1638  N   ASP A 219      37.364 -25.685  15.679  1.00 30.03           N  
ANISOU 1638  N   ASP A 219     4058   3763   3587     61     92    256       N  
ATOM   1639  CA  ASP A 219      36.329 -25.279  16.603  1.00 29.81           C  
ANISOU 1639  CA  ASP A 219     4051   3731   3541     61    119    263       C  
ATOM   1640  C   ASP A 219      36.171 -23.788  16.686  1.00 28.82           C  
ANISOU 1640  C   ASP A 219     3942   3624   3384     51    109    240       C  
ATOM   1641  O   ASP A 219      35.079 -23.294  16.798  1.00 28.28           O  
ANISOU 1641  O   ASP A 219     3877   3546   3319     46    132    229       O  
ATOM   1642  CB  ASP A 219      36.639 -25.795  17.986  1.00 35.93           C  
ANISOU 1642  CB  ASP A 219     4852   4514   4286     73    127    298       C  
ATOM   1643  CG  ASP A 219      36.377 -27.271  18.099  1.00 46.18           C  
ANISOU 1643  CG  ASP A 219     6138   5787   5621     83    149    326       C  
ATOM   1644  OD1 ASP A 219      35.630 -27.797  17.230  1.00 52.90           O  
ANISOU 1644  OD1 ASP A 219     6964   6613   6522     79    166    313       O  
ATOM   1645  OD2 ASP A 219      36.905 -27.927  19.035  1.00 51.32           O  
ANISOU 1645  OD2 ASP A 219     6803   6443   6254     95    150    360       O  
ATOM   1646  N   ARG A 220      37.257 -23.051  16.678  1.00 26.98           N  
ANISOU 1646  N   ARG A 220     3714   3414   3121     48     77    231       N  
ATOM   1647  CA  ARG A 220      37.150 -21.636  16.877  1.00 27.01           C  
ANISOU 1647  CA  ARG A 220     3733   3433   3096     39     70    211       C  
ATOM   1648  C   ARG A 220      36.481 -21.086  15.626  1.00 25.92           C  
ANISOU 1648  C   ARG A 220     3572   3285   2990     29     73    183       C  
ATOM   1649  O   ARG A 220      35.612 -20.221  15.706  1.00 26.54           O  
ANISOU 1649  O   ARG A 220     3657   3359   3065     23     87    169       O  
ATOM   1650  CB  ARG A 220      38.552 -21.075  17.063  1.00 26.98           C  
ANISOU 1650  CB  ARG A 220     3736   3455   3061     38     33    208       C  
ATOM   1651  CG  ARG A 220      38.596 -19.585  17.388  1.00 28.06           C  
ANISOU 1651  CG  ARG A 220     3888   3606   3166     29     22    186       C  
ATOM   1652  CD  ARG A 220      40.035 -19.180  17.818  1.00 27.48           C  
ANISOU 1652  CD  ARG A 220     3822   3557   3060     29    -14    187       C  
ATOM   1653  NE  ARG A 220      39.912 -17.819  18.271  1.00 26.40           N  
ANISOU 1653  NE  ARG A 220     3702   3432   2896     21    -18    166       N  
ATOM   1654  CZ  ARG A 220      40.851 -16.881  18.183  1.00 27.59           C  
ANISOU 1654  CZ  ARG A 220     3852   3598   3033     14    -48    149       C  
ATOM   1655  NH1 ARG A 220      42.028 -17.123  17.618  1.00 28.55           N  
ANISOU 1655  NH1 ARG A 220     3955   3727   3163     14    -77    153       N  
ATOM   1656  NH2 ARG A 220      40.586 -15.658  18.634  1.00 26.43           N  
ANISOU 1656  NH2 ARG A 220     3719   3456   2864      6    -48    128       N  
ATOM   1657  N   THR A 221      36.792 -21.656  14.475  1.00 24.90           N  
ANISOU 1657  N   THR A 221     3416   3149   2894     29     62    177       N  
ATOM   1658  CA  THR A 221      36.159 -21.159  13.218  1.00 24.56           C  
ANISOU 1658  CA  THR A 221     3351   3100   2879     20     63    152       C  
ATOM   1659  C   THR A 221      34.667 -21.383  13.318  1.00 25.17           C  
ANISOU 1659  C   THR A 221     3427   3156   2980     20     96    151       C  
ATOM   1660  O   THR A 221      33.919 -20.470  13.142  1.00 26.99           O  
ANISOU 1660  O   THR A 221     3658   3385   3211     13    104    135       O  
ATOM   1661  CB  THR A 221      36.717 -21.916  12.035  1.00 23.99           C  
ANISOU 1661  CB  THR A 221     3251   3025   2837     22     49    147       C  
ATOM   1662  OG1 THR A 221      38.139 -21.826  12.071  1.00 24.90           O  
ANISOU 1662  OG1 THR A 221     3368   3158   2932     24     21    152       O  
ATOM   1663  CG2 THR A 221      36.181 -21.443  10.643  1.00 23.65           C  
ANISOU 1663  CG2 THR A 221     3184   2980   2819     15     46    121       C  
ATOM   1664  N   VAL A 222      34.233 -22.589  13.684  1.00 24.81           N  
ANISOU 1664  N   VAL A 222     3378   3092   2954     27    117    168       N  
ATOM   1665  CA  VAL A 222      32.822 -22.891  13.654  1.00 24.59           C  
ANISOU 1665  CA  VAL A 222     3343   3041   2957     26    149    166       C  
ATOM   1666  C   VAL A 222      32.092 -21.941  14.588  1.00 25.16           C  
ANISOU 1666  C   VAL A 222     3439   3116   3004     24    167    166       C  
ATOM   1667  O   VAL A 222      30.951 -21.550  14.309  1.00 23.85           O  
ANISOU 1667  O   VAL A 222     3265   2936   2858     19    186    153       O  
ATOM   1668  CB  VAL A 222      32.508 -24.348  14.094  1.00 25.32           C  
ANISOU 1668  CB  VAL A 222     3431   3112   3076     35    172    189       C  
ATOM   1669  CG1 VAL A 222      31.001 -24.513  14.218  1.00 25.68           C  
ANISOU 1669  CG1 VAL A 222     3470   3133   3151     33    207    187       C  
ATOM   1670  CG2 VAL A 222      33.089 -25.382  13.126  1.00 24.42           C  
ANISOU 1670  CG2 VAL A 222     3290   2990   2996     38    158    186       C  
ATOM   1671  N   ASN A 223      32.735 -21.608  15.718  1.00 24.72           N  
ANISOU 1671  N   ASN A 223     3412   3077   2904     27    163    180       N  
ATOM   1672  CA  ASN A 223      32.133 -20.806  16.720  1.00 26.89           C  
ANISOU 1672  CA  ASN A 223     3712   3355   3150     26    181    180       C  
ATOM   1673  C   ASN A 223      32.506 -19.289  16.693  1.00 29.07           C  
ANISOU 1673  C   ASN A 223     3998   3649   3396     18    161    157       C  
ATOM   1674  O   ASN A 223      32.432 -18.635  17.794  1.00 28.96           O  
ANISOU 1674  O   ASN A 223     4012   3645   3345     19    170    158       O  
ATOM   1675  CB  ASN A 223      32.609 -21.375  18.063  1.00 27.81           C  
ANISOU 1675  CB  ASN A 223     3855   3480   3231     37    189    209       C  
ATOM   1676  CG  ASN A 223      32.076 -22.819  18.290  1.00 31.31           C  
ANISOU 1676  CG  ASN A 223     4290   3900   3704     46    217    235       C  
ATOM   1677  OD1 ASN A 223      32.803 -23.686  18.767  1.00 33.23           O  
ANISOU 1677  OD1 ASN A 223     4538   4147   3938     55    211    260       O  
ATOM   1678  ND2 ASN A 223      30.825 -23.072  17.875  1.00 28.35           N  
ANISOU 1678  ND2 ASN A 223     3899   3500   3371     43    245    229       N  
ATOM   1679  N   THR A 224      33.007 -18.769  15.563  1.00 25.20           N  
ANISOU 1679  N   THR A 224     3489   3166   2919     11    135    139       N  
ATOM   1680  CA  THR A 224      33.548 -17.358  15.556  1.00 26.46           C  
ANISOU 1680  CA  THR A 224     3658   3343   3052      3    114    120       C  
ATOM   1681  C   THR A 224      32.486 -16.313  15.921  1.00 28.27           C  
ANISOU 1681  C   THR A 224     3896   3564   3278     -1    136    106       C  
ATOM   1682  O   THR A 224      32.719 -15.432  16.743  1.00 28.51           O  
ANISOU 1682  O   THR A 224     3949   3605   3276     -3    134     99       O  
ATOM   1683  CB  THR A 224      34.096 -16.903  14.195  1.00 25.28           C  
ANISOU 1683  CB  THR A 224     3483   3199   2922     -2     88    104       C  
ATOM   1684  OG1 THR A 224      35.156 -17.768  13.795  1.00 24.58           O  
ANISOU 1684  OG1 THR A 224     3384   3118   2837      1     67    114       O  
ATOM   1685  CG2 THR A 224      34.593 -15.400  14.251  1.00 24.44           C  
ANISOU 1685  CG2 THR A 224     3385   3106   2793    -10     70     87       C  
ATOM   1686  N   ALA A 225      31.345 -16.401  15.248  1.00 28.51           N  
ANISOU 1686  N   ALA A 225     3909   3576   3346     -3    155     99       N  
ATOM   1687  CA  ALA A 225      30.269 -15.475  15.469  1.00 31.23           C  
ANISOU 1687  CA  ALA A 225     4257   3910   3696     -7    177     86       C  
ATOM   1688  C   ALA A 225      29.860 -15.476  16.919  1.00 30.25           C  
ANISOU 1688  C   ALA A 225     4163   3785   3544     -3    204     95       C  
ATOM   1689  O   ALA A 225      29.706 -14.382  17.485  1.00 32.09           O  
ANISOU 1689  O   ALA A 225     4413   4023   3756     -6    209     82       O  
ATOM   1690  CB  ALA A 225      29.072 -15.736  14.547  1.00 30.33           C  
ANISOU 1690  CB  ALA A 225     4116   3775   3629     -9    194     80       C  
ATOM   1691  N   LEU A 226      29.695 -16.654  17.524  1.00 30.36           N  
ANISOU 1691  N   LEU A 226     4184   3793   3557      5    222    118       N  
ATOM   1692  CA  LEU A 226      29.532 -16.717  19.040  1.00 32.71           C  
ANISOU 1692  CA  LEU A 226     4515   4096   3816     12    246    131       C  
ATOM   1693  C   LEU A 226      30.669 -16.092  19.871  1.00 32.85           C  
ANISOU 1693  C   LEU A 226     4559   4140   3779     12    222    128       C  
ATOM   1694  O   LEU A 226      30.449 -15.528  20.980  1.00 36.49           O  
ANISOU 1694  O   LEU A 226     5048   4610   4205     14    237    125       O  
ATOM   1695  CB  LEU A 226      29.342 -18.178  19.568  1.00 31.89           C  
ANISOU 1695  CB  LEU A 226     4414   3983   3719     22    267    162       C  
ATOM   1696  CG  LEU A 226      28.959 -18.322  21.068  1.00 35.63           C  
ANISOU 1696  CG  LEU A 226     4919   4460   4156     31    298    180       C  
ATOM   1697  CD1 LEU A 226      27.722 -17.488  21.457  1.00 35.17           C  
ANISOU 1697  CD1 LEU A 226     4869   4390   4102     27    332    166       C  
ATOM   1698  CD2 LEU A 226      28.694 -19.803  21.477  1.00 36.58           C  
ANISOU 1698  CD2 LEU A 226     5038   4567   4291     42    322    215       C  
ATOM   1699  N   GLU A 227      31.904 -16.294  19.432  1.00 29.87           N  
ANISOU 1699  N   GLU A 227     4175   3778   3395     12    185    131       N  
ATOM   1700  CA  GLU A 227      32.987 -15.817  20.231  1.00 30.84           C  
ANISOU 1700  CA  GLU A 227     4320   3926   3470     12    161    129       C  
ATOM   1701  C   GLU A 227      32.943 -14.276  20.238  1.00 29.64           C  
ANISOU 1701  C   GLU A 227     4175   3780   3307      2    154     98       C  
ATOM   1702  O   GLU A 227      33.189 -13.630  21.235  1.00 28.30           O  
ANISOU 1702  O   GLU A 227     4030   3624   3096      2    152     90       O  
ATOM   1703  CB  GLU A 227      34.299 -16.299  19.625  1.00 32.90           C  
ANISOU 1703  CB  GLU A 227     4567   4199   3733     13    124    136       C  
ATOM   1704  CG  GLU A 227      35.554 -15.972  20.446  1.00 33.40           C  
ANISOU 1704  CG  GLU A 227     4651   4289   3750     15     94    137       C  
ATOM   1705  CD  GLU A 227      36.835 -16.327  19.690  1.00 32.76           C  
ANISOU 1705  CD  GLU A 227     4550   4217   3678     14     57    141       C  
ATOM   1706  OE1 GLU A 227      36.776 -16.819  18.532  1.00 32.79           O  
ANISOU 1706  OE1 GLU A 227     4527   4208   3722     13     55    142       O  
ATOM   1707  OE2 GLU A 227      37.907 -16.115  20.268  1.00 35.43           O  
ANISOU 1707  OE2 GLU A 227     4900   4576   3983     16     30    142       O  
ATOM   1708  N   ILE A 228      32.613 -13.702  19.110  1.00 27.19           N  
ANISOU 1708  N   ILE A 228     3840   3457   3032     -5    149     82       N  
ATOM   1709  CA  ILE A 228      32.599 -12.259  19.003  1.00 27.13           C  
ANISOU 1709  CA  ILE A 228     3834   3452   3022    -14    142     55       C  
ATOM   1710  C   ILE A 228      31.443 -11.677  19.850  1.00 28.15           C  
ANISOU 1710  C   ILE A 228     3981   3570   3142    -14    178     45       C  
ATOM   1711  O   ILE A 228      31.558 -10.586  20.320  1.00 28.72           O  
ANISOU 1711  O   ILE A 228     4067   3649   3196    -19    175     24       O  
ATOM   1712  CB  ILE A 228      32.404 -11.863  17.516  1.00 25.42           C  
ANISOU 1712  CB  ILE A 228     3585   3223   2849    -21    132     45       C  
ATOM   1713  CG1 ILE A 228      33.617 -12.339  16.681  1.00 24.20           C  
ANISOU 1713  CG1 ILE A 228     3413   3080   2699    -22     97     52       C  
ATOM   1714  CG2 ILE A 228      32.308 -10.355  17.407  1.00 24.74           C  
ANISOU 1714  CG2 ILE A 228     3498   3135   2764    -31    128     20       C  
ATOM   1715  CD1 ILE A 228      33.645 -11.983  15.243  1.00 25.04           C  
ANISOU 1715  CD1 ILE A 228     3490   3182   2841    -27     84     44       C  
ATOM   1716  N   VAL A 229      30.310 -12.384  19.976  1.00 28.61           N  
ANISOU 1716  N   VAL A 229     4037   3611   3219     -9    213     58       N  
ATOM   1717  CA  VAL A 229      29.110 -11.758  20.563  1.00 28.19           C  
ANISOU 1717  CA  VAL A 229     3995   3545   3169     -9    249     47       C  
ATOM   1718  C   VAL A 229      29.343 -11.859  22.053  1.00 29.44           C  
ANISOU 1718  C   VAL A 229     4189   3720   3275     -3    261     53       C  
ATOM   1719  O   VAL A 229      29.019 -10.960  22.787  1.00 28.44           O  
ANISOU 1719  O   VAL A 229     4082   3596   3127     -5    275     35       O  
ATOM   1720  CB  VAL A 229      27.768 -12.435  20.154  1.00 29.40           C  
ANISOU 1720  CB  VAL A 229     4130   3673   3366     -6    284     58       C  
ATOM   1721  CG1 VAL A 229      26.588 -11.846  20.917  1.00 29.27           C  
ANISOU 1721  CG1 VAL A 229     4127   3643   3349     -6    324     49       C  
ATOM   1722  CG2 VAL A 229      27.475 -12.272  18.682  1.00 27.72           C  
ANISOU 1722  CG2 VAL A 229     3882   3446   3202    -13    271     50       C  
ATOM   1723  N   ASN A 230      29.975 -12.957  22.458  1.00 30.67           N  
ANISOU 1723  N   ASN A 230     4354   3888   3410      5    253     78       N  
ATOM   1724  CA  ASN A 230      30.429 -13.117  23.813  1.00 32.71           C  
ANISOU 1724  CA  ASN A 230     4647   4168   3613     13    256     87       C  
ATOM   1725  C   ASN A 230      31.361 -12.039  24.241  1.00 32.02           C  
ANISOU 1725  C   ASN A 230     4575   4103   3488      7    226     62       C  
ATOM   1726  O   ASN A 230      31.380 -11.754  25.409  1.00 31.63           O  
ANISOU 1726  O   ASN A 230     4555   4069   3392     11    235     57       O  
ATOM   1727  CB  ASN A 230      31.022 -14.520  24.102  1.00 34.41           C  
ANISOU 1727  CB  ASN A 230     4866   4393   3816     24    249    122       C  
ATOM   1728  CG  ASN A 230      29.942 -15.595  24.215  1.00 38.65           C  
ANISOU 1728  CG  ASN A 230     5397   4908   4378     32    290    149       C  
ATOM   1729  OD1 ASN A 230      28.774 -15.279  24.445  1.00 41.33           O  
ANISOU 1729  OD1 ASN A 230     5740   5232   4732     31    327    142       O  
ATOM   1730  ND2 ASN A 230      30.322 -16.878  24.033  1.00 37.36           N  
ANISOU 1730  ND2 ASN A 230     5225   4742   4227     40    285    179       N  
ATOM   1731  N   LEU A 231      32.083 -11.385  23.320  1.00 30.65           N  
ANISOU 1731  N   LEU A 231     4381   3930   3332     -2    192     45       N  
ATOM   1732  CA  LEU A 231      32.975 -10.274  23.747  1.00 29.05           C  
ANISOU 1732  CA  LEU A 231     4191   3745   3098     -9    164     18       C  
ATOM   1733  C   LEU A 231      32.308  -8.883  23.734  1.00 28.01           C  
ANISOU 1733  C   LEU A 231     4060   3602   2978    -18    178    -14       C  
ATOM   1734  O   LEU A 231      32.984  -7.845  23.723  1.00 26.19           O  
ANISOU 1734  O   LEU A 231     3830   3378   2740    -27    154    -40       O  
ATOM   1735  CB  LEU A 231      34.272 -10.253  22.947  1.00 28.84           C  
ANISOU 1735  CB  LEU A 231     4147   3730   3081    -14    119     17       C  
ATOM   1736  CG  LEU A 231      35.215 -11.411  23.272  1.00 30.38           C  
ANISOU 1736  CG  LEU A 231     4347   3942   3252     -4     98     45       C  
ATOM   1737  CD1 LEU A 231      36.186 -11.651  22.140  1.00 31.41           C  
ANISOU 1737  CD1 LEU A 231     4449   4074   3410     -9     64     49       C  
ATOM   1738  CD2 LEU A 231      35.927 -11.159  24.576  1.00 31.05           C  
ANISOU 1738  CD2 LEU A 231     4463   4056   3279      0     83     39       C  
ATOM   1739  N   HIS A 232      30.975  -8.881  23.683  1.00 28.15           N  
ANISOU 1739  N   HIS A 232     4075   3599   3021    -16    218    -13       N  
ATOM   1740  CA  HIS A 232      30.168  -7.635  23.524  1.00 28.35           C  
ANISOU 1740  CA  HIS A 232     4095   3606   3069    -24    237    -42       C  
ATOM   1741  C   HIS A 232      30.349  -6.889  22.228  1.00 27.90           C  
ANISOU 1741  C   HIS A 232     4007   3535   3056    -35    216    -54       C  
ATOM   1742  O   HIS A 232      30.259  -5.660  22.237  1.00 29.52           O  
ANISOU 1742  O   HIS A 232     4211   3734   3269    -42    216    -81       O  
ATOM   1743  CB  HIS A 232      30.323  -6.687  24.735  1.00 28.19           C  
ANISOU 1743  CB  HIS A 232     4105   3599   3004    -26    241    -69       C  
ATOM   1744  CG  HIS A 232      29.069  -5.898  25.049  1.00 28.16           C  
ANISOU 1744  CG  HIS A 232     4106   3575   3016    -28    282    -89       C  
ATOM   1745  ND1 HIS A 232      29.025  -4.523  25.019  1.00 28.97           N  
ANISOU 1745  ND1 HIS A 232     4207   3670   3130    -37    279   -123       N  
ATOM   1746  CD2 HIS A 232      27.812  -6.316  25.434  1.00 27.11           C  
ANISOU 1746  CD2 HIS A 232     3979   3428   2891    -21    327    -78       C  
ATOM   1747  CE1 HIS A 232      27.778  -4.118  25.328  1.00 27.58           C  
ANISOU 1747  CE1 HIS A 232     4034   3474   2969    -35    322   -133       C  
ATOM   1748  NE2 HIS A 232      27.039  -5.206  25.568  1.00 28.62           N  
ANISOU 1748  NE2 HIS A 232     4170   3603   3100    -26    351   -105       N  
ATOM   1749  N   ALA A 233      30.577  -7.611  21.125  1.00 26.80           N  
ANISOU 1749  N   ALA A 233     3843   3392   2947    -34    200    -35       N  
ATOM   1750  CA  ALA A 233      30.543  -7.054  19.764  1.00 27.06           C  
ANISOU 1750  CA  ALA A 233     3843   3412   3025    -42    186    -42       C  
ATOM   1751  C   ALA A 233      29.678  -7.877  18.839  1.00 28.46           C  
ANISOU 1751  C   ALA A 233     3997   3573   3243    -38    201    -23       C  
ATOM   1752  O   ALA A 233      28.960  -8.814  19.246  1.00 28.96           O  
ANISOU 1752  O   ALA A 233     4066   3630   3305    -31    227     -8       O  
ATOM   1753  CB  ALA A 233      31.937  -6.985  19.181  1.00 26.26           C  
ANISOU 1753  CB  ALA A 233     3731   3325   2918    -46    144    -41       C  
ATOM   1754  N   SER A 234      29.816  -7.609  17.559  1.00 30.16           N  
ANISOU 1754  N   SER A 234     4184   3783   3492    -43    184    -24       N  
ATOM   1755  CA  SER A 234      28.925  -8.210  16.559  1.00 31.04           C  
ANISOU 1755  CA  SER A 234     4270   3879   3645    -40    195    -13       C  
ATOM   1756  C   SER A 234      29.664  -8.367  15.204  1.00 29.77           C  
ANISOU 1756  C   SER A 234     4082   3724   3502    -42    163     -8       C  
ATOM   1757  O   SER A 234      30.284  -7.406  14.706  1.00 28.08           O  
ANISOU 1757  O   SER A 234     3860   3516   3292    -49    143    -18       O  
ATOM   1758  CB  SER A 234      27.707  -7.270  16.387  1.00 34.15           C  
ANISOU 1758  CB  SER A 234     4654   4252   4068    -43    220    -26       C  
ATOM   1759  OG  SER A 234      26.517  -7.990  16.123  1.00 38.93           O  
ANISOU 1759  OG  SER A 234     5246   4841   4703    -38    246    -16       O  
ATOM   1760  N   PRO A 235      29.616  -9.573  14.605  1.00 28.64           N  
ANISOU 1760  N   PRO A 235     3924   3581   3373    -37    160      7       N  
ATOM   1761  CA  PRO A 235      30.322  -9.803  13.351  1.00 28.22           C  
ANISOU 1761  CA  PRO A 235     3849   3538   3336    -39    132     11       C  
ATOM   1762  C   PRO A 235      29.671  -9.113  12.144  1.00 27.66           C  
ANISOU 1762  C   PRO A 235     3751   3458   3301    -42    131      4       C  
ATOM   1763  O   PRO A 235      28.667  -9.620  11.598  1.00 27.50           O  
ANISOU 1763  O   PRO A 235     3714   3426   3308    -39    145      8       O  
ATOM   1764  CB  PRO A 235      30.240 -11.354  13.188  1.00 29.46           C  
ANISOU 1764  CB  PRO A 235     3999   3693   3499    -32    136     27       C  
ATOM   1765  CG  PRO A 235      29.107 -11.774  14.093  1.00 28.64           C  
ANISOU 1765  CG  PRO A 235     3908   3574   3399    -28    172     32       C  
ATOM   1766  CD  PRO A 235      29.235 -10.851  15.254  1.00 29.98           C  
ANISOU 1766  CD  PRO A 235     4104   3748   3536    -30    180     23       C  
ATOM   1767  N   TYR A 236      30.183  -7.954  11.726  1.00 25.77           N  
ANISOU 1767  N   TYR A 236     3505   3223   3061    -47    115     -4       N  
ATOM   1768  CA  TYR A 236      29.603  -7.363  10.545  1.00 24.33           C  
ANISOU 1768  CA  TYR A 236     3297   3034   2912    -49    113     -5       C  
ATOM   1769  C   TYR A 236      30.599  -6.856   9.534  1.00 23.31           C  
ANISOU 1769  C   TYR A 236     3152   2918   2784    -51     84     -4       C  
ATOM   1770  O   TYR A 236      30.281  -6.717   8.348  1.00 23.99           O  
ANISOU 1770  O   TYR A 236     3215   3006   2894    -50     78      0       O  
ATOM   1771  CB  TYR A 236      28.535  -6.292  10.863  1.00 26.51           C  
ANISOU 1771  CB  TYR A 236     3574   3292   3205    -51    135    -15       C  
ATOM   1772  CG  TYR A 236      28.974  -5.214  11.798  1.00 29.63           C  
ANISOU 1772  CG  TYR A 236     3989   3685   3581    -57    137    -28       C  
ATOM   1773  CD1 TYR A 236      29.749  -4.100  11.348  1.00 29.55           C  
ANISOU 1773  CD1 TYR A 236     3971   3679   3575    -62    118    -34       C  
ATOM   1774  CD2 TYR A 236      28.592  -5.270  13.160  1.00 29.71           C  
ANISOU 1774  CD2 TYR A 236     4026   3690   3572    -56    160    -36       C  
ATOM   1775  CE1 TYR A 236      30.130  -3.070  12.235  1.00 32.39           C  
ANISOU 1775  CE1 TYR A 236     4348   4035   3922    -68    120    -50       C  
ATOM   1776  CE2 TYR A 236      29.000  -4.270  14.069  1.00 32.41           C  
ANISOU 1776  CE2 TYR A 236     4387   4031   3894    -61    161    -52       C  
ATOM   1777  CZ  TYR A 236      29.775  -3.157  13.613  1.00 35.18           C  
ANISOU 1777  CZ  TYR A 236     4729   4385   4252    -68    140    -61       C  
ATOM   1778  OH  TYR A 236      30.124  -2.153  14.548  1.00 33.57           O  
ANISOU 1778  OH  TYR A 236     4544   4178   4033    -74    143    -81       O  
ATOM   1779  N   VAL A 237      31.805  -6.576   9.947  1.00 22.49           N  
ANISOU 1779  N   VAL A 237     3060   2826   2657    -55     67     -6       N  
ATOM   1780  CA  VAL A 237      32.855  -6.148   8.976  1.00 22.46           C  
ANISOU 1780  CA  VAL A 237     3041   2836   2657    -57     41     -2       C  
ATOM   1781  C   VAL A 237      33.324  -7.253   8.025  1.00 22.24           C  
ANISOU 1781  C   VAL A 237     2997   2821   2631    -52     26      8       C  
ATOM   1782  O   VAL A 237      33.274  -7.146   6.679  1.00 20.92           O  
ANISOU 1782  O   VAL A 237     2806   2660   2482    -50     17     13       O  
ATOM   1783  CB  VAL A 237      34.048  -5.584   9.739  1.00 23.22           C  
ANISOU 1783  CB  VAL A 237     3153   2939   2731    -63     26     -9       C  
ATOM   1784  CG1 VAL A 237      35.112  -5.076   8.765  1.00 24.59           C  
ANISOU 1784  CG1 VAL A 237     3307   3122   2911    -66      2     -4       C  
ATOM   1785  CG2 VAL A 237      33.578  -4.427  10.556  1.00 22.48           C  
ANISOU 1785  CG2 VAL A 237     3072   2832   2638    -69     40    -23       C  
ATOM   1786  N   ALA A 238      33.711  -8.364   8.674  1.00 21.89           N  
ANISOU 1786  N   ALA A 238     2965   2781   2568    -49     25     12       N  
ATOM   1787  CA  ALA A 238      34.007  -9.564   7.894  1.00 21.25           C  
ANISOU 1787  CA  ALA A 238     2872   2709   2493    -43     16     20       C  
ATOM   1788  C   ALA A 238      32.909  -9.937   6.881  1.00 21.23           C  
ANISOU 1788  C   ALA A 238     2848   2701   2517    -39     25     20       C  
ATOM   1789  O   ALA A 238      33.169 -10.082   5.702  1.00 21.12           O  
ANISOU 1789  O   ALA A 238     2813   2697   2512    -37     12     21       O  
ATOM   1790  CB  ALA A 238      34.377 -10.701   8.767  1.00 22.54           C  
ANISOU 1790  CB  ALA A 238     3050   2874   2639    -39     18     26       C  
ATOM   1791  N   PRO A 239      31.652 -10.092   7.344  1.00 21.37           N  
ANISOU 1791  N   PRO A 239     2868   2702   2546    -38     49     17       N  
ATOM   1792  CA  PRO A 239      30.629 -10.423   6.370  1.00 20.02           C  
ANISOU 1792  CA  PRO A 239     2676   2526   2403    -35     55     15       C  
ATOM   1793  C   PRO A 239      30.543  -9.494   5.164  1.00 21.09           C  
ANISOU 1793  C   PRO A 239     2790   2669   2552    -36     42     14       C  
ATOM   1794  O   PRO A 239      30.554  -9.990   4.008  1.00 21.67           O  
ANISOU 1794  O   PRO A 239     2843   2753   2634    -32     31     14       O  
ATOM   1795  CB  PRO A 239      29.341 -10.456   7.200  1.00 20.47           C  
ANISOU 1795  CB  PRO A 239     2741   2562   2472    -35     83     12       C  
ATOM   1796  CG  PRO A 239      29.828 -10.836   8.596  1.00 19.97           C  
ANISOU 1796  CG  PRO A 239     2706   2498   2384    -35     92     16       C  
ATOM   1797  CD  PRO A 239      31.199 -10.268   8.747  1.00 20.11           C  
ANISOU 1797  CD  PRO A 239     2733   2530   2375    -38     70     17       C  
ATOM   1798  N   ALA A 240      30.456  -8.170   5.433  1.00 20.58           N  
ANISOU 1798  N   ALA A 240     2731   2599   2488    -40     46     13       N  
ATOM   1799  CA  ALA A 240      30.454  -7.174   4.454  1.00 19.44           C  
ANISOU 1799  CA  ALA A 240     2570   2461   2356    -40     36     15       C  
ATOM   1800  C   ALA A 240      31.596  -7.314   3.503  1.00 19.41           C  
ANISOU 1800  C   ALA A 240     2555   2478   2342    -39     13     22       C  
ATOM   1801  O   ALA A 240      31.355  -7.330   2.244  1.00 18.01           O  
ANISOU 1801  O   ALA A 240     2355   2311   2175    -34      4     25       O  
ATOM   1802  CB  ALA A 240      30.432  -5.789   5.092  1.00 19.29           C  
ANISOU 1802  CB  ALA A 240     2560   2429   2338    -46     44     13       C  
ATOM   1803  N   ALA A 241      32.831  -7.435   4.001  1.00 18.57           N  
ANISOU 1803  N   ALA A 241     2461   2378   2215    -42      2     23       N  
ATOM   1804  CA  ALA A 241      33.878  -7.607   3.013  1.00 19.90           C  
ANISOU 1804  CA  ALA A 241     2616   2567   2377    -40    -16     29       C  
ATOM   1805  C   ALA A 241      33.778  -8.891   2.187  1.00 20.76           C  
ANISOU 1805  C   ALA A 241     2712   2686   2488    -33    -22     28       C  
ATOM   1806  O   ALA A 241      34.094  -8.872   0.995  1.00 20.48           O  
ANISOU 1806  O   ALA A 241     2659   2667   2454    -29    -33     32       O  
ATOM   1807  CB  ALA A 241      35.252  -7.517   3.624  1.00 22.34           C  
ANISOU 1807  CB  ALA A 241     2937   2881   2667    -44    -28     30       C  
ATOM   1808  N   ALA A 242      33.321  -9.991   2.761  1.00 20.37           N  
ANISOU 1808  N   ALA A 242     2669   2628   2439    -31    -12     23       N  
ATOM   1809  CA  ALA A 242      33.242 -11.200   1.922  1.00 21.39           C  
ANISOU 1809  CA  ALA A 242     2784   2766   2575    -25    -17     20       C  
ATOM   1810  C   ALA A 242      32.129 -10.982   0.896  1.00 24.53           C  
ANISOU 1810  C   ALA A 242     3161   3166   2991    -22    -15     16       C  
ATOM   1811  O   ALA A 242      32.220 -11.420  -0.283  1.00 22.22           O  
ANISOU 1811  O   ALA A 242     2851   2890   2702    -17    -27     12       O  
ATOM   1812  CB  ALA A 242      32.852 -12.391   2.765  1.00 22.13           C  
ANISOU 1812  CB  ALA A 242     2888   2847   2673    -24     -5     17       C  
ATOM   1813  N   ILE A 243      31.063 -10.276   1.311  1.00 23.96           N  
ANISOU 1813  N   ILE A 243     3091   3078   2932    -24     -1     15       N  
ATOM   1814  CA  ILE A 243      30.070 -10.064   0.270  1.00 23.70           C  
ANISOU 1814  CA  ILE A 243     3036   3049   2917    -20     -3     13       C  
ATOM   1815  C   ILE A 243      30.573  -9.228  -0.832  1.00 23.77           C  
ANISOU 1815  C   ILE A 243     3033   3078   2920    -17    -19     20       C  
ATOM   1816  O   ILE A 243      30.262  -9.508  -2.013  1.00 25.98           O  
ANISOU 1816  O   ILE A 243     3292   3373   3203    -11    -29     18       O  
ATOM   1817  CB  ILE A 243      28.808  -9.377   0.853  1.00 24.34           C  
ANISOU 1817  CB  ILE A 243     3120   3110   3018    -22     14     12       C  
ATOM   1818  CG1 ILE A 243      28.213 -10.276   1.910  1.00 23.41           C  
ANISOU 1818  CG1 ILE A 243     3013   2972   2906    -23     33      6       C  
ATOM   1819  CG2 ILE A 243      27.793  -9.137  -0.277  1.00 22.84           C  
ANISOU 1819  CG2 ILE A 243     2905   2925   2847    -17      9     10       C  
ATOM   1820  CD1 ILE A 243      27.243  -9.533   2.804  1.00 27.10           C  
ANISOU 1820  CD1 ILE A 243     3490   3418   3388    -26     55      5       C  
ATOM   1821  N   ILE A 244      31.278  -8.130  -0.499  1.00 23.03           N  
ANISOU 1821  N   ILE A 244     2948   2983   2817    -22    -20     30       N  
ATOM   1822  CA  ILE A 244      31.792  -7.254  -1.552  1.00 23.50           C  
ANISOU 1822  CA  ILE A 244     2994   3060   2873    -19    -33     41       C  
ATOM   1823  C   ILE A 244      32.793  -8.001  -2.493  1.00 25.68           C  
ANISOU 1823  C   ILE A 244     3262   3362   3134    -14    -48     42       C  
ATOM   1824  O   ILE A 244      32.763  -7.904  -3.815  1.00 24.58           O  
ANISOU 1824  O   ILE A 244     3103   3243   2991     -7    -59     47       O  
ATOM   1825  CB  ILE A 244      32.289  -5.929  -0.952  1.00 23.43           C  
ANISOU 1825  CB  ILE A 244     2995   3041   2865    -25    -29     50       C  
ATOM   1826  CG1 ILE A 244      31.103  -5.135  -0.403  1.00 21.75           C  
ANISOU 1826  CG1 ILE A 244     2783   2806   2672    -28    -13     48       C  
ATOM   1827  CG2 ILE A 244      33.003  -5.044  -1.982  1.00 23.60           C  
ANISOU 1827  CG2 ILE A 244     3003   3079   2885    -23    -40     65       C  
ATOM   1828  CD1 ILE A 244      29.991  -4.994  -1.468  1.00 20.99           C  
ANISOU 1828  CD1 ILE A 244     2665   2715   2592    -20    -14     53       C  
ATOM   1829  N   GLU A 245      33.618  -8.856  -1.881  1.00 25.83           N  
ANISOU 1829  N   GLU A 245     3292   3379   3141    -17    -50     36       N  
ATOM   1830  CA  GLU A 245      34.437  -9.742  -2.764  1.00 26.38           C  
ANISOU 1830  CA  GLU A 245     3352   3470   3200    -11    -62     34       C  
ATOM   1831  C   GLU A 245      33.636 -10.505  -3.844  1.00 25.76           C  
ANISOU 1831  C   GLU A 245     3256   3405   3127     -4    -66     24       C  
ATOM   1832  O   GLU A 245      34.046 -10.578  -5.005  1.00 24.97           O  
ANISOU 1832  O   GLU A 245     3142   3328   3018      1    -77     25       O  
ATOM   1833  CB  GLU A 245      35.341 -10.682  -1.983  1.00 28.30           C  
ANISOU 1833  CB  GLU A 245     3608   3709   3434    -14    -63     29       C  
ATOM   1834  CG  GLU A 245      36.286 -11.544  -2.883  1.00 28.91           C  
ANISOU 1834  CG  GLU A 245     3674   3807   3503     -8    -74     26       C  
ATOM   1835  CD  GLU A 245      37.451 -12.180  -2.124  1.00 29.81           C  
ANISOU 1835  CD  GLU A 245     3799   3917   3609    -10    -78     28       C  
ATOM   1836  OE1 GLU A 245      37.332 -12.433  -0.907  1.00 34.57           O  
ANISOU 1836  OE1 GLU A 245     4418   4503   4213    -14    -71     27       O  
ATOM   1837  OE2 GLU A 245      38.524 -12.407  -2.717  1.00 30.02           O  
ANISOU 1837  OE2 GLU A 245     3818   3959   3627     -7    -87     30       O  
ATOM   1838  N   MET A 246      32.491 -11.084  -3.442  1.00 27.43           N  
ANISOU 1838  N   MET A 246     3466   3600   3354     -4    -57     13       N  
ATOM   1839  CA  MET A 246      31.712 -11.852  -4.384  1.00 27.24           C  
ANISOU 1839  CA  MET A 246     3424   3586   3339      1    -62      0       C  
ATOM   1840  C   MET A 246      31.114 -10.910  -5.435  1.00 26.18           C  
ANISOU 1840  C   MET A 246     3274   3467   3204      6    -70      6       C  
ATOM   1841  O   MET A 246      31.241 -11.133  -6.686  1.00 28.83           O  
ANISOU 1841  O   MET A 246     3593   3828   3529     13    -83      2       O  
ATOM   1842  CB  MET A 246      30.625 -12.688  -3.651  1.00 29.62           C  
ANISOU 1842  CB  MET A 246     3727   3863   3661      0    -49    -12       C  
ATOM   1843  CG  MET A 246      31.104 -13.734  -2.635  1.00 32.71           C  
ANISOU 1843  CG  MET A 246     4134   4240   4055     -3    -40    -17       C  
ATOM   1844  SD  MET A 246      29.972 -14.118  -1.213  1.00 36.01           S  
ANISOU 1844  SD  MET A 246     4564   4623   4495     -8    -16    -18       S  
ATOM   1845  CE  MET A 246      28.597 -14.641  -2.255  1.00 36.37           C  
ANISOU 1845  CE  MET A 246     4581   4670   4567     -4    -19    -36       C  
ATOM   1846  N   ALA A 247      30.421  -9.855  -4.953  1.00 24.47           N  
ANISOU 1846  N   ALA A 247     3061   3236   3000      3    -61     16       N  
ATOM   1847  CA  ALA A 247      29.894  -8.807  -5.844  1.00 23.16           C  
ANISOU 1847  CA  ALA A 247     2880   3081   2836      8    -67     28       C  
ATOM   1848  C   ALA A 247      30.904  -8.261  -6.895  1.00 22.09           C  
ANISOU 1848  C   ALA A 247     2737   2974   2680     13    -80     43       C  
ATOM   1849  O   ALA A 247      30.616  -8.089  -8.102  1.00 21.12           O  
ANISOU 1849  O   ALA A 247     2598   2876   2551     22    -91     47       O  
ATOM   1850  CB  ALA A 247      29.262  -7.672  -5.025  1.00 21.86           C  
ANISOU 1850  CB  ALA A 247     2722   2893   2689      3    -54     39       C  
ATOM   1851  N   GLU A 248      32.097  -8.015  -6.424  1.00 22.27           N  
ANISOU 1851  N   GLU A 248     2773   2995   2692      8    -78     50       N  
ATOM   1852  CA  GLU A 248      33.159  -7.466  -7.238  1.00 24.32           C  
ANISOU 1852  CA  GLU A 248     3028   3278   2935     12    -86     66       C  
ATOM   1853  C   GLU A 248      33.654  -8.409  -8.336  1.00 24.38           C  
ANISOU 1853  C   GLU A 248     3024   3314   2924     20    -97     57       C  
ATOM   1854  O   GLU A 248      33.896  -8.012  -9.471  1.00 24.23           O  
ANISOU 1854  O   GLU A 248     2993   3321   2891     28   -104     68       O  
ATOM   1855  CB  GLU A 248      34.322  -7.089  -6.352  1.00 26.44           C  
ANISOU 1855  CB  GLU A 248     3311   3533   3200      4    -81     73       C  
ATOM   1856  CG  GLU A 248      35.413  -6.383  -7.135  1.00 28.94           C  
ANISOU 1856  CG  GLU A 248     3620   3869   3505      7    -87     91       C  
ATOM   1857  CD  GLU A 248      36.616  -6.125  -6.263  1.00 32.38           C  
ANISOU 1857  CD  GLU A 248     4068   4292   3940     -1    -85     94       C  
ATOM   1858  OE1 GLU A 248      36.975  -7.094  -5.574  1.00 32.38           O  
ANISOU 1858  OE1 GLU A 248     4079   4286   3935     -4    -85     80       O  
ATOM   1859  OE2 GLU A 248      37.195  -4.990  -6.264  1.00 33.58           O  
ANISOU 1859  OE2 GLU A 248     4219   4441   4098     -4    -83    111       O  
ATOM   1860  N   SER A 249      33.763  -9.684  -7.964  1.00 24.61           N  
ANISOU 1860  N   SER A 249     3058   3338   2953     18    -97     37       N  
ATOM   1861  CA  SER A 249      34.096 -10.692  -8.891  1.00 22.98           C  
ANISOU 1861  CA  SER A 249     2841   3154   2733     25   -105     23       C  
ATOM   1862  C   SER A 249      33.061 -10.808  -9.977  1.00 23.65           C  
ANISOU 1862  C   SER A 249     2909   3259   2817     34   -114     15       C  
ATOM   1863  O   SER A 249      33.397 -11.129 -11.126  1.00 25.52           O  
ANISOU 1863  O   SER A 249     3135   3526   3036     42   -123     10       O  
ATOM   1864  CB  SER A 249      34.130 -11.976  -8.130  1.00 21.86           C  
ANISOU 1864  CB  SER A 249     2706   2995   2601     21   -101      3       C  
ATOM   1865  OG  SER A 249      34.766 -12.939  -8.896  1.00 23.75           O  
ANISOU 1865  OG  SER A 249     2938   3254   2829     27   -107     -9       O  
ATOM   1866  N   TYR A 250      31.788 -10.647  -9.640  1.00 24.06           N  
ANISOU 1866  N   TYR A 250     2958   3295   2888     32   -111     11       N  
ATOM   1867  CA  TYR A 250      30.730 -10.588 -10.703  1.00 23.04           C  
ANISOU 1867  CA  TYR A 250     2809   3184   2758     41   -122      5       C  
ATOM   1868  C   TYR A 250      30.824  -9.328 -11.561  1.00 24.48           C  
ANISOU 1868  C   TYR A 250     2984   3388   2927     48   -128     31       C  
ATOM   1869  O   TYR A 250      30.873  -9.396 -12.839  1.00 25.98           O  
ANISOU 1869  O   TYR A 250     3160   3613   3095     58   -141     31       O  
ATOM   1870  CB  TYR A 250      29.342 -10.672 -10.066  1.00 22.80           C  
ANISOU 1870  CB  TYR A 250     2776   3129   2758     37   -117     -3       C  
ATOM   1871  CG  TYR A 250      28.199 -10.360 -11.032  1.00 24.05           C  
ANISOU 1871  CG  TYR A 250     2913   3304   2919     45   -129     -4       C  
ATOM   1872  CD1 TYR A 250      27.754 -11.321 -11.931  1.00 24.59           C  
ANISOU 1872  CD1 TYR A 250     2965   3392   2983     51   -144    -28       C  
ATOM   1873  CD2 TYR A 250      27.598  -9.087 -11.067  1.00 24.29           C  
ANISOU 1873  CD2 TYR A 250     2940   3331   2959     47   -128     18       C  
ATOM   1874  CE1 TYR A 250      26.756 -11.038 -12.849  1.00 26.06           C  
ANISOU 1874  CE1 TYR A 250     3133   3598   3171     59   -159    -30       C  
ATOM   1875  CE2 TYR A 250      26.589  -8.809 -11.958  1.00 24.05           C  
ANISOU 1875  CE2 TYR A 250     2889   3317   2932     55   -141     19       C  
ATOM   1876  CZ  TYR A 250      26.175  -9.774 -12.842  1.00 25.52           C  
ANISOU 1876  CZ  TYR A 250     3059   3525   3110     62   -158     -4       C  
ATOM   1877  OH  TYR A 250      25.151  -9.526 -13.714  1.00 25.40           O  
ANISOU 1877  OH  TYR A 250     3024   3528   3098     70   -174     -5       O  
ATOM   1878  N   LEU A 251      30.807  -8.161 -10.909  1.00 23.77           N  
ANISOU 1878  N   LEU A 251     2901   3280   2849     43   -119     54       N  
ATOM   1879  CA  LEU A 251      30.837  -6.899 -11.686  1.00 25.00           C  
ANISOU 1879  CA  LEU A 251     3049   3453   2998     50   -122     82       C  
ATOM   1880  C   LEU A 251      32.072  -6.710 -12.558  1.00 27.13           C  
ANISOU 1880  C   LEU A 251     3316   3750   3239     56   -126     96       C  
ATOM   1881  O   LEU A 251      31.954  -6.261 -13.703  1.00 26.17           O  
ANISOU 1881  O   LEU A 251     3182   3658   3102     67   -135    111       O  
ATOM   1882  CB  LEU A 251      30.647  -5.678 -10.778  1.00 24.33           C  
ANISOU 1882  CB  LEU A 251     2971   3338   2935     43   -110    101       C  
ATOM   1883  CG  LEU A 251      29.279  -5.559 -10.051  1.00 24.56           C  
ANISOU 1883  CG  LEU A 251     2999   3339   2993     39   -103     93       C  
ATOM   1884  CD1 LEU A 251      29.440  -4.689  -8.805  1.00 23.89           C  
ANISOU 1884  CD1 LEU A 251     2928   3220   2926     29    -87    102       C  
ATOM   1885  CD2 LEU A 251      28.154  -5.045 -10.896  1.00 23.32           C  
ANISOU 1885  CD2 LEU A 251     2821   3194   2843     49   -112    103       C  
ATOM   1886  N   LYS A 252      33.246  -7.095 -12.050  1.00 27.23           N  
ANISOU 1886  N   LYS A 252     3340   3757   3246     50   -121     92       N  
ATOM   1887  CA  LYS A 252      34.472  -6.912 -12.802  1.00 28.60           C  
ANISOU 1887  CA  LYS A 252     3512   3956   3398     55   -122    106       C  
ATOM   1888  C   LYS A 252      34.900  -8.195 -13.525  1.00 30.12           C  
ANISOU 1888  C   LYS A 252     3701   4174   3569     61   -129     83       C  
ATOM   1889  O   LYS A 252      35.990  -8.234 -14.143  1.00 29.82           O  
ANISOU 1889  O   LYS A 252     3661   4157   3512     65   -128     91       O  
ATOM   1890  CB  LYS A 252      35.576  -6.516 -11.861  1.00 30.44           C  
ANISOU 1890  CB  LYS A 252     3758   4167   3639     45   -112    115       C  
ATOM   1891  CG  LYS A 252      35.645  -5.033 -11.621  1.00 36.37           C  
ANISOU 1891  CG  LYS A 252     4509   4905   4404     42   -105    143       C  
ATOM   1892  CD  LYS A 252      36.543  -4.822 -10.405  1.00 37.27           C  
ANISOU 1892  CD  LYS A 252     4637   4991   4530     29    -97    143       C  
ATOM   1893  CE  LYS A 252      36.682  -3.357  -9.954  1.00 39.10           C  
ANISOU 1893  CE  LYS A 252     4870   5203   4782     23    -89    165       C  
ATOM   1894  NZ  LYS A 252      37.507  -3.473  -8.674  1.00 45.10           N  
ANISOU 1894  NZ  LYS A 252     5646   5939   5551     10    -85    154       N  
ATOM   1895  N   ASP A 253      34.076  -9.253 -13.424  1.00 29.07           N  
ANISOU 1895  N   ASP A 253     3565   4037   3442     61   -135     54       N  
ATOM   1896  CA  ASP A 253      34.269 -10.486 -14.236  1.00 28.93           C  
ANISOU 1896  CA  ASP A 253     3539   4043   3406     67   -143     28       C  
ATOM   1897  C   ASP A 253      35.642 -11.087 -14.037  1.00 27.51           C  
ANISOU 1897  C   ASP A 253     3368   3864   3219     65   -137     23       C  
ATOM   1898  O   ASP A 253      36.308 -11.451 -15.032  1.00 25.42           O  
ANISOU 1898  O   ASP A 253     3096   3629   2931     73   -140     19       O  
ATOM   1899  CB  ASP A 253      33.916 -10.253 -15.731  1.00 29.61           C  
ANISOU 1899  CB  ASP A 253     3610   4171   3467     81   -155     32       C  
ATOM   1900  CG  ASP A 253      34.041 -11.535 -16.603  1.00 34.88           C  
ANISOU 1900  CG  ASP A 253     4270   4866   4116     88   -164      0       C  
ATOM   1901  OD1 ASP A 253      33.557 -12.683 -16.289  1.00 32.74           O  
ANISOU 1901  OD1 ASP A 253     3997   4582   3859     85   -167    -33       O  
ATOM   1902  OD2 ASP A 253      34.648 -11.381 -17.675  1.00 37.04           O  
ANISOU 1902  OD2 ASP A 253     4538   5175   4359     99   -167      7       O  
ATOM   1903  N   LEU A 254      36.025 -11.177 -12.744  1.00 22.60           N  
ANISOU 1903  N   LEU A 254     2759   3209   2616     54   -128     24       N  
ATOM   1904  CA  LEU A 254      37.276 -11.654 -12.341  1.00 23.35           C  
ANISOU 1904  CA  LEU A 254     2862   3299   2709     50   -123     23       C  
ATOM   1905  C   LEU A 254      37.313 -13.176 -12.477  1.00 23.63           C  
ANISOU 1905  C   LEU A 254     2893   3336   2746     52   -125     -7       C  
ATOM   1906  O   LEU A 254      38.412 -13.686 -12.609  1.00 23.24           O  
ANISOU 1906  O   LEU A 254     2844   3294   2690     54   -123    -10       O  
ATOM   1907  CB  LEU A 254      37.558 -11.307 -10.835  1.00 23.09           C  
ANISOU 1907  CB  LEU A 254     2845   3231   2696     38   -115     32       C  
ATOM   1908  CG  LEU A 254      37.466  -9.812 -10.609  1.00 23.91           C  
ANISOU 1908  CG  LEU A 254     2951   3328   2804     35   -112     58       C  
ATOM   1909  CD1 LEU A 254      37.605  -9.392  -9.154  1.00 24.53           C  
ANISOU 1909  CD1 LEU A 254     3046   3373   2899     23   -105     64       C  
ATOM   1910  CD2 LEU A 254      38.620  -9.235 -11.411  1.00 26.10           C  
ANISOU 1910  CD2 LEU A 254     3222   3627   3066     39   -112     77       C  
ATOM   1911  N   LYS A 255      36.158 -13.874 -12.540  1.00 22.68           N  
ANISOU 1911  N   LYS A 255     2768   3212   2637     53   -130    -30       N  
ATOM   1912  CA  LYS A 255      36.095 -15.386 -12.542  1.00 22.13           C  
ANISOU 1912  CA  LYS A 255     2694   3137   2578     54   -130    -62       C  
ATOM   1913  C   LYS A 255      36.945 -15.962 -11.403  1.00 22.19           C  
ANISOU 1913  C   LYS A 255     2714   3118   2599     47   -121    -60       C  
ATOM   1914  O   LYS A 255      37.741 -16.923 -11.588  1.00 22.62           O  
ANISOU 1914  O   LYS A 255     2765   3175   2653     49   -120    -74       O  
ATOM   1915  CB  LYS A 255      36.546 -16.001 -13.869  1.00 22.37           C  
ANISOU 1915  CB  LYS A 255     2711   3202   2587     64   -137    -79       C  
ATOM   1916  CG  LYS A 255      35.886 -15.429 -15.158  1.00 22.00           C  
ANISOU 1916  CG  LYS A 255     2652   3190   2516     74   -148    -79       C  
ATOM   1917  CD  LYS A 255      36.457 -16.169 -16.336  1.00 23.55           C  
ANISOU 1917  CD  LYS A 255     2838   3420   2690     84   -152   -100       C  
ATOM   1918  CE  LYS A 255      35.991 -15.663 -17.722  1.00 25.25           C  
ANISOU 1918  CE  LYS A 255     3042   3678   2874     96   -164    -99       C  
ATOM   1919  NZ  LYS A 255      34.538 -15.386 -17.580  1.00 25.39           N  
ANISOU 1919  NZ  LYS A 255     3054   3687   2905     94   -174   -103       N  
ATOM   1920  N   LYS A 256      36.794 -15.380 -10.230  1.00 22.04           N  
ANISOU 1920  N   LYS A 256     2708   3072   2592     38   -115    -43       N  
ATOM   1921  CA  LYS A 256      37.394 -15.956  -9.020  1.00 23.53           C  
ANISOU 1921  CA  LYS A 256     2909   3234   2794     32   -108    -42       C  
ATOM   1922  C   LYS A 256      36.702 -17.252  -8.593  1.00 24.21           C  
ANISOU 1922  C   LYS A 256     2994   3301   2903     31   -104    -64       C  
ATOM   1923  O   LYS A 256      35.471 -17.442  -8.775  1.00 23.82           O  
ANISOU 1923  O   LYS A 256     2936   3247   2865     31   -104    -77       O  
ATOM   1924  CB  LYS A 256      37.420 -14.940  -7.879  1.00 24.41           C  
ANISOU 1924  CB  LYS A 256     3038   3327   2910     24   -103    -20       C  
ATOM   1925  CG  LYS A 256      38.669 -14.064  -8.007  1.00 27.88           C  
ANISOU 1925  CG  LYS A 256     3479   3778   3334     23   -105      0       C  
ATOM   1926  CD  LYS A 256      38.493 -12.670  -7.400  1.00 28.00           C  
ANISOU 1926  CD  LYS A 256     3504   3783   3351     17   -103     19       C  
ATOM   1927  CE  LYS A 256      39.261 -12.684  -6.062  1.00 32.11           C  
ANISOU 1927  CE  LYS A 256     4040   4282   3876      9   -101     26       C  
ATOM   1928  NZ  LYS A 256      38.993 -11.501  -5.200  1.00 29.81           N  
ANISOU 1928  NZ  LYS A 256     3760   3974   3588      1    -97     39       N  
ATOM   1929  N   VAL A 257      37.497 -18.123  -8.004  1.00 24.17           N  
ANISOU 1929  N   VAL A 257     2994   3284   2906     30   -100    -67       N  
ATOM   1930  CA  VAL A 257      36.971 -19.277  -7.300  1.00 24.35           C  
ANISOU 1930  CA  VAL A 257     3016   3280   2952     28    -92    -80       C  
ATOM   1931  C   VAL A 257      36.643 -18.973  -5.871  1.00 24.51           C  
ANISOU 1931  C   VAL A 257     3055   3274   2983     21    -83    -64       C  
ATOM   1932  O   VAL A 257      37.543 -18.618  -5.046  1.00 24.34           O  
ANISOU 1932  O   VAL A 257     3048   3247   2953     18    -82    -46       O  
ATOM   1933  CB  VAL A 257      37.926 -20.465  -7.401  1.00 24.30           C  
ANISOU 1933  CB  VAL A 257     3006   3273   2954     32    -91    -91       C  
ATOM   1934  CG1 VAL A 257      37.268 -21.622  -6.674  1.00 23.29           C  
ANISOU 1934  CG1 VAL A 257     2877   3115   2856     30    -82   -103       C  
ATOM   1935  CG2 VAL A 257      38.057 -20.775  -8.910  1.00 22.76           C  
ANISOU 1935  CG2 VAL A 257     2792   3106   2748     39    -99   -113       C  
ATOM   1936  N   LEU A 258      35.346 -19.075  -5.559  1.00 23.65           N  
ANISOU 1936  N   LEU A 258     2945   3148   2890     18    -77    -71       N  
ATOM   1937  CA  LEU A 258      34.854 -18.515  -4.299  1.00 24.24           C  
ANISOU 1937  CA  LEU A 258     3037   3202   2971     12    -66    -55       C  
ATOM   1938  C   LEU A 258      33.845 -19.517  -3.837  1.00 25.11           C  
ANISOU 1938  C   LEU A 258     3143   3288   3109     11    -55    -67       C  
ATOM   1939  O   LEU A 258      33.080 -20.002  -4.682  1.00 25.03           O  
ANISOU 1939  O   LEU A 258     3115   3282   3113     14    -58    -87       O  
ATOM   1940  CB  LEU A 258      34.161 -17.136  -4.514  1.00 23.53           C  
ANISOU 1940  CB  LEU A 258     2948   3119   2872     10    -68    -46       C  
ATOM   1941  CG  LEU A 258      35.083 -16.024  -5.002  1.00 24.45           C  
ANISOU 1941  CG  LEU A 258     3066   3257   2965     10    -78    -32       C  
ATOM   1942  CD1 LEU A 258      34.338 -14.788  -5.476  1.00 25.70           C  
ANISOU 1942  CD1 LEU A 258     3220   3423   3119     10    -81    -24       C  
ATOM   1943  CD2 LEU A 258      36.052 -15.640  -3.887  1.00 25.68           C  
ANISOU 1943  CD2 LEU A 258     3241   3402   3111      5    -75    -15       C  
ATOM   1944  N   ILE A 259      33.798 -19.808  -2.538  1.00 23.49           N  
ANISOU 1944  N   ILE A 259     2954   3059   2912      8    -41    -55       N  
ATOM   1945  CA  ILE A 259      32.777 -20.734  -2.089  1.00 24.90           C  
ANISOU 1945  CA  ILE A 259     3128   3213   3120      7    -27    -64       C  
ATOM   1946  C   ILE A 259      31.434 -20.081  -1.699  1.00 27.85           C  
ANISOU 1946  C   ILE A 259     3503   3574   3505      3    -16    -62       C  
ATOM   1947  O   ILE A 259      31.328 -19.375  -0.643  1.00 26.04           O  
ANISOU 1947  O   ILE A 259     3292   3333   3266      0     -6    -45       O  
ATOM   1948  CB  ILE A 259      33.260 -21.590  -0.926  1.00 25.82           C  
ANISOU 1948  CB  ILE A 259     3257   3308   3244      7    -15    -51       C  
ATOM   1949  CG1 ILE A 259      34.372 -22.503  -1.451  1.00 26.70           C  
ANISOU 1949  CG1 ILE A 259     3360   3428   3357     12    -24    -58       C  
ATOM   1950  CG2 ILE A 259      32.105 -22.416  -0.354  1.00 24.36           C  
ANISOU 1950  CG2 ILE A 259     3068   3095   3092      6      3    -56       C  
ATOM   1951  CD1 ILE A 259      35.271 -23.074  -0.390  1.00 27.87           C  
ANISOU 1951  CD1 ILE A 259     3523   3564   3503     14    -18    -40       C  
ATOM   1952  N   CYS A 260      30.392 -20.376  -2.506  1.00 26.48           N  
ANISOU 1952  N   CYS A 260     3308   3400   3352      4    -18    -81       N  
ATOM   1953  CA  CYS A 260      29.057 -19.771  -2.236  1.00 26.64           C  
ANISOU 1953  CA  CYS A 260     3327   3408   3388      1     -9    -81       C  
ATOM   1954  C   CYS A 260      27.998 -20.839  -2.001  1.00 26.06           C  
ANISOU 1954  C   CYS A 260     3240   3309   3353      0      5    -94       C  
ATOM   1955  O   CYS A 260      28.216 -21.981  -2.426  1.00 24.82           O  
ANISOU 1955  O   CYS A 260     3070   3149   3212      2      2   -109       O  
ATOM   1956  CB  CYS A 260      28.709 -18.949  -3.458  1.00 28.20           C  
ANISOU 1956  CB  CYS A 260     3508   3629   3575      3    -26    -89       C  
ATOM   1957  SG  CYS A 260      30.035 -17.684  -3.631  1.00 38.58           S  
ANISOU 1957  SG  CYS A 260     4838   4970   4848      4    -39    -69       S  
ATOM   1958  N   SER A 261      26.866 -20.485  -1.381  1.00 24.11           N  
ANISOU 1958  N   SER A 261     2993   3041   3123     -3     21    -89       N  
ATOM   1959  CA  SER A 261      25.731 -21.368  -1.405  1.00 24.85           C  
ANISOU 1959  CA  SER A 261     3069   3114   3259     -4     32   -104       C  
ATOM   1960  C   SER A 261      25.120 -21.303  -2.844  1.00 24.17           C  
ANISOU 1960  C   SER A 261     2955   3046   3183     -2     11   -129       C  
ATOM   1961  O   SER A 261      24.875 -20.236  -3.315  1.00 23.66           O  
ANISOU 1961  O   SER A 261     2888   2998   3102     -1      0   -126       O  
ATOM   1962  CB  SER A 261      24.726 -20.894  -0.408  1.00 25.23           C  
ANISOU 1962  CB  SER A 261     3125   3138   3322     -7     55    -91       C  
ATOM   1963  OG  SER A 261      23.731 -21.897  -0.340  1.00 26.91           O  
ANISOU 1963  OG  SER A 261     3319   3326   3579     -8     69   -104       O  
ATOM   1964  N   THR A 262      24.887 -22.422  -3.520  1.00 23.81           N  
ANISOU 1964  N   THR A 262     2886   2997   3162      0      5   -154       N  
ATOM   1965  CA  THR A 262      24.395 -22.412  -4.922  1.00 23.82           C  
ANISOU 1965  CA  THR A 262     2861   3020   3167      1    -17   -181       C  
ATOM   1966  C   THR A 262      23.461 -23.649  -5.144  1.00 24.10           C  
ANISOU 1966  C   THR A 262     2870   3034   3252      0    -12   -208       C  
ATOM   1967  O   THR A 262      23.470 -24.584  -4.344  1.00 24.89           O  
ANISOU 1967  O   THR A 262     2973   3103   3378     -2      7   -206       O  
ATOM   1968  CB  THR A 262      25.626 -22.318  -5.874  1.00 23.80           C  
ANISOU 1968  CB  THR A 262     2862   3054   3128      7    -39   -186       C  
ATOM   1969  OG1 THR A 262      25.298 -22.264  -7.292  1.00 23.92           O  
ANISOU 1969  OG1 THR A 262     2853   3096   3136     11    -63   -211       O  
ATOM   1970  CG2 THR A 262      26.491 -23.534  -5.663  1.00 25.47           C  
ANISOU 1970  CG2 THR A 262     3075   3255   3347      7    -33   -194       C  
ATOM   1971  N   LEU A 263      22.691 -23.684  -6.243  1.00 25.44           N  
ANISOU 1971  N   LEU A 263     3014   3218   3433      1    -31   -235       N  
ATOM   1972  CA  LEU A 263      21.734 -24.747  -6.470  1.00 25.83           C  
ANISOU 1972  CA  LEU A 263     3036   3246   3532     -1    -29   -264       C  
ATOM   1973  C   LEU A 263      22.508 -26.009  -6.870  1.00 27.18           C  
ANISOU 1973  C   LEU A 263     3199   3415   3711      0    -32   -286       C  
ATOM   1974  O   LEU A 263      23.252 -25.991  -7.872  1.00 29.33           O  
ANISOU 1974  O   LEU A 263     3469   3721   3954      5    -54   -301       O  
ATOM   1975  CB  LEU A 263      20.766 -24.381  -7.640  1.00 26.98           C  
ANISOU 1975  CB  LEU A 263     3153   3412   3683      0    -54   -288       C  
ATOM   1976  CG  LEU A 263      19.736 -25.493  -8.010  1.00 26.18           C  
ANISOU 1976  CG  LEU A 263     3019   3291   3636     -2    -56   -324       C  
ATOM   1977  CD1 LEU A 263      18.785 -25.708  -6.857  1.00 26.43           C  
ANISOU 1977  CD1 LEU A 263     3047   3278   3714     -9    -26   -311       C  
ATOM   1978  CD2 LEU A 263      18.888 -25.169  -9.229  1.00 27.90           C  
ANISOU 1978  CD2 LEU A 263     3209   3535   3855      0    -85   -351       C  
ATOM   1979  N   LEU A 264      22.269 -27.122  -6.189  1.00 28.01           N  
ANISOU 1979  N   LEU A 264     3298   3483   3860     -3    -11   -291       N  
ATOM   1980  CA  LEU A 264      22.903 -28.408  -6.573  1.00 27.87           C  
ANISOU 1980  CA  LEU A 264     3269   3460   3860     -2    -13   -315       C  
ATOM   1981  C   LEU A 264      21.942 -29.100  -7.464  1.00 28.66           C  
ANISOU 1981  C   LEU A 264     3333   3555   3998     -4    -26   -357       C  
ATOM   1982  O   LEU A 264      20.777 -29.242  -7.116  1.00 30.16           O  
ANISOU 1982  O   LEU A 264     3508   3719   4230     -9    -15   -361       O  
ATOM   1983  CB  LEU A 264      23.152 -29.281  -5.381  1.00 26.56           C  
ANISOU 1983  CB  LEU A 264     3112   3253   3724     -4     16   -296       C  
ATOM   1984  CG  LEU A 264      23.894 -28.552  -4.258  1.00 27.26           C  
ANISOU 1984  CG  LEU A 264     3236   3342   3777     -3     30   -252       C  
ATOM   1985  CD1 LEU A 264      24.049 -29.540  -3.133  1.00 26.63           C  
ANISOU 1985  CD1 LEU A 264     3163   3224   3730     -4     59   -235       C  
ATOM   1986  CD2 LEU A 264      25.265 -28.092  -4.750  1.00 26.69           C  
ANISOU 1986  CD2 LEU A 264     3180   3305   3654      1     12   -247       C  
ATOM   1987  N   GLU A 265      22.425 -29.482  -8.623  1.00 29.36           N  
ANISOU 1987  N   GLU A 265     3410   3671   4073      0    -49   -390       N  
ATOM   1988  CA  GLU A 265      21.634 -30.205  -9.552  1.00 33.72           C  
ANISOU 1988  CA  GLU A 265     3929   4224   4660     -2    -64   -436       C  
ATOM   1989  C   GLU A 265      22.319 -31.561  -9.643  1.00 34.18           C  
ANISOU 1989  C   GLU A 265     3977   4263   4743     -1    -57   -459       C  
ATOM   1990  O   GLU A 265      22.686 -32.005 -10.727  1.00 32.81           O  
ANISOU 1990  O   GLU A 265     3791   4114   4561      1    -77   -495       O  
ATOM   1991  CB  GLU A 265      21.607 -29.506 -10.918  1.00 34.64           C  
ANISOU 1991  CB  GLU A 265     4036   4390   4733      3    -99   -458       C  
ATOM   1992  CG  GLU A 265      21.078 -28.056 -10.897  1.00 38.27           C  
ANISOU 1992  CG  GLU A 265     4506   4872   5163      5   -108   -430       C  
ATOM   1993  CD  GLU A 265      21.310 -27.312 -12.236  1.00 40.68           C  
ANISOU 1993  CD  GLU A 265     4807   5231   5417     13   -141   -443       C  
ATOM   1994  OE1 GLU A 265      22.445 -26.870 -12.489  1.00 41.48           O  
ANISOU 1994  OE1 GLU A 265     4928   5359   5470     19   -145   -428       O  
ATOM   1995  OE2 GLU A 265      20.379 -27.187 -13.083  1.00 41.66           O  
ANISOU 1995  OE2 GLU A 265     4907   5372   5548     15   -163   -469       O  
ATOM   1996  N   GLY A 266      22.495 -32.215  -8.490  1.00 32.59           N  
ANISOU 1996  N   GLY A 266     3784   4020   4575     -5    -27   -436       N  
ATOM   1997  CA  GLY A 266      23.043 -33.585  -8.485  1.00 32.31           C  
ANISOU 1997  CA  GLY A 266     3737   3960   4576     -5    -16   -456       C  
ATOM   1998  C   GLY A 266      24.500 -33.726  -8.016  1.00 31.39           C  
ANISOU 1998  C   GLY A 266     3646   3846   4431      0     -6   -429       C  
ATOM   1999  O   GLY A 266      24.975 -34.855  -7.882  1.00 30.56           O  
ANISOU 1999  O   GLY A 266     3533   3716   4359      0      5   -440       O  
ATOM   2000  N   GLN A 267      25.218 -32.612  -7.821  1.00 30.08           N  
ANISOU 2000  N   GLN A 267     3510   3710   4208      4    -12   -397       N  
ATOM   2001  CA  GLN A 267      26.595 -32.673  -7.237  1.00 32.22           C  
ANISOU 2001  CA  GLN A 267     3805   3982   4453      8     -3   -367       C  
ATOM   2002  C   GLN A 267      26.505 -33.177  -5.820  1.00 31.12           C  
ANISOU 2002  C   GLN A 267     3676   3799   4346      6     27   -334       C  
ATOM   2003  O   GLN A 267      25.610 -32.808  -5.084  1.00 30.18           O  
ANISOU 2003  O   GLN A 267     3561   3663   4241      1     40   -316       O  
ATOM   2004  CB  GLN A 267      27.335 -31.292  -7.156  1.00 31.99           C  
ANISOU 2004  CB  GLN A 267     3805   3990   4359     11    -13   -336       C  
ATOM   2005  CG  GLN A 267      27.606 -30.603  -8.475  1.00 31.11           C  
ANISOU 2005  CG  GLN A 267     3689   3926   4206     16    -41   -358       C  
ATOM   2006  CD  GLN A 267      26.336 -29.974  -8.958  1.00 34.06           C  
ANISOU 2006  CD  GLN A 267     4049   4309   4581     13    -53   -371       C  
ATOM   2007  OE1 GLN A 267      25.282 -30.163  -8.322  1.00 34.66           O  
ANISOU 2007  OE1 GLN A 267     4117   4355   4696      7    -40   -368       O  
ATOM   2008  NE2 GLN A 267      26.398 -29.221 -10.068  1.00 32.19           N  
ANISOU 2008  NE2 GLN A 267     3809   4115   4305     17    -78   -384       N  
ATOM   2009  N   TYR A 268      27.467 -34.004  -5.446  1.00 32.18           N  
ANISOU 2009  N   TYR A 268     3815   3918   4491      9     38   -325       N  
ATOM   2010  CA  TYR A 268      27.539 -34.616  -4.115  1.00 32.53           C  
ANISOU 2010  CA  TYR A 268     3870   3924   4566      9     66   -291       C  
ATOM   2011  C   TYR A 268      26.349 -35.525  -3.874  1.00 33.51           C  
ANISOU 2011  C   TYR A 268     3968   4005   4756      4     85   -305       C  
ATOM   2012  O   TYR A 268      26.015 -35.828  -2.694  1.00 30.31           O  
ANISOU 2012  O   TYR A 268     3572   3567   4377      3    112   -273       O  
ATOM   2013  CB  TYR A 268      27.551 -33.550  -3.040  1.00 32.04           C  
ANISOU 2013  CB  TYR A 268     3839   3867   4468      9     75   -246       C  
ATOM   2014  CG  TYR A 268      28.710 -32.591  -3.168  1.00 32.71           C  
ANISOU 2014  CG  TYR A 268     3948   3989   4490     13     58   -229       C  
ATOM   2015  CD1 TYR A 268      30.026 -33.028  -3.042  1.00 32.38           C  
ANISOU 2015  CD1 TYR A 268     3915   3951   4436     19     57   -218       C  
ATOM   2016  CD2 TYR A 268      28.478 -31.256  -3.505  1.00 32.31           C  
ANISOU 2016  CD2 TYR A 268     3908   3971   4397     11     42   -226       C  
ATOM   2017  CE1 TYR A 268      31.086 -32.131  -3.172  1.00 33.41           C  
ANISOU 2017  CE1 TYR A 268     4065   4115   4514     22     41   -203       C  
ATOM   2018  CE2 TYR A 268      29.512 -30.360  -3.619  1.00 33.75           C  
ANISOU 2018  CE2 TYR A 268     4110   4185   4528     14     28   -210       C  
ATOM   2019  CZ  TYR A 268      30.803 -30.788  -3.438  1.00 34.35           C  
ANISOU 2019  CZ  TYR A 268     4194   4262   4592     19     28   -199       C  
ATOM   2020  OH  TYR A 268      31.789 -29.851  -3.576  1.00 35.00           O  
ANISOU 2020  OH  TYR A 268     4294   4376   4626     22     14   -184       O  
ATOM   2021  N   GLY A 269      25.675 -35.867  -4.984  1.00 31.72           N  
ANISOU 2021  N   GLY A 269     3713   3784   4555      1     70   -353       N  
ATOM   2022  CA  GLY A 269      24.494 -36.731  -4.939  1.00 32.50           C  
ANISOU 2022  CA  GLY A 269     3782   3844   4721     -4     84   -375       C  
ATOM   2023  C   GLY A 269      23.265 -35.981  -4.446  1.00 34.20           C  
ANISOU 2023  C   GLY A 269     3998   4052   4942    -10     92   -360       C  
ATOM   2024  O   GLY A 269      22.349 -36.612  -3.953  1.00 34.14           O  
ANISOU 2024  O   GLY A 269     3974   4005   4991    -15    113   -360       O  
ATOM   2025  N   HIS A 270      23.210 -34.646  -4.563  1.00 34.03           N  
ANISOU 2025  N   HIS A 270     3996   4066   4867     -9     76   -347       N  
ATOM   2026  CA  HIS A 270      22.027 -33.890  -4.086  1.00 33.65           C  
ANISOU 2026  CA  HIS A 270     3948   4010   4826    -14     85   -333       C  
ATOM   2027  C   HIS A 270      21.448 -32.969  -5.115  1.00 33.78           C  
ANISOU 2027  C   HIS A 270     3955   4062   4818    -15     56   -357       C  
ATOM   2028  O   HIS A 270      22.186 -32.363  -5.876  1.00 35.16           O  
ANISOU 2028  O   HIS A 270     4138   4276   4941    -10     31   -364       O  
ATOM   2029  CB  HIS A 270      22.404 -33.086  -2.905  1.00 33.39           C  
ANISOU 2029  CB  HIS A 270     3951   3978   4757    -12    102   -283       C  
ATOM   2030  CG  HIS A 270      22.748 -33.887  -1.687  1.00 33.76           C  
ANISOU 2030  CG  HIS A 270     4010   3989   4828    -10    134   -251       C  
ATOM   2031  ND1 HIS A 270      21.803 -34.467  -0.914  1.00 35.18           N  
ANISOU 2031  ND1 HIS A 270     4179   4127   5060    -14    164   -240       N  
ATOM   2032  CD2 HIS A 270      23.972 -34.065  -1.025  1.00 33.40           C  
ANISOU 2032  CD2 HIS A 270     3989   3944   4755     -4    141   -221       C  
ATOM   2033  CE1 HIS A 270      22.393 -35.015   0.193  1.00 35.69           C  
ANISOU 2033  CE1 HIS A 270     4262   4169   5130    -10    190   -203       C  
ATOM   2034  NE2 HIS A 270      23.729 -34.773   0.113  1.00 34.48           N  
ANISOU 2034  NE2 HIS A 270     4130   4043   4927     -4    174   -192       N  
ATOM   2035  N   SER A 271      20.126 -32.847  -5.136  1.00 33.96           N  
ANISOU 2035  N   SER A 271     3957   4069   4875    -20     59   -368       N  
ATOM   2036  CA  SER A 271      19.371 -32.055  -6.135  1.00 36.58           C  
ANISOU 2036  CA  SER A 271     4273   4432   5194    -21     31   -393       C  
ATOM   2037  C   SER A 271      18.326 -31.153  -5.466  1.00 35.25           C  
ANISOU 2037  C   SER A 271     4108   4253   5031    -24     44   -369       C  
ATOM   2038  O   SER A 271      17.924 -31.435  -4.352  1.00 33.88           O  
ANISOU 2038  O   SER A 271     3940   4042   4890    -27     76   -344       O  
ATOM   2039  CB  SER A 271      18.644 -32.990  -7.085  1.00 38.60           C  
ANISOU 2039  CB  SER A 271     4488   4678   5498    -25     16   -445       C  
ATOM   2040  OG  SER A 271      19.414 -33.116  -8.257  1.00 48.83           O  
ANISOU 2040  OG  SER A 271     5780   6011   6761    -20    -12   -476       O  
ATOM   2041  N   ASP A 272      17.925 -30.064  -6.130  1.00 35.30           N  
ANISOU 2041  N   ASP A 272     4113   4292   5007    -22     20   -374       N  
ATOM   2042  CA  ASP A 272      16.822 -29.182  -5.687  1.00 35.13           C  
ANISOU 2042  CA  ASP A 272     4088   4261   4995    -25     28   -357       C  
ATOM   2043  C   ASP A 272      16.943 -28.645  -4.245  1.00 32.27           C  
ANISOU 2043  C   ASP A 272     3757   3879   4623    -26     62   -310       C  
ATOM   2044  O   ASP A 272      15.940 -28.471  -3.533  1.00 28.18           O  
ANISOU 2044  O   ASP A 272     3234   3334   4139    -29     85   -297       O  
ATOM   2045  CB  ASP A 272      15.466 -29.896  -5.865  1.00 41.30           C  
ANISOU 2045  CB  ASP A 272     4830   5012   5847    -31     33   -385       C  
ATOM   2046  CG  ASP A 272      14.263 -28.965  -5.626  1.00 48.50           C  
ANISOU 2046  CG  ASP A 272     5733   5919   6772    -33     37   -373       C  
ATOM   2047  OD1 ASP A 272      14.354 -27.757  -5.977  1.00 49.57           O  
ANISOU 2047  OD1 ASP A 272     5883   6089   6863    -29     19   -361       O  
ATOM   2048  OD2 ASP A 272      13.211 -29.437  -5.084  1.00 57.74           O  
ANISOU 2048  OD2 ASP A 272     6883   7050   8002    -39     59   -375       O  
ATOM   2049  N   ILE A 273      18.193 -28.389  -3.852  1.00 29.10           N  
ANISOU 2049  N   ILE A 273     3388   3492   4174    -22     65   -286       N  
ATOM   2050  CA  ILE A 273      18.546 -27.826  -2.552  1.00 27.15           C  
ANISOU 2050  CA  ILE A 273     3175   3235   3906    -21     91   -244       C  
ATOM   2051  C   ILE A 273      19.812 -26.991  -2.894  1.00 27.14           C  
ANISOU 2051  C   ILE A 273     3200   3273   3838    -16     70   -232       C  
ATOM   2052  O   ILE A 273      20.555 -27.290  -3.870  1.00 26.16           O  
ANISOU 2052  O   ILE A 273     3068   3173   3695    -13     46   -253       O  
ATOM   2053  CB  ILE A 273      18.851 -28.920  -1.548  1.00 25.70           C  
ANISOU 2053  CB  ILE A 273     2999   3016   3750    -22    122   -228       C  
ATOM   2054  CG1 ILE A 273      18.809 -28.399  -0.088  1.00 26.71           C  
ANISOU 2054  CG1 ILE A 273     3157   3127   3864    -22    154   -186       C  
ATOM   2055  CG2 ILE A 273      20.239 -29.488  -1.860  1.00 25.06           C  
ANISOU 2055  CG2 ILE A 273     2929   2950   3643    -18    109   -232       C  
ATOM   2056  CD1 ILE A 273      17.445 -28.093   0.560  1.00 26.66           C  
ANISOU 2056  CD1 ILE A 273     3142   3094   3893    -26    180   -177       C  
ATOM   2057  N   PHE A 274      20.027 -25.923  -2.149  1.00 25.86           N  
ANISOU 2057  N   PHE A 274     3065   3118   3642    -15     80   -202       N  
ATOM   2058  CA  PHE A 274      21.209 -25.101  -2.382  1.00 24.89           C  
ANISOU 2058  CA  PHE A 274     2965   3028   3462    -11     62   -189       C  
ATOM   2059  C   PHE A 274      22.216 -25.530  -1.336  1.00 23.96           C  
ANISOU 2059  C   PHE A 274     2874   2898   3329    -10     80   -165       C  
ATOM   2060  O   PHE A 274      21.814 -25.805  -0.213  1.00 25.13           O  
ANISOU 2060  O   PHE A 274     3032   3018   3497    -12    109   -146       O  
ATOM   2061  CB  PHE A 274      20.899 -23.606  -2.111  1.00 24.58           C  
ANISOU 2061  CB  PHE A 274     2940   3001   3394    -12     62   -170       C  
ATOM   2062  CG  PHE A 274      20.442 -22.880  -3.302  1.00 24.92           C  
ANISOU 2062  CG  PHE A 274     2965   3072   3430    -10     35   -186       C  
ATOM   2063  CD1 PHE A 274      19.250 -23.258  -3.956  1.00 25.65           C  
ANISOU 2063  CD1 PHE A 274     3025   3157   3563    -11     28   -211       C  
ATOM   2064  CD2 PHE A 274      21.178 -21.807  -3.797  1.00 24.38           C  
ANISOU 2064  CD2 PHE A 274     2910   3037   3315     -6     16   -176       C  
ATOM   2065  CE1 PHE A 274      18.826 -22.580  -5.085  1.00 24.63           C  
ANISOU 2065  CE1 PHE A 274     2878   3055   3423     -8      0   -225       C  
ATOM   2066  CE2 PHE A 274      20.759 -21.146  -4.936  1.00 25.00           C  
ANISOU 2066  CE2 PHE A 274     2972   3142   3385     -3     -8   -188       C  
ATOM   2067  CZ  PHE A 274      19.569 -21.521  -5.564  1.00 24.78           C  
ANISOU 2067  CZ  PHE A 274     2913   3109   3394     -3    -16   -212       C  
ATOM   2068  N   GLY A 275      23.502 -25.543  -1.666  1.00 22.34           N  
ANISOU 2068  N   GLY A 275     2681   2716   3089     -7     65   -163       N  
ATOM   2069  CA  GLY A 275      24.509 -25.816  -0.627  1.00 23.27           C  
ANISOU 2069  CA  GLY A 275     2825   2825   3189     -5     79   -136       C  
ATOM   2070  C   GLY A 275      25.854 -25.202  -0.991  1.00 22.37           C  
ANISOU 2070  C   GLY A 275     2727   2744   3026     -2     58   -129       C  
ATOM   2071  O   GLY A 275      26.048 -24.830  -2.159  1.00 21.66           O  
ANISOU 2071  O   GLY A 275     2625   2681   2921      0     34   -147       O  
ATOM   2072  N   GLY A 276      26.754 -25.072  -0.002  1.00 22.18           N  
ANISOU 2072  N   GLY A 276     2730   2718   2978      0     67   -102       N  
ATOM   2073  CA  GLY A 276      28.060 -24.399  -0.238  1.00 24.15           C  
ANISOU 2073  CA  GLY A 276     2995   2997   3183      1     48    -93       C  
ATOM   2074  C   GLY A 276      29.045 -25.293  -0.954  1.00 24.91           C  
ANISOU 2074  C   GLY A 276     3081   3102   3280      5     35   -107       C  
ATOM   2075  O   GLY A 276      29.175 -26.514  -0.626  1.00 24.65           O  
ANISOU 2075  O   GLY A 276     3041   3047   3275      7     47   -108       O  
ATOM   2076  N   THR A 277      29.643 -24.711  -1.990  1.00 25.76           N  
ANISOU 2076  N   THR A 277     3184   3241   3362      7     13   -117       N  
ATOM   2077  CA  THR A 277      30.563 -25.394  -2.901  1.00 26.53           C  
ANISOU 2077  CA  THR A 277     3269   3353   3455     11      0   -134       C  
ATOM   2078  C   THR A 277      31.323 -24.301  -3.670  1.00 26.92           C  
ANISOU 2078  C   THR A 277     3324   3439   3464     13    -20   -132       C  
ATOM   2079  O   THR A 277      30.771 -23.246  -3.912  1.00 26.74           O  
ANISOU 2079  O   THR A 277     3303   3429   3427     11    -26   -129       O  
ATOM   2080  CB  THR A 277      29.888 -26.395  -3.853  1.00 27.59           C  
ANISOU 2080  CB  THR A 277     3375   3483   3625     12     -3   -169       C  
ATOM   2081  OG1 THR A 277      30.880 -27.209  -4.514  1.00 25.90           O  
ANISOU 2081  OG1 THR A 277     3152   3278   3411     17    -12   -184       O  
ATOM   2082  CG2 THR A 277      28.997 -25.727  -4.918  1.00 26.60           C  
ANISOU 2082  CG2 THR A 277     3233   3378   3494     12    -19   -190       C  
ATOM   2083  N   PRO A 278      32.616 -24.522  -3.977  1.00 25.96           N  
ANISOU 2083  N   PRO A 278     3205   3332   3325     17    -29   -130       N  
ATOM   2084  CA  PRO A 278      33.333 -23.498  -4.728  1.00 25.42           C  
ANISOU 2084  CA  PRO A 278     3139   3297   3220     19    -45   -126       C  
ATOM   2085  C   PRO A 278      32.662 -23.418  -6.116  1.00 24.47           C  
ANISOU 2085  C   PRO A 278     2997   3197   3099     22    -58   -153       C  
ATOM   2086  O   PRO A 278      32.133 -24.428  -6.614  1.00 22.74           O  
ANISOU 2086  O   PRO A 278     2760   2971   2906     23    -57   -180       O  
ATOM   2087  CB  PRO A 278      34.745 -24.062  -4.843  1.00 25.33           C  
ANISOU 2087  CB  PRO A 278     3130   3293   3200     23    -49   -124       C  
ATOM   2088  CG  PRO A 278      34.584 -25.604  -4.623  1.00 26.99           C  
ANISOU 2088  CG  PRO A 278     3328   3476   3447     25    -38   -138       C  
ATOM   2089  CD  PRO A 278      33.476 -25.670  -3.620  1.00 27.01           C  
ANISOU 2089  CD  PRO A 278     3337   3451   3472     21    -23   -129       C  
ATOM   2090  N   VAL A 279      32.565 -22.193  -6.626  1.00 23.96           N  
ANISOU 2090  N   VAL A 279     2936   3158   3009     22    -68   -145       N  
ATOM   2091  CA  VAL A 279      32.025 -21.945  -7.949  1.00 24.40           C  
ANISOU 2091  CA  VAL A 279     2974   3240   3057     26    -83   -165       C  
ATOM   2092  C   VAL A 279      32.960 -20.878  -8.511  1.00 26.89           C  
ANISOU 2092  C   VAL A 279     3297   3586   3334     30    -93   -149       C  
ATOM   2093  O   VAL A 279      33.731 -20.233  -7.743  1.00 28.42           O  
ANISOU 2093  O   VAL A 279     3508   3774   3515     27    -88   -123       O  
ATOM   2094  CB  VAL A 279      30.603 -21.359  -7.865  1.00 23.62           C  
ANISOU 2094  CB  VAL A 279     2870   3133   2971     23    -82   -165       C  
ATOM   2095  CG1 VAL A 279      29.619 -22.239  -7.075  1.00 22.21           C  
ANISOU 2095  CG1 VAL A 279     2686   2918   2833     18    -67   -175       C  
ATOM   2096  CG2 VAL A 279      30.632 -19.937  -7.264  1.00 23.42           C  
ANISOU 2096  CG2 VAL A 279     2861   3108   2926     20    -79   -135       C  
ATOM   2097  N   VAL A 280      32.931 -20.722  -9.826  1.00 26.40           N  
ANISOU 2097  N   VAL A 280     3220   3554   3254     36   -107   -163       N  
ATOM   2098  CA  VAL A 280      33.576 -19.649 -10.474  1.00 26.56           C  
ANISOU 2098  CA  VAL A 280     3244   3605   3242     40   -115   -147       C  
ATOM   2099  C   VAL A 280      32.569 -18.478 -10.706  1.00 27.26           C  
ANISOU 2099  C   VAL A 280     3330   3701   3324     40   -121   -135       C  
ATOM   2100  O   VAL A 280      31.505 -18.668 -11.347  1.00 28.63           O  
ANISOU 2100  O   VAL A 280     3488   3882   3506     42   -129   -153       O  
ATOM   2101  CB  VAL A 280      34.207 -20.186 -11.778  1.00 28.25           C  
ANISOU 2101  CB  VAL A 280     3444   3850   3437     48   -125   -167       C  
ATOM   2102  CG1 VAL A 280      34.663 -19.048 -12.703  1.00 26.93           C  
ANISOU 2102  CG1 VAL A 280     3277   3719   3234     55   -133   -151       C  
ATOM   2103  CG2 VAL A 280      35.405 -21.054 -11.378  1.00 27.44           C  
ANISOU 2103  CG2 VAL A 280     3347   3736   3340     48   -117   -170       C  
ATOM   2104  N   LEU A 281      32.888 -17.281 -10.209  1.00 25.89           N  
ANISOU 2104  N   LEU A 281     3171   3527   3139     37   -117   -105       N  
ATOM   2105  CA  LEU A 281      31.977 -16.080 -10.340  1.00 26.09           C  
ANISOU 2105  CA  LEU A 281     3194   3556   3163     37   -120    -90       C  
ATOM   2106  C   LEU A 281      32.431 -15.071 -11.352  1.00 25.83           C  
ANISOU 2106  C   LEU A 281     3156   3556   3100     44   -130    -74       C  
ATOM   2107  O   LEU A 281      33.413 -14.401 -11.148  1.00 25.10           O  
ANISOU 2107  O   LEU A 281     3074   3466   2994     43   -126    -53       O  
ATOM   2108  CB  LEU A 281      31.862 -15.305  -9.027  1.00 25.08           C  
ANISOU 2108  CB  LEU A 281     3083   3400   3045     29   -107    -68       C  
ATOM   2109  CG  LEU A 281      31.071 -15.667  -7.755  1.00 25.97           C  
ANISOU 2109  CG  LEU A 281     3204   3476   3186     21    -93    -70       C  
ATOM   2110  CD1 LEU A 281      30.582 -14.336  -7.225  1.00 25.47           C  
ANISOU 2110  CD1 LEU A 281     3149   3403   3124     18    -87    -49       C  
ATOM   2111  CD2 LEU A 281      29.813 -16.554  -7.907  1.00 26.94           C  
ANISOU 2111  CD2 LEU A 281     3311   3587   3335     22    -92    -94       C  
ATOM   2112  N   GLY A 282      31.693 -14.885 -12.442  1.00 28.64           N  
ANISOU 2112  N   GLY A 282     3496   3936   3447     51   -143    -82       N  
ATOM   2113  CA  GLY A 282      32.126 -13.898 -13.432  1.00 28.38           C  
ANISOU 2113  CA  GLY A 282     3459   3936   3385     60   -150    -62       C  
ATOM   2114  C   GLY A 282      30.953 -13.087 -13.955  1.00 30.55           C  
ANISOU 2114  C   GLY A 282     3723   4222   3662     64   -160    -53       C  
ATOM   2115  O   GLY A 282      29.893 -13.096 -13.298  1.00 27.29           O  
ANISOU 2115  O   GLY A 282     3308   3784   3276     59   -157    -58       O  
ATOM   2116  N   ALA A 283      31.142 -12.448 -15.146  1.00 28.12           N  
ANISOU 2116  N   ALA A 283     3407   3952   3326     75   -170    -41       N  
ATOM   2117  CA  ALA A 283      30.103 -11.654 -15.842  1.00 30.75           C  
ANISOU 2117  CA  ALA A 283     3726   4301   3655     83   -182    -29       C  
ATOM   2118  C   ALA A 283      28.785 -12.371 -16.036  1.00 31.79           C  
ANISOU 2118  C   ALA A 283     3842   4430   3804     84   -194    -58       C  
ATOM   2119  O   ALA A 283      27.723 -11.743 -16.063  1.00 33.42           O  
ANISOU 2119  O   ALA A 283     4039   4632   4025     85   -200    -48       O  
ATOM   2120  CB  ALA A 283      30.609 -11.087 -17.199  1.00 30.31           C  
ANISOU 2120  CB  ALA A 283     3663   4291   3560     96   -192    -13       C  
ATOM   2121  N   ASN A 284      28.860 -13.685 -16.156  1.00 33.33           N  
ANISOU 2121  N   ASN A 284     4034   4626   4003     82   -197    -93       N  
ATOM   2122  CA  ASN A 284      27.722 -14.545 -16.396  1.00 35.44           C  
ANISOU 2122  CA  ASN A 284     4284   4891   4290     82   -209   -126       C  
ATOM   2123  C   ASN A 284      27.122 -15.159 -15.156  1.00 35.67           C  
ANISOU 2123  C   ASN A 284     4316   4874   4361     70   -195   -139       C  
ATOM   2124  O   ASN A 284      26.367 -16.120 -15.270  1.00 41.64           O  
ANISOU 2124  O   ASN A 284     5058   5623   5138     69   -202   -170       O  
ATOM   2125  CB  ASN A 284      28.163 -15.705 -17.293  1.00 42.03           C  
ANISOU 2125  CB  ASN A 284     5110   5751   5106     88   -219   -161       C  
ATOM   2126  CG  ASN A 284      28.114 -15.353 -18.764  1.00 51.56           C  
ANISOU 2126  CG  ASN A 284     6306   7010   6274    102   -239   -162       C  
ATOM   2127  OD1 ASN A 284      28.940 -15.823 -19.567  1.00 64.42           O  
ANISOU 2127  OD1 ASN A 284     7934   8669   7873    109   -243   -175       O  
ATOM   2128  ND2 ASN A 284      27.144 -14.534 -19.136  1.00 49.70           N  
ANISOU 2128  ND2 ASN A 284     6058   6785   6037    107   -252   -147       N  
ATOM   2129  N   GLY A 285      27.502 -14.670 -13.983  1.00 31.48           N  
ANISOU 2129  N   GLY A 285     3804   4313   3843     62   -177   -116       N  
ATOM   2130  CA  GLY A 285      27.014 -15.188 -12.706  1.00 29.26           C  
ANISOU 2130  CA  GLY A 285     3529   3988   3599     51   -160   -123       C  
ATOM   2131  C   GLY A 285      27.886 -16.325 -12.281  1.00 27.88           C  
ANISOU 2131  C   GLY A 285     3363   3803   3427     47   -152   -139       C  
ATOM   2132  O   GLY A 285      29.115 -16.254 -12.355  1.00 25.73           O  
ANISOU 2132  O   GLY A 285     3102   3542   3132     49   -149   -129       O  
ATOM   2133  N   VAL A 286      27.236 -17.397 -11.856  1.00 26.71           N  
ANISOU 2133  N   VAL A 286     3207   3630   3310     43   -146   -163       N  
ATOM   2134  CA  VAL A 286      27.916 -18.595 -11.496  1.00 27.26           C  
ANISOU 2134  CA  VAL A 286     3281   3686   3389     39   -138   -180       C  
ATOM   2135  C   VAL A 286      28.289 -19.245 -12.796  1.00 27.65           C  
ANISOU 2135  C   VAL A 286     3316   3768   3419     47   -155   -207       C  
ATOM   2136  O   VAL A 286      27.427 -19.785 -13.432  1.00 28.87           O  
ANISOU 2136  O   VAL A 286     3451   3930   3587     49   -167   -234       O  
ATOM   2137  CB  VAL A 286      26.985 -19.524 -10.676  1.00 27.32           C  
ANISOU 2137  CB  VAL A 286     3283   3657   3441     32   -126   -197       C  
ATOM   2138  CG1 VAL A 286      27.574 -20.925 -10.571  1.00 26.00           C  
ANISOU 2138  CG1 VAL A 286     3113   3477   3286     31   -121   -219       C  
ATOM   2139  CG2 VAL A 286      26.784 -18.935  -9.288  1.00 26.27           C  
ANISOU 2139  CG2 VAL A 286     3168   3492   3321     25   -106   -170       C  
ATOM   2140  N   GLU A 287      29.566 -19.186 -13.211  1.00 28.24           N  
ANISOU 2140  N   GLU A 287     3399   3865   3464     52   -156   -200       N  
ATOM   2141  CA  GLU A 287      29.948 -19.742 -14.522  1.00 28.80           C  
ANISOU 2141  CA  GLU A 287     3457   3972   3512     60   -171   -226       C  
ATOM   2142  C   GLU A 287      30.277 -21.214 -14.383  1.00 27.93           C  
ANISOU 2142  C   GLU A 287     3342   3846   3425     58   -165   -257       C  
ATOM   2143  O   GLU A 287      30.207 -21.951 -15.343  1.00 26.57           O  
ANISOU 2143  O   GLU A 287     3154   3693   3247     63   -176   -290       O  
ATOM   2144  CB  GLU A 287      31.116 -18.977 -15.134  1.00 30.84           C  
ANISOU 2144  CB  GLU A 287     3724   4262   3729     67   -173   -204       C  
ATOM   2145  CG  GLU A 287      30.783 -17.498 -15.049  1.00 33.65           C  
ANISOU 2145  CG  GLU A 287     4087   4625   4073     68   -175   -169       C  
ATOM   2146  CD  GLU A 287      31.593 -16.623 -15.949  1.00 39.88           C  
ANISOU 2146  CD  GLU A 287     4878   5451   4822     77   -180   -148       C  
ATOM   2147  OE1 GLU A 287      32.727 -17.044 -16.322  1.00 44.61           O  
ANISOU 2147  OE1 GLU A 287     5480   6065   5403     80   -177   -153       O  
ATOM   2148  OE2 GLU A 287      31.113 -15.490 -16.252  1.00 41.11           O  
ANISOU 2148  OE2 GLU A 287     5032   5620   4967     81   -186   -125       O  
ATOM   2149  N   GLN A 288      30.622 -21.654 -13.183  1.00 25.57           N  
ANISOU 2149  N   GLN A 288     3054   3509   3149     51   -147   -247       N  
ATOM   2150  CA  GLN A 288      31.084 -23.034 -13.015  1.00 27.00           C  
ANISOU 2150  CA  GLN A 288     3231   3673   3353     49   -140   -272       C  
ATOM   2151  C   GLN A 288      30.756 -23.391 -11.603  1.00 27.25           C  
ANISOU 2151  C   GLN A 288     3272   3661   3421     41   -122   -259       C  
ATOM   2152  O   GLN A 288      30.832 -22.531 -10.743  1.00 25.27           O  
ANISOU 2152  O   GLN A 288     3038   3399   3164     37   -114   -227       O  
ATOM   2153  CB  GLN A 288      32.607 -23.118 -13.207  1.00 27.61           C  
ANISOU 2153  CB  GLN A 288     3317   3765   3405     54   -136   -263       C  
ATOM   2154  CG  GLN A 288      32.996 -22.822 -14.665  1.00 28.73           C  
ANISOU 2154  CG  GLN A 288     3450   3954   3509     64   -151   -276       C  
ATOM   2155  CD  GLN A 288      34.470 -23.085 -14.934  1.00 30.82           C  
ANISOU 2155  CD  GLN A 288     3721   4232   3755     68   -145   -273       C  
ATOM   2156  OE1 GLN A 288      34.942 -24.224 -14.811  1.00 28.80           O  
ANISOU 2156  OE1 GLN A 288     3460   3961   3519     68   -138   -294       O  
ATOM   2157  NE2 GLN A 288      35.215 -22.005 -15.337  1.00 30.08           N  
ANISOU 2157  NE2 GLN A 288     3637   4167   3625     73   -147   -246       N  
ATOM   2158  N   VAL A 289      30.293 -24.612 -11.400  1.00 26.71           N  
ANISOU 2158  N   VAL A 289     3190   3567   3389     38   -116   -285       N  
ATOM   2159  CA  VAL A 289      30.016 -25.100 -10.082  1.00 29.08           C  
ANISOU 2159  CA  VAL A 289     3499   3825   3725     31    -96   -272       C  
ATOM   2160  C   VAL A 289      31.052 -26.190 -10.012  1.00 30.32           C  
ANISOU 2160  C   VAL A 289     3656   3973   3892     33    -90   -282       C  
ATOM   2161  O   VAL A 289      31.052 -27.018 -10.911  1.00 29.93           O  
ANISOU 2161  O   VAL A 289     3587   3932   3850     37    -97   -317       O  
ATOM   2162  CB  VAL A 289      28.620 -25.734  -9.964  1.00 27.84           C  
ANISOU 2162  CB  VAL A 289     3322   3642   3610     27    -93   -294       C  
ATOM   2163  CG1 VAL A 289      28.431 -26.247  -8.572  1.00 27.10           C  
ANISOU 2163  CG1 VAL A 289     3238   3505   3550     21    -69   -277       C  
ATOM   2164  CG2 VAL A 289      27.537 -24.701 -10.291  1.00 30.14           C  
ANISOU 2164  CG2 VAL A 289     3608   3947   3894     26   -104   -290       C  
ATOM   2165  N   ILE A 290      31.970 -26.147  -9.026  1.00 28.24           N  
ANISOU 2165  N   ILE A 290     3411   3694   3623     32    -77   -253       N  
ATOM   2166  CA  ILE A 290      32.958 -27.168  -8.962  1.00 27.45           C  
ANISOU 2166  CA  ILE A 290     3309   3585   3534     35    -71   -261       C  
ATOM   2167  C   ILE A 290      32.587 -28.093  -7.795  1.00 28.85           C  
ANISOU 2167  C   ILE A 290     3488   3718   3755     31    -52   -254       C  
ATOM   2168  O   ILE A 290      32.319 -27.585  -6.708  1.00 29.83           O  
ANISOU 2168  O   ILE A 290     3628   3825   3878     27    -42   -225       O  
ATOM   2169  CB  ILE A 290      34.350 -26.571  -8.731  1.00 27.57           C  
ANISOU 2169  CB  ILE A 290     3341   3615   3516     38    -72   -234       C  
ATOM   2170  CG1 ILE A 290      34.479 -25.287  -9.501  1.00 27.75           C  
ANISOU 2170  CG1 ILE A 290     3369   3675   3498     40    -86   -226       C  
ATOM   2171  CG2 ILE A 290      35.411 -27.520  -9.309  1.00 27.03           C  
ANISOU 2171  CG2 ILE A 290     3264   3553   3452     44    -73   -252       C  
ATOM   2172  CD1 ILE A 290      35.866 -24.727  -9.482  1.00 28.76           C  
ANISOU 2172  CD1 ILE A 290     3509   3820   3596     43    -88   -204       C  
ATOM   2173  N   GLU A 291      32.524 -29.404  -8.045  1.00 27.91           N  
ANISOU 2173  N   GLU A 291     3351   3581   3672     32    -47   -281       N  
ATOM   2174  CA  GLU A 291      32.195 -30.435  -7.055  1.00 27.65           C  
ANISOU 2174  CA  GLU A 291     3315   3504   3685     29    -27   -275       C  
ATOM   2175  C   GLU A 291      33.495 -31.030  -6.596  1.00 27.04           C  
ANISOU 2175  C   GLU A 291     3246   3419   3609     34    -19   -260       C  
ATOM   2176  O   GLU A 291      34.203 -31.570  -7.441  1.00 25.89           O  
ANISOU 2176  O   GLU A 291     3088   3286   3463     39    -26   -283       O  
ATOM   2177  CB  GLU A 291      31.432 -31.555  -7.705  1.00 29.33           C  
ANISOU 2177  CB  GLU A 291     3500   3702   3942     28    -26   -316       C  
ATOM   2178  CG  GLU A 291      30.925 -32.533  -6.657  1.00 31.33           C  
ANISOU 2178  CG  GLU A 291     3748   3906   4247     25     -3   -307       C  
ATOM   2179  CD  GLU A 291      30.176 -33.750  -7.220  1.00 36.00           C  
ANISOU 2179  CD  GLU A 291     4309   4475   4892     23      0   -349       C  
ATOM   2180  OE1 GLU A 291      29.607 -33.721  -8.359  1.00 34.59           O  
ANISOU 2180  OE1 GLU A 291     4111   4317   4713     22    -16   -388       O  
ATOM   2181  OE2 GLU A 291      30.114 -34.758  -6.478  1.00 37.97           O  
ANISOU 2181  OE2 GLU A 291     4553   4685   5188     22     20   -342       O  
ATOM   2182  N   LEU A 292      33.845 -30.864  -5.303  1.00 24.92           N  
ANISOU 2182  N   LEU A 292     2997   3131   3338     33     -7   -221       N  
ATOM   2183  CA  LEU A 292      35.014 -31.501  -4.702  1.00 26.09           C  
ANISOU 2183  CA  LEU A 292     3152   3267   3492     37      0   -202       C  
ATOM   2184  C   LEU A 292      34.870 -33.040  -4.578  1.00 27.55           C  
ANISOU 2184  C   LEU A 292     3318   3416   3731     40     14   -217       C  
ATOM   2185  O   LEU A 292      33.834 -33.526  -4.143  1.00 27.83           O  
ANISOU 2185  O   LEU A 292     3347   3424   3803     36     27   -220       O  
ATOM   2186  CB  LEU A 292      35.231 -30.947  -3.320  1.00 26.25           C  
ANISOU 2186  CB  LEU A 292     3199   3278   3497     36      7   -159       C  
ATOM   2187  CG  LEU A 292      35.431 -29.427  -3.342  1.00 26.51           C  
ANISOU 2187  CG  LEU A 292     3250   3341   3480     33     -5   -143       C  
ATOM   2188  CD1 LEU A 292      35.746 -28.959  -1.934  1.00 25.68           C  
ANISOU 2188  CD1 LEU A 292     3170   3225   3359     32      2   -104       C  
ATOM   2189  CD2 LEU A 292      36.596 -29.098  -4.256  1.00 24.14           C  
ANISOU 2189  CD2 LEU A 292     2947   3072   3152     38    -21   -151       C  
ATOM   2190  N   GLN A 293      35.899 -33.796  -4.972  1.00 30.03           N  
ANISOU 2190  N   GLN A 293     3623   3730   4054     46     13   -227       N  
ATOM   2191  CA  GLN A 293      35.818 -35.294  -5.036  1.00 28.91           C  
ANISOU 2191  CA  GLN A 293     3459   3554   3969     48     26   -246       C  
ATOM   2192  C   GLN A 293      36.064 -35.829  -3.644  1.00 27.93           C  
ANISOU 2192  C   GLN A 293     3347   3397   3868     50     44   -206       C  
ATOM   2193  O   GLN A 293      37.177 -36.239  -3.304  1.00 29.16           O  
ANISOU 2193  O   GLN A 293     3506   3548   4024     57     46   -188       O  
ATOM   2194  CB  GLN A 293      36.834 -35.803  -6.041  1.00 29.12           C  
ANISOU 2194  CB  GLN A 293     3471   3596   3994     55     18   -273       C  
ATOM   2195  CG  GLN A 293      36.387 -35.485  -7.454  1.00 29.79           C  
ANISOU 2195  CG  GLN A 293     3542   3712   4063     53      3   -318       C  
ATOM   2196  CD  GLN A 293      37.468 -35.498  -8.532  1.00 30.81           C  
ANISOU 2196  CD  GLN A 293     3665   3872   4169     60     -7   -340       C  
ATOM   2197  OE1 GLN A 293      38.576 -36.027  -8.373  1.00 34.02           O  
ANISOU 2197  OE1 GLN A 293     4070   4271   4583     66     -1   -331       O  
ATOM   2198  NE2 GLN A 293      37.141 -34.907  -9.653  1.00 31.71           N  
ANISOU 2198  NE2 GLN A 293     3774   4022   4253     60    -22   -368       N  
ATOM   2199  N   LEU A 294      35.035 -35.712  -2.810  1.00 27.37           N  
ANISOU 2199  N   LEU A 294     3283   3306   3811     46     57   -189       N  
ATOM   2200  CA  LEU A 294      35.101 -36.023  -1.356  1.00 28.00           C  
ANISOU 2200  CA  LEU A 294     3378   3356   3902     48     76   -145       C  
ATOM   2201  C   LEU A 294      35.305 -37.510  -1.094  1.00 29.21           C  
ANISOU 2201  C   LEU A 294     3513   3471   4112     53     94   -144       C  
ATOM   2202  O   LEU A 294      34.886 -38.320  -1.885  1.00 27.52           O  
ANISOU 2202  O   LEU A 294     3272   3242   3939     52     97   -181       O  
ATOM   2203  CB  LEU A 294      33.770 -35.635  -0.646  1.00 27.87           C  
ANISOU 2203  CB  LEU A 294     3370   3326   3894     41     90   -132       C  
ATOM   2204  CG  LEU A 294      33.469 -34.124  -0.747  1.00 28.34           C  
ANISOU 2204  CG  LEU A 294     3447   3418   3900     36     76   -128       C  
ATOM   2205  CD1 LEU A 294      32.343 -33.685   0.196  1.00 27.68           C  
ANISOU 2205  CD1 LEU A 294     3376   3320   3820     32     92   -108       C  
ATOM   2206  CD2 LEU A 294      34.750 -33.295  -0.583  1.00 26.02           C  
ANISOU 2206  CD2 LEU A 294     3175   3155   3555     40     60   -107       C  
ATOM   2207  N   ASN A 295      35.873 -37.857   0.065  1.00 31.14           N  
ANISOU 2207  N   ASN A 295     3771   3697   4360     59    106   -101       N  
ATOM   2208  CA  ASN A 295      35.916 -39.238   0.435  1.00 30.98           C  
ANISOU 2208  CA  ASN A 295     3735   3637   4398     64    126    -94       C  
ATOM   2209  C   ASN A 295      34.640 -39.575   1.175  1.00 32.29           C  
ANISOU 2209  C   ASN A 295     3898   3770   4598     60    150    -81       C  
ATOM   2210  O   ASN A 295      33.791 -38.697   1.398  1.00 30.10           O  
ANISOU 2210  O   ASN A 295     3634   3504   4297     54    150    -78       O  
ATOM   2211  CB  ASN A 295      37.177 -39.545   1.229  1.00 32.80           C  
ANISOU 2211  CB  ASN A 295     3978   3865   4620     74    127    -55       C  
ATOM   2212  CG  ASN A 295      37.229 -38.786   2.524  1.00 32.43           C  
ANISOU 2212  CG  ASN A 295     3963   3826   4532     76    129     -6       C  
ATOM   2213  OD1 ASN A 295      36.216 -38.587   3.178  1.00 31.96           O  
ANISOU 2213  OD1 ASN A 295     3912   3755   4476     72    144      6       O  
ATOM   2214  ND2 ASN A 295      38.410 -38.355   2.894  1.00 33.14           N  
ANISOU 2214  ND2 ASN A 295     4069   3938   4584     81    114     17       N  
ATOM   2215  N   SER A 296      34.483 -40.858   1.548  1.00 32.30           N  
ANISOU 2215  N   SER A 296     3882   3729   4660     64    173    -74       N  
ATOM   2216  CA  SER A 296      33.296 -41.249   2.288  1.00 32.48           C  
ANISOU 2216  CA  SER A 296     3901   3717   4721     61    199    -58       C  
ATOM   2217  C   SER A 296      32.983 -40.461   3.600  1.00 31.34           C  
ANISOU 2217  C   SER A 296     3790   3580   4538     62    210     -9       C  
ATOM   2218  O   SER A 296      31.848 -40.107   3.811  1.00 30.33           O  
ANISOU 2218  O   SER A 296     3663   3444   4416     55    221    -12       O  
ATOM   2219  CB  SER A 296      33.278 -42.804   2.473  1.00 34.67           C  
ANISOU 2219  CB  SER A 296     4153   3944   5074     66    223    -55       C  
ATOM   2220  OG  SER A 296      32.546 -43.172   3.622  1.00 34.22           O  
ANISOU 2220  OG  SER A 296     4102   3855   5044     68    253    -16       O  
ATOM   2221  N   GLU A 297      33.936 -40.183   4.487  1.00 33.20           N  
ANISOU 2221  N   GLU A 297     4051   3828   4735     70    206     32       N  
ATOM   2222  CA  GLU A 297      33.578 -39.526   5.741  1.00 34.68           C  
ANISOU 2222  CA  GLU A 297     4268   4020   4888     71    218     74       C  
ATOM   2223  C   GLU A 297      33.265 -38.035   5.445  1.00 34.96           C  
ANISOU 2223  C   GLU A 297     4322   4094   4867     62    199     59       C  
ATOM   2224  O   GLU A 297      32.532 -37.424   6.205  1.00 32.23           O  
ANISOU 2224  O   GLU A 297     3994   3749   4501     60    212     78       O  
ATOM   2225  CB  GLU A 297      34.708 -39.505   6.774  1.00 39.70           C  
ANISOU 2225  CB  GLU A 297     4929   4666   5490     82    215    122       C  
ATOM   2226  CG  GLU A 297      35.485 -40.767   7.099  1.00 50.53           C  
ANISOU 2226  CG  GLU A 297     6287   6009   6900     93    225    146       C  
ATOM   2227  CD  GLU A 297      36.491 -40.556   8.269  1.00 61.36           C  
ANISOU 2227  CD  GLU A 297     7687   7397   8229    104    219    197       C  
ATOM   2228  OE1 GLU A 297      36.067 -40.079   9.354  1.00 70.66           O  
ANISOU 2228  OE1 GLU A 297     8891   8580   9376    105    231    231       O  
ATOM   2229  OE2 GLU A 297      37.715 -40.840   8.134  1.00 64.09           O  
ANISOU 2229  OE2 GLU A 297     8029   7751   8569    112    203    205       O  
ATOM   2230  N   GLU A 298      33.834 -37.478   4.355  1.00 32.70           N  
ANISOU 2230  N   GLU A 298     4030   3838   4556     59    171     26       N  
ATOM   2231  CA  GLU A 298      33.561 -36.115   3.909  1.00 34.43           C  
ANISOU 2231  CA  GLU A 298     4261   4092   4727     52    153      9       C  
ATOM   2232  C   GLU A 298      32.125 -36.043   3.313  1.00 33.34           C  
ANISOU 2232  C   GLU A 298     4105   3942   4618     43    161    -21       C  
ATOM   2233  O   GLU A 298      31.333 -35.117   3.586  1.00 31.34           O  
ANISOU 2233  O   GLU A 298     3864   3698   4342     37    163    -18       O  
ATOM   2234  CB  GLU A 298      34.641 -35.624   2.895  1.00 33.93           C  
ANISOU 2234  CB  GLU A 298     4195   4063   4632     52    123    -12       C  
ATOM   2235  CG  GLU A 298      36.084 -35.481   3.466  1.00 32.61           C  
ANISOU 2235  CG  GLU A 298     4045   3911   4431     60    111     17       C  
ATOM   2236  CD  GLU A 298      37.203 -35.449   2.403  1.00 34.26           C  
ANISOU 2236  CD  GLU A 298     4243   4142   4629     62     89     -5       C  
ATOM   2237  OE1 GLU A 298      36.934 -35.582   1.179  1.00 34.71           O  
ANISOU 2237  OE1 GLU A 298     4279   4206   4701     59     82    -46       O  
ATOM   2238  OE2 GLU A 298      38.414 -35.292   2.772  1.00 37.70           O  
ANISOU 2238  OE2 GLU A 298     4690   4592   5041     68     77     16       O  
ATOM   2239  N   LYS A 299      31.767 -37.024   2.521  1.00 34.13           N  
ANISOU 2239  N   LYS A 299     4175   4021   4770     42    165    -53       N  
ATOM   2240  CA  LYS A 299      30.382 -37.117   2.051  1.00 36.37           C  
ANISOU 2240  CA  LYS A 299     4438   4289   5090     34    174    -82       C  
ATOM   2241  C   LYS A 299      29.389 -37.150   3.240  1.00 33.97           C  
ANISOU 2241  C   LYS A 299     4143   3958   4803     32    204    -50       C  
ATOM   2242  O   LYS A 299      28.412 -36.419   3.263  1.00 33.85           O  
ANISOU 2242  O   LYS A 299     4132   3948   4782     26    206    -56       O  
ATOM   2243  CB  LYS A 299      30.199 -38.387   1.243  1.00 40.27           C  
ANISOU 2243  CB  LYS A 299     4896   4756   5646     34    178   -117       C  
ATOM   2244  CG  LYS A 299      29.744 -38.207  -0.193  1.00 45.02           C  
ANISOU 2244  CG  LYS A 299     5475   5377   6253     27    157   -171       C  
ATOM   2245  CD  LYS A 299      30.652 -39.056  -1.103  1.00 50.29           C  
ANISOU 2245  CD  LYS A 299     6123   6045   6939     32    145   -201       C  
ATOM   2246  CE  LYS A 299      29.874 -39.601  -2.292  1.00 53.49           C  
ANISOU 2246  CE  LYS A 299     6494   6443   7384     26    138   -257       C  
ATOM   2247  NZ  LYS A 299      28.940 -38.572  -2.862  1.00 58.52           N  
ANISOU 2247  NZ  LYS A 299     7131   7107   7995     19    122   -278       N  
ATOM   2248  N   ALA A 300      29.685 -37.968   4.243  1.00 34.36           N  
ANISOU 2248  N   ALA A 300     4199   3980   4875     39    226    -14       N  
ATOM   2249  CA  ALA A 300      28.797 -38.133   5.413  1.00 32.74           C  
ANISOU 2249  CA  ALA A 300     4003   3747   4689     39    259     19       C  
ATOM   2250  C   ALA A 300      28.529 -36.750   6.073  1.00 32.56           C  
ANISOU 2250  C   ALA A 300     4012   3752   4607     37    257     39       C  
ATOM   2251  O   ALA A 300      27.386 -36.380   6.349  1.00 31.87           O  
ANISOU 2251  O   ALA A 300     3924   3654   4529     32    273     39       O  
ATOM   2252  CB  ALA A 300      29.366 -39.128   6.411  1.00 31.54           C  
ANISOU 2252  CB  ALA A 300     3856   3568   4557     50    281     61       C  
ATOM   2253  N   LYS A 301      29.578 -35.980   6.283  1.00 31.19           N  
ANISOU 2253  N   LYS A 301     3864   3611   4373     41    237     53       N  
ATOM   2254  CA  LYS A 301      29.411 -34.631   6.822  1.00 31.30           C  
ANISOU 2254  CA  LYS A 301     3906   3652   4332     38    232     67       C  
ATOM   2255  C   LYS A 301      28.634 -33.676   5.898  1.00 29.17           C  
ANISOU 2255  C   LYS A 301     3627   3400   4054     29    217     31       C  
ATOM   2256  O   LYS A 301      27.790 -32.898   6.349  1.00 29.04           O  
ANISOU 2256  O   LYS A 301     3622   3385   4025     25    228     37       O  
ATOM   2257  CB  LYS A 301      30.770 -34.043   7.124  1.00 32.82           C  
ANISOU 2257  CB  LYS A 301     4124   3876   4469     43    210     85       C  
ATOM   2258  CG  LYS A 301      31.585 -34.817   8.120  1.00 36.88           C  
ANISOU 2258  CG  LYS A 301     4650   4378   4982     54    220    124       C  
ATOM   2259  CD  LYS A 301      30.970 -34.725   9.506  1.00 40.15           C  
ANISOU 2259  CD  LYS A 301     5087   4780   5386     57    249    162       C  
ATOM   2260  CE  LYS A 301      32.144 -34.637  10.479  1.00 47.29           C  
ANISOU 2260  CE  LYS A 301     6019   5702   6247     66    241    200       C  
ATOM   2261  NZ  LYS A 301      31.936 -35.425  11.727  1.00 48.36           N  
ANISOU 2261  NZ  LYS A 301     6165   5813   6394     76    272    244       N  
ATOM   2262  N   PHE A 302      28.930 -33.731   4.601  1.00 28.95           N  
ANISOU 2262  N   PHE A 302     3579   3386   4032     26    193     -5       N  
ATOM   2263  CA  PHE A 302      28.201 -32.961   3.640  1.00 27.50           C  
ANISOU 2263  CA  PHE A 302     3383   3220   3845     19    178    -38       C  
ATOM   2264  C   PHE A 302      26.697 -33.290   3.742  1.00 28.31           C  
ANISOU 2264  C   PHE A 302     3467   3291   3995     14    200    -47       C  
ATOM   2265  O   PHE A 302      25.844 -32.400   3.807  1.00 28.82           O  
ANISOU 2265  O   PHE A 302     3537   3364   4050      9    203    -50       O  
ATOM   2266  CB  PHE A 302      28.793 -33.189   2.237  1.00 28.32           C  
ANISOU 2266  CB  PHE A 302     3466   3342   3951     19    150    -75       C  
ATOM   2267  CG  PHE A 302      28.296 -32.202   1.196  1.00 29.02           C  
ANISOU 2267  CG  PHE A 302     3547   3459   4020     13    129   -105       C  
ATOM   2268  CD1 PHE A 302      27.000 -32.304   0.666  1.00 29.52           C  
ANISOU 2268  CD1 PHE A 302     3587   3510   4119      8    133   -131       C  
ATOM   2269  CD2 PHE A 302      29.090 -31.095   0.819  1.00 28.12           C  
ANISOU 2269  CD2 PHE A 302     3449   3383   3851     14    105   -103       C  
ATOM   2270  CE1 PHE A 302      26.536 -31.347  -0.243  1.00 28.88           C  
ANISOU 2270  CE1 PHE A 302     3500   3456   4017      4    112   -154       C  
ATOM   2271  CE2 PHE A 302      28.634 -30.154  -0.087  1.00 28.24           C  
ANISOU 2271  CE2 PHE A 302     3458   3423   3847     10     87   -125       C  
ATOM   2272  CZ  PHE A 302      27.340 -30.278  -0.599  1.00 29.82           C  
ANISOU 2272  CZ  PHE A 302     3635   3612   4080      6     90   -149       C  
ATOM   2273  N   ASP A 303      26.365 -34.569   3.739  1.00 28.79           N  
ANISOU 2273  N   ASP A 303     3505   3318   4114     14    218    -53       N  
ATOM   2274  CA  ASP A 303      25.003 -35.038   3.906  1.00 28.83           C  
ANISOU 2274  CA  ASP A 303     3490   3289   4173     10    242    -60       C  
ATOM   2275  C   ASP A 303      24.314 -34.548   5.139  1.00 28.12           C  
ANISOU 2275  C   ASP A 303     3420   3187   4074     10    270    -25       C  
ATOM   2276  O   ASP A 303      23.140 -34.261   5.092  1.00 27.23           O  
ANISOU 2276  O   ASP A 303     3296   3063   3984      4    282    -35       O  
ATOM   2277  CB  ASP A 303      24.940 -36.599   3.895  1.00 29.69           C  
ANISOU 2277  CB  ASP A 303     3573   3358   4349     11    261    -64       C  
ATOM   2278  CG  ASP A 303      25.325 -37.210   2.528  1.00 31.70           C  
ANISOU 2278  CG  ASP A 303     3799   3619   4627     10    236   -111       C  
ATOM   2279  OD1 ASP A 303      25.527 -36.467   1.515  1.00 33.37           O  
ANISOU 2279  OD1 ASP A 303     4008   3865   4804      8    205   -140       O  
ATOM   2280  OD2 ASP A 303      25.449 -38.473   2.435  1.00 34.52           O  
ANISOU 2280  OD2 ASP A 303     4134   3943   5036     12    248   -118       O  
ATOM   2281  N   GLU A 304      24.982 -34.487   6.272  1.00 29.63           N  
ANISOU 2281  N   GLU A 304     3642   3381   4235     16    284     16       N  
ATOM   2282  CA  GLU A 304      24.306 -33.977   7.431  1.00 30.21           C  
ANISOU 2282  CA  GLU A 304     3737   3446   4295     17    311     46       C  
ATOM   2283  C   GLU A 304      24.088 -32.447   7.327  1.00 30.19           C  
ANISOU 2283  C   GLU A 304     3752   3476   4242     12    296     39       C  
ATOM   2284  O   GLU A 304      23.123 -31.923   7.922  1.00 29.57           O  
ANISOU 2284  O   GLU A 304     3679   3388   4165     10    317     48       O  
ATOM   2285  CB  GLU A 304      25.126 -34.222   8.661  1.00 35.92           C  
ANISOU 2285  CB  GLU A 304     4489   4169   4989     26    326     92       C  
ATOM   2286  CG  GLU A 304      25.493 -35.652   8.901  1.00 40.52           C  
ANISOU 2286  CG  GLU A 304     5059   4722   5616     32    342    107       C  
ATOM   2287  CD  GLU A 304      26.672 -35.721   9.854  1.00 46.61           C  
ANISOU 2287  CD  GLU A 304     5859   5505   6343     43    341    148       C  
ATOM   2288  OE1 GLU A 304      26.500 -35.291  11.009  1.00 47.63           O  
ANISOU 2288  OE1 GLU A 304     6016   5638   6441     47    360    182       O  
ATOM   2289  OE2 GLU A 304      27.780 -36.181   9.449  1.00 55.03           O  
ANISOU 2289  OE2 GLU A 304     6922   6580   7406     47    320    145       O  
ATOM   2290  N   ALA A 305      24.936 -31.726   6.575  1.00 27.79           N  
ANISOU 2290  N   ALA A 305     3454   3207   3896     12    261     22       N  
ATOM   2291  CA  ALA A 305      24.661 -30.298   6.450  1.00 27.60           C  
ANISOU 2291  CA  ALA A 305     3444   3209   3832      7    248     15       C  
ATOM   2292  C   ALA A 305      23.446 -30.199   5.537  1.00 29.32           C  
ANISOU 2292  C   ALA A 305     3631   3419   4089      1    246    -16       C  
ATOM   2293  O   ALA A 305      22.502 -29.461   5.873  1.00 28.93           O  
ANISOU 2293  O   ALA A 305     3585   3365   4039     -2    259    -13       O  
ATOM   2294  CB  ALA A 305      25.853 -29.506   5.880  1.00 26.83           C  
ANISOU 2294  CB  ALA A 305     3359   3150   3683      8    213      8       C  
ATOM   2295  N   ILE A 306      23.408 -30.959   4.431  1.00 26.73           N  
ANISOU 2295  N   ILE A 306     3273   3086   3796      0    231    -47       N  
ATOM   2296  CA  ILE A 306      22.224 -30.844   3.556  1.00 26.79           C  
ANISOU 2296  CA  ILE A 306     3251   3088   3840     -6    225    -80       C  
ATOM   2297  C   ILE A 306      20.892 -31.175   4.254  1.00 28.75           C  
ANISOU 2297  C   ILE A 306     3487   3299   4136    -10    260    -71       C  
ATOM   2298  O   ILE A 306      19.978 -30.362   4.265  1.00 30.67           O  
ANISOU 2298  O   ILE A 306     3728   3545   4380    -13    264    -75       O  
ATOM   2299  CB  ILE A 306      22.357 -31.600   2.242  1.00 25.35           C  
ANISOU 2299  CB  ILE A 306     3037   2908   3686     -8    202   -119       C  
ATOM   2300  CG1 ILE A 306      23.553 -31.096   1.437  1.00 24.72           C  
ANISOU 2300  CG1 ILE A 306     2966   2868   3556     -5    168   -130       C  
ATOM   2301  CG2 ILE A 306      21.035 -31.517   1.479  1.00 26.09           C  
ANISOU 2301  CG2 ILE A 306     3099   2995   3819    -14    197   -151       C  
ATOM   2302  CD1 ILE A 306      23.557 -29.603   1.194  1.00 23.88           C  
ANISOU 2302  CD1 ILE A 306     2875   2795   3400     -6    150   -127       C  
ATOM   2303  N   ALA A 307      20.819 -32.314   4.923  1.00 29.78           N  
ANISOU 2303  N   ALA A 307     3612   3396   4305     -7    287    -55       N  
ATOM   2304  CA  ALA A 307      19.655 -32.667   5.734  1.00 31.11           C  
ANISOU 2304  CA  ALA A 307     3773   3528   4518     -9    326    -39       C  
ATOM   2305  C   ALA A 307      19.213 -31.545   6.660  1.00 31.50           C  
ANISOU 2305  C   ALA A 307     3849   3585   4532     -9    343    -14       C  
ATOM   2306  O   ALA A 307      18.033 -31.353   6.907  1.00 31.44           O  
ANISOU 2306  O   ALA A 307     3830   3558   4556    -13    365    -15       O  
ATOM   2307  CB  ALA A 307      19.938 -33.912   6.561  1.00 30.80           C  
ANISOU 2307  CB  ALA A 307     3734   3455   4510     -4    355    -12       C  
ATOM   2308  N   GLU A 308      20.151 -30.785   7.177  1.00 31.70           N  
ANISOU 2308  N   GLU A 308     3910   3638   4495     -4    334      6       N  
ATOM   2309  CA  GLU A 308      19.743 -29.776   8.131  1.00 32.91           C  
ANISOU 2309  CA  GLU A 308     4090   3797   4616     -4    354     28       C  
ATOM   2310  C   GLU A 308      19.128 -28.599   7.364  1.00 31.22           C  
ANISOU 2310  C   GLU A 308     3866   3602   4392    -10    334      3       C  
ATOM   2311  O   GLU A 308      18.079 -28.061   7.721  1.00 32.42           O  
ANISOU 2311  O   GLU A 308     4016   3742   4559    -12    354      5       O  
ATOM   2312  CB  GLU A 308      20.895 -29.368   9.048  1.00 32.12           C  
ANISOU 2312  CB  GLU A 308     4030   3719   4455      1    352     58       C  
ATOM   2313  CG  GLU A 308      20.570 -28.112   9.841  1.00 34.03           C  
ANISOU 2313  CG  GLU A 308     4299   3974   4656      1    364     72       C  
ATOM   2314  CD  GLU A 308      19.514 -28.377  10.925  1.00 37.12           C  
ANISOU 2314  CD  GLU A 308     4694   4335   5073      3    411     94       C  
ATOM   2315  OE1 GLU A 308      19.053 -29.547  11.111  1.00 35.93           O  
ANISOU 2315  OE1 GLU A 308     4525   4152   4972      4    435    103       O  
ATOM   2316  OE2 GLU A 308      19.136 -27.401  11.615  1.00 37.21           O  
ANISOU 2316  OE2 GLU A 308     4727   4354   5056      3    425    103       O  
ATOM   2317  N   THR A 309      19.751 -28.218   6.265  1.00 31.35           N  
ANISOU 2317  N   THR A 309     3876   3646   4387    -11    295    -20       N  
ATOM   2318  CA  THR A 309      19.102 -27.297   5.336  1.00 31.73           C  
ANISOU 2318  CA  THR A 309     3907   3710   4436    -15    274    -46       C  
ATOM   2319  C   THR A 309      17.642 -27.706   4.998  1.00 30.90           C  
ANISOU 2319  C   THR A 309     3767   3577   4395    -20    288    -64       C  
ATOM   2320  O   THR A 309      16.733 -26.873   4.982  1.00 31.10           O  
ANISOU 2320  O   THR A 309     3788   3603   4427    -23    293    -68       O  
ATOM   2321  CB  THR A 309      19.972 -27.052   4.090  1.00 32.29           C  
ANISOU 2321  CB  THR A 309     3972   3814   4481    -15    232    -69       C  
ATOM   2322  OG1 THR A 309      21.169 -26.413   4.533  1.00 34.30           O  
ANISOU 2322  OG1 THR A 309     4260   4094   4678    -12    222    -50       O  
ATOM   2323  CG2 THR A 309      19.314 -26.125   3.094  1.00 31.03           C  
ANISOU 2323  CG2 THR A 309     3795   3673   4321    -18    209    -92       C  
ATOM   2324  N   LYS A 310      17.465 -28.978   4.714  1.00 31.04           N  
ANISOU 2324  N   LYS A 310     3761   3571   4461    -21    294    -76       N  
ATOM   2325  CA  LYS A 310      16.184 -29.575   4.458  1.00 32.87           C  
ANISOU 2325  CA  LYS A 310     3957   3772   4759    -26    308    -93       C  
ATOM   2326  C   LYS A 310      15.253 -29.572   5.674  1.00 31.72           C  
ANISOU 2326  C   LYS A 310     3818   3595   4640    -26    354    -66       C  
ATOM   2327  O   LYS A 310      14.075 -29.263   5.518  1.00 33.42           O  
ANISOU 2327  O   LYS A 310     4011   3796   4889    -30    363    -77       O  
ATOM   2328  CB  LYS A 310      16.387 -31.004   3.971  1.00 36.11           C  
ANISOU 2328  CB  LYS A 310     4341   4162   5215    -27    306   -111       C  
ATOM   2329  CG  LYS A 310      16.711 -31.064   2.495  1.00 37.65           C  
ANISOU 2329  CG  LYS A 310     4514   4382   5406    -28    262   -151       C  
ATOM   2330  CD  LYS A 310      16.959 -32.498   2.059  1.00 36.98           C  
ANISOU 2330  CD  LYS A 310     4405   4276   5368    -29    261   -171       C  
ATOM   2331  CE  LYS A 310      17.321 -32.514   0.581  1.00 40.40           C  
ANISOU 2331  CE  LYS A 310     4819   4739   5791    -30    219   -214       C  
ATOM   2332  NZ  LYS A 310      17.683 -33.898   0.147  1.00 46.08           N  
ANISOU 2332  NZ  LYS A 310     5516   5439   6552    -30    217   -236       N  
ATOM   2333  N   ARG A 311      15.742 -29.875   6.887  1.00 30.44           N  
ANISOU 2333  N   ARG A 311     3683   3421   4459    -21    383    -30       N  
ATOM   2334  CA  ARG A 311      14.848 -29.822   8.009  1.00 28.26           C  
ANISOU 2334  CA  ARG A 311     3415   3119   4203    -21    428     -4       C  
ATOM   2335  C   ARG A 311      14.268 -28.397   8.089  1.00 28.03           C  
ANISOU 2335  C   ARG A 311     3395   3106   4147    -22    426     -7       C  
ATOM   2336  O   ARG A 311      13.088 -28.220   8.361  1.00 28.49           O  
ANISOU 2336  O   ARG A 311     3439   3143   4243    -25    451     -6       O  
ATOM   2337  CB  ARG A 311      15.607 -30.155   9.294  1.00 29.55           C  
ANISOU 2337  CB  ARG A 311     3614   3279   4335    -13    455     36       C  
ATOM   2338  CG  ARG A 311      14.683 -30.623  10.444  1.00 29.74           C  
ANISOU 2338  CG  ARG A 311     3638   3266   4394    -11    508     64       C  
ATOM   2339  CD  ARG A 311      15.402 -30.610  11.806  1.00 29.78           C  
ANISOU 2339  CD  ARG A 311     3687   3278   4351     -2    533    107       C  
ATOM   2340  NE  ARG A 311      16.142 -29.344  12.002  1.00 29.88           N  
ANISOU 2340  NE  ARG A 311     3734   3330   4288     -1    512    110       N  
ATOM   2341  CZ  ARG A 311      15.640 -28.208  12.504  1.00 31.20           C  
ANISOU 2341  CZ  ARG A 311     3919   3507   4428     -1    524    113       C  
ATOM   2342  NH1 ARG A 311      14.361 -28.092  12.879  1.00 30.54           N  
ANISOU 2342  NH1 ARG A 311     3821   3398   4382     -3    559    116       N  
ATOM   2343  NH2 ARG A 311      16.425 -27.142  12.624  1.00 31.55           N  
ANISOU 2343  NH2 ARG A 311     3993   3586   4408      0    501    113       N  
ATOM   2344  N   MET A 312      15.078 -27.355   7.907  1.00 27.58           N  
ANISOU 2344  N   MET A 312     3363   3085   4028    -21    399     -7       N  
ATOM   2345  CA  MET A 312      14.555 -25.985   8.075  1.00 26.76           C  
ANISOU 2345  CA  MET A 312     3270   2994   3901    -22    401     -7       C  
ATOM   2346  C   MET A 312      13.731 -25.510   6.875  1.00 27.40           C  
ANISOU 2346  C   MET A 312     3317   3081   4012    -26    376    -39       C  
ATOM   2347  O   MET A 312      12.701 -24.886   7.059  1.00 28.14           O  
ANISOU 2347  O   MET A 312     3401   3163   4126    -28    392    -39       O  
ATOM   2348  CB  MET A 312      15.662 -25.017   8.425  1.00 28.09           C  
ANISOU 2348  CB  MET A 312     3477   3196   3998    -18    386      4       C  
ATOM   2349  CG  MET A 312      16.324 -25.379   9.774  1.00 30.53           C  
ANISOU 2349  CG  MET A 312     3821   3500   4276    -13    413     38       C  
ATOM   2350  SD  MET A 312      17.674 -24.225  10.101  1.00 33.39           S  
ANISOU 2350  SD  MET A 312     4226   3904   4557    -10    389     47       S  
ATOM   2351  CE  MET A 312      18.776 -24.653   8.696  1.00 30.51           C  
ANISOU 2351  CE  MET A 312     3844   3562   4185    -11    339     25       C  
ATOM   2352  N   LYS A 313      14.127 -25.835   5.660  1.00 26.58           N  
ANISOU 2352  N   LYS A 313     3192   2993   3913    -28    338    -65       N  
ATOM   2353  CA  LYS A 313      13.321 -25.484   4.499  1.00 27.38           C  
ANISOU 2353  CA  LYS A 313     3259   3100   4042    -31    313    -94       C  
ATOM   2354  C   LYS A 313      11.833 -25.885   4.688  1.00 29.36           C  
ANISOU 2354  C   LYS A 313     3478   3315   4361    -35    340   -100       C  
ATOM   2355  O   LYS A 313      10.986 -25.025   4.626  1.00 28.93           O  
ANISOU 2355  O   LYS A 313     3415   3260   4316    -36    343   -103       O  
ATOM   2356  CB  LYS A 313      13.932 -26.145   3.282  1.00 27.59           C  
ANISOU 2356  CB  LYS A 313     3267   3144   4070    -32    275   -122       C  
ATOM   2357  CG  LYS A 313      13.344 -25.767   1.949  1.00 28.55           C  
ANISOU 2357  CG  LYS A 313     3357   3283   4207    -34    240   -154       C  
ATOM   2358  CD  LYS A 313      13.889 -26.819   1.025  1.00 28.64           C  
ANISOU 2358  CD  LYS A 313     3349   3300   4230    -34    216   -180       C  
ATOM   2359  CE  LYS A 313      13.582 -26.508  -0.404  1.00 30.65           C  
ANISOU 2359  CE  LYS A 313     3576   3581   4486    -34    175   -214       C  
ATOM   2360  NZ  LYS A 313      14.158 -27.629  -1.194  1.00 29.62           N  
ANISOU 2360  NZ  LYS A 313     3429   3455   4367    -35    155   -241       N  
ATOM   2361  N   ALA A 314      11.548 -27.178   4.903  1.00 31.08           N  
ANISOU 2361  N   ALA A 314     3678   3500   4628    -37    360   -102       N  
ATOM   2362  CA  ALA A 314      10.251 -27.700   5.298  1.00 33.81           C  
ANISOU 2362  CA  ALA A 314     3996   3806   5042    -41    394   -102       C  
ATOM   2363  C   ALA A 314       9.486 -26.875   6.355  1.00 36.98           C  
ANISOU 2363  C   ALA A 314     4413   4194   5442    -40    432    -77       C  
ATOM   2364  O   ALA A 314       8.286 -26.924   6.367  1.00 40.13           O  
ANISOU 2364  O   ALA A 314     4784   4568   5895    -43    450    -83       O  
ATOM   2365  CB  ALA A 314      10.406 -29.127   5.807  1.00 33.31           C  
ANISOU 2365  CB  ALA A 314     3928   3711   5017    -41    420    -92       C  
ATOM   2366  N   LEU A 315      10.164 -26.121   7.222  1.00 38.88           N  
ANISOU 2366  N   LEU A 315     4697   4452   5624    -35    444    -50       N  
ATOM   2367  CA  LEU A 315       9.482 -25.333   8.270  1.00 42.09           C  
ANISOU 2367  CA  LEU A 315     5120   4846   6025    -33    482    -29       C  
ATOM   2368  C   LEU A 315       9.230 -23.879   7.888  1.00 43.98           C  
ANISOU 2368  C   LEU A 315     5363   5109   6239    -33    463    -38       C  
ATOM   2369  O   LEU A 315       8.766 -23.081   8.710  1.00 44.02           O  
ANISOU 2369  O   LEU A 315     5384   5107   6233    -31    492    -23       O  
ATOM   2370  CB  LEU A 315      10.285 -25.329   9.566  1.00 39.59           C  
ANISOU 2370  CB  LEU A 315     4848   4533   5659    -28    511      4       C  
ATOM   2371  CG  LEU A 315      10.416 -26.635  10.353  1.00 41.20           C  
ANISOU 2371  CG  LEU A 315     5056   4710   5886    -25    544     26       C  
ATOM   2372  CD1 LEU A 315      11.468 -26.379  11.395  1.00 38.30           C  
ANISOU 2372  CD1 LEU A 315     4738   4362   5453    -19    555     55       C  
ATOM   2373  CD2 LEU A 315       9.101 -27.062  10.994  1.00 41.75           C  
ANISOU 2373  CD2 LEU A 315     5106   4739   6018    -27    593     37       C  
ATOM   2374  N   ALA A 316       9.576 -23.511   6.661  1.00 45.72           N  
ANISOU 2374  N   ALA A 316     5569   5355   6445    -34    416    -62       N  
ATOM   2375  CA  ALA A 316       9.520 -22.099   6.273  1.00 49.43           C  
ANISOU 2375  CA  ALA A 316     6045   5850   6886    -33    396    -66       C  
ATOM   2376  C   ALA A 316       8.132 -21.893   5.733  1.00 52.25           C  
ANISOU 2376  C   ALA A 316     6362   6190   7300    -36    396    -82       C  
ATOM   2377  O   ALA A 316       7.608 -20.760   5.695  1.00 55.15           O  
ANISOU 2377  O   ALA A 316     6727   6562   7664    -34    396    -81       O  
ATOM   2378  CB  ALA A 316      10.572 -21.760   5.219  1.00 43.85           C  
ANISOU 2378  CB  ALA A 316     5343   5182   6135    -32    346    -80       C  
ATOM   2379  OXT ALA A 316       7.537 -22.910   5.353  1.00 52.74           O  
ANISOU 2379  OXT ALA A 316     6391   6231   7416    -39    398    -97       O  
TER    2380      ALA A 316                                                      
ATOM   2381  N   PRO B   3      59.710  -1.533  12.293  1.00 62.17           N  
ANISOU 2381  N   PRO B   3     8213   7907   7499    131   -210    125       N  
ATOM   2382  CA  PRO B   3      58.835  -2.573  11.704  1.00 61.59           C  
ANISOU 2382  CA  PRO B   3     8161   7821   7417    139   -186    119       C  
ATOM   2383  C   PRO B   3      57.676  -1.915  10.922  1.00 60.38           C  
ANISOU 2383  C   PRO B   3     8021   7663   7255    133   -176     89       C  
ATOM   2384  O   PRO B   3      57.882  -0.825  10.347  1.00 64.89           O  
ANISOU 2384  O   PRO B   3     8583   8234   7838    131   -179     82       O  
ATOM   2385  CB  PRO B   3      58.326  -3.355  12.934  1.00 59.55           C  
ANISOU 2385  CB  PRO B   3     7915   7573   7138    132   -193    121       C  
ATOM   2386  CG  PRO B   3      59.080  -2.818  14.125  1.00 59.86           C  
ANISOU 2386  CG  PRO B   3     7939   7630   7173    123   -221    131       C  
ATOM   2387  CD  PRO B   3      60.167  -1.893  13.646  1.00 61.13           C  
ANISOU 2387  CD  PRO B   3     8077   7791   7358    125   -231    140       C  
ATOM   2388  N   LYS B   4      56.492  -2.545  10.891  1.00 48.05           N  
ANISOU 2388  N   LYS B   4     6480   6096   5678    130   -166     75       N  
ATOM   2389  CA  LYS B   4      55.282  -1.908  10.333  1.00 41.79           C  
ANISOU 2389  CA  LYS B   4     5699   5301   4878    122   -161     48       C  
ATOM   2390  C   LYS B   4      54.792  -0.833  11.282  1.00 38.46           C  
ANISOU 2390  C   LYS B   4     5274   4893   4445    106   -178     32       C  
ATOM   2391  O   LYS B   4      55.019  -0.953  12.461  1.00 37.36           O  
ANISOU 2391  O   LYS B   4     5133   4765   4296     99   -191     38       O  
ATOM   2392  CB  LYS B   4      54.194  -2.934  10.253  1.00 42.46           C  
ANISOU 2392  CB  LYS B   4     5803   5376   4951    122   -148     40       C  
ATOM   2393  CG  LYS B   4      53.446  -2.958   8.929  1.00 38.15           C  
ANISOU 2393  CG  LYS B   4     5269   4816   4407    126   -134     25       C  
ATOM   2394  CD  LYS B   4      52.525  -4.169   8.947  1.00 42.13           C  
ANISOU 2394  CD  LYS B   4     5791   5310   4904    125   -124     21       C  
ATOM   2395  CE  LYS B   4      53.168  -5.351   9.668  1.00 41.04           C  
ANISOU 2395  CE  LYS B   4     5653   5171   4767    132   -120     42       C  
ATOM   2396  NZ  LYS B   4      52.821  -6.673   9.076  1.00 43.13           N  
ANISOU 2396  NZ  LYS B   4     5934   5418   5035    140   -102     44       N  
ATOM   2397  N   ALA B   5      54.146   0.223  10.795  1.00 35.83           N  
ANISOU 2397  N   ALA B   5     4940   4558   4113     99   -178     13       N  
ATOM   2398  CA  ALA B   5      53.565   1.260  11.680  1.00 33.41           C  
ANISOU 2398  CA  ALA B   5     4633   4262   3797     83   -190     -4       C  
ATOM   2399  C   ALA B   5      52.503   0.713  12.674  1.00 30.68           C  
ANISOU 2399  C   ALA B   5     4304   3921   3430     74   -189    -13       C  
ATOM   2400  O   ALA B   5      51.689  -0.099  12.266  1.00 30.93           O  
ANISOU 2400  O   ALA B   5     4347   3943   3459     77   -176    -15       O  
ATOM   2401  CB  ALA B   5      52.963   2.370  10.823  1.00 33.47           C  
ANISOU 2401  CB  ALA B   5     4638   4265   3813     79   -186    -21       C  
ATOM   2402  N   LYS B   6      52.586   1.062  13.976  1.00 28.61           N  
ANISOU 2402  N   LYS B   6     4043   3672   3155     64   -202    -15       N  
ATOM   2403  CA  LYS B   6      51.547   0.741  14.969  1.00 26.28           C  
ANISOU 2403  CA  LYS B   6     3764   3381   2839     56   -199    -24       C  
ATOM   2404  C   LYS B   6      50.614   1.948  15.091  1.00 27.14           C  
ANISOU 2404  C   LYS B   6     3875   3489   2945     44   -197    -48       C  
ATOM   2405  O   LYS B   6      51.066   3.103  15.280  1.00 27.19           O  
ANISOU 2405  O   LYS B   6     3873   3502   2955     37   -209    -57       O  
ATOM   2406  CB  LYS B   6      52.181   0.537  16.340  1.00 28.24           C  
ANISOU 2406  CB  LYS B   6     4014   3644   3070     52   -214    -14       C  
ATOM   2407  CG  LYS B   6      51.275  -0.133  17.342  1.00 27.64           C  
ANISOU 2407  CG  LYS B   6     3957   3572   2973     48   -206    -15       C  
ATOM   2408  CD  LYS B   6      51.914  -0.205  18.690  1.00 28.99           C  
ANISOU 2408  CD  LYS B   6     4132   3760   3123     44   -223     -6       C  
ATOM   2409  CE  LYS B   6      50.958  -0.831  19.682  1.00 29.72           C  
ANISOU 2409  CE  LYS B   6     4243   3855   3192     42   -213     -6       C  
ATOM   2410  NZ  LYS B   6      51.634  -0.853  20.991  1.00 32.20           N  
ANISOU 2410  NZ  LYS B   6     4564   4188   3483     38   -231      3       N  
ATOM   2411  N   ILE B   7      49.321   1.700  14.951  1.00 26.38           N  
ANISOU 2411  N   ILE B   7     3789   3386   2847     42   -182    -59       N  
ATOM   2412  CA  ILE B   7      48.313   2.732  14.982  1.00 24.92           C  
ANISOU 2412  CA  ILE B   7     3606   3199   2663     32   -177    -79       C  
ATOM   2413  C   ILE B   7      47.390   2.420  16.159  1.00 24.82           C  
ANISOU 2413  C   ILE B   7     3608   3189   2632     26   -169    -84       C  
ATOM   2414  O   ILE B   7      46.881   1.290  16.317  1.00 25.52           O  
ANISOU 2414  O   ILE B   7     3706   3274   2717     30   -159    -75       O  
ATOM   2415  CB  ILE B   7      47.464   2.694  13.702  1.00 24.35           C  
ANISOU 2415  CB  ILE B   7     3530   3112   2607     35   -165    -85       C  
ATOM   2416  CG1 ILE B   7      48.380   3.021  12.525  1.00 24.59           C  
ANISOU 2416  CG1 ILE B   7     3548   3139   2653     43   -170    -79       C  
ATOM   2417  CG2 ILE B   7      46.320   3.701  13.830  1.00 24.49           C  
ANISOU 2417  CG2 ILE B   7     3548   3126   2628     26   -158   -103       C  
ATOM   2418  CD1 ILE B   7      47.766   2.879  11.140  1.00 23.17           C  
ANISOU 2418  CD1 ILE B   7     3368   2948   2486     48   -161    -81       C  
ATOM   2419  N   VAL B   8      47.124   3.382  16.984  1.00 22.51           N  
ANISOU 2419  N   VAL B   8     3320   2902   2329     16   -171    -98       N  
ATOM   2420  CA  VAL B   8      46.339   3.008  18.145  1.00 22.64           C  
ANISOU 2420  CA  VAL B   8     3353   2921   2326     12   -161   -101       C  
ATOM   2421  C   VAL B   8      45.113   3.841  18.121  1.00 22.05           C  
ANISOU 2421  C   VAL B   8     3281   2838   2259      5   -146   -119       C  
ATOM   2422  O   VAL B   8      45.202   5.107  17.946  1.00 21.22           O  
ANISOU 2422  O   VAL B   8     3169   2732   2161      0   -150   -133       O  
ATOM   2423  CB  VAL B   8      47.112   3.266  19.498  1.00 22.28           C  
ANISOU 2423  CB  VAL B   8     3318   2892   2255      7   -176   -100       C  
ATOM   2424  CG1 VAL B   8      46.212   2.947  20.661  1.00 21.65           C  
ANISOU 2424  CG1 VAL B   8     3258   2815   2153      4   -162   -103       C  
ATOM   2425  CG2 VAL B   8      48.301   2.326  19.544  1.00 22.08           C  
ANISOU 2425  CG2 VAL B   8     3288   2875   2226     14   -191    -78       C  
ATOM   2426  N   LEU B   9      43.974   3.170  18.228  1.00 22.19           N  
ANISOU 2426  N   LEU B   9     3305   2848   2278      6   -128   -116       N  
ATOM   2427  CA  LEU B   9      42.747   3.936  18.167  1.00 23.90           C  
ANISOU 2427  CA  LEU B   9     3521   3054   2505      0   -112   -130       C  
ATOM   2428  C   LEU B   9      42.298   4.110  19.607  1.00 23.74           C  
ANISOU 2428  C   LEU B   9     3517   3038   2461     -3   -101   -136       C  
ATOM   2429  O   LEU B   9      41.897   3.153  20.251  1.00 23.73           O  
ANISOU 2429  O   LEU B   9     3527   3038   2449      0    -91   -126       O  
ATOM   2430  CB  LEU B   9      41.700   3.230  17.355  1.00 23.91           C  
ANISOU 2430  CB  LEU B   9     3517   3042   2526      3   -100   -125       C  
ATOM   2431  CG  LEU B   9      42.166   2.994  15.907  1.00 26.52           C  
ANISOU 2431  CG  LEU B   9     3834   3367   2873      8   -111   -120       C  
ATOM   2432  CD1 LEU B   9      41.213   2.092  15.144  1.00 26.99           C  
ANISOU 2432  CD1 LEU B   9     3891   3413   2949     10   -103   -114       C  
ATOM   2433  CD2 LEU B   9      42.289   4.303  15.133  1.00 25.54           C  
ANISOU 2433  CD2 LEU B   9     3696   3241   2763      5   -116   -131       C  
ATOM   2434  N   VAL B  10      42.321   5.331  20.096  1.00 24.65           N  
ANISOU 2434  N   VAL B  10     3637   3156   2571    -10   -101   -153       N  
ATOM   2435  CA  VAL B  10      41.902   5.511  21.507  1.00 26.44           C  
ANISOU 2435  CA  VAL B  10     3884   3387   2772    -14    -89   -160       C  
ATOM   2436  C   VAL B  10      40.404   5.846  21.506  1.00 25.68           C  
ANISOU 2436  C   VAL B  10     3789   3276   2692    -16    -60   -167       C  
ATOM   2437  O   VAL B  10      40.008   7.017  21.362  1.00 24.26           O  
ANISOU 2437  O   VAL B  10     3605   3089   2524    -21    -53   -183       O  
ATOM   2438  CB  VAL B  10      42.752   6.554  22.243  1.00 27.30           C  
ANISOU 2438  CB  VAL B  10     4003   3507   2862    -22   -103   -175       C  
ATOM   2439  CG1 VAL B  10      42.211   6.752  23.651  1.00 28.50           C  
ANISOU 2439  CG1 VAL B  10     4181   3662   2985    -26    -88   -185       C  
ATOM   2440  CG2 VAL B  10      44.213   6.073  22.278  1.00 27.24           C  
ANISOU 2440  CG2 VAL B  10     3993   3514   2842    -20   -132   -163       C  
ATOM   2441  N   GLY B  11      39.589   4.798  21.635  1.00 24.41           N  
ANISOU 2441  N   GLY B  11     3631   3109   2534    -11    -44   -154       N  
ATOM   2442  CA  GLY B  11      38.140   4.931  21.412  1.00 27.46           C  
ANISOU 2442  CA  GLY B  11     4011   3478   2943    -11    -19   -155       C  
ATOM   2443  C   GLY B  11      37.734   3.993  20.269  1.00 28.29           C  
ANISOU 2443  C   GLY B  11     4099   3573   3074     -8    -22   -141       C  
ATOM   2444  O   GLY B  11      38.247   4.099  19.127  1.00 30.27           O  
ANISOU 2444  O   GLY B  11     4336   3825   3340     -7    -40   -141       O  
ATOM   2445  N   SER B  12      36.882   3.016  20.587  1.00 27.41           N  
ANISOU 2445  N   SER B  12     3991   3454   2968     -5     -5   -129       N  
ATOM   2446  CA  SER B  12      36.495   1.998  19.594  1.00 27.92           C  
ANISOU 2446  CA  SER B  12     4041   3508   3056     -2     -9   -116       C  
ATOM   2447  C   SER B  12      34.977   1.906  19.424  1.00 26.30           C  
ANISOU 2447  C   SER B  12     3826   3284   2879     -5     11   -113       C  
ATOM   2448  O   SER B  12      34.415   0.788  19.499  1.00 26.44           O  
ANISOU 2448  O   SER B  12     3844   3295   2907     -3     19    -99       O  
ATOM   2449  CB  SER B  12      36.966   0.616  20.015  1.00 30.03           C  
ANISOU 2449  CB  SER B  12     4318   3780   3309      3    -12   -100       C  
ATOM   2450  OG  SER B  12      38.195   0.723  20.715  1.00 35.41           O  
ANISOU 2450  OG  SER B  12     5013   4480   3959      5    -25   -101       O  
ATOM   2451  N   GLY B  13      34.334   3.059  19.275  1.00 23.39           N  
ANISOU 2451  N   GLY B  13     3450   2909   2526     -9     20   -123       N  
ATOM   2452  CA  GLY B  13      32.921   3.140  19.021  1.00 24.00           C  
ANISOU 2452  CA  GLY B  13     3514   2970   2636    -12     38   -119       C  
ATOM   2453  C   GLY B  13      32.882   3.029  17.525  1.00 23.60           C  
ANISOU 2453  C   GLY B  13     3443   2913   2608    -15     17   -118       C  
ATOM   2454  O   GLY B  13      33.864   2.577  16.966  1.00 24.35           O  
ANISOU 2454  O   GLY B  13     3541   3017   2692    -12     -3   -117       O  
ATOM   2455  N   MET B  14      31.815   3.473  16.891  1.00 23.89           N  
ANISOU 2455  N   MET B  14     3462   2936   2677    -19     23   -116       N  
ATOM   2456  CA  MET B  14      31.638   3.341  15.436  1.00 26.33           C  
ANISOU 2456  CA  MET B  14     3754   3239   3008    -22      2   -114       C  
ATOM   2457  C   MET B  14      32.753   3.865  14.555  1.00 27.05           C  
ANISOU 2457  C   MET B  14     3844   3342   3088    -21    -20   -123       C  
ATOM   2458  O   MET B  14      33.231   3.110  13.692  1.00 31.37           O  
ANISOU 2458  O   MET B  14     4392   3891   3633    -19    -39   -119       O  
ATOM   2459  CB  MET B  14      30.261   3.880  14.963  1.00 28.26           C  
ANISOU 2459  CB  MET B  14     3977   3468   3290    -28     11   -110       C  
ATOM   2460  CG  MET B  14      29.044   3.048  15.426  1.00 29.93           C  
ANISOU 2460  CG  MET B  14     4183   3664   3525    -30     29    -97       C  
ATOM   2461  SD  MET B  14      29.273   1.267  15.129  1.00 40.85           S  
ANISOU 2461  SD  MET B  14     5573   5044   4904    -30     15    -87       S  
ATOM   2462  CE  MET B  14      29.367   1.126  13.270  1.00 37.48           C  
ANISOU 2462  CE  MET B  14     5133   4615   4492    -35    -20    -90       C  
ATOM   2463  N   ILE B  15      33.087   5.153  14.703  1.00 25.46           N  
ANISOU 2463  N   ILE B  15     3642   3147   2884    -21    -17   -133       N  
ATOM   2464  CA  ILE B  15      34.167   5.823  13.982  1.00 26.23           C  
ANISOU 2464  CA  ILE B  15     3737   3254   2972    -19    -36   -140       C  
ATOM   2465  C   ILE B  15      35.470   5.016  14.047  1.00 26.15           C  
ANISOU 2465  C   ILE B  15     3741   3257   2935    -14    -51   -139       C  
ATOM   2466  O   ILE B  15      36.126   4.830  13.014  1.00 24.12           O  
ANISOU 2466  O   ILE B  15     3481   3004   2679    -11    -69   -137       O  
ATOM   2467  CB  ILE B  15      34.453   7.253  14.520  1.00 25.28           C  
ANISOU 2467  CB  ILE B  15     3618   3139   2849    -20    -27   -152       C  
ATOM   2468  CG1 ILE B  15      33.160   8.047  14.463  1.00 27.79           C  
ANISOU 2468  CG1 ILE B  15     3920   3441   3195    -24     -9   -152       C  
ATOM   2469  CG2 ILE B  15      35.650   7.909  13.782  1.00 25.78           C  
ANISOU 2469  CG2 ILE B  15     3677   3211   2905    -18    -46   -158       C  
ATOM   2470  CD1 ILE B  15      33.221   9.531  14.842  1.00 29.73           C  
ANISOU 2470  CD1 ILE B  15     4163   3685   3445    -26      2   -164       C  
ATOM   2471  N   GLY B  16      35.827   4.598  15.265  1.00 25.88           N  
ANISOU 2471  N   GLY B  16     3723   3230   2880    -12    -43   -138       N  
ATOM   2472  CA  GLY B  16      36.941   3.677  15.496  1.00 27.37           C  
ANISOU 2472  CA  GLY B  16     3923   3429   3046     -7    -54   -133       C  
ATOM   2473  C   GLY B  16      36.805   2.349  14.747  1.00 26.40           C  
ANISOU 2473  C   GLY B  16     3800   3300   2931     -4    -61   -122       C  
ATOM   2474  O   GLY B  16      37.780   1.872  14.131  1.00 25.61           O  
ANISOU 2474  O   GLY B  16     3701   3204   2823      0    -76   -118       O  
ATOM   2475  N   GLY B  17      35.608   1.767  14.767  1.00 26.54           N  
ANISOU 2475  N   GLY B  17     3813   3303   2965     -7    -50   -116       N  
ATOM   2476  CA  GLY B  17      35.352   0.587  13.930  1.00 27.63           C  
ANISOU 2476  CA  GLY B  17     3949   3432   3115     -7    -58   -108       C  
ATOM   2477  C   GLY B  17      35.657   0.893  12.446  1.00 25.95           C  
ANISOU 2477  C   GLY B  17     3728   3218   2911     -7    -77   -113       C  
ATOM   2478  O   GLY B  17      36.322   0.087  11.753  1.00 26.66           O  
ANISOU 2478  O   GLY B  17     3824   3309   2996     -3    -89   -110       O  
ATOM   2479  N   VAL B  18      35.275   2.066  11.961  1.00 24.71           N  
ANISOU 2479  N   VAL B  18     3559   3061   2766    -10    -79   -119       N  
ATOM   2480  CA  VAL B  18      35.473   2.335  10.466  1.00 24.75           C  
ANISOU 2480  CA  VAL B  18     3558   3066   2780     -9    -97   -121       C  
ATOM   2481  C   VAL B  18      36.952   2.644  10.245  1.00 24.09           C  
ANISOU 2481  C   VAL B  18     3479   2994   2676     -2   -106   -124       C  
ATOM   2482  O   VAL B  18      37.542   2.278   9.255  1.00 24.44           O  
ANISOU 2482  O   VAL B  18     3527   3039   2717      2   -118   -122       O  
ATOM   2483  CB  VAL B  18      34.475   3.362   9.803  1.00 24.55           C  
ANISOU 2483  CB  VAL B  18     3514   3034   2777    -15    -98   -123       C  
ATOM   2484  CG1 VAL B  18      34.623   3.512   8.246  1.00 23.36           C  
ANISOU 2484  CG1 VAL B  18     3360   2884   2632    -14   -117   -124       C  
ATOM   2485  CG2 VAL B  18      33.023   2.937  10.056  1.00 23.84           C  
ANISOU 2485  CG2 VAL B  18     3416   2929   2710    -23    -89   -118       C  
ATOM   2486  N   MET B  19      37.598   3.198  11.241  1.00 24.29           N  
ANISOU 2486  N   MET B  19     3509   3029   2689      0    -99   -127       N  
ATOM   2487  CA  MET B  19      39.087   3.378  11.135  1.00 24.38           C  
ANISOU 2487  CA  MET B  19     3525   3053   2684      5   -109   -127       C  
ATOM   2488  C   MET B  19      39.879   2.094  10.967  1.00 23.57           C  
ANISOU 2488  C   MET B  19     3433   2952   2570     12   -115   -118       C  
ATOM   2489  O   MET B  19      40.667   1.992  10.007  1.00 25.26           O  
ANISOU 2489  O   MET B  19     3646   3167   2783     19   -124   -116       O  
ATOM   2490  CB  MET B  19      39.623   4.225  12.262  1.00 23.54           C  
ANISOU 2490  CB  MET B  19     3420   2956   2566      4   -105   -132       C  
ATOM   2491  CG  MET B  19      39.020   5.587  12.055  1.00 24.52           C  
ANISOU 2491  CG  MET B  19     3532   3076   2705      0   -100   -141       C  
ATOM   2492  SD  MET B  19      39.828   6.813  12.965  1.00 25.28           S  
ANISOU 2492  SD  MET B  19     3630   3182   2792     -3    -99   -151       S  
ATOM   2493  CE  MET B  19      39.456   6.479  14.714  1.00 24.02           C  
ANISOU 2493  CE  MET B  19     3487   3026   2613     -7    -85   -155       C  
ATOM   2494  N   ALA B  20      39.646   1.102  11.836  1.00 22.29           N  
ANISOU 2494  N   ALA B  20     3280   2788   2402     12   -108   -112       N  
ATOM   2495  CA  ALA B  20      40.256  -0.244  11.666  1.00 20.26           C  
ANISOU 2495  CA  ALA B  20     3031   2527   2136     19   -110   -103       C  
ATOM   2496  C   ALA B  20      40.055  -0.788  10.256  1.00 20.55           C  
ANISOU 2496  C   ALA B  20     3068   2554   2184     21   -117   -103       C  
ATOM   2497  O   ALA B  20      40.957  -1.301   9.632  1.00 21.31           O  
ANISOU 2497  O   ALA B  20     3171   2651   2276     29   -122    -99       O  
ATOM   2498  CB  ALA B  20      39.608  -1.174  12.606  1.00 20.32           C  
ANISOU 2498  CB  ALA B  20     3045   2530   2143     16    -99    -96       C  
ATOM   2499  N   THR B  21      38.804  -0.832   9.858  1.00 20.20           N  
ANISOU 2499  N   THR B  21     3020   2499   2156     13   -116   -107       N  
ATOM   2500  CA  THR B  21      38.373  -1.363   8.597  1.00 19.61           C  
ANISOU 2500  CA  THR B  21     2946   2413   2090     12   -125   -110       C  
ATOM   2501  C   THR B  21      39.180  -0.791   7.471  1.00 19.30           C  
ANISOU 2501  C   THR B  21     2907   2378   2045     19   -135   -112       C  
ATOM   2502  O   THR B  21      39.746  -1.550   6.759  1.00 20.45           O  
ANISOU 2502  O   THR B  21     3063   2520   2185     25   -138   -111       O  
ATOM   2503  CB  THR B  21      36.876  -1.153   8.400  1.00 19.50           C  
ANISOU 2503  CB  THR B  21     2923   2388   2096      1   -125   -113       C  
ATOM   2504  OG1 THR B  21      36.170  -1.968   9.331  1.00 20.41           O  
ANISOU 2504  OG1 THR B  21     3040   2496   2219     -2   -113   -108       O  
ATOM   2505  CG2 THR B  21      36.388  -1.590   6.974  1.00 19.03           C  
ANISOU 2505  CG2 THR B  21     2866   2318   2046     -1   -139   -117       C  
ATOM   2506  N   LEU B  22      39.146   0.539   7.278  1.00 18.62           N  
ANISOU 2506  N   LEU B  22     2810   2299   1963     17   -137   -116       N  
ATOM   2507  CA  LEU B  22      39.931   1.273   6.290  1.00 18.43           C  
ANISOU 2507  CA  LEU B  22     2784   2281   1936     24   -144   -117       C  
ATOM   2508  C   LEU B  22      41.467   1.049   6.337  1.00 17.83           C  
ANISOU 2508  C   LEU B  22     2714   2212   1846     36   -143   -111       C  
ATOM   2509  O   LEU B  22      42.112   0.926   5.282  1.00 16.92           O  
ANISOU 2509  O   LEU B  22     2604   2096   1727     44   -147   -109       O  
ATOM   2510  CB  LEU B  22      39.657   2.794   6.493  1.00 18.80           C  
ANISOU 2510  CB  LEU B  22     2816   2335   1991     20   -143   -121       C  
ATOM   2511  CG  LEU B  22      38.229   3.141   6.098  1.00 19.89           C  
ANISOU 2511  CG  LEU B  22     2944   2464   2146     11   -145   -124       C  
ATOM   2512  CD1 LEU B  22      38.000   4.681   6.094  1.00 19.64           C  
ANISOU 2512  CD1 LEU B  22     2897   2437   2126      9   -142   -126       C  
ATOM   2513  CD2 LEU B  22      38.054   2.556   4.699  1.00 19.49           C  
ANISOU 2513  CD2 LEU B  22     2900   2408   2094     13   -157   -123       C  
ATOM   2514  N   ILE B  23      42.040   1.060   7.538  1.00 16.96           N  
ANISOU 2514  N   ILE B  23     2604   2110   1730     36   -138   -108       N  
ATOM   2515  CA  ILE B  23      43.438   0.767   7.725  1.00 17.22           C  
ANISOU 2515  CA  ILE B  23     2639   2149   1753     46   -139    -99       C  
ATOM   2516  C   ILE B  23      43.770  -0.651   7.300  1.00 17.80           C  
ANISOU 2516  C   ILE B  23     2725   2213   1822     53   -136    -92       C  
ATOM   2517  O   ILE B  23      44.889  -0.929   6.882  1.00 18.56           O  
ANISOU 2517  O   ILE B  23     2824   2311   1915     63   -136    -84       O  
ATOM   2518  CB  ILE B  23      43.771   0.828   9.312  1.00 17.79           C  
ANISOU 2518  CB  ILE B  23     2711   2231   1818     42   -136    -96       C  
ATOM   2519  CG1 ILE B  23      43.767   2.249   9.832  1.00 17.74           C  
ANISOU 2519  CG1 ILE B  23     2694   2233   1813     36   -138   -104       C  
ATOM   2520  CG2 ILE B  23      45.128   0.185   9.543  1.00 17.35           C  
ANISOU 2520  CG2 ILE B  23     2657   2179   1753     52   -138    -84       C  
ATOM   2521  CD1 ILE B  23      43.676   2.367  11.381  1.00 18.58           C  
ANISOU 2521  CD1 ILE B  23     2803   2346   1908     29   -135   -106       C  
ATOM   2522  N   VAL B  24      42.844  -1.612   7.408  1.00 17.92           N  
ANISOU 2522  N   VAL B  24     2748   2219   1840     48   -133    -94       N  
ATOM   2523  CA  VAL B  24      43.182  -2.987   6.932  1.00 18.12           C  
ANISOU 2523  CA  VAL B  24     2787   2233   1863     55   -130    -89       C  
ATOM   2524  C   VAL B  24      42.995  -3.009   5.343  1.00 19.56           C  
ANISOU 2524  C   VAL B  24     2977   2407   2047     57   -135    -96       C  
ATOM   2525  O   VAL B  24      43.764  -3.695   4.636  1.00 19.59           O  
ANISOU 2525  O   VAL B  24     2993   2404   2046     68   -131    -92       O  
ATOM   2526  CB  VAL B  24      42.302  -4.061   7.610  1.00 17.72           C  
ANISOU 2526  CB  VAL B  24     2742   2173   1817     48   -124    -88       C  
ATOM   2527  CG1 VAL B  24      42.500  -5.437   7.005  1.00 18.40           C  
ANISOU 2527  CG1 VAL B  24     2842   2244   1904     54   -120    -85       C  
ATOM   2528  CG2 VAL B  24      42.607  -4.200   9.143  1.00 17.69           C  
ANISOU 2528  CG2 VAL B  24     2734   2178   1806     48   -117    -78       C  
ATOM   2529  N   GLN B  25      42.040  -2.264   4.819  1.00 20.18           N  
ANISOU 2529  N   GLN B  25     3050   2484   2131     49   -142   -105       N  
ATOM   2530  CA  GLN B  25      41.919  -2.244   3.328  1.00 23.17           C  
ANISOU 2530  CA  GLN B  25     3438   2857   2507     52   -149   -111       C  
ATOM   2531  C   GLN B  25      43.167  -1.632   2.667  1.00 23.63           C  
ANISOU 2531  C   GLN B  25     3497   2923   2558     66   -146   -105       C  
ATOM   2532  O   GLN B  25      43.759  -2.273   1.890  1.00 26.74           O  
ANISOU 2532  O   GLN B  25     3904   3309   2944     75   -143   -103       O  
ATOM   2533  CB  GLN B  25      40.740  -1.451   2.851  1.00 21.59           C  
ANISOU 2533  CB  GLN B  25     3229   2657   2316     42   -159   -118       C  
ATOM   2534  CG  GLN B  25      39.414  -1.957   3.367  1.00 23.16           C  
ANISOU 2534  CG  GLN B  25     3424   2847   2526     28   -162   -122       C  
ATOM   2535  CD  GLN B  25      38.954  -3.189   2.667  1.00 23.30           C  
ANISOU 2535  CD  GLN B  25     3457   2849   2544     25   -168   -127       C  
ATOM   2536  OE1 GLN B  25      38.859  -3.242   1.368  1.00 25.20           O  
ANISOU 2536  OE1 GLN B  25     3710   3086   2779     26   -178   -133       O  
ATOM   2537  NE2 GLN B  25      38.598  -4.185   3.460  1.00 20.96           N  
ANISOU 2537  NE2 GLN B  25     3164   2544   2255     21   -161   -125       N  
ATOM   2538  N   LYS B  26      43.542  -0.407   2.964  1.00 24.48           N  
ANISOU 2538  N   LYS B  26     3589   3042   2669     67   -147   -102       N  
ATOM   2539  CA  LYS B  26      44.855   0.124   2.583  1.00 26.20           C  
ANISOU 2539  CA  LYS B  26     3803   3265   2884     80   -142    -94       C  
ATOM   2540  C   LYS B  26      46.088  -0.517   3.307  1.00 28.96           C  
ANISOU 2540  C   LYS B  26     4153   3617   3231     88   -134    -82       C  
ATOM   2541  O   LYS B  26      47.132   0.045   3.302  1.00 29.48           O  
ANISOU 2541  O   LYS B  26     4211   3689   3300     96   -132    -74       O  
ATOM   2542  CB  LYS B  26      44.851   1.648   2.878  1.00 25.36           C  
ANISOU 2542  CB  LYS B  26     3678   3170   2786     76   -146    -94       C  
ATOM   2543  CG  LYS B  26      43.494   2.289   2.729  1.00 25.81           C  
ANISOU 2543  CG  LYS B  26     3729   3227   2850     64   -152   -103       C  
ATOM   2544  CD  LYS B  26      43.483   3.799   2.930  1.00 26.08           C  
ANISOU 2544  CD  LYS B  26     3744   3268   2895     61   -153   -104       C  
ATOM   2545  CE  LYS B  26      42.282   4.358   2.202  1.00 28.90           C  
ANISOU 2545  CE  LYS B  26     4097   3623   3259     55   -159   -109       C  
ATOM   2546  NZ  LYS B  26      42.513   4.323   0.723  1.00 30.15           N  
ANISOU 2546  NZ  LYS B  26     4264   3779   3411     64   -163   -105       N  
ATOM   2547  N   ASN B  27      45.997  -1.672   3.970  1.00 30.15           N  
ANISOU 2547  N   ASN B  27     4312   3762   3379     87   -131    -80       N  
ATOM   2548  CA  ASN B  27      47.240  -2.266   4.544  1.00 31.14           C  
ANISOU 2548  CA  ASN B  27     4437   3889   3504     97   -124    -66       C  
ATOM   2549  C   ASN B  27      48.220  -1.271   5.272  1.00 30.86           C  
ANISOU 2549  C   ASN B  27     4383   3868   3472     99   -127    -57       C  
ATOM   2550  O   ASN B  27      49.444  -1.374   5.195  1.00 28.63           O  
ANISOU 2550  O   ASN B  27     4097   3587   3193    110   -124    -43       O  
ATOM   2551  CB  ASN B  27      47.942  -3.168   3.498  1.00 32.22           C  
ANISOU 2551  CB  ASN B  27     4589   4014   3638    111   -114    -60       C  
ATOM   2552  CG  ASN B  27      48.968  -4.139   4.129  1.00 34.67           C  
ANISOU 2552  CG  ASN B  27     4900   4321   3951    120   -104    -44       C  
ATOM   2553  OD1 ASN B  27      48.869  -4.574   5.299  1.00 32.88           O  
ANISOU 2553  OD1 ASN B  27     4668   4098   3724    115   -106    -39       O  
ATOM   2554  ND2 ASN B  27      49.989  -4.441   3.364  1.00 34.25           N  
ANISOU 2554  ND2 ASN B  27     4851   4261   3899    136    -94    -34       N  
ATOM   2555  N   LEU B  28      47.655  -0.306   5.991  1.00 27.63           N  
ANISOU 2555  N   LEU B  28     3964   3468   3065     87   -135    -65       N  
ATOM   2556  CA  LEU B  28      48.410   0.779   6.483  1.00 27.87           C  
ANISOU 2556  CA  LEU B  28     3979   3509   3100     86   -140    -61       C  
ATOM   2557  C   LEU B  28      49.264   0.555   7.833  1.00 28.29           C  
ANISOU 2557  C   LEU B  28     4026   3572   3150     85   -145    -51       C  
ATOM   2558  O   LEU B  28      50.162   1.318   8.148  1.00 26.70           O  
ANISOU 2558  O   LEU B  28     3812   3378   2953     86   -151    -45       O  
ATOM   2559  CB  LEU B  28      47.424   1.882   6.740  1.00 28.23           C  
ANISOU 2559  CB  LEU B  28     4017   3559   3148     74   -145    -75       C  
ATOM   2560  CG  LEU B  28      47.394   3.064   5.821  1.00 30.27           C  
ANISOU 2560  CG  LEU B  28     4267   3817   3415     76   -146    -79       C  
ATOM   2561  CD1 LEU B  28      46.567   4.065   6.582  1.00 30.85           C  
ANISOU 2561  CD1 LEU B  28     4332   3896   3493     62   -149    -91       C  
ATOM   2562  CD2 LEU B  28      48.764   3.645   5.501  1.00 30.60           C  
ANISOU 2562  CD2 LEU B  28     4298   3863   3465     85   -146    -68       C  
ATOM   2563  N   GLY B  29      48.991  -0.467   8.617  1.00 28.60           N  
ANISOU 2563  N   GLY B  29     4074   3610   3181     84   -143    -47       N  
ATOM   2564  CA  GLY B  29      49.706  -0.553   9.911  1.00 28.58           C  
ANISOU 2564  CA  GLY B  29     4066   3618   3172     82   -150    -37       C  
ATOM   2565  C   GLY B  29      49.015  -1.570  10.784  1.00 27.60           C  
ANISOU 2565  C   GLY B  29     3954   3494   3039     78   -145    -35       C  
ATOM   2566  O   GLY B  29      47.902  -1.944  10.480  1.00 26.70           O  
ANISOU 2566  O   GLY B  29     3849   3371   2925     74   -139    -45       O  
ATOM   2567  N   ASP B  30      49.670  -2.052  11.849  1.00 27.32           N  
ANISOU 2567  N   ASP B  30     3918   3467   2996     79   -150    -22       N  
ATOM   2568  CA  ASP B  30      48.950  -2.811  12.827  1.00 27.69           C  
ANISOU 2568  CA  ASP B  30     3974   3514   3031     75   -145    -20       C  
ATOM   2569  C   ASP B  30      48.006  -1.848  13.500  1.00 27.36           C  
ANISOU 2569  C   ASP B  30     3934   3479   2981     62   -148    -37       C  
ATOM   2570  O   ASP B  30      48.271  -0.622  13.526  1.00 26.26           O  
ANISOU 2570  O   ASP B  30     3787   3347   2843     57   -156    -46       O  
ATOM   2571  CB  ASP B  30      49.926  -3.433  13.801  1.00 31.16           C  
ANISOU 2571  CB  ASP B  30     4412   3963   3463     80   -151      0       C  
ATOM   2572  CG  ASP B  30      50.755  -4.584  13.127  1.00 36.09           C  
ANISOU 2572  CG  ASP B  30     5036   4577   4099     94   -143     18       C  
ATOM   2573  OD1 ASP B  30      50.300  -5.130  12.043  1.00 32.44           O  
ANISOU 2573  OD1 ASP B  30     4580   4098   3645     99   -131     12       O  
ATOM   2574  OD2 ASP B  30      51.862  -4.905  13.691  1.00 33.71           O  
ANISOU 2574  OD2 ASP B  30     4728   4284   3797    100   -150     38       O  
ATOM   2575  N   VAL B  31      46.896  -2.370  13.995  1.00 24.85           N  
ANISOU 2575  N   VAL B  31     3626   3157   2659     57   -138    -41       N  
ATOM   2576  CA  VAL B  31      45.856  -1.513  14.594  1.00 24.97           C  
ANISOU 2576  CA  VAL B  31     3642   3174   2669     46   -135    -56       C  
ATOM   2577  C   VAL B  31      45.541  -1.995  16.014  1.00 24.32           C  
ANISOU 2577  C   VAL B  31     3570   3099   2570     43   -130    -50       C  
ATOM   2578  O   VAL B  31      45.324  -3.228  16.215  1.00 23.99           O  
ANISOU 2578  O   VAL B  31     3534   3050   2528     48   -121    -37       O  
ATOM   2579  CB  VAL B  31      44.524  -1.642  13.821  1.00 25.65           C  
ANISOU 2579  CB  VAL B  31     3730   3246   2769     42   -125    -66       C  
ATOM   2580  CG1 VAL B  31      43.424  -0.851  14.497  1.00 26.64           C  
ANISOU 2580  CG1 VAL B  31     3856   3372   2893     32   -118    -79       C  
ATOM   2581  CG2 VAL B  31      44.681  -1.223  12.361  1.00 25.47           C  
ANISOU 2581  CG2 VAL B  31     3700   3216   2760     45   -129    -72       C  
ATOM   2582  N   VAL B  32      45.537  -1.098  17.000  1.00 22.95           N  
ANISOU 2582  N   VAL B  32     3400   2937   2382     36   -134    -57       N  
ATOM   2583  CA  VAL B  32      45.023  -1.491  18.330  1.00 21.49           C  
ANISOU 2583  CA  VAL B  32     3228   2758   2179     33   -126    -53       C  
ATOM   2584  C   VAL B  32      43.731  -0.755  18.574  1.00 21.66           C  
ANISOU 2584  C   VAL B  32     3253   2773   2202     25   -113    -70       C  
ATOM   2585  O   VAL B  32      43.699   0.499  18.493  1.00 21.04           O  
ANISOU 2585  O   VAL B  32     3171   2698   2125     19   -117    -85       O  
ATOM   2586  CB  VAL B  32      45.966  -1.162  19.516  1.00 21.89           C  
ANISOU 2586  CB  VAL B  32     3284   2826   2204     32   -140    -48       C  
ATOM   2587  CG1 VAL B  32      45.245  -1.413  20.840  1.00 22.07           C  
ANISOU 2587  CG1 VAL B  32     3324   2854   2205     29   -128    -47       C  
ATOM   2588  CG2 VAL B  32      47.270  -1.981  19.480  1.00 22.42           C  
ANISOU 2588  CG2 VAL B  32     3347   2901   2270     41   -153    -27       C  
ATOM   2589  N   LEU B  33      42.692  -1.484  18.943  1.00 21.86           N  
ANISOU 2589  N   LEU B  33     3285   2790   2229     25    -95    -65       N  
ATOM   2590  CA  LEU B  33      41.409  -0.834  19.244  1.00 23.06           C  
ANISOU 2590  CA  LEU B  33     3440   2935   2387     19    -79    -78       C  
ATOM   2591  C   LEU B  33      41.327  -0.706  20.746  1.00 24.82           C  
ANISOU 2591  C   LEU B  33     3679   3169   2583     17    -71    -76       C  
ATOM   2592  O   LEU B  33      41.127  -1.676  21.441  1.00 23.77           O  
ANISOU 2592  O   LEU B  33     3555   3036   2440     22    -61    -62       O  
ATOM   2593  CB  LEU B  33      40.217  -1.620  18.748  1.00 22.90           C  
ANISOU 2593  CB  LEU B  33     3415   2897   2388     19    -64    -73       C  
ATOM   2594  CG  LEU B  33      39.954  -1.474  17.206  1.00 23.12           C  
ANISOU 2594  CG  LEU B  33     3429   2913   2442     17    -71    -80       C  
ATOM   2595  CD1 LEU B  33      39.338  -2.755  16.623  1.00 23.74           C  
ANISOU 2595  CD1 LEU B  33     3506   2976   2538     19    -65    -71       C  
ATOM   2596  CD2 LEU B  33      39.018  -0.321  16.905  1.00 24.19           C  
ANISOU 2596  CD2 LEU B  33     3556   3042   2591     10    -65    -95       C  
ATOM   2597  N   PHE B  34      41.427   0.519  21.233  1.00 26.47           N  
ANISOU 2597  N   PHE B  34     3892   3385   2779     11    -74    -92       N  
ATOM   2598  CA  PHE B  34      41.380   0.669  22.641  1.00 29.29           C  
ANISOU 2598  CA  PHE B  34     4268   3752   3107     10    -67    -92       C  
ATOM   2599  C   PHE B  34      40.056   1.277  23.101  1.00 29.76           C  
ANISOU 2599  C   PHE B  34     4334   3801   3170      6    -41   -104       C  
ATOM   2600  O   PHE B  34      39.476   2.070  22.384  1.00 29.60           O  
ANISOU 2600  O   PHE B  34     4302   3770   3173      1    -36   -116       O  
ATOM   2601  CB  PHE B  34      42.536   1.502  23.125  1.00 29.29           C  
ANISOU 2601  CB  PHE B  34     4274   3769   3085      5    -89   -101       C  
ATOM   2602  CG  PHE B  34      42.337   1.961  24.530  1.00 30.77           C  
ANISOU 2602  CG  PHE B  34     4485   3966   3241      1    -81   -109       C  
ATOM   2603  CD1 PHE B  34      41.662   3.146  24.794  1.00 32.91           C  
ANISOU 2603  CD1 PHE B  34     4761   4230   3511     -5    -68   -130       C  
ATOM   2604  CD2 PHE B  34      42.772   1.202  25.562  1.00 31.94           C  
ANISOU 2604  CD2 PHE B  34     4648   4126   3359      6    -85    -94       C  
ATOM   2605  CE1 PHE B  34      41.418   3.561  26.104  1.00 33.91           C  
ANISOU 2605  CE1 PHE B  34     4913   4363   3606     -8    -58   -139       C  
ATOM   2606  CE2 PHE B  34      42.578   1.610  26.881  1.00 32.36           C  
ANISOU 2606  CE2 PHE B  34     4727   4189   3378      3    -78   -101       C  
ATOM   2607  CZ  PHE B  34      41.887   2.776  27.144  1.00 33.07           C  
ANISOU 2607  CZ  PHE B  34     4826   4273   3467     -4    -64   -125       C  
ATOM   2608  N   ASP B  35      39.607   0.905  24.295  1.00 31.42           N  
ANISOU 2608  N   ASP B  35     4563   4014   3358      8    -24    -98       N  
ATOM   2609  CA  ASP B  35      38.467   1.566  24.940  1.00 33.82           C  
ANISOU 2609  CA  ASP B  35     4878   4311   3662      5      2   -108       C  
ATOM   2610  C   ASP B  35      38.455   1.288  26.448  1.00 34.05           C  
ANISOU 2610  C   ASP B  35     4934   4350   3652      9     15   -103       C  
ATOM   2611  O   ASP B  35      38.979   0.266  26.873  1.00 36.56           O  
ANISOU 2611  O   ASP B  35     5258   4677   3953     15      8    -84       O  
ATOM   2612  CB  ASP B  35      37.138   1.131  24.330  1.00 34.34           C  
ANISOU 2612  CB  ASP B  35     4929   4355   3762      7     25   -102       C  
ATOM   2613  CG  ASP B  35      36.078   2.268  24.365  1.00 39.06           C  
ANISOU 2613  CG  ASP B  35     5524   4940   4375      2     47   -117       C  
ATOM   2614  OD1 ASP B  35      35.648   2.649  25.488  1.00 39.83           O  
ANISOU 2614  OD1 ASP B  35     5641   5038   4453      2     68   -122       O  
ATOM   2615  OD2 ASP B  35      35.673   2.782  23.275  1.00 39.02           O  
ANISOU 2615  OD2 ASP B  35     5498   4923   4402     -1     43   -124       O  
ATOM   2616  N   ILE B  36      37.819   2.125  27.259  1.00 34.22           N  
ANISOU 2616  N   ILE B  36     4972   4369   3660      6     35   -116       N  
ATOM   2617  CA  ILE B  36      37.572   1.661  28.637  1.00 37.43           C  
ANISOU 2617  CA  ILE B  36     5406   4783   4032     11     54   -107       C  
ATOM   2618  C   ILE B  36      36.472   0.613  28.755  1.00 36.31           C  
ANISOU 2618  C   ILE B  36     5260   4626   3907     20     84    -86       C  
ATOM   2619  O   ILE B  36      36.433  -0.068  29.747  1.00 41.54           O  
ANISOU 2619  O   ILE B  36     5942   5297   4545     26     97    -72       O  
ATOM   2620  CB  ILE B  36      37.397   2.792  29.707  1.00 39.56           C  
ANISOU 2620  CB  ILE B  36     5703   5056   4270      7     67   -128       C  
ATOM   2621  CG1 ILE B  36      35.981   3.367  29.687  1.00 39.92           C  
ANISOU 2621  CG1 ILE B  36     5746   5080   4339      8    106   -136       C  
ATOM   2622  CG2 ILE B  36      38.449   3.880  29.560  1.00 40.89           C  
ANISOU 2622  CG2 ILE B  36     5873   5235   4426     -2     37   -150       C  
ATOM   2623  CD1 ILE B  36      35.598   3.772  28.302  1.00 38.71           C  
ANISOU 2623  CD1 ILE B  36     5560   4911   4234      3    101   -141       C  
ATOM   2624  N   VAL B  37      35.580   0.480  27.768  1.00 36.71           N  
ANISOU 2624  N   VAL B  37     5287   4657   4003     19     96    -84       N  
ATOM   2625  CA  VAL B  37      34.498  -0.496  27.827  1.00 36.64           C  
ANISOU 2625  CA  VAL B  37     5271   4632   4016     25    123    -64       C  
ATOM   2626  C   VAL B  37      35.148  -1.857  27.701  1.00 38.91           C  
ANISOU 2626  C   VAL B  37     5556   4927   4301     31    108    -43       C  
ATOM   2627  O   VAL B  37      35.749  -2.166  26.660  1.00 38.74           O  
ANISOU 2627  O   VAL B  37     5517   4905   4297     28     83    -43       O  
ATOM   2628  CB  VAL B  37      33.487  -0.397  26.634  1.00 37.24           C  
ANISOU 2628  CB  VAL B  37     5319   4686   4145     21    130    -66       C  
ATOM   2629  CG1 VAL B  37      32.523  -1.587  26.658  1.00 35.21           C  
ANISOU 2629  CG1 VAL B  37     5052   4412   3913     26    153    -43       C  
ATOM   2630  CG2 VAL B  37      32.712   0.915  26.650  1.00 36.51           C  
ANISOU 2630  CG2 VAL B  37     5224   4583   4064     16    148    -83       C  
ATOM   2631  N   LYS B  38      35.036  -2.668  28.745  1.00 38.09           N  
ANISOU 2631  N   LYS B  38     5469   4828   4176     39    125    -25       N  
ATOM   2632  CA  LYS B  38      35.575  -4.009  28.697  1.00 37.65           C  
ANISOU 2632  CA  LYS B  38     5409   4775   4119     46    115     -2       C  
ATOM   2633  C   LYS B  38      35.106  -4.875  27.514  1.00 35.63           C  
ANISOU 2633  C   LYS B  38     5126   4499   3910     45    114      6       C  
ATOM   2634  O   LYS B  38      33.981  -4.722  27.013  1.00 34.21           O  
ANISOU 2634  O   LYS B  38     4932   4299   3765     41    131      3       O  
ATOM   2635  CB  LYS B  38      35.375  -4.681  30.052  1.00 41.93           C  
ANISOU 2635  CB  LYS B  38     5975   5324   4632     55    138     17       C  
ATOM   2636  CG  LYS B  38      36.462  -4.175  31.012  1.00 46.70           C  
ANISOU 2636  CG  LYS B  38     6604   5955   5182     56    120     12       C  
ATOM   2637  CD  LYS B  38      36.313  -4.624  32.458  1.00 49.26           C  
ANISOU 2637  CD  LYS B  38     6958   6290   5468     65    141     29       C  
ATOM   2638  CE  LYS B  38      37.124  -3.702  33.373  1.00 51.57           C  
ANISOU 2638  CE  LYS B  38     7279   6606   5708     62    124     13       C  
ATOM   2639  NZ  LYS B  38      36.699  -3.738  34.809  1.00 57.34           N  
ANISOU 2639  NZ  LYS B  38     8044   7345   6398     70    152     21       N  
ATOM   2640  N   ASN B  39      36.017  -5.748  27.066  1.00 33.78           N  
ANISOU 2640  N   ASN B  39     4886   4270   3676     48     93     18       N  
ATOM   2641  CA  ASN B  39      35.804  -6.750  26.005  1.00 34.91           C  
ANISOU 2641  CA  ASN B  39     5009   4396   3857     48     89     27       C  
ATOM   2642  C   ASN B  39      35.391  -6.319  24.622  1.00 32.57           C  
ANISOU 2642  C   ASN B  39     4692   4086   3597     39     78     11       C  
ATOM   2643  O   ASN B  39      35.849  -6.901  23.652  1.00 32.15           O  
ANISOU 2643  O   ASN B  39     4628   4027   3560     39     62     12       O  
ATOM   2644  CB  ASN B  39      34.878  -7.861  26.478  1.00 36.78           C  
ANISOU 2644  CB  ASN B  39     5245   4617   4111     54    118     49       C  
ATOM   2645  CG  ASN B  39      35.336  -8.413  27.797  1.00 39.80           C  
ANISOU 2645  CG  ASN B  39     5648   5015   4459     64    128     69       C  
ATOM   2646  OD1 ASN B  39      36.425  -8.928  27.890  1.00 41.46           O  
ANISOU 2646  OD1 ASN B  39     5863   5239   4651     69    109     79       O  
ATOM   2647  ND2 ASN B  39      34.553  -8.208  28.834  1.00 41.53           N  
ANISOU 2647  ND2 ASN B  39     5881   5232   4664     68    156     74       N  
ATOM   2648  N   MET B  40      34.484  -5.360  24.498  1.00 34.18           N  
ANISOU 2648  N   MET B  40     4890   4280   3813     33     90     -2       N  
ATOM   2649  CA  MET B  40      33.963  -5.012  23.139  1.00 33.30           C  
ANISOU 2649  CA  MET B  40     4758   4154   3738     25     80    -15       C  
ATOM   2650  C   MET B  40      35.088  -4.736  22.087  1.00 32.23           C  
ANISOU 2650  C   MET B  40     4616   4028   3599     23     47    -26       C  
ATOM   2651  O   MET B  40      34.940  -5.058  20.938  1.00 31.45           O  
ANISOU 2651  O   MET B  40     4504   3918   3526     19     36    -29       O  
ATOM   2652  CB  MET B  40      33.032  -3.817  23.291  1.00 31.87           C  
ANISOU 2652  CB  MET B  40     4573   3967   3566     20     95    -28       C  
ATOM   2653  CG  MET B  40      32.625  -3.155  22.016  1.00 34.28           C  
ANISOU 2653  CG  MET B  40     4859   4263   3902     11     82    -41       C  
ATOM   2654  SD  MET B  40      33.783  -1.903  21.384  1.00 34.29           S  
ANISOU 2654  SD  MET B  40     4860   4281   3885      8     54    -62       S  
ATOM   2655  CE  MET B  40      33.665  -0.487  22.473  1.00 31.93           C  
ANISOU 2655  CE  MET B  40     4576   3992   3564      7     70    -76       C  
ATOM   2656  N   PRO B  41      36.210  -4.083  22.490  1.00 33.82           N  
ANISOU 2656  N   PRO B  41     4828   4250   3769     24     33    -33       N  
ATOM   2657  CA  PRO B  41      37.243  -3.828  21.439  1.00 33.22           C  
ANISOU 2657  CA  PRO B  41     4745   4181   3695     23      5    -41       C  
ATOM   2658  C   PRO B  41      37.899  -5.140  20.951  1.00 31.16           C  
ANISOU 2658  C   PRO B  41     4481   3916   3439     29     -4    -26       C  
ATOM   2659  O   PRO B  41      38.157  -5.308  19.734  1.00 34.42           O  
ANISOU 2659  O   PRO B  41     4884   4322   3870     28    -17    -31       O  
ATOM   2660  CB  PRO B  41      38.258  -2.909  22.121  1.00 34.12           C  
ANISOU 2660  CB  PRO B  41     4870   4315   3776     23     -7    -49       C  
ATOM   2661  CG  PRO B  41      37.633  -2.479  23.436  1.00 35.24           C  
ANISOU 2661  CG  PRO B  41     5027   4461   3898     22     14    -51       C  
ATOM   2662  CD  PRO B  41      36.567  -3.488  23.801  1.00 33.98           C  
ANISOU 2662  CD  PRO B  41     4869   4288   3753     26     39    -35       C  
ATOM   2663  N   HIS B  42      38.125  -6.070  21.852  1.00 29.27           N  
ANISOU 2663  N   HIS B  42     4252   3681   3186     36      4     -8       N  
ATOM   2664  CA  HIS B  42      38.553  -7.431  21.471  1.00 29.02           C  
ANISOU 2664  CA  HIS B  42     4218   3642   3165     42      2      7       C  
ATOM   2665  C   HIS B  42      37.621  -8.024  20.467  1.00 27.48           C  
ANISOU 2665  C   HIS B  42     4011   3423   3006     38      8      5       C  
ATOM   2666  O   HIS B  42      38.056  -8.590  19.460  1.00 24.83           O  
ANISOU 2666  O   HIS B  42     3669   3079   2683     39     -3      4       O  
ATOM   2667  CB  HIS B  42      38.637  -8.299  22.677  1.00 32.25           C  
ANISOU 2667  CB  HIS B  42     4639   4057   3558     50     16     29       C  
ATOM   2668  CG  HIS B  42      39.526  -7.737  23.767  1.00 35.53           C  
ANISOU 2668  CG  HIS B  42     5067   4496   3934     53      7     32       C  
ATOM   2669  ND1 HIS B  42      40.877  -7.814  23.715  1.00 35.21           N  
ANISOU 2669  ND1 HIS B  42     5028   4471   3879     57    -13     38       N  
ATOM   2670  CD2 HIS B  42      39.211  -7.052  24.948  1.00 41.09           C  
ANISOU 2670  CD2 HIS B  42     5787   5213   4611     52     18     29       C  
ATOM   2671  CE1 HIS B  42      41.410  -7.229  24.809  1.00 39.85           C  
ANISOU 2671  CE1 HIS B  42     5629   5080   4431     57    -20     39       C  
ATOM   2672  NE2 HIS B  42      40.393  -6.775  25.579  1.00 45.33           N  
ANISOU 2672  NE2 HIS B  42     6334   5773   5116     54      0     33       N  
ATOM   2673  N   GLY B  43      36.316  -7.861  20.692  1.00 26.94           N  
ANISOU 2673  N   GLY B  43     3938   3342   2953     33     25      2       N  
ATOM   2674  CA  GLY B  43      35.338  -8.389  19.749  1.00 24.75           C  
ANISOU 2674  CA  GLY B  43     3648   3041   2712     27     28      0       C  
ATOM   2675  C   GLY B  43      35.394  -7.799  18.350  1.00 23.68           C  
ANISOU 2675  C   GLY B  43     3503   2903   2592     20      8    -17       C  
ATOM   2676  O   GLY B  43      35.438  -8.510  17.368  1.00 23.14           O  
ANISOU 2676  O   GLY B  43     3430   2821   2539     19      0    -18       O  
ATOM   2677  N   LYS B  44      35.428  -6.472  18.264  1.00 23.25           N  
ANISOU 2677  N   LYS B  44     3445   2858   2528     16      2    -31       N  
ATOM   2678  CA  LYS B  44      35.523  -5.800  17.001  1.00 22.51           C  
ANISOU 2678  CA  LYS B  44     3344   2763   2446     11    -15    -46       C  
ATOM   2679  C   LYS B  44      36.896  -6.052  16.343  1.00 22.15           C  
ANISOU 2679  C   LYS B  44     3302   2726   2385     17    -34    -47       C  
ATOM   2680  O   LYS B  44      37.022  -6.081  15.098  1.00 21.98           O  
ANISOU 2680  O   LYS B  44     3276   2698   2376     15    -48    -54       O  
ATOM   2681  CB  LYS B  44      35.354  -4.250  17.226  1.00 22.90           C  
ANISOU 2681  CB  LYS B  44     3390   2823   2488      7    -15    -58       C  
ATOM   2682  CG  LYS B  44      34.014  -3.723  17.740  1.00 22.58           C  
ANISOU 2682  CG  LYS B  44     3343   2773   2463      2      3    -59       C  
ATOM   2683  CD  LYS B  44      33.834  -2.184  17.530  1.00 22.87           C  
ANISOU 2683  CD  LYS B  44     3372   2814   2500     -2      1    -74       C  
ATOM   2684  CE  LYS B  44      32.374  -1.639  17.674  1.00 22.27           C  
ANISOU 2684  CE  LYS B  44     3284   2724   2451     -8     20    -74       C  
ATOM   2685  NZ  LYS B  44      32.396  -0.122  17.481  1.00 21.70           N  
ANISOU 2685  NZ  LYS B  44     3207   2658   2378    -11     17    -88       N  
ATOM   2686  N   ALA B  45      37.956  -6.130  17.140  1.00 21.74           N  
ANISOU 2686  N   ALA B  45     3260   2690   2309     25    -35    -39       N  
ATOM   2687  CA  ALA B  45      39.283  -6.406  16.590  1.00 22.13           C  
ANISOU 2687  CA  ALA B  45     3311   2746   2349     31    -50    -36       C  
ATOM   2688  C   ALA B  45      39.260  -7.768  15.887  1.00 23.30           C  
ANISOU 2688  C   ALA B  45     3460   2877   2513     35    -48    -28       C  
ATOM   2689  O   ALA B  45      39.694  -7.930  14.665  1.00 23.62           O  
ANISOU 2689  O   ALA B  45     3499   2911   2562     36    -59    -34       O  
ATOM   2690  CB  ALA B  45      40.303  -6.431  17.740  1.00 24.27           C  
ANISOU 2690  CB  ALA B  45     3591   3036   2593     38    -51    -24       C  
ATOM   2691  N   LEU B  46      38.650  -8.730  16.586  1.00 22.19           N  
ANISOU 2691  N   LEU B  46     3323   2728   2380     36    -33    -16       N  
ATOM   2692  CA  LEU B  46      38.618 -10.090  16.057  1.00 23.46           C  
ANISOU 2692  CA  LEU B  46     3485   2870   2557     38    -29     -8       C  
ATOM   2693  C   LEU B  46      37.791 -10.091  14.710  1.00 24.61           C  
ANISOU 2693  C   LEU B  46     3625   2998   2728     29    -37    -24       C  
ATOM   2694  O   LEU B  46      38.257 -10.682  13.723  1.00 24.22           O  
ANISOU 2694  O   LEU B  46     3579   2938   2684     32    -45    -27       O  
ATOM   2695  CB  LEU B  46      37.976 -10.999  17.105  1.00 24.26           C  
ANISOU 2695  CB  LEU B  46     3589   2963   2665     40     -9      8       C  
ATOM   2696  CG  LEU B  46      37.922 -12.471  16.755  1.00 26.09           C  
ANISOU 2696  CG  LEU B  46     3822   3174   2915     43     -2     18       C  
ATOM   2697  CD1 LEU B  46      39.263 -13.022  16.261  1.00 26.79           C  
ANISOU 2697  CD1 LEU B  46     3916   3266   2996     53    -10     23       C  
ATOM   2698  CD2 LEU B  46      37.431 -13.207  18.002  1.00 27.86           C  
ANISOU 2698  CD2 LEU B  46     4048   3395   3142     47     18     38       C  
ATOM   2699  N   ASP B  47      36.665  -9.340  14.647  1.00 24.25           N  
ANISOU 2699  N   ASP B  47     3571   2948   2693     20    -36    -33       N  
ATOM   2700  CA  ASP B  47      35.811  -9.280  13.447  1.00 25.39           C  
ANISOU 2700  CA  ASP B  47     3709   3077   2861     10    -46    -46       C  
ATOM   2701  C   ASP B  47      36.630  -8.634  12.301  1.00 25.98           C  
ANISOU 2701  C   ASP B  47     3786   3160   2925     12    -65    -59       C  
ATOM   2702  O   ASP B  47      36.798  -9.215  11.284  1.00 30.07           O  
ANISOU 2702  O   ASP B  47     4309   3667   3449     12    -74    -64       O  
ATOM   2703  CB  ASP B  47      34.458  -8.549  13.735  1.00 25.51           C  
ANISOU 2703  CB  ASP B  47     3711   3087   2892      0    -40    -50       C  
ATOM   2704  CG  ASP B  47      33.581  -8.361  12.467  1.00 26.41           C  
ANISOU 2704  CG  ASP B  47     3816   3188   3030    -10    -56    -62       C  
ATOM   2705  OD1 ASP B  47      33.599  -9.234  11.545  1.00 24.74           O  
ANISOU 2705  OD1 ASP B  47     3609   2962   2828    -12    -66    -66       O  
ATOM   2706  OD2 ASP B  47      32.916  -7.283  12.330  1.00 27.15           O  
ANISOU 2706  OD2 ASP B  47     3899   3285   3131    -16    -58    -68       O  
ATOM   2707  N   THR B  48      37.219  -7.477  12.533  1.00 25.33           N  
ANISOU 2707  N   THR B  48     3701   3096   2825     15    -69    -62       N  
ATOM   2708  CA  THR B  48      37.997  -6.805  11.553  1.00 24.78           C  
ANISOU 2708  CA  THR B  48     3632   3034   2747     18    -84    -71       C  
ATOM   2709  C   THR B  48      39.197  -7.586  11.043  1.00 24.95           C  
ANISOU 2709  C   THR B  48     3664   3054   2759     28    -87    -67       C  
ATOM   2710  O   THR B  48      39.464  -7.626   9.825  1.00 24.86           O  
ANISOU 2710  O   THR B  48     3657   3037   2750     30    -96    -75       O  
ATOM   2711  CB  THR B  48      38.388  -5.441  12.117  1.00 23.83           C  
ANISOU 2711  CB  THR B  48     3507   2932   2612     19    -85    -75       C  
ATOM   2712  OG1 THR B  48      37.199  -4.869  12.607  1.00 23.30           O  
ANISOU 2712  OG1 THR B  48     3433   2863   2557     10    -77    -78       O  
ATOM   2713  CG2 THR B  48      38.996  -4.535  11.047  1.00 24.11           C  
ANISOU 2713  CG2 THR B  48     3539   2974   2644     21    -99    -84       C  
ATOM   2714  N   SER B  49      39.945  -8.163  11.957  1.00 25.76           N  
ANISOU 2714  N   SER B  49     3771   3163   2852     36    -79    -53       N  
ATOM   2715  CA  SER B  49      41.138  -8.954  11.559  1.00 26.08           C  
ANISOU 2715  CA  SER B  49     3819   3201   2886     47    -79    -45       C  
ATOM   2716  C   SER B  49      40.901  -9.972  10.445  1.00 25.43           C  
ANISOU 2716  C   SER B  49     3745   3097   2817     47    -79    -50       C  
ATOM   2717  O   SER B  49      41.755 -10.067   9.556  1.00 24.94           O  
ANISOU 2717  O   SER B  49     3690   3034   2752     55    -82    -52       O  
ATOM   2718  CB  SER B  49      41.731  -9.640  12.769  1.00 24.66           C  
ANISOU 2718  CB  SER B  49     3642   3028   2698     54    -69    -26       C  
ATOM   2719  OG  SER B  49      40.869 -10.696  13.085  1.00 26.15           O  
ANISOU 2719  OG  SER B  49     3833   3200   2901     51    -57    -20       O  
ATOM   2720  N   HIS B  50      39.752 -10.681  10.445  1.00 25.02           N  
ANISOU 2720  N   HIS B  50     3693   3028   2782     39    -74    -53       N  
ATOM   2721  CA  HIS B  50      39.417 -11.623   9.313  1.00 25.45           C  
ANISOU 2721  CA  HIS B  50     3757   3060   2850     36    -77    -62       C  
ATOM   2722  C   HIS B  50      39.435 -11.005   7.958  1.00 24.29           C  
ANISOU 2722  C   HIS B  50     3616   2913   2701     33    -92    -78       C  
ATOM   2723  O   HIS B  50      39.657 -11.685   6.909  1.00 22.63           O  
ANISOU 2723  O   HIS B  50     3418   2687   2491     35    -94    -86       O  
ATOM   2724  CB  HIS B  50      38.085 -12.384   9.485  1.00 26.33           C  
ANISOU 2724  CB  HIS B  50     3866   3152   2985     24    -73    -64       C  
ATOM   2725  CG  HIS B  50      37.942 -12.986  10.833  1.00 27.59           C  
ANISOU 2725  CG  HIS B  50     4022   3312   3150     27    -56    -46       C  
ATOM   2726  ND1 HIS B  50      36.817 -12.841  11.593  1.00 27.46           N  
ANISOU 2726  ND1 HIS B  50     3994   3291   3145     18    -50    -42       N  
ATOM   2727  CD2 HIS B  50      38.869 -13.667  11.618  1.00 27.57           C  
ANISOU 2727  CD2 HIS B  50     4023   3313   3138     39    -43    -28       C  
ATOM   2728  CE1 HIS B  50      37.046 -13.391  12.806  1.00 27.24           C  
ANISOU 2728  CE1 HIS B  50     3967   3267   3115     25    -33    -24       C  
ATOM   2729  NE2 HIS B  50      38.296 -13.876  12.824  1.00 28.75           N  
ANISOU 2729  NE2 HIS B  50     4166   3463   3292     37    -31    -15       N  
ATOM   2730  N   THR B  51      39.266  -9.693   7.942  1.00 22.92           N  
ANISOU 2730  N   THR B  51     3432   2754   2520     30   -100    -83       N  
ATOM   2731  CA  THR B  51      39.214  -9.036   6.648  1.00 21.66           C  
ANISOU 2731  CA  THR B  51     3276   2596   2358     28   -114    -97       C  
ATOM   2732  C   THR B  51      40.610  -8.901   6.008  1.00 21.51           C  
ANISOU 2732  C   THR B  51     3266   2583   2322     42   -113    -95       C  
ATOM   2733  O   THR B  51      40.751  -8.663   4.758  1.00 20.09           O  
ANISOU 2733  O   THR B  51     3095   2401   2137     44   -122   -105       O  
ATOM   2734  CB  THR B  51      38.513  -7.626   6.705  1.00 21.88           C  
ANISOU 2734  CB  THR B  51     3289   2636   2388     20   -123   -102       C  
ATOM   2735  OG1 THR B  51      39.348  -6.739   7.337  1.00 18.92           O  
ANISOU 2735  OG1 THR B  51     2907   2279   2000     27   -119    -96       O  
ATOM   2736  CG2 THR B  51      37.101  -7.634   7.422  1.00 21.99           C  
ANISOU 2736  CG2 THR B  51     3290   2643   2419      7   -121   -101       C  
ATOM   2737  N   ASN B  52      41.667  -9.122   6.795  1.00 21.66           N  
ANISOU 2737  N   ASN B  52     3284   2610   2334     53   -103    -81       N  
ATOM   2738  CA  ASN B  52      42.952  -9.252   6.068  1.00 23.10           C  
ANISOU 2738  CA  ASN B  52     3475   2794   2508     67   -100    -77       C  
ATOM   2739  C   ASN B  52      42.889 -10.106   4.800  1.00 22.93           C  
ANISOU 2739  C   ASN B  52     3473   2752   2488     69    -99    -87       C  
ATOM   2740  O   ASN B  52      43.625  -9.853   3.853  1.00 22.74           O  
ANISOU 2740  O   ASN B  52     3456   2728   2454     78    -99    -90       O  
ATOM   2741  CB  ASN B  52      44.059  -9.762   6.955  1.00 23.01           C  
ANISOU 2741  CB  ASN B  52     3461   2787   2493     78    -88    -59       C  
ATOM   2742  CG  ASN B  52      44.510  -8.692   7.918  1.00 24.11           C  
ANISOU 2742  CG  ASN B  52     3586   2949   2625     78    -93    -51       C  
ATOM   2743  OD1 ASN B  52      45.249  -7.726   7.530  1.00 24.56           O  
ANISOU 2743  OD1 ASN B  52     3637   3017   2676     83    -99    -51       O  
ATOM   2744  ND2 ASN B  52      43.998  -8.766   9.132  1.00 22.79           N  
ANISOU 2744  ND2 ASN B  52     3412   2787   2458     72    -91    -45       N  
ATOM   2745  N   VAL B  53      42.073 -11.176   4.853  1.00 23.14           N  
ANISOU 2745  N   VAL B  53     3506   2760   2525     61    -96    -92       N  
ATOM   2746  CA  VAL B  53      42.047 -12.172   3.853  1.00 22.51           C  
ANISOU 2746  CA  VAL B  53     3446   2659   2447     62    -94   -101       C  
ATOM   2747  C   VAL B  53      41.406 -11.626   2.549  1.00 24.41           C  
ANISOU 2747  C   VAL B  53     3695   2897   2681     55   -111   -120       C  
ATOM   2748  O   VAL B  53      41.941 -11.794   1.405  1.00 22.78           O  
ANISOU 2748  O   VAL B  53     3508   2683   2463     62   -110   -128       O  
ATOM   2749  CB  VAL B  53      41.289 -13.493   4.341  1.00 22.69           C  
ANISOU 2749  CB  VAL B  53     3472   2660   2487     55    -87   -101       C  
ATOM   2750  CG1 VAL B  53      41.247 -14.458   3.194  1.00 20.75           C  
ANISOU 2750  CG1 VAL B  53     3249   2391   2243     54    -87   -115       C  
ATOM   2751  CG2 VAL B  53      41.962 -14.137   5.578  1.00 20.60           C  
ANISOU 2751  CG2 VAL B  53     3200   2398   2228     64    -70    -79       C  
ATOM   2752  N   MET B  54      40.244 -10.998   2.712  1.00 25.15           N  
ANISOU 2752  N   MET B  54     3776   2995   2782     40   -125   -126       N  
ATOM   2753  CA  MET B  54      39.558 -10.500   1.528  1.00 26.36           C  
ANISOU 2753  CA  MET B  54     3936   3146   2931     32   -144   -142       C  
ATOM   2754  C   MET B  54      40.423  -9.358   0.978  1.00 26.89           C  
ANISOU 2754  C   MET B  54     4003   3232   2982     43   -145   -139       C  
ATOM   2755  O   MET B  54      40.487  -9.134  -0.266  1.00 25.09           O  
ANISOU 2755  O   MET B  54     3789   3001   2740     45   -153   -149       O  
ATOM   2756  CB  MET B  54      38.161  -9.973   1.862  1.00 28.76           C  
ANISOU 2756  CB  MET B  54     4223   3453   3251     15   -158   -145       C  
ATOM   2757  CG  MET B  54      37.129 -11.091   2.071  1.00 32.79           C  
ANISOU 2757  CG  MET B  54     4733   3941   3781      1   -161   -149       C  
ATOM   2758  SD  MET B  54      37.299 -11.919   3.646  1.00 41.29           S  
ANISOU 2758  SD  MET B  54     5802   5014   4873      5   -138   -133       S  
ATOM   2759  CE  MET B  54      36.554 -10.852   4.834  1.00 37.18           C  
ANISOU 2759  CE  MET B  54     5254   4510   4362     -1   -137   -123       C  
ATOM   2760  N   ALA B  55      41.166  -8.692   1.849  1.00 23.22           N  
ANISOU 2760  N   ALA B  55     3522   2783   2514     51   -136   -126       N  
ATOM   2761  CA  ALA B  55      41.808  -7.471   1.284  1.00 24.71           C  
ANISOU 2761  CA  ALA B  55     3708   2988   2692     59   -139   -125       C  
ATOM   2762  C   ALA B  55      43.243  -7.716   0.877  1.00 25.21           C  
ANISOU 2762  C   ALA B  55     3782   3050   2744     77   -125   -117       C  
ATOM   2763  O   ALA B  55      43.918  -6.804   0.412  1.00 24.47           O  
ANISOU 2763  O   ALA B  55     3684   2967   2643     86   -124   -113       O  
ATOM   2764  CB  ALA B  55      41.689  -6.297   2.190  1.00 21.78           C  
ANISOU 2764  CB  ALA B  55     3314   2635   2326     56   -141   -118       C  
ATOM   2765  N   TYR B  56      43.684  -8.952   1.007  1.00 25.35           N  
ANISOU 2765  N   TYR B  56     3813   3055   2765     83   -112   -114       N  
ATOM   2766  CA  TYR B  56      45.072  -9.234   0.728  1.00 28.41           C  
ANISOU 2766  CA  TYR B  56     4207   3439   3145    102    -96   -103       C  
ATOM   2767  C   TYR B  56      46.034  -8.420   1.581  1.00 28.36           C  
ANISOU 2767  C   TYR B  56     4181   3452   3142    110    -92    -86       C  
ATOM   2768  O   TYR B  56      47.019  -7.947   1.055  1.00 27.70           O  
ANISOU 2768  O   TYR B  56     4098   3373   3054    123    -85    -79       O  
ATOM   2769  CB  TYR B  56      45.432  -9.029  -0.753  1.00 31.36           C  
ANISOU 2769  CB  TYR B  56     4600   3808   3505    111    -95   -111       C  
ATOM   2770  CG  TYR B  56      46.284 -10.212  -1.234  1.00 35.09           C  
ANISOU 2770  CG  TYR B  56     5095   4262   3975    125    -75   -109       C  
ATOM   2771  CD1 TYR B  56      47.185 -10.832  -0.367  1.00 36.39           C  
ANISOU 2771  CD1 TYR B  56     5251   4423   4149    135    -58    -91       C  
ATOM   2772  CD2 TYR B  56      46.167 -10.706  -2.512  1.00 37.14           C  
ANISOU 2772  CD2 TYR B  56     5383   4506   4221    128    -73   -123       C  
ATOM   2773  CE1 TYR B  56      47.956 -11.905  -0.756  1.00 38.01           C  
ANISOU 2773  CE1 TYR B  56     5474   4610   4356    148    -38    -86       C  
ATOM   2774  CE2 TYR B  56      46.947 -11.776  -2.935  1.00 40.29           C  
ANISOU 2774  CE2 TYR B  56     5803   4885   4618    142    -51   -121       C  
ATOM   2775  CZ  TYR B  56      47.837 -12.379  -2.052  1.00 40.59           C  
ANISOU 2775  CZ  TYR B  56     5830   4920   4670    152    -33   -102       C  
ATOM   2776  OH  TYR B  56      48.609 -13.460  -2.467  1.00 41.49           O  
ANISOU 2776  OH  TYR B  56     5964   5013   4786    166     -9    -99       O  
ATOM   2777  N   SER B  57      45.778  -8.296   2.884  1.00 25.79           N  
ANISOU 2777  N   SER B  57     3838   3136   2824    102    -95    -79       N  
ATOM   2778  CA  SER B  57      46.567  -7.396   3.684  1.00 25.10           C  
ANISOU 2778  CA  SER B  57     3732   3067   2737    107    -95    -66       C  
ATOM   2779  C   SER B  57      47.220  -8.187   4.674  1.00 26.87           C  
ANISOU 2779  C   SER B  57     3953   3291   2965    112    -86    -50       C  
ATOM   2780  O   SER B  57      46.915  -9.339   4.753  1.00 27.66           O  
ANISOU 2780  O   SER B  57     4063   3376   3069    112    -79    -50       O  
ATOM   2781  CB  SER B  57      45.629  -6.588   4.523  1.00 25.94           C  
ANISOU 2781  CB  SER B  57     3824   3185   2845     92   -107    -71       C  
ATOM   2782  OG  SER B  57      45.656  -5.279   4.064  1.00 27.31           O  
ANISOU 2782  OG  SER B  57     3990   3370   3017     91   -115    -76       O  
ATOM   2783  N   ASN B  58      47.998  -7.556   5.577  1.00 27.98           N  
ANISOU 2783  N   ASN B  58     4077   3448   3106    115    -89    -37       N  
ATOM   2784  CA  ASN B  58      48.600  -8.312   6.631  1.00 30.73           C  
ANISOU 2784  CA  ASN B  58     4420   3797   3457    120    -82    -19       C  
ATOM   2785  C   ASN B  58      48.822  -7.452   7.833  1.00 31.01           C  
ANISOU 2785  C   ASN B  58     4439   3852   3488    114    -93    -12       C  
ATOM   2786  O   ASN B  58      49.969  -7.246   8.299  1.00 30.93           O  
ANISOU 2786  O   ASN B  58     4418   3852   3479    122    -94      3       O  
ATOM   2787  CB  ASN B  58      49.871  -9.086   6.148  1.00 33.45           C  
ANISOU 2787  CB  ASN B  58     4769   4132   3807    137    -68     -3       C  
ATOM   2788  CG  ASN B  58      50.452  -9.976   7.244  1.00 36.92           C  
ANISOU 2788  CG  ASN B  58     5203   4572   4252    143    -62     17       C  
ATOM   2789  OD1 ASN B  58      49.782 -10.263   8.242  1.00 37.28           O  
ANISOU 2789  OD1 ASN B  58     5247   4622   4296    134    -66     18       O  
ATOM   2790  ND2 ASN B  58      51.721 -10.375   7.085  1.00 40.18           N  
ANISOU 2790  ND2 ASN B  58     5612   4981   4673    158    -52     37       N  
ATOM   2791  N   CYS B  59      47.700  -6.912   8.304  1.00 29.95           N  
ANISOU 2791  N   CYS B  59     4303   3724   3351    101   -100    -25       N  
ATOM   2792  CA  CYS B  59      47.661  -6.116   9.497  1.00 31.47           C  
ANISOU 2792  CA  CYS B  59     4484   3934   3537     93   -109    -23       C  
ATOM   2793  C   CYS B  59      47.123  -6.857  10.678  1.00 30.22           C  
ANISOU 2793  C   CYS B  59     4329   3777   3375     88   -105    -16       C  
ATOM   2794  O   CYS B  59      46.024  -7.399  10.602  1.00 31.33           O  
ANISOU 2794  O   CYS B  59     4477   3906   3520     82    -99    -24       O  
ATOM   2795  CB  CYS B  59      46.771  -4.885   9.255  1.00 34.82           C  
ANISOU 2795  CB  CYS B  59     4903   4363   3960     82   -116    -41       C  
ATOM   2796  SG  CYS B  59      47.398  -3.779   7.952  1.00 32.04           S  
ANISOU 2796  SG  CYS B  59     4546   4014   3613     88   -121    -47       S  
ATOM   2797  N   LYS B  60      47.861  -6.811  11.791  1.00 29.28           N  
ANISOU 2797  N   LYS B  60     4204   3671   3248     91   -108     -2       N  
ATOM   2798  CA  LYS B  60      47.407  -7.303  13.082  1.00 28.40           C  
ANISOU 2798  CA  LYS B  60     4095   3564   3128     87   -105      5       C  
ATOM   2799  C   LYS B  60      46.415  -6.358  13.674  1.00 27.55           C  
ANISOU 2799  C   LYS B  60     3987   3465   3014     74   -109     -9       C  
ATOM   2800  O   LYS B  60      46.638  -5.149  13.755  1.00 26.24           O  
ANISOU 2800  O   LYS B  60     3815   3311   2843     70   -119    -18       O  
ATOM   2801  CB  LYS B  60      48.575  -7.329  14.045  1.00 33.55           C  
ANISOU 2801  CB  LYS B  60     4742   4232   3771     92   -113     24       C  
ATOM   2802  CG  LYS B  60      49.294  -8.647  14.156  1.00 40.53           C  
ANISOU 2802  CG  LYS B  60     5628   5110   4662    104   -104     47       C  
ATOM   2803  CD  LYS B  60      49.876  -8.766  15.584  1.00 46.95           C  
ANISOU 2803  CD  LYS B  60     6438   5940   5461    105   -112     66       C  
ATOM   2804  CE  LYS B  60      50.949  -9.867  15.631  1.00 47.37           C  
ANISOU 2804  CE  LYS B  60     6486   5989   5522    119   -107     94       C  
ATOM   2805  NZ  LYS B  60      51.760  -9.839  14.383  1.00 48.53           N  
ANISOU 2805  NZ  LYS B  60     6627   6124   5685    128   -104     94       N  
ATOM   2806  N   VAL B  61      45.279  -6.875  14.090  1.00 26.26           N  
ANISOU 2806  N   VAL B  61     3831   3295   2853     69    -99    -12       N  
ATOM   2807  CA  VAL B  61      44.253  -5.984  14.609  1.00 26.44           C  
ANISOU 2807  CA  VAL B  61     3852   3322   2871     58    -98    -25       C  
ATOM   2808  C   VAL B  61      43.867  -6.488  15.979  1.00 25.92           C  
ANISOU 2808  C   VAL B  61     3793   3261   2794     56    -90    -15       C  
ATOM   2809  O   VAL B  61      43.300  -7.566  16.108  1.00 28.67           O  
ANISOU 2809  O   VAL B  61     4146   3597   3151     58    -78     -7       O  
ATOM   2810  CB  VAL B  61      42.995  -5.974  13.716  1.00 25.25           C  
ANISOU 2810  CB  VAL B  61     3701   3154   2736     51    -94    -39       C  
ATOM   2811  CG1 VAL B  61      42.003  -4.952  14.218  1.00 25.08           C  
ANISOU 2811  CG1 VAL B  61     3675   3137   2714     40    -91    -51       C  
ATOM   2812  CG2 VAL B  61      43.386  -5.736  12.273  1.00 27.12           C  
ANISOU 2812  CG2 VAL B  61     3936   3386   2982     54   -101    -47       C  
ATOM   2813  N   SER B  62      44.163  -5.726  16.984  1.00 26.80           N  
ANISOU 2813  N   SER B  62     3905   3388   2887     54    -95    -15       N  
ATOM   2814  CA  SER B  62      44.003  -6.099  18.427  1.00 27.28           C  
ANISOU 2814  CA  SER B  62     3975   3459   2930     54    -88     -3       C  
ATOM   2815  C   SER B  62      42.999  -5.257  19.208  1.00 27.12           C  
ANISOU 2815  C   SER B  62     3959   3442   2900     45    -80    -15       C  
ATOM   2816  O   SER B  62      42.792  -4.090  18.897  1.00 26.61           O  
ANISOU 2816  O   SER B  62     3891   3380   2838     39    -85    -33       O  
ATOM   2817  CB  SER B  62      45.281  -5.631  19.115  1.00 28.29           C  
ANISOU 2817  CB  SER B  62     4103   3607   3038     57   -104      4       C  
ATOM   2818  OG  SER B  62      46.183  -6.657  19.049  1.00 36.28           O  
ANISOU 2818  OG  SER B  62     5113   4619   4052     66   -107     24       O  
ATOM   2819  N   GLY B  63      42.592  -5.756  20.362  1.00 27.94           N  
ANISOU 2819  N   GLY B  63     4074   3550   2990     47    -67     -5       N  
ATOM   2820  CA  GLY B  63      41.736  -5.010  21.249  1.00 29.60           C  
ANISOU 2820  CA  GLY B  63     4292   3763   3188     41    -56    -14       C  
ATOM   2821  C   GLY B  63      42.514  -4.787  22.533  1.00 32.59           C  
ANISOU 2821  C   GLY B  63     4684   4164   3534     42    -64     -7       C  
ATOM   2822  O   GLY B  63      43.480  -5.496  22.862  1.00 31.06           O  
ANISOU 2822  O   GLY B  63     4492   3979   3329     49    -74     10       O  
ATOM   2823  N   SER B  64      42.070  -3.796  23.281  1.00 33.90           N  
ANISOU 2823  N   SER B  64     4860   4337   3683     36    -59    -20       N  
ATOM   2824  CA  SER B  64      42.792  -3.386  24.428  1.00 35.03           C  
ANISOU 2824  CA  SER B  64     5017   4500   3792     35    -70    -19       C  
ATOM   2825  C   SER B  64      41.913  -2.578  25.352  1.00 37.52           C  
ANISOU 2825  C   SER B  64     5348   4816   4089     30    -53    -33       C  
ATOM   2826  O   SER B  64      41.113  -1.711  24.901  1.00 38.46           O  
ANISOU 2826  O   SER B  64     5462   4924   4224     24    -43    -51       O  
ATOM   2827  CB  SER B  64      43.956  -2.512  24.004  1.00 35.49           C  
ANISOU 2827  CB  SER B  64     5067   4569   3847     31    -97    -29       C  
ATOM   2828  OG  SER B  64      44.596  -2.081  25.183  1.00 39.05           O  
ANISOU 2828  OG  SER B  64     5534   5039   4264     28   -110    -29       O  
ATOM   2829  N   ASN B  65      42.096  -2.869  26.631  1.00 35.07           N  
ANISOU 2829  N   ASN B  65     5058   4520   3746     33    -50    -22       N  
ATOM   2830  CA  ASN B  65      41.634  -2.048  27.706  1.00 36.09           C  
ANISOU 2830  CA  ASN B  65     5208   4656   3847     29    -39    -35       C  
ATOM   2831  C   ASN B  65      42.749  -1.430  28.583  1.00 35.27           C  
ANISOU 2831  C   ASN B  65     5120   4575   3704     24    -65    -40       C  
ATOM   2832  O   ASN B  65      42.420  -0.894  29.625  1.00 36.43           O  
ANISOU 2832  O   ASN B  65     5290   4728   3821     22    -55    -50       O  
ATOM   2833  CB  ASN B  65      40.630  -2.827  28.598  1.00 37.81           C  
ANISOU 2833  CB  ASN B  65     5441   4868   4055     36     -8    -20       C  
ATOM   2834  CG  ASN B  65      39.333  -3.202  27.843  1.00 38.45           C  
ANISOU 2834  CG  ASN B  65     5507   4924   4176     37     18    -19       C  
ATOM   2835  OD1 ASN B  65      38.823  -4.336  27.959  1.00 38.71           O  
ANISOU 2835  OD1 ASN B  65     5538   4948   4221     45     35      0       O  
ATOM   2836  ND2 ASN B  65      38.813  -2.270  27.056  1.00 37.76           N  
ANISOU 2836  ND2 ASN B  65     5408   4825   4113     30     20    -40       N  
ATOM   2837  N   THR B  66      44.033  -1.464  28.196  1.00 34.42           N  
ANISOU 2837  N   THR B  66     5001   4479   3598     23    -96    -35       N  
ATOM   2838  CA  THR B  66      45.098  -0.762  29.000  1.00 36.75           C  
ANISOU 2838  CA  THR B  66     5309   4795   3860     17   -125    -42       C  
ATOM   2839  C   THR B  66      45.772   0.289  28.184  1.00 36.33           C  
ANISOU 2839  C   THR B  66     5239   4740   3824      8   -147    -60       C  
ATOM   2840  O   THR B  66      46.141   0.012  27.022  1.00 35.71           O  
ANISOU 2840  O   THR B  66     5136   4653   3777     11   -154    -54       O  
ATOM   2841  CB  THR B  66      46.400  -1.557  29.131  1.00 39.35           C  
ANISOU 2841  CB  THR B  66     5631   5140   4181     21   -153    -16       C  
ATOM   2842  OG1 THR B  66      46.281  -2.840  28.518  1.00 40.16           O  
ANISOU 2842  OG1 THR B  66     5718   5231   4308     33   -141      6       O  
ATOM   2843  CG2 THR B  66      47.006  -1.540  30.547  1.00 39.92           C  
ANISOU 2843  CG2 THR B  66     5727   5235   4206     19   -170     -9       C  
ATOM   2844  N   TYR B  67      46.079   1.430  28.778  1.00 36.91           N  
ANISOU 2844  N   TYR B  67     5324   4822   3875     -2   -161    -81       N  
ATOM   2845  CA  TYR B  67      46.881   2.380  28.028  1.00 37.37           C  
ANISOU 2845  CA  TYR B  67     5365   4879   3953    -10   -184    -95       C  
ATOM   2846  C   TYR B  67      48.313   1.869  27.885  1.00 37.91           C  
ANISOU 2846  C   TYR B  67     5419   4961   4023     -8   -217    -75       C  
ATOM   2847  O   TYR B  67      49.154   2.505  27.275  1.00 37.23           O  
ANISOU 2847  O   TYR B  67     5315   4875   3954    -13   -239    -80       O  
ATOM   2848  CB  TYR B  67      46.876   3.734  28.675  1.00 38.62           C  
ANISOU 2848  CB  TYR B  67     5540   5042   4092    -23   -191   -124       C  
ATOM   2849  CG  TYR B  67      45.624   4.495  28.488  1.00 40.47           C  
ANISOU 2849  CG  TYR B  67     5779   5259   4337    -26   -160   -146       C  
ATOM   2850  CD1 TYR B  67      45.309   5.086  27.238  1.00 42.44           C  
ANISOU 2850  CD1 TYR B  67     6006   5492   4627    -27   -153   -156       C  
ATOM   2851  CD2 TYR B  67      44.756   4.687  29.550  1.00 42.86           C  
ANISOU 2851  CD2 TYR B  67     6111   5561   4611    -27   -137   -156       C  
ATOM   2852  CE1 TYR B  67      44.137   5.822  27.073  1.00 44.12           C  
ANISOU 2852  CE1 TYR B  67     6221   5688   4853    -30   -125   -174       C  
ATOM   2853  CE2 TYR B  67      43.596   5.437  29.406  1.00 45.30           C  
ANISOU 2853  CE2 TYR B  67     6424   5853   4933    -29   -107   -175       C  
ATOM   2854  CZ  TYR B  67      43.281   5.988  28.161  1.00 45.33           C  
ANISOU 2854  CZ  TYR B  67     6402   5841   4980    -30   -101   -184       C  
ATOM   2855  OH  TYR B  67      42.117   6.704  28.021  1.00 49.59           O  
ANISOU 2855  OH  TYR B  67     6944   6363   5536    -32    -71   -199       O  
ATOM   2856  N   ASP B  68      48.605   0.684  28.389  1.00 38.07           N  
ANISOU 2856  N   ASP B  68     5443   4991   4028      0   -219    -48       N  
ATOM   2857  CA  ASP B  68      49.966   0.221  28.209  1.00 40.36           C  
ANISOU 2857  CA  ASP B  68     5717   5292   4324      3   -249    -26       C  
ATOM   2858  C   ASP B  68      50.270  -0.126  26.796  1.00 39.15           C  
ANISOU 2858  C   ASP B  68     5535   5125   4214     10   -246    -17       C  
ATOM   2859  O   ASP B  68      51.446  -0.177  26.410  1.00 38.79           O  
ANISOU 2859  O   ASP B  68     5472   5084   4182     11   -270     -4       O  
ATOM   2860  CB  ASP B  68      50.319  -0.914  29.158  1.00 47.27           C  
ANISOU 2860  CB  ASP B  68     6604   6182   5173     11   -255      2       C  
ATOM   2861  CG  ASP B  68      50.345  -0.459  30.597  1.00 49.29           C  
ANISOU 2861  CG  ASP B  68     6888   6456   5381      3   -267     -5       C  
ATOM   2862  OD1 ASP B  68      50.042   0.734  30.877  1.00 53.74           O  
ANISOU 2862  OD1 ASP B  68     7466   7019   5932     -8   -269    -35       O  
ATOM   2863  OD2 ASP B  68      50.666  -1.298  31.444  1.00 58.73           O  
ANISOU 2863  OD2 ASP B  68     8095   7666   6552      9   -274     18       O  
ATOM   2864  N   ASP B  69      49.210  -0.336  26.020  1.00 36.42           N  
ANISOU 2864  N   ASP B  69     5186   4760   3889     14   -218    -24       N  
ATOM   2865  CA  ASP B  69      49.339  -0.727  24.641  1.00 35.00           C  
ANISOU 2865  CA  ASP B  69     4984   4566   3746     21   -212    -17       C  
ATOM   2866  C   ASP B  69      49.636   0.440  23.726  1.00 33.83           C  
ANISOU 2866  C   ASP B  69     4820   4411   3620     15   -221    -36       C  
ATOM   2867  O   ASP B  69      49.702   0.273  22.507  1.00 34.20           O  
ANISOU 2867  O   ASP B  69     4851   4446   3697     20   -215    -34       O  
ATOM   2868  CB  ASP B  69      48.040  -1.390  24.209  1.00 38.91           C  
ANISOU 2868  CB  ASP B  69     5484   5045   4255     27   -181    -18       C  
ATOM   2869  CG  ASP B  69      47.944  -2.834  24.685  1.00 42.51           C  
ANISOU 2869  CG  ASP B  69     5946   5502   4704     37   -170      7       C  
ATOM   2870  OD1 ASP B  69      49.004  -3.400  25.039  1.00 44.52           O  
ANISOU 2870  OD1 ASP B  69     6196   5767   4950     42   -187     29       O  
ATOM   2871  OD2 ASP B  69      46.827  -3.399  24.689  1.00 42.02           O  
ANISOU 2871  OD2 ASP B  69     5890   5428   4646     40   -145      8       O  
ATOM   2872  N   LEU B  70      49.775   1.626  24.299  1.00 32.51           N  
ANISOU 2872  N   LEU B  70     4660   4251   3438      3   -234    -56       N  
ATOM   2873  CA  LEU B  70      50.334   2.782  23.594  1.00 32.89           C  
ANISOU 2873  CA  LEU B  70     4692   4296   3507     -3   -248    -71       C  
ATOM   2874  C   LEU B  70      51.809   2.591  23.363  1.00 33.12           C  
ANISOU 2874  C   LEU B  70     4704   4334   3547     -1   -274    -53       C  
ATOM   2875  O   LEU B  70      52.406   3.342  22.605  1.00 35.85           O  
ANISOU 2875  O   LEU B  70     5030   4673   3914     -3   -285    -58       O  
ATOM   2876  CB  LEU B  70      50.161   4.086  24.384  1.00 31.50           C  
ANISOU 2876  CB  LEU B  70     4529   4124   3312    -17   -255    -98       C  
ATOM   2877  CG  LEU B  70      48.753   4.663  24.468  1.00 30.87           C  
ANISOU 2877  CG  LEU B  70     4464   4034   3230    -21   -227   -120       C  
ATOM   2878  CD1 LEU B  70      48.731   5.804  25.473  1.00 29.98           C  
ANISOU 2878  CD1 LEU B  70     4369   3927   3093    -34   -235   -144       C  
ATOM   2879  CD2 LEU B  70      48.255   5.070  23.083  1.00 27.57           C  
ANISOU 2879  CD2 LEU B  70     4027   3599   2850    -18   -213   -127       C  
ATOM   2880  N   ALA B  71      52.398   1.584  23.982  1.00 32.15           N  
ANISOU 2880  N   ALA B  71     4584   4221   3409      4   -285    -28       N  
ATOM   2881  CA  ALA B  71      53.846   1.444  23.834  1.00 35.01           C  
ANISOU 2881  CA  ALA B  71     4926   4591   3783      6   -311     -8       C  
ATOM   2882  C   ALA B  71      54.230   1.184  22.386  1.00 34.42           C  
ANISOU 2882  C   ALA B  71     4828   4502   3747     17   -302      1       C  
ATOM   2883  O   ALA B  71      53.746   0.238  21.752  1.00 34.85           O  
ANISOU 2883  O   ALA B  71     4882   4546   3812     28   -280     11       O  
ATOM   2884  CB  ALA B  71      54.442   0.392  24.778  1.00 35.35           C  
ANISOU 2884  CB  ALA B  71     4975   4649   3805     12   -325     19       C  
ATOM   2885  N   GLY B  72      55.066   2.068  21.849  1.00 35.02           N  
ANISOU 2885  N   GLY B  72     4885   4576   3843     13   -318     -2       N  
ATOM   2886  CA  GLY B  72      55.544   1.901  20.475  1.00 32.97           C  
ANISOU 2886  CA  GLY B  72     4603   4302   3619     24   -309      8       C  
ATOM   2887  C   GLY B  72      54.593   2.380  19.397  1.00 32.22           C  
ANISOU 2887  C   GLY B  72     4509   4192   3540     25   -286    -10       C  
ATOM   2888  O   GLY B  72      54.875   2.217  18.236  1.00 33.88           O  
ANISOU 2888  O   GLY B  72     4705   4391   3775     35   -276     -3       O  
ATOM   2889  N   ALA B  73      53.479   3.008  19.762  1.00 33.59           N  
ANISOU 2889  N   ALA B  73     4698   4364   3699     16   -276    -35       N  
ATOM   2890  CA  ALA B  73      52.565   3.618  18.767  1.00 33.15           C  
ANISOU 2890  CA  ALA B  73     4641   4294   3660     16   -257    -53       C  
ATOM   2891  C   ALA B  73      53.276   4.652  17.890  1.00 32.10           C  
ANISOU 2891  C   ALA B  73     4486   4155   3552     14   -265    -58       C  
ATOM   2892  O   ALA B  73      54.036   5.445  18.393  1.00 33.42           O  
ANISOU 2892  O   ALA B  73     4647   4330   3720      6   -285    -62       O  
ATOM   2893  CB  ALA B  73      51.376   4.290  19.470  1.00 32.05           C  
ANISOU 2893  CB  ALA B  73     4519   4155   3503      5   -247    -78       C  
ATOM   2894  N   ASP B  74      53.042   4.602  16.585  1.00 29.98           N  
ANISOU 2894  N   ASP B  74     4209   3874   3305     23   -250    -56       N  
ATOM   2895  CA  ASP B  74      53.493   5.658  15.688  1.00 29.75           C  
ANISOU 2895  CA  ASP B  74     4162   3838   3302     23   -252    -61       C  
ATOM   2896  C   ASP B  74      52.418   6.716  15.388  1.00 27.39           C  
ANISOU 2896  C   ASP B  74     3867   3532   3007     16   -240    -85       C  
ATOM   2897  O   ASP B  74      52.747   7.867  15.143  1.00 27.39           O  
ANISOU 2897  O   ASP B  74     3855   3529   3022     10   -246    -94       O  
ATOM   2898  CB  ASP B  74      53.912   5.033  14.398  1.00 30.56           C  
ANISOU 2898  CB  ASP B  74     4254   3931   3423     39   -241    -44       C  
ATOM   2899  CG  ASP B  74      55.011   4.049  14.601  1.00 33.12           C  
ANISOU 2899  CG  ASP B  74     4573   4261   3750     47   -249    -19       C  
ATOM   2900  OD1 ASP B  74      56.125   4.575  14.829  1.00 31.52           O  
ANISOU 2900  OD1 ASP B  74     4354   4062   3558     45   -267    -10       O  
ATOM   2901  OD2 ASP B  74      54.763   2.784  14.562  1.00 36.13           O  
ANISOU 2901  OD2 ASP B  74     4964   4639   4122     56   -239     -7       O  
ATOM   2902  N   VAL B  75      51.153   6.325  15.480  1.00 24.78           N  
ANISOU 2902  N   VAL B  75     3551   3198   2665     15   -224    -94       N  
ATOM   2903  CA  VAL B  75      50.025   7.208  15.311  1.00 23.42           C  
ANISOU 2903  CA  VAL B  75     3383   3018   2496      8   -211   -114       C  
ATOM   2904  C   VAL B  75      49.014   6.883  16.364  1.00 23.12           C  
ANISOU 2904  C   VAL B  75     3364   2983   2436      2   -203   -124       C  
ATOM   2905  O   VAL B  75      48.683   5.703  16.629  1.00 22.95           O  
ANISOU 2905  O   VAL B  75     3352   2963   2402      7   -197   -113       O  
ATOM   2906  CB  VAL B  75      49.417   7.028  13.894  1.00 23.22           C  
ANISOU 2906  CB  VAL B  75     3351   2981   2489     17   -196   -112       C  
ATOM   2907  CG1 VAL B  75      48.159   7.876  13.741  1.00 23.71           C  
ANISOU 2907  CG1 VAL B  75     3415   3036   2557     11   -183   -129       C  
ATOM   2908  CG2 VAL B  75      50.460   7.493  12.892  1.00 22.49           C  
ANISOU 2908  CG2 VAL B  75     3240   2886   2417     24   -202   -102       C  
ATOM   2909  N   VAL B  76      48.519   7.918  17.004  1.00 22.89           N  
ANISOU 2909  N   VAL B  76     3340   2953   2402     -8   -201   -143       N  
ATOM   2910  CA  VAL B  76      47.399   7.742  17.892  1.00 22.02           C  
ANISOU 2910  CA  VAL B  76     3249   2843   2274    -13   -187   -153       C  
ATOM   2911  C   VAL B  76      46.257   8.573  17.524  1.00 20.73           C  
ANISOU 2911  C   VAL B  76     3083   2668   2124    -16   -169   -168       C  
ATOM   2912  O   VAL B  76      46.376   9.808  17.298  1.00 20.88           O  
ANISOU 2912  O   VAL B  76     3093   2682   2157    -22   -170   -181       O  
ATOM   2913  CB  VAL B  76      47.769   8.186  19.314  1.00 22.62           C  
ANISOU 2913  CB  VAL B  76     3339   2929   2324    -23   -198   -163       C  
ATOM   2914  CG1 VAL B  76      46.627   7.977  20.273  1.00 21.79           C  
ANISOU 2914  CG1 VAL B  76     3256   2824   2199    -26   -179   -172       C  
ATOM   2915  CG2 VAL B  76      49.074   7.522  19.728  1.00 23.60           C  
ANISOU 2915  CG2 VAL B  76     3462   3067   2436    -20   -221   -147       C  
ATOM   2916  N   ILE B  77      45.116   7.958  17.584  1.00 20.51           N  
ANISOU 2916  N   ILE B  77     3064   2635   2094    -14   -151   -167       N  
ATOM   2917  CA  ILE B  77      43.931   8.655  17.187  1.00 21.61           C  
ANISOU 2917  CA  ILE B  77     3198   2761   2249    -17   -133   -177       C  
ATOM   2918  C   ILE B  77      42.934   8.688  18.315  1.00 22.80           C  
ANISOU 2918  C   ILE B  77     3367   2910   2386    -22   -115   -187       C  
ATOM   2919  O   ILE B  77      42.557   7.653  18.859  1.00 22.57           O  
ANISOU 2919  O   ILE B  77     3349   2884   2342    -19   -108   -178       O  
ATOM   2920  CB  ILE B  77      43.296   7.983  15.969  1.00 20.28           C  
ANISOU 2920  CB  ILE B  77     3020   2584   2100     -9   -126   -166       C  
ATOM   2921  CG1 ILE B  77      44.337   7.956  14.854  1.00 19.64           C  
ANISOU 2921  CG1 ILE B  77     2926   2506   2031     -3   -141   -157       C  
ATOM   2922  CG2 ILE B  77      41.990   8.705  15.641  1.00 20.28           C  
ANISOU 2922  CG2 ILE B  77     3015   2572   2119    -13   -108   -175       C  
ATOM   2923  CD1 ILE B  77      43.900   7.440  13.468  1.00 20.21           C  
ANISOU 2923  CD1 ILE B  77     2989   2569   2120      3   -137   -148       C  
ATOM   2924  N   VAL B  78      42.511   9.907  18.670  1.00 23.54           N  
ANISOU 2924  N   VAL B  78     3461   2997   2484    -29   -105   -204       N  
ATOM   2925  CA  VAL B  78      41.737  10.017  19.862  1.00 24.18           C  
ANISOU 2925  CA  VAL B  78     3562   3077   2548    -33    -87   -214       C  
ATOM   2926  C   VAL B  78      40.284  10.437  19.572  1.00 24.55           C  
ANISOU 2926  C   VAL B  78     3603   3107   2616    -33    -60   -218       C  
ATOM   2927  O   VAL B  78      39.983  11.609  19.471  1.00 24.83           O  
ANISOU 2927  O   VAL B  78     3632   3133   2666    -38    -52   -231       O  
ATOM   2928  CB  VAL B  78      42.419  10.892  20.887  1.00 23.99           C  
ANISOU 2928  CB  VAL B  78     3552   3059   2503    -42    -96   -231       C  
ATOM   2929  CG1 VAL B  78      41.597  10.889  22.168  1.00 24.91           C  
ANISOU 2929  CG1 VAL B  78     3694   3174   2596    -45    -75   -240       C  
ATOM   2930  CG2 VAL B  78      43.835  10.360  21.108  1.00 23.83           C  
ANISOU 2930  CG2 VAL B  78     3534   3056   2465    -42   -125   -222       C  
ATOM   2931  N   THR B  79      39.400   9.437  19.528  1.00 25.69           N  
ANISOU 2931  N   THR B  79     3749   3247   2764    -28    -47   -205       N  
ATOM   2932  CA  THR B  79      37.949   9.653  19.521  1.00 25.43           C  
ANISOU 2932  CA  THR B  79     3712   3198   2749    -29    -20   -206       C  
ATOM   2933  C   THR B  79      37.241   9.483  20.886  1.00 26.63           C  
ANISOU 2933  C   THR B  79     3887   3349   2882    -29      3   -210       C  
ATOM   2934  O   THR B  79      36.105   9.866  21.006  1.00 26.84           O  
ANISOU 2934  O   THR B  79     3909   3361   2925    -30     28   -211       O  
ATOM   2935  CB  THR B  79      37.252   8.758  18.498  1.00 24.25           C  
ANISOU 2935  CB  THR B  79     3547   3043   2623    -24    -20   -189       C  
ATOM   2936  OG1 THR B  79      37.520   7.400  18.852  1.00 25.43           O  
ANISOU 2936  OG1 THR B  79     3707   3199   2754    -20    -25   -177       O  
ATOM   2937  CG2 THR B  79      37.819   8.989  17.112  1.00 23.96           C  
ANISOU 2937  CG2 THR B  79     3491   3006   2604    -22    -40   -186       C  
ATOM   2938  N   ALA B  80      37.893   9.010  21.945  1.00 29.78           N  
ANISOU 2938  N   ALA B  80     4308   3761   3246    -29     -2   -210       N  
ATOM   2939  CA  ALA B  80      37.103   8.732  23.172  1.00 30.19           C  
ANISOU 2939  CA  ALA B  80     4381   3809   3278    -28     23   -211       C  
ATOM   2940  C   ALA B  80      36.604  10.018  23.831  1.00 32.54           C  
ANISOU 2940  C   ALA B  80     4690   4098   3575    -33     45   -231       C  
ATOM   2941  O   ALA B  80      37.217  11.087  23.689  1.00 32.74           O  
ANISOU 2941  O   ALA B  80     4714   4124   3601    -39     34   -247       O  
ATOM   2942  CB  ALA B  80      37.856   7.890  24.167  1.00 29.91           C  
ANISOU 2942  CB  ALA B  80     4368   3791   3203    -25     13   -204       C  
ATOM   2943  N   GLY B  81      35.464   9.920  24.513  1.00 33.88           N  
ANISOU 2943  N   GLY B  81     4871   4257   3745    -29     79   -229       N  
ATOM   2944  CA  GLY B  81      34.930  11.044  25.317  1.00 36.00           C  
ANISOU 2944  CA  GLY B  81     5156   4515   4008    -32    106   -248       C  
ATOM   2945  C   GLY B  81      33.417  11.062  25.464  1.00 35.98           C  
ANISOU 2945  C   GLY B  81     5148   4491   4029    -28    146   -240       C  
ATOM   2946  O   GLY B  81      32.704  10.491  24.641  1.00 32.81           O  
ANISOU 2946  O   GLY B  81     4723   4081   3661    -24    150   -222       O  
ATOM   2947  N   PHE B  82      32.945  11.692  26.546  1.00 38.62           N  
ANISOU 2947  N   PHE B  82     5507   4818   4347    -27    177   -254       N  
ATOM   2948  CA  PHE B  82      31.518  11.988  26.757  1.00 35.42           C  
ANISOU 2948  CA  PHE B  82     5098   4390   3969    -22    220   -249       C  
ATOM   2949  C   PHE B  82      30.957  12.812  25.599  1.00 36.59           C  
ANISOU 2949  C   PHE B  82     5211   4521   4167    -25    224   -248       C  
ATOM   2950  O   PHE B  82      31.569  13.797  25.184  1.00 34.67           O  
ANISOU 2950  O   PHE B  82     4962   4279   3929    -31    208   -265       O  
ATOM   2951  CB  PHE B  82      31.378  12.742  28.026  1.00 35.85           C  
ANISOU 2951  CB  PHE B  82     5186   4440   3993    -23    249   -268       C  
ATOM   2952  CG  PHE B  82      31.856  11.964  29.216  1.00 38.59           C  
ANISOU 2952  CG  PHE B  82     5569   4804   4288    -20    247   -268       C  
ATOM   2953  CD1 PHE B  82      31.090  10.917  29.737  1.00 39.48           C  
ANISOU 2953  CD1 PHE B  82     5688   4913   4396    -10    272   -246       C  
ATOM   2954  CD2 PHE B  82      33.079  12.207  29.772  1.00 37.75           C  
ANISOU 2954  CD2 PHE B  82     5487   4716   4138    -26    219   -285       C  
ATOM   2955  CE1 PHE B  82      31.536  10.147  30.818  1.00 39.17           C  
ANISOU 2955  CE1 PHE B  82     5682   4891   4309     -6    270   -242       C  
ATOM   2956  CE2 PHE B  82      33.522  11.453  30.873  1.00 39.22           C  
ANISOU 2956  CE2 PHE B  82     5706   4919   4274    -23    215   -282       C  
ATOM   2957  CZ  PHE B  82      32.754  10.422  31.387  1.00 37.59           C  
ANISOU 2957  CZ  PHE B  82     5508   4711   4063    -12    241   -259       C  
ATOM   2958  N   THR B  83      29.822  12.366  25.067  1.00 37.07           N  
ANISOU 2958  N   THR B  83     5249   4569   4267    -20    241   -228       N  
ATOM   2959  CA  THR B  83      29.072  13.108  24.037  1.00 40.50           C  
ANISOU 2959  CA  THR B  83     5650   4985   4751    -21    248   -223       C  
ATOM   2960  C   THR B  83      27.579  13.395  24.383  1.00 43.34           C  
ANISOU 2960  C   THR B  83     6002   5320   5144    -16    295   -213       C  
ATOM   2961  O   THR B  83      27.066  14.417  23.957  1.00 41.70           O  
ANISOU 2961  O   THR B  83     5777   5097   4969    -17    309   -216       O  
ATOM   2962  CB  THR B  83      29.110  12.434  22.673  1.00 37.59           C  
ANISOU 2962  CB  THR B  83     5250   4621   4410    -23    218   -205       C  
ATOM   2963  OG1 THR B  83      28.757  11.070  22.845  1.00 38.36           O  
ANISOU 2963  OG1 THR B  83     5349   4721   4503    -19    218   -187       O  
ATOM   2964  CG2 THR B  83      30.495  12.495  22.065  1.00 38.25           C  
ANISOU 2964  CG2 THR B  83     5334   4724   4475    -27    176   -215       C  
ATOM   2965  N   LYS B  84      26.897  12.550  25.167  1.00 50.56           N  
ANISOU 2965  N   LYS B  84     6928   6230   6051    -10    320   -199       N  
ATOM   2966  CA  LYS B  84      25.459  12.808  25.477  1.00 55.78           C  
ANISOU 2966  CA  LYS B  84     7579   6866   6748     -4    367   -187       C  
ATOM   2967  C   LYS B  84      25.095  13.277  26.915  1.00 57.62           C  
ANISOU 2967  C   LYS B  84     7846   7088   6955      1    413   -198       C  
ATOM   2968  O   LYS B  84      25.880  13.139  27.854  1.00 59.09           O  
ANISOU 2968  O   LYS B  84     8071   7290   7090      1    410   -214       O  
ATOM   2969  CB  LYS B  84      24.556  11.665  24.963  1.00 59.12           C  
ANISOU 2969  CB  LYS B  84     7976   7281   7205     -1    368   -157       C  
ATOM   2970  CG  LYS B  84      24.504  10.380  25.791  1.00 62.27           C  
ANISOU 2970  CG  LYS B  84     8394   7687   7578      3    376   -144       C  
ATOM   2971  CD  LYS B  84      23.554   9.329  25.174  1.00 66.54           C  
ANISOU 2971  CD  LYS B  84     8904   8216   8161      4    376   -115       C  
ATOM   2972  CE  LYS B  84      22.072   9.493  25.586  1.00 71.05           C  
ANISOU 2972  CE  LYS B  84     9461   8759   8773     11    425    -97       C  
ATOM   2973  NZ  LYS B  84      21.056   8.953  24.618  1.00 64.83           N  
ANISOU 2973  NZ  LYS B  84     8631   7956   8044      8    419    -72       N  
ATOM   2974  N   ALA B  85      23.901  13.858  27.041  1.00 61.23           N  
ANISOU 2974  N   ALA B  85     8292   7521   7452      6    456   -190       N  
ATOM   2975  CA  ALA B  85      23.355  14.393  28.298  1.00 61.90           C  
ANISOU 2975  CA  ALA B  85     8407   7590   7521     14    507   -199       C  
ATOM   2976  C   ALA B  85      23.416  13.412  29.462  1.00 61.95           C  
ANISOU 2976  C   ALA B  85     8447   7605   7484     21    523   -194       C  
ATOM   2977  O   ALA B  85      22.939  12.287  29.329  1.00 60.31           O  
ANISOU 2977  O   ALA B  85     8226   7398   7291     25    523   -168       O  
ATOM   2978  CB  ALA B  85      21.920  14.823  28.064  1.00 60.66           C  
ANISOU 2978  CB  ALA B  85     8220   7402   7423     20    550   -180       C  
ATOM   2979  N   GLU B  92      16.886  22.848  28.618  1.00 79.74           N  
ANISOU 2979  N   GLU B  92    10576   9624  10096     51    846   -196       N  
ATOM   2980  CA  GLU B  92      17.647  21.644  28.922  1.00 87.63           C  
ANISOU 2980  CA  GLU B  92    11600  10654  11039     47    808   -201       C  
ATOM   2981  C   GLU B  92      19.024  21.879  29.573  1.00 91.80           C  
ANISOU 2981  C   GLU B  92    12178  11204  11495     39    784   -242       C  
ATOM   2982  O   GLU B  92      19.286  22.931  30.173  1.00 98.74           O  
ANISOU 2982  O   GLU B  92    13087  12071  12357     39    809   -272       O  
ATOM   2983  CB  GLU B  92      17.772  20.764  27.667  1.00 82.75           C  
ANISOU 2983  CB  GLU B  92    10939  10056  10444     40    752   -176       C  
ATOM   2984  CG  GLU B  92      16.548  19.909  27.416  1.00 86.43           C  
ANISOU 2984  CG  GLU B  92    11370  10509  10958     46    769   -136       C  
ATOM   2985  CD  GLU B  92      15.855  19.490  28.711  1.00 89.88           C  
ANISOU 2985  CD  GLU B  92    11837  10931  11383     59    825   -129       C  
ATOM   2986  OE1 GLU B  92      15.088  20.309  29.267  1.00 92.77           O  
ANISOU 2986  OE1 GLU B  92    12206  11267  11772     68    883   -129       O  
ATOM   2987  OE2 GLU B  92      16.083  18.356  29.184  1.00 90.59           O  
ANISOU 2987  OE2 GLU B  92    11945  11037  11437     60    815   -125       O  
ATOM   2988  N   TRP B  93      19.879  20.865  29.448  1.00 86.82           N  
ANISOU 2988  N   TRP B  93    11557  10606  10824     33    735   -244       N  
ATOM   2989  CA  TRP B  93      21.250  20.843  29.977  1.00 73.85           C  
ANISOU 2989  CA  TRP B  93     9957   8988   9113     24    701   -277       C  
ATOM   2990  C   TRP B  93      22.203  21.521  29.015  1.00 65.70           C  
ANISOU 2990  C   TRP B  93     8906   7967   8087     12    654   -292       C  
ATOM   2991  O   TRP B  93      21.869  21.812  27.849  1.00 64.23           O  
ANISOU 2991  O   TRP B  93     8675   7775   7954     10    641   -275       O  
ATOM   2992  CB  TRP B  93      21.609  19.372  30.329  1.00 70.79           C  
ANISOU 2992  CB  TRP B  93     9584   8627   8686     25    677   -265       C  
ATOM   2993  CG  TRP B  93      22.951  18.784  29.913  1.00 64.71           C  
ANISOU 2993  CG  TRP B  93     8818   7890   7876     15    613   -275       C  
ATOM   2994  CD1 TRP B  93      24.009  18.428  30.754  1.00 63.53           C  
ANISOU 2994  CD1 TRP B  93     8713   7764   7660     11    592   -296       C  
ATOM   2995  CD2 TRP B  93      23.403  18.397  28.547  1.00 60.99           C  
ANISOU 2995  CD2 TRP B  93     8308   7434   7431      7    560   -261       C  
ATOM   2996  NE1 TRP B  93      25.059  17.907  30.032  1.00 60.60           N  
ANISOU 2996  NE1 TRP B  93     8329   7418   7275      2    533   -296       N  
ATOM   2997  CE2 TRP B  93      24.773  17.861  28.707  1.00 58.54           C  
ANISOU 2997  CE2 TRP B  93     8020   7155   7066      0    513   -277       C  
ATOM   2998  CE3 TRP B  93      22.852  18.472  27.266  1.00 56.23           C  
ANISOU 2998  CE3 TRP B  93     7655   6823   6886      6    547   -239       C  
ATOM   2999  CZ2 TRP B  93      25.532  17.423  27.622  1.00 51.55           C  
ANISOU 2999  CZ2 TRP B  93     7110   6289   6187     -6    460   -270       C  
ATOM   3000  CZ3 TRP B  93      23.629  18.022  26.180  1.00 54.49           C  
ANISOU 3000  CZ3 TRP B  93     7412   6624   6667     -1    492   -234       C  
ATOM   3001  CH2 TRP B  93      24.932  17.505  26.358  1.00 54.63           C  
ANISOU 3001  CH2 TRP B  93     7454   6669   6633     -7    451   -249       C  
ATOM   3002  N   ASN B  94      23.401  21.792  29.495  1.00 58.83           N  
ANISOU 3002  N   ASN B  94     8071   7114   7164      4    629   -324       N  
ATOM   3003  CA  ASN B  94      24.354  22.531  28.709  1.00 54.54           C  
ANISOU 3003  CA  ASN B  94     7515   6579   6626     -6    589   -341       C  
ATOM   3004  C   ASN B  94      25.544  21.690  28.162  1.00 50.80           C  
ANISOU 3004  C   ASN B  94     7037   6140   6124    -15    525   -340       C  
ATOM   3005  O   ASN B  94      26.380  21.229  28.908  1.00 47.47           O  
ANISOU 3005  O   ASN B  94     6650   5738   5647    -18    507   -356       O  
ATOM   3006  CB  ASN B  94      24.806  23.709  29.570  1.00 56.02           C  
ANISOU 3006  CB  ASN B  94     7740   6755   6787    -11    609   -380       C  
ATOM   3007  CG  ASN B  94      25.442  24.811  28.767  1.00 60.26           C  
ANISOU 3007  CG  ASN B  94     8257   7287   7349    -20    587   -395       C  
ATOM   3008  OD1 ASN B  94      26.345  24.569  27.961  1.00 61.67           O  
ANISOU 3008  OD1 ASN B  94     8418   7487   7524    -28    535   -393       O  
ATOM   3009  ND2 ASN B  94      24.984  26.040  28.987  1.00 60.84           N  
ANISOU 3009  ND2 ASN B  94     8335   7332   7449    -19    627   -410       N  
ATOM   3010  N   ARG B  95      25.648  21.506  26.849  1.00 51.14           N  
ANISOU 3010  N   ARG B  95     7038   6191   6202    -17    492   -321       N  
ATOM   3011  CA  ARG B  95      26.802  20.773  26.297  1.00 49.59           C  
ANISOU 3011  CA  ARG B  95     6838   6024   5980    -24    435   -321       C  
ATOM   3012  C   ARG B  95      28.191  21.181  26.882  1.00 45.87           C  
ANISOU 3012  C   ARG B  95     6400   5568   5459    -34    408   -353       C  
ATOM   3013  O   ARG B  95      29.117  20.364  26.923  1.00 41.85           O  
ANISOU 3013  O   ARG B  95     5901   5084   4914    -38    370   -354       O  
ATOM   3014  CB  ARG B  95      26.824  20.881  24.790  1.00 49.69           C  
ANISOU 3014  CB  ARG B  95     6804   6038   6036    -26    406   -303       C  
ATOM   3015  CG  ARG B  95      27.521  19.711  24.132  1.00 54.83           C  
ANISOU 3015  CG  ARG B  95     7445   6715   6671    -29    359   -289       C  
ATOM   3016  CD  ARG B  95      26.952  19.498  22.731  1.00 60.43           C  
ANISOU 3016  CD  ARG B  95     8110   7421   7429    -27    344   -262       C  
ATOM   3017  NE  ARG B  95      25.491  19.619  22.745  1.00 70.66           N  
ANISOU 3017  NE  ARG B  95     9386   8692   8766    -20    384   -243       N  
ATOM   3018  CZ  ARG B  95      24.647  18.657  22.369  1.00 74.40           C  
ANISOU 3018  CZ  ARG B  95     9840   9165   9262    -16    385   -216       C  
ATOM   3019  NH1 ARG B  95      25.119  17.497  21.902  1.00 67.27           N  
ANISOU 3019  NH1 ARG B  95     8933   8282   8343    -18    348   -206       N  
ATOM   3020  NH2 ARG B  95      23.331  18.866  22.441  1.00 72.00           N  
ANISOU 3020  NH2 ARG B  95     9518   8838   9001    -11    423   -198       N  
ATOM   3021  N   ASP B  96      28.319  22.442  27.288  1.00 41.83           N  
ANISOU 3021  N   ASP B  96     5904   5041   4949    -38    428   -380       N  
ATOM   3022  CA  ASP B  96      29.518  22.949  27.959  1.00 44.64           C  
ANISOU 3022  CA  ASP B  96     6292   5406   5260    -49    406   -413       C  
ATOM   3023  C   ASP B  96      29.916  22.147  29.197  1.00 42.12           C  
ANISOU 3023  C   ASP B  96     6018   5105   4878    -49    403   -423       C  
ATOM   3024  O   ASP B  96      31.088  22.146  29.551  1.00 43.12           O  
ANISOU 3024  O   ASP B  96     6166   5250   4965    -58    368   -441       O  
ATOM   3025  CB  ASP B  96      29.328  24.416  28.423  1.00 45.35           C  
ANISOU 3025  CB  ASP B  96     6397   5470   5361    -52    440   -441       C  
ATOM   3026  CG  ASP B  96      29.554  25.457  27.307  1.00 46.02           C  
ANISOU 3026  CG  ASP B  96     6446   5544   5495    -57    428   -442       C  
ATOM   3027  OD1 ASP B  96      29.748  25.116  26.114  1.00 44.64           O  
ANISOU 3027  OD1 ASP B  96     6233   5379   5348    -56    398   -420       O  
ATOM   3028  OD2 ASP B  96      29.529  26.662  27.654  1.00 48.82           O  
ANISOU 3028  OD2 ASP B  96     6812   5876   5859    -61    452   -467       O  
ATOM   3029  N   ASP B  97      28.944  21.506  29.856  1.00 42.22           N  
ANISOU 3029  N   ASP B  97     6046   5111   4884    -38    440   -409       N  
ATOM   3030  CA  ASP B  97      29.151  20.717  31.097  1.00 43.22           C  
ANISOU 3030  CA  ASP B  97     6217   5253   4952    -36    444   -414       C  
ATOM   3031  C   ASP B  97      30.105  19.505  30.897  1.00 42.93           C  
ANISOU 3031  C   ASP B  97     6177   5248   4884    -39    394   -401       C  
ATOM   3032  O   ASP B  97      30.695  18.988  31.868  1.00 43.09           O  
ANISOU 3032  O   ASP B  97     6234   5286   4850    -40    383   -410       O  
ATOM   3033  CB  ASP B  97      27.789  20.269  31.713  1.00 44.67           C  
ANISOU 3033  CB  ASP B  97     6409   5420   5144    -22    500   -396       C  
ATOM   3034  CG  ASP B  97      26.824  21.480  32.007  1.00 49.00           C  
ANISOU 3034  CG  ASP B  97     6961   5933   5723    -17    556   -408       C  
ATOM   3035  OD1 ASP B  97      27.316  22.511  32.483  1.00 48.76           O  
ANISOU 3035  OD1 ASP B  97     6957   5895   5673    -25    560   -441       O  
ATOM   3036  OD2 ASP B  97      25.584  21.422  31.755  1.00 51.29           O  
ANISOU 3036  OD2 ASP B  97     7228   6202   6058     -6    596   -385       O  
ATOM   3037  N   LEU B  98      30.278  19.095  29.638  1.00 39.38           N  
ANISOU 3037  N   LEU B  98     5685   4806   4470    -39    363   -380       N  
ATOM   3038  CA  LEU B  98      31.077  17.916  29.285  1.00 37.92           C  
ANISOU 3038  CA  LEU B  98     5493   4649   4266    -40    320   -364       C  
ATOM   3039  C   LEU B  98      32.535  18.259  29.225  1.00 36.74           C  
ANISOU 3039  C   LEU B  98     5351   4516   4089    -52    274   -384       C  
ATOM   3040  O   LEU B  98      33.381  17.363  29.247  1.00 39.15           O  
ANISOU 3040  O   LEU B  98     5661   4845   4368    -53    239   -376       O  
ATOM   3041  CB  LEU B  98      30.645  17.354  27.923  1.00 36.48           C  
ANISOU 3041  CB  LEU B  98     5264   4465   4132    -36    307   -336       C  
ATOM   3042  CG  LEU B  98      29.245  16.738  27.814  1.00 36.84           C  
ANISOU 3042  CG  LEU B  98     5293   4494   4209    -26    343   -310       C  
ATOM   3043  CD1 LEU B  98      28.978  16.300  26.387  1.00 35.91           C  
ANISOU 3043  CD1 LEU B  98     5130   4376   4136    -25    321   -286       C  
ATOM   3044  CD2 LEU B  98      29.084  15.534  28.722  1.00 34.03           C  
ANISOU 3044  CD2 LEU B  98     4962   4149   3817    -19    352   -297       C  
ATOM   3045  N   LEU B  99      32.835  19.552  29.118  1.00 36.08           N  
ANISOU 3045  N   LEU B  99     5268   4421   4019    -60    275   -408       N  
ATOM   3046  CA  LEU B  99      34.200  20.033  28.934  1.00 35.34           C  
ANISOU 3046  CA  LEU B  99     5176   4341   3911    -72    232   -426       C  
ATOM   3047  C   LEU B  99      35.214  19.662  30.048  1.00 36.17           C  
ANISOU 3047  C   LEU B  99     5320   4467   3954    -79    206   -442       C  
ATOM   3048  O   LEU B  99      36.312  19.168  29.744  1.00 35.64           O  
ANISOU 3048  O   LEU B  99     5245   4420   3873    -84    162   -436       O  
ATOM   3049  CB  LEU B  99      34.161  21.549  28.769  1.00 37.06           C  
ANISOU 3049  CB  LEU B  99     5389   4536   4155    -79    246   -450       C  
ATOM   3050  CG  LEU B  99      33.720  22.053  27.404  1.00 38.25           C  
ANISOU 3050  CG  LEU B  99     5494   4673   4367    -76    250   -436       C  
ATOM   3051  CD1 LEU B  99      33.486  23.547  27.535  1.00 40.00           C  
ANISOU 3051  CD1 LEU B  99     5718   4868   4610    -81    276   -460       C  
ATOM   3052  CD2 LEU B  99      34.766  21.796  26.333  1.00 38.59           C  
ANISOU 3052  CD2 LEU B  99     5508   4733   4421    -80    202   -425       C  
ATOM   3053  N   PRO B 100      34.864  19.909  31.338  1.00 35.35           N  
ANISOU 3053  N   PRO B 100     5259   4357   3812    -79    234   -460       N  
ATOM   3054  CA  PRO B 100      35.815  19.462  32.328  1.00 36.86           C  
ANISOU 3054  CA  PRO B 100     5486   4571   3944    -85    205   -471       C  
ATOM   3055  C   PRO B 100      35.940  17.958  32.338  1.00 36.54           C  
ANISOU 3055  C   PRO B 100     5443   4554   3886    -77    189   -441       C  
ATOM   3056  O   PRO B 100      37.008  17.450  32.675  1.00 36.09           O  
ANISOU 3056  O   PRO B 100     5397   4520   3793    -82    150   -440       O  
ATOM   3057  CB  PRO B 100      35.213  19.934  33.698  1.00 37.66           C  
ANISOU 3057  CB  PRO B 100     5638   4662   4008    -84    246   -494       C  
ATOM   3058  CG  PRO B 100      33.934  20.666  33.384  1.00 38.04           C  
ANISOU 3058  CG  PRO B 100     5673   4678   4101    -77    298   -495       C  
ATOM   3059  CD  PRO B 100      33.805  20.785  31.886  1.00 35.05           C  
ANISOU 3059  CD  PRO B 100     5239   4292   3784    -75    287   -476       C  
ATOM   3060  N   LEU B 101      34.878  17.229  31.983  1.00 37.11           N  
ANISOU 3060  N   LEU B 101     5498   4618   3983    -64    219   -414       N  
ATOM   3061  CA  LEU B 101      34.979  15.755  32.096  1.00 37.27           C  
ANISOU 3061  CA  LEU B 101     5517   4658   3984    -56    206   -386       C  
ATOM   3062  C   LEU B 101      35.926  15.259  31.023  1.00 37.28           C  
ANISOU 3062  C   LEU B 101     5485   4674   4003    -59    159   -372       C  
ATOM   3063  O   LEU B 101      36.755  14.408  31.287  1.00 38.80           O  
ANISOU 3063  O   LEU B 101     5685   4889   4166    -60    129   -362       O  
ATOM   3064  CB  LEU B 101      33.626  15.059  31.966  1.00 37.84           C  
ANISOU 3064  CB  LEU B 101     5577   4716   4081    -42    247   -361       C  
ATOM   3065  CG  LEU B 101      32.572  15.526  32.974  1.00 44.60           C  
ANISOU 3065  CG  LEU B 101     6464   5554   4926    -36    301   -371       C  
ATOM   3066  CD1 LEU B 101      31.224  14.847  32.713  1.00 44.00           C  
ANISOU 3066  CD1 LEU B 101     6369   5462   4885    -23    340   -343       C  
ATOM   3067  CD2 LEU B 101      33.061  15.355  34.419  1.00 42.08           C  
ANISOU 3067  CD2 LEU B 101     6198   5250   4539    -37    301   -386       C  
ATOM   3068  N   ASN B 102      35.802  15.808  29.815  1.00 37.02           N  
ANISOU 3068  N   ASN B 102     5416   4630   4020    -61    155   -370       N  
ATOM   3069  CA  ASN B 102      36.637  15.374  28.717  1.00 36.01           C  
ANISOU 3069  CA  ASN B 102     5255   4513   3911    -63    115   -356       C  
ATOM   3070  C   ASN B 102      38.029  15.948  28.891  1.00 37.36           C  
ANISOU 3070  C   ASN B 102     5434   4697   4061    -75     77   -375       C  
ATOM   3071  O   ASN B 102      38.994  15.342  28.491  1.00 36.89           O  
ANISOU 3071  O   ASN B 102     5363   4655   3996    -76     40   -363       O  
ATOM   3072  CB  ASN B 102      36.017  15.735  27.365  1.00 34.06           C  
ANISOU 3072  CB  ASN B 102     4968   4250   3721    -60    124   -346       C  
ATOM   3073  CG  ASN B 102      34.847  14.815  27.000  1.00 33.59           C  
ANISOU 3073  CG  ASN B 102     4894   4183   3684    -49    148   -320       C  
ATOM   3074  OD1 ASN B 102      34.831  13.634  27.330  1.00 35.87           O  
ANISOU 3074  OD1 ASN B 102     5191   4484   3953    -44    145   -303       O  
ATOM   3075  ND2 ASN B 102      33.884  15.344  26.342  1.00 32.55           N  
ANISOU 3075  ND2 ASN B 102     4740   4031   3594    -47    172   -316       N  
ATOM   3076  N   ASN B 103      38.155  17.078  29.576  1.00 40.46           N  
ANISOU 3076  N   ASN B 103     5849   5081   4439    -84     84   -404       N  
ATOM   3077  CA  ASN B 103      39.498  17.497  30.033  1.00 40.63           C  
ANISOU 3077  CA  ASN B 103     5886   5118   4433    -97     45   -423       C  
ATOM   3078  C   ASN B 103      40.182  16.417  30.857  1.00 39.57           C  
ANISOU 3078  C   ASN B 103     5775   5009   4251    -96     20   -412       C  
ATOM   3079  O   ASN B 103      41.379  16.144  30.688  1.00 38.96           O  
ANISOU 3079  O   ASN B 103     5689   4949   4165   -102    -21   -407       O  
ATOM   3080  CB  ASN B 103      39.426  18.783  30.821  1.00 41.57           C  
ANISOU 3080  CB  ASN B 103     6032   5222   4538   -107     60   -458       C  
ATOM   3081  CG  ASN B 103      40.746  19.484  30.906  1.00 45.19           C  
ANISOU 3081  CG  ASN B 103     6493   5688   4987   -123     18   -478       C  
ATOM   3082  OD1 ASN B 103      41.757  19.033  30.383  1.00 46.19           O  
ANISOU 3082  OD1 ASN B 103     6599   5831   5119   -125    -21   -464       O  
ATOM   3083  ND2 ASN B 103      40.739  20.632  31.556  1.00 48.19           N  
ANISOU 3083  ND2 ASN B 103     6897   6054   5357   -133     28   -511       N  
ATOM   3084  N   LYS B 104      39.426  15.791  31.752  1.00 41.87           N  
ANISOU 3084  N   LYS B 104     6094   5302   4512    -88     48   -406       N  
ATOM   3085  CA  LYS B 104      40.001  14.749  32.647  1.00 41.90           C  
ANISOU 3085  CA  LYS B 104     6122   5330   4465    -86     28   -394       C  
ATOM   3086  C   LYS B 104      40.498  13.522  31.854  1.00 41.30           C  
ANISOU 3086  C   LYS B 104     6016   5269   4405    -79      2   -361       C  
ATOM   3087  O   LYS B 104      41.487  12.898  32.205  1.00 40.40           O  
ANISOU 3087  O   LYS B 104     5909   5177   4263    -81    -31   -352       O  
ATOM   3088  CB  LYS B 104      38.980  14.306  33.686  1.00 41.51           C  
ANISOU 3088  CB  LYS B 104     6106   5277   4385    -76     68   -390       C  
ATOM   3089  CG  LYS B 104      39.373  14.649  35.104  1.00 44.80           C  
ANISOU 3089  CG  LYS B 104     6573   5705   4743    -83     64   -413       C  
ATOM   3090  CD  LYS B 104      39.372  16.143  35.323  1.00 50.51           C  
ANISOU 3090  CD  LYS B 104     7312   6412   5468    -95     72   -451       C  
ATOM   3091  CE  LYS B 104      37.963  16.717  35.474  1.00 55.98           C  
ANISOU 3091  CE  LYS B 104     8014   7077   6179    -88    131   -460       C  
ATOM   3092  NZ  LYS B 104      37.516  16.744  36.896  1.00 56.65           N  
ANISOU 3092  NZ  LYS B 104     8152   7162   6210    -84    160   -474       N  
ATOM   3093  N   ILE B 105      39.775  13.184  30.793  1.00 38.18           N  
ANISOU 3093  N   ILE B 105     5590   4862   4055    -70     20   -343       N  
ATOM   3094  CA  ILE B 105      40.177  12.140  29.885  1.00 38.68           C  
ANISOU 3094  CA  ILE B 105     5623   4934   4137    -64      0   -316       C  
ATOM   3095  C   ILE B 105      41.461  12.532  29.132  1.00 37.39           C  
ANISOU 3095  C   ILE B 105     5437   4778   3988    -72    -42   -319       C  
ATOM   3096  O   ILE B 105      42.348  11.681  28.933  1.00 36.24           O  
ANISOU 3096  O   ILE B 105     5282   4650   3836    -70    -71   -301       O  
ATOM   3097  CB  ILE B 105      39.030  11.844  28.912  1.00 39.23           C  
ANISOU 3097  CB  ILE B 105     5667   4987   4252    -55     27   -301       C  
ATOM   3098  CG1 ILE B 105      37.872  11.193  29.697  1.00 39.47           C  
ANISOU 3098  CG1 ILE B 105     5716   5011   4268    -46     66   -291       C  
ATOM   3099  CG2 ILE B 105      39.518  10.986  27.737  1.00 41.64           C  
ANISOU 3099  CG2 ILE B 105     5940   5298   4583    -50      3   -278       C  
ATOM   3100  CD1 ILE B 105      36.639  10.900  28.855  1.00 39.43           C  
ANISOU 3100  CD1 ILE B 105     5686   4987   4308    -38     94   -275       C  
ATOM   3101  N   MET B 106      41.577  13.806  28.733  1.00 34.46           N  
ANISOU 3101  N   MET B 106     5057   4396   3640    -81    -43   -341       N  
ATOM   3102  CA  MET B 106      42.776  14.248  27.988  1.00 35.34           C  
ANISOU 3102  CA  MET B 106     5144   4511   3769    -88    -80   -343       C  
ATOM   3103  C   MET B 106      44.032  14.171  28.882  1.00 33.93           C  
ANISOU 3103  C   MET B 106     4985   4353   3552    -98   -117   -349       C  
ATOM   3104  O   MET B 106      45.041  13.580  28.494  1.00 35.00           O  
ANISOU 3104  O   MET B 106     5104   4502   3690    -97   -149   -332       O  
ATOM   3105  CB  MET B 106      42.546  15.627  27.386  1.00 36.84           C  
ANISOU 3105  CB  MET B 106     5320   4682   3993    -95    -69   -363       C  
ATOM   3106  CG  MET B 106      41.428  15.630  26.342  1.00 39.45           C  
ANISOU 3106  CG  MET B 106     5626   4995   4366    -85    -40   -352       C  
ATOM   3107  SD  MET B 106      41.790  14.541  24.943  1.00 41.38           S  
ANISOU 3107  SD  MET B 106     5835   5248   4638    -75    -59   -319       S  
ATOM   3108  CE  MET B 106      40.162  13.920  24.481  1.00 41.56           C  
ANISOU 3108  CE  MET B 106     5850   5257   4684    -64    -21   -304       C  
ATOM   3109  N   ILE B 107      43.907  14.635  30.124  1.00 34.34           N  
ANISOU 3109  N   ILE B 107     5074   4407   3565   -105   -111   -370       N  
ATOM   3110  CA  ILE B 107      44.917  14.436  31.195  1.00 34.38           C  
ANISOU 3110  CA  ILE B 107     5105   4433   3524   -114   -145   -375       C  
ATOM   3111  C   ILE B 107      45.445  13.022  31.231  1.00 35.45           C  
ANISOU 3111  C   ILE B 107     5234   4588   3644   -105   -165   -343       C  
ATOM   3112  O   ILE B 107      46.656  12.778  31.134  1.00 36.99           O  
ANISOU 3112  O   ILE B 107     5417   4798   3836   -110   -205   -333       O  
ATOM   3113  CB  ILE B 107      44.379  14.902  32.594  1.00 34.92           C  
ANISOU 3113  CB  ILE B 107     5221   4500   3546   -119   -126   -400       C  
ATOM   3114  CG1 ILE B 107      44.199  16.435  32.548  1.00 35.02           C  
ANISOU 3114  CG1 ILE B 107     5237   4491   3575   -131   -115   -435       C  
ATOM   3115  CG2 ILE B 107      45.341  14.513  33.724  1.00 34.31           C  
ANISOU 3115  CG2 ILE B 107     5173   4447   3416   -126   -162   -401       C  
ATOM   3116  CD1 ILE B 107      43.393  17.105  33.656  1.00 35.39           C  
ANISOU 3116  CD1 ILE B 107     5329   4528   3590   -134    -82   -463       C  
ATOM   3117  N   GLU B 108      44.507  12.089  31.307  1.00 35.38           N  
ANISOU 3117  N   GLU B 108     5231   4579   3632    -91   -135   -325       N  
ATOM   3118  CA  GLU B 108      44.806  10.698  31.442  1.00 35.74           C  
ANISOU 3118  CA  GLU B 108     5275   4641   3662    -81   -146   -294       C  
ATOM   3119  C   GLU B 108      45.529  10.207  30.227  1.00 34.07           C  
ANISOU 3119  C   GLU B 108     5024   4431   3487    -78   -168   -273       C  
ATOM   3120  O   GLU B 108      46.649   9.730  30.355  1.00 33.84           O  
ANISOU 3120  O   GLU B 108     4990   4419   3447    -79   -202   -260       O  
ATOM   3121  CB  GLU B 108      43.501   9.978  31.631  1.00 40.01           C  
ANISOU 3121  CB  GLU B 108     5825   5173   4201    -68   -103   -282       C  
ATOM   3122  CG  GLU B 108      43.615   8.545  32.050  1.00 47.44           C  
ANISOU 3122  CG  GLU B 108     6773   6130   5121    -58   -107   -252       C  
ATOM   3123  CD  GLU B 108      42.252   7.976  32.372  1.00 55.45           C  
ANISOU 3123  CD  GLU B 108     7799   7133   6133    -46    -62   -243       C  
ATOM   3124  OE1 GLU B 108      41.269   8.776  32.481  1.00 59.26           O  
ANISOU 3124  OE1 GLU B 108     8292   7600   6625    -48    -29   -262       O  
ATOM   3125  OE2 GLU B 108      42.163   6.733  32.502  1.00 59.10           O  
ANISOU 3125  OE2 GLU B 108     8261   7604   6590    -36    -58   -216       O  
ATOM   3126  N   ILE B 109      44.915  10.343  29.042  1.00 33.47           N  
ANISOU 3126  N   ILE B 109     4921   4338   3456    -72   -149   -270       N  
ATOM   3127  CA  ILE B 109      45.580   9.986  27.823  1.00 31.92           C  
ANISOU 3127  CA  ILE B 109     4690   4142   3294    -68   -167   -253       C  
ATOM   3128  C   ILE B 109      46.955  10.624  27.729  1.00 33.38           C  
ANISOU 3128  C   ILE B 109     4865   4335   3482    -79   -206   -260       C  
ATOM   3129  O   ILE B 109      47.936   9.939  27.476  1.00 34.15           O  
ANISOU 3129  O   ILE B 109     4947   4444   3581    -76   -232   -239       O  
ATOM   3130  CB  ILE B 109      44.789  10.435  26.597  1.00 33.24           C  
ANISOU 3130  CB  ILE B 109     4833   4289   3506    -65   -145   -257       C  
ATOM   3131  CG1 ILE B 109      43.428   9.751  26.599  1.00 34.77           C  
ANISOU 3131  CG1 ILE B 109     5032   4473   3703    -55   -109   -247       C  
ATOM   3132  CG2 ILE B 109      45.574  10.156  25.328  1.00 30.23           C  
ANISOU 3132  CG2 ILE B 109     4419   3908   3156    -60   -165   -241       C  
ATOM   3133  CD1 ILE B 109      42.504  10.167  25.470  1.00 33.33           C  
ANISOU 3133  CD1 ILE B 109     4828   4272   3563    -52    -87   -249       C  
ATOM   3134  N   GLY B 110      47.018  11.950  27.928  1.00 35.47           N  
ANISOU 3134  N   GLY B 110     5135   4592   3750    -91   -208   -288       N  
ATOM   3135  CA  GLY B 110      48.247  12.726  27.794  1.00 34.33           C  
ANISOU 3135  CA  GLY B 110     4978   4451   3614   -103   -243   -297       C  
ATOM   3136  C   GLY B 110      49.427  12.208  28.578  1.00 37.14           C  
ANISOU 3136  C   GLY B 110     5342   4828   3940   -108   -281   -286       C  
ATOM   3137  O   GLY B 110      50.527  12.087  28.034  1.00 35.49           O  
ANISOU 3137  O   GLY B 110     5108   4624   3750   -109   -310   -272       O  
ATOM   3138  N   GLY B 111      49.199  11.882  29.855  1.00 36.53           N  
ANISOU 3138  N   GLY B 111     5300   4763   3816   -110   -281   -291       N  
ATOM   3139  CA  GLY B 111      50.279  11.354  30.683  1.00 38.97           C  
ANISOU 3139  CA  GLY B 111     5618   5094   4092   -115   -319   -278       C  
ATOM   3140  C   GLY B 111      50.730   9.951  30.288  1.00 41.12           C  
ANISOU 3140  C   GLY B 111     5873   5378   4372   -101   -328   -240       C  
ATOM   3141  O   GLY B 111      51.913   9.572  30.470  1.00 38.60           O  
ANISOU 3141  O   GLY B 111     5543   5074   4048   -104   -364   -223       O  
ATOM   3142  N   HIS B 112      49.800   9.181  29.730  1.00 39.77           N  
ANISOU 3142  N   HIS B 112     5695   5199   4214    -87   -294   -226       N  
ATOM   3143  CA  HIS B 112      50.176   7.901  29.145  1.00 39.23           C  
ANISOU 3143  CA  HIS B 112     5607   5136   4160    -73   -298   -192       C  
ATOM   3144  C   HIS B 112      50.946   8.040  27.873  1.00 38.97           C  
ANISOU 3144  C   HIS B 112     5537   5096   4172    -71   -312   -182       C  
ATOM   3145  O   HIS B 112      51.838   7.200  27.608  1.00 34.79           O  
ANISOU 3145  O   HIS B 112     4991   4576   3651    -65   -331   -155       O  
ATOM   3146  CB  HIS B 112      48.977   7.001  28.946  1.00 39.45           C  
ANISOU 3146  CB  HIS B 112     5641   5157   4191    -59   -260   -180       C  
ATOM   3147  CG  HIS B 112      48.413   6.459  30.242  1.00 41.50           C  
ANISOU 3147  CG  HIS B 112     5935   5427   4406    -57   -248   -177       C  
ATOM   3148  ND1 HIS B 112      48.985   5.445  30.905  1.00 40.58           N  
ANISOU 3148  ND1 HIS B 112     5826   5328   4264    -51   -264   -153       N  
ATOM   3149  CD2 HIS B 112      47.236   6.784  30.952  1.00 41.88           C  
ANISOU 3149  CD2 HIS B 112     6011   5468   4432    -57   -216   -194       C  
ATOM   3150  CE1 HIS B 112      48.228   5.140  31.996  1.00 41.66           C  
ANISOU 3150  CE1 HIS B 112     5996   5470   4362    -49   -244   -154       C  
ATOM   3151  NE2 HIS B 112      47.166   5.970  32.019  1.00 39.74           N  
ANISOU 3151  NE2 HIS B 112     5765   5211   4121    -52   -214   -180       N  
ATOM   3152  N   ILE B 113      50.639   9.085  27.081  1.00 39.17           N  
ANISOU 3152  N   ILE B 113     5549   5105   4227    -76   -301   -202       N  
ATOM   3153  CA  ILE B 113      51.423   9.377  25.862  1.00 37.30           C  
ANISOU 3153  CA  ILE B 113     5278   4861   4032    -74   -314   -193       C  
ATOM   3154  C   ILE B 113      52.829   9.839  26.288  1.00 37.89           C  
ANISOU 3154  C   ILE B 113     5344   4947   4104    -86   -355   -193       C  
ATOM   3155  O   ILE B 113      53.832   9.365  25.778  1.00 36.95           O  
ANISOU 3155  O   ILE B 113     5202   4833   4004    -81   -374   -170       O  
ATOM   3156  CB  ILE B 113      50.717  10.375  24.889  1.00 35.67           C  
ANISOU 3156  CB  ILE B 113     5058   4634   3858    -75   -291   -212       C  
ATOM   3157  CG1 ILE B 113      49.537   9.725  24.156  1.00 34.37           C  
ANISOU 3157  CG1 ILE B 113     4891   4459   3707    -62   -257   -204       C  
ATOM   3158  CG2 ILE B 113      51.687  10.958  23.853  1.00 35.03           C  
ANISOU 3158  CG2 ILE B 113     4946   4548   3816    -76   -308   -207       C  
ATOM   3159  CD1 ILE B 113      48.633  10.726  23.386  1.00 32.29           C  
ANISOU 3159  CD1 ILE B 113     4619   4177   3471    -64   -233   -222       C  
ATOM   3160  N   LYS B 114      52.907  10.749  27.244  1.00 42.01           N  
ANISOU 3160  N   LYS B 114     5886   5472   4602   -101   -368   -218       N  
ATOM   3161  CA  LYS B 114      54.220  11.041  27.881  1.00 45.40           C  
ANISOU 3161  CA  LYS B 114     6313   5915   5022   -114   -412   -216       C  
ATOM   3162  C   LYS B 114      55.022   9.763  28.188  1.00 43.78           C  
ANISOU 3162  C   LYS B 114     6102   5728   4804   -106   -434   -181       C  
ATOM   3163  O   LYS B 114      56.175   9.658  27.782  1.00 42.64           O  
ANISOU 3163  O   LYS B 114     5931   5587   4683   -106   -461   -163       O  
ATOM   3164  CB  LYS B 114      54.076  11.909  29.134  1.00 46.10           C  
ANISOU 3164  CB  LYS B 114     6434   6008   5073   -131   -424   -247       C  
ATOM   3165  CG  LYS B 114      55.104  13.027  29.206  1.00 46.08           C  
ANISOU 3165  CG  LYS B 114     6420   6003   5086   -149   -460   -263       C  
ATOM   3166  CD  LYS B 114      54.871  13.922  30.418  1.00 46.29           C  
ANISOU 3166  CD  LYS B 114     6482   6030   5073   -167   -469   -298       C  
ATOM   3167  CE  LYS B 114      53.675  14.843  30.208  1.00 48.64           C  
ANISOU 3167  CE  LYS B 114     6793   6307   5379   -169   -429   -329       C  
ATOM   3168  NZ  LYS B 114      54.030  16.212  30.677  1.00 49.46           N  
ANISOU 3168  NZ  LYS B 114     6907   6402   5482   -190   -447   -364       N  
ATOM   3169  N   LYS B 115      54.399   8.758  28.809  1.00 44.44           N  
ANISOU 3169  N   LYS B 115     6207   5821   4855    -97   -419   -170       N  
ATOM   3170  CA  LYS B 115      55.145   7.517  29.165  1.00 44.13           C  
ANISOU 3170  CA  LYS B 115     6164   5799   4804    -88   -438   -135       C  
ATOM   3171  C   LYS B 115      55.539   6.609  28.008  1.00 43.04           C  
ANISOU 3171  C   LYS B 115     5994   5655   4704    -72   -430   -104       C  
ATOM   3172  O   LYS B 115      56.656   6.099  28.005  1.00 41.49           O  
ANISOU 3172  O   LYS B 115     5778   5467   4515    -70   -457    -78       O  
ATOM   3173  CB  LYS B 115      54.433   6.674  30.239  1.00 46.64           C  
ANISOU 3173  CB  LYS B 115     6516   6130   5075    -83   -425   -128       C  
ATOM   3174  CG  LYS B 115      55.383   6.159  31.334  1.00 51.51           C  
ANISOU 3174  CG  LYS B 115     7142   6770   5658    -87   -463   -109       C  
ATOM   3175  CD  LYS B 115      55.389   4.629  31.534  1.00 55.48           C  
ANISOU 3175  CD  LYS B 115     7645   7283   6150    -70   -455    -72       C  
ATOM   3176  CE  LYS B 115      54.344   4.105  32.531  1.00 57.00           C  
ANISOU 3176  CE  LYS B 115     7875   7483   6297    -65   -431    -74       C  
ATOM   3177  NZ  LYS B 115      53.002   3.812  31.911  1.00 55.66           N  
ANISOU 3177  NZ  LYS B 115     7708   7294   6143    -54   -382    -80       N  
ATOM   3178  N   ASN B 116      54.640   6.393  27.034  1.00 40.75           N  
ANISOU 3178  N   ASN B 116     5697   5349   4437    -61   -394   -105       N  
ATOM   3179  CA  ASN B 116      54.789   5.275  26.078  1.00 39.89           C  
ANISOU 3179  CA  ASN B 116     5567   5233   4353    -44   -381    -76       C  
ATOM   3180  C   ASN B 116      55.001   5.629  24.618  1.00 40.87           C  
ANISOU 3180  C   ASN B 116     5663   5341   4523    -38   -372    -76       C  
ATOM   3181  O   ASN B 116      55.514   4.815  23.858  1.00 41.55           O  
ANISOU 3181  O   ASN B 116     5729   5424   4631    -26   -369    -51       O  
ATOM   3182  CB  ASN B 116      53.577   4.351  26.093  1.00 39.85           C  
ANISOU 3182  CB  ASN B 116     5579   5225   4337    -33   -347    -72       C  
ATOM   3183  CG  ASN B 116      53.156   3.966  27.468  1.00 44.98           C  
ANISOU 3183  CG  ASN B 116     6258   5888   4941    -35   -347    -72       C  
ATOM   3184  OD1 ASN B 116      52.324   4.610  28.062  1.00 47.44           O  
ANISOU 3184  OD1 ASN B 116     6593   6198   5231    -43   -335    -96       O  
ATOM   3185  ND2 ASN B 116      53.693   2.882  27.963  1.00 49.60           N  
ANISOU 3185  ND2 ASN B 116     6845   6486   5513    -28   -358    -43       N  
ATOM   3186  N   CYS B 117      54.560   6.792  24.176  1.00 35.84           N  
ANISOU 3186  N   CYS B 117     5024   4693   3900    -46   -363   -102       N  
ATOM   3187  CA  CYS B 117      54.814   7.107  22.776  1.00 36.78           C  
ANISOU 3187  CA  CYS B 117     5116   4798   4061    -40   -355    -98       C  
ATOM   3188  C   CYS B 117      54.920   8.613  22.541  1.00 36.46           C  
ANISOU 3188  C   CYS B 117     5066   4748   4037    -52   -361   -123       C  
ATOM   3189  O   CYS B 117      54.173   9.186  21.717  1.00 39.51           O  
ANISOU 3189  O   CYS B 117     5448   5120   4442    -50   -338   -136       O  
ATOM   3190  CB  CYS B 117      53.755   6.496  21.899  1.00 33.12           C  
ANISOU 3190  CB  CYS B 117     4654   4322   3608    -27   -321    -96       C  
ATOM   3191  SG  CYS B 117      52.157   6.930  22.617  1.00 35.45           S  
ANISOU 3191  SG  CYS B 117     4978   4613   3877    -34   -297   -124       S  
ATOM   3192  N   PRO B 118      55.899   9.235  23.218  1.00 35.81           N  
ANISOU 3192  N   PRO B 118     4980   4674   3951    -65   -393   -127       N  
ATOM   3193  CA  PRO B 118      56.164  10.665  23.071  1.00 35.17           C  
ANISOU 3193  CA  PRO B 118     4890   4584   3888    -78   -403   -149       C  
ATOM   3194  C   PRO B 118      56.570  11.022  21.652  1.00 33.12           C  
ANISOU 3194  C   PRO B 118     4599   4310   3674    -70   -394   -139       C  
ATOM   3195  O   PRO B 118      56.542  12.185  21.284  1.00 33.66           O  
ANISOU 3195  O   PRO B 118     4658   4366   3764    -78   -393   -157       O  
ATOM   3196  CB  PRO B 118      57.348  10.891  24.013  1.00 35.35           C  
ANISOU 3196  CB  PRO B 118     4910   4619   3899    -92   -445   -146       C  
ATOM   3197  CG  PRO B 118      57.950   9.529  24.267  1.00 33.89           C  
ANISOU 3197  CG  PRO B 118     4723   4450   3705    -81   -456   -112       C  
ATOM   3198  CD  PRO B 118      56.760   8.626  24.259  1.00 34.54           C  
ANISOU 3198  CD  PRO B 118     4825   4531   3765    -69   -424   -110       C  
ATOM   3199  N   ASN B 119      56.961  10.065  20.847  1.00 31.38           N  
ANISOU 3199  N   ASN B 119     4362   4088   3470    -54   -388   -111       N  
ATOM   3200  CA  ASN B 119      57.272  10.441  19.476  1.00 31.22           C  
ANISOU 3200  CA  ASN B 119     4316   4054   3491    -45   -376   -103       C  
ATOM   3201  C   ASN B 119      56.118  10.147  18.526  1.00 29.44           C  
ANISOU 3201  C   ASN B 119     4097   3819   3270    -33   -341   -107       C  
ATOM   3202  O   ASN B 119      56.270  10.257  17.343  1.00 29.39           O  
ANISOU 3202  O   ASN B 119     4074   3802   3291    -23   -328    -98       O  
ATOM   3203  CB  ASN B 119      58.635   9.861  19.012  1.00 33.37           C  
ANISOU 3203  CB  ASN B 119     4563   4329   3787    -36   -391    -71       C  
ATOM   3204  CG  ASN B 119      59.773  10.095  20.084  1.00 39.82           C  
ANISOU 3204  CG  ASN B 119     5372   5157   4598    -50   -431    -66       C  
ATOM   3205  OD1 ASN B 119      60.012  11.229  20.562  1.00 41.53           O  
ANISOU 3205  OD1 ASN B 119     5588   5373   4819    -67   -449    -86       O  
ATOM   3206  ND2 ASN B 119      60.457   9.025  20.454  1.00 38.32           N  
ANISOU 3206  ND2 ASN B 119     5179   4979   4401    -43   -444    -38       N  
ATOM   3207  N   ALA B 120      54.951   9.768  19.029  1.00 28.61           N  
ANISOU 3207  N   ALA B 120     4017   3716   3138    -34   -325   -119       N  
ATOM   3208  CA  ALA B 120      53.794   9.503  18.104  1.00 26.36           C  
ANISOU 3208  CA  ALA B 120     3735   3420   2859    -24   -294   -122       C  
ATOM   3209  C   ALA B 120      53.177  10.708  17.447  1.00 24.73           C  
ANISOU 3209  C   ALA B 120     3522   3200   2672    -28   -281   -141       C  
ATOM   3210  O   ALA B 120      53.073  11.727  18.036  1.00 23.58           O  
ANISOU 3210  O   ALA B 120     3380   3053   2524    -40   -286   -161       O  
ATOM   3211  CB  ALA B 120      52.678   8.739  18.812  1.00 26.38           C  
ANISOU 3211  CB  ALA B 120     3763   3426   2832    -23   -280   -127       C  
ATOM   3212  N   PHE B 121      52.718  10.561  16.200  1.00 25.76           N  
ANISOU 3212  N   PHE B 121     3644   3321   2822    -16   -262   -135       N  
ATOM   3213  CA  PHE B 121      51.826  11.532  15.608  1.00 25.60           C  
ANISOU 3213  CA  PHE B 121     3620   3288   2816    -19   -245   -151       C  
ATOM   3214  C   PHE B 121      50.469  11.378  16.253  1.00 25.68           C  
ANISOU 3214  C   PHE B 121     3652   3299   2806    -23   -229   -166       C  
ATOM   3215  O   PHE B 121      49.973  10.262  16.381  1.00 25.62           O  
ANISOU 3215  O   PHE B 121     3656   3294   2782    -17   -222   -157       O  
ATOM   3216  CB  PHE B 121      51.680  11.309  14.091  1.00 26.72           C  
ANISOU 3216  CB  PHE B 121     3750   3422   2981     -5   -230   -137       C  
ATOM   3217  CG  PHE B 121      51.090  12.482  13.382  1.00 27.58           C  
ANISOU 3217  CG  PHE B 121     3848   3519   3110     -7   -218   -149       C  
ATOM   3218  CD1 PHE B 121      51.734  13.711  13.393  1.00 28.85           C  
ANISOU 3218  CD1 PHE B 121     3994   3676   3291    -14   -226   -156       C  
ATOM   3219  CD2 PHE B 121      49.880  12.373  12.708  1.00 30.67           C  
ANISOU 3219  CD2 PHE B 121     4244   3904   3504     -2   -199   -152       C  
ATOM   3220  CE1 PHE B 121      51.197  14.821  12.738  1.00 29.53           C  
ANISOU 3220  CE1 PHE B 121     4070   3750   3399    -15   -213   -165       C  
ATOM   3221  CE2 PHE B 121      49.339  13.454  12.034  1.00 28.20           C  
ANISOU 3221  CE2 PHE B 121     3920   3581   3211     -3   -188   -160       C  
ATOM   3222  CZ  PHE B 121      49.986  14.686  12.063  1.00 29.42           C  
ANISOU 3222  CZ  PHE B 121     4060   3731   3385     -9   -193   -166       C  
ATOM   3223  N   ILE B 122      49.860  12.487  16.674  1.00 25.97           N  
ANISOU 3223  N   ILE B 122     3692   3329   2844    -34   -222   -187       N  
ATOM   3224  CA  ILE B 122      48.582  12.420  17.385  1.00 25.99           C  
ANISOU 3224  CA  ILE B 122     3715   3329   2829    -38   -205   -201       C  
ATOM   3225  C   ILE B 122      47.522  13.175  16.644  1.00 25.55           C  
ANISOU 3225  C   ILE B 122     3652   3260   2795    -37   -184   -210       C  
ATOM   3226  O   ILE B 122      47.721  14.339  16.240  1.00 27.04           O  
ANISOU 3226  O   ILE B 122     3828   3440   3005    -41   -183   -219       O  
ATOM   3227  CB  ILE B 122      48.642  13.019  18.799  1.00 25.79           C  
ANISOU 3227  CB  ILE B 122     3708   3309   2781    -52   -212   -221       C  
ATOM   3228  CG1 ILE B 122      49.868  12.558  19.585  1.00 26.78           C  
ANISOU 3228  CG1 ILE B 122     3838   3449   2887    -56   -240   -213       C  
ATOM   3229  CG2 ILE B 122      47.347  12.785  19.551  1.00 26.00           C  
ANISOU 3229  CG2 ILE B 122     3757   3334   2788    -54   -191   -231       C  
ATOM   3230  CD1 ILE B 122      49.981  11.060  19.661  1.00 26.63           C  
ANISOU 3230  CD1 ILE B 122     3825   3441   2852    -46   -242   -191       C  
ATOM   3231  N   ILE B 123      46.393  12.526  16.466  1.00 24.90           N  
ANISOU 3231  N   ILE B 123     3577   3174   2708    -32   -166   -207       N  
ATOM   3232  CA  ILE B 123      45.237  13.160  15.821  1.00 24.19           C  
ANISOU 3232  CA  ILE B 123     3480   3071   2638    -32   -146   -213       C  
ATOM   3233  C   ILE B 123      44.042  13.174  16.778  1.00 23.94           C  
ANISOU 3233  C   ILE B 123     3466   3036   2594    -37   -127   -225       C  
ATOM   3234  O   ILE B 123      43.612  12.085  17.262  1.00 23.21           O  
ANISOU 3234  O   ILE B 123     3388   2948   2483    -34   -122   -217       O  
ATOM   3235  CB  ILE B 123      44.832  12.464  14.494  1.00 23.50           C  
ANISOU 3235  CB  ILE B 123     3381   2980   2565    -21   -141   -196       C  
ATOM   3236  CG1 ILE B 123      45.994  12.483  13.515  1.00 24.44           C  
ANISOU 3236  CG1 ILE B 123     3486   3102   2698    -13   -155   -184       C  
ATOM   3237  CG2 ILE B 123      43.569  13.086  13.905  1.00 23.81           C  
ANISOU 3237  CG2 ILE B 123     3413   3007   2625    -21   -122   -200       C  
ATOM   3238  CD1 ILE B 123      45.786  11.649  12.230  1.00 24.14           C  
ANISOU 3238  CD1 ILE B 123     3442   3062   2667     -2   -152   -167       C  
ATOM   3239  N   VAL B 124      43.501  14.374  17.037  1.00 23.58           N  
ANISOU 3239  N   VAL B 124     3420   2979   2560    -44   -113   -241       N  
ATOM   3240  CA  VAL B 124      42.392  14.500  18.018  1.00 26.89           C  
ANISOU 3240  CA  VAL B 124     3856   3392   2967    -48    -91   -253       C  
ATOM   3241  C   VAL B 124      41.067  14.732  17.323  1.00 27.82           C  
ANISOU 3241  C   VAL B 124     3962   3496   3111    -44    -68   -249       C  
ATOM   3242  O   VAL B 124      41.025  15.389  16.269  1.00 31.43           O  
ANISOU 3242  O   VAL B 124     4398   3945   3595    -42    -68   -246       O  
ATOM   3243  CB  VAL B 124      42.726  15.482  19.172  1.00 27.10           C  
ANISOU 3243  CB  VAL B 124     3898   3417   2979    -59    -91   -276       C  
ATOM   3244  CG1 VAL B 124      41.573  15.690  20.162  1.00 27.92           C  
ANISOU 3244  CG1 VAL B 124     4022   3513   3071    -62    -63   -289       C  
ATOM   3245  CG2 VAL B 124      43.979  15.023  19.887  1.00 26.49           C  
ANISOU 3245  CG2 VAL B 124     3833   3356   2874    -63   -118   -276       C  
ATOM   3246  N   VAL B 125      40.023  14.029  17.803  1.00 29.49           N  
ANISOU 3246  N   VAL B 125     4185   3705   3314    -42    -51   -246       N  
ATOM   3247  CA  VAL B 125      38.681  14.039  17.168  1.00 28.71           C  
ANISOU 3247  CA  VAL B 125     4073   3592   3241    -39    -31   -238       C  
ATOM   3248  C   VAL B 125      37.550  14.470  18.132  1.00 30.51           C  
ANISOU 3248  C   VAL B 125     4313   3809   3469    -42     -1   -248       C  
ATOM   3249  O   VAL B 125      36.562  15.050  17.713  1.00 30.02           O  
ANISOU 3249  O   VAL B 125     4237   3733   3435    -41     17   -246       O  
ATOM   3250  CB  VAL B 125      38.383  12.663  16.556  1.00 29.95           C  
ANISOU 3250  CB  VAL B 125     4227   3754   3397    -32    -37   -219       C  
ATOM   3251  CG1 VAL B 125      36.986  12.626  15.965  1.00 28.64           C  
ANISOU 3251  CG1 VAL B 125     4048   3575   3258    -31    -20   -210       C  
ATOM   3252  CG2 VAL B 125      39.401  12.359  15.450  1.00 28.77           C  
ANISOU 3252  CG2 VAL B 125     4065   3613   3252    -28    -61   -209       C  
ATOM   3253  N   THR B 126      37.723  14.167  19.419  1.00 30.90           N  
ANISOU 3253  N   THR B 126     4387   3864   3487    -45      3   -256       N  
ATOM   3254  CA  THR B 126      36.808  14.465  20.461  1.00 31.81           C  
ANISOU 3254  CA  THR B 126     4519   3969   3595    -47     32   -266       C  
ATOM   3255  C   THR B 126      36.365  15.931  20.453  1.00 32.84           C  
ANISOU 3255  C   THR B 126     4645   4084   3749    -51     52   -281       C  
ATOM   3256  O   THR B 126      37.194  16.839  20.517  1.00 30.31           O  
ANISOU 3256  O   THR B 126     4325   3764   3426    -57     40   -297       O  
ATOM   3257  CB  THR B 126      37.536  14.225  21.770  1.00 32.72           C  
ANISOU 3257  CB  THR B 126     4666   4098   3668    -50     26   -277       C  
ATOM   3258  OG1 THR B 126      38.137  12.937  21.701  1.00 36.73           O  
ANISOU 3258  OG1 THR B 126     5176   4621   4157    -46      5   -262       O  
ATOM   3259  CG2 THR B 126      36.581  14.231  22.934  1.00 34.32           C  
ANISOU 3259  CG2 THR B 126     4891   4292   3855    -50     58   -284       C  
ATOM   3260  N   ASN B 127      35.041  16.155  20.421  1.00 34.55           N  
ANISOU 3260  N   ASN B 127     4854   4284   3989    -48     82   -277       N  
ATOM   3261  CA  ASN B 127      34.507  17.509  20.343  1.00 33.53           C  
ANISOU 3261  CA  ASN B 127     4716   4137   3887    -50    104   -288       C  
ATOM   3262  C   ASN B 127      34.348  18.178  21.650  1.00 33.55           C  
ANISOU 3262  C   ASN B 127     4745   4130   3870    -54    128   -310       C  
ATOM   3263  O   ASN B 127      34.129  17.515  22.663  1.00 31.87           O  
ANISOU 3263  O   ASN B 127     4557   3922   3627    -53    139   -311       O  
ATOM   3264  CB  ASN B 127      33.237  17.544  19.530  1.00 37.51           C  
ANISOU 3264  CB  ASN B 127     5194   4626   4432    -45    123   -270       C  
ATOM   3265  CG  ASN B 127      33.527  17.386  18.017  1.00 41.10           C  
ANISOU 3265  CG  ASN B 127     5619   5085   4909    -43     96   -254       C  
ATOM   3266  OD1 ASN B 127      34.106  18.267  17.344  1.00 44.51           O  
ANISOU 3266  OD1 ASN B 127     6038   5516   5356    -44     85   -259       O  
ATOM   3267  ND2 ASN B 127      33.170  16.258  17.500  1.00 40.69           N  
ANISOU 3267  ND2 ASN B 127     5560   5040   4859    -39     86   -236       N  
ATOM   3268  N   PRO B 128      34.514  19.523  21.666  1.00 35.25           N  
ANISOU 3268  N   PRO B 128     4958   4333   4100    -59    137   -328       N  
ATOM   3269  CA  PRO B 128      34.926  20.406  20.526  1.00 32.36           C  
ANISOU 3269  CA  PRO B 128     4563   3962   3768    -61    123   -326       C  
ATOM   3270  C   PRO B 128      36.438  20.293  20.240  1.00 30.81           C  
ANISOU 3270  C   PRO B 128     4367   3783   3553    -66     84   -331       C  
ATOM   3271  O   PRO B 128      37.272  20.457  21.152  1.00 29.90           O  
ANISOU 3271  O   PRO B 128     4276   3675   3408    -73     73   -350       O  
ATOM   3272  CB  PRO B 128      34.536  21.803  21.020  1.00 32.05           C  
ANISOU 3272  CB  PRO B 128     4530   3902   3745    -65    152   -347       C  
ATOM   3273  CG  PRO B 128      34.679  21.738  22.504  1.00 30.59           C  
ANISOU 3273  CG  PRO B 128     4384   3718   3519    -70    164   -368       C  
ATOM   3274  CD  PRO B 128      34.347  20.304  22.918  1.00 32.44           C  
ANISOU 3274  CD  PRO B 128     4631   3966   3726    -64    163   -353       C  
ATOM   3275  N   VAL B 129      36.781  20.011  18.986  1.00 30.01           N  
ANISOU 3275  N   VAL B 129     4240   3689   3472    -61     63   -313       N  
ATOM   3276  CA  VAL B 129      38.079  19.412  18.714  1.00 30.22           C  
ANISOU 3276  CA  VAL B 129     4267   3735   3479    -62     28   -309       C  
ATOM   3277  C   VAL B 129      39.208  20.395  18.926  1.00 30.73           C  
ANISOU 3277  C   VAL B 129     4333   3799   3542    -70     13   -327       C  
ATOM   3278  O   VAL B 129      40.251  20.038  19.513  1.00 32.40           O  
ANISOU 3278  O   VAL B 129     4560   4025   3725    -75     -9   -334       O  
ATOM   3279  CB  VAL B 129      38.176  18.796  17.325  1.00 31.19           C  
ANISOU 3279  CB  VAL B 129     4365   3864   3620    -55     11   -285       C  
ATOM   3280  CG1 VAL B 129      37.382  19.605  16.327  1.00 29.63           C  
ANISOU 3280  CG1 VAL B 129     4141   3651   3463    -51     26   -277       C  
ATOM   3281  CG2 VAL B 129      39.635  18.723  16.937  1.00 33.90           C  
ANISOU 3281  CG2 VAL B 129     4704   4220   3954    -56    -19   -284       C  
ATOM   3282  N   ASP B 130      38.934  21.654  18.567  1.00 30.74           N  
ANISOU 3282  N   ASP B 130     4320   3782   3574    -73     28   -335       N  
ATOM   3283  CA  ASP B 130      39.916  22.741  18.669  1.00 29.89           C  
ANISOU 3283  CA  ASP B 130     4210   3670   3475    -81     16   -353       C  
ATOM   3284  C   ASP B 130      40.378  22.963  20.130  1.00 30.06           C  
ANISOU 3284  C   ASP B 130     4265   3693   3462    -93     13   -380       C  
ATOM   3285  O   ASP B 130      41.579  23.210  20.393  1.00 29.12           O  
ANISOU 3285  O   ASP B 130     4149   3581   3331   -101    -12   -390       O  
ATOM   3286  CB  ASP B 130      39.408  23.990  17.959  1.00 30.55           C  
ANISOU 3286  CB  ASP B 130     4271   3733   3602    -80     36   -353       C  
ATOM   3287  CG  ASP B 130      39.141  23.734  16.446  1.00 35.27           C  
ANISOU 3287  CG  ASP B 130     4838   4334   4230    -69     31   -325       C  
ATOM   3288  OD1 ASP B 130      40.138  23.727  15.660  1.00 35.74           O  
ANISOU 3288  OD1 ASP B 130     4881   4400   4295    -67      8   -316       O  
ATOM   3289  OD2 ASP B 130      37.941  23.545  16.041  1.00 33.72           O  
ANISOU 3289  OD2 ASP B 130     4632   4130   4050    -62     51   -311       O  
ATOM   3290  N   VAL B 131      39.449  22.776  21.069  1.00 29.44           N  
ANISOU 3290  N   VAL B 131     4210   3610   3365    -92     39   -389       N  
ATOM   3291  CA  VAL B 131      39.788  22.785  22.494  1.00 28.99           C  
ANISOU 3291  CA  VAL B 131     4190   3557   3267   -102     37   -412       C  
ATOM   3292  C   VAL B 131      40.448  21.451  22.905  1.00 29.99           C  
ANISOU 3292  C   VAL B 131     4331   3709   3354   -100     10   -401       C  
ATOM   3293  O   VAL B 131      41.520  21.453  23.567  1.00 30.48           O  
ANISOU 3293  O   VAL B 131     4408   3782   3388   -109    -16   -414       O  
ATOM   3294  CB  VAL B 131      38.538  22.998  23.339  1.00 29.48           C  
ANISOU 3294  CB  VAL B 131     4274   3604   3322   -100     78   -423       C  
ATOM   3295  CG1 VAL B 131      38.873  22.966  24.849  1.00 30.88           C  
ANISOU 3295  CG1 VAL B 131     4494   3787   3451   -108     77   -448       C  
ATOM   3296  CG2 VAL B 131      37.902  24.314  22.972  1.00 29.27           C  
ANISOU 3296  CG2 VAL B 131     4233   3552   3337   -100    107   -432       C  
ATOM   3297  N   MET B 132      39.811  20.325  22.559  1.00 29.07           N  
ANISOU 3297  N   MET B 132     4208   3599   3235    -90     16   -378       N  
ATOM   3298  CA  MET B 132      40.357  19.052  22.983  1.00 29.72           C  
ANISOU 3298  CA  MET B 132     4305   3704   3283    -87     -4   -367       C  
ATOM   3299  C   MET B 132      41.822  18.854  22.570  1.00 28.82           C  
ANISOU 3299  C   MET B 132     4179   3604   3164    -91    -45   -361       C  
ATOM   3300  O   MET B 132      42.658  18.534  23.434  1.00 28.04           O  
ANISOU 3300  O   MET B 132     4101   3520   3033    -97    -66   -368       O  
ATOM   3301  CB  MET B 132      39.452  17.874  22.639  1.00 29.40           C  
ANISOU 3301  CB  MET B 132     4259   3666   3245    -76      8   -343       C  
ATOM   3302  CG  MET B 132      38.156  17.904  23.462  1.00 31.15           C  
ANISOU 3302  CG  MET B 132     4500   3876   3460    -73     47   -348       C  
ATOM   3303  SD  MET B 132      38.435  17.905  25.258  1.00 35.27           S  
ANISOU 3303  SD  MET B 132     5068   4405   3927    -80     52   -370       S  
ATOM   3304  CE  MET B 132      37.142  19.009  25.810  1.00 33.50           C  
ANISOU 3304  CE  MET B 132     4857   4154   3717    -80    101   -389       C  
ATOM   3305  N   VAL B 133      42.133  19.132  21.302  1.00 26.78           N  
ANISOU 3305  N   VAL B 133     3889   3342   2941    -87    -54   -349       N  
ATOM   3306  CA  VAL B 133      43.486  19.009  20.805  1.00 26.60           C  
ANISOU 3306  CA  VAL B 133     3852   3331   2922    -89    -87   -341       C  
ATOM   3307  C   VAL B 133      44.501  19.821  21.569  1.00 27.36           C  
ANISOU 3307  C   VAL B 133     3959   3429   3007   -103   -107   -363       C  
ATOM   3308  O   VAL B 133      45.598  19.327  21.784  1.00 27.33           O  
ANISOU 3308  O   VAL B 133     3957   3440   2987   -105   -137   -357       O  
ATOM   3309  CB  VAL B 133      43.636  19.335  19.278  1.00 25.94           C  
ANISOU 3309  CB  VAL B 133     3734   3241   2879    -82    -90   -326       C  
ATOM   3310  CG1 VAL B 133      43.435  20.811  19.016  1.00 25.92           C  
ANISOU 3310  CG1 VAL B 133     3720   3219   2907    -87    -76   -341       C  
ATOM   3311  CG2 VAL B 133      45.030  18.945  18.793  1.00 25.21           C  
ANISOU 3311  CG2 VAL B 133     3629   3161   2787    -81   -122   -313       C  
ATOM   3312  N   GLN B 134      44.188  21.082  21.919  1.00 28.34           N  
ANISOU 3312  N   GLN B 134     4089   3536   3143   -111    -92   -387       N  
ATOM   3313  CA  GLN B 134      45.139  21.870  22.669  1.00 30.18           C  
ANISOU 3313  CA  GLN B 134     4333   3768   3365   -126   -112   -410       C  
ATOM   3314  C   GLN B 134      45.329  21.303  24.048  1.00 30.69           C  
ANISOU 3314  C   GLN B 134     4433   3846   3379   -133   -123   -421       C  
ATOM   3315  O   GLN B 134      46.427  21.315  24.592  1.00 33.73           O  
ANISOU 3315  O   GLN B 134     4826   4242   3746   -143   -155   -428       O  
ATOM   3316  CB  GLN B 134      44.710  23.330  22.821  1.00 31.10           C  
ANISOU 3316  CB  GLN B 134     4451   3861   3504   -134    -91   -435       C  
ATOM   3317  CG  GLN B 134      45.836  24.170  23.401  1.00 31.49           C  
ANISOU 3317  CG  GLN B 134     4507   3908   3549   -151   -118   -458       C  
ATOM   3318  CD  GLN B 134      45.616  25.674  23.332  1.00 31.31           C  
ANISOU 3318  CD  GLN B 134     4479   3859   3558   -159   -100   -482       C  
ATOM   3319  OE1 GLN B 134      44.494  26.131  23.246  1.00 31.14           O  
ANISOU 3319  OE1 GLN B 134     4460   3821   3550   -154    -63   -487       O  
ATOM   3320  NE2 GLN B 134      46.702  26.441  23.389  1.00 29.67           N  
ANISOU 3320  NE2 GLN B 134     4263   3647   3363   -173   -126   -495       N  
ATOM   3321  N   LEU B 135      44.251  20.834  24.644  1.00 31.26           N  
ANISOU 3321  N   LEU B 135     4528   3918   3430   -127    -96   -422       N  
ATOM   3322  CA  LEU B 135      44.338  20.295  26.035  1.00 32.16           C  
ANISOU 3322  CA  LEU B 135     4681   4045   3492   -132   -102   -433       C  
ATOM   3323  C   LEU B 135      45.247  19.034  26.071  1.00 32.48           C  
ANISOU 3323  C   LEU B 135     4719   4111   3511   -128   -135   -409       C  
ATOM   3324  O   LEU B 135      46.038  18.804  27.038  1.00 30.17           O  
ANISOU 3324  O   LEU B 135     4448   3833   3181   -137   -162   -417       O  
ATOM   3325  CB  LEU B 135      42.936  19.934  26.555  1.00 31.74           C  
ANISOU 3325  CB  LEU B 135     4649   3986   3425   -124    -61   -433       C  
ATOM   3326  CG  LEU B 135      42.078  21.163  26.934  1.00 33.37           C  
ANISOU 3326  CG  LEU B 135     4869   4168   3642   -128    -26   -459       C  
ATOM   3327  CD1 LEU B 135      40.630  20.731  27.199  1.00 32.54           C  
ANISOU 3327  CD1 LEU B 135     4774   4053   3533   -117     16   -451       C  
ATOM   3328  CD2 LEU B 135      42.646  21.823  28.189  1.00 34.54           C  
ANISOU 3328  CD2 LEU B 135     5053   4316   3753   -143    -38   -491       C  
ATOM   3329  N   LEU B 136      45.157  18.250  24.997  1.00 30.30           N  
ANISOU 3329  N   LEU B 136     4415   3838   3256   -116   -135   -382       N  
ATOM   3330  CA  LEU B 136      45.987  17.047  24.924  1.00 32.83           C  
ANISOU 3330  CA  LEU B 136     4731   4179   3562   -111   -163   -358       C  
ATOM   3331  C   LEU B 136      47.435  17.355  24.498  1.00 34.02           C  
ANISOU 3331  C   LEU B 136     4861   4336   3727   -118   -200   -354       C  
ATOM   3332  O   LEU B 136      48.368  16.865  25.158  1.00 33.30           O  
ANISOU 3332  O   LEU B 136     4780   4262   3611   -123   -230   -350       O  
ATOM   3333  CB  LEU B 136      45.323  15.921  24.149  1.00 32.48           C  
ANISOU 3333  CB  LEU B 136     4674   4137   3529    -96   -147   -331       C  
ATOM   3334  CG  LEU B 136      46.088  14.593  24.075  1.00 33.86           C  
ANISOU 3334  CG  LEU B 136     4845   4331   3689    -89   -171   -306       C  
ATOM   3335  CD1 LEU B 136      46.079  13.882  25.414  1.00 33.97           C  
ANISOU 3335  CD1 LEU B 136     4890   4359   3656    -90   -174   -306       C  
ATOM   3336  CD2 LEU B 136      45.492  13.698  23.009  1.00 32.03           C  
ANISOU 3336  CD2 LEU B 136     4595   4096   3479    -75   -156   -283       C  
ATOM   3337  N   HIS B 137      47.633  18.231  23.482  1.00 33.86           N  
ANISOU 3337  N   HIS B 137     4813   4302   3749   -118   -199   -356       N  
ATOM   3338  CA  HIS B 137      48.949  18.858  23.284  1.00 32.43           C  
ANISOU 3338  CA  HIS B 137     4615   4122   3584   -128   -230   -359       C  
ATOM   3339  C   HIS B 137      49.584  19.157  24.634  1.00 34.88           C  
ANISOU 3339  C   HIS B 137     4951   4440   3860   -144   -254   -380       C  
ATOM   3340  O   HIS B 137      50.682  18.726  24.954  1.00 33.61           O  
ANISOU 3340  O   HIS B 137     4788   4294   3686   -148   -288   -370       O  
ATOM   3341  CB  HIS B 137      48.805  20.189  22.593  1.00 31.92           C  
ANISOU 3341  CB  HIS B 137     4531   4037   3560   -132   -218   -373       C  
ATOM   3342  CG  HIS B 137      50.128  20.852  22.305  1.00 31.62           C  
ANISOU 3342  CG  HIS B 137     4472   3997   3544   -141   -248   -373       C  
ATOM   3343  ND1 HIS B 137      50.363  22.168  22.542  1.00 33.29           N  
ANISOU 3343  ND1 HIS B 137     4682   4192   3772   -155   -250   -398       N  
ATOM   3344  CD2 HIS B 137      51.303  20.335  21.774  1.00 31.22           C  
ANISOU 3344  CD2 HIS B 137     4398   3956   3506   -137   -275   -350       C  
ATOM   3345  CE1 HIS B 137      51.627  22.483  22.165  1.00 31.55           C  
ANISOU 3345  CE1 HIS B 137     4438   3973   3576   -160   -279   -391       C  
ATOM   3346  NE2 HIS B 137      52.205  21.356  21.696  1.00 31.45           N  
ANISOU 3346  NE2 HIS B 137     4411   3976   3560   -149   -294   -361       N  
ATOM   3347  N   GLN B 138      48.871  19.919  25.434  1.00 36.28           N  
ANISOU 3347  N   GLN B 138     5155   4607   4022   -152   -236   -408       N  
ATOM   3348  CA  GLN B 138      49.400  20.406  26.692  1.00 38.26           C  
ANISOU 3348  CA  GLN B 138     5434   4863   4240   -169   -258   -433       C  
ATOM   3349  C   GLN B 138      49.702  19.343  27.727  1.00 43.00           C  
ANISOU 3349  C   GLN B 138     6060   5486   4789   -170   -277   -425       C  
ATOM   3350  O   GLN B 138      50.725  19.452  28.408  1.00 48.09           O  
ANISOU 3350  O   GLN B 138     6713   6142   5414   -183   -314   -432       O  
ATOM   3351  CB  GLN B 138      48.499  21.493  27.264  1.00 40.02           C  
ANISOU 3351  CB  GLN B 138     5681   5066   4458   -177   -228   -467       C  
ATOM   3352  CG  GLN B 138      48.634  22.871  26.580  1.00 40.99           C  
ANISOU 3352  CG  GLN B 138     5781   5165   4627   -185   -222   -483       C  
ATOM   3353  CD  GLN B 138      47.514  23.874  26.950  1.00 43.93           C  
ANISOU 3353  CD  GLN B 138     6173   5515   5003   -188   -183   -511       C  
ATOM   3354  OE1 GLN B 138      46.420  23.494  27.388  1.00 45.63           O  
ANISOU 3354  OE1 GLN B 138     6410   5728   5197   -180   -151   -513       O  
ATOM   3355  NE2 GLN B 138      47.780  25.158  26.740  1.00 45.86           N  
ANISOU 3355  NE2 GLN B 138     6407   5739   5278   -199   -182   -532       N  
ATOM   3356  N   HIS B 139      48.864  18.308  27.869  1.00 42.30           N  
ANISOU 3356  N   HIS B 139     5985   5406   4681   -156   -254   -409       N  
ATOM   3357  CA  HIS B 139      49.164  17.288  28.898  1.00 42.07           C  
ANISOU 3357  CA  HIS B 139     5981   5398   4602   -155   -272   -399       C  
ATOM   3358  C   HIS B 139      50.047  16.160  28.397  1.00 40.62           C  
ANISOU 3358  C   HIS B 139     5774   5232   4425   -147   -298   -365       C  
ATOM   3359  O   HIS B 139      50.574  15.391  29.174  1.00 43.29           O  
ANISOU 3359  O   HIS B 139     6127   5589   4729   -148   -321   -354       O  
ATOM   3360  CB  HIS B 139      47.903  16.671  29.518  1.00 41.13           C  
ANISOU 3360  CB  HIS B 139     5891   5280   4454   -145   -235   -398       C  
ATOM   3361  CG  HIS B 139      46.807  17.642  29.812  1.00 41.88           C  
ANISOU 3361  CG  HIS B 139     6006   5355   4551   -148   -198   -426       C  
ATOM   3362  ND1 HIS B 139      46.977  18.710  30.599  1.00 44.94           N  
ANISOU 3362  ND1 HIS B 139     6417   5735   4921   -163   -203   -459       N  
ATOM   3363  CD2 HIS B 139      45.453  17.625  29.452  1.00 43.72           C  
ANISOU 3363  CD2 HIS B 139     6237   5572   4800   -137   -152   -424       C  
ATOM   3364  CE1 HIS B 139      45.803  19.375  30.720  1.00 45.95           C  
ANISOU 3364  CE1 HIS B 139     6559   5842   5056   -161   -159   -478       C  
ATOM   3365  NE2 HIS B 139      44.872  18.708  30.012  1.00 47.16           N  
ANISOU 3365  NE2 HIS B 139     6695   5992   5231   -144   -129   -455       N  
ATOM   3366  N   SER B 140      50.171  16.019  27.093  1.00 37.77           N  
ANISOU 3366  N   SER B 140     5377   4864   4107   -138   -293   -346       N  
ATOM   3367  CA  SER B 140      50.944  14.932  26.529  1.00 36.32           C  
ANISOU 3367  CA  SER B 140     5172   4694   3933   -128   -313   -313       C  
ATOM   3368  C   SER B 140      52.409  15.340  26.397  1.00 35.64           C  
ANISOU 3368  C   SER B 140     5064   4612   3862   -138   -353   -309       C  
ATOM   3369  O   SER B 140      53.306  14.473  26.300  1.00 35.94           O  
ANISOU 3369  O   SER B 140     5090   4664   3900   -133   -377   -283       O  
ATOM   3370  CB  SER B 140      50.403  14.542  25.143  1.00 35.89           C  
ANISOU 3370  CB  SER B 140     5090   4628   3916   -112   -288   -295       C  
ATOM   3371  OG  SER B 140      50.634  15.557  24.182  1.00 34.47           O  
ANISOU 3371  OG  SER B 140     4885   4434   3778   -115   -287   -302       O  
ATOM   3372  N   GLY B 141      52.610  16.653  26.338  1.00 32.72           N  
ANISOU 3372  N   GLY B 141     4690   4229   3512   -151   -358   -334       N  
ATOM   3373  CA  GLY B 141      53.873  17.247  26.055  1.00 33.22           C  
ANISOU 3373  CA  GLY B 141     4728   4291   3601   -161   -391   -332       C  
ATOM   3374  C   GLY B 141      54.454  17.022  24.679  1.00 33.26           C  
ANISOU 3374  C   GLY B 141     4693   4291   3652   -149   -392   -306       C  
ATOM   3375  O   GLY B 141      55.627  17.203  24.522  1.00 34.34           O  
ANISOU 3375  O   GLY B 141     4808   4430   3807   -155   -422   -296       O  
ATOM   3376  N   VAL B 142      53.678  16.662  23.648  1.00 33.52           N  
ANISOU 3376  N   VAL B 142     4714   4316   3705   -133   -360   -293       N  
ATOM   3377  CA  VAL B 142      54.344  16.287  22.414  1.00 31.19           C  
ANISOU 3377  CA  VAL B 142     4385   4018   3446   -121   -363   -265       C  
ATOM   3378  C   VAL B 142      54.695  17.549  21.678  1.00 31.91           C  
ANISOU 3378  C   VAL B 142     4452   4092   3579   -126   -363   -275       C  
ATOM   3379  O   VAL B 142      54.129  18.598  21.946  1.00 32.13           O  
ANISOU 3379  O   VAL B 142     4490   4108   3610   -136   -351   -302       O  
ATOM   3380  CB  VAL B 142      53.478  15.377  21.522  1.00 31.91           C  
ANISOU 3380  CB  VAL B 142     4472   4107   3542   -101   -333   -247       C  
ATOM   3381  CG1 VAL B 142      53.229  13.995  22.179  1.00 30.26           C  
ANISOU 3381  CG1 VAL B 142     4283   3914   3297    -94   -333   -233       C  
ATOM   3382  CG2 VAL B 142      52.191  16.082  21.120  1.00 31.46           C  
ANISOU 3382  CG2 VAL B 142     4421   4035   3496   -100   -299   -266       C  
ATOM   3383  N   PRO B 143      55.600  17.468  20.697  1.00 31.43           N  
ANISOU 3383  N   PRO B 143     4358   4028   3553   -119   -372   -252       N  
ATOM   3384  CA  PRO B 143      55.874  18.759  20.034  1.00 31.30           C  
ANISOU 3384  CA  PRO B 143     4320   3995   3578   -124   -368   -262       C  
ATOM   3385  C   PRO B 143      54.664  19.226  19.183  1.00 31.02           C  
ANISOU 3385  C   PRO B 143     4284   3944   3558   -115   -330   -270       C  
ATOM   3386  O   PRO B 143      53.735  18.474  18.990  1.00 28.54           O  
ANISOU 3386  O   PRO B 143     3981   3633   3226   -104   -309   -264       O  
ATOM   3387  CB  PRO B 143      57.099  18.449  19.165  1.00 32.06           C  
ANISOU 3387  CB  PRO B 143     4383   4091   3706   -115   -383   -232       C  
ATOM   3388  CG  PRO B 143      57.597  17.105  19.653  1.00 30.57           C  
ANISOU 3388  CG  PRO B 143     4202   3922   3491   -110   -401   -210       C  
ATOM   3389  CD  PRO B 143      56.371  16.370  20.104  1.00 29.71           C  
ANISOU 3389  CD  PRO B 143     4124   3821   3344   -105   -380   -218       C  
ATOM   3390  N   LYS B 144      54.672  20.490  18.750  1.00 30.16           N  
ANISOU 3390  N   LYS B 144     4159   3817   3481   -121   -323   -282       N  
ATOM   3391  CA  LYS B 144      53.510  21.112  18.212  1.00 29.38           C  
ANISOU 3391  CA  LYS B 144     4062   3704   3395   -116   -290   -293       C  
ATOM   3392  C   LYS B 144      53.247  20.730  16.747  1.00 27.72           C  
ANISOU 3392  C   LYS B 144     3831   3491   3208    -97   -270   -268       C  
ATOM   3393  O   LYS B 144      52.121  20.820  16.323  1.00 25.46           O  
ANISOU 3393  O   LYS B 144     3550   3199   2924    -90   -244   -271       O  
ATOM   3394  CB  LYS B 144      53.634  22.637  18.344  1.00 32.40           C  
ANISOU 3394  CB  LYS B 144     4436   4068   3804   -130   -289   -317       C  
ATOM   3395  CG  LYS B 144      54.808  23.220  17.582  1.00 34.84           C  
ANISOU 3395  CG  LYS B 144     4711   4369   4155   -130   -304   -303       C  
ATOM   3396  CD  LYS B 144      54.967  24.683  17.958  1.00 39.90           C  
ANISOU 3396  CD  LYS B 144     5347   4991   4820   -148   -307   -329       C  
ATOM   3397  CE  LYS B 144      56.413  25.137  17.792  1.00 46.18           C  
ANISOU 3397  CE  LYS B 144     6116   5782   5648   -155   -335   -320       C  
ATOM   3398  NZ  LYS B 144      56.743  25.307  16.351  1.00 48.12           N  
ANISOU 3398  NZ  LYS B 144     6326   6018   5936   -139   -320   -292       N  
ATOM   3399  N   ASN B 145      54.272  20.309  16.011  1.00 27.35           N  
ANISOU 3399  N   ASN B 145     3761   3448   3180    -88   -283   -243       N  
ATOM   3400  CA  ASN B 145      54.071  19.776  14.672  1.00 28.66           C  
ANISOU 3400  CA  ASN B 145     3914   3614   3361    -68   -265   -218       C  
ATOM   3401  C   ASN B 145      53.668  18.285  14.760  1.00 28.83           C  
ANISOU 3401  C   ASN B 145     3953   3649   3350    -58   -262   -205       C  
ATOM   3402  O   ASN B 145      53.440  17.637  13.713  1.00 25.70           O  
ANISOU 3402  O   ASN B 145     3551   3254   2960    -42   -248   -186       O  
ATOM   3403  CB  ASN B 145      55.352  19.915  13.861  1.00 32.26           C  
ANISOU 3403  CB  ASN B 145     4341   4066   3850    -61   -275   -196       C  
ATOM   3404  CG  ASN B 145      56.505  19.151  14.496  1.00 35.51           C  
ANISOU 3404  CG  ASN B 145     4751   4490   4250    -64   -304   -183       C  
ATOM   3405  OD1 ASN B 145      56.731  19.217  15.699  1.00 41.45           O  
ANISOU 3405  OD1 ASN B 145     5516   5249   4982    -80   -325   -199       O  
ATOM   3406  ND2 ASN B 145      57.185  18.360  13.695  1.00 37.87           N  
ANISOU 3406  ND2 ASN B 145     5036   4793   4559    -49   -303   -155       N  
ATOM   3407  N   LYS B 146      53.490  17.745  15.990  1.00 25.75           N  
ANISOU 3407  N   LYS B 146     3587   3271   2926    -67   -273   -216       N  
ATOM   3408  CA  LYS B 146      53.095  16.330  15.996  1.00 25.83           C  
ANISOU 3408  CA  LYS B 146     3611   3293   2911    -56   -268   -202       C  
ATOM   3409  C   LYS B 146      51.698  16.097  16.515  1.00 24.95           C  
ANISOU 3409  C   LYS B 146     3523   3181   2775    -58   -249   -217       C  
ATOM   3410  O   LYS B 146      51.332  14.952  16.776  1.00 25.02           O  
ANISOU 3410  O   LYS B 146     3547   3199   2760    -52   -246   -208       O  
ATOM   3411  CB  LYS B 146      54.045  15.443  16.784  1.00 27.43           C  
ANISOU 3411  CB  LYS B 146     3818   3509   3092    -58   -293   -191       C  
ATOM   3412  CG  LYS B 146      55.532  15.666  16.587  1.00 28.43           C  
ANISOU 3412  CG  LYS B 146     3921   3637   3242    -60   -317   -176       C  
ATOM   3413  CD  LYS B 146      55.965  15.199  15.211  1.00 30.48           C  
ANISOU 3413  CD  LYS B 146     4160   3892   3527    -41   -306   -149       C  
ATOM   3414  CE  LYS B 146      55.638  13.709  15.025  1.00 31.31           C  
ANISOU 3414  CE  LYS B 146     4278   4006   3612    -28   -297   -132       C  
ATOM   3415  NZ  LYS B 146      56.458  12.865  15.940  1.00 35.21           N  
ANISOU 3415  NZ  LYS B 146     4777   4514   4088    -30   -320   -120       N  
ATOM   3416  N   ILE B 147      50.899  17.151  16.636  1.00 23.71           N  
ANISOU 3416  N   ILE B 147     3370   3013   2626    -65   -234   -238       N  
ATOM   3417  CA  ILE B 147      49.525  16.974  17.066  1.00 24.52           C  
ANISOU 3417  CA  ILE B 147     3493   3113   2711    -66   -213   -250       C  
ATOM   3418  C   ILE B 147      48.523  17.836  16.330  1.00 23.93           C  
ANISOU 3418  C   ILE B 147     3409   3023   2661    -63   -188   -256       C  
ATOM   3419  O   ILE B 147      48.780  19.027  15.999  1.00 25.70           O  
ANISOU 3419  O   ILE B 147     3618   3235   2911    -68   -186   -265       O  
ATOM   3420  CB  ILE B 147      49.384  17.119  18.623  1.00 25.46           C  
ANISOU 3420  CB  ILE B 147     3638   3237   2797    -79   -219   -271       C  
ATOM   3421  CG1 ILE B 147      47.977  16.703  19.038  1.00 25.29           C  
ANISOU 3421  CG1 ILE B 147     3637   3213   2757    -77   -193   -277       C  
ATOM   3422  CG2 ILE B 147      49.749  18.551  19.039  1.00 26.10           C  
ANISOU 3422  CG2 ILE B 147     3717   3307   2892    -94   -225   -294       C  
ATOM   3423  CD1 ILE B 147      47.703  16.817  20.544  1.00 24.34           C  
ANISOU 3423  CD1 ILE B 147     3546   3097   2602    -88   -193   -298       C  
ATOM   3424  N   ILE B 148      47.419  17.224  15.969  1.00 22.81           N  
ANISOU 3424  N   ILE B 148     3272   2879   2514    -55   -169   -250       N  
ATOM   3425  CA  ILE B 148      46.425  17.949  15.221  1.00 23.43           C  
ANISOU 3425  CA  ILE B 148     3340   2944   2617    -52   -147   -253       C  
ATOM   3426  C   ILE B 148      45.040  17.525  15.534  1.00 23.54           C  
ANISOU 3426  C   ILE B 148     3368   2955   2620    -51   -126   -256       C  
ATOM   3427  O   ILE B 148      44.828  16.421  15.936  1.00 22.45           O  
ANISOU 3427  O   ILE B 148     3244   2826   2460    -48   -128   -249       O  
ATOM   3428  CB  ILE B 148      46.616  17.869  13.655  1.00 22.05           C  
ANISOU 3428  CB  ILE B 148     3142   2766   2467    -39   -146   -232       C  
ATOM   3429  CG1 ILE B 148      46.594  16.434  13.169  1.00 22.58           C  
ANISOU 3429  CG1 ILE B 148     3214   2844   2520    -29   -150   -213       C  
ATOM   3430  CG2 ILE B 148      47.868  18.669  13.266  1.00 22.77           C  
ANISOU 3430  CG2 ILE B 148     3214   2855   2580    -41   -160   -229       C  
ATOM   3431  CD1 ILE B 148      46.633  16.179  11.646  1.00 22.12           C  
ANISOU 3431  CD1 ILE B 148     3140   2784   2479    -16   -148   -194       C  
ATOM   3432  N   GLY B 149      44.071  18.392  15.233  1.00 25.19           N  
ANISOU 3432  N   GLY B 149     3570   3150   2851    -52   -105   -263       N  
ATOM   3433  CA  GLY B 149      42.664  17.997  15.307  1.00 26.74           C  
ANISOU 3433  CA  GLY B 149     3772   3340   3044    -49    -84   -261       C  
ATOM   3434  C   GLY B 149      42.082  17.825  13.926  1.00 26.81           C  
ANISOU 3434  C   GLY B 149     3763   3346   3078    -39    -78   -243       C  
ATOM   3435  O   GLY B 149      42.483  18.466  12.990  1.00 26.48           O  
ANISOU 3435  O   GLY B 149     3701   3300   3058    -35    -82   -236       O  
ATOM   3436  N   LEU B 150      41.136  16.914  13.847  1.00 28.74           N  
ANISOU 3436  N   LEU B 150     4012   3591   3315    -35    -70   -234       N  
ATOM   3437  CA  LEU B 150      40.184  16.794  12.759  1.00 29.04           C  
ANISOU 3437  CA  LEU B 150     4035   3622   3374    -28    -62   -220       C  
ATOM   3438  C   LEU B 150      39.264  17.988  12.761  1.00 30.97           C  
ANISOU 3438  C   LEU B 150     4269   3852   3645    -32    -41   -227       C  
ATOM   3439  O   LEU B 150      38.651  18.324  13.789  1.00 33.45           O  
ANISOU 3439  O   LEU B 150     4594   4158   3955    -37    -23   -240       O  
ATOM   3440  CB  LEU B 150      39.325  15.525  12.940  1.00 26.97           C  
ANISOU 3440  CB  LEU B 150     3784   3364   3100    -26    -58   -212       C  
ATOM   3441  CG  LEU B 150      38.264  15.247  11.834  1.00 28.11           C  
ANISOU 3441  CG  LEU B 150     3914   3502   3264    -22    -54   -197       C  
ATOM   3442  CD1 LEU B 150      38.868  14.965  10.447  1.00 25.83           C  
ANISOU 3442  CD1 LEU B 150     3614   3219   2981    -14    -71   -183       C  
ATOM   3443  CD2 LEU B 150      37.400  14.050  12.254  1.00 28.46           C  
ANISOU 3443  CD2 LEU B 150     3969   3546   3298    -22    -48   -192       C  
ATOM   3444  N   GLY B 151      39.107  18.588  11.588  1.00 32.71           N  
ANISOU 3444  N   GLY B 151     4469   4067   3892    -27    -41   -216       N  
ATOM   3445  CA  GLY B 151      38.145  19.668  11.363  1.00 28.37           C  
ANISOU 3445  CA  GLY B 151     3904   3501   3372    -28    -21   -216       C  
ATOM   3446  C   GLY B 151      37.822  19.783   9.872  1.00 27.35           C  
ANISOU 3446  C   GLY B 151     3753   3371   3265    -19    -26   -196       C  
ATOM   3447  O   GLY B 151      36.846  19.186   9.398  1.00 28.23           O  
ANISOU 3447  O   GLY B 151     3861   3483   3382    -17    -25   -184       O  
ATOM   3448  N   GLY B 152      38.602  20.548   9.127  1.00 25.39           N  
ANISOU 3448  N   GLY B 152     3491   3123   3031    -16    -33   -192       N  
ATOM   3449  CA  GLY B 152      38.242  20.834   7.683  1.00 25.35           C  
ANISOU 3449  CA  GLY B 152     3466   3117   3047     -7    -36   -172       C  
ATOM   3450  C   GLY B 152      38.281  19.775   6.635  1.00 24.88           C  
ANISOU 3450  C   GLY B 152     3408   3069   2975      0    -53   -155       C  
ATOM   3451  O   GLY B 152      37.642  19.883   5.542  1.00 26.15           O  
ANISOU 3451  O   GLY B 152     3556   3229   3150      5    -55   -139       O  
ATOM   3452  N   VAL B 153      39.025  18.712   6.891  1.00 24.73           N  
ANISOU 3452  N   VAL B 153     3406   3061   2928      0    -67   -158       N  
ATOM   3453  CA  VAL B 153      38.993  17.665   5.913  1.00 23.99           C  
ANISOU 3453  CA  VAL B 153     3316   2976   2822      7    -81   -144       C  
ATOM   3454  C   VAL B 153      37.547  17.151   5.878  1.00 24.02           C  
ANISOU 3454  C   VAL B 153     3319   2974   2830      3    -77   -140       C  
ATOM   3455  O   VAL B 153      36.969  16.925   4.801  1.00 23.47           O  
ANISOU 3455  O   VAL B 153     3243   2906   2768      8    -85   -126       O  
ATOM   3456  CB  VAL B 153      40.029  16.575   6.200  1.00 23.47           C  
ANISOU 3456  CB  VAL B 153     3268   2921   2729      9    -94   -147       C  
ATOM   3457  CG1 VAL B 153      39.744  15.304   5.394  1.00 22.92           C  
ANISOU 3457  CG1 VAL B 153     3206   2856   2643     14   -105   -136       C  
ATOM   3458  CG2 VAL B 153      41.488  17.098   6.037  1.00 22.19           C  
ANISOU 3458  CG2 VAL B 153     3101   2762   2566     14    -99   -147       C  
ATOM   3459  N   LEU B 154      36.954  16.980   7.042  1.00 24.05           N  
ANISOU 3459  N   LEU B 154     3331   2974   2833     -3    -65   -150       N  
ATOM   3460  CA  LEU B 154      35.596  16.463   7.100  1.00 25.59           C  
ANISOU 3460  CA  LEU B 154     3523   3163   3036     -7    -60   -145       C  
ATOM   3461  C   LEU B 154      34.633  17.533   6.647  1.00 26.75           C  
ANISOU 3461  C   LEU B 154     3648   3299   3216     -7    -48   -137       C  
ATOM   3462  O   LEU B 154      33.829  17.300   5.674  1.00 28.89           O  
ANISOU 3462  O   LEU B 154     3908   3569   3499     -5    -57   -121       O  
ATOM   3463  CB  LEU B 154      35.258  15.951   8.524  1.00 27.77           C  
ANISOU 3463  CB  LEU B 154     3814   3436   3299    -13    -47   -157       C  
ATOM   3464  CG  LEU B 154      33.787  15.593   8.870  1.00 27.18           C  
ANISOU 3464  CG  LEU B 154     3736   3352   3240    -18    -34   -152       C  
ATOM   3465  CD1 LEU B 154      33.277  14.419   8.041  1.00 26.06           C  
ANISOU 3465  CD1 LEU B 154     3593   3213   3095    -17    -51   -139       C  
ATOM   3466  CD2 LEU B 154      33.663  15.349  10.382  1.00 27.41           C  
ANISOU 3466  CD2 LEU B 154     3781   3377   3254    -22    -17   -164       C  
ATOM   3467  N   ASP B 155      34.737  18.735   7.258  1.00 25.88           N  
ANISOU 3467  N   ASP B 155     3531   3179   3120     -9    -30   -146       N  
ATOM   3468  CA  ASP B 155      33.819  19.792   6.866  1.00 27.04           C  
ANISOU 3468  CA  ASP B 155     3657   3314   3303     -9    -16   -136       C  
ATOM   3469  C   ASP B 155      33.847  20.064   5.367  1.00 26.15           C  
ANISOU 3469  C   ASP B 155     3527   3206   3201     -1    -31   -117       C  
ATOM   3470  O   ASP B 155      32.794  20.146   4.777  1.00 27.45           O  
ANISOU 3470  O   ASP B 155     3677   3366   3387     -1    -31   -102       O  
ATOM   3471  CB  ASP B 155      34.005  21.070   7.641  1.00 28.63           C  
ANISOU 3471  CB  ASP B 155     3854   3504   3520    -11      5   -150       C  
ATOM   3472  CG  ASP B 155      33.680  20.905   9.090  1.00 33.83           C  
ANISOU 3472  CG  ASP B 155     4528   4155   4168    -18     23   -167       C  
ATOM   3473  OD1 ASP B 155      32.622  20.299   9.411  1.00 39.37           O  
ANISOU 3473  OD1 ASP B 155     5231   4852   4873    -20     31   -162       O  
ATOM   3474  OD2 ASP B 155      34.494  21.353   9.925  1.00 34.78           O  
ANISOU 3474  OD2 ASP B 155     4662   4275   4276    -22     28   -185       O  
ATOM   3475  N   THR B 156      35.028  20.222   4.761  1.00 25.79           N  
ANISOU 3475  N   THR B 156     3484   3169   3144      4    -43   -117       N  
ATOM   3476  CA  THR B 156      35.092  20.524   3.296  1.00 25.14           C  
ANISOU 3476  CA  THR B 156     3388   3091   3071     12    -55    -97       C  
ATOM   3477  C   THR B 156      34.672  19.437   2.417  1.00 25.32           C  
ANISOU 3477  C   THR B 156     3417   3124   3080     14    -75    -85       C  
ATOM   3478  O   THR B 156      34.368  19.686   1.226  1.00 24.84           O  
ANISOU 3478  O   THR B 156     3345   3065   3026     20    -85    -68       O  
ATOM   3479  CB  THR B 156      36.528  20.948   2.791  1.00 23.97           C  
ANISOU 3479  CB  THR B 156     3242   2950   2916     20    -60    -97       C  
ATOM   3480  OG1 THR B 156      37.422  19.823   2.835  1.00 21.28           O  
ANISOU 3480  OG1 THR B 156     2921   2620   2542     22    -75   -102       O  
ATOM   3481  CG2 THR B 156      37.091  22.227   3.550  1.00 23.26           C  
ANISOU 3481  CG2 THR B 156     3142   2849   2844     17    -42   -109       C  
ATOM   3482  N   SER B 157      34.687  18.195   2.934  1.00 26.72           N  
ANISOU 3482  N   SER B 157     3612   3305   3232     10    -83    -94       N  
ATOM   3483  CA  SER B 157      34.204  17.107   2.139  1.00 25.58           C  
ANISOU 3483  CA  SER B 157     3475   3166   3076     10   -102    -85       C  
ATOM   3484  C   SER B 157      32.665  17.215   1.834  1.00 27.29           C  
ANISOU 3484  C   SER B 157     3675   3375   3317      5   -103    -72       C  
ATOM   3485  O   SER B 157      32.187  17.005   0.676  1.00 25.21           O  
ANISOU 3485  O   SER B 157     3405   3115   3055      7   -120    -58       O  
ATOM   3486  CB  SER B 157      34.621  15.783   2.792  1.00 26.58           C  
ANISOU 3486  CB  SER B 157     3624   3298   3174      7   -108    -97       C  
ATOM   3487  OG  SER B 157      33.686  15.324   3.733  1.00 25.24           O  
ANISOU 3487  OG  SER B 157     3455   3120   3011      0    -99   -102       O  
ATOM   3488  N   ARG B 158      31.882  17.673   2.792  1.00 26.72           N  
ANISOU 3488  N   ARG B 158     3592   3291   3267      0    -83    -76       N  
ATOM   3489  CA  ARG B 158      30.461  17.907   2.447  1.00 27.38           C  
ANISOU 3489  CA  ARG B 158     3655   3366   3381     -4    -82    -60       C  
ATOM   3490  C   ARG B 158      30.323  18.912   1.343  1.00 28.00           C  
ANISOU 3490  C   ARG B 158     3713   3445   3479      1    -87    -43       C  
ATOM   3491  O   ARG B 158      29.527  18.695   0.389  1.00 26.64           O  
ANISOU 3491  O   ARG B 158     3531   3275   3316      1   -105    -25       O  
ATOM   3492  CB  ARG B 158      29.651  18.477   3.590  1.00 28.06           C  
ANISOU 3492  CB  ARG B 158     3730   3436   3493     -9    -55    -64       C  
ATOM   3493  CG  ARG B 158      29.305  17.461   4.622  1.00 29.77           C  
ANISOU 3493  CG  ARG B 158     3962   3650   3699    -16    -48    -75       C  
ATOM   3494  CD  ARG B 158      30.514  17.043   5.357  1.00 26.68           C  
ANISOU 3494  CD  ARG B 158     3595   3267   3274    -15    -47    -94       C  
ATOM   3495  NE  ARG B 158      30.164  15.922   6.199  1.00 29.72           N  
ANISOU 3495  NE  ARG B 158     3994   3650   3646    -20    -44   -100       N  
ATOM   3496  CZ  ARG B 158      30.044  15.956   7.511  1.00 26.98           C  
ANISOU 3496  CZ  ARG B 158     3656   3296   3296    -23    -21   -112       C  
ATOM   3497  NH1 ARG B 158      30.216  17.068   8.136  1.00 26.58           N  
ANISOU 3497  NH1 ARG B 158     3603   3239   3255    -22      0   -120       N  
ATOM   3498  NH2 ARG B 158      29.718  14.877   8.161  1.00 26.44           N  
ANISOU 3498  NH2 ARG B 158     3600   3228   3217    -26    -19   -114       N  
ATOM   3499  N   LEU B 159      31.034  20.049   1.532  1.00 28.66           N  
ANISOU 3499  N   LEU B 159     3791   3526   3571      7    -71    -47       N  
ATOM   3500  CA  LEU B 159      30.919  21.243   0.687  1.00 26.48           C  
ANISOU 3500  CA  LEU B 159     3493   3248   3320     13    -68    -30       C  
ATOM   3501  C   LEU B 159      31.317  20.871  -0.717  1.00 25.95           C  
ANISOU 3501  C   LEU B 159     3431   3195   3234     21    -94    -16       C  
ATOM   3502  O   LEU B 159      30.586  21.058  -1.698  1.00 24.80           O  
ANISOU 3502  O   LEU B 159     3271   3051   3100     23   -106      4       O  
ATOM   3503  CB  LEU B 159      31.838  22.385   1.209  1.00 28.53           C  
ANISOU 3503  CB  LEU B 159     3750   3501   3589     17    -46    -40       C  
ATOM   3504  CG  LEU B 159      31.880  23.728   0.447  1.00 30.12           C  
ANISOU 3504  CG  LEU B 159     3928   3697   3818     25    -38    -24       C  
ATOM   3505  CD1 LEU B 159      30.468  24.202   0.085  1.00 29.85           C  
ANISOU 3505  CD1 LEU B 159     3869   3654   3819     24    -33     -3       C  
ATOM   3506  CD2 LEU B 159      32.584  24.747   1.369  1.00 30.35           C  
ANISOU 3506  CD2 LEU B 159     3955   3714   3860     24    -13    -40       C  
ATOM   3507  N   LYS B 160      32.484  20.261  -0.775  1.00 26.08           N  
ANISOU 3507  N   LYS B 160     3469   3221   3218     24   -102    -28       N  
ATOM   3508  CA  LYS B 160      32.978  19.652  -2.008  1.00 24.98           C  
ANISOU 3508  CA  LYS B 160     3342   3095   3052     32   -124    -19       C  
ATOM   3509  C   LYS B 160      31.936  18.746  -2.677  1.00 24.24           C  
ANISOU 3509  C   LYS B 160     3251   3005   2953     27   -147     -9       C  
ATOM   3510  O   LYS B 160      31.626  18.908  -3.901  1.00 23.11           O  
ANISOU 3510  O   LYS B 160     3102   2868   2809     32   -164      8       O  
ATOM   3511  CB  LYS B 160      34.228  18.893  -1.610  1.00 23.94           C  
ANISOU 3511  CB  LYS B 160     3235   2970   2890     34   -126    -35       C  
ATOM   3512  CG  LYS B 160      35.343  19.829  -1.325  1.00 22.68           C  
ANISOU 3512  CG  LYS B 160     3071   2809   2737     40   -110    -40       C  
ATOM   3513  CD  LYS B 160      36.584  19.003  -1.508  1.00 23.61           C  
ANISOU 3513  CD  LYS B 160     3210   2935   2822     46   -118    -47       C  
ATOM   3514  CE  LYS B 160      37.879  19.777  -1.339  1.00 24.26           C  
ANISOU 3514  CE  LYS B 160     3290   3018   2910     53   -107    -49       C  
ATOM   3515  NZ  LYS B 160      38.397  19.480   0.032  1.00 23.34           N  
ANISOU 3515  NZ  LYS B 160     3182   2898   2787     45   -100    -70       N  
ATOM   3516  N   TYR B 161      31.393  17.815  -1.875  1.00 23.06           N  
ANISOU 3516  N   TYR B 161     3110   2851   2800     16   -149    -20       N  
ATOM   3517  CA  TYR B 161      30.447  16.855  -2.385  1.00 24.55           C  
ANISOU 3517  CA  TYR B 161     3301   3041   2984      9   -171    -14       C  
ATOM   3518  C   TYR B 161      29.168  17.505  -2.910  1.00 23.88           C  
ANISOU 3518  C   TYR B 161     3189   2950   2932      6   -177      6       C  
ATOM   3519  O   TYR B 161      28.768  17.290  -4.092  1.00 21.86           O  
ANISOU 3519  O   TYR B 161     2933   2703   2671      7   -203     21       O  
ATOM   3520  CB  TYR B 161      30.128  15.723  -1.371  1.00 26.98           C  
ANISOU 3520  CB  TYR B 161     3621   3344   3286      0   -169    -29       C  
ATOM   3521  CG  TYR B 161      29.254  14.658  -2.011  1.00 30.84           C  
ANISOU 3521  CG  TYR B 161     4114   3833   3771     -7   -195    -23       C  
ATOM   3522  CD1 TYR B 161      29.800  13.767  -2.942  1.00 30.30           C  
ANISOU 3522  CD1 TYR B 161     4068   3774   3669     -4   -218    -26       C  
ATOM   3523  CD2 TYR B 161      27.849  14.613  -1.770  1.00 32.49           C  
ANISOU 3523  CD2 TYR B 161     4302   4030   4010    -18   -198    -13       C  
ATOM   3524  CE1 TYR B 161      29.011  12.813  -3.557  1.00 33.23           C  
ANISOU 3524  CE1 TYR B 161     4444   4144   4036    -13   -244    -23       C  
ATOM   3525  CE2 TYR B 161      27.053  13.648  -2.374  1.00 32.11           C  
ANISOU 3525  CE2 TYR B 161     4256   3982   3961    -26   -224     -7       C  
ATOM   3526  CZ  TYR B 161      27.634  12.768  -3.272  1.00 34.68           C  
ANISOU 3526  CZ  TYR B 161     4606   4317   4251    -25   -249    -13       C  
ATOM   3527  OH  TYR B 161      26.871  11.842  -3.941  1.00 36.88           O  
ANISOU 3527  OH  TYR B 161     4889   4594   4528    -34   -278    -10       O  
ATOM   3528  N   TYR B 162      28.578  18.360  -2.075  1.00 23.64           N  
ANISOU 3528  N   TYR B 162     3136   2907   2936      3   -154      9       N  
ATOM   3529  CA  TYR B 162      27.357  19.078  -2.456  1.00 25.89           C  
ANISOU 3529  CA  TYR B 162     3392   3185   3259      1   -155     31       C  
ATOM   3530  C   TYR B 162      27.498  19.895  -3.724  1.00 27.99           C  
ANISOU 3530  C   TYR B 162     3646   3459   3528     10   -167     52       C  
ATOM   3531  O   TYR B 162      26.591  19.850  -4.631  1.00 28.81           O  
ANISOU 3531  O   TYR B 162     3736   3566   3643      7   -189     73       O  
ATOM   3532  CB  TYR B 162      26.850  19.990  -1.337  1.00 26.54           C  
ANISOU 3532  CB  TYR B 162     3454   3251   3378      0   -121     30       C  
ATOM   3533  CG  TYR B 162      26.470  19.217  -0.123  1.00 26.93           C  
ANISOU 3533  CG  TYR B 162     3512   3291   3427     -9   -108     15       C  
ATOM   3534  CD1 TYR B 162      25.940  17.921  -0.228  1.00 30.20           C  
ANISOU 3534  CD1 TYR B 162     3935   3707   3830    -17   -129     14       C  
ATOM   3535  CD2 TYR B 162      26.705  19.723   1.147  1.00 27.80           C  
ANISOU 3535  CD2 TYR B 162     3624   3390   3545     -9    -75      0       C  
ATOM   3536  CE1 TYR B 162      25.610  17.195   0.922  1.00 31.47           C  
ANISOU 3536  CE1 TYR B 162     4104   3859   3992    -24   -115      2       C  
ATOM   3537  CE2 TYR B 162      26.401  19.001   2.282  1.00 28.08           C  
ANISOU 3537  CE2 TYR B 162     3671   3419   3578    -16    -62    -12       C  
ATOM   3538  CZ  TYR B 162      25.841  17.741   2.165  1.00 29.80           C  
ANISOU 3538  CZ  TYR B 162     3895   3638   3787    -23    -81    -10       C  
ATOM   3539  OH  TYR B 162      25.509  17.031   3.312  1.00 33.34           O  
ANISOU 3539  OH  TYR B 162     4353   4078   4234    -28    -66    -21       O  
ATOM   3540  N   ILE B 163      28.601  20.647  -3.808  1.00 26.42           N  
ANISOU 3540  N   ILE B 163     3452   3264   3321     20   -153     47       N  
ATOM   3541  CA  ILE B 163      28.837  21.343  -5.042  1.00 27.57           C  
ANISOU 3541  CA  ILE B 163     3590   3418   3465     31   -163     68       C  
ATOM   3542  C   ILE B 163      29.041  20.411  -6.257  1.00 27.90           C  
ANISOU 3542  C   ILE B 163     3652   3476   3469     33   -196     73       C  
ATOM   3543  O   ILE B 163      28.534  20.721  -7.403  1.00 26.77           O  
ANISOU 3543  O   ILE B 163     3500   3340   3330     37   -215     96       O  
ATOM   3544  CB  ILE B 163      30.013  22.386  -4.905  1.00 28.83           C  
ANISOU 3544  CB  ILE B 163     3748   3576   3627     42   -139     64       C  
ATOM   3545  CG1 ILE B 163      29.567  23.656  -4.150  1.00 27.61           C  
ANISOU 3545  CG1 ILE B 163     3566   3405   3517     41   -109     68       C  
ATOM   3546  CG2 ILE B 163      30.577  22.781  -6.268  1.00 26.24           C  
ANISOU 3546  CG2 ILE B 163     3422   3261   3285     55   -151     82       C  
ATOM   3547  CD1 ILE B 163      30.775  24.259  -3.399  1.00 29.95           C  
ANISOU 3547  CD1 ILE B 163     3869   3696   3811     45    -85     49       C  
ATOM   3548  N   SER B 164      29.806  19.306  -6.077  1.00 25.53           N  
ANISOU 3548  N   SER B 164     3383   3183   3134     32   -203     52       N  
ATOM   3549  CA  SER B 164      30.071  18.500  -7.241  1.00 24.85           C  
ANISOU 3549  CA  SER B 164     3319   3109   3012     36   -231     55       C  
ATOM   3550  C   SER B 164      28.795  17.966  -7.845  1.00 26.86           C  
ANISOU 3550  C   SER B 164     3567   3365   3271     26   -260     67       C  
ATOM   3551  O   SER B 164      28.691  17.781  -9.129  1.00 24.99           O  
ANISOU 3551  O   SER B 164     3340   3139   3013     29   -287     80       O  
ATOM   3552  CB  SER B 164      30.985  17.372  -6.927  1.00 23.67           C  
ANISOU 3552  CB  SER B 164     3201   2963   2827     36   -232     33       C  
ATOM   3553  OG  SER B 164      30.212  16.363  -6.284  1.00 23.76           O  
ANISOU 3553  OG  SER B 164     3216   2968   2841     22   -241     22       O  
ATOM   3554  N   GLN B 165      27.838  17.704  -6.939  1.00 27.90           N  
ANISOU 3554  N   GLN B 165     3685   3485   3431     13   -256     64       N  
ATOM   3555  CA  GLN B 165      26.497  17.203  -7.316  1.00 32.27           C  
ANISOU 3555  CA  GLN B 165     4226   4036   3999      0   -283     76       C  
ATOM   3556  C   GLN B 165      25.690  18.174  -8.171  1.00 33.10           C  
ANISOU 3556  C   GLN B 165     4303   4143   4129      3   -294    106       C  
ATOM   3557  O   GLN B 165      25.096  17.769  -9.156  1.00 32.22           O  
ANISOU 3557  O   GLN B 165     4194   4039   4009     -1   -328    118       O  
ATOM   3558  CB  GLN B 165      25.654  16.714  -6.102  1.00 33.89           C  
ANISOU 3558  CB  GLN B 165     4419   4226   4231    -12   -272     67       C  
ATOM   3559  CG  GLN B 165      26.066  15.368  -5.488  1.00 35.82           C  
ANISOU 3559  CG  GLN B 165     4690   4468   4449    -18   -274     43       C  
ATOM   3560  CD  GLN B 165      26.719  14.369  -6.457  1.00 38.90           C  
ANISOU 3560  CD  GLN B 165     5114   4870   4795    -16   -301     34       C  
ATOM   3561  OE1 GLN B 165      27.881  14.545  -6.906  1.00 42.47           O  
ANISOU 3561  OE1 GLN B 165     5586   5333   5218     -4   -296     28       O  
ATOM   3562  NE2 GLN B 165      25.988  13.285  -6.763  1.00 42.74           N  
ANISOU 3562  NE2 GLN B 165     5607   5354   5276    -29   -328     31       N  
ATOM   3563  N   LYS B 166      25.689  19.459  -7.783  1.00 32.40           N  
ANISOU 3563  N   LYS B 166     4189   4047   4072     10   -267    117       N  
ATOM   3564  CA  LYS B 166      25.059  20.476  -8.564  1.00 29.17           C  
ANISOU 3564  CA  LYS B 166     3753   3640   3689     14   -273    147       C  
ATOM   3565  C   LYS B 166      25.761  20.563  -9.883  1.00 29.06           C  
ANISOU 3565  C   LYS B 166     3756   3643   3639     26   -293    156       C  
ATOM   3566  O   LYS B 166      25.123  20.662 -10.938  1.00 28.61           O  
ANISOU 3566  O   LYS B 166     3692   3596   3582     25   -321    179       O  
ATOM   3567  CB  LYS B 166      25.142  21.825  -7.845  1.00 31.68           C  
ANISOU 3567  CB  LYS B 166     4045   3946   4046     21   -234    154       C  
ATOM   3568  CG  LYS B 166      24.556  22.997  -8.623  1.00 35.93           C  
ANISOU 3568  CG  LYS B 166     4552   4484   4615     28   -236    187       C  
ATOM   3569  CD  LYS B 166      23.025  22.962  -8.588  1.00 38.24           C  
ANISOU 3569  CD  LYS B 166     4814   4768   4947     17   -249    208       C  
ATOM   3570  CE  LYS B 166      22.461  23.546  -9.879  1.00 41.25           C  
ANISOU 3570  CE  LYS B 166     5175   5159   5337     22   -274    244       C  
ATOM   3571  NZ  LYS B 166      21.035  23.823  -9.609  1.00 41.96           N  
ANISOU 3571  NZ  LYS B 166     5227   5235   5478     13   -276    267       N  
ATOM   3572  N   LEU B 167      27.089  20.546  -9.872  1.00 28.53           N  
ANISOU 3572  N   LEU B 167     3714   3583   3543     37   -278    141       N  
ATOM   3573  CA  LEU B 167      27.815  20.817 -11.147  1.00 28.84           C  
ANISOU 3573  CA  LEU B 167     3768   3637   3551     51   -289    153       C  
ATOM   3574  C   LEU B 167      28.072  19.631 -12.045  1.00 29.55           C  
ANISOU 3574  C   LEU B 167     3893   3740   3592     50   -321    145       C  
ATOM   3575  O   LEU B 167      28.681  19.767 -13.099  1.00 30.19           O  
ANISOU 3575  O   LEU B 167     3992   3834   3644     62   -329    154       O  
ATOM   3576  CB  LEU B 167      29.102  21.518 -10.833  1.00 26.88           C  
ANISOU 3576  CB  LEU B 167     3524   3387   3300     65   -257    146       C  
ATOM   3577  CG  LEU B 167      28.880  22.958 -10.391  1.00 25.92           C  
ANISOU 3577  CG  LEU B 167     3368   3255   3225     69   -230    161       C  
ATOM   3578  CD1 LEU B 167      30.220  23.593 -10.074  1.00 26.20           C  
ANISOU 3578  CD1 LEU B 167     3408   3287   3257     81   -200    152       C  
ATOM   3579  CD2 LEU B 167      28.192  23.724 -11.451  1.00 26.12           C  
ANISOU 3579  CD2 LEU B 167     3372   3286   3265     75   -243    195       C  
ATOM   3580  N   ASN B 168      27.635  18.443 -11.624  1.00 29.82           N  
ANISOU 3580  N   ASN B 168     3941   3770   3617     35   -336    127       N  
ATOM   3581  CA  ASN B 168      27.914  17.237 -12.378  1.00 29.68           C  
ANISOU 3581  CA  ASN B 168     3960   3762   3553     33   -364    114       C  
ATOM   3582  C   ASN B 168      29.386  16.995 -12.634  1.00 28.15           C  
ANISOU 3582  C   ASN B 168     3798   3575   3321     48   -349    100       C  
ATOM   3583  O   ASN B 168      29.808  16.847 -13.797  1.00 24.87           O  
ANISOU 3583  O   ASN B 168     3405   3171   2870     58   -363    107       O  
ATOM   3584  CB  ASN B 168      27.182  17.246 -13.746  1.00 34.79           C  
ANISOU 3584  CB  ASN B 168     4609   4421   4187     32   -401    135       C  
ATOM   3585  CG  ASN B 168      26.036  16.277 -13.761  1.00 43.51           C  
ANISOU 3585  CG  ASN B 168     5713   5521   5297     12   -435    131       C  
ATOM   3586  OD1 ASN B 168      24.991  16.518 -13.111  1.00 50.71           O  
ANISOU 3586  OD1 ASN B 168     6591   6422   6252      0   -435    140       O  
ATOM   3587  ND2 ASN B 168      26.230  15.128 -14.434  1.00 44.02           N  
ANISOU 3587  ND2 ASN B 168     5814   5592   5318      8   -462    116       N  
ATOM   3588  N   VAL B 169      30.179  16.925 -11.561  1.00 26.42           N  
ANISOU 3588  N   VAL B 169     3581   3348   3108     50   -320     82       N  
ATOM   3589  CA  VAL B 169      31.606  16.717 -11.735  1.00 27.25           C  
ANISOU 3589  CA  VAL B 169     3713   3458   3182     64   -304     72       C  
ATOM   3590  C   VAL B 169      32.084  15.790 -10.635  1.00 27.23           C  
ANISOU 3590  C   VAL B 169     3724   3447   3174     57   -293     46       C  
ATOM   3591  O   VAL B 169      31.414  15.636  -9.620  1.00 28.63           O  
ANISOU 3591  O   VAL B 169     3885   3614   3375     45   -289     38       O  
ATOM   3592  CB  VAL B 169      32.479  18.038 -11.653  1.00 26.17           C  
ANISOU 3592  CB  VAL B 169     3560   3321   3061     80   -274     83       C  
ATOM   3593  CG1 VAL B 169      32.130  19.048 -12.699  1.00 25.26           C  
ANISOU 3593  CG1 VAL B 169     3429   3213   2953     89   -281    112       C  
ATOM   3594  CG2 VAL B 169      32.559  18.589 -10.212  1.00 25.32           C  
ANISOU 3594  CG2 VAL B 169     3429   3201   2990     74   -247     73       C  
ATOM   3595  N   CYS B 170      33.228  15.167 -10.863  1.00 29.00           N  
ANISOU 3595  N   CYS B 170     3977   3675   3365     67   -286     34       N  
ATOM   3596  CA  CYS B 170      33.840  14.335  -9.860  1.00 30.12           C  
ANISOU 3596  CA  CYS B 170     4132   3810   3500     63   -274     12       C  
ATOM   3597  C   CYS B 170      33.955  15.091  -8.521  1.00 26.76           C  
ANISOU 3597  C   CYS B 170     3681   3377   3109     60   -249      8       C  
ATOM   3598  O   CYS B 170      34.452  16.185  -8.471  1.00 27.91           O  
ANISOU 3598  O   CYS B 170     3810   3522   3269     69   -231     17       O  
ATOM   3599  CB  CYS B 170      35.213  13.908 -10.376  1.00 34.00           C  
ANISOU 3599  CB  CYS B 170     4651   4307   3959     78   -265      7       C  
ATOM   3600  SG  CYS B 170      35.986  12.718  -9.269  1.00 37.32           S  
ANISOU 3600  SG  CYS B 170     5090   4720   4369     74   -253    -16       S  
ATOM   3601  N   PRO B 171      33.412  14.555  -7.443  1.00 26.71           N  
ANISOU 3601  N   PRO B 171     3669   3362   3115     46   -247     -4       N  
ATOM   3602  CA  PRO B 171      33.472  15.200  -6.076  1.00 25.69           C  
ANISOU 3602  CA  PRO B 171     3520   3224   3014     42   -223    -10       C  
ATOM   3603  C   PRO B 171      34.826  15.839  -5.745  1.00 26.18           C  
ANISOU 3603  C   PRO B 171     3583   3288   3074     54   -201    -14       C  
ATOM   3604  O   PRO B 171      34.922  17.070  -5.422  1.00 26.84           O  
ANISOU 3604  O   PRO B 171     3645   3368   3183     56   -184     -7       O  
ATOM   3605  CB  PRO B 171      33.173  14.043  -5.167  1.00 24.01           C  
ANISOU 3605  CB  PRO B 171     3319   3006   2796     31   -225    -27       C  
ATOM   3606  CG  PRO B 171      32.209  13.258  -5.913  1.00 24.67           C  
ANISOU 3606  CG  PRO B 171     3409   3090   2874     23   -251    -23       C  
ATOM   3607  CD  PRO B 171      32.862  13.190  -7.324  1.00 26.93           C  
ANISOU 3607  CD  PRO B 171     3714   3387   3130     35   -264    -16       C  
ATOM   3608  N   ARG B 172      35.876  15.062  -5.976  1.00 25.74           N  
ANISOU 3608  N   ARG B 172     3552   3237   2990     61   -202    -21       N  
ATOM   3609  CA  ARG B 172      37.236  15.405  -5.597  1.00 27.41           C  
ANISOU 3609  CA  ARG B 172     3766   3450   3198     71   -184    -25       C  
ATOM   3610  C   ARG B 172      37.805  16.637  -6.393  1.00 27.65           C  
ANISOU 3610  C   ARG B 172     3784   3483   3238     84   -174     -8       C  
ATOM   3611  O   ARG B 172      38.782  17.283  -5.952  1.00 28.19           O  
ANISOU 3611  O   ARG B 172     3844   3548   3316     90   -157     -9       O  
ATOM   3612  CB  ARG B 172      38.102  14.146  -5.836  1.00 28.96           C  
ANISOU 3612  CB  ARG B 172     3992   3649   3362     76   -188    -34       C  
ATOM   3613  CG  ARG B 172      39.586  14.249  -5.517  1.00 31.53           C  
ANISOU 3613  CG  ARG B 172     4321   3975   3681     87   -172    -36       C  
ATOM   3614  CD  ARG B 172      39.839  14.134  -4.028  1.00 29.69           C  
ANISOU 3614  CD  ARG B 172     4082   3737   3459     77   -163    -50       C  
ATOM   3615  NE  ARG B 172      41.244  14.359  -3.641  1.00 27.23           N  
ANISOU 3615  NE  ARG B 172     3770   3426   3147     85   -150    -51       N  
ATOM   3616  CZ  ARG B 172      41.669  14.107  -2.397  1.00 27.46           C  
ANISOU 3616  CZ  ARG B 172     3799   3453   3179     79   -145    -63       C  
ATOM   3617  NH1 ARG B 172      40.827  13.561  -1.520  1.00 25.74           N  
ANISOU 3617  NH1 ARG B 172     3584   3232   2960     66   -149    -74       N  
ATOM   3618  NH2 ARG B 172      42.906  14.362  -2.025  1.00 26.40           N  
ANISOU 3618  NH2 ARG B 172     3663   3320   3048     84   -137    -63       N  
ATOM   3619  N   ASP B 173      37.245  16.866  -7.578  1.00 26.39           N  
ANISOU 3619  N   ASP B 173     3624   3328   3073     89   -186      6       N  
ATOM   3620  CA  ASP B 173      37.655  17.923  -8.421  1.00 28.59           C  
ANISOU 3620  CA  ASP B 173     3892   3611   3360    103   -178     25       C  
ATOM   3621  C   ASP B 173      37.149  19.270  -7.867  1.00 29.53           C  
ANISOU 3621  C   ASP B 173     3978   3722   3519     98   -165     32       C  
ATOM   3622  O   ASP B 173      37.509  20.299  -8.385  1.00 33.69           O  
ANISOU 3622  O   ASP B 173     4491   4249   4060    109   -154     48       O  
ATOM   3623  CB  ASP B 173      37.170  17.694  -9.856  1.00 28.42           C  
ANISOU 3623  CB  ASP B 173     3883   3598   3316    109   -197     40       C  
ATOM   3624  CG  ASP B 173      38.074  16.681 -10.646  1.00 32.06           C  
ANISOU 3624  CG  ASP B 173     4378   4065   3736    120   -202     36       C  
ATOM   3625  OD1 ASP B 173      39.065  16.193 -10.098  1.00 30.68           O  
ANISOU 3625  OD1 ASP B 173     4214   3887   3553    124   -189     25       O  
ATOM   3626  OD2 ASP B 173      37.832  16.378 -11.857  1.00 33.18           O  
ANISOU 3626  OD2 ASP B 173     4538   4214   3852    127   -217     46       O  
ATOM   3627  N   VAL B 174      36.344  19.272  -6.824  1.00 27.48           N  
ANISOU 3627  N   VAL B 174     3706   3454   3279     84   -163     22       N  
ATOM   3628  CA  VAL B 174      35.978  20.534  -6.220  1.00 26.47           C  
ANISOU 3628  CA  VAL B 174     3550   3317   3189     81   -146     26       C  
ATOM   3629  C   VAL B 174      36.879  20.708  -5.016  1.00 28.18           C  
ANISOU 3629  C   VAL B 174     3766   3526   3412     78   -128      8       C  
ATOM   3630  O   VAL B 174      37.087  19.775  -4.230  1.00 26.06           O  
ANISOU 3630  O   VAL B 174     3515   3259   3128     71   -131     -9       O  
ATOM   3631  CB  VAL B 174      34.488  20.591  -5.838  1.00 25.00           C  
ANISOU 3631  CB  VAL B 174     3348   3124   3025     68   -152     28       C  
ATOM   3632  CG1 VAL B 174      34.197  21.874  -5.095  1.00 23.21           C  
ANISOU 3632  CG1 VAL B 174     3094   2885   2837     65   -129     30       C  
ATOM   3633  CG2 VAL B 174      33.613  20.532  -7.129  1.00 24.62           C  
ANISOU 3633  CG2 VAL B 174     3297   3084   2973     71   -173     50       C  
ATOM   3634  N   ASN B 175      37.460  21.903  -4.902  1.00 28.41           N  
ANISOU 3634  N   ASN B 175     3779   3550   3465     83   -111     13       N  
ATOM   3635  CA  ASN B 175      38.316  22.157  -3.824  1.00 26.53           C  
ANISOU 3635  CA  ASN B 175     3540   3305   3234     79    -97     -3       C  
ATOM   3636  C   ASN B 175      37.710  23.357  -3.213  1.00 27.12           C  
ANISOU 3636  C   ASN B 175     3591   3367   3345     73    -80     -4       C  
ATOM   3637  O   ASN B 175      37.181  24.177  -3.955  1.00 23.44           O  
ANISOU 3637  O   ASN B 175     3108   2898   2900     79    -77     14       O  
ATOM   3638  CB  ASN B 175      39.711  22.507  -4.303  1.00 29.60           C  
ANISOU 3638  CB  ASN B 175     3930   3696   3619     92    -90      2       C  
ATOM   3639  CG  ASN B 175      40.752  22.012  -3.338  1.00 35.28           C  
ANISOU 3639  CG  ASN B 175     4661   4415   4327     88    -88    -16       C  
ATOM   3640  OD1 ASN B 175      40.547  22.000  -2.054  1.00 33.51           O  
ANISOU 3640  OD1 ASN B 175     4437   4184   4110     75    -84    -35       O  
ATOM   3641  ND2 ASN B 175      41.859  21.489  -3.920  1.00 34.94           N  
ANISOU 3641  ND2 ASN B 175     4631   4379   4265     99    -91    -10       N  
ATOM   3642  N   ALA B 176      37.851  23.492  -1.874  1.00 23.27           N  
ANISOU 3642  N   ALA B 176     3105   2871   2866     63    -69    -25       N  
ATOM   3643  CA  ALA B 176      37.061  24.481  -1.148  1.00 24.09           C  
ANISOU 3643  CA  ALA B 176     3189   2959   3002     55    -51    -29       C  
ATOM   3644  C   ALA B 176      37.734  24.546   0.242  1.00 23.68           C  
ANISOU 3644  C   ALA B 176     3147   2901   2949     46    -41    -55       C  
ATOM   3645  O   ALA B 176      38.354  23.583   0.655  1.00 21.35           O  
ANISOU 3645  O   ALA B 176     2871   2614   2625     44    -52    -67       O  
ATOM   3646  CB  ALA B 176      35.619  24.040  -0.993  1.00 24.14           C  
ANISOU 3646  CB  ALA B 176     3193   2963   3013     48    -55    -26       C  
ATOM   3647  N   HIS B 177      37.666  25.684   0.909  1.00 24.08           N  
ANISOU 3647  N   HIS B 177     3183   2937   3028     41    -22    -63       N  
ATOM   3648  CA  HIS B 177      38.351  25.749   2.202  1.00 25.37           C  
ANISOU 3648  CA  HIS B 177     3358   3095   3185     32    -16    -88       C  
ATOM   3649  C   HIS B 177      37.427  26.132   3.335  1.00 26.52           C  
ANISOU 3649  C   HIS B 177     3504   3227   3345     21      1   -104       C  
ATOM   3650  O   HIS B 177      36.662  27.109   3.258  1.00 29.49           O  
ANISOU 3650  O   HIS B 177     3862   3589   3754     21     18    -97       O  
ATOM   3651  CB  HIS B 177      39.499  26.746   2.061  1.00 24.31           C  
ANISOU 3651  CB  HIS B 177     3212   2953   3068     35    -10    -89       C  
ATOM   3652  CG  HIS B 177      40.573  26.318   1.098  1.00 25.25           C  
ANISOU 3652  CG  HIS B 177     3334   3085   3173     47    -24    -75       C  
ATOM   3653  ND1 HIS B 177      41.814  25.921   1.514  1.00 26.09           N  
ANISOU 3653  ND1 HIS B 177     3451   3196   3263     45    -32    -85       N  
ATOM   3654  CD2 HIS B 177      40.604  26.277  -0.312  1.00 25.90           C  
ANISOU 3654  CD2 HIS B 177     3409   3175   3255     61    -29    -49       C  
ATOM   3655  CE1 HIS B 177      42.564  25.578   0.453  1.00 25.49           C  
ANISOU 3655  CE1 HIS B 177     3375   3130   3178     58    -41    -67       C  
ATOM   3656  NE2 HIS B 177      41.826  25.781  -0.674  1.00 25.41           N  
ANISOU 3656  NE2 HIS B 177     3356   3122   3175     68    -39    -46       N  
ATOM   3657  N   ILE B 178      37.548  25.467   4.466  1.00 28.85           N  
ANISOU 3657  N   ILE B 178     3818   3523   3618     12      0   -125       N  
ATOM   3658  CA  ILE B 178      36.718  25.807   5.648  1.00 28.61           C  
ANISOU 3658  CA  ILE B 178     3793   3480   3598      2     19   -141       C  
ATOM   3659  C   ILE B 178      37.650  25.899   6.833  1.00 27.47           C  
ANISOU 3659  C   ILE B 178     3666   3334   3437     -5     20   -167       C  
ATOM   3660  O   ILE B 178      38.299  24.921   7.169  1.00 26.87           O  
ANISOU 3660  O   ILE B 178     3608   3271   3330     -7      4   -174       O  
ATOM   3661  CB  ILE B 178      35.560  24.813   5.919  1.00 28.23           C  
ANISOU 3661  CB  ILE B 178     3752   3434   3537      0     19   -138       C  
ATOM   3662  CG1 ILE B 178      34.532  24.833   4.762  1.00 28.58           C  
ANISOU 3662  CG1 ILE B 178     3777   3480   3602      6     16   -112       C  
ATOM   3663  CG2 ILE B 178      34.854  25.197   7.227  1.00 28.86           C  
ANISOU 3663  CG2 ILE B 178     3838   3499   3625     -8     44   -156       C  
ATOM   3664  CD1 ILE B 178      33.576  23.645   4.764  1.00 29.00           C  
ANISOU 3664  CD1 ILE B 178     3838   3539   3642      4      7   -105       C  
ATOM   3665  N   VAL B 179      37.708  27.083   7.447  1.00 27.55           N  
ANISOU 3665  N   VAL B 179     3670   3327   3470    -11     39   -181       N  
ATOM   3666  CA  VAL B 179      38.766  27.376   8.437  1.00 28.16           C  
ANISOU 3666  CA  VAL B 179     3761   3401   3535    -20     36   -206       C  
ATOM   3667  C   VAL B 179      38.258  27.792   9.784  1.00 28.14           C  
ANISOU 3667  C   VAL B 179     3774   3386   3532    -30     56   -231       C  
ATOM   3668  O   VAL B 179      37.081  27.949   9.973  1.00 30.19           O  
ANISOU 3668  O   VAL B 179     4031   3635   3805    -30     77   -228       O  
ATOM   3669  CB  VAL B 179      39.783  28.419   7.862  1.00 27.73           C  
ANISOU 3669  CB  VAL B 179     3689   3340   3505    -17     34   -202       C  
ATOM   3670  CG1 VAL B 179      40.385  27.867   6.557  1.00 25.27           C  
ANISOU 3670  CG1 VAL B 179     3368   3045   3189     -5     15   -178       C  
ATOM   3671  CG2 VAL B 179      39.074  29.729   7.537  1.00 24.83           C  
ANISOU 3671  CG2 VAL B 179     3300   2953   3181    -15     59   -197       C  
ATOM   3672  N   GLY B 180      39.144  27.915  10.747  1.00 28.25           N  
ANISOU 3672  N   GLY B 180     3806   3400   3529    -40     50   -254       N  
ATOM   3673  CA  GLY B 180      38.783  28.546  11.971  1.00 28.56           C  
ANISOU 3673  CA  GLY B 180     3860   3423   3568    -50     70   -280       C  
ATOM   3674  C   GLY B 180      38.583  27.612  13.114  1.00 31.06           C  
ANISOU 3674  C   GLY B 180     4206   3748   3845    -56     68   -295       C  
ATOM   3675  O   GLY B 180      39.440  27.526  14.002  1.00 30.02           O  
ANISOU 3675  O   GLY B 180     4095   3621   3689    -65     56   -316       O  
ATOM   3676  N   ALA B 181      37.396  27.003  13.136  1.00 30.71           N  
ANISOU 3676  N   ALA B 181     4164   3704   3798    -51     82   -285       N  
ATOM   3677  CA  ALA B 181      37.045  25.990  14.090  1.00 31.39           C  
ANISOU 3677  CA  ALA B 181     4276   3799   3850    -54     83   -293       C  
ATOM   3678  C   ALA B 181      36.172  24.996  13.381  1.00 33.13           C  
ANISOU 3678  C   ALA B 181     4487   4028   4072    -46     80   -268       C  
ATOM   3679  O   ALA B 181      35.568  25.309  12.349  1.00 33.87           O  
ANISOU 3679  O   ALA B 181     4556   4116   4195    -39     85   -248       O  
ATOM   3680  CB  ALA B 181      36.328  26.591  15.340  1.00 32.05           C  
ANISOU 3680  CB  ALA B 181     4379   3865   3933    -61    114   -315       C  
ATOM   3681  N   HIS B 182      36.167  23.776  13.891  1.00 34.14           N  
ANISOU 3681  N   HIS B 182     4634   4169   4166    -46     70   -268       N  
ATOM   3682  CA  HIS B 182      35.217  22.778  13.502  1.00 35.11           C  
ANISOU 3682  CA  HIS B 182     4753   4297   4289    -41     71   -250       C  
ATOM   3683  C   HIS B 182      33.953  23.078  14.246  1.00 37.97           C  
ANISOU 3683  C   HIS B 182     5118   4642   4664    -42    104   -253       C  
ATOM   3684  O   HIS B 182      34.011  23.506  15.401  1.00 44.37           O  
ANISOU 3684  O   HIS B 182     5949   5445   5462    -47    122   -275       O  
ATOM   3685  CB  HIS B 182      35.756  21.405  13.880  1.00 35.14           C  
ANISOU 3685  CB  HIS B 182     4776   4319   4254    -41     51   -250       C  
ATOM   3686  CG  HIS B 182      34.882  20.271  13.456  1.00 37.49           C  
ANISOU 3686  CG  HIS B 182     5070   4622   4551    -36     49   -231       C  
ATOM   3687  ND1 HIS B 182      34.282  20.220  12.208  1.00 37.68           N  
ANISOU 3687  ND1 HIS B 182     5071   4644   4600    -31     44   -210       N  
ATOM   3688  CD2 HIS B 182      34.484  19.108  14.142  1.00 38.06           C  
ANISOU 3688  CD2 HIS B 182     5159   4699   4600    -37     51   -230       C  
ATOM   3689  CE1 HIS B 182      33.543  19.078  12.116  1.00 37.77           C  
ANISOU 3689  CE1 HIS B 182     5085   4659   4606    -29     41   -198       C  
ATOM   3690  NE2 HIS B 182      33.665  18.401  13.302  1.00 40.74           N  
ANISOU 3690  NE2 HIS B 182     5484   5039   4953    -33     46   -210       N  
ATOM   3691  N   GLY B 183      32.795  22.874  13.620  1.00 37.20           N  
ANISOU 3691  N   GLY B 183     5002   4538   4591    -37    114   -233       N  
ATOM   3692  CA  GLY B 183      31.529  23.097  14.327  1.00 35.40           C  
ANISOU 3692  CA  GLY B 183     4775   4292   4380    -37    149   -233       C  
ATOM   3693  C   GLY B 183      30.863  24.379  13.856  1.00 34.80           C  
ANISOU 3693  C   GLY B 183     4675   4196   4349    -34    171   -226       C  
ATOM   3694  O   GLY B 183      31.134  24.873  12.758  1.00 35.12           O  
ANISOU 3694  O   GLY B 183     4693   4239   4411    -31    157   -214       O  
ATOM   3695  N   ASN B 184      29.980  24.876  14.699  1.00 32.82           N  
ANISOU 3695  N   ASN B 184     4429   3927   4113    -35    207   -233       N  
ATOM   3696  CA  ASN B 184      29.098  25.989  14.492  1.00 37.72           C  
ANISOU 3696  CA  ASN B 184     5028   4524   4779    -32    237   -225       C  
ATOM   3697  C   ASN B 184      29.714  27.220  13.834  1.00 34.83           C  
ANISOU 3697  C   ASN B 184     4645   4151   4437    -31    234   -228       C  
ATOM   3698  O   ASN B 184      29.147  27.822  12.922  1.00 32.60           O  
ANISOU 3698  O   ASN B 184     4333   3860   4194    -26    240   -207       O  
ATOM   3699  CB  ASN B 184      28.786  26.486  15.902  1.00 46.72           C  
ANISOU 3699  CB  ASN B 184     6193   5646   5912    -34    275   -248       C  
ATOM   3700  CG  ASN B 184      27.338  26.550  16.165  1.00 53.34           C  
ANISOU 3700  CG  ASN B 184     7020   6465   6781    -29    311   -234       C  
ATOM   3701  OD1 ASN B 184      26.553  26.036  15.360  1.00 56.50           O  
ANISOU 3701  OD1 ASN B 184     7395   6867   7205    -25    304   -205       O  
ATOM   3702  ND2 ASN B 184      26.949  27.162  17.308  1.00 58.20           N  
ANISOU 3702  ND2 ASN B 184     7655   7060   7397    -30    351   -252       N  
ATOM   3703  N   LYS B 185      30.857  27.633  14.353  1.00 30.84           N  
ANISOU 3703  N   LYS B 185     4159   3649   3908    -37    227   -253       N  
ATOM   3704  CA  LYS B 185      31.446  28.855  13.840  1.00 32.19           C  
ANISOU 3704  CA  LYS B 185     4314   3809   4104    -38    227   -257       C  
ATOM   3705  C   LYS B 185      32.474  28.637  12.746  1.00 30.12           C  
ANISOU 3705  C   LYS B 185     4039   3566   3836    -36    190   -246       C  
ATOM   3706  O   LYS B 185      33.163  29.585  12.349  1.00 29.29           O  
ANISOU 3706  O   LYS B 185     3923   3455   3749    -36    188   -250       O  
ATOM   3707  CB  LYS B 185      31.885  29.754  14.980  1.00 35.09           C  
ANISOU 3707  CB  LYS B 185     4704   4160   4464    -46    248   -291       C  
ATOM   3708  CG  LYS B 185      30.626  30.275  15.722  1.00 37.30           C  
ANISOU 3708  CG  LYS B 185     4989   4416   4768    -44    294   -294       C  
ATOM   3709  CD  LYS B 185      30.971  31.060  16.966  1.00 42.82           C  
ANISOU 3709  CD  LYS B 185     5717   5097   5453    -52    318   -330       C  
ATOM   3710  CE  LYS B 185      29.804  31.115  17.979  1.00 45.36           C  
ANISOU 3710  CE  LYS B 185     6055   5399   5778    -49    362   -337       C  
ATOM   3711  NZ  LYS B 185      28.665  31.934  17.485  1.00 48.41           N  
ANISOU 3711  NZ  LYS B 185     6411   5760   6220    -41    397   -317       N  
ATOM   3712  N   MET B 186      32.511  27.428  12.200  1.00 29.27           N  
ANISOU 3712  N   MET B 186     3932   3480   3708    -33    164   -230       N  
ATOM   3713  CA  MET B 186      33.338  27.167  10.999  1.00 30.73           C  
ANISOU 3713  CA  MET B 186     4103   3682   3891    -28    132   -215       C  
ATOM   3714  C   MET B 186      33.281  28.306   9.961  1.00 29.23           C  
ANISOU 3714  C   MET B 186     3883   3481   3741    -22    138   -199       C  
ATOM   3715  O   MET B 186      32.251  28.878   9.720  1.00 28.45           O  
ANISOU 3715  O   MET B 186     3765   3367   3676    -19    159   -186       O  
ATOM   3716  CB  MET B 186      33.032  25.821  10.359  1.00 29.65           C  
ANISOU 3716  CB  MET B 186     3965   3563   3735    -24    110   -196       C  
ATOM   3717  CG  MET B 186      31.835  25.832   9.432  1.00 29.89           C  
ANISOU 3717  CG  MET B 186     3970   3588   3797    -18    114   -169       C  
ATOM   3718  SD  MET B 186      31.453  24.186   8.748  1.00 37.84           S  
ANISOU 3718  SD  MET B 186     4980   4615   4782    -16     86   -150       S  
ATOM   3719  CE  MET B 186      31.455  23.112  10.185  1.00 35.15           C  
ANISOU 3719  CE  MET B 186     4670   4277   4405    -22     91   -170       C  
ATOM   3720  N   VAL B 187      34.420  28.656   9.384  1.00 30.81           N  
ANISOU 3720  N   VAL B 187     4078   3688   3940    -21    120   -199       N  
ATOM   3721  CA  VAL B 187      34.432  29.693   8.331  1.00 29.77           C  
ANISOU 3721  CA  VAL B 187     3917   3548   3846    -14    125   -181       C  
ATOM   3722  C   VAL B 187      34.445  29.147   6.919  1.00 29.41           C  
ANISOU 3722  C   VAL B 187     3856   3518   3799     -4    102   -152       C  
ATOM   3723  O   VAL B 187      35.449  28.637   6.459  1.00 30.29           O  
ANISOU 3723  O   VAL B 187     3973   3646   3889     -2     78   -150       O  
ATOM   3724  CB  VAL B 187      35.585  30.679   8.568  1.00 29.55           C  
ANISOU 3724  CB  VAL B 187     3889   3510   3826    -18    127   -198       C  
ATOM   3725  CG1 VAL B 187      35.639  31.739   7.501  1.00 28.37           C  
ANISOU 3725  CG1 VAL B 187     3710   3352   3718    -10    134   -178       C  
ATOM   3726  CG2 VAL B 187      35.372  31.348   9.904  1.00 28.64           C  
ANISOU 3726  CG2 VAL B 187     3789   3375   3716    -28    153   -227       C  
ATOM   3727  N   LEU B 188      33.334  29.277   6.213  1.00 30.99           N  
ANISOU 3727  N   LEU B 188     4035   3714   4024      1    109   -128       N  
ATOM   3728  CA  LEU B 188      33.244  28.855   4.793  1.00 30.37           C  
ANISOU 3728  CA  LEU B 188     3941   3650   3945     10     87    -99       C  
ATOM   3729  C   LEU B 188      33.760  29.940   3.844  1.00 29.97           C  
ANISOU 3729  C   LEU B 188     3869   3595   3921     18     89    -84       C  
ATOM   3730  O   LEU B 188      33.215  31.057   3.764  1.00 30.11           O  
ANISOU 3730  O   LEU B 188     3866   3595   3978     20    112    -75       O  
ATOM   3731  CB  LEU B 188      31.812  28.425   4.435  1.00 35.30           C  
ANISOU 3731  CB  LEU B 188     4555   4274   4583     11     88    -79       C  
ATOM   3732  CG  LEU B 188      31.196  27.409   5.435  1.00 40.06           C  
ANISOU 3732  CG  LEU B 188     5177   4878   5166      4     90    -92       C  
ATOM   3733  CD1 LEU B 188      30.550  28.166   6.579  1.00 43.37           C  
ANISOU 3733  CD1 LEU B 188     5595   5274   5607      0    126   -106       C  
ATOM   3734  CD2 LEU B 188      30.210  26.424   4.802  1.00 40.60           C  
ANISOU 3734  CD2 LEU B 188     5239   4956   5232      5     74    -71       C  
ATOM   3735  N   LEU B 189      34.858  29.660   3.164  1.00 27.31           N  
ANISOU 3735  N   LEU B 189     3536   3273   3565     23     68    -79       N  
ATOM   3736  CA  LEU B 189      35.468  30.701   2.385  1.00 27.32           C  
ANISOU 3736  CA  LEU B 189     3519   3268   3591     31     73    -66       C  
ATOM   3737  C   LEU B 189      35.019  30.614   0.963  1.00 26.81           C  
ANISOU 3737  C   LEU B 189     3438   3214   3533     43     62    -33       C  
ATOM   3738  O   LEU B 189      35.651  29.964   0.218  1.00 26.77           O  
ANISOU 3738  O   LEU B 189     3440   3225   3502     49     41    -24       O  
ATOM   3739  CB  LEU B 189      36.974  30.569   2.418  1.00 25.66           C  
ANISOU 3739  CB  LEU B 189     3320   3066   3362     31     61    -78       C  
ATOM   3740  CG  LEU B 189      37.581  30.953   3.775  1.00 25.59           C  
ANISOU 3740  CG  LEU B 189     3324   3045   3352     19     71   -110       C  
ATOM   3741  CD1 LEU B 189      39.076  30.752   3.581  1.00 25.83           C  
ANISOU 3741  CD1 LEU B 189     3361   3085   3367     20     54   -114       C  
ATOM   3742  CD2 LEU B 189      37.313  32.421   4.168  1.00 25.84           C  
ANISOU 3742  CD2 LEU B 189     3339   3051   3427     16    100   -117       C  
ATOM   3743  N   LYS B 190      33.988  31.336   0.572  1.00 27.91           N  
ANISOU 3743  N   LYS B 190     3554   3342   3706     46     76    -13       N  
ATOM   3744  CA  LYS B 190      33.476  31.305  -0.832  1.00 29.65           C  
ANISOU 3744  CA  LYS B 190     3758   3574   3932     58     62     20       C  
ATOM   3745  C   LYS B 190      34.504  31.703  -1.911  1.00 31.17           C  
ANISOU 3745  C   LYS B 190     3945   3775   4123     70     54     37       C  
ATOM   3746  O   LYS B 190      34.488  31.202  -3.047  1.00 30.22           O  
ANISOU 3746  O   LYS B 190     3825   3671   3984     79     34     59       O  
ATOM   3747  CB  LYS B 190      32.293  32.233  -0.919  1.00 30.84           C  
ANISOU 3747  CB  LYS B 190     3881   3708   4127     59     82     39       C  
ATOM   3748  CG  LYS B 190      31.656  32.364  -2.296  1.00 37.05           C  
ANISOU 3748  CG  LYS B 190     4647   4503   4924     70     69     77       C  
ATOM   3749  CD  LYS B 190      30.463  33.322  -2.223  1.00 38.38           C  
ANISOU 3749  CD  LYS B 190     4786   4652   5142     71     92     95       C  
ATOM   3750  CE  LYS B 190      29.955  33.591  -3.644  1.00 42.59           C  
ANISOU 3750  CE  LYS B 190     5298   5196   5689     83     77    136       C  
ATOM   3751  NZ  LYS B 190      28.507  33.957  -3.667  1.00 45.13           N  
ANISOU 3751  NZ  LYS B 190     5592   5505   6047     82     87    158       N  
ATOM   3752  N   ARG B 191      35.422  32.592  -1.553  1.00 30.40           N  
ANISOU 3752  N   ARG B 191     3841   3664   4042     70     71     26       N  
ATOM   3753  CA  ARG B 191      36.379  33.087  -2.520  1.00 32.52           C  
ANISOU 3753  CA  ARG B 191     4102   3938   4317     82     68     44       C  
ATOM   3754  C   ARG B 191      37.427  32.016  -2.852  1.00 33.62           C  
ANISOU 3754  C   ARG B 191     4264   4096   4412     86     46     39       C  
ATOM   3755  O   ARG B 191      38.187  32.168  -3.789  1.00 32.64           O  
ANISOU 3755  O   ARG B 191     4136   3979   4285     98     41     56       O  
ATOM   3756  CB  ARG B 191      37.025  34.370  -1.956  1.00 34.29           C  
ANISOU 3756  CB  ARG B 191     4311   4139   4577     80     93     33       C  
ATOM   3757  CG  ARG B 191      37.322  35.455  -2.969  1.00 34.80           C  
ANISOU 3757  CG  ARG B 191     4350   4196   4674     94    105     61       C  
ATOM   3758  CD  ARG B 191      37.551  36.798  -2.322  1.00 33.44           C  
ANISOU 3758  CD  ARG B 191     4160   3996   4548     89    133     50       C  
ATOM   3759  NE  ARG B 191      38.211  36.623  -1.029  1.00 31.87           N  
ANISOU 3759  NE  ARG B 191     3980   3790   4339     74    134     12       N  
ATOM   3760  CZ  ARG B 191      39.533  36.657  -0.791  1.00 31.59           C  
ANISOU 3760  CZ  ARG B 191     3951   3753   4296     71    128     -2       C  
ATOM   3761  NH1 ARG B 191      40.436  36.887  -1.757  1.00 30.17           N  
ANISOU 3761  NH1 ARG B 191     3761   3579   4123     83    124     19       N  
ATOM   3762  NH2 ARG B 191      39.951  36.452   0.462  1.00 28.33           N  
ANISOU 3762  NH2 ARG B 191     3557   3335   3872     55    126    -37       N  
ATOM   3763  N   TYR B 192      37.450  30.916  -2.099  1.00 32.44           N  
ANISOU 3763  N   TYR B 192     4138   3955   4230     76     33     16       N  
ATOM   3764  CA  TYR B 192      38.551  29.969  -2.188  1.00 33.43           C  
ANISOU 3764  CA  TYR B 192     4285   4095   4320     78     16      8       C  
ATOM   3765  C   TYR B 192      38.036  28.656  -2.781  1.00 33.94           C  
ANISOU 3765  C   TYR B 192     4368   4179   4349     80     -6     16       C  
ATOM   3766  O   TYR B 192      38.603  27.610  -2.563  1.00 38.13           O  
ANISOU 3766  O   TYR B 192     4919   4720   4846     78    -20      4       O  
ATOM   3767  CB  TYR B 192      39.180  29.740  -0.777  1.00 33.33           C  
ANISOU 3767  CB  TYR B 192     4287   4077   4298     64     18    -24       C  
ATOM   3768  CG  TYR B 192      40.186  30.815  -0.364  1.00 34.20           C  
ANISOU 3768  CG  TYR B 192     4386   4172   4435     62     32    -34       C  
ATOM   3769  CD1 TYR B 192      39.768  32.019   0.184  1.00 34.22           C  
ANISOU 3769  CD1 TYR B 192     4372   4153   4475     56     54    -41       C  
ATOM   3770  CD2 TYR B 192      41.557  30.640  -0.602  1.00 34.76           C  
ANISOU 3770  CD2 TYR B 192     4461   4249   4496     67     23    -33       C  
ATOM   3771  CE1 TYR B 192      40.670  33.027   0.514  1.00 35.00           C  
ANISOU 3771  CE1 TYR B 192     4459   4236   4601     54     65    -49       C  
ATOM   3772  CE2 TYR B 192      42.481  31.623  -0.249  1.00 35.40           C  
ANISOU 3772  CE2 TYR B 192     4529   4315   4605     64     34    -40       C  
ATOM   3773  CZ  TYR B 192      42.031  32.814   0.313  1.00 36.21           C  
ANISOU 3773  CZ  TYR B 192     4616   4396   4744     57     54    -50       C  
ATOM   3774  OH  TYR B 192      42.949  33.800   0.630  1.00 36.78           O  
ANISOU 3774  OH  TYR B 192     4675   4452   4846     53     63    -58       O  
ATOM   3775  N   ILE B 193      36.908  28.705  -3.476  1.00 30.71           N  
ANISOU 3775  N   ILE B 193     3947   3772   3946     84    -10     35       N  
ATOM   3776  CA  ILE B 193      36.318  27.489  -3.981  1.00 27.07           C  
ANISOU 3776  CA  ILE B 193     3503   3327   3454     83    -33     41       C  
ATOM   3777  C   ILE B 193      36.701  27.463  -5.441  1.00 26.02           C  
ANISOU 3777  C   ILE B 193     3371   3207   3308     99    -44     66       C  
ATOM   3778  O   ILE B 193      36.725  28.537  -6.058  1.00 25.74           O  
ANISOU 3778  O   ILE B 193     3314   3165   3298    108    -32     86       O  
ATOM   3779  CB  ILE B 193      34.777  27.504  -3.861  1.00 26.52           C  
ANISOU 3779  CB  ILE B 193     3421   3253   3402     76    -34     48       C  
ATOM   3780  CG1 ILE B 193      34.376  27.537  -2.397  1.00 26.10           C  
ANISOU 3780  CG1 ILE B 193     3369   3186   3361     63    -18     24       C  
ATOM   3781  CG2 ILE B 193      34.203  26.300  -4.610  1.00 25.57           C  
ANISOU 3781  CG2 ILE B 193     3315   3147   3250     77    -61     57       C  
ATOM   3782  CD1 ILE B 193      32.853  27.593  -2.173  1.00 27.37           C  
ANISOU 3782  CD1 ILE B 193     3515   3338   3544     56    -14     32       C  
ATOM   3783  N   THR B 194      37.036  26.265  -5.943  1.00 24.63           N  
ANISOU 3783  N   THR B 194     3219   3046   3092    102    -64     64       N  
ATOM   3784  CA  THR B 194      37.402  26.030  -7.303  1.00 25.26           C  
ANISOU 3784  CA  THR B 194     3307   3139   3150    116    -75     85       C  
ATOM   3785  C   THR B 194      36.894  24.645  -7.713  1.00 25.36           C  
ANISOU 3785  C   THR B 194     3344   3165   3125    113   -101     81       C  
ATOM   3786  O   THR B 194      36.732  23.776  -6.868  1.00 24.02           O  
ANISOU 3786  O   THR B 194     3187   2994   2942    101   -107     60       O  
ATOM   3787  CB  THR B 194      38.957  25.960  -7.503  1.00 26.98           C  
ANISOU 3787  CB  THR B 194     3537   3360   3354    127    -68     82       C  
ATOM   3788  OG1 THR B 194      39.490  24.888  -6.745  1.00 26.73           O  
ANISOU 3788  OG1 THR B 194     3527   3331   3298    119    -75     59       O  
ATOM   3789  CG2 THR B 194      39.756  27.354  -7.245  1.00 23.43           C  
ANISOU 3789  CG2 THR B 194     3063   2895   2942    132    -44     87       C  
ATOM   3790  N   VAL B 195      36.599  24.496  -9.015  1.00 24.54           N  
ANISOU 3790  N   VAL B 195     3246   3073   3005    122   -115    103       N  
ATOM   3791  CA  VAL B 195      36.122  23.291  -9.607  1.00 25.43           C  
ANISOU 3791  CA  VAL B 195     3382   3197   3082    120   -141    102       C  
ATOM   3792  C   VAL B 195      37.052  23.021 -10.783  1.00 26.87           C  
ANISOU 3792  C   VAL B 195     3585   3390   3233    137   -145    113       C  
ATOM   3793  O   VAL B 195      37.220  23.920 -11.593  1.00 27.83           O  
ANISOU 3793  O   VAL B 195     3695   3514   3365    150   -137    136       O  
ATOM   3794  CB  VAL B 195      34.741  23.441 -10.319  1.00 24.18           C  
ANISOU 3794  CB  VAL B 195     3212   3043   2931    116   -160    121       C  
ATOM   3795  CG1 VAL B 195      34.122  22.065 -10.365  1.00 23.74           C  
ANISOU 3795  CG1 VAL B 195     3178   2993   2847    106   -186    109       C  
ATOM   3796  CG2 VAL B 195      33.809  24.369  -9.581  1.00 24.06           C  
ANISOU 3796  CG2 VAL B 195     3165   3015   2962    108   -147    126       C  
ATOM   3797  N   GLY B 196      37.596  21.796 -10.900  1.00 26.04           N  
ANISOU 3797  N   GLY B 196     3510   3292   3091    138   -155     99       N  
ATOM   3798  CA  GLY B 196      38.800  21.578 -11.718  1.00 25.97           C  
ANISOU 3798  CA  GLY B 196     3521   3289   3055    155   -148    106       C  
ATOM   3799  C   GLY B 196      39.839  22.731 -11.695  1.00 27.86           C  
ANISOU 3799  C   GLY B 196     3742   3522   3320    168   -121    118       C  
ATOM   3800  O   GLY B 196      40.349  23.089 -12.754  1.00 25.41           O  
ANISOU 3800  O   GLY B 196     3436   3217   3000    185   -115    138       O  
ATOM   3801  N   GLY B 197      40.249  23.238 -10.509  1.00 26.96           N  
ANISOU 3801  N   GLY B 197     3610   3397   3236    160   -106    104       N  
ATOM   3802  CA  GLY B 197      41.282  24.304 -10.462  1.00 26.78           C  
ANISOU 3802  CA  GLY B 197     3569   3366   3240    170    -82    114       C  
ATOM   3803  C   GLY B 197      40.717  25.706 -10.825  1.00 29.97           C  
ANISOU 3803  C   GLY B 197     3943   3763   3679    174    -72    136       C  
ATOM   3804  O   GLY B 197      41.419  26.712 -10.701  1.00 29.44           O  
ANISOU 3804  O   GLY B 197     3856   3686   3641    181    -52    144       O  
ATOM   3805  N   ILE B 198      39.450  25.767 -11.293  1.00 30.79           N  
ANISOU 3805  N   ILE B 198     4043   3873   3783    171    -86    147       N  
ATOM   3806  CA  ILE B 198      38.809  26.992 -11.863  1.00 30.00           C  
ANISOU 3806  CA  ILE B 198     3916   3770   3713    177    -79    173       C  
ATOM   3807  C   ILE B 198      37.903  27.720 -10.848  1.00 29.77           C  
ANISOU 3807  C   ILE B 198     3859   3727   3724    162    -71    166       C  
ATOM   3808  O   ILE B 198      37.005  27.078 -10.311  1.00 28.06           O  
ANISOU 3808  O   ILE B 198     3647   3510   3502    148    -85    152       O  
ATOM   3809  CB  ILE B 198      37.928  26.616 -13.111  1.00 30.01           C  
ANISOU 3809  CB  ILE B 198     3928   3786   3687    183   -102    194       C  
ATOM   3810  CG1 ILE B 198      38.705  25.798 -14.126  1.00 29.60           C  
ANISOU 3810  CG1 ILE B 198     3908   3747   3588    197   -109    199       C  
ATOM   3811  CG2 ILE B 198      37.367  27.844 -13.828  1.00 30.08           C  
ANISOU 3811  CG2 ILE B 198     3910   3794   3724    192    -95    226       C  
ATOM   3812  CD1 ILE B 198      37.849  25.167 -15.181  1.00 30.39           C  
ANISOU 3812  CD1 ILE B 198     4028   3863   3655    198   -137    211       C  
ATOM   3813  N   PRO B 199      38.060  29.065 -10.645  1.00 29.01           N  
ANISOU 3813  N   PRO B 199     3734   3616   3671    166    -48    176       N  
ATOM   3814  CA  PRO B 199      37.262  29.665  -9.584  1.00 28.06           C  
ANISOU 3814  CA  PRO B 199     3592   3481   3588    151    -38    165       C  
ATOM   3815  C   PRO B 199      35.784  29.462  -9.833  1.00 28.14           C  
ANISOU 3815  C   PRO B 199     3595   3495   3600    145    -54    176       C  
ATOM   3816  O   PRO B 199      35.328  29.515 -10.969  1.00 26.28           O  
ANISOU 3816  O   PRO B 199     3358   3270   3355    154    -67    202       O  
ATOM   3817  CB  PRO B 199      37.642  31.181  -9.651  1.00 29.70           C  
ANISOU 3817  CB  PRO B 199     3770   3672   3840    159    -11    181       C  
ATOM   3818  CG  PRO B 199      38.935  31.222 -10.432  1.00 29.08           C  
ANISOU 3818  CG  PRO B 199     3700   3600   3746    176     -6    192       C  
ATOM   3819  CD  PRO B 199      38.796  30.097 -11.418  1.00 29.68           C  
ANISOU 3819  CD  PRO B 199     3804   3698   3774    183    -30    201       C  
ATOM   3820  N   LEU B 200      35.045  29.234  -8.753  1.00 30.11           N  
ANISOU 3820  N   LEU B 200     3842   3736   3863    129    -53    156       N  
ATOM   3821  CA  LEU B 200      33.598  28.940  -8.800  1.00 31.11           C  
ANISOU 3821  CA  LEU B 200     3959   3863   3995    120    -67    165       C  
ATOM   3822  C   LEU B 200      32.874  30.042  -9.515  1.00 32.52           C  
ANISOU 3822  C   LEU B 200     4108   4038   4208    128    -61    198       C  
ATOM   3823  O   LEU B 200      31.923  29.774 -10.266  1.00 30.40           O  
ANISOU 3823  O   LEU B 200     3836   3779   3935    128    -82    218       O  
ATOM   3824  CB  LEU B 200      33.022  28.927  -7.387  1.00 33.49           C  
ANISOU 3824  CB  LEU B 200     4254   4149   4319    105    -54    141       C  
ATOM   3825  CG  LEU B 200      32.129  27.803  -6.863  1.00 34.77           C  
ANISOU 3825  CG  LEU B 200     4429   4315   4467     91    -71    128       C  
ATOM   3826  CD1 LEU B 200      31.305  28.419  -5.777  1.00 31.99           C  
ANISOU 3826  CD1 LEU B 200     4057   3944   4154     81    -49    121       C  
ATOM   3827  CD2 LEU B 200      31.275  26.982  -7.843  1.00 32.53           C  
ANISOU 3827  CD2 LEU B 200     4151   4046   4162     90   -103    145       C  
ATOM   3828  N   GLN B 201      33.345  31.287  -9.278  1.00 33.08           N  
ANISOU 3828  N   GLN B 201     4158   4094   4315    134    -33    203       N  
ATOM   3829  CA  GLN B 201      32.696  32.488  -9.814  1.00 32.80           C  
ANISOU 3829  CA  GLN B 201     4090   4049   4320    142    -20    235       C  
ATOM   3830  C   GLN B 201      32.461  32.335 -11.309  1.00 31.91           C  
ANISOU 3830  C   GLN B 201     3980   3956   4186    155    -43    268       C  
ATOM   3831  O   GLN B 201      31.439  32.772 -11.846  1.00 31.94           O  
ANISOU 3831  O   GLN B 201     3963   3962   4211    157    -50    296       O  
ATOM   3832  CB  GLN B 201      33.492  33.759  -9.476  1.00 34.62           C  
ANISOU 3832  CB  GLN B 201     4303   4262   4588    149     12    234       C  
ATOM   3833  CG  GLN B 201      32.750  35.071  -9.759  1.00 35.58           C  
ANISOU 3833  CG  GLN B 201     4388   4369   4760    155     31    264       C  
ATOM   3834  CD  GLN B 201      31.391  35.162  -9.050  1.00 38.53           C  
ANISOU 3834  CD  GLN B 201     4744   4730   5162    143     35    262       C  
ATOM   3835  OE1 GLN B 201      31.272  34.971  -7.819  1.00 38.84           O  
ANISOU 3835  OE1 GLN B 201     4790   4756   5209    129     47    231       O  
ATOM   3836  NE2 GLN B 201      30.359  35.434  -9.821  1.00 36.15           N  
ANISOU 3836  NE2 GLN B 201     4423   4433   4878    148     26    296       N  
ATOM   3837  N   GLU B 202      33.362  31.645 -11.987  1.00 31.88           N  
ANISOU 3837  N   GLU B 202     4003   3969   4138    163    -57    266       N  
ATOM   3838  CA  GLU B 202      33.186  31.446 -13.430  1.00 31.51           C  
ANISOU 3838  CA  GLU B 202     3964   3942   4064    176    -79    296       C  
ATOM   3839  C   GLU B 202      31.934  30.624 -13.735  1.00 32.70           C  
ANISOU 3839  C   GLU B 202     4120   4104   4198    166   -112    301       C  
ATOM   3840  O   GLU B 202      31.270  30.809 -14.801  1.00 33.61           O  
ANISOU 3840  O   GLU B 202     4229   4231   4309    173   -131    332       O  
ATOM   3841  CB  GLU B 202      34.402  30.771 -14.027  1.00 32.70           C  
ANISOU 3841  CB  GLU B 202     4148   4107   4170    187    -84    289       C  
ATOM   3842  CG  GLU B 202      35.670  31.618 -13.985  1.00 33.60           C  
ANISOU 3842  CG  GLU B 202     4253   4210   4300    200    -54    292       C  
ATOM   3843  CD  GLU B 202      36.678  31.353 -15.122  1.00 37.63           C  
ANISOU 3843  CD  GLU B 202     4786   4735   4774    219    -56    307       C  
ATOM   3844  OE1 GLU B 202      36.347  30.815 -16.221  1.00 38.14           O  
ANISOU 3844  OE1 GLU B 202     4870   4818   4802    227    -78    324       O  
ATOM   3845  OE2 GLU B 202      37.852  31.743 -14.946  1.00 42.85           O  
ANISOU 3845  OE2 GLU B 202     5447   5388   5446    227    -33    303       O  
ATOM   3846  N   PHE B 203      31.634  29.682 -12.836  1.00 30.58           N  
ANISOU 3846  N   PHE B 203     3866   3833   3919    150   -121    271       N  
ATOM   3847  CA  PHE B 203      30.446  28.835 -13.005  1.00 33.46           C  
ANISOU 3847  CA  PHE B 203     4234   4206   4272    137   -152    274       C  
ATOM   3848  C   PHE B 203      29.161  29.588 -12.573  1.00 33.37           C  
ANISOU 3848  C   PHE B 203     4185   4181   4313    130   -145    290       C  
ATOM   3849  O   PHE B 203      28.099  29.381 -13.131  1.00 32.59           O  
ANISOU 3849  O   PHE B 203     4076   4088   4216    126   -170    310       O  
ATOM   3850  CB  PHE B 203      30.586  27.459 -12.300  1.00 31.51           C  
ANISOU 3850  CB  PHE B 203     4015   3960   3994    124   -165    239       C  
ATOM   3851  CG  PHE B 203      31.696  26.585 -12.868  1.00 31.85           C  
ANISOU 3851  CG  PHE B 203     4096   4018   3985    132   -176    226       C  
ATOM   3852  CD1 PHE B 203      33.029  26.840 -12.553  1.00 32.27           C  
ANISOU 3852  CD1 PHE B 203     4158   4067   4033    140   -152    214       C  
ATOM   3853  CD2 PHE B 203      31.408  25.522 -13.726  1.00 32.97           C  
ANISOU 3853  CD2 PHE B 203     4265   4177   4086    130   -209    228       C  
ATOM   3854  CE1 PHE B 203      34.063  26.057 -13.047  1.00 31.90           C  
ANISOU 3854  CE1 PHE B 203     4144   4031   3944    149   -158    204       C  
ATOM   3855  CE2 PHE B 203      32.431  24.732 -14.234  1.00 32.31           C  
ANISOU 3855  CE2 PHE B 203     4216   4103   3956    138   -215    216       C  
ATOM   3856  CZ  PHE B 203      33.756  24.994 -13.890  1.00 32.53           C  
ANISOU 3856  CZ  PHE B 203     4251   4126   3981    148   -188    205       C  
ATOM   3857  N   ILE B 204      29.297  30.474 -11.603  1.00 35.02           N  
ANISOU 3857  N   ILE B 204     4373   4369   4563    129   -111    282       N  
ATOM   3858  CA  ILE B 204      28.178  31.376 -11.247  1.00 37.17           C  
ANISOU 3858  CA  ILE B 204     4608   4625   4889    125    -96    301       C  
ATOM   3859  C   ILE B 204      27.826  32.325 -12.362  1.00 36.69           C  
ANISOU 3859  C   ILE B 204     4523   4569   4849    138    -99    343       C  
ATOM   3860  O   ILE B 204      26.668  32.557 -12.601  1.00 36.69           O  
ANISOU 3860  O   ILE B 204     4498   4566   4874    135   -109    368       O  
ATOM   3861  CB  ILE B 204      28.426  32.151  -9.957  1.00 34.51           C  
ANISOU 3861  CB  ILE B 204     4258   4263   4591    121    -56    281       C  
ATOM   3862  CG1 ILE B 204      28.569  31.140  -8.816  1.00 34.21           C  
ANISOU 3862  CG1 ILE B 204     4243   4222   4532    106    -57    242       C  
ATOM   3863  CG2 ILE B 204      27.236  33.061  -9.691  1.00 34.36           C  
ANISOU 3863  CG2 ILE B 204     4201   4227   4628    119    -39    303       C  
ATOM   3864  CD1 ILE B 204      29.315  31.660  -7.607  1.00 30.77           C  
ANISOU 3864  CD1 ILE B 204     3809   3768   4112    103    -23    213       C  
ATOM   3865  N   ASN B 205      28.845  32.863 -13.029  1.00 40.33           N  
ANISOU 3865  N   ASN B 205     4989   5036   5298    154    -89    353       N  
ATOM   3866  CA  ASN B 205      28.663  33.803 -14.136  1.00 42.45           C  
ANISOU 3866  CA  ASN B 205     5236   5309   5582    170    -89    395       C  
ATOM   3867  C   ASN B 205      28.052  33.099 -15.338  1.00 41.44           C  
ANISOU 3867  C   ASN B 205     5120   5206   5419    172   -131    419       C  
ATOM   3868  O   ASN B 205      27.332  33.703 -16.084  1.00 43.67           O  
ANISOU 3868  O   ASN B 205     5379   5492   5720    178   -140    456       O  
ATOM   3869  CB  ASN B 205      29.995  34.407 -14.599  1.00 44.29           C  
ANISOU 3869  CB  ASN B 205     5476   5543   5806    187    -69    400       C  
ATOM   3870  CG  ASN B 205      30.717  35.208 -13.522  1.00 45.98           C  
ANISOU 3870  CG  ASN B 205     5678   5732   6057    185    -28    378       C  
ATOM   3871  OD1 ASN B 205      30.149  35.587 -12.480  1.00 44.23           O  
ANISOU 3871  OD1 ASN B 205     5439   5491   5874    174    -10    365       O  
ATOM   3872  ND2 ASN B 205      32.001  35.467 -13.774  1.00 43.71           N  
ANISOU 3872  ND2 ASN B 205     5403   5447   5758    197    -14    375       N  
ATOM   3873  N   ASN B 206      28.380  31.826 -15.531  1.00 42.55           N  
ANISOU 3873  N   ASN B 206     5298   5362   5506    166   -158    397       N  
ATOM   3874  CA  ASN B 206      27.766  31.018 -16.575  1.00 41.61           C  
ANISOU 3874  CA  ASN B 206     5195   5265   5349    164   -202    412       C  
ATOM   3875  C   ASN B 206      26.370  30.511 -16.237  1.00 42.57           C  
ANISOU 3875  C   ASN B 206     5301   5384   5488    146   -226    414       C  
ATOM   3876  O   ASN B 206      25.729  29.882 -17.096  1.00 39.37           O  
ANISOU 3876  O   ASN B 206     4905   4996   5057    142   -266    428       O  
ATOM   3877  CB  ASN B 206      28.639  29.819 -16.871  1.00 42.72           C  
ANISOU 3877  CB  ASN B 206     5382   5421   5429    164   -219    385       C  
ATOM   3878  CG  ASN B 206      29.798  30.167 -17.730  1.00 46.51           C  
ANISOU 3878  CG  ASN B 206     5879   5910   5881    185   -207    396       C  
ATOM   3879  OD1 ASN B 206      29.624  30.667 -18.824  1.00 49.80           O  
ANISOU 3879  OD1 ASN B 206     6290   6338   6291    198   -217    430       O  
ATOM   3880  ND2 ASN B 206      30.998  29.912 -17.243  1.00 47.64           N  
ANISOU 3880  ND2 ASN B 206     6042   6048   6009    188   -186    370       N  
ATOM   3881  N   LYS B 207      25.929  30.784 -14.996  1.00 42.66           N  
ANISOU 3881  N   LYS B 207     5290   5373   5543    135   -202    399       N  
ATOM   3882  CA  LYS B 207      24.673  30.271 -14.394  1.00 43.94           C  
ANISOU 3882  CA  LYS B 207     5437   5528   5730    117   -216    396       C  
ATOM   3883  C   LYS B 207      24.561  28.751 -14.409  1.00 43.18           C  
ANISOU 3883  C   LYS B 207     5373   5443   5588    104   -251    372       C  
ATOM   3884  O   LYS B 207      23.501  28.193 -14.730  1.00 42.45           O  
ANISOU 3884  O   LYS B 207     5274   5356   5498     92   -284    383       O  
ATOM   3885  CB  LYS B 207      23.416  30.871 -15.018  1.00 46.42           C  
ANISOU 3885  CB  LYS B 207     5714   5842   6080    117   -233    439       C  
ATOM   3886  CG  LYS B 207      23.225  32.345 -14.732  1.00 50.23           C  
ANISOU 3886  CG  LYS B 207     6157   6306   6620    127   -194    463       C  
ATOM   3887  CD  LYS B 207      23.975  33.126 -15.789  1.00 55.43           C  
ANISOU 3887  CD  LYS B 207     6817   6976   7266    147   -191    488       C  
ATOM   3888  CE  LYS B 207      23.486  32.773 -17.198  1.00 61.07           C  
ANISOU 3888  CE  LYS B 207     7538   7717   7949    151   -237    520       C  
ATOM   3889  NZ  LYS B 207      22.220  33.479 -17.565  1.00 59.67           N  
ANISOU 3889  NZ  LYS B 207     7316   7535   7818    151   -247    564       N  
ATOM   3890  N   LEU B 208      25.643  28.088 -14.035  1.00 37.70           N  
ANISOU 3890  N   LEU B 208     4714   4752   4858    104   -243    338       N  
ATOM   3891  CA  LEU B 208      25.602  26.640 -13.878  1.00 37.50           C  
ANISOU 3891  CA  LEU B 208     4719   4733   4794     91   -269    311       C  
ATOM   3892  C   LEU B 208      25.223  26.436 -12.449  1.00 33.66           C  
ANISOU 3892  C   LEU B 208     4222   4228   4337     78   -248    288       C  
ATOM   3893  O   LEU B 208      24.874  25.351 -12.054  1.00 33.03           O  
ANISOU 3893  O   LEU B 208     4157   4148   4244     64   -264    269       O  
ATOM   3894  CB  LEU B 208      26.980  25.999 -14.184  1.00 35.63           C  
ANISOU 3894  CB  LEU B 208     4524   4508   4503     99   -269    288       C  
ATOM   3895  CG  LEU B 208      27.494  26.378 -15.581  1.00 34.53           C  
ANISOU 3895  CG  LEU B 208     4396   4387   4335    117   -280    313       C  
ATOM   3896  CD1 LEU B 208      28.814  25.748 -15.941  1.00 31.93           C  
ANISOU 3896  CD1 LEU B 208     4108   4068   3956    126   -278    293       C  
ATOM   3897  CD2 LEU B 208      26.412  26.058 -16.616  1.00 34.49           C  
ANISOU 3897  CD2 LEU B 208     4389   4396   4319    111   -323    337       C  
ATOM   3898  N   ILE B 209      25.286  27.508 -11.685  1.00 33.18           N  
ANISOU 3898  N   ILE B 209     4136   4150   4319     82   -210    291       N  
ATOM   3899  CA  ILE B 209      24.919  27.481 -10.257  1.00 33.87           C  
ANISOU 3899  CA  ILE B 209     4213   4217   4438     71   -184    270       C  
ATOM   3900  C   ILE B 209      24.748  28.946  -9.794  1.00 34.49           C  
ANISOU 3900  C   ILE B 209     4257   4276   4568     78   -145    285       C  
ATOM   3901  O   ILE B 209      25.440  29.841 -10.281  1.00 34.62           O  
ANISOU 3901  O   ILE B 209     4269   4294   4589     92   -132    296       O  
ATOM   3902  CB  ILE B 209      25.915  26.674  -9.384  1.00 31.90           C  
ANISOU 3902  CB  ILE B 209     3997   3967   4156     67   -173    230       C  
ATOM   3903  CG1 ILE B 209      25.584  26.867  -7.878  1.00 33.74           C  
ANISOU 3903  CG1 ILE B 209     4219   4178   4422     58   -141    210       C  
ATOM   3904  CG2 ILE B 209      27.338  27.072  -9.758  1.00 31.77           C  
ANISOU 3904  CG2 ILE B 209     3998   3958   4115     81   -161    223       C  
ATOM   3905  CD1 ILE B 209      26.261  25.964  -6.870  1.00 32.56           C  
ANISOU 3905  CD1 ILE B 209     4098   4027   4245     50   -133    173       C  
ATOM   3906  N   SER B 210      23.804  29.187  -8.882  1.00 35.01           N  
ANISOU 3906  N   SER B 210     4301   4324   4678     69   -127    285       N  
ATOM   3907  CA  SER B 210      23.445  30.559  -8.512  1.00 36.92           C  
ANISOU 3907  CA  SER B 210     4507   4544   4973     76    -91    302       C  
ATOM   3908  C   SER B 210      23.993  30.877  -7.123  1.00 37.79           C  
ANISOU 3908  C   SER B 210     4626   4636   5096     73    -50    269       C  
ATOM   3909  O   SER B 210      24.395  29.976  -6.382  1.00 37.38           O  
ANISOU 3909  O   SER B 210     4601   4585   5015     64    -52    237       O  
ATOM   3910  CB  SER B 210      21.933  30.686  -8.510  1.00 36.81           C  
ANISOU 3910  CB  SER B 210     4460   4521   5004     69    -96    329       C  
ATOM   3911  OG  SER B 210      21.438  30.240  -7.265  1.00 39.57           O  
ANISOU 3911  OG  SER B 210     4811   4854   5369     58    -78    308       O  
ATOM   3912  N   ASP B 211      24.013  32.160  -6.774  1.00 38.68           N  
ANISOU 3912  N   ASP B 211     4715   4728   5250     80    -14    277       N  
ATOM   3913  CA  ASP B 211      24.499  32.602  -5.464  1.00 38.12           C  
ANISOU 3913  CA  ASP B 211     4652   4637   5193     76     24    245       C  
ATOM   3914  C   ASP B 211      23.662  32.107  -4.280  1.00 36.88           C  
ANISOU 3914  C   ASP B 211     4495   4465   5050     64     38    229       C  
ATOM   3915  O   ASP B 211      24.194  31.860  -3.178  1.00 36.36           O  
ANISOU 3915  O   ASP B 211     4453   4392   4971     58     57    194       O  
ATOM   3916  CB  ASP B 211      24.532  34.145  -5.438  1.00 45.95           C  
ANISOU 3916  CB  ASP B 211     5616   5609   6233     86     59    261       C  
ATOM   3917  CG  ASP B 211      25.876  34.706  -5.877  1.00 51.45           C  
ANISOU 3917  CG  ASP B 211     6322   6311   6913     96     64    255       C  
ATOM   3918  OD1 ASP B 211      26.884  33.970  -5.702  1.00 55.20           O  
ANISOU 3918  OD1 ASP B 211     6830   6799   7344     93     52    228       O  
ATOM   3919  OD2 ASP B 211      25.948  35.867  -6.358  1.00 53.01           O  
ANISOU 3919  OD2 ASP B 211     6496   6499   7145    106     81    278       O  
ATOM   3920  N   ALA B 212      22.351  31.959  -4.496  1.00 34.38           N  
ANISOU 3920  N   ALA B 212     4155   4145   4763     61     30    255       N  
ATOM   3921  CA  ALA B 212      21.466  31.503  -3.443  1.00 34.45           C  
ANISOU 3921  CA  ALA B 212     4161   4138   4790     51     45    244       C  
ATOM   3922  C   ALA B 212      21.531  29.957  -3.337  1.00 34.04           C  
ANISOU 3922  C   ALA B 212     4137   4103   4692     40     13    226       C  
ATOM   3923  O   ALA B 212      21.468  29.408  -2.226  1.00 35.29           O  
ANISOU 3923  O   ALA B 212     4311   4252   4844     33     29    200       O  
ATOM   3924  CB  ALA B 212      20.049  31.990  -3.671  1.00 33.60           C  
ANISOU 3924  CB  ALA B 212     4012   4016   4737     51     52    281       C  
ATOM   3925  N   GLU B 213      21.661  29.264  -4.464  1.00 33.25           N  
ANISOU 3925  N   GLU B 213     4045   4027   4562     40    -29    238       N  
ATOM   3926  CA  GLU B 213      21.962  27.808  -4.411  1.00 34.74           C  
ANISOU 3926  CA  GLU B 213     4265   4230   4702     31    -58    216       C  
ATOM   3927  C   GLU B 213      23.215  27.584  -3.550  1.00 35.15           C  
ANISOU 3927  C   GLU B 213     4351   4284   4721     31    -40    177       C  
ATOM   3928  O   GLU B 213      23.224  26.732  -2.665  1.00 37.86           O  
ANISOU 3928  O   GLU B 213     4713   4624   5047     23    -37    154       O  
ATOM   3929  CB  GLU B 213      22.145  27.242  -5.814  1.00 36.65           C  
ANISOU 3929  CB  GLU B 213     4516   4497   4911     33   -104    232       C  
ATOM   3930  CG  GLU B 213      20.845  27.252  -6.645  1.00 40.10           C  
ANISOU 3930  CG  GLU B 213     4922   4936   5377     30   -130    269       C  
ATOM   3931  CD  GLU B 213      21.052  26.929  -8.129  1.00 44.37           C  
ANISOU 3931  CD  GLU B 213     5471   5500   5884     34   -174    287       C  
ATOM   3932  OE1 GLU B 213      22.108  27.278  -8.718  1.00 44.75           O  
ANISOU 3932  OE1 GLU B 213     5536   5561   5904     45   -175    284       O  
ATOM   3933  OE2 GLU B 213      20.130  26.322  -8.730  1.00 48.91           O  
ANISOU 3933  OE2 GLU B 213     6037   6083   6463     25   -209    305       O  
ATOM   3934  N   LEU B 214      24.234  28.426  -3.727  1.00 32.93           N  
ANISOU 3934  N   LEU B 214     4074   4004   4434     41    -26    172       N  
ATOM   3935  CA  LEU B 214      25.474  28.200  -2.990  1.00 33.59           C  
ANISOU 3935  CA  LEU B 214     4187   4089   4485     40    -15    138       C  
ATOM   3936  C   LEU B 214      25.302  28.416  -1.488  1.00 33.31           C  
ANISOU 3936  C   LEU B 214     4155   4033   4467     34     20    114       C  
ATOM   3937  O   LEU B 214      25.881  27.704  -0.654  1.00 31.55           O  
ANISOU 3937  O   LEU B 214     3959   3812   4214     28     22     85       O  
ATOM   3938  CB  LEU B 214      26.582  29.102  -3.558  1.00 32.11           C  
ANISOU 3938  CB  LEU B 214     4001   3906   4294     52     -8    141       C  
ATOM   3939  CG  LEU B 214      28.015  28.851  -3.163  1.00 33.18           C  
ANISOU 3939  CG  LEU B 214     4164   4047   4394     53     -5    112       C  
ATOM   3940  CD1 LEU B 214      28.547  27.453  -3.565  1.00 30.97           C  
ANISOU 3940  CD1 LEU B 214     3915   3789   4063     51    -38    101       C  
ATOM   3941  CD2 LEU B 214      28.811  29.967  -3.827  1.00 33.21           C  
ANISOU 3941  CD2 LEU B 214     4157   4050   4409     65      4    124       C  
ATOM   3942  N   GLU B 215      24.516  29.439  -1.172  1.00 34.94           N  
ANISOU 3942  N   GLU B 215     4334   4218   4721     36     49    128       N  
ATOM   3943  CA  GLU B 215      24.121  29.753   0.176  1.00 37.47           C  
ANISOU 3943  CA  GLU B 215     4654   4516   5063     31     86    110       C  
ATOM   3944  C   GLU B 215      23.400  28.616   0.906  1.00 33.55           C  
ANISOU 3944  C   GLU B 215     4169   4019   4557     21     82    101       C  
ATOM   3945  O   GLU B 215      23.693  28.302   2.083  1.00 32.44           O  
ANISOU 3945  O   GLU B 215     4052   3872   4402     16    101     73       O  
ATOM   3946  CB  GLU B 215      23.218  30.985   0.131  1.00 42.33           C  
ANISOU 3946  CB  GLU B 215     5235   5110   5737     36    115    135       C  
ATOM   3947  CG  GLU B 215      23.887  32.128   0.810  1.00 47.97           C  
ANISOU 3947  CG  GLU B 215     5951   5806   6467     40    151    116       C  
ATOM   3948  CD  GLU B 215      24.204  31.754   2.252  1.00 54.42           C  
ANISOU 3948  CD  GLU B 215     6798   6615   7264     32    173     78       C  
ATOM   3949  OE1 GLU B 215      23.236  31.438   2.983  1.00 59.07           O  
ANISOU 3949  OE1 GLU B 215     7383   7190   7868     27    190     78       O  
ATOM   3950  OE2 GLU B 215      25.401  31.778   2.664  1.00 54.96           O  
ANISOU 3950  OE2 GLU B 215     6891   6688   7301     30    173     50       O  
ATOM   3951  N   ALA B 216      22.458  28.012   0.222  1.00 31.76           N  
ANISOU 3951  N   ALA B 216     3926   3799   4340     19     58    126       N  
ATOM   3952  CA  ALA B 216      21.781  26.803   0.714  1.00 33.12           C  
ANISOU 3952  CA  ALA B 216     4108   3972   4504      9     48    121       C  
ATOM   3953  C   ALA B 216      22.816  25.659   1.022  1.00 32.98           C  
ANISOU 3953  C   ALA B 216     4129   3971   4428      5     29     91       C  
ATOM   3954  O   ALA B 216      22.849  25.054   2.145  1.00 34.04           O  
ANISOU 3954  O   ALA B 216     4283   4100   4550      0     45     69       O  
ATOM   3955  CB  ALA B 216      20.724  26.349  -0.306  1.00 34.48           C  
ANISOU 3955  CB  ALA B 216     4256   4151   4694      6     16    154       C  
ATOM   3956  N   ILE B 217      23.706  25.420   0.056  1.00 31.74           N  
ANISOU 3956  N   ILE B 217     3985   3835   4240      9      0     91       N  
ATOM   3957  CA  ILE B 217      24.829  24.457   0.214  1.00 28.70           C  
ANISOU 3957  CA  ILE B 217     3635   3465   3802      7    -16     65       C  
ATOM   3958  C   ILE B 217      25.648  24.798   1.471  1.00 28.83           C  
ANISOU 3958  C   ILE B 217     3670   3473   3808      6     14     35       C  
ATOM   3959  O   ILE B 217      26.033  23.893   2.190  1.00 27.72           O  
ANISOU 3959  O   ILE B 217     3555   3337   3639      1     11     14       O  
ATOM   3960  CB  ILE B 217      25.666  24.393  -1.084  1.00 27.76           C  
ANISOU 3960  CB  ILE B 217     3524   3366   3656     13    -45     73       C  
ATOM   3961  CG1 ILE B 217      24.809  23.718  -2.153  1.00 26.80           C  
ANISOU 3961  CG1 ILE B 217     3392   3253   3535     10    -80     96       C  
ATOM   3962  CG2 ILE B 217      27.018  23.719  -0.913  1.00 25.93           C  
ANISOU 3962  CG2 ILE B 217     3326   3148   3379     15    -54     48       C  
ATOM   3963  CD1 ILE B 217      25.334  23.783  -3.560  1.00 27.50           C  
ANISOU 3963  CD1 ILE B 217     3485   3361   3603     18   -108    110       C  
ATOM   3964  N   PHE B 218      25.861  26.088   1.760  1.00 29.53           N  
ANISOU 3964  N   PHE B 218     3748   3549   3922     11     41     34       N  
ATOM   3965  CA  PHE B 218      26.729  26.494   2.878  1.00 30.81           C  
ANISOU 3965  CA  PHE B 218     3929   3704   4073     10     66      4       C  
ATOM   3966  C   PHE B 218      26.068  26.132   4.185  1.00 30.95           C  
ANISOU 3966  C   PHE B 218     3956   3708   4095      3     90     -9       C  
ATOM   3967  O   PHE B 218      26.688  25.539   5.099  1.00 34.11           O  
ANISOU 3967  O   PHE B 218     4384   4112   4464      0     93    -34       O  
ATOM   3968  CB  PHE B 218      26.931  28.043   2.873  1.00 33.69           C  
ANISOU 3968  CB  PHE B 218     4275   4052   4471     16     93      8       C  
ATOM   3969  CG  PHE B 218      28.069  28.559   1.994  1.00 34.98           C  
ANISOU 3969  CG  PHE B 218     4439   4227   4624     23     79     11       C  
ATOM   3970  CD1 PHE B 218      28.779  27.730   1.139  1.00 36.34           C  
ANISOU 3970  CD1 PHE B 218     4624   4421   4760     26     46     14       C  
ATOM   3971  CD2 PHE B 218      28.365  29.910   1.982  1.00 36.74           C  
ANISOU 3971  CD2 PHE B 218     4646   4435   4876     28    102     13       C  
ATOM   3972  CE1 PHE B 218      29.815  28.241   0.348  1.00 39.54           C  
ANISOU 3972  CE1 PHE B 218     5028   4834   5158     34     38     19       C  
ATOM   3973  CE2 PHE B 218      29.396  30.440   1.193  1.00 38.55           C  
ANISOU 3973  CE2 PHE B 218     4873   4672   5100     35     93     18       C  
ATOM   3974  CZ  PHE B 218      30.131  29.604   0.388  1.00 37.84           C  
ANISOU 3974  CZ  PHE B 218     4797   4605   4974     39     61     21       C  
ATOM   3975  N   ASP B 219      24.810  26.549   4.335  1.00 33.32           N  
ANISOU 3975  N   ASP B 219     4232   3991   4437      3    110      8       N  
ATOM   3976  CA  ASP B 219      23.999  26.177   5.514  1.00 33.81           C  
ANISOU 3976  CA  ASP B 219     4300   4038   4507     -1    136      0       C  
ATOM   3977  C   ASP B 219      23.896  24.641   5.646  1.00 31.17           C  
ANISOU 3977  C   ASP B 219     3984   3718   4142     -7    112     -4       C  
ATOM   3978  O   ASP B 219      23.959  24.092   6.753  1.00 28.84           O  
ANISOU 3978  O   ASP B 219     3710   3418   3828    -11    127    -23       O  
ATOM   3979  CB  ASP B 219      22.586  26.760   5.432  1.00 37.19           C  
ANISOU 3979  CB  ASP B 219     4694   4446   4990      0    158     26       C  
ATOM   3980  CG  ASP B 219      22.581  28.275   5.569  1.00 47.86           C  
ANISOU 3980  CG  ASP B 219     6030   5778   6376      6    191     28       C  
ATOM   3981  OD1 ASP B 219      23.564  28.851   6.141  1.00 48.91           O  
ANISOU 3981  OD1 ASP B 219     6182   5907   6492      6    206      1       O  
ATOM   3982  OD2 ASP B 219      21.599  28.896   5.077  1.00 53.43           O  
ANISOU 3982  OD2 ASP B 219     6701   6470   7128     10    201     57       O  
ATOM   3983  N   ARG B 220      23.661  23.975   4.533  1.00 28.43           N  
ANISOU 3983  N   ARG B 220     3627   3385   3791     -8     77     14       N  
ATOM   3984  CA  ARG B 220      23.692  22.497   4.588  1.00 29.83           C  
ANISOU 3984  CA  ARG B 220     3822   3574   3936    -14     52      8       C  
ATOM   3985  C   ARG B 220      25.024  21.914   5.145  1.00 28.32           C  
ANISOU 3985  C   ARG B 220     3668   3396   3696    -14     47    -20       C  
ATOM   3986  O   ARG B 220      25.025  20.921   5.868  1.00 27.62           O  
ANISOU 3986  O   ARG B 220     3597   3309   3586    -19     47    -32       O  
ATOM   3987  CB  ARG B 220      23.367  21.891   3.229  1.00 28.86           C  
ANISOU 3987  CB  ARG B 220     3688   3464   3812    -15     12     29       C  
ATOM   3988  CG  ARG B 220      22.761  20.540   3.462  1.00 32.04           C  
ANISOU 3988  CG  ARG B 220     4098   3869   4207    -23     -1     29       C  
ATOM   3989  CD  ARG B 220      22.877  19.615   2.283  1.00 33.67           C  
ANISOU 3989  CD  ARG B 220     4309   4092   4392    -26    -45     37       C  
ATOM   3990  NE  ARG B 220      22.154  18.363   2.490  1.00 34.56           N  
ANISOU 3990  NE  ARG B 220     4424   4201   4504    -35    -58     40       N  
ATOM   3991  CZ  ARG B 220      21.726  17.574   1.485  1.00 36.15           C  
ANISOU 3991  CZ  ARG B 220     4621   4410   4702    -41    -95     52       C  
ATOM   3992  NH1 ARG B 220      21.975  17.880   0.205  1.00 31.21           N  
ANISOU 3992  NH1 ARG B 220     3990   3797   4069    -38   -123     63       N  
ATOM   3993  NH2 ARG B 220      21.044  16.456   1.772  1.00 35.17           N  
ANISOU 3993  NH2 ARG B 220     4498   4281   4584    -50   -104     53       N  
ATOM   3994  N   THR B 221      26.160  22.539   4.804  1.00 27.37           N  
ANISOU 3994  N   THR B 221     3555   3284   3560    -10     42    -30       N  
ATOM   3995  CA  THR B 221      27.463  22.006   5.196  1.00 24.64           C  
ANISOU 3995  CA  THR B 221     3239   2952   3171    -10     33    -53       C  
ATOM   3996  C   THR B 221      27.578  22.254   6.714  1.00 25.33           C  
ANISOU 3996  C   THR B 221     3342   3028   3254    -13     64    -75       C  
ATOM   3997  O   THR B 221      27.955  21.381   7.468  1.00 25.39           O  
ANISOU 3997  O   THR B 221     3373   3041   3231    -17     62    -91       O  
ATOM   3998  CB  THR B 221      28.559  22.783   4.420  1.00 24.73           C  
ANISOU 3998  CB  THR B 221     3249   2972   3176     -3     23    -53       C  
ATOM   3999  OG1 THR B 221      28.417  22.518   3.001  1.00 23.14           O  
ANISOU 3999  OG1 THR B 221     3035   2781   2974      0     -4    -32       O  
ATOM   4000  CG2 THR B 221      29.971  22.463   4.869  1.00 22.38           C  
ANISOU 4000  CG2 THR B 221     2977   2684   2840     -3     17    -76       C  
ATOM   4001  N   VAL B 222      27.214  23.428   7.180  1.00 25.99           N  
ANISOU 4001  N   VAL B 222     3413   3093   3366    -12     94    -77       N  
ATOM   4002  CA  VAL B 222      27.373  23.729   8.587  1.00 27.84           C  
ANISOU 4002  CA  VAL B 222     3666   3316   3593    -15    124   -100       C  
ATOM   4003  C   VAL B 222      26.484  22.823   9.423  1.00 28.40           C  
ANISOU 4003  C   VAL B 222     3747   3383   3662    -18    136   -100       C  
ATOM   4004  O   VAL B 222      26.837  22.451  10.540  1.00 30.62           O  
ANISOU 4004  O   VAL B 222     4053   3663   3915    -21    148   -120       O  
ATOM   4005  CB  VAL B 222      26.978  25.201   8.924  1.00 29.22           C  
ANISOU 4005  CB  VAL B 222     3826   3469   3805    -13    158   -102       C  
ATOM   4006  CG1 VAL B 222      27.178  25.417  10.441  1.00 29.81           C  
ANISOU 4006  CG1 VAL B 222     3928   3533   3865    -17    188   -130       C  
ATOM   4007  CG2 VAL B 222      27.836  26.175   8.111  1.00 27.47           C  
ANISOU 4007  CG2 VAL B 222     3594   3251   3592     -9    149   -100       C  
ATOM   4008  N   ASN B 223      25.304  22.497   8.914  1.00 28.30           N  
ANISOU 4008  N   ASN B 223     3711   3363   3677    -18    134    -76       N  
ATOM   4009  CA  ASN B 223      24.399  21.672   9.698  1.00 28.99           C  
ANISOU 4009  CA  ASN B 223     3803   3443   3768    -21    149    -73       C  
ATOM   4010  C   ASN B 223      24.369  20.216   9.340  1.00 29.90           C  
ANISOU 4010  C   ASN B 223     3926   3572   3861    -25    119    -67       C  
ATOM   4011  O   ASN B 223      23.393  19.534   9.685  1.00 29.35           O  
ANISOU 4011  O   ASN B 223     3850   3493   3806    -27    127    -57       O  
ATOM   4012  CB  ASN B 223      23.001  22.229   9.648  1.00 29.99           C  
ANISOU 4012  CB  ASN B 223     3900   3548   3945    -20    174    -51       C  
ATOM   4013  CG  ASN B 223      22.950  23.589  10.237  1.00 32.34           C  
ANISOU 4013  CG  ASN B 223     4194   3827   4264    -16    211    -59       C  
ATOM   4014  OD1 ASN B 223      22.926  24.564   9.529  1.00 35.68           O  
ANISOU 4014  OD1 ASN B 223     4595   4245   4714    -13    212    -49       O  
ATOM   4015  ND2 ASN B 223      23.107  23.663  11.555  1.00 34.95           N  
ANISOU 4015  ND2 ASN B 223     4550   4149   4578    -16    242    -82       N  
ATOM   4016  N   THR B 224      25.413  19.726   8.663  1.00 28.47           N  
ANISOU 4016  N   THR B 224     3757   3411   3648    -25     86    -74       N  
ATOM   4017  CA  THR B 224      25.353  18.299   8.201  1.00 29.68           C  
ANISOU 4017  CA  THR B 224     3917   3576   3782    -28     57    -67       C  
ATOM   4018  C   THR B 224      25.269  17.303   9.352  1.00 28.58           C  
ANISOU 4018  C   THR B 224     3799   3435   3623    -31     69    -78       C  
ATOM   4019  O   THR B 224      24.507  16.351   9.314  1.00 30.61           O  
ANISOU 4019  O   THR B 224     4051   3689   3888    -35     63    -67       O  
ATOM   4020  CB  THR B 224      26.417  17.920   7.107  1.00 29.41           C  
ANISOU 4020  CB  THR B 224     3891   3561   3720    -27     20    -69       C  
ATOM   4021  OG1 THR B 224      26.080  18.569   5.856  1.00 30.65           O  
ANISOU 4021  OG1 THR B 224     4024   3719   3901    -24      5    -50       O  
ATOM   4022  CG2 THR B 224      26.385  16.390   6.816  1.00 27.09           C  
ANISOU 4022  CG2 THR B 224     3609   3277   3405    -31     -4    -67       C  
ATOM   4023  N   ALA B 225      26.052  17.510  10.397  1.00 30.84           N  
ANISOU 4023  N   ALA B 225     4109   3723   3883    -30     86    -99       N  
ATOM   4024  CA  ALA B 225      26.008  16.606  11.515  1.00 29.94           C  
ANISOU 4024  CA  ALA B 225     4017   3609   3747    -32     98   -108       C  
ATOM   4025  C   ALA B 225      24.582  16.521  12.073  1.00 30.85           C  
ANISOU 4025  C   ALA B 225     4119   3705   3896    -33    127    -94       C  
ATOM   4026  O   ALA B 225      24.021  15.408  12.271  1.00 31.71           O  
ANISOU 4026  O   ALA B 225     4229   3812   4005    -35    124    -86       O  
ATOM   4027  CB  ALA B 225      27.026  17.004  12.606  1.00 29.87           C  
ANISOU 4027  CB  ALA B 225     4037   3605   3706    -31    113   -133       C  
ATOM   4028  N   LEU B 226      23.999  17.678  12.333  1.00 30.75           N  
ANISOU 4028  N   LEU B 226     4093   3677   3914    -30    156    -92       N  
ATOM   4029  CA  LEU B 226      22.630  17.774  12.811  1.00 32.52           C  
ANISOU 4029  CA  LEU B 226     4300   3879   4175    -29    187    -76       C  
ATOM   4030  C   LEU B 226      21.649  17.114  11.886  1.00 33.27           C  
ANISOU 4030  C   LEU B 226     4366   3971   4302    -33    167    -50       C  
ATOM   4031  O   LEU B 226      20.831  16.355  12.397  1.00 34.56           O  
ANISOU 4031  O   LEU B 226     4526   4124   4478    -34    180    -40       O  
ATOM   4032  CB  LEU B 226      22.216  19.238  12.976  1.00 37.20           C  
ANISOU 4032  CB  LEU B 226     4878   4454   4800    -26    218    -75       C  
ATOM   4033  CG  LEU B 226      20.839  19.347  13.616  1.00 38.86           C  
ANISOU 4033  CG  LEU B 226     5073   4640   5050    -23    257    -60       C  
ATOM   4034  CD1 LEU B 226      20.837  18.654  14.996  1.00 38.61           C  
ANISOU 4034  CD1 LEU B 226     5073   4606   4991    -22    284    -73       C  
ATOM   4035  CD2 LEU B 226      20.511  20.839  13.724  1.00 41.39           C  
ANISOU 4035  CD2 LEU B 226     5379   4942   5403    -19    289    -59       C  
ATOM   4036  N   GLU B 227      21.736  17.363  10.558  1.00 29.78           N  
ANISOU 4036  N   GLU B 227     3905   3537   3873    -34    135    -39       N  
ATOM   4037  CA  GLU B 227      20.877  16.721   9.625  1.00 31.53           C  
ANISOU 4037  CA  GLU B 227     4101   3756   4120    -39    110    -15       C  
ATOM   4038  C   GLU B 227      20.955  15.170   9.817  1.00 33.96           C  
ANISOU 4038  C   GLU B 227     4426   4071   4404    -44     93    -18       C  
ATOM   4039  O   GLU B 227      19.947  14.449   9.866  1.00 37.14           O  
ANISOU 4039  O   GLU B 227     4814   4463   4833    -49     93     -2       O  
ATOM   4040  CB  GLU B 227      21.279  17.147   8.184  1.00 32.96           C  
ANISOU 4040  CB  GLU B 227     4268   3950   4302    -39     75     -8       C  
ATOM   4041  CG  GLU B 227      20.369  16.711   7.025  1.00 32.60           C  
ANISOU 4041  CG  GLU B 227     4196   3904   4285    -45     44     17       C  
ATOM   4042  CD  GLU B 227      20.885  17.097   5.620  1.00 34.80           C  
ANISOU 4042  CD  GLU B 227     4468   4198   4556    -44      8     22       C  
ATOM   4043  OE1 GLU B 227      21.955  17.774   5.474  1.00 35.92           O  
ANISOU 4043  OE1 GLU B 227     4622   4350   4673    -38      9      9       O  
ATOM   4044  OE2 GLU B 227      20.250  16.704   4.615  1.00 31.46           O  
ANISOU 4044  OE2 GLU B 227     4027   3778   4149    -49    -21     41       O  
ATOM   4045  N   ILE B 228      22.152  14.647   9.957  1.00 32.55           N  
ANISOU 4045  N   ILE B 228     4276   3909   4179    -43     78    -38       N  
ATOM   4046  CA  ILE B 228      22.304  13.183   9.927  1.00 32.83           C  
ANISOU 4046  CA  ILE B 228     4326   3953   4194    -48     57    -40       C  
ATOM   4047  C   ILE B 228      21.705  12.618  11.218  1.00 33.71           C  
ANISOU 4047  C   ILE B 228     4446   4052   4311    -47     89    -39       C  
ATOM   4048  O   ILE B 228      21.011  11.584  11.206  1.00 32.25           O  
ANISOU 4048  O   ILE B 228     4253   3859   4139    -52     83    -27       O  
ATOM   4049  CB  ILE B 228      23.814  12.777   9.715  1.00 31.47           C  
ANISOU 4049  CB  ILE B 228     4182   3801   3971    -46     34    -59       C  
ATOM   4050  CG1 ILE B 228      24.204  12.893   8.241  1.00 30.30           C  
ANISOU 4050  CG1 ILE B 228     4025   3664   3820    -46     -1    -54       C  
ATOM   4051  CG2 ILE B 228      24.089  11.349  10.103  1.00 30.90           C  
ANISOU 4051  CG2 ILE B 228     4130   3734   3874    -48     26    -64       C  
ATOM   4052  CD1 ILE B 228      25.679  13.040   8.083  1.00 29.75           C  
ANISOU 4052  CD1 ILE B 228     3978   3612   3712    -42    -13    -71       C  
ATOM   4053  N   VAL B 229      22.016  13.266  12.342  1.00 34.76           N  
ANISOU 4053  N   VAL B 229     4594   4180   4430    -42    123    -52       N  
ATOM   4054  CA  VAL B 229      21.410  12.867  13.586  1.00 36.68           C  
ANISOU 4054  CA  VAL B 229     4847   4412   4678    -40    158    -50       C  
ATOM   4055  C   VAL B 229      19.878  12.945  13.440  1.00 37.44           C  
ANISOU 4055  C   VAL B 229     4909   4485   4829    -42    175    -24       C  
ATOM   4056  O   VAL B 229      19.179  11.981  13.678  1.00 41.36           O  
ANISOU 4056  O   VAL B 229     5400   4973   5340    -44    178    -12       O  
ATOM   4057  CB  VAL B 229      21.944  13.701  14.764  1.00 35.11           C  
ANISOU 4057  CB  VAL B 229     4672   4211   4455    -34    192    -69       C  
ATOM   4058  CG1 VAL B 229      21.059  13.559  15.982  1.00 34.18           C  
ANISOU 4058  CG1 VAL B 229     4559   4076   4350    -30    236    -63       C  
ATOM   4059  CG2 VAL B 229      23.352  13.273  15.086  1.00 32.51           C  
ANISOU 4059  CG2 VAL B 229     4376   3903   4072    -33    175    -90       C  
ATOM   4060  N   ASN B 230      19.344  14.062  13.009  1.00 39.35           N  
ANISOU 4060  N   ASN B 230     5127   4718   5106    -40    184    -15       N  
ATOM   4061  CA  ASN B 230      17.892  14.116  12.752  1.00 42.01           C  
ANISOU 4061  CA  ASN B 230     5427   5033   5499    -43    195     12       C  
ATOM   4062  C   ASN B 230      17.347  12.931  11.965  1.00 42.73           C  
ANISOU 4062  C   ASN B 230     5502   5125   5607    -51    160     29       C  
ATOM   4063  O   ASN B 230      16.194  12.520  12.165  1.00 43.39           O  
ANISOU 4063  O   ASN B 230     5564   5191   5731    -54    174     50       O  
ATOM   4064  CB  ASN B 230      17.471  15.417  12.090  1.00 42.51           C  
ANISOU 4064  CB  ASN B 230     5463   5089   5599    -41    199     24       C  
ATOM   4065  CG  ASN B 230      17.656  16.613  13.015  1.00 47.11           C  
ANISOU 4065  CG  ASN B 230     6057   5662   6180    -32    244     11       C  
ATOM   4066  OD1 ASN B 230      17.866  16.445  14.224  1.00 49.08           O  
ANISOU 4066  OD1 ASN B 230     6333   5907   6405    -28    275     -3       O  
ATOM   4067  ND2 ASN B 230      17.616  17.825  12.452  1.00 45.42           N  
ANISOU 4067  ND2 ASN B 230     5825   5443   5988    -30    246     15       N  
ATOM   4068  N   LEU B 231      18.164  12.370  11.079  1.00 38.82           N  
ANISOU 4068  N   LEU B 231     5018   4650   5082    -56    117     20       N  
ATOM   4069  CA  LEU B 231      17.676  11.312  10.227  1.00 36.53           C  
ANISOU 4069  CA  LEU B 231     4714   4360   4806    -66     81     33       C  
ATOM   4070  C   LEU B 231      17.771   9.983  10.940  1.00 39.32           C  
ANISOU 4070  C   LEU B 231     5085   4711   5140    -68     85     28       C  
ATOM   4071  O   LEU B 231      17.556   8.929  10.341  1.00 39.72           O  
ANISOU 4071  O   LEU B 231     5132   4763   5196    -76     55     33       O  
ATOM   4072  CB  LEU B 231      18.407  11.292   8.882  1.00 33.65           C  
ANISOU 4072  CB  LEU B 231     4351   4013   4418    -69     34     27       C  
ATOM   4073  CG  LEU B 231      17.914  12.402   7.989  1.00 32.41           C  
ANISOU 4073  CG  LEU B 231     4166   3855   4294    -69     25     42       C  
ATOM   4074  CD1 LEU B 231      18.764  12.458   6.717  1.00 31.16           C  
ANISOU 4074  CD1 LEU B 231     4015   3717   4107    -71    -16     35       C  
ATOM   4075  CD2 LEU B 231      16.467  12.070   7.668  1.00 33.16           C  
ANISOU 4075  CD2 LEU B 231     4225   3932   4442    -78     19     70       C  
ATOM   4076  N   HIS B 232      18.068  10.019  12.232  1.00 43.74           N  
ANISOU 4076  N   HIS B 232     5668   5269   5681    -60    123     17       N  
ATOM   4077  CA  HIS B 232      18.220   8.781  12.964  1.00 48.70           C  
ANISOU 4077  CA  HIS B 232     6316   5897   6290    -60    129     14       C  
ATOM   4078  C   HIS B 232      19.430   8.038  12.466  1.00 47.24           C  
ANISOU 4078  C   HIS B 232     6155   5733   6058    -62     94     -2       C  
ATOM   4079  O   HIS B 232      19.414   6.823  12.254  1.00 45.41           O  
ANISOU 4079  O   HIS B 232     5928   5502   5824    -67     75      0       O  
ATOM   4080  CB  HIS B 232      16.930   7.937  12.910  1.00 52.60           C  
ANISOU 4080  CB  HIS B 232     6783   6371   6830    -67    130     38       C  
ATOM   4081  CG  HIS B 232      15.775   8.590  13.626  1.00 60.32           C  
ANISOU 4081  CG  HIS B 232     7739   7326   7853    -63    174     56       C  
ATOM   4082  ND1 HIS B 232      14.768   9.208  12.973  1.00 63.94           N  
ANISOU 4082  ND1 HIS B 232     8159   7770   8362    -67    171     77       N  
ATOM   4083  CD2 HIS B 232      15.522   8.754  14.986  1.00 64.06           C  
ANISOU 4083  CD2 HIS B 232     8225   7788   8325    -53    225     57       C  
ATOM   4084  CE1 HIS B 232      13.898   9.711  13.864  1.00 65.41           C  
ANISOU 4084  CE1 HIS B 232     8333   7936   8582    -60    218     91       C  
ATOM   4085  NE2 HIS B 232      14.359   9.430  15.098  1.00 69.67           N  
ANISOU 4085  NE2 HIS B 232     8904   8476   9088    -51    252     78       N  
ATOM   4086  N   ALA B 233      20.507   8.780  12.284  1.00 47.84           N  
ANISOU 4086  N   ALA B 233     6248   5825   6102    -58     86    -20       N  
ATOM   4087  CA  ALA B 233      21.791   8.158  12.095  1.00 49.27           C  
ANISOU 4087  CA  ALA B 233     6456   6026   6236    -57     63    -37       C  
ATOM   4088  C   ALA B 233      22.801   8.876  13.039  1.00 52.62           C  
ANISOU 4088  C   ALA B 233     6906   6460   6624    -49     84    -55       C  
ATOM   4089  O   ALA B 233      22.409   9.479  14.062  1.00 52.92           O  
ANISOU 4089  O   ALA B 233     6947   6490   6669    -44    121    -56       O  
ATOM   4090  CB  ALA B 233      22.186   8.198  10.624  1.00 43.38           C  
ANISOU 4090  CB  ALA B 233     5703   5291   5487    -61     21    -38       C  
ATOM   4091  N   SER B 234      24.089   8.765  12.734  1.00 50.43           N  
ANISOU 4091  N   SER B 234     6649   6202   6309    -47     62    -71       N  
ATOM   4092  CA  SER B 234      25.098   9.651  13.339  1.00 48.92           C  
ANISOU 4092  CA  SER B 234     6476   6021   6087    -41     74    -88       C  
ATOM   4093  C   SER B 234      26.420   9.542  12.529  1.00 39.85           C  
ANISOU 4093  C   SER B 234     5340   4892   4908    -40     41    -99       C  
ATOM   4094  O   SER B 234      26.798   8.437  12.130  1.00 41.96           O  
ANISOU 4094  O   SER B 234     5615   5165   5161    -42     20    -98       O  
ATOM   4095  CB  SER B 234      25.318   9.337  14.827  1.00 51.59           C  
ANISOU 4095  CB  SER B 234     6840   6360   6401    -37    102    -96       C  
ATOM   4096  OG  SER B 234      25.615  10.554  15.512  1.00 51.50           O  
ANISOU 4096  OG  SER B 234     6837   6349   6381    -34    124   -109       O  
ATOM   4097  N   PRO B 235      27.055  10.678  12.220  1.00 31.87           N  
ANISOU 4097  N   PRO B 235     4327   3887   3892    -38     38   -108       N  
ATOM   4098  CA  PRO B 235      28.212  10.648  11.353  1.00 29.93           C  
ANISOU 4098  CA  PRO B 235     4088   3657   3624    -36      9   -115       C  
ATOM   4099  C   PRO B 235      29.348   9.835  11.892  1.00 28.77           C  
ANISOU 4099  C   PRO B 235     3967   3523   3439    -34      2   -125       C  
ATOM   4100  O   PRO B 235      29.888  10.153  12.964  1.00 30.66           O  
ANISOU 4100  O   PRO B 235     4223   3767   3658    -32     17   -136       O  
ATOM   4101  CB  PRO B 235      28.650  12.111  11.307  1.00 28.07           C  
ANISOU 4101  CB  PRO B 235     3848   3423   3393    -34     17   -123       C  
ATOM   4102  CG  PRO B 235      27.450  12.889  11.659  1.00 27.50           C  
ANISOU 4102  CG  PRO B 235     3758   3334   3355    -35     44   -116       C  
ATOM   4103  CD  PRO B 235      26.721  12.045  12.648  1.00 29.60           C  
ANISOU 4103  CD  PRO B 235     4031   3591   3622    -37     63   -112       C  
ATOM   4104  N   TYR B 236      29.732   8.790  11.180  1.00 29.01           N  
ANISOU 4104  N   TYR B 236     4003   3560   3459    -34    -21   -121       N  
ATOM   4105  CA  TYR B 236      30.995   8.143  11.506  1.00 27.99           C  
ANISOU 4105  CA  TYR B 236     3896   3445   3295    -30    -30   -129       C  
ATOM   4106  C   TYR B 236      31.799   7.661  10.335  1.00 26.80           C  
ANISOU 4106  C   TYR B 236     3746   3302   3132    -27    -57   -128       C  
ATOM   4107  O   TYR B 236      33.009   7.539  10.446  1.00 24.82           O  
ANISOU 4107  O   TYR B 236     3510   3063   2857    -23    -65   -134       O  
ATOM   4108  CB  TYR B 236      30.820   7.020  12.480  1.00 32.14           C  
ANISOU 4108  CB  TYR B 236     4434   3967   3808    -30    -19   -126       C  
ATOM   4109  CG  TYR B 236      29.780   6.004  12.137  1.00 36.76           C  
ANISOU 4109  CG  TYR B 236     5010   4540   4413    -34    -22   -114       C  
ATOM   4110  CD1 TYR B 236      28.486   6.159  12.619  1.00 40.57           C  
ANISOU 4110  CD1 TYR B 236     5481   5009   4925    -38     -1   -106       C  
ATOM   4111  CD2 TYR B 236      30.082   4.811  11.453  1.00 39.77           C  
ANISOU 4111  CD2 TYR B 236     5398   4923   4788    -35    -42   -111       C  
ATOM   4112  CE1 TYR B 236      27.485   5.232  12.370  1.00 44.31           C  
ANISOU 4112  CE1 TYR B 236     5944   5470   5422    -43     -3    -94       C  
ATOM   4113  CE2 TYR B 236      29.065   3.866  11.177  1.00 44.26           C  
ANISOU 4113  CE2 TYR B 236     5958   5479   5379    -40    -45   -101       C  
ATOM   4114  CZ  TYR B 236      27.760   4.096  11.664  1.00 49.33           C  
ANISOU 4114  CZ  TYR B 236     6585   6107   6051    -45    -26    -92       C  
ATOM   4115  OH  TYR B 236      26.673   3.242  11.494  1.00 50.03           O  
ANISOU 4115  OH  TYR B 236     6661   6180   6167    -51    -27    -80       O  
ATOM   4116  N   VAL B 237      31.141   7.340   9.229  1.00 26.35           N  
ANISOU 4116  N   VAL B 237     3678   3239   3093    -30    -72   -119       N  
ATOM   4117  CA  VAL B 237      31.853   6.913   8.019  1.00 28.17           C  
ANISOU 4117  CA  VAL B 237     3913   3477   3311    -27    -97   -119       C  
ATOM   4118  C   VAL B 237      32.839   7.982   7.476  1.00 27.60           C  
ANISOU 4118  C   VAL B 237     3839   3415   3230    -21   -102   -123       C  
ATOM   4119  O   VAL B 237      34.046   7.766   7.460  1.00 27.98           O  
ANISOU 4119  O   VAL B 237     3901   3473   3256    -15   -108   -128       O  
ATOM   4120  CB  VAL B 237      30.830   6.435   6.969  1.00 29.13           C  
ANISOU 4120  CB  VAL B 237     4023   3589   3453    -33   -112   -110       C  
ATOM   4121  CG1 VAL B 237      31.503   5.955   5.709  1.00 28.91           C  
ANISOU 4121  CG1 VAL B 237     4005   3568   3410    -29   -136   -111       C  
ATOM   4122  CG2 VAL B 237      30.076   5.244   7.550  1.00 29.46           C  
ANISOU 4122  CG2 VAL B 237     4068   3621   3502    -38   -107   -106       C  
ATOM   4123  N   ALA B 238      32.297   9.132   7.084  1.00 25.95           N  
ANISOU 4123  N   ALA B 238     3612   3202   3042    -22    -99   -120       N  
ATOM   4124  CA  ALA B 238      33.105  10.291   6.656  1.00 23.65           C  
ANISOU 4124  CA  ALA B 238     3316   2918   2749    -17   -100   -123       C  
ATOM   4125  C   ALA B 238      34.108  10.761   7.658  1.00 21.70           C  
ANISOU 4125  C   ALA B 238     3079   2677   2487    -14    -89   -134       C  
ATOM   4126  O   ALA B 238      35.278  10.906   7.342  1.00 21.43           O  
ANISOU 4126  O   ALA B 238     3050   2651   2438     -9    -97   -137       O  
ATOM   4127  CB  ALA B 238      32.235  11.408   6.125  1.00 24.47           C  
ANISOU 4127  CB  ALA B 238     3399   3015   2883    -19    -96   -116       C  
ATOM   4128  N   PRO B 239      33.715  10.919   8.916  1.00 20.90           N  
ANISOU 4128  N   PRO B 239     2981   2570   2387    -18    -70   -140       N  
ATOM   4129  CA  PRO B 239      34.816  11.281   9.850  1.00 19.31           C  
ANISOU 4129  CA  PRO B 239     2793   2377   2166    -17    -64   -152       C  
ATOM   4130  C   PRO B 239      35.974  10.295   9.868  1.00 18.35           C  
ANISOU 4130  C   PRO B 239     2687   2267   2017    -13    -79   -152       C  
ATOM   4131  O   PRO B 239      37.156  10.711   9.764  1.00 18.49           O  
ANISOU 4131  O   PRO B 239     2707   2292   2024     -9    -86   -156       O  
ATOM   4132  CB  PRO B 239      34.089  11.395  11.215  1.00 19.96           C  
ANISOU 4132  CB  PRO B 239     2881   2452   2249    -22    -41   -158       C  
ATOM   4133  CG  PRO B 239      32.645  11.754  10.814  1.00 20.24           C  
ANISOU 4133  CG  PRO B 239     2897   2474   2317    -25    -30   -149       C  
ATOM   4134  CD  PRO B 239      32.387  11.030   9.532  1.00 21.35           C  
ANISOU 4134  CD  PRO B 239     3030   2616   2465    -24    -51   -137       C  
ATOM   4135  N   ALA B 240      35.675   8.977   9.941  1.00 17.72           N  
ANISOU 4135  N   ALA B 240     2617   2186   1929    -13    -82   -147       N  
ATOM   4136  CA  ALA B 240      36.709   7.997   9.863  1.00 17.10           C  
ANISOU 4136  CA  ALA B 240     2551   2116   1828     -8    -94   -145       C  
ATOM   4137  C   ALA B 240      37.519   8.204   8.617  1.00 17.33           C  
ANISOU 4137  C   ALA B 240     2577   2150   1857     -2   -109   -142       C  
ATOM   4138  O   ALA B 240      38.736   8.230   8.688  1.00 17.45           O  
ANISOU 4138  O   ALA B 240     2598   2174   1859      2   -115   -142       O  
ATOM   4139  CB  ALA B 240      36.157   6.534   9.919  1.00 16.80           C  
ANISOU 4139  CB  ALA B 240     2522   2074   1787     -9    -96   -138       C  
ATOM   4140  N   ALA B 241      36.887   8.255   7.418  1.00 17.33           N  
ANISOU 4140  N   ALA B 241     2568   2145   1871     -1   -117   -136       N  
ATOM   4141  CA  ALA B 241      37.666   8.278   6.237  1.00 17.88           C  
ANISOU 4141  CA  ALA B 241     2638   2219   1935      5   -130   -132       C  
ATOM   4142  C   ALA B 241      38.570   9.534   6.250  1.00 19.72           C  
ANISOU 4142  C   ALA B 241     2863   2458   2171      9   -127   -134       C  
ATOM   4143  O   ALA B 241      39.727   9.485   5.790  1.00 20.73           O  
ANISOU 4143  O   ALA B 241     2994   2592   2289     17   -133   -131       O  
ATOM   4144  CB  ALA B 241      36.692   8.364   5.038  1.00 18.10           C  
ANISOU 4144  CB  ALA B 241     2656   2241   1977      4   -138   -125       C  
ATOM   4145  N   ALA B 242      38.041  10.668   6.749  1.00 19.67           N  
ANISOU 4145  N   ALA B 242     2844   2448   2180      4   -116   -138       N  
ATOM   4146  CA  ALA B 242      38.772  11.886   6.582  1.00 22.32           C  
ANISOU 4146  CA  ALA B 242     3170   2786   2524      7   -114   -140       C  
ATOM   4147  C   ALA B 242      40.049  11.775   7.457  1.00 26.83           C  
ANISOU 4147  C   ALA B 242     3751   3364   3078      8   -116   -147       C  
ATOM   4148  O   ALA B 242      41.136  12.180   6.989  1.00 29.39           O  
ANISOU 4148  O   ALA B 242     4071   3693   3403     14   -121   -144       O  
ATOM   4149  CB  ALA B 242      37.920  13.075   7.037  1.00 21.62           C  
ANISOU 4149  CB  ALA B 242     3068   2688   2456      1   -100   -145       C  
ATOM   4150  N   ILE B 243      39.911  11.198   8.682  1.00 25.23           N  
ANISOU 4150  N   ILE B 243     3560   3162   2862      2   -111   -153       N  
ATOM   4151  CA  ILE B 243      41.030  10.935   9.584  1.00 26.11           C  
ANISOU 4151  CA  ILE B 243     3681   3282   2955      2   -115   -157       C  
ATOM   4152  C   ILE B 243      42.068   9.983   8.993  1.00 27.49           C  
ANISOU 4152  C   ILE B 243     3862   3463   3118     11   -128   -147       C  
ATOM   4153  O   ILE B 243      43.266  10.228   9.095  1.00 28.76           O  
ANISOU 4153  O   ILE B 243     4022   3630   3275     14   -134   -146       O  
ATOM   4154  CB  ILE B 243      40.535  10.200  10.844  1.00 24.97           C  
ANISOU 4154  CB  ILE B 243     3552   3139   2797     -2   -108   -162       C  
ATOM   4155  CG1 ILE B 243      39.776  11.162  11.723  1.00 24.91           C  
ANISOU 4155  CG1 ILE B 243     3543   3125   2796    -10    -93   -174       C  
ATOM   4156  CG2 ILE B 243      41.706   9.670  11.616  1.00 26.66           C  
ANISOU 4156  CG2 ILE B 243     3777   3362   2988     -1   -117   -162       C  
ATOM   4157  CD1 ILE B 243      38.426  10.636  12.168  1.00 26.15           C  
ANISOU 4157  CD1 ILE B 243     3703   3274   2956    -13    -79   -172       C  
ATOM   4158  N   ILE B 244      41.618   8.888   8.408  1.00 27.32           N  
ANISOU 4158  N   ILE B 244     3847   3439   3092     14   -130   -140       N  
ATOM   4159  CA  ILE B 244      42.558   8.005   7.711  1.00 28.83           C  
ANISOU 4159  CA  ILE B 244     4045   3634   3274     24   -138   -131       C  
ATOM   4160  C   ILE B 244      43.283   8.736   6.516  1.00 30.12           C  
ANISOU 4160  C   ILE B 244     4198   3798   3446     32   -142   -125       C  
ATOM   4161  O   ILE B 244      44.449   8.477   6.262  1.00 27.63           O  
ANISOU 4161  O   ILE B 244     3884   3486   3125     40   -146   -118       O  
ATOM   4162  CB  ILE B 244      41.910   6.638   7.361  1.00 28.46           C  
ANISOU 4162  CB  ILE B 244     4009   3582   3220     25   -139   -127       C  
ATOM   4163  CG1 ILE B 244      41.406   5.899   8.623  1.00 25.96           C  
ANISOU 4163  CG1 ILE B 244     3702   3266   2895     19   -133   -130       C  
ATOM   4164  CG2 ILE B 244      42.813   5.763   6.492  1.00 29.45           C  
ANISOU 4164  CG2 ILE B 244     4143   3708   3337     36   -145   -118       C  
ATOM   4165  CD1 ILE B 244      42.410   5.770   9.775  1.00 27.45           C  
ANISOU 4165  CD1 ILE B 244     3896   3463   3069     19   -134   -129       C  
ATOM   4166  N   GLU B 245      42.604   9.643   5.792  1.00 32.06           N  
ANISOU 4166  N   GLU B 245     4434   4040   3708     31   -140   -126       N  
ATOM   4167  CA  GLU B 245      43.354  10.545   4.867  1.00 32.43           C  
ANISOU 4167  CA  GLU B 245     4469   4088   3765     39   -141   -120       C  
ATOM   4168  C   GLU B 245      44.516  11.337   5.534  1.00 28.60           C  
ANISOU 4168  C   GLU B 245     3975   3606   3284     39   -141   -121       C  
ATOM   4169  O   GLU B 245      45.626  11.407   5.046  1.00 26.95           O  
ANISOU 4169  O   GLU B 245     3762   3398   3076     48   -143   -113       O  
ATOM   4170  CB  GLU B 245      42.467  11.465   4.039  1.00 32.65           C  
ANISOU 4170  CB  GLU B 245     4485   4111   3809     39   -138   -118       C  
ATOM   4171  CG  GLU B 245      43.164  11.961   2.787  1.00 36.41           C  
ANISOU 4171  CG  GLU B 245     4954   4587   4290     50   -139   -107       C  
ATOM   4172  CD  GLU B 245      42.244  12.738   1.848  1.00 44.62           C  
ANISOU 4172  CD  GLU B 245     5984   5625   5344     51   -138   -102       C  
ATOM   4173  OE1 GLU B 245      41.020  12.758   2.117  1.00 47.57           O  
ANISOU 4173  OE1 GLU B 245     6355   5994   5723     42   -138   -106       O  
ATOM   4174  OE2 GLU B 245      42.713  13.294   0.807  1.00 46.27           O  
ANISOU 4174  OE2 GLU B 245     6187   5834   5557     61   -138    -91       O  
ATOM   4175  N   MET B 246      44.250  11.901   6.678  1.00 30.12           N  
ANISOU 4175  N   MET B 246     4166   3798   3480     29   -138   -133       N  
ATOM   4176  CA  MET B 246      45.281  12.545   7.464  1.00 28.90           C  
ANISOU 4176  CA  MET B 246     4006   3647   3328     25   -141   -137       C  
ATOM   4177  C   MET B 246      46.400  11.597   7.864  1.00 28.69           C  
ANISOU 4177  C   MET B 246     3987   3627   3285     29   -150   -131       C  
ATOM   4178  O   MET B 246      47.589  11.889   7.624  1.00 27.86           O  
ANISOU 4178  O   MET B 246     3874   3524   3188     35   -156   -123       O  
ATOM   4179  CB  MET B 246      44.651  13.170   8.665  1.00 31.37           C  
ANISOU 4179  CB  MET B 246     4320   3957   3640     13   -136   -153       C  
ATOM   4180  CG  MET B 246      43.963  14.521   8.376  1.00 32.12           C  
ANISOU 4180  CG  MET B 246     4402   4044   3759      9   -125   -159       C  
ATOM   4181  SD  MET B 246      42.647  14.873   9.571  1.00 32.23           S  
ANISOU 4181  SD  MET B 246     4423   4051   3772     -2   -111   -175       S  
ATOM   4182  CE  MET B 246      43.515  15.295  11.101  1.00 31.87           C  
ANISOU 4182  CE  MET B 246     4387   4009   3712    -12   -116   -191       C  
ATOM   4183  N   ALA B 247      46.038  10.434   8.420  1.00 27.59           N  
ANISOU 4183  N   ALA B 247     3863   3491   3128     28   -151   -131       N  
ATOM   4184  CA  ALA B 247      47.041   9.571   8.979  1.00 27.00           C  
ANISOU 4184  CA  ALA B 247     3795   3423   3040     31   -159   -124       C  
ATOM   4185  C   ALA B 247      47.864   8.947   7.911  1.00 25.61           C  
ANISOU 4185  C   ALA B 247     3616   3246   2866     44   -161   -108       C  
ATOM   4186  O   ALA B 247      49.022   8.687   8.149  1.00 23.68           O  
ANISOU 4186  O   ALA B 247     3370   3006   2621     49   -167    -99       O  
ATOM   4187  CB  ALA B 247      46.470   8.532   9.943  1.00 28.60           C  
ANISOU 4187  CB  ALA B 247     4013   3629   3224     26   -158   -126       C  
ATOM   4188  N   GLU B 248      47.319   8.860   6.702  1.00 25.46           N  
ANISOU 4188  N   GLU B 248     3598   3221   2852     51   -155   -105       N  
ATOM   4189  CA  GLU B 248      47.974   8.250   5.595  1.00 26.18           C  
ANISOU 4189  CA  GLU B 248     3692   3310   2942     64   -153    -92       C  
ATOM   4190  C   GLU B 248      48.899   9.202   4.809  1.00 25.88           C  
ANISOU 4190  C   GLU B 248     3640   3271   2921     73   -151    -83       C  
ATOM   4191  O   GLU B 248      49.900   8.773   4.211  1.00 24.23           O  
ANISOU 4191  O   GLU B 248     3430   3061   2713     85   -149    -70       O  
ATOM   4192  CB  GLU B 248      46.904   7.684   4.656  1.00 30.33           C  
ANISOU 4192  CB  GLU B 248     4230   3831   3464     67   -149    -94       C  
ATOM   4193  CG  GLU B 248      47.481   7.096   3.385  1.00 34.83           C  
ANISOU 4193  CG  GLU B 248     4806   4397   4029     81   -145    -82       C  
ATOM   4194  CD  GLU B 248      46.466   6.808   2.282  1.00 38.90           C  
ANISOU 4194  CD  GLU B 248     5332   4906   4539     83   -145    -85       C  
ATOM   4195  OE1 GLU B 248      45.688   7.730   1.915  1.00 43.26           O  
ANISOU 4195  OE1 GLU B 248     5875   5459   5100     78   -146    -89       O  
ATOM   4196  OE2 GLU B 248      46.502   5.666   1.737  1.00 39.53           O  
ANISOU 4196  OE2 GLU B 248     5429   4982   4608     89   -144    -82       O  
ATOM   4197  N   SER B 249      48.558  10.481   4.772  1.00 24.49           N  
ANISOU 4197  N   SER B 249     3451   3094   2759     67   -150    -90       N  
ATOM   4198  CA  SER B 249      49.453  11.487   4.254  1.00 23.90           C  
ANISOU 4198  CA  SER B 249     3359   3016   2703     73   -148    -82       C  
ATOM   4199  C   SER B 249      50.694  11.550   5.176  1.00 24.60           C  
ANISOU 4199  C   SER B 249     3439   3109   2797     70   -156    -78       C  
ATOM   4200  O   SER B 249      51.841  11.755   4.685  1.00 23.91           O  
ANISOU 4200  O   SER B 249     3340   3019   2723     80   -155    -64       O  
ATOM   4201  CB  SER B 249      48.762  12.829   4.336  1.00 25.04           C  
ANISOU 4201  CB  SER B 249     3491   3157   2863     65   -145    -91       C  
ATOM   4202  OG  SER B 249      49.422  13.741   3.498  1.00 27.82           O  
ANISOU 4202  OG  SER B 249     3827   3506   3235     73   -140    -81       O  
ATOM   4203  N   TYR B 250      50.491  11.377   6.495  1.00 23.80           N  
ANISOU 4203  N   TYR B 250     3344   3013   2686     58   -164    -90       N  
ATOM   4204  CA  TYR B 250      51.624  11.328   7.388  1.00 23.37           C  
ANISOU 4204  CA  TYR B 250     3283   2963   2633     54   -176    -86       C  
ATOM   4205  C   TYR B 250      52.454  10.042   7.230  1.00 26.32           C  
ANISOU 4205  C   TYR B 250     3663   3339   2998     65   -178    -69       C  
ATOM   4206  O   TYR B 250      53.713  10.097   6.997  1.00 27.69           O  
ANISOU 4206  O   TYR B 250     3823   3512   3185     73   -181    -53       O  
ATOM   4207  CB  TYR B 250      51.107  11.356   8.790  1.00 25.43           C  
ANISOU 4207  CB  TYR B 250     3553   3230   2879     39   -184   -102       C  
ATOM   4208  CG  TYR B 250      52.190  11.103   9.817  1.00 25.85           C  
ANISOU 4208  CG  TYR B 250     3604   3290   2927     35   -200    -97       C  
ATOM   4209  CD1 TYR B 250      53.064  12.097  10.163  1.00 26.35           C  
ANISOU 4209  CD1 TYR B 250     3652   3353   3006     28   -211    -99       C  
ATOM   4210  CD2 TYR B 250      52.364   9.850  10.407  1.00 28.49           C  
ANISOU 4210  CD2 TYR B 250     3951   3631   3242     37   -205    -90       C  
ATOM   4211  CE1 TYR B 250      54.068  11.911  11.110  1.00 26.30           C  
ANISOU 4211  CE1 TYR B 250     3641   3353   2996     22   -229    -95       C  
ATOM   4212  CE2 TYR B 250      53.390   9.647  11.355  1.00 28.42           C  
ANISOU 4212  CE2 TYR B 250     3939   3631   3229     32   -222    -83       C  
ATOM   4213  CZ  TYR B 250      54.243  10.697  11.667  1.00 27.42           C  
ANISOU 4213  CZ  TYR B 250     3795   3504   3118     25   -235    -86       C  
ATOM   4214  OH  TYR B 250      55.251  10.537  12.606  1.00 30.90           O  
ANISOU 4214  OH  TYR B 250     4232   3953   3555     19   -256    -79       O  
ATOM   4215  N   LEU B 251      51.782   8.877   7.302  1.00 24.66           N  
ANISOU 4215  N   LEU B 251     3470   3131   2768     67   -174    -70       N  
ATOM   4216  CA  LEU B 251      52.485   7.592   7.266  1.00 25.25           C  
ANISOU 4216  CA  LEU B 251     3551   3205   2834     77   -174    -54       C  
ATOM   4217  C   LEU B 251      53.249   7.361   5.978  1.00 26.21           C  
ANISOU 4217  C   LEU B 251     3668   3320   2967     94   -163    -37       C  
ATOM   4218  O   LEU B 251      54.327   6.802   5.989  1.00 27.30           O  
ANISOU 4218  O   LEU B 251     3802   3458   3111    103   -163    -21       O  
ATOM   4219  CB  LEU B 251      51.499   6.396   7.489  1.00 23.99           C  
ANISOU 4219  CB  LEU B 251     3413   3046   2655     76   -169    -59       C  
ATOM   4220  CG  LEU B 251      51.010   6.233   8.917  1.00 24.48           C  
ANISOU 4220  CG  LEU B 251     3482   3116   2703     63   -177    -69       C  
ATOM   4221  CD1 LEU B 251      49.842   5.248   9.081  1.00 23.47           C  
ANISOU 4221  CD1 LEU B 251     3371   2984   2560     60   -170    -75       C  
ATOM   4222  CD2 LEU B 251      52.159   5.918   9.916  1.00 23.86           C  
ANISOU 4222  CD2 LEU B 251     3398   3045   2621     62   -190    -58       C  
ATOM   4223  N   LYS B 252      52.654   7.722   4.843  1.00 29.71           N  
ANISOU 4223  N   LYS B 252     4115   3758   3413    100   -153    -40       N  
ATOM   4224  CA  LYS B 252      53.300   7.636   3.526  1.00 28.69           C  
ANISOU 4224  CA  LYS B 252     3985   3622   3293    117   -141    -26       C  
ATOM   4225  C   LYS B 252      54.052   8.922   3.075  1.00 29.90           C  
ANISOU 4225  C   LYS B 252     4116   3773   3470    121   -138    -18       C  
ATOM   4226  O   LYS B 252      54.487   9.053   1.926  1.00 31.91           O  
ANISOU 4226  O   LYS B 252     4369   4021   3732    136   -126     -5       O  
ATOM   4227  CB  LYS B 252      52.229   7.285   2.530  1.00 30.58           C  
ANISOU 4227  CB  LYS B 252     4241   3857   3519    121   -133    -33       C  
ATOM   4228  CG  LYS B 252      51.898   5.786   2.627  1.00 35.76           C  
ANISOU 4228  CG  LYS B 252     4919   4511   4157    123   -131    -34       C  
ATOM   4229  CD  LYS B 252      50.469   5.547   2.269  1.00 39.06           C  
ANISOU 4229  CD  LYS B 252     5351   4927   4562    116   -132    -48       C  
ATOM   4230  CE  LYS B 252      50.252   4.057   1.980  1.00 44.94           C  
ANISOU 4230  CE  LYS B 252     6117   5665   5292    121   -127    -47       C  
ATOM   4231  NZ  LYS B 252      49.315   3.817   0.813  1.00 48.52           N  
ANISOU 4231  NZ  LYS B 252     6586   6112   5734    123   -125    -55       N  
ATOM   4232  N   ASP B 253      54.224   9.883   3.976  1.00 31.68           N  
ANISOU 4232  N   ASP B 253     4326   4002   3708    108   -150    -25       N  
ATOM   4233  CA  ASP B 253      54.925  11.126   3.602  1.00 29.25           C  
ANISOU 4233  CA  ASP B 253     3996   3690   3427    111   -148    -18       C  
ATOM   4234  C   ASP B 253      54.369  11.595   2.230  1.00 27.45           C  
ANISOU 4234  C   ASP B 253     3770   3456   3200    121   -133    -15       C  
ATOM   4235  O   ASP B 253      55.119  11.799   1.303  1.00 25.65           O  
ANISOU 4235  O   ASP B 253     3534   3223   2986    136   -121      1       O  
ATOM   4236  CB  ASP B 253      56.472  10.893   3.544  1.00 31.80           C  
ANISOU 4236  CB  ASP B 253     4304   4011   3768    121   -148      3       C  
ATOM   4237  CG  ASP B 253      57.261  12.200   3.174  1.00 34.07           C  
ANISOU 4237  CG  ASP B 253     4565   4291   4087    123   -145     13       C  
ATOM   4238  OD1 ASP B 253      57.087  13.184   3.881  1.00 31.14           O  
ANISOU 4238  OD1 ASP B 253     4182   3921   3726    108   -157      0       O  
ATOM   4239  OD2 ASP B 253      57.985  12.260   2.140  1.00 39.59           O  
ANISOU 4239  OD2 ASP B 253     5256   4983   4801    140   -130     32       O  
ATOM   4240  N   LEU B 254      53.054  11.808   2.100  1.00 25.81           N  
ANISOU 4240  N   LEU B 254     3573   3251   2983    114   -133    -30       N  
ATOM   4241  CA  LEU B 254      52.550  12.282   0.784  1.00 25.03           C  
ANISOU 4241  CA  LEU B 254     3476   3148   2886    124   -121    -25       C  
ATOM   4242  C   LEU B 254      52.651  13.847   0.670  1.00 25.10           C  
ANISOU 4242  C   LEU B 254     3461   3152   2920    120   -119    -24       C  
ATOM   4243  O   LEU B 254      52.637  14.377  -0.453  1.00 23.08           O  
ANISOU 4243  O   LEU B 254     3202   2893   2673    132   -107    -14       O  
ATOM   4244  CB  LEU B 254      51.103  11.851   0.584  1.00 25.61           C  
ANISOU 4244  CB  LEU B 254     3567   3223   2939    118   -123    -38       C  
ATOM   4245  CG  LEU B 254      50.996  10.350   0.387  1.00 25.39           C  
ANISOU 4245  CG  LEU B 254     3562   3196   2888    123   -123    -37       C  
ATOM   4246  CD1 LEU B 254      49.695   9.916   0.995  1.00 25.39           C  
ANISOU 4246  CD1 LEU B 254     3573   3198   2874    110   -131    -54       C  
ATOM   4247  CD2 LEU B 254      51.055  10.100  -1.139  1.00 27.55           C  
ANISOU 4247  CD2 LEU B 254     3848   3466   3154    140   -111    -26       C  
ATOM   4248  N   LYS B 255      52.829  14.555   1.801  1.00 23.51           N  
ANISOU 4248  N   LYS B 255     3247   2952   2733    106   -128    -35       N  
ATOM   4249  CA  LYS B 255      52.716  16.068   1.835  1.00 24.49           C  
ANISOU 4249  CA  LYS B 255     3350   3070   2883     99   -126    -39       C  
ATOM   4250  C   LYS B 255      51.520  16.634   1.035  1.00 27.60           C  
ANISOU 4250  C   LYS B 255     3746   3461   3276    101   -117    -42       C  
ATOM   4251  O   LYS B 255      51.654  17.465   0.103  1.00 28.11           O  
ANISOU 4251  O   LYS B 255     3799   3522   3359    111   -107    -30       O  
ATOM   4252  CB  LYS B 255      54.041  16.716   1.395  1.00 24.60           C  
ANISOU 4252  CB  LYS B 255     3343   3078   2925    109   -121    -21       C  
ATOM   4253  CG  LYS B 255      55.326  15.921   1.668  1.00 25.74           C  
ANISOU 4253  CG  LYS B 255     3485   3224   3071    115   -125     -8       C  
ATOM   4254  CD  LYS B 255      56.552  16.588   1.022  1.00 28.62           C  
ANISOU 4254  CD  LYS B 255     3826   3579   3467    127   -116     12       C  
ATOM   4255  CE  LYS B 255      57.840  15.769   1.127  1.00 28.90           C  
ANISOU 4255  CE  LYS B 255     3856   3614   3508    136   -118     31       C  
ATOM   4256  NZ  LYS B 255      58.108  15.783   2.599  1.00 33.40           N  
ANISOU 4256  NZ  LYS B 255     4421   4189   4079    116   -141     17       N  
ATOM   4257  N   LYS B 256      50.346  16.105   1.371  1.00 27.85           N  
ANISOU 4257  N   LYS B 256     3794   3497   3289     93   -121    -55       N  
ATOM   4258  CA  LYS B 256      49.113  16.585   0.874  1.00 28.48           C  
ANISOU 4258  CA  LYS B 256     3874   3575   3369     91   -117    -59       C  
ATOM   4259  C   LYS B 256      48.846  17.876   1.615  1.00 25.17           C  
ANISOU 4259  C   LYS B 256     3438   3151   2974     79   -115    -70       C  
ATOM   4260  O   LYS B 256      49.246  18.044   2.792  1.00 24.80           O  
ANISOU 4260  O   LYS B 256     3388   3103   2930     67   -122    -83       O  
ATOM   4261  CB  LYS B 256      48.015  15.588   1.242  1.00 31.21           C  
ANISOU 4261  CB  LYS B 256     4239   3926   3691     84   -123    -70       C  
ATOM   4262  CG  LYS B 256      47.823  14.505   0.186  1.00 35.77           C  
ANISOU 4262  CG  LYS B 256     4834   4506   4248     95   -123    -61       C  
ATOM   4263  CD  LYS B 256      46.776  13.492   0.615  1.00 39.31           C  
ANISOU 4263  CD  LYS B 256     5300   4958   4678     87   -129    -72       C  
ATOM   4264  CE  LYS B 256      45.994  12.896  -0.557  1.00 40.53           C  
ANISOU 4264  CE  LYS B 256     5469   5113   4819     93   -131    -67       C  
ATOM   4265  NZ  LYS B 256      45.190  11.721  -0.060  1.00 43.16           N  
ANISOU 4265  NZ  LYS B 256     5817   5446   5134     85   -138    -77       N  
ATOM   4266  N   VAL B 257      48.143  18.776   0.967  1.00 23.31           N  
ANISOU 4266  N   VAL B 257     3193   2911   2753     81   -107    -67       N  
ATOM   4267  CA  VAL B 257      47.636  19.932   1.726  1.00 23.31           C  
ANISOU 4267  CA  VAL B 257     3178   2902   2773     68   -103    -80       C  
ATOM   4268  C   VAL B 257      46.161  19.628   2.161  1.00 24.30           C  
ANISOU 4268  C   VAL B 257     3315   3029   2888     58   -103    -92       C  
ATOM   4269  O   VAL B 257      45.253  19.399   1.308  1.00 21.69           O  
ANISOU 4269  O   VAL B 257     2987   2700   2552     64   -101    -84       O  
ATOM   4270  CB  VAL B 257      47.632  21.181   0.900  1.00 23.49           C  
ANISOU 4270  CB  VAL B 257     3181   2916   2824     74    -91    -68       C  
ATOM   4271  CG1 VAL B 257      47.239  22.370   1.800  1.00 23.41           C  
ANISOU 4271  CG1 VAL B 257     3158   2896   2839     60    -86    -84       C  
ATOM   4272  CG2 VAL B 257      48.990  21.350   0.207  1.00 23.85           C  
ANISOU 4272  CG2 VAL B 257     3217   2962   2883     87    -89    -50       C  
ATOM   4273  N   LEU B 258      45.987  19.671   3.476  1.00 23.92           N  
ANISOU 4273  N   LEU B 258     3271   2979   2837     44   -105   -111       N  
ATOM   4274  CA  LEU B 258      44.805  19.268   4.189  1.00 27.53           C  
ANISOU 4274  CA  LEU B 258     3740   3437   3282     35   -104   -123       C  
ATOM   4275  C   LEU B 258      44.528  20.296   5.288  1.00 27.98           C  
ANISOU 4275  C   LEU B 258     3790   3484   3354     22    -96   -141       C  
ATOM   4276  O   LEU B 258      45.411  20.572   6.179  1.00 29.20           O  
ANISOU 4276  O   LEU B 258     3947   3638   3509     14   -101   -153       O  
ATOM   4277  CB  LEU B 258      45.046  17.903   4.884  1.00 29.00           C  
ANISOU 4277  CB  LEU B 258     3946   3631   3439     32   -114   -129       C  
ATOM   4278  CG  LEU B 258      45.413  16.775   3.940  1.00 29.60           C  
ANISOU 4278  CG  LEU B 258     4032   3715   3499     44   -121   -114       C  
ATOM   4279  CD1 LEU B 258      45.711  15.499   4.664  1.00 34.82           C  
ANISOU 4279  CD1 LEU B 258     4711   4383   4136     41   -129   -119       C  
ATOM   4280  CD2 LEU B 258      44.323  16.555   2.935  1.00 31.12           C  
ANISOU 4280  CD2 LEU B 258     4225   3906   3690     49   -118   -106       C  
ATOM   4281  N   ILE B 259      43.309  20.820   5.309  1.00 25.73           N  
ANISOU 4281  N   ILE B 259     3501   3191   3081     18    -84   -144       N  
ATOM   4282  CA  ILE B 259      42.957  21.649   6.444  1.00 26.58           C  
ANISOU 4282  CA  ILE B 259     3608   3289   3200      6    -74   -163       C  
ATOM   4283  C   ILE B 259      42.766  20.939   7.786  1.00 27.93           C  
ANISOU 4283  C   ILE B 259     3800   3464   3346     -3    -76   -181       C  
ATOM   4284  O   ILE B 259      41.885  20.079   7.916  1.00 27.54           O  
ANISOU 4284  O   ILE B 259     3761   3418   3283     -4    -75   -179       O  
ATOM   4285  CB  ILE B 259      41.663  22.384   6.201  1.00 28.37           C  
ANISOU 4285  CB  ILE B 259     3823   3505   3448      5    -57   -161       C  
ATOM   4286  CG1 ILE B 259      41.730  23.095   4.856  1.00 27.72           C  
ANISOU 4286  CG1 ILE B 259     3721   3419   3390     16    -54   -141       C  
ATOM   4287  CG2 ILE B 259      41.362  23.287   7.415  1.00 26.05           C  
ANISOU 4287  CG2 ILE B 259     3531   3198   3166     -6    -43   -182       C  
ATOM   4288  CD1 ILE B 259      40.562  23.995   4.642  1.00 29.66           C  
ANISOU 4288  CD1 ILE B 259     3952   3654   3663     15    -38   -137       C  
ATOM   4289  N   CYS B 260      43.500  21.336   8.841  1.00 28.00           N  
ANISOU 4289  N   CYS B 260     3815   3471   3351    -13    -79   -197       N  
ATOM   4290  CA  CYS B 260      43.291  20.675  10.103  1.00 27.06           C  
ANISOU 4290  CA  CYS B 260     3718   3358   3206    -21    -81   -212       C  
ATOM   4291  C   CYS B 260      43.472  21.646  11.236  1.00 28.33           C  
ANISOU 4291  C   CYS B 260     3884   3509   3371    -33    -75   -235       C  
ATOM   4292  O   CYS B 260      43.973  22.763  11.059  1.00 27.17           O  
ANISOU 4292  O   CYS B 260     3723   3353   3248    -36    -73   -239       O  
ATOM   4293  CB  CYS B 260      44.377  19.628  10.320  1.00 30.96           C  
ANISOU 4293  CB  CYS B 260     4222   3866   3675    -19   -101   -208       C  
ATOM   4294  SG  CYS B 260      44.753  18.568   8.922  1.00 38.87           S  
ANISOU 4294  SG  CYS B 260     5219   4877   4673     -4   -111   -183       S  
ATOM   4295  N   SER B 261      43.164  21.200  12.427  1.00 26.31           N  
ANISOU 4295  N   SER B 261     3649   3256   3090    -41    -74   -249       N  
ATOM   4296  CA  SER B 261      43.342  22.085  13.547  1.00 27.28           C  
ANISOU 4296  CA  SER B 261     3782   3371   3212    -53    -69   -273       C  
ATOM   4297  C   SER B 261      44.786  22.004  14.062  1.00 27.80           C  
ANISOU 4297  C   SER B 261     3852   3445   3263    -60    -93   -280       C  
ATOM   4298  O   SER B 261      45.247  20.943  14.388  1.00 26.70           O  
ANISOU 4298  O   SER B 261     3725   3320   3098    -58   -109   -274       O  
ATOM   4299  CB  SER B 261      42.371  21.695  14.630  1.00 26.50           C  
ANISOU 4299  CB  SER B 261     3706   3271   3091    -58    -54   -286       C  
ATOM   4300  OG  SER B 261      42.414  22.738  15.570  1.00 28.84           O  
ANISOU 4300  OG  SER B 261     4011   3555   3389    -69    -44   -310       O  
ATOM   4301  N   THR B 262      45.491  23.142  14.150  1.00 29.87           N  
ANISOU 4301  N   THR B 262     4104   3698   3546    -67    -97   -291       N  
ATOM   4302  CA  THR B 262      46.901  23.159  14.528  1.00 29.79           C  
ANISOU 4302  CA  THR B 262     4094   3694   3530    -74   -123   -294       C  
ATOM   4303  C   THR B 262      47.202  24.384  15.384  1.00 29.81           C  
ANISOU 4303  C   THR B 262     4101   3684   3542    -89   -123   -321       C  
ATOM   4304  O   THR B 262      46.408  25.307  15.416  1.00 30.10           O  
ANISOU 4304  O   THR B 262     4136   3704   3597    -92   -101   -333       O  
ATOM   4305  CB  THR B 262      47.796  23.290  13.259  1.00 30.14           C  
ANISOU 4305  CB  THR B 262     4111   3739   3602    -64   -133   -272       C  
ATOM   4306  OG1 THR B 262      49.091  22.691  13.492  1.00 28.63           O  
ANISOU 4306  OG1 THR B 262     3918   3559   3398    -66   -159   -265       O  
ATOM   4307  CG2 THR B 262      47.939  24.755  12.873  1.00 27.49           C  
ANISOU 4307  CG2 THR B 262     3754   3384   3304    -68   -123   -278       C  
ATOM   4308  N   LEU B 263      48.348  24.394  16.065  1.00 27.51           N  
ANISOU 4308  N   LEU B 263     3814   3398   3239    -99   -149   -330       N  
ATOM   4309  CA  LEU B 263      48.618  25.486  16.979  1.00 28.77           C  
ANISOU 4309  CA  LEU B 263     3982   3545   3403   -116   -152   -358       C  
ATOM   4310  C   LEU B 263      48.892  26.736  16.132  1.00 27.86           C  
ANISOU 4310  C   LEU B 263     3838   3410   3335   -116   -144   -356       C  
ATOM   4311  O   LEU B 263      49.687  26.678  15.188  1.00 26.41           O  
ANISOU 4311  O   LEU B 263     3630   3229   3175   -108   -155   -335       O  
ATOM   4312  CB  LEU B 263      49.838  25.176  17.869  1.00 28.30           C  
ANISOU 4312  CB  LEU B 263     3933   3496   3320   -128   -187   -366       C  
ATOM   4313  CG  LEU B 263      50.248  26.258  18.878  1.00 30.22           C  
ANISOU 4313  CG  LEU B 263     4188   3728   3565   -149   -197   -398       C  
ATOM   4314  CD1 LEU B 263      49.163  26.526  19.936  1.00 29.88           C  
ANISOU 4314  CD1 LEU B 263     4179   3678   3495   -156   -176   -426       C  
ATOM   4315  CD2 LEU B 263      51.618  25.967  19.526  1.00 28.31           C  
ANISOU 4315  CD2 LEU B 263     3948   3498   3308   -161   -238   -400       C  
ATOM   4316  N   LEU B 264      48.177  27.817  16.422  1.00 28.70           N  
ANISOU 4316  N   LEU B 264     3948   3496   3458   -123   -121   -377       N  
ATOM   4317  CA  LEU B 264      48.462  29.129  15.820  1.00 30.09           C  
ANISOU 4317  CA  LEU B 264     4099   3652   3681   -125   -113   -379       C  
ATOM   4318  C   LEU B 264      49.613  29.838  16.561  1.00 30.66           C  
ANISOU 4318  C   LEU B 264     4172   3716   3759   -143   -137   -400       C  
ATOM   4319  O   LEU B 264      49.576  29.956  17.814  1.00 32.22           O  
ANISOU 4319  O   LEU B 264     4399   3913   3930   -159   -144   -429       O  
ATOM   4320  CB  LEU B 264      47.189  29.977  15.825  1.00 29.11           C  
ANISOU 4320  CB  LEU B 264     3978   3508   3575   -124    -76   -390       C  
ATOM   4321  CG  LEU B 264      46.174  29.192  14.960  1.00 30.75           C  
ANISOU 4321  CG  LEU B 264     4179   3725   3779   -106    -59   -364       C  
ATOM   4322  CD1 LEU B 264      44.951  30.011  14.624  1.00 30.33           C  
ANISOU 4322  CD1 LEU B 264     4118   3652   3754   -101    -24   -365       C  
ATOM   4323  CD2 LEU B 264      46.720  28.644  13.660  1.00 28.07           C  
ANISOU 4323  CD2 LEU B 264     3815   3397   3452    -91    -71   -331       C  
ATOM   4324  N   GLU B 265      50.647  30.231  15.810  1.00 30.65           N  
ANISOU 4324  N   GLU B 265     4142   3711   3792   -142   -151   -385       N  
ATOM   4325  CA  GLU B 265      51.787  30.970  16.365  1.00 33.10           C  
ANISOU 4325  CA  GLU B 265     4446   4011   4118   -160   -176   -402       C  
ATOM   4326  C   GLU B 265      51.900  32.367  15.744  1.00 34.12           C  
ANISOU 4326  C   GLU B 265     4548   4113   4301   -162   -159   -404       C  
ATOM   4327  O   GLU B 265      52.933  32.728  15.175  1.00 34.59           O  
ANISOU 4327  O   GLU B 265     4580   4167   4393   -162   -174   -390       O  
ATOM   4328  CB  GLU B 265      53.103  30.208  16.204  1.00 35.22           C  
ANISOU 4328  CB  GLU B 265     4702   4297   4382   -159   -210   -382       C  
ATOM   4329  CG  GLU B 265      53.086  28.799  16.802  1.00 38.12           C  
ANISOU 4329  CG  GLU B 265     5094   4691   4699   -157   -227   -377       C  
ATOM   4330  CD  GLU B 265      54.459  28.133  16.797  1.00 43.33           C  
ANISOU 4330  CD  GLU B 265     5740   5364   5356   -158   -263   -359       C  
ATOM   4331  OE1 GLU B 265      54.859  27.663  15.707  1.00 44.96           O  
ANISOU 4331  OE1 GLU B 265     5923   5576   5581   -142   -260   -327       O  
ATOM   4332  OE2 GLU B 265      55.158  28.108  17.866  1.00 43.42           O  
ANISOU 4332  OE2 GLU B 265     5765   5381   5349   -176   -293   -376       O  
ATOM   4333  N   GLY B 266      50.822  33.139  15.858  1.00 33.99           N  
ANISOU 4333  N   GLY B 266     4540   4079   4295   -163   -128   -420       N  
ATOM   4334  CA  GLY B 266      50.743  34.458  15.225  1.00 34.49           C  
ANISOU 4334  CA  GLY B 266     4578   4115   4411   -162   -107   -420       C  
ATOM   4335  C   GLY B 266      49.915  34.489  13.936  1.00 33.71           C  
ANISOU 4335  C   GLY B 266     4457   4014   4336   -140    -77   -390       C  
ATOM   4336  O   GLY B 266      49.440  35.558  13.541  1.00 32.40           O  
ANISOU 4336  O   GLY B 266     4275   3825   4208   -138    -51   -391       O  
ATOM   4337  N   GLN B 267      49.747  33.358  13.256  1.00 32.23           N  
ANISOU 4337  N   GLN B 267     4267   3850   4128   -124    -80   -362       N  
ATOM   4338  CA  GLN B 267      48.989  33.391  11.942  1.00 33.20           C  
ANISOU 4338  CA  GLN B 267     4370   3972   4273   -103    -55   -332       C  
ATOM   4339  C   GLN B 267      47.576  33.938  12.177  1.00 33.25           C  
ANISOU 4339  C   GLN B 267     4385   3964   4284   -103    -23   -344       C  
ATOM   4340  O   GLN B 267      46.960  33.669  13.227  1.00 34.23           O  
ANISOU 4340  O   GLN B 267     4537   4088   4378   -112    -19   -368       O  
ATOM   4341  CB  GLN B 267      48.788  31.993  11.334  1.00 33.12           C  
ANISOU 4341  CB  GLN B 267     4364   3987   4231    -88    -63   -306       C  
ATOM   4342  CG  GLN B 267      50.034  31.243  10.946  1.00 31.73           C  
ANISOU 4342  CG  GLN B 267     4179   3828   4049    -83    -90   -288       C  
ATOM   4343  CD  GLN B 267      50.750  30.613  12.134  1.00 32.60           C  
ANISOU 4343  CD  GLN B 267     4310   3949   4125    -98   -118   -307       C  
ATOM   4344  OE1 GLN B 267      50.353  30.754  13.348  1.00 32.91           O  
ANISOU 4344  OE1 GLN B 267     4375   3986   4143   -113   -120   -337       O  
ATOM   4345  NE2 GLN B 267      51.833  29.899  11.807  1.00 29.06           N  
ANISOU 4345  NE2 GLN B 267     3853   3515   3672    -93   -141   -288       N  
ATOM   4346  N   TYR B 268      47.044  34.691  11.222  1.00 34.13           N  
ANISOU 4346  N   TYR B 268     4472   4061   4434    -92      0   -326       N  
ATOM   4347  CA  TYR B 268      45.658  35.233  11.335  1.00 34.81           C  
ANISOU 4347  CA  TYR B 268     4561   4131   4531    -89     33   -332       C  
ATOM   4348  C   TYR B 268      45.578  36.229  12.498  1.00 34.50           C  
ANISOU 4348  C   TYR B 268     4538   4068   4502   -107     45   -370       C  
ATOM   4349  O   TYR B 268      44.498  36.684  12.901  1.00 35.03           O  
ANISOU 4349  O   TYR B 268     4613   4120   4574   -108     74   -382       O  
ATOM   4350  CB  TYR B 268      44.642  34.075  11.552  1.00 32.66           C  
ANISOU 4350  CB  TYR B 268     4311   3878   4220    -83     37   -328       C  
ATOM   4351  CG  TYR B 268      44.671  33.137  10.402  1.00 31.09           C  
ANISOU 4351  CG  TYR B 268     4100   3701   4012    -66     26   -294       C  
ATOM   4352  CD1 TYR B 268      44.278  33.567   9.140  1.00 30.77           C  
ANISOU 4352  CD1 TYR B 268     4032   3655   4003    -52     40   -265       C  
ATOM   4353  CD2 TYR B 268      45.112  31.819  10.556  1.00 30.57           C  
ANISOU 4353  CD2 TYR B 268     4050   3659   3906    -65      1   -289       C  
ATOM   4354  CE1 TYR B 268      44.329  32.707   8.058  1.00 31.49           C  
ANISOU 4354  CE1 TYR B 268     4115   3766   4083    -37     29   -236       C  
ATOM   4355  CE2 TYR B 268      45.183  30.968   9.491  1.00 28.75           C  
ANISOU 4355  CE2 TYR B 268     3809   3445   3667    -50     -7   -260       C  
ATOM   4356  CZ  TYR B 268      44.778  31.406   8.243  1.00 30.15           C  
ANISOU 4356  CZ  TYR B 268     3962   3618   3873    -36      6   -234       C  
ATOM   4357  OH  TYR B 268      44.837  30.611   7.150  1.00 29.04           O  
ANISOU 4357  OH  TYR B 268     3816   3495   3723    -21     -2   -207       O  
ATOM   4358  N   GLY B 269      46.743  36.518  13.055  1.00 35.13           N  
ANISOU 4358  N   GLY B 269     4621   4144   4582   -122     22   -389       N  
ATOM   4359  CA  GLY B 269      46.880  37.343  14.242  1.00 34.40           C  
ANISOU 4359  CA  GLY B 269     4548   4031   4491   -142     25   -428       C  
ATOM   4360  C   GLY B 269      46.583  36.642  15.548  1.00 35.52           C  
ANISOU 4360  C   GLY B 269     4731   4184   4580   -153     17   -456       C  
ATOM   4361  O   GLY B 269      46.344  37.320  16.531  1.00 37.78           O  
ANISOU 4361  O   GLY B 269     5038   4451   4862   -167     28   -489       O  
ATOM   4362  N   HIS B 270      46.642  35.308  15.607  1.00 34.74           N  
ANISOU 4362  N   HIS B 270     4645   4115   4439   -147     -2   -443       N  
ATOM   4363  CA  HIS B 270      46.335  34.610  16.872  1.00 35.61           C  
ANISOU 4363  CA  HIS B 270     4794   4236   4498   -156     -8   -467       C  
ATOM   4364  C   HIS B 270      47.419  33.744  17.361  1.00 36.49           C  
ANISOU 4364  C   HIS B 270     4918   4370   4575   -164    -48   -470       C  
ATOM   4365  O   HIS B 270      48.131  33.152  16.556  1.00 37.32           O  
ANISOU 4365  O   HIS B 270     5003   4491   4686   -156    -68   -442       O  
ATOM   4366  CB  HIS B 270      45.106  33.751  16.697  1.00 36.75           C  
ANISOU 4366  CB  HIS B 270     4949   4393   4622   -142     12   -451       C  
ATOM   4367  CG  HIS B 270      43.850  34.547  16.466  1.00 37.98           C  
ANISOU 4367  CG  HIS B 270     5097   4525   4807   -135     54   -451       C  
ATOM   4368  ND1 HIS B 270      43.169  35.109  17.469  1.00 36.43           N  
ANISOU 4368  ND1 HIS B 270     4925   4311   4603   -144     78   -480       N  
ATOM   4369  CD2 HIS B 270      43.179  34.876  15.286  1.00 38.22           C  
ANISOU 4369  CD2 HIS B 270     5097   4548   4875   -120     75   -423       C  
ATOM   4370  CE1 HIS B 270      42.114  35.750  16.979  1.00 40.12           C  
ANISOU 4370  CE1 HIS B 270     5378   4760   5106   -134    115   -470       C  
ATOM   4371  NE2 HIS B 270      42.121  35.607  15.631  1.00 41.73           N  
ANISOU 4371  NE2 HIS B 270     5547   4971   5337   -120    111   -435       N  
ATOM   4372  N   SER B 271      47.525  33.628  18.686  1.00 37.48           N  
ANISOU 4372  N   SER B 271     5079   4498   4663   -180    -59   -500       N  
ATOM   4373  CA  SER B 271      48.538  32.826  19.348  1.00 39.98           C  
ANISOU 4373  CA  SER B 271     5411   4837   4943   -189    -99   -505       C  
ATOM   4374  C   SER B 271      47.965  31.948  20.467  1.00 39.97           C  
ANISOU 4374  C   SER B 271     5450   4851   4884   -192    -99   -519       C  
ATOM   4375  O   SER B 271      46.886  32.237  20.951  1.00 38.45           O  
ANISOU 4375  O   SER B 271     5278   4646   4682   -191    -67   -535       O  
ATOM   4376  CB  SER B 271      49.588  33.750  19.948  1.00 41.59           C  
ANISOU 4376  CB  SER B 271     5615   5026   5159   -210   -123   -531       C  
ATOM   4377  OG  SER B 271      50.588  33.944  18.974  1.00 45.20           O  
ANISOU 4377  OG  SER B 271     6034   5483   5655   -207   -141   -508       O  
ATOM   4378  N   ASP B 272      48.671  30.867  20.841  1.00 40.85           N  
ANISOU 4378  N   ASP B 272     5572   4988   4959   -193   -132   -511       N  
ATOM   4379  CA  ASP B 272      48.388  30.103  22.098  1.00 43.53           C  
ANISOU 4379  CA  ASP B 272     5953   5343   5242   -199   -138   -527       C  
ATOM   4380  C   ASP B 272      47.009  29.460  22.041  1.00 38.12           C  
ANISOU 4380  C   ASP B 272     5280   4661   4540   -184   -103   -517       C  
ATOM   4381  O   ASP B 272      46.364  29.190  23.077  1.00 34.67           O  
ANISOU 4381  O   ASP B 272     4880   4227   4065   -187    -91   -534       O  
ATOM   4382  CB  ASP B 272      48.450  31.004  23.341  1.00 50.79           C  
ANISOU 4382  CB  ASP B 272     6905   6247   6145   -219   -139   -569       C  
ATOM   4383  CG  ASP B 272      49.789  31.750  23.486  1.00 64.42           C  
ANISOU 4383  CG  ASP B 272     8619   7966   7889   -238   -175   -583       C  
ATOM   4384  OD1 ASP B 272      50.846  31.086  23.653  1.00 68.55           O  
ANISOU 4384  OD1 ASP B 272     9139   8510   8397   -243   -216   -573       O  
ATOM   4385  OD2 ASP B 272      49.783  33.019  23.471  1.00 75.33           O  
ANISOU 4385  OD2 ASP B 272     9995   9321   9304   -248   -163   -605       O  
ATOM   4386  N   ILE B 273      46.568  29.242  20.807  1.00 34.60           N  
ANISOU 4386  N   ILE B 273     4805   4215   4125   -167    -88   -487       N  
ATOM   4387  CA  ILE B 273      45.277  28.649  20.538  1.00 34.28           C  
ANISOU 4387  CA  ILE B 273     4768   4177   4079   -153    -58   -473       C  
ATOM   4388  C   ILE B 273      45.393  27.742  19.331  1.00 31.44           C  
ANISOU 4388  C   ILE B 273     4381   3832   3730   -137    -67   -436       C  
ATOM   4389  O   ILE B 273      46.341  27.930  18.542  1.00 30.64           O  
ANISOU 4389  O   ILE B 273     4254   3733   3653   -136    -87   -423       O  
ATOM   4390  CB  ILE B 273      44.198  29.731  20.352  1.00 34.74           C  
ANISOU 4390  CB  ILE B 273     4821   4208   4170   -150    -17   -483       C  
ATOM   4391  CG1 ILE B 273      42.822  29.211  20.813  1.00 35.93           C  
ANISOU 4391  CG1 ILE B 273     4993   4358   4300   -142     14   -482       C  
ATOM   4392  CG2 ILE B 273      44.212  30.256  18.934  1.00 32.50           C  
ANISOU 4392  CG2 ILE B 273     4497   3915   3936   -141    -10   -459       C  
ATOM   4393  CD1 ILE B 273      42.754  28.980  22.316  1.00 35.77           C  
ANISOU 4393  CD1 ILE B 273     5016   4342   4232   -153     15   -509       C  
ATOM   4394  N   PHE B 274      44.522  26.717  19.231  1.00 28.55           N  
ANISOU 4394  N   PHE B 274     4023   3477   3345   -126    -54   -420       N  
ATOM   4395  CA  PHE B 274      44.502  25.889  18.002  1.00 26.69           C  
ANISOU 4395  CA  PHE B 274     3764   3255   3122   -111    -60   -387       C  
ATOM   4396  C   PHE B 274      43.441  26.361  17.052  1.00 25.02           C  
ANISOU 4396  C   PHE B 274     3531   3028   2945   -100    -31   -374       C  
ATOM   4397  O   PHE B 274      42.384  26.809  17.497  1.00 24.24           O  
ANISOU 4397  O   PHE B 274     3443   2916   2851   -101     -3   -385       O  
ATOM   4398  CB  PHE B 274      44.331  24.365  18.277  1.00 25.98           C  
ANISOU 4398  CB  PHE B 274     3689   3186   2995   -104    -70   -373       C  
ATOM   4399  CG  PHE B 274      45.597  23.690  18.680  1.00 26.75           C  
ANISOU 4399  CG  PHE B 274     3794   3302   3067   -109   -104   -371       C  
ATOM   4400  CD1 PHE B 274      46.226  24.030  19.885  1.00 27.16           C  
ANISOU 4400  CD1 PHE B 274     3867   3355   3095   -124   -120   -396       C  
ATOM   4401  CD2 PHE B 274      46.124  22.695  17.922  1.00 26.18           C  
ANISOU 4401  CD2 PHE B 274     3708   3245   2993    -99   -121   -346       C  
ATOM   4402  CE1 PHE B 274      47.387  23.417  20.276  1.00 27.47           C  
ANISOU 4402  CE1 PHE B 274     3912   3412   3113   -129   -154   -391       C  
ATOM   4403  CE2 PHE B 274      47.284  22.064  18.305  1.00 27.28           C  
ANISOU 4403  CE2 PHE B 274     3852   3400   3112   -103   -152   -341       C  
ATOM   4404  CZ  PHE B 274      47.930  22.432  19.489  1.00 27.53           C  
ANISOU 4404  CZ  PHE B 274     3902   3433   3123   -118   -169   -363       C  
ATOM   4405  N   GLY B 275      43.631  26.180  15.734  1.00 24.49           N  
ANISOU 4405  N   GLY B 275     3436   2965   2901    -89    -37   -348       N  
ATOM   4406  CA  GLY B 275      42.529  26.535  14.885  1.00 23.27           C  
ANISOU 4406  CA  GLY B 275     3265   2800   2776    -79    -12   -334       C  
ATOM   4407  C   GLY B 275      42.678  26.027  13.484  1.00 23.31           C  
ANISOU 4407  C   GLY B 275     3246   2814   2794    -66    -22   -304       C  
ATOM   4408  O   GLY B 275      43.778  25.606  13.077  1.00 24.52           O  
ANISOU 4408  O   GLY B 275     3394   2979   2942    -64    -45   -294       O  
ATOM   4409  N   GLY B 276      41.581  26.027  12.745  1.00 22.33           N  
ANISOU 4409  N   GLY B 276     3110   2685   2688    -57     -4   -288       N  
ATOM   4410  CA  GLY B 276      41.546  25.264  11.497  1.00 23.46           C  
ANISOU 4410  CA  GLY B 276     3239   2840   2834    -44    -14   -261       C  
ATOM   4411  C   GLY B 276      42.260  26.075  10.479  1.00 23.30           C  
ANISOU 4411  C   GLY B 276     3194   2814   2842    -39    -18   -249       C  
ATOM   4412  O   GLY B 276      41.901  27.203  10.282  1.00 23.74           O  
ANISOU 4412  O   GLY B 276     3235   2853   2929    -40     -1   -251       O  
ATOM   4413  N   THR B 277      43.340  25.548   9.913  1.00 26.31           N  
ANISOU 4413  N   THR B 277     3571   3209   3216    -34    -40   -237       N  
ATOM   4414  CA  THR B 277      43.923  26.095   8.648  1.00 27.39           C  
ANISOU 4414  CA  THR B 277     3683   3343   3380    -24    -42   -217       C  
ATOM   4415  C   THR B 277      44.599  25.025   7.774  1.00 29.18           C  
ANISOU 4415  C   THR B 277     3910   3587   3590    -13    -59   -196       C  
ATOM   4416  O   THR B 277      44.904  23.915   8.234  1.00 27.72           O  
ANISOU 4416  O   THR B 277     3742   3415   3375    -14    -73   -199       O  
ATOM   4417  CB  THR B 277      44.939  27.215   8.957  1.00 29.75           C  
ANISOU 4417  CB  THR B 277     3971   3629   3701    -31    -44   -228       C  
ATOM   4418  OG1 THR B 277      45.411  27.852   7.752  1.00 30.20           O  
ANISOU 4418  OG1 THR B 277     4002   3681   3789    -21    -41   -208       O  
ATOM   4419  CG2 THR B 277      46.095  26.720   9.824  1.00 30.51           C  
ANISOU 4419  CG2 THR B 277     4081   3735   3776    -41    -66   -241       C  
ATOM   4420  N   PRO B 278      44.804  25.332   6.482  1.00 28.18           N  
ANISOU 4420  N   PRO B 278     3764   3459   3483      0    -57   -174       N  
ATOM   4421  CA  PRO B 278      45.544  24.324   5.738  1.00 27.70           C  
ANISOU 4421  CA  PRO B 278     3706   3412   3404      9    -72   -157       C  
ATOM   4422  C   PRO B 278      46.977  24.121   6.251  1.00 26.12           C  
ANISOU 4422  C   PRO B 278     3508   3216   3198      6    -87   -162       C  
ATOM   4423  O   PRO B 278      47.666  25.074   6.537  1.00 24.73           O  
ANISOU 4423  O   PRO B 278     3320   3030   3044      0    -87   -168       O  
ATOM   4424  CB  PRO B 278      45.550  24.846   4.273  1.00 26.98           C  
ANISOU 4424  CB  PRO B 278     3596   3318   3335     24    -64   -133       C  
ATOM   4425  CG  PRO B 278      44.814  26.185   4.266  1.00 28.12           C  
ANISOU 4425  CG  PRO B 278     3724   3446   3512     20    -46   -136       C  
ATOM   4426  CD  PRO B 278      44.213  26.403   5.639  1.00 28.51           C  
ANISOU 4426  CD  PRO B 278     3785   3488   3558      5    -40   -162       C  
ATOM   4427  N   VAL B 279      47.403  22.858   6.329  1.00 24.78           N  
ANISOU 4427  N   VAL B 279     3353   3061   3001      9   -101   -157       N  
ATOM   4428  CA  VAL B 279      48.766  22.514   6.613  1.00 24.51           C  
ANISOU 4428  CA  VAL B 279     3318   3032   2962      9   -116   -154       C  
ATOM   4429  C   VAL B 279      49.257  21.517   5.617  1.00 25.73           C  
ANISOU 4429  C   VAL B 279     3473   3196   3105     24   -121   -132       C  
ATOM   4430  O   VAL B 279      48.464  21.031   4.832  1.00 27.86           O  
ANISOU 4430  O   VAL B 279     3749   3469   3365     33   -114   -123       O  
ATOM   4431  CB  VAL B 279      48.890  21.841   7.965  1.00 24.96           C  
ANISOU 4431  CB  VAL B 279     3394   3096   2992     -3   -129   -172       C  
ATOM   4432  CG1 VAL B 279      48.391  22.764   9.039  1.00 24.28           C  
ANISOU 4432  CG1 VAL B 279     3313   3001   2912    -18   -124   -197       C  
ATOM   4433  CG2 VAL B 279      48.144  20.510   7.975  1.00 26.52           C  
ANISOU 4433  CG2 VAL B 279     3611   3305   3159      1   -130   -168       C  
ATOM   4434  N   VAL B 280      50.558  21.215   5.615  1.00 24.90           N  
ANISOU 4434  N   VAL B 280     3363   3094   3002     28   -131   -123       N  
ATOM   4435  CA  VAL B 280      51.074  20.206   4.725  1.00 24.26           C  
ANISOU 4435  CA  VAL B 280     3285   3021   2909     43   -133   -102       C  
ATOM   4436  C   VAL B 280      51.477  19.116   5.649  1.00 24.74           C  
ANISOU 4436  C   VAL B 280     3362   3092   2946     38   -147   -108       C  
ATOM   4437  O   VAL B 280      52.282  19.389   6.552  1.00 27.83           O  
ANISOU 4437  O   VAL B 280     3748   3482   3342     28   -160   -115       O  
ATOM   4438  CB  VAL B 280      52.358  20.624   3.991  1.00 23.41           C  
ANISOU 4438  CB  VAL B 280     3158   2908   2826     54   -131    -83       C  
ATOM   4439  CG1 VAL B 280      52.833  19.492   3.128  1.00 22.88           C  
ANISOU 4439  CG1 VAL B 280     3100   2849   2745     71   -129    -63       C  
ATOM   4440  CG2 VAL B 280      52.160  21.854   3.182  1.00 22.92           C  
ANISOU 4440  CG2 VAL B 280     3078   2835   2794     59   -117    -76       C  
ATOM   4441  N   LEU B 281      50.902  17.943   5.461  1.00 23.91           N  
ANISOU 4441  N   LEU B 281     3275   2995   2815     43   -147   -105       N  
ATOM   4442  CA  LEU B 281      51.228  16.731   6.204  1.00 24.93           C  
ANISOU 4442  CA  LEU B 281     3420   3133   2919     41   -158   -106       C  
ATOM   4443  C   LEU B 281      52.166  15.733   5.571  1.00 24.67           C  
ANISOU 4443  C   LEU B 281     3387   3104   2880     55   -160    -86       C  
ATOM   4444  O   LEU B 281      51.968  15.242   4.486  1.00 23.52           O  
ANISOU 4444  O   LEU B 281     3247   2958   2730     69   -150    -74       O  
ATOM   4445  CB  LEU B 281      49.976  15.978   6.623  1.00 25.88           C  
ANISOU 4445  CB  LEU B 281     3560   3258   3014     36   -156   -117       C  
ATOM   4446  CG  LEU B 281      49.195  16.474   7.824  1.00 28.73           C  
ANISOU 4446  CG  LEU B 281     3927   3617   3369     20   -156   -139       C  
ATOM   4447  CD1 LEU B 281      48.097  15.449   8.083  1.00 28.99           C  
ANISOU 4447  CD1 LEU B 281     3979   3654   3379     19   -152   -143       C  
ATOM   4448  CD2 LEU B 281      50.083  16.637   9.090  1.00 29.39           C  
ANISOU 4448  CD2 LEU B 281     4012   3704   3448      9   -171   -148       C  
ATOM   4449  N   GLY B 282      53.231  15.413   6.308  1.00 26.93           N  
ANISOU 4449  N   GLY B 282     3671   3394   3167     52   -173    -82       N  
ATOM   4450  CA  GLY B 282      54.212  14.434   5.805  1.00 27.49           C  
ANISOU 4450  CA  GLY B 282     3740   3467   3234     66   -173    -61       C  
ATOM   4451  C   GLY B 282      54.948  13.822   6.944  1.00 28.01           C  
ANISOU 4451  C   GLY B 282     3809   3540   3292     58   -190    -61       C  
ATOM   4452  O   GLY B 282      54.511  13.962   8.117  1.00 28.29           O  
ANISOU 4452  O   GLY B 282     3852   3580   3314     43   -201    -78       O  
ATOM   4453  N   ALA B 283      56.064  13.179   6.599  1.00 27.71           N  
ANISOU 4453  N   ALA B 283     3764   3503   3262     70   -191    -39       N  
ATOM   4454  CA  ALA B 283      56.787  12.333   7.496  1.00 30.93           C  
ANISOU 4454  CA  ALA B 283     4173   3917   3659     67   -206    -33       C  
ATOM   4455  C   ALA B 283      57.203  13.045   8.791  1.00 31.91           C  
ANISOU 4455  C   ALA B 283     4289   4046   3788     48   -228    -44       C  
ATOM   4456  O   ALA B 283      57.274  12.440   9.821  1.00 34.73           O  
ANISOU 4456  O   ALA B 283     4656   4412   4126     41   -242    -48       O  
ATOM   4457  CB  ALA B 283      57.991  11.746   6.776  1.00 34.39           C  
ANISOU 4457  CB  ALA B 283     4600   4352   4114     84   -200     -5       C  
ATOM   4458  N   ASN B 284      57.412  14.353   8.732  1.00 34.09           N  
ANISOU 4458  N   ASN B 284     4548   4315   4088     41   -231    -52       N  
ATOM   4459  CA  ASN B 284      57.778  15.193   9.868  1.00 34.98           C  
ANISOU 4459  CA  ASN B 284     4654   4430   4207     22   -252    -66       C  
ATOM   4460  C   ASN B 284      56.559  15.777  10.548  1.00 32.56           C  
ANISOU 4460  C   ASN B 284     4363   4123   3882      8   -250    -95       C  
ATOM   4461  O   ASN B 284      56.657  16.837  11.169  1.00 31.96           O  
ANISOU 4461  O   ASN B 284     4282   4043   3818     -6   -260   -112       O  
ATOM   4462  CB  ASN B 284      58.528  16.438   9.347  1.00 38.30           C  
ANISOU 4462  CB  ASN B 284     5046   4837   4666     21   -252    -61       C  
ATOM   4463  CG  ASN B 284      60.035  16.299   9.362  1.00 45.97           C  
ANISOU 4463  CG  ASN B 284     5995   5808   5663     24   -266    -38       C  
ATOM   4464  OD1 ASN B 284      60.602  15.188   9.338  1.00 45.34           O  
ANISOU 4464  OD1 ASN B 284     5917   5734   5575     34   -269    -18       O  
ATOM   4465  ND2 ASN B 284      60.715  17.465   9.375  1.00 49.59           N  
ANISOU 4465  ND2 ASN B 284     6429   6256   6155     16   -274    -39       N  
ATOM   4466  N   GLY B 285      55.390  15.182  10.346  1.00 34.55           N  
ANISOU 4466  N   GLY B 285     4636   4378   4112     12   -235   -102       N  
ATOM   4467  CA  GLY B 285      54.147  15.709  10.928  1.00 29.78           C  
ANISOU 4467  CA  GLY B 285     4046   3773   3494      0   -229   -127       C  
ATOM   4468  C   GLY B 285      53.677  16.913  10.166  1.00 28.74           C  
ANISOU 4468  C   GLY B 285     3902   3628   3387      1   -215   -133       C  
ATOM   4469  O   GLY B 285      53.597  16.884   8.916  1.00 26.51           O  
ANISOU 4469  O   GLY B 285     3612   3342   3119     15   -201   -118       O  
ATOM   4470  N   VAL B 286      53.301  17.952  10.924  1.00 26.93           N  
ANISOU 4470  N   VAL B 286     3673   3394   3162    -13   -217   -155       N  
ATOM   4471  CA  VAL B 286      52.953  19.245  10.299  1.00 27.28           C  
ANISOU 4471  CA  VAL B 286     3704   3425   3236    -14   -203   -161       C  
ATOM   4472  C   VAL B 286      54.179  19.890   9.659  1.00 27.86           C  
ANISOU 4472  C   VAL B 286     3750   3491   3343     -9   -208   -146       C  
ATOM   4473  O   VAL B 286      55.040  20.365  10.396  1.00 28.90           O  
ANISOU 4473  O   VAL B 286     3874   3621   3485    -21   -226   -152       O  
ATOM   4474  CB  VAL B 286      52.327  20.189  11.323  1.00 25.13           C  
ANISOU 4474  CB  VAL B 286     3439   3146   2961    -31   -202   -189       C  
ATOM   4475  CG1 VAL B 286      52.172  21.604  10.783  1.00 26.84           C  
ANISOU 4475  CG1 VAL B 286     3638   3346   3213    -33   -190   -194       C  
ATOM   4476  CG2 VAL B 286      50.990  19.671  11.773  1.00 22.83           C  
ANISOU 4476  CG2 VAL B 286     3171   2859   2643    -33   -190   -200       C  
ATOM   4477  N   GLU B 287      54.285  19.892   8.321  1.00 27.06           N  
ANISOU 4477  N   GLU B 287     3636   3385   3258      6   -194   -125       N  
ATOM   4478  CA  GLU B 287      55.521  20.380   7.673  1.00 28.84           C  
ANISOU 4478  CA  GLU B 287     3836   3604   3517     13   -196   -106       C  
ATOM   4479  C   GLU B 287      55.519  21.857   7.349  1.00 29.30           C  
ANISOU 4479  C   GLU B 287     3875   3647   3611      9   -187   -111       C  
ATOM   4480  O   GLU B 287      56.581  22.476   7.201  1.00 28.98           O  
ANISOU 4480  O   GLU B 287     3811   3598   3601      8   -193   -102       O  
ATOM   4481  CB  GLU B 287      55.881  19.577   6.413  1.00 31.56           C  
ANISOU 4481  CB  GLU B 287     4177   3950   3862     35   -184    -79       C  
ATOM   4482  CG  GLU B 287      55.817  18.057   6.644  1.00 35.22           C  
ANISOU 4482  CG  GLU B 287     4661   4426   4292     41   -189    -73       C  
ATOM   4483  CD  GLU B 287      57.080  17.305   6.251  1.00 37.35           C  
ANISOU 4483  CD  GLU B 287     4922   4698   4570     54   -193    -48       C  
ATOM   4484  OE1 GLU B 287      58.094  17.981   5.968  1.00 47.48           O  
ANISOU 4484  OE1 GLU B 287     6181   5973   5885     56   -194    -35       O  
ATOM   4485  OE2 GLU B 287      57.119  16.034   6.318  1.00 38.47           O  
ANISOU 4485  OE2 GLU B 287     5079   4848   4689     60   -194    -41       O  
ATOM   4486  N   GLN B 288      54.334  22.427   7.184  1.00 29.80           N  
ANISOU 4486  N   GLN B 288     3944   3704   3672      7   -172   -124       N  
ATOM   4487  CA  GLN B 288      54.142  23.879   6.886  1.00 28.88           C  
ANISOU 4487  CA  GLN B 288     3810   3572   3591      3   -160   -130       C  
ATOM   4488  C   GLN B 288      52.681  24.148   7.280  1.00 29.51           C  
ANISOU 4488  C   GLN B 288     3905   3650   3656     -3   -148   -150       C  
ATOM   4489  O   GLN B 288      51.795  23.228   7.244  1.00 28.60           O  
ANISOU 4489  O   GLN B 288     3809   3544   3511      1   -144   -150       O  
ATOM   4490  CB  GLN B 288      54.243  24.217   5.378  1.00 29.68           C  
ANISOU 4490  CB  GLN B 288     3893   3667   3715     23   -141   -104       C  
ATOM   4491  CG  GLN B 288      55.386  23.636   4.545  1.00 30.43           C  
ANISOU 4491  CG  GLN B 288     3977   3765   3819     39   -142    -76       C  
ATOM   4492  CD  GLN B 288      55.134  23.860   3.046  1.00 32.52           C  
ANISOU 4492  CD  GLN B 288     4234   4026   4095     59   -119    -53       C  
ATOM   4493  OE1 GLN B 288      54.551  24.860   2.661  1.00 31.54           O  
ANISOU 4493  OE1 GLN B 288     4099   3892   3990     59   -106    -54       O  
ATOM   4494  NE2 GLN B 288      55.523  22.887   2.215  1.00 32.61           N  
ANISOU 4494  NE2 GLN B 288     4251   4045   4092     77   -115    -31       N  
ATOM   4495  N   VAL B 289      52.420  25.393   7.631  1.00 29.02           N  
ANISOU 4495  N   VAL B 289     3834   3573   3617    -14   -142   -166       N  
ATOM   4496  CA  VAL B 289      51.100  25.845   8.097  1.00 28.73           C  
ANISOU 4496  CA  VAL B 289     3809   3530   3574    -22   -128   -186       C  
ATOM   4497  C   VAL B 289      50.878  26.891   7.089  1.00 29.48           C  
ANISOU 4497  C   VAL B 289     3882   3612   3705    -13   -109   -173       C  
ATOM   4498  O   VAL B 289      51.665  27.815   7.048  1.00 31.82           O  
ANISOU 4498  O   VAL B 289     4160   3896   4034    -17   -110   -173       O  
ATOM   4499  CB  VAL B 289      51.195  26.470   9.503  1.00 27.19           C  
ANISOU 4499  CB  VAL B 289     3624   3328   3378    -43   -137   -216       C  
ATOM   4500  CG1 VAL B 289      49.891  27.116   9.914  1.00 25.25           C  
ANISOU 4500  CG1 VAL B 289     3388   3072   3132    -49   -117   -235       C  
ATOM   4501  CG2 VAL B 289      51.557  25.377  10.510  1.00 26.79           C  
ANISOU 4501  CG2 VAL B 289     3595   3293   3288    -50   -158   -225       C  
ATOM   4502  N   ILE B 290      49.874  26.724   6.232  1.00 29.02           N  
ANISOU 4502  N   ILE B 290     3826   3556   3644     -1    -93   -161       N  
ATOM   4503  CA  ILE B 290      49.582  27.738   5.243  1.00 29.53           C  
ANISOU 4503  CA  ILE B 290     3869   3609   3743      7    -75   -147       C  
ATOM   4504  C   ILE B 290      48.557  28.761   5.782  1.00 30.42           C  
ANISOU 4504  C   ILE B 290     3980   3706   3872     -3    -59   -165       C  
ATOM   4505  O   ILE B 290      47.493  28.384   6.286  1.00 31.68           O  
ANISOU 4505  O   ILE B 290     4157   3869   4011     -7    -54   -177       O  
ATOM   4506  CB  ILE B 290      49.134  27.083   3.961  1.00 29.80           C  
ANISOU 4506  CB  ILE B 290     3904   3653   3766     26    -68   -121       C  
ATOM   4507  CG1 ILE B 290      50.253  26.120   3.577  1.00 30.46           C  
ANISOU 4507  CG1 ILE B 290     3989   3748   3834     35    -82   -106       C  
ATOM   4508  CG2 ILE B 290      48.894  28.147   2.855  1.00 29.29           C  
ANISOU 4508  CG2 ILE B 290     3816   3576   3735     37    -50   -102       C  
ATOM   4509  CD1 ILE B 290      49.940  25.285   2.386  1.00 30.52           C  
ANISOU 4509  CD1 ILE B 290     4004   3767   3824     53    -78    -84       C  
ATOM   4510  N   GLU B 291      48.909  30.037   5.748  1.00 31.09           N  
ANISOU 4510  N   GLU B 291     4045   3772   3994     -7    -50   -168       N  
ATOM   4511  CA  GLU B 291      48.026  31.096   6.277  1.00 30.76           C  
ANISOU 4511  CA  GLU B 291     4001   3712   3973    -16    -32   -187       C  
ATOM   4512  C   GLU B 291      47.406  31.776   5.081  1.00 30.28           C  
ANISOU 4512  C   GLU B 291     3919   3643   3941     -2    -11   -163       C  
ATOM   4513  O   GLU B 291      48.129  32.332   4.245  1.00 31.08           O  
ANISOU 4513  O   GLU B 291     3999   3739   4070      6     -7   -144       O  
ATOM   4514  CB  GLU B 291      48.800  32.115   7.101  1.00 32.72           C  
ANISOU 4514  CB  GLU B 291     4242   3942   4246    -32    -35   -208       C  
ATOM   4515  CG  GLU B 291      47.943  33.340   7.439  1.00 35.34           C  
ANISOU 4515  CG  GLU B 291     4569   4251   4606    -40    -11   -224       C  
ATOM   4516  CD  GLU B 291      48.583  34.325   8.405  1.00 38.75           C  
ANISOU 4516  CD  GLU B 291     4999   4663   5059    -58    -14   -252       C  
ATOM   4517  OE1 GLU B 291      49.768  34.163   8.778  1.00 40.99           O  
ANISOU 4517  OE1 GLU B 291     5282   4950   5340    -67    -37   -258       O  
ATOM   4518  OE2 GLU B 291      47.884  35.293   8.803  1.00 40.52           O  
ANISOU 4518  OE2 GLU B 291     5223   4867   5305    -65      6   -269       O  
ATOM   4519  N   LEU B 292      46.084  31.673   4.957  1.00 29.17           N  
ANISOU 4519  N   LEU B 292     3785   3504   3794      0      1   -161       N  
ATOM   4520  CA  LEU B 292      45.386  32.169   3.775  1.00 28.38           C  
ANISOU 4520  CA  LEU B 292     3666   3400   3717     15     18   -135       C  
ATOM   4521  C   LEU B 292      45.387  33.689   3.919  1.00 28.39           C  
ANISOU 4521  C   LEU B 292     3647   3376   3764     10     38   -141       C  
ATOM   4522  O   LEU B 292      45.400  34.170   5.038  1.00 28.09           O  
ANISOU 4522  O   LEU B 292     3616   3324   3731     -5     41   -169       O  
ATOM   4523  CB  LEU B 292      43.971  31.644   3.750  1.00 28.20           C  
ANISOU 4523  CB  LEU B 292     3653   3383   3676     17     24   -133       C  
ATOM   4524  CG  LEU B 292      43.950  30.103   3.703  1.00 28.27           C  
ANISOU 4524  CG  LEU B 292     3684   3415   3640     20      5   -130       C  
ATOM   4525  CD1 LEU B 292      42.524  29.577   3.755  1.00 26.73           C  
ANISOU 4525  CD1 LEU B 292     3499   3225   3432     20     10   -129       C  
ATOM   4526  CD2 LEU B 292      44.576  29.606   2.385  1.00 28.38           C  
ANISOU 4526  CD2 LEU B 292     3692   3442   3648     36     -4   -102       C  
ATOM   4527  N   GLN B 293      45.413  34.404   2.806  1.00 27.13           N  
ANISOU 4527  N   GLN B 293     3462   3209   3635     23     50   -114       N  
ATOM   4528  CA  GLN B 293      45.509  35.867   2.797  1.00 29.73           C  
ANISOU 4528  CA  GLN B 293     3768   3512   4013     20     70   -115       C  
ATOM   4529  C   GLN B 293      44.071  36.466   2.848  1.00 28.47           C  
ANISOU 4529  C   GLN B 293     3604   3340   3870     21     93   -115       C  
ATOM   4530  O   GLN B 293      43.522  36.849   1.810  1.00 25.74           O  
ANISOU 4530  O   GLN B 293     3240   2994   3544     35    106    -86       O  
ATOM   4531  CB  GLN B 293      46.322  36.291   1.555  1.00 31.29           C  
ANISOU 4531  CB  GLN B 293     3942   3709   4236     37     74    -83       C  
ATOM   4532  CG  GLN B 293      47.815  36.080   1.845  1.00 33.03           C  
ANISOU 4532  CG  GLN B 293     4162   3931   4455     31     56    -90       C  
ATOM   4533  CD  GLN B 293      48.756  36.110   0.653  1.00 33.58           C  
ANISOU 4533  CD  GLN B 293     4214   4005   4538     49     57    -57       C  
ATOM   4534  OE1 GLN B 293      48.608  36.883  -0.284  1.00 38.53           O  
ANISOU 4534  OE1 GLN B 293     4820   4624   5196     62     75    -32       O  
ATOM   4535  NE2 GLN B 293      49.759  35.251   0.706  1.00 38.42           N  
ANISOU 4535  NE2 GLN B 293     4836   4632   5130     50     38    -56       N  
ATOM   4536  N   LEU B 294      43.489  36.467   4.059  1.00 27.53           N  
ANISOU 4536  N   LEU B 294     3503   3214   3743      6     98   -145       N  
ATOM   4537  CA  LEU B 294      42.076  36.781   4.292  1.00 28.35           C  
ANISOU 4537  CA  LEU B 294     3606   3307   3856      5    120   -147       C  
ATOM   4538  C   LEU B 294      41.792  38.280   4.177  1.00 30.01           C  
ANISOU 4538  C   LEU B 294     3793   3489   4120      6    148   -144       C  
ATOM   4539  O   LEU B 294      42.658  39.099   4.568  1.00 28.53           O  
ANISOU 4539  O   LEU B 294     3599   3284   3957     -2    152   -160       O  
ATOM   4540  CB  LEU B 294      41.633  36.274   5.676  1.00 27.44           C  
ANISOU 4540  CB  LEU B 294     3519   3191   3712     -9    119   -180       C  
ATOM   4541  CG  LEU B 294      41.698  34.724   5.738  1.00 27.78           C  
ANISOU 4541  CG  LEU B 294     3585   3263   3704     -8     93   -179       C  
ATOM   4542  CD1 LEU B 294      41.074  34.201   7.035  1.00 27.16           C  
ANISOU 4542  CD1 LEU B 294     3534   3185   3598    -20     96   -207       C  
ATOM   4543  CD2 LEU B 294      41.080  34.066   4.484  1.00 25.34           C  
ANISOU 4543  CD2 LEU B 294     3267   2971   3388      8     88   -145       C  
ATOM   4544  N   ASN B 295      40.627  38.645   3.596  1.00 30.60           N  
ANISOU 4544  N   ASN B 295     3852   3558   4216     16    168   -122       N  
ATOM   4545  CA  ASN B 295      40.185  40.020   3.659  1.00 29.80           C  
ANISOU 4545  CA  ASN B 295     3730   3427   4165     15    199   -122       C  
ATOM   4546  C   ASN B 295      39.551  40.288   5.023  1.00 30.23           C  
ANISOU 4546  C   ASN B 295     3803   3463   4219      0    216   -157       C  
ATOM   4547  O   ASN B 295      39.475  39.414   5.885  1.00 29.43           O  
ANISOU 4547  O   ASN B 295     3729   3373   4078     -8    204   -180       O  
ATOM   4548  CB  ASN B 295      39.295  40.373   2.487  1.00 31.23           C  
ANISOU 4548  CB  ASN B 295     3885   3608   4371     32    212    -82       C  
ATOM   4549  CG  ASN B 295      38.001  39.615   2.470  1.00 32.11           C  
ANISOU 4549  CG  ASN B 295     4004   3731   4462     35    211    -73       C  
ATOM   4550  OD1 ASN B 295      37.470  39.206   3.503  1.00 32.33           O  
ANISOU 4550  OD1 ASN B 295     4053   3758   4474     24    215    -98       O  
ATOM   4551  ND2 ASN B 295      37.468  39.448   1.283  1.00 30.93           N  
ANISOU 4551  ND2 ASN B 295     3837   3595   4317     50    207    -35       N  
ATOM   4552  N   SER B 296      39.109  41.518   5.230  1.00 30.16           N  
ANISOU 4552  N   SER B 296     3779   3424   4256     -1    248   -161       N  
ATOM   4553  CA  SER B 296      38.644  41.920   6.514  1.00 30.40           C  
ANISOU 4553  CA  SER B 296     3828   3432   4289    -14    268   -196       C  
ATOM   4554  C   SER B 296      37.364  41.188   7.000  1.00 30.12           C  
ANISOU 4554  C   SER B 296     3809   3404   4230    -14    277   -198       C  
ATOM   4555  O   SER B 296      37.222  40.891   8.163  1.00 31.05           O  
ANISOU 4555  O   SER B 296     3955   3518   4324    -26    280   -230       O  
ATOM   4556  CB  SER B 296      38.508  43.449   6.476  1.00 32.25           C  
ANISOU 4556  CB  SER B 296     4039   3630   4582    -14    302   -197       C  
ATOM   4557  OG  SER B 296      37.278  43.840   7.012  1.00 32.81           O  
ANISOU 4557  OG  SER B 296     4113   3682   4670    -15    334   -203       O  
ATOM   4558  N   GLU B 297      36.448  40.838   6.140  1.00 32.36           N  
ANISOU 4558  N   GLU B 297     4075   3698   4519      0    279   -164       N  
ATOM   4559  CA  GLU B 297      35.263  40.122   6.659  1.00 37.01           C  
ANISOU 4559  CA  GLU B 297     4679   4293   5090     -1    287   -166       C  
ATOM   4560  C   GLU B 297      35.565  38.622   6.991  1.00 33.24           C  
ANISOU 4560  C   GLU B 297     4229   3845   4553     -6    255   -176       C  
ATOM   4561  O   GLU B 297      35.084  38.077   8.006  1.00 32.28           O  
ANISOU 4561  O   GLU B 297     4133   3724   4407    -14    260   -198       O  
ATOM   4562  CB  GLU B 297      34.093  40.263   5.697  1.00 44.21           C  
ANISOU 4562  CB  GLU B 297     5562   5204   6030     12    299   -126       C  
ATOM   4563  CG  GLU B 297      34.115  39.238   4.588  1.00 57.95           C  
ANISOU 4563  CG  GLU B 297     7296   6977   7744     22    266    -95       C  
ATOM   4564  CD  GLU B 297      33.153  39.531   3.440  1.00 74.68           C  
ANISOU 4564  CD  GLU B 297     9383   9096   9894     36    273    -52       C  
ATOM   4565  OE1 GLU B 297      32.063  40.149   3.670  1.00 74.57           O  
ANISOU 4565  OE1 GLU B 297     9355   9061   9916     38    302    -44       O  
ATOM   4566  OE2 GLU B 297      33.508  39.122   2.295  1.00 82.72           O  
ANISOU 4566  OE2 GLU B 297    10392  10136  10901     46    248    -26       O  
ATOM   4567  N   GLU B 298      36.424  37.995   6.192  1.00 30.84           N  
ANISOU 4567  N   GLU B 298     3923   3565   4228     -1    223   -162       N  
ATOM   4568  CA  GLU B 298      36.776  36.591   6.419  1.00 29.54           C  
ANISOU 4568  CA  GLU B 298     3783   3428   4011     -4    194   -169       C  
ATOM   4569  C   GLU B 298      37.501  36.549   7.759  1.00 30.94           C  
ANISOU 4569  C   GLU B 298     3989   3600   4165    -20    191   -210       C  
ATOM   4570  O   GLU B 298      37.247  35.692   8.596  1.00 30.84           O  
ANISOU 4570  O   GLU B 298     4002   3597   4117    -26    185   -227       O  
ATOM   4571  CB  GLU B 298      37.642  36.091   5.286  1.00 28.60           C  
ANISOU 4571  CB  GLU B 298     3655   3331   3879      4    166   -147       C  
ATOM   4572  CG  GLU B 298      36.973  36.142   3.917  1.00 27.45           C  
ANISOU 4572  CG  GLU B 298     3484   3192   3751     20    166   -107       C  
ATOM   4573  CD  GLU B 298      38.015  36.192   2.810  1.00 29.39           C  
ANISOU 4573  CD  GLU B 298     3717   3449   3997     30    149    -86       C  
ATOM   4574  OE1 GLU B 298      39.217  36.419   3.100  1.00 31.14           O  
ANISOU 4574  OE1 GLU B 298     3944   3669   4217     25    142   -101       O  
ATOM   4575  OE2 GLU B 298      37.676  36.050   1.622  1.00 29.05           O  
ANISOU 4575  OE2 GLU B 298     3660   3418   3959     43    142    -54       O  
ATOM   4576  N   LYS B 299      38.321  37.553   8.000  1.00 31.54           N  
ANISOU 4576  N   LYS B 299     4059   3658   4264    -26    197   -225       N  
ATOM   4577  CA  LYS B 299      39.057  37.647   9.222  1.00 32.84           C  
ANISOU 4577  CA  LYS B 299     4249   3816   4410    -42    192   -263       C  
ATOM   4578  C   LYS B 299      38.149  37.913  10.428  1.00 31.59           C  
ANISOU 4578  C   LYS B 299     4112   3640   4249    -51    219   -290       C  
ATOM   4579  O   LYS B 299      38.452  37.499  11.523  1.00 30.85           O  
ANISOU 4579  O   LYS B 299     4049   3550   4121    -63    212   -320       O  
ATOM   4580  CB  LYS B 299      40.093  38.758   9.069  1.00 36.88           C  
ANISOU 4580  CB  LYS B 299     4746   4310   4955    -47    193   -271       C  
ATOM   4581  CG  LYS B 299      41.355  38.557   9.893  1.00 43.56           C  
ANISOU 4581  CG  LYS B 299     5613   5161   5776    -62    168   -300       C  
ATOM   4582  CD  LYS B 299      42.451  39.454   9.303  1.00 48.26           C  
ANISOU 4582  CD  LYS B 299     6182   5744   6407    -62    162   -294       C  
ATOM   4583  CE  LYS B 299      42.234  39.576   7.803  1.00 46.30           C  
ANISOU 4583  CE  LYS B 299     5902   5501   6186    -43    167   -250       C  
ATOM   4584  NZ  LYS B 299      43.131  40.581   7.171  1.00 54.80           N  
ANISOU 4584  NZ  LYS B 299     6951   6562   7306    -41    170   -240       N  
ATOM   4585  N   ALA B 300      37.032  38.597  10.226  1.00 31.32           N  
ANISOU 4585  N   ALA B 300     4062   3586   4250    -44    252   -278       N  
ATOM   4586  CA  ALA B 300      36.054  38.796  11.346  1.00 30.77           C  
ANISOU 4586  CA  ALA B 300     4013   3498   4179    -50    284   -301       C  
ATOM   4587  C   ALA B 300      35.396  37.459  11.714  1.00 29.98           C  
ANISOU 4587  C   ALA B 300     3933   3419   4037    -48    275   -297       C  
ATOM   4588  O   ALA B 300      35.244  37.113  12.889  1.00 30.21           O  
ANISOU 4588  O   ALA B 300     3994   3447   4036    -57    281   -325       O  
ATOM   4589  CB  ALA B 300      35.016  39.869  11.025  1.00 28.29           C  
ANISOU 4589  CB  ALA B 300     3675   3155   3918    -42    324   -286       C  
ATOM   4590  N   LYS B 301      35.078  36.674  10.712  1.00 32.34           N  
ANISOU 4590  N   LYS B 301     4216   3740   4332    -37    257   -264       N  
ATOM   4591  CA  LYS B 301      34.611  35.262  10.969  1.00 34.33           C  
ANISOU 4591  CA  LYS B 301     4486   4014   4542    -36    243   -260       C  
ATOM   4592  C   LYS B 301      35.642  34.348  11.624  1.00 31.51           C  
ANISOU 4592  C   LYS B 301     4158   3678   4135    -45    213   -282       C  
ATOM   4593  O   LYS B 301      35.291  33.569  12.514  1.00 31.83           O  
ANISOU 4593  O   LYS B 301     4225   3725   4143    -50    214   -295       O  
ATOM   4594  CB  LYS B 301      34.090  34.624   9.684  1.00 36.01           C  
ANISOU 4594  CB  LYS B 301     4675   4245   4762    -24    228   -221       C  
ATOM   4595  CG  LYS B 301      32.788  35.232   9.185  1.00 40.50           C  
ANISOU 4595  CG  LYS B 301     5217   4797   5375    -15    256   -197       C  
ATOM   4596  CD  LYS B 301      31.663  34.712  10.078  1.00 49.65           C  
ANISOU 4596  CD  LYS B 301     6391   5949   6524    -17    276   -203       C  
ATOM   4597  CE  LYS B 301      30.315  35.351   9.790  1.00 55.49           C  
ANISOU 4597  CE  LYS B 301     7104   6667   7310    -10    308   -181       C  
ATOM   4598  NZ  LYS B 301      30.251  36.763  10.285  1.00 59.36           N  
ANISOU 4598  NZ  LYS B 301     7589   7125   7838    -12    345   -195       N  
ATOM   4599  N   PHE B 302      36.896  34.405  11.169  1.00 30.04           N  
ANISOU 4599  N   PHE B 302     3967   3502   3944    -47    187   -282       N  
ATOM   4600  CA  PHE B 302      37.969  33.645  11.838  1.00 29.49           C  
ANISOU 4600  CA  PHE B 302     3923   3450   3831    -56    158   -302       C  
ATOM   4601  C   PHE B 302      38.022  33.973  13.329  1.00 29.36           C  
ANISOU 4601  C   PHE B 302     3937   3420   3797    -70    171   -340       C  
ATOM   4602  O   PHE B 302      38.095  33.090  14.178  1.00 28.73           O  
ANISOU 4602  O   PHE B 302     3886   3354   3676    -75    160   -354       O  
ATOM   4603  CB  PHE B 302      39.352  33.974  11.250  1.00 30.36           C  
ANISOU 4603  CB  PHE B 302     4020   3565   3949    -57    134   -299       C  
ATOM   4604  CG  PHE B 302      40.380  32.893  11.504  1.00 31.11           C  
ANISOU 4604  CG  PHE B 302     4133   3685   4002    -61    100   -304       C  
ATOM   4605  CD1 PHE B 302      41.085  32.836  12.732  1.00 31.91           C  
ANISOU 4605  CD1 PHE B 302     4260   3786   4076    -76     89   -336       C  
ATOM   4606  CD2 PHE B 302      40.627  31.896  10.548  1.00 30.47           C  
ANISOU 4606  CD2 PHE B 302     4043   3626   3906    -50     78   -278       C  
ATOM   4607  CE1 PHE B 302      42.006  31.822  12.968  1.00 30.01           C  
ANISOU 4607  CE1 PHE B 302     4033   3568   3799    -79     57   -338       C  
ATOM   4608  CE2 PHE B 302      41.556  30.883  10.801  1.00 29.67           C  
ANISOU 4608  CE2 PHE B 302     3958   3546   3769    -53     49   -281       C  
ATOM   4609  CZ  PHE B 302      42.229  30.847  12.008  1.00 30.04           C  
ANISOU 4609  CZ  PHE B 302     4027   3593   3793    -67     39   -310       C  
ATOM   4610  N   ASP B 303      37.972  35.255  13.627  1.00 28.62           N  
ANISOU 4610  N   ASP B 303     3838   3299   3735    -75    195   -356       N  
ATOM   4611  CA  ASP B 303      38.103  35.753  14.960  1.00 30.95           C  
ANISOU 4611  CA  ASP B 303     4163   3579   4017    -89    207   -394       C  
ATOM   4612  C   ASP B 303      36.967  35.291  15.831  1.00 31.65           C  
ANISOU 4612  C   ASP B 303     4276   3664   4085    -88    232   -403       C  
ATOM   4613  O   ASP B 303      37.160  34.977  17.009  1.00 32.90           O  
ANISOU 4613  O   ASP B 303     4470   3825   4206    -98    230   -431       O  
ATOM   4614  CB  ASP B 303      38.157  37.307  14.910  1.00 33.31           C  
ANISOU 4614  CB  ASP B 303     4447   3845   4363    -93    232   -406       C  
ATOM   4615  CG  ASP B 303      39.551  37.874  14.391  1.00 34.99           C  
ANISOU 4615  CG  ASP B 303     4643   4057   4594    -99    206   -407       C  
ATOM   4616  OD1 ASP B 303      40.542  37.096  14.096  1.00 33.98           O  
ANISOU 4616  OD1 ASP B 303     4515   3954   4442   -100    169   -400       O  
ATOM   4617  OD2 ASP B 303      39.650  39.136  14.292  1.00 36.03           O  
ANISOU 4617  OD2 ASP B 303     4760   4161   4768   -102    226   -415       O  
ATOM   4618  N   GLU B 304      35.757  35.239  15.274  1.00 33.85           N  
ANISOU 4618  N   GLU B 304     4535   3936   4387    -76    256   -377       N  
ATOM   4619  CA  GLU B 304      34.656  34.752  16.060  1.00 35.48           C  
ANISOU 4619  CA  GLU B 304     4762   4139   4578    -74    281   -382       C  
ATOM   4620  C   GLU B 304      34.849  33.265  16.354  1.00 32.49           C  
ANISOU 4620  C   GLU B 304     4403   3790   4149    -74    254   -378       C  
ATOM   4621  O   GLU B 304      34.614  32.798  17.487  1.00 30.21           O  
ANISOU 4621  O   GLU B 304     4148   3503   3827    -79    263   -398       O  
ATOM   4622  CB  GLU B 304      33.352  34.898  15.302  1.00 43.12           C  
ANISOU 4622  CB  GLU B 304     5701   5096   5585    -61    308   -350       C  
ATOM   4623  CG  GLU B 304      32.698  36.262  15.360  1.00 48.11           C  
ANISOU 4623  CG  GLU B 304     6318   5693   6266    -59    349   -354       C  
ATOM   4624  CD  GLU B 304      31.585  36.328  14.342  1.00 52.38           C  
ANISOU 4624  CD  GLU B 304     6822   6229   6848    -45    364   -314       C  
ATOM   4625  OE1 GLU B 304      30.571  35.593  14.491  1.00 59.01           O  
ANISOU 4625  OE1 GLU B 304     7665   7074   7683    -40    375   -300       O  
ATOM   4626  OE2 GLU B 304      31.742  37.093  13.384  1.00 53.91           O  
ANISOU 4626  OE2 GLU B 304     6986   6416   7081    -40    364   -296       O  
ATOM   4627  N   ALA B 305      35.280  32.527  15.331  1.00 29.82           N  
ANISOU 4627  N   ALA B 305     4047   3475   3807    -68    222   -353       N  
ATOM   4628  CA  ALA B 305      35.581  31.103  15.563  1.00 29.69           C  
ANISOU 4628  CA  ALA B 305     4049   3486   3745    -68    195   -350       C  
ATOM   4629  C   ALA B 305      36.572  30.958  16.676  1.00 30.02           C  
ANISOU 4629  C   ALA B 305     4122   3534   3747    -81    180   -381       C  
ATOM   4630  O   ALA B 305      36.317  30.179  17.602  1.00 33.04           O  
ANISOU 4630  O   ALA B 305     4533   3925   4093    -83    182   -391       O  
ATOM   4631  CB  ALA B 305      36.034  30.408  14.316  1.00 28.56           C  
ANISOU 4631  CB  ALA B 305     3883   3363   3603    -61    164   -322       C  
ATOM   4632  N   ILE B 306      37.607  31.799  16.705  1.00 28.87           N  
ANISOU 4632  N   ILE B 306     3974   3381   3610    -89    168   -397       N  
ATOM   4633  CA  ILE B 306      38.671  31.610  17.710  1.00 28.70           C  
ANISOU 4633  CA  ILE B 306     3982   3369   3551   -102    145   -425       C  
ATOM   4634  C   ILE B 306      38.158  31.947  19.092  1.00 29.99           C  
ANISOU 4634  C   ILE B 306     4181   3518   3694   -111    170   -456       C  
ATOM   4635  O   ILE B 306      38.437  31.220  20.071  1.00 32.44           O  
ANISOU 4635  O   ILE B 306     4524   3843   3958   -117    158   -471       O  
ATOM   4636  CB  ILE B 306      39.928  32.427  17.388  1.00 28.38           C  
ANISOU 4636  CB  ILE B 306     3929   3324   3529   -110    123   -434       C  
ATOM   4637  CG1 ILE B 306      40.552  32.021  16.040  1.00 27.98           C  
ANISOU 4637  CG1 ILE B 306     3846   3289   3493   -101     98   -402       C  
ATOM   4638  CG2 ILE B 306      40.947  32.328  18.494  1.00 27.51           C  
ANISOU 4638  CG2 ILE B 306     3848   3221   3382   -126     99   -464       C  
ATOM   4639  CD1 ILE B 306      40.809  30.514  15.922  1.00 28.28           C  
ANISOU 4639  CD1 ILE B 306     3893   3357   3493    -96     72   -387       C  
ATOM   4640  N   ALA B 307      37.414  33.055  19.189  1.00 30.87           N  
ANISOU 4640  N   ALA B 307     4288   3601   3840   -110    207   -465       N  
ATOM   4641  CA  ALA B 307      36.868  33.487  20.437  1.00 31.40           C  
ANISOU 4641  CA  ALA B 307     4388   3649   3891   -116    238   -494       C  
ATOM   4642  C   ALA B 307      35.932  32.380  20.991  1.00 32.14           C  
ANISOU 4642  C   ALA B 307     4502   3755   3954   -109    252   -485       C  
ATOM   4643  O   ALA B 307      35.917  32.100  22.185  1.00 33.56           O  
ANISOU 4643  O   ALA B 307     4721   3937   4093   -115    258   -508       O  
ATOM   4644  CB  ALA B 307      36.153  34.857  20.311  1.00 31.09           C  
ANISOU 4644  CB  ALA B 307     4335   3574   3900   -115    280   -501       C  
ATOM   4645  N   GLU B 308      35.189  31.713  20.138  1.00 32.46           N  
ANISOU 4645  N   GLU B 308     4517   3804   4010    -96    256   -452       N  
ATOM   4646  CA  GLU B 308      34.426  30.559  20.629  1.00 33.96           C  
ANISOU 4646  CA  GLU B 308     4724   4006   4171    -90    264   -441       C  
ATOM   4647  C   GLU B 308      35.296  29.419  21.206  1.00 32.67           C  
ANISOU 4647  C   GLU B 308     4587   3872   3954    -95    229   -448       C  
ATOM   4648  O   GLU B 308      34.965  28.890  22.210  1.00 35.33           O  
ANISOU 4648  O   GLU B 308     4954   4211   4256    -96    240   -458       O  
ATOM   4649  CB  GLU B 308      33.443  30.042  19.571  1.00 34.20           C  
ANISOU 4649  CB  GLU B 308     4721   4038   4232    -77    272   -404       C  
ATOM   4650  CG  GLU B 308      32.572  28.858  20.020  1.00 35.79           C  
ANISOU 4650  CG  GLU B 308     4936   4250   4412    -70    282   -391       C  
ATOM   4651  CD  GLU B 308      31.699  29.114  21.277  1.00 35.38           C  
ANISOU 4651  CD  GLU B 308     4914   4179   4350    -70    326   -408       C  
ATOM   4652  OE1 GLU B 308      31.567  30.285  21.773  1.00 34.52           O  
ANISOU 4652  OE1 GLU B 308     4814   4045   4256    -74    355   -430       O  
ATOM   4653  OE2 GLU B 308      31.105  28.112  21.746  1.00 34.20           O  
ANISOU 4653  OE2 GLU B 308     4777   4038   4178    -65    334   -399       O  
ATOM   4654  N   THR B 309      36.408  29.076  20.581  1.00 31.40           N  
ANISOU 4654  N   THR B 309     4413   3729   3786    -98    188   -441       N  
ATOM   4655  CA  THR B 309      37.319  28.049  21.103  1.00 29.23           C  
ANISOU 4655  CA  THR B 309     4160   3480   3463   -103    153   -445       C  
ATOM   4656  C   THR B 309      37.903  28.469  22.456  1.00 30.93           C  
ANISOU 4656  C   THR B 309     4414   3693   3643   -116    151   -481       C  
ATOM   4657  O   THR B 309      38.109  27.629  23.353  1.00 28.83           O  
ANISOU 4657  O   THR B 309     4178   3443   3331   -119    140   -488       O  
ATOM   4658  CB  THR B 309      38.491  27.820  20.122  1.00 28.83           C  
ANISOU 4658  CB  THR B 309     4085   3446   3420   -104    113   -431       C  
ATOM   4659  OG1 THR B 309      37.985  27.295  18.869  1.00 26.63           O  
ANISOU 4659  OG1 THR B 309     3776   3174   3167    -91    111   -398       O  
ATOM   4660  CG2 THR B 309      39.554  26.866  20.717  1.00 27.53           C  
ANISOU 4660  CG2 THR B 309     3942   3307   3210   -109     76   -436       C  
ATOM   4661  N   LYS B 310      38.165  29.770  22.568  1.00 31.56           N  
ANISOU 4661  N   LYS B 310     4493   3752   3746   -125    161   -503       N  
ATOM   4662  CA  LYS B 310      38.731  30.352  23.728  1.00 33.47           C  
ANISOU 4662  CA  LYS B 310     4770   3987   3960   -139    157   -540       C  
ATOM   4663  C   LYS B 310      37.736  30.300  24.838  1.00 33.08           C  
ANISOU 4663  C   LYS B 310     4756   3927   3886   -137    195   -555       C  
ATOM   4664  O   LYS B 310      38.098  29.989  25.954  1.00 35.05           O  
ANISOU 4664  O   LYS B 310     5044   4186   4088   -145    186   -577       O  
ATOM   4665  CB  LYS B 310      39.110  31.825  23.486  1.00 36.07           C  
ANISOU 4665  CB  LYS B 310     5086   4291   4328   -148    164   -559       C  
ATOM   4666  CG  LYS B 310      40.530  31.988  22.983  1.00 38.27           C  
ANISOU 4666  CG  LYS B 310     5346   4580   4613   -157    119   -559       C  
ATOM   4667  CD  LYS B 310      40.972  33.439  23.023  1.00 42.15           C  
ANISOU 4667  CD  LYS B 310     5833   5045   5138   -169    125   -584       C  
ATOM   4668  CE  LYS B 310      42.482  33.517  22.882  1.00 45.79           C  
ANISOU 4668  CE  LYS B 310     6284   5517   5596   -182     78   -589       C  
ATOM   4669  NZ  LYS B 310      42.849  34.601  21.932  1.00 47.95           N  
ANISOU 4669  NZ  LYS B 310     6520   5770   5925   -183     80   -584       N  
ATOM   4670  N   ARG B 311      36.490  30.650  24.542  1.00 34.88           N  
ANISOU 4670  N   ARG B 311     4970   4134   4146   -127    238   -544       N  
ATOM   4671  CA  ARG B 311      35.459  30.677  25.546  1.00 35.48           C  
ANISOU 4671  CA  ARG B 311     5078   4195   4205   -123    281   -557       C  
ATOM   4672  C   ARG B 311      35.265  29.254  26.070  1.00 37.89           C  
ANISOU 4672  C   ARG B 311     5403   4526   4465   -117    273   -543       C  
ATOM   4673  O   ARG B 311      35.251  29.046  27.305  1.00 37.50           O  
ANISOU 4673  O   ARG B 311     5397   4479   4370   -121    282   -565       O  
ATOM   4674  CB  ARG B 311      34.164  31.274  25.032  1.00 36.10           C  
ANISOU 4674  CB  ARG B 311     5133   4247   4334   -112    328   -542       C  
ATOM   4675  CG  ARG B 311      33.105  31.380  26.122  1.00 35.79           C  
ANISOU 4675  CG  ARG B 311     5126   4189   4280   -107    378   -555       C  
ATOM   4676  CD  ARG B 311      31.708  31.421  25.515  1.00 36.27           C  
ANISOU 4676  CD  ARG B 311     5157   4233   4388    -92    419   -525       C  
ATOM   4677  NE  ARG B 311      31.251  30.155  24.904  1.00 38.90           N  
ANISOU 4677  NE  ARG B 311     5469   4587   4722    -82    406   -489       N  
ATOM   4678  CZ  ARG B 311      30.816  29.071  25.571  1.00 40.07           C  
ANISOU 4678  CZ  ARG B 311     5640   4749   4837    -76    413   -481       C  
ATOM   4679  NH1 ARG B 311      30.805  29.014  26.904  1.00 44.17           N  
ANISOU 4679  NH1 ARG B 311     6206   5265   5312    -79    431   -506       N  
ATOM   4680  NH2 ARG B 311      30.407  28.001  24.911  1.00 40.47           N  
ANISOU 4680  NH2 ARG B 311     5666   4814   4894    -68    400   -448       N  
ATOM   4681  N   MET B 312      35.156  28.272  25.173  1.00 36.22           N  
ANISOU 4681  N   MET B 312     5164   4333   4265   -108    255   -509       N  
ATOM   4682  CA  MET B 312      35.126  26.907  25.688  1.00 37.91           C  
ANISOU 4682  CA  MET B 312     5396   4570   4435   -104    243   -498       C  
ATOM   4683  C   MET B 312      36.392  26.505  26.430  1.00 37.24           C  
ANISOU 4683  C   MET B 312     5340   4507   4300   -115    203   -516       C  
ATOM   4684  O   MET B 312      36.297  25.860  27.482  1.00 37.81           O  
ANISOU 4684  O   MET B 312     5448   4590   4327   -115    208   -523       O  
ATOM   4685  CB  MET B 312      34.762  25.902  24.631  1.00 39.28           C  
ANISOU 4685  CB  MET B 312     5536   4757   4628    -93    231   -461       C  
ATOM   4686  CG  MET B 312      33.274  25.959  24.315  1.00 40.99           C  
ANISOU 4686  CG  MET B 312     5737   4955   4882    -82    274   -442       C  
ATOM   4687  SD  MET B 312      32.831  25.139  22.773  1.00 46.23           S  
ANISOU 4687  SD  MET B 312     6353   5628   5582    -71    257   -400       S  
ATOM   4688  CE  MET B 312      34.010  25.814  21.569  1.00 42.18           C  
ANISOU 4688  CE  MET B 312     5811   5122   5094    -77    219   -399       C  
ATOM   4689  N   LYS B 313      37.559  26.939  25.957  1.00 35.91           N  
ANISOU 4689  N   LYS B 313     5157   4345   4139   -125    166   -523       N  
ATOM   4690  CA  LYS B 313      38.805  26.515  26.590  1.00 35.50           C  
ANISOU 4690  CA  LYS B 313     5128   4316   4044   -135    125   -535       C  
ATOM   4691  C   LYS B 313      38.886  26.951  28.062  1.00 37.33           C  
ANISOU 4691  C   LYS B 313     5409   4542   4232   -146    134   -571       C  
ATOM   4692  O   LYS B 313      39.427  26.232  28.880  1.00 37.64           O  
ANISOU 4692  O   LYS B 313     5476   4602   4223   -150    112   -575       O  
ATOM   4693  CB  LYS B 313      40.049  27.008  25.868  1.00 35.35           C  
ANISOU 4693  CB  LYS B 313     5083   4301   4045   -145     85   -537       C  
ATOM   4694  CG  LYS B 313      41.287  26.397  26.514  1.00 37.23           C  
ANISOU 4694  CG  LYS B 313     5341   4564   4240   -155     41   -544       C  
ATOM   4695  CD  LYS B 313      42.637  26.729  25.920  1.00 38.47           C  
ANISOU 4695  CD  LYS B 313     5474   4727   4413   -164      0   -543       C  
ATOM   4696  CE  LYS B 313      43.088  28.176  26.016  1.00 37.47           C  
ANISOU 4696  CE  LYS B 313     5346   4578   4311   -178     -1   -572       C  
ATOM   4697  NZ  LYS B 313      44.427  28.297  25.329  1.00 40.35           N  
ANISOU 4697  NZ  LYS B 313     5682   4951   4695   -185    -44   -563       N  
ATOM   4698  N   ALA B 314      38.344  28.123  28.358  1.00 37.28           N  
ANISOU 4698  N   ALA B 314     5413   4508   4244   -150    169   -594       N  
ATOM   4699  CA  ALA B 314      38.361  28.721  29.673  1.00 39.97           C  
ANISOU 4699  CA  ALA B 314     5801   4838   4548   -160    183   -632       C  
ATOM   4700  C   ALA B 314      37.516  27.956  30.698  1.00 41.28           C  
ANISOU 4700  C   ALA B 314     6004   5008   4669   -151    212   -630       C  
ATOM   4701  O   ALA B 314      37.658  28.187  31.906  1.00 39.60           O  
ANISOU 4701  O   ALA B 314     5839   4794   4412   -159    218   -660       O  
ATOM   4702  CB  ALA B 314      37.859  30.162  29.564  1.00 40.70           C  
ANISOU 4702  CB  ALA B 314     5889   4894   4680   -163    219   -653       C  
ATOM   4703  N   LEU B 315      36.619  27.096  30.199  1.00 40.39           N  
ANISOU 4703  N   LEU B 315     5872   4901   4573   -135    233   -597       N  
ATOM   4704  CA  LEU B 315      35.688  26.351  31.008  1.00 41.91           C  
ANISOU 4704  CA  LEU B 315     6093   5095   4736   -124    266   -589       C  
ATOM   4705  C   LEU B 315      36.175  24.922  31.236  1.00 46.47           C  
ANISOU 4705  C   LEU B 315     6678   5705   5273   -120    234   -569       C  
ATOM   4706  O   LEU B 315      35.661  24.193  32.124  1.00 44.96           O  
ANISOU 4706  O   LEU B 315     6517   5520   5043   -113    253   -565       O  
ATOM   4707  CB  LEU B 315      34.327  26.290  30.325  1.00 40.37           C  
ANISOU 4707  CB  LEU B 315     5868   4881   4588   -108    310   -563       C  
ATOM   4708  CG  LEU B 315      33.395  27.492  30.340  1.00 40.66           C  
ANISOU 4708  CG  LEU B 315     5903   4882   4663   -105    361   -577       C  
ATOM   4709  CD1 LEU B 315      32.135  27.065  29.597  1.00 39.56           C  
ANISOU 4709  CD1 LEU B 315     5728   4732   4568    -89    393   -541       C  
ATOM   4710  CD2 LEU B 315      33.054  27.860  31.771  1.00 40.96           C  
ANISOU 4710  CD2 LEU B 315     5995   4907   4659   -107    396   -607       C  
ATOM   4711  N   ALA B 316      37.160  24.527  30.424  1.00 49.40           N  
ANISOU 4711  N   ALA B 316     7019   6095   5654   -125    186   -555       N  
ATOM   4712  CA  ALA B 316      37.786  23.187  30.460  1.00 54.72           C  
ANISOU 4712  CA  ALA B 316     7693   6800   6296   -122    150   -533       C  
ATOM   4713  C   ALA B 316      38.341  22.817  31.838  1.00 57.62           C  
ANISOU 4713  C   ALA B 316     8109   7184   6599   -129    136   -551       C  
ATOM   4714  O   ALA B 316      38.289  21.657  32.267  1.00 59.57           O  
ANISOU 4714  O   ALA B 316     8369   7450   6813   -121    131   -532       O  
ATOM   4715  CB  ALA B 316      38.910  23.105  29.422  1.00 54.77           C  
ANISOU 4715  CB  ALA B 316     7663   6819   6325   -128    103   -522       C  
ATOM   4716  OXT ALA B 316      38.876  23.679  32.535  1.00 62.16           O  
ANISOU 4716  OXT ALA B 316     8711   7753   7151   -142    127   -583       O  
TER    4717      ALA B 316                                                      
ATOM   4718  N   ALA C   2      61.526   9.999   5.382  1.00 52.43           N  
ANISOU 4718  N   ALA C   2     6286   6578   7055   -169    313   -478       N  
ATOM   4719  CA  ALA C   2      62.654   9.063   5.067  1.00 55.76           C  
ANISOU 4719  CA  ALA C   2     6706   7021   7457   -173    290   -446       C  
ATOM   4720  C   ALA C   2      62.883   7.996   6.175  1.00 58.75           C  
ANISOU 4720  C   ALA C   2     7080   7452   7788   -190    273   -446       C  
ATOM   4721  O   ALA C   2      63.800   8.138   6.981  1.00 65.91           O  
ANISOU 4721  O   ALA C   2     7980   8382   8679   -217    265   -463       O  
ATOM   4722  CB  ALA C   2      63.918   9.858   4.774  1.00 54.61           C  
ANISOU 4722  CB  ALA C   2     6557   6859   7334   -186    290   -451       C  
ATOM   4723  N   PRO C   3      62.068   6.904   6.213  1.00 62.50           N  
ANISOU 4723  N   PRO C   3     7558   7948   8241   -176    264   -425       N  
ATOM   4724  CA  PRO C   3      61.072   6.358   5.257  1.00 61.26           C  
ANISOU 4724  CA  PRO C   3     7407   7773   8093   -147    266   -397       C  
ATOM   4725  C   PRO C   3      60.222   7.509   4.678  1.00 63.85           C  
ANISOU 4725  C   PRO C   3     7740   8060   8460   -132    289   -411       C  
ATOM   4726  O   PRO C   3      59.516   8.187   5.453  1.00 74.84           O  
ANISOU 4726  O   PRO C   3     9130   9450   9853   -140    305   -445       O  
ATOM   4727  CB  PRO C   3      60.206   5.439   6.150  1.00 64.08           C  
ANISOU 4727  CB  PRO C   3     7764   8168   8415   -150    258   -396       C  
ATOM   4728  CG  PRO C   3      60.365   5.989   7.552  1.00 60.69           C  
ANISOU 4728  CG  PRO C   3     7327   7765   7966   -179    264   -437       C  
ATOM   4729  CD  PRO C   3      61.823   6.385   7.580  1.00 63.03           C  
ANISOU 4729  CD  PRO C   3     7619   8061   8268   -197    257   -442       C  
ATOM   4730  N   LYS C   4      60.204   7.736   3.366  1.00 52.21           N  
ANISOU 4730  N   LYS C   4     6270   6552   7015   -112    292   -386       N  
ATOM   4731  CA  LYS C   4      60.181   6.726   2.346  1.00 45.04           C  
ANISOU 4731  CA  LYS C   4     5367   5645   6101    -93    279   -345       C  
ATOM   4732  C   LYS C   4      61.345   5.792   2.174  1.00 37.99           C  
ANISOU 4732  C   LYS C   4     4472   4772   5190    -98    260   -323       C  
ATOM   4733  O   LYS C   4      62.480   6.134   2.420  1.00 36.44           O  
ANISOU 4733  O   LYS C   4     4269   4580   4995   -114    257   -332       O  
ATOM   4734  CB  LYS C   4      59.806   7.358   1.010  1.00 48.57           C  
ANISOU 4734  CB  LYS C   4     5817   6052   6584    -74    290   -327       C  
ATOM   4735  CG  LYS C   4      58.288   7.409   0.792  1.00 51.69           C  
ANISOU 4735  CG  LYS C   4     6215   6435   6987    -57    299   -322       C  
ATOM   4736  CD  LYS C   4      57.920   8.384  -0.318  1.00 55.93           C  
ANISOU 4736  CD  LYS C   4     6753   6931   7567    -43    313   -310       C  
ATOM   4737  CE  LYS C   4      58.696   9.690  -0.124  1.00 57.13           C  
ANISOU 4737  CE  LYS C   4     6899   7059   7748    -57    325   -335       C  
ATOM   4738  NZ  LYS C   4      58.018  10.886  -0.695  1.00 52.01           N  
ANISOU 4738  NZ  LYS C   4     6246   6367   7145    -47    342   -335       N  
ATOM   4739  N   ALA C   5      61.001   4.606   1.721  1.00 33.19           N  
ANISOU 4739  N   ALA C   5     3867   4176   4566    -84    247   -295       N  
ATOM   4740  CA  ALA C   5      61.946   3.648   1.233  1.00 31.89           C  
ANISOU 4740  CA  ALA C   5     3701   4022   4391    -80    232   -269       C  
ATOM   4741  C   ALA C   5      62.685   4.286   0.050  1.00 30.89           C  
ANISOU 4741  C   ALA C   5     3575   3868   4292    -73    239   -258       C  
ATOM   4742  O   ALA C   5      62.180   5.219  -0.563  1.00 32.88           O  
ANISOU 4742  O   ALA C   5     3830   4092   4569    -66    253   -261       O  
ATOM   4743  CB  ALA C   5      61.240   2.364   0.862  1.00 27.85           C  
ANISOU 4743  CB  ALA C   5     3195   3521   3865    -64    220   -244       C  
ATOM   4744  N   LYS C   6      63.932   3.883  -0.154  1.00 29.70           N  
ANISOU 4744  N   LYS C   6     3418   3726   4138    -78    229   -247       N  
ATOM   4745  CA  LYS C   6      64.729   4.302  -1.279  1.00 28.44           C  
ANISOU 4745  CA  LYS C   6     3258   3548   4000    -72    235   -233       C  
ATOM   4746  C   LYS C   6      65.072   2.998  -1.965  1.00 28.49           C  
ANISOU 4746  C   LYS C   6     3264   3565   3994    -58    223   -207       C  
ATOM   4747  O   LYS C   6      65.614   2.079  -1.351  1.00 26.88           O  
ANISOU 4747  O   LYS C   6     3054   3385   3773    -64    209   -202       O  
ATOM   4748  CB  LYS C   6      65.992   5.030  -0.827  1.00 29.35           C  
ANISOU 4748  CB  LYS C   6     3362   3666   4124    -92    235   -247       C  
ATOM   4749  CG  LYS C   6      66.826   5.613  -1.943  1.00 29.85           C  
ANISOU 4749  CG  LYS C   6     3422   3709   4210    -89    242   -233       C  
ATOM   4750  CD  LYS C   6      68.107   6.187  -1.390  1.00 28.70           C  
ANISOU 4750  CD  LYS C   6     3264   3569   4069   -110    239   -245       C  
ATOM   4751  CE  LYS C   6      69.044   6.563  -2.516  1.00 30.73           C  
ANISOU 4751  CE  LYS C   6     3516   3813   4346   -107    244   -227       C  
ATOM   4752  NZ  LYS C   6      70.392   6.912  -1.936  1.00 33.27           N  
ANISOU 4752  NZ  LYS C   6     3824   4146   4669   -128    238   -234       N  
ATOM   4753  N   ILE C   7      64.707   2.925  -3.250  1.00 28.12           N  
ANISOU 4753  N   ILE C   7     3224   3501   3957    -41    229   -188       N  
ATOM   4754  CA  ILE C   7      64.880   1.754  -4.009  1.00 26.91           C  
ANISOU 4754  CA  ILE C   7     3073   3356   3794    -27    222   -167       C  
ATOM   4755  C   ILE C   7      65.840   2.130  -5.130  1.00 27.96           C  
ANISOU 4755  C   ILE C   7     3202   3478   3942    -24    229   -156       C  
ATOM   4756  O   ILE C   7      65.584   3.075  -5.822  1.00 29.32           O  
ANISOU 4756  O   ILE C   7     3376   3632   4130    -23    241   -153       O  
ATOM   4757  CB  ILE C   7      63.505   1.319  -4.563  1.00 26.96           C  
ANISOU 4757  CB  ILE C   7     3092   3355   3795    -12    223   -157       C  
ATOM   4758  CG1 ILE C   7      62.557   1.033  -3.382  1.00 26.29           C  
ANISOU 4758  CG1 ILE C   7     3009   3282   3696    -17    216   -169       C  
ATOM   4759  CG2 ILE C   7      63.705   0.100  -5.438  1.00 25.55           C  
ANISOU 4759  CG2 ILE C   7     2916   3182   3607      0    215   -138       C  
ATOM   4760  CD1 ILE C   7      61.075   1.047  -3.644  1.00 25.45           C  
ANISOU 4760  CD1 ILE C   7     2912   3167   3589     -7    220   -164       C  
ATOM   4761  N   VAL C   8      66.954   1.415  -5.282  1.00 28.12           N  
ANISOU 4761  N   VAL C   8     3214   3511   3958    -24    223   -148       N  
ATOM   4762  CA  VAL C   8      67.905   1.664  -6.367  1.00 26.63           C  
ANISOU 4762  CA  VAL C   8     3020   3317   3781    -20    231   -136       C  
ATOM   4763  C   VAL C   8      67.828   0.557  -7.412  1.00 26.76           C  
ANISOU 4763  C   VAL C   8     3041   3337   3789     -3    230   -120       C  
ATOM   4764  O   VAL C   8      68.026  -0.640  -7.102  1.00 27.13           O  
ANISOU 4764  O   VAL C   8     3086   3397   3825      2    220   -118       O  
ATOM   4765  CB  VAL C   8      69.348   1.744  -5.837  1.00 27.42           C  
ANISOU 4765  CB  VAL C   8     3103   3428   3885    -33    227   -139       C  
ATOM   4766  CG1 VAL C   8      70.343   2.085  -6.954  1.00 26.12           C  
ANISOU 4766  CG1 VAL C   8     2931   3259   3732    -30    236   -127       C  
ATOM   4767  CG2 VAL C   8      69.447   2.751  -4.699  1.00 26.53           C  
ANISOU 4767  CG2 VAL C   8     2986   3315   3777    -53    226   -158       C  
ATOM   4768  N   LEU C   9      67.497   0.949  -8.640  1.00 24.74           N  
ANISOU 4768  N   LEU C   9     2790   3070   3537      3    241   -110       N  
ATOM   4769  CA  LEU C   9      67.476   0.044  -9.748  1.00 23.24           C  
ANISOU 4769  CA  LEU C   9     2606   2885   3339     16    243    -98       C  
ATOM   4770  C   LEU C   9      68.869   0.110 -10.379  1.00 23.97           C  
ANISOU 4770  C   LEU C   9     2685   2983   3438     15    251    -93       C  
ATOM   4771  O   LEU C   9      69.227   1.150 -11.006  1.00 23.61           O  
ANISOU 4771  O   LEU C   9     2635   2931   3403      9    261    -87       O  
ATOM   4772  CB  LEU C   9      66.362   0.475 -10.729  1.00 22.02           C  
ANISOU 4772  CB  LEU C   9     2463   2719   3183     21    251    -88       C  
ATOM   4773  CG  LEU C   9      64.968   0.810 -10.138  1.00 22.30           C  
ANISOU 4773  CG  LEU C   9     2508   2745   3218     21    247    -91       C  
ATOM   4774  CD1 LEU C   9      63.859   0.960 -11.236  1.00 21.28           C  
ANISOU 4774  CD1 LEU C   9     2389   2609   3087     27    252    -76       C  
ATOM   4775  CD2 LEU C   9      64.592  -0.344  -9.185  1.00 21.67           C  
ANISOU 4775  CD2 LEU C   9     2432   2676   3124     25    233    -99       C  
ATOM   4776  N   VAL C  10      69.660  -0.964 -10.219  1.00 23.44           N  
ANISOU 4776  N   VAL C  10     2610   2928   3367     21    245    -94       N  
ATOM   4777  CA  VAL C  10      71.024  -1.037 -10.822  1.00 24.28           C  
ANISOU 4777  CA  VAL C  10     2701   3042   3479     22    254    -89       C  
ATOM   4778  C   VAL C  10      70.885  -1.624 -12.212  1.00 24.23           C  
ANISOU 4778  C   VAL C  10     2701   3039   3465     35    264    -83       C  
ATOM   4779  O   VAL C  10      70.703  -2.854 -12.385  1.00 23.06           O  
ANISOU 4779  O   VAL C  10     2557   2894   3309     47    260    -86       O  
ATOM   4780  CB  VAL C  10      72.037  -1.849  -9.957  1.00 24.81           C  
ANISOU 4780  CB  VAL C  10     2753   3120   3551     23    244    -92       C  
ATOM   4781  CG1 VAL C  10      73.409  -1.909 -10.603  1.00 24.49           C  
ANISOU 4781  CG1 VAL C  10     2696   3088   3519     25    253    -87       C  
ATOM   4782  CG2 VAL C  10      72.213  -1.214  -8.563  1.00 24.74           C  
ANISOU 4782  CG2 VAL C  10     2739   3114   3547      6    233    -99       C  
ATOM   4783  N   GLY C  11      70.839  -0.749 -13.209  1.00 25.16           N  
ANISOU 4783  N   GLY C  11     2821   3155   3584     30    276    -75       N  
ATOM   4784  CA  GLY C  11      70.375  -1.190 -14.570  1.00 25.42           C  
ANISOU 4784  CA  GLY C  11     2863   3192   3603     39    286    -69       C  
ATOM   4785  C   GLY C  11      69.086  -0.463 -14.948  1.00 26.18           C  
ANISOU 4785  C   GLY C  11     2972   3279   3695     34    286    -60       C  
ATOM   4786  O   GLY C  11      67.996  -0.676 -14.408  1.00 26.45           O  
ANISOU 4786  O   GLY C  11     3019   3305   3725     37    276    -63       O  
ATOM   4787  N   SER C  12      69.191   0.435 -15.894  1.00 27.48           N  
ANISOU 4787  N   SER C  12     3133   3444   3861     27    296    -46       N  
ATOM   4788  CA  SER C  12      68.047   1.241 -16.199  1.00 26.49           C  
ANISOU 4788  CA  SER C  12     3018   3309   3738     22    296    -34       C  
ATOM   4789  C   SER C  12      67.580   0.867 -17.620  1.00 26.14           C  
ANISOU 4789  C   SER C  12     2979   3277   3673     24    302    -21       C  
ATOM   4790  O   SER C  12      67.177   1.741 -18.364  1.00 25.23           O  
ANISOU 4790  O   SER C  12     2864   3161   3561     16    307     -3       O  
ATOM   4791  CB  SER C  12      68.442   2.714 -16.171  1.00 26.70           C  
ANISOU 4791  CB  SER C  12     3033   3325   3786      9    301    -23       C  
ATOM   4792  OG  SER C  12      68.753   3.167 -14.863  1.00 27.70           O  
ANISOU 4792  OG  SER C  12     3155   3440   3929      4    295    -37       O  
ATOM   4793  N   GLY C  13      67.639  -0.418 -17.983  1.00 26.70           N  
ANISOU 4793  N   GLY C  13     3056   3360   3726     33    302    -32       N  
ATOM   4794  CA  GLY C  13      67.141  -0.868 -19.301  1.00 26.62           C  
ANISOU 4794  CA  GLY C  13     3055   3365   3694     33    308    -24       C  
ATOM   4795  C   GLY C  13      65.597  -1.030 -19.288  1.00 28.47           C  
ANISOU 4795  C   GLY C  13     3305   3592   3920     34    298    -18       C  
ATOM   4796  O   GLY C  13      64.892  -0.376 -18.472  1.00 28.19           O  
ANISOU 4796  O   GLY C  13     3271   3539   3898     32    290    -13       O  
ATOM   4797  N   MET C  14      65.050  -1.877 -20.163  1.00 29.16           N  
ANISOU 4797  N   MET C  14     3403   3691   3984     36    298    -19       N  
ATOM   4798  CA  MET C  14      63.572  -2.029 -20.268  1.00 32.42           C  
ANISOU 4798  CA  MET C  14     3829   4099   4387     35    288     -9       C  
ATOM   4799  C   MET C  14      62.937  -2.503 -18.963  1.00 30.81           C  
ANISOU 4799  C   MET C  14     3632   3879   4192     43    274    -20       C  
ATOM   4800  O   MET C  14      61.941  -1.992 -18.546  1.00 29.40           O  
ANISOU 4800  O   MET C  14     3457   3690   4021     41    267    -10       O  
ATOM   4801  CB  MET C  14      63.138  -2.940 -21.423  1.00 35.26           C  
ANISOU 4801  CB  MET C  14     4200   4478   4718     33    290    -11       C  
ATOM   4802  CG  MET C  14      63.686  -2.573 -22.819  1.00 35.39           C  
ANISOU 4802  CG  MET C  14     4210   4517   4718     22    304      0       C  
ATOM   4803  SD  MET C  14      63.482  -0.791 -23.021  1.00 46.51           S  
ANISOU 4803  SD  MET C  14     5607   5921   6144      9    305     33       S  
ATOM   4804  CE  MET C  14      61.775  -0.723 -23.554  1.00 45.36           C  
ANISOU 4804  CE  MET C  14     5472   5777   5985      1    294     56       C  
ATOM   4805  N   ILE C  15      63.519  -3.467 -18.299  1.00 31.23           N  
ANISOU 4805  N   ILE C  15     3685   3931   4248     52    271    -40       N  
ATOM   4806  CA  ILE C  15      62.886  -3.940 -17.084  1.00 31.96           C  
ANISOU 4806  CA  ILE C  15     3784   4013   4347     58    256    -47       C  
ATOM   4807  C   ILE C  15      62.900  -2.820 -16.010  1.00 30.59           C  
ANISOU 4807  C   ILE C  15     3602   3827   4193     54    254    -44       C  
ATOM   4808  O   ILE C  15      61.921  -2.624 -15.288  1.00 28.61           O  
ANISOU 4808  O   ILE C  15     3356   3568   3946     54    246    -42       O  
ATOM   4809  CB  ILE C  15      63.542  -5.226 -16.559  1.00 31.10           C  
ANISOU 4809  CB  ILE C  15     3674   3904   4239     67    251    -65       C  
ATOM   4810  CG1 ILE C  15      63.295  -6.378 -17.546  1.00 31.13           C  
ANISOU 4810  CG1 ILE C  15     3687   3915   4224     71    253    -71       C  
ATOM   4811  CG2 ILE C  15      63.023  -5.600 -15.184  1.00 29.26           C  
ANISOU 4811  CG2 ILE C  15     3441   3661   4012     70    236    -69       C  
ATOM   4812  CD1 ILE C  15      64.256  -7.531 -17.359  1.00 30.25           C  
ANISOU 4812  CD1 ILE C  15     3570   3803   4119     81    254    -89       C  
ATOM   4813  N   GLY C  16      64.023  -2.113 -15.925  1.00 31.12           N  
ANISOU 4813  N   GLY C  16     3656   3894   4272     50    263    -46       N  
ATOM   4814  CA  GLY C  16      64.220  -1.063 -14.913  1.00 29.12           C  
ANISOU 4814  CA  GLY C  16     3394   3630   4039     44    262    -47       C  
ATOM   4815  C   GLY C  16      63.176   0.032 -15.135  1.00 27.33           C  
ANISOU 4815  C   GLY C  16     3171   3392   3821     38    264    -33       C  
ATOM   4816  O   GLY C  16      62.641   0.589 -14.195  1.00 24.02           O  
ANISOU 4816  O   GLY C  16     2751   2960   3414     36    260    -37       O  
ATOM   4817  N   GLY C  17      62.918   0.308 -16.412  1.00 25.67           N  
ANISOU 4817  N   GLY C  17     2962   3187   3603     35    270    -15       N  
ATOM   4818  CA  GLY C  17      61.933   1.257 -16.834  1.00 26.68           C  
ANISOU 4818  CA  GLY C  17     3091   3306   3740     30    271      3       C  
ATOM   4819  C   GLY C  17      60.521   0.945 -16.371  1.00 26.92           C  
ANISOU 4819  C   GLY C  17     3131   3329   3767     35    262      5       C  
ATOM   4820  O   GLY C  17      59.831   1.836 -15.860  1.00 27.11           O  
ANISOU 4820  O   GLY C  17     3152   3338   3811     34    262     10       O  
ATOM   4821  N   VAL C  18      60.073  -0.301 -16.569  1.00 25.18           N  
ANISOU 4821  N   VAL C  18     2921   3120   3524     41    254      0       N  
ATOM   4822  CA  VAL C  18      58.732  -0.701 -16.146  1.00 26.36           C  
ANISOU 4822  CA  VAL C  18     3080   3266   3669     45    244      3       C  
ATOM   4823  C   VAL C  18      58.730  -0.717 -14.598  1.00 24.77           C  
ANISOU 4823  C   VAL C  18     2876   3055   3479     48    239    -14       C  
ATOM   4824  O   VAL C  18      57.787  -0.237 -13.950  1.00 25.83           O  
ANISOU 4824  O   VAL C  18     3010   3180   3624     49    237    -12       O  
ATOM   4825  CB  VAL C  18      58.307  -2.063 -16.730  1.00 26.46           C  
ANISOU 4825  CB  VAL C  18     3104   3291   3656     48    236      2       C  
ATOM   4826  CG1 VAL C  18      56.951  -2.525 -16.139  1.00 25.19           C  
ANISOU 4826  CG1 VAL C  18     2951   3126   3491     51    224      5       C  
ATOM   4827  CG2 VAL C  18      58.263  -1.975 -18.256  1.00 28.69           C  
ANISOU 4827  CG2 VAL C  18     3389   3587   3924     41    242     19       C  
ATOM   4828  N   MET C  19      59.799  -1.190 -13.987  1.00 25.76           N  
ANISOU 4828  N   MET C  19     2997   3185   3604     49    238    -31       N  
ATOM   4829  CA  MET C  19      59.840  -1.193 -12.478  1.00 23.45           C  
ANISOU 4829  CA  MET C  19     2701   2889   3319     49    233    -47       C  
ATOM   4830  C   MET C  19      59.634   0.183 -11.871  1.00 23.80           C  
ANISOU 4830  C   MET C  19     2738   2919   3384     44    239    -50       C  
ATOM   4831  O   MET C  19      58.903   0.361 -10.824  1.00 24.87           O  
ANISOU 4831  O   MET C  19     2874   3051   3524     43    236    -59       O  
ATOM   4832  CB  MET C  19      61.164  -1.720 -12.035  1.00 24.79           C  
ANISOU 4832  CB  MET C  19     2864   3065   3487     49    231    -61       C  
ATOM   4833  CG  MET C  19      61.262  -3.275 -12.188  1.00 25.47           C  
ANISOU 4833  CG  MET C  19     2957   3162   3558     57    222    -63       C  
ATOM   4834  SD  MET C  19      62.613  -3.914 -11.143  1.00 26.57           S  
ANISOU 4834  SD  MET C  19     3084   3308   3702     57    216    -77       S  
ATOM   4835  CE  MET C  19      64.025  -3.161 -11.943  1.00 26.10           C  
ANISOU 4835  CE  MET C  19     3014   3249   3653     54    231    -77       C  
ATOM   4836  N   ALA C  20      60.311   1.186 -12.460  1.00 22.18           N  
ANISOU 4836  N   ALA C  20     2526   2707   3194     38    250    -44       N  
ATOM   4837  CA  ALA C  20      60.215   2.536 -11.875  1.00 22.12           C  
ANISOU 4837  CA  ALA C  20     2510   2682   3211     32    257    -49       C  
ATOM   4838  C   ALA C  20      58.770   2.992 -11.965  1.00 21.86           C  
ANISOU 4838  C   ALA C  20     2480   2638   3187     36    258    -38       C  
ATOM   4839  O   ALA C  20      58.220   3.516 -11.026  1.00 23.94           O  
ANISOU 4839  O   ALA C  20     2741   2891   3463     35    260    -50       O  
ATOM   4840  CB  ALA C  20      61.143   3.514 -12.596  1.00 21.80           C  
ANISOU 4840  CB  ALA C  20     2460   2633   3187     25    267    -40       C  
ATOM   4841  N   THR C  21      58.169   2.832 -13.116  1.00 20.75           N  
ANISOU 4841  N   THR C  21     2343   2499   3039     39    257    -15       N  
ATOM   4842  CA  THR C  21      56.772   3.104 -13.295  1.00 21.40           C  
ANISOU 4842  CA  THR C  21     2427   2573   3128     42    256      0       C  
ATOM   4843  C   THR C  21      55.822   2.453 -12.304  1.00 21.95           C  
ANISOU 4843  C   THR C  21     2502   2647   3188     48    249    -11       C  
ATOM   4844  O   THR C  21      54.891   3.110 -11.837  1.00 23.09           O  
ANISOU 4844  O   THR C  21     2643   2779   3350     50    252    -11       O  
ATOM   4845  CB  THR C  21      56.344   2.537 -14.646  1.00 21.63           C  
ANISOU 4845  CB  THR C  21     2463   2615   3139     43    251     24       C  
ATOM   4846  OG1 THR C  21      57.177   3.109 -15.665  1.00 23.60           O  
ANISOU 4846  OG1 THR C  21     2706   2866   3393     36    258     38       O  
ATOM   4847  CG2 THR C  21      54.947   2.901 -14.930  1.00 22.29           C  
ANISOU 4847  CG2 THR C  21     2546   2692   3231     45    249     45       C  
ATOM   4848  N   LEU C  22      55.999   1.158 -12.048  1.00 22.52           N  
ANISOU 4848  N   LEU C  22     2583   2736   3235     50    238    -20       N  
ATOM   4849  CA  LEU C  22      55.153   0.431 -11.152  1.00 24.10           C  
ANISOU 4849  CA  LEU C  22     2788   2943   3424     54    230    -28       C  
ATOM   4850  C   LEU C  22      55.393   0.929  -9.725  1.00 24.40           C  
ANISOU 4850  C   LEU C  22     2819   2978   3473     51    234    -51       C  
ATOM   4851  O   LEU C  22      54.471   0.876  -8.877  1.00 25.30           O  
ANISOU 4851  O   LEU C  22     2932   3094   3586     52    232    -58       O  
ATOM   4852  CB  LEU C  22      55.438  -1.122 -11.213  1.00 24.95           C  
ANISOU 4852  CB  LEU C  22     2904   3068   3505     56    217    -30       C  
ATOM   4853  CG  LEU C  22      55.158  -1.912 -12.516  1.00 27.19           C  
ANISOU 4853  CG  LEU C  22     3197   3359   3773     58    212    -13       C  
ATOM   4854  CD1 LEU C  22      55.289  -3.411 -12.328  1.00 27.61           C  
ANISOU 4854  CD1 LEU C  22     3258   3423   3807     61    199    -20       C  
ATOM   4855  CD2 LEU C  22      53.727  -1.703 -13.046  1.00 30.41           C  
ANISOU 4855  CD2 LEU C  22     3609   3765   4181     59    209      6       C  
ATOM   4856  N   ILE C  23      56.620   1.373  -9.431  1.00 23.74           N  
ANISOU 4856  N   ILE C  23     2729   2892   3397     45    239    -65       N  
ATOM   4857  CA  ILE C  23      56.936   1.764  -8.039  1.00 23.49           C  
ANISOU 4857  CA  ILE C  23     2692   2862   3371     38    241    -90       C  
ATOM   4858  C   ILE C  23      56.185   3.075  -7.762  1.00 25.59           C  
ANISOU 4858  C   ILE C  23     2952   3108   3662     37    254    -96       C  
ATOM   4859  O   ILE C  23      55.736   3.330  -6.605  1.00 24.80           O  
ANISOU 4859  O   ILE C  23     2848   3009   3564     34    257   -115       O  
ATOM   4860  CB  ILE C  23      58.441   2.013  -7.883  1.00 22.43           C  
ANISOU 4860  CB  ILE C  23     2552   2729   3241     30    243   -102       C  
ATOM   4861  CG1 ILE C  23      59.155   0.683  -7.771  1.00 21.06           C  
ANISOU 4861  CG1 ILE C  23     2381   2575   3045     31    231   -101       C  
ATOM   4862  CG2 ILE C  23      58.734   2.941  -6.722  1.00 23.03           C  
ANISOU 4862  CG2 ILE C  23     2619   2799   3329     20    250   -126       C  
ATOM   4863  CD1 ILE C  23      60.621   0.726  -8.142  1.00 22.15           C  
ANISOU 4863  CD1 ILE C  23     2513   2715   3187     27    233   -103       C  
ATOM   4864  N   VAL C  24      56.002   3.861  -8.826  1.00 26.40           N  
ANISOU 4864  N   VAL C  24     3052   3193   3785     40    261    -77       N  
ATOM   4865  CA  VAL C  24      55.344   5.168  -8.685  1.00 28.06           C  
ANISOU 4865  CA  VAL C  24     3254   3379   4027     41    274    -79       C  
ATOM   4866  C   VAL C  24      53.840   4.921  -8.588  1.00 29.08           C  
ANISOU 4866  C   VAL C  24     3385   3509   4155     49    272    -69       C  
ATOM   4867  O   VAL C  24      53.159   5.484  -7.693  1.00 28.27           O  
ANISOU 4867  O   VAL C  24     3276   3398   4066     50    281    -86       O  
ATOM   4868  CB  VAL C  24      55.616   6.144  -9.869  1.00 28.79           C  
ANISOU 4868  CB  VAL C  24     3341   3452   4145     40    281    -56       C  
ATOM   4869  CG1 VAL C  24      54.717   7.427  -9.742  1.00 28.62           C  
ANISOU 4869  CG1 VAL C  24     3309   3402   4163     43    293    -54       C  
ATOM   4870  CG2 VAL C  24      57.087   6.566  -9.904  1.00 27.79           C  
ANISOU 4870  CG2 VAL C  24     3210   3322   4025     30    284    -66       C  
ATOM   4871  N   GLN C  25      53.323   4.055  -9.476  1.00 29.56           N  
ANISOU 4871  N   GLN C  25     3453   3581   4197     55    262    -44       N  
ATOM   4872  CA  GLN C  25      51.903   3.719  -9.427  1.00 28.95           C  
ANISOU 4872  CA  GLN C  25     3377   3507   4116     62    259    -32       C  
ATOM   4873  C   GLN C  25      51.603   3.304  -8.009  1.00 30.84           C  
ANISOU 4873  C   GLN C  25     3615   3758   4343     61    257    -58       C  
ATOM   4874  O   GLN C  25      50.588   3.690  -7.459  1.00 31.94           O  
ANISOU 4874  O   GLN C  25     3749   3892   4493     65    264    -62       O  
ATOM   4875  CB  GLN C  25      51.559   2.596 -10.362  1.00 29.46           C  
ANISOU 4875  CB  GLN C  25     3450   3587   4154     64    245     -9       C  
ATOM   4876  CG  GLN C  25      51.699   3.023 -11.815  1.00 31.66           C  
ANISOU 4876  CG  GLN C  25     3728   3859   4441     62    246     18       C  
ATOM   4877  CD  GLN C  25      50.572   3.936 -12.241  1.00 34.75           C  
ANISOU 4877  CD  GLN C  25     4109   4234   4858     66    252     41       C  
ATOM   4878  OE1 GLN C  25      49.386   3.630 -12.005  1.00 33.96           O  
ANISOU 4878  OE1 GLN C  25     4009   4137   4755     71    248     49       O  
ATOM   4879  NE2 GLN C  25      50.917   5.047 -12.923  1.00 33.82           N  
ANISOU 4879  NE2 GLN C  25     3983   4099   4768     64    260     55       N  
ATOM   4880  N   LYS C  26      52.506   2.584  -7.380  1.00 28.71           N  
ANISOU 4880  N   LYS C  26     3350   3505   4052     55    250    -75       N  
ATOM   4881  CA  LYS C  26      52.125   1.968  -6.151  1.00 29.62           C  
ANISOU 4881  CA  LYS C  26     3465   3637   4149     52    245    -92       C  
ATOM   4882  C   LYS C  26      52.618   2.731  -4.953  1.00 28.91           C  
ANISOU 4882  C   LYS C  26     3367   3546   4068     44    255   -123       C  
ATOM   4883  O   LYS C  26      52.475   2.249  -3.867  1.00 27.44           O  
ANISOU 4883  O   LYS C  26     3181   3380   3865     38    251   -139       O  
ATOM   4884  CB  LYS C  26      52.630   0.520  -6.096  1.00 31.08           C  
ANISOU 4884  CB  LYS C  26     3659   3845   4305     50    228    -87       C  
ATOM   4885  CG  LYS C  26      51.967  -0.399  -7.097  1.00 29.51           C  
ANISOU 4885  CG  LYS C  26     3468   3650   4093     57    217    -61       C  
ATOM   4886  CD  LYS C  26      52.908  -1.602  -7.177  1.00 30.80           C  
ANISOU 4886  CD  LYS C  26     3638   3828   4237     54    203    -61       C  
ATOM   4887  CE  LYS C  26      52.272  -2.794  -7.795  1.00 31.81           C  
ANISOU 4887  CE  LYS C  26     3775   3963   4347     58    189    -43       C  
ATOM   4888  NZ  LYS C  26      50.966  -3.187  -7.190  1.00 36.00           N  
ANISOU 4888  NZ  LYS C  26     4304   4501   4869     59    183    -37       N  
ATOM   4889  N   ASN C  27      53.076   3.965  -5.172  1.00 29.63           N  
ANISOU 4889  N   ASN C  27     3453   3615   4188     41    269   -132       N  
ATOM   4890  CA  ASN C  27      53.714   4.797  -4.165  1.00 30.08           C  
ANISOU 4890  CA  ASN C  27     3503   3668   4256     31    280   -164       C  
ATOM   4891  C   ASN C  27      54.778   4.080  -3.306  1.00 29.59           C  
ANISOU 4891  C   ASN C  27     3443   3632   4167     18    269   -181       C  
ATOM   4892  O   ASN C  27      54.873   4.380  -2.129  1.00 29.82           O  
ANISOU 4892  O   ASN C  27     3467   3669   4191      8    274   -208       O  
ATOM   4893  CB  ASN C  27      52.660   5.485  -3.250  1.00 30.79           C  
ANISOU 4893  CB  ASN C  27     3586   3751   4359     32    293   -185       C  
ATOM   4894  CG  ASN C  27      53.149   6.817  -2.616  1.00 31.22           C  
ANISOU 4894  CG  ASN C  27     3633   3788   4442     23    311   -217       C  
ATOM   4895  OD1 ASN C  27      53.971   7.552  -3.169  1.00 33.54           O  
ANISOU 4895  OD1 ASN C  27     3925   4061   4757     19    315   -216       O  
ATOM   4896  ND2 ASN C  27      52.591   7.145  -1.486  1.00 32.73           N  
ANISOU 4896  ND2 ASN C  27     3819   3985   4632     18    321   -247       N  
ATOM   4897  N   LEU C  28      55.587   3.160  -3.858  1.00 29.02           N  
ANISOU 4897  N   LEU C  28     3376   3570   4078     19    256   -165       N  
ATOM   4898  CA  LEU C  28      56.470   2.366  -2.972  1.00 29.52           C  
ANISOU 4898  CA  LEU C  28     3438   3660   4118      8    244   -176       C  
ATOM   4899  C   LEU C  28      57.675   3.045  -2.357  1.00 29.82           C  
ANISOU 4899  C   LEU C  28     3470   3698   4162     -6    248   -198       C  
ATOM   4900  O   LEU C  28      58.087   2.709  -1.254  1.00 31.05           O  
ANISOU 4900  O   LEU C  28     3620   3875   4299    -19    241   -214       O  
ATOM   4901  CB  LEU C  28      56.950   1.062  -3.589  1.00 30.07           C  
ANISOU 4901  CB  LEU C  28     3513   3741   4169     13    228   -155       C  
ATOM   4902  CG  LEU C  28      55.856   0.103  -3.981  1.00 29.58           C  
ANISOU 4902  CG  LEU C  28     3458   3685   4094     24    219   -135       C  
ATOM   4903  CD1 LEU C  28      56.500  -1.217  -4.400  1.00 29.56           C  
ANISOU 4903  CD1 LEU C  28     3460   3694   4075     27    203   -121       C  
ATOM   4904  CD2 LEU C  28      54.913  -0.121  -2.827  1.00 29.92           C  
ANISOU 4904  CD2 LEU C  28     3499   3744   4125     19    216   -145       C  
ATOM   4905  N   GLY C  29      58.277   3.979  -3.061  1.00 28.89           N  
ANISOU 4905  N   GLY C  29     3350   3558   4069     -6    258   -197       N  
ATOM   4906  CA  GLY C  29      59.324   4.748  -2.422  1.00 29.17           C  
ANISOU 4906  CA  GLY C  29     3378   3592   4113    -22    262   -220       C  
ATOM   4907  C   GLY C  29      60.057   5.557  -3.435  1.00 27.75           C  
ANISOU 4907  C   GLY C  29     3196   3389   3958    -21    270   -210       C  
ATOM   4908  O   GLY C  29      59.708   5.561  -4.628  1.00 25.51           O  
ANISOU 4908  O   GLY C  29     2915   3091   3684     -8    272   -185       O  
ATOM   4909  N   ASP C  30      61.084   6.244  -2.972  1.00 28.17           N  
ANISOU 4909  N   ASP C  30     3242   3439   4021    -36    273   -227       N  
ATOM   4910  CA  ASP C  30      61.945   6.960  -3.903  1.00 29.92           C  
ANISOU 4910  CA  ASP C  30     3460   3642   4265    -37    278   -216       C  
ATOM   4911  C   ASP C  30      62.732   5.903  -4.764  1.00 29.98           C  
ANISOU 4911  C   ASP C  30     3468   3665   4255    -31    267   -190       C  
ATOM   4912  O   ASP C  30      63.038   4.799  -4.295  1.00 30.35           O  
ANISOU 4912  O   ASP C  30     3517   3737   4278    -31    255   -190       O  
ATOM   4913  CB  ASP C  30      62.823   7.938  -3.145  1.00 30.51           C  
ANISOU 4913  CB  ASP C  30     3527   3711   4354    -57    284   -242       C  
ATOM   4914  CG  ASP C  30      61.992   9.022  -2.360  1.00 34.54           C  
ANISOU 4914  CG  ASP C  30     4036   4201   4885    -62    297   -271       C  
ATOM   4915  OD1 ASP C  30      60.857   9.385  -2.791  1.00 33.05           O  
ANISOU 4915  OD1 ASP C  30     3850   3992   4713    -49    307   -264       O  
ATOM   4916  OD2 ASP C  30      62.456   9.475  -1.259  1.00 36.45           O  
ANISOU 4916  OD2 ASP C  30     4273   4450   5124    -81    299   -303       O  
ATOM   4917  N   VAL C  31      62.956   6.256  -6.030  1.00 30.95           N  
ANISOU 4917  N   VAL C  31     3591   3773   4393    -24    272   -168       N  
ATOM   4918  CA  VAL C  31      63.551   5.439  -7.093  1.00 30.17           C  
ANISOU 4918  CA  VAL C  31     3494   3685   4283    -16    267   -145       C  
ATOM   4919  C   VAL C  31      64.773   6.132  -7.644  1.00 29.43           C  
ANISOU 4919  C   VAL C  31     3391   3585   4205    -24    272   -139       C  
ATOM   4920  O   VAL C  31      64.717   7.298  -7.990  1.00 31.47           O  
ANISOU 4920  O   VAL C  31     3645   3821   4489    -29    282   -137       O  
ATOM   4921  CB  VAL C  31      62.621   5.364  -8.318  1.00 30.71           C  
ANISOU 4921  CB  VAL C  31     3568   3744   4354     -3    271   -121       C  
ATOM   4922  CG1 VAL C  31      63.276   4.534  -9.420  1.00 29.23           C  
ANISOU 4922  CG1 VAL C  31     3382   3570   4152      2    267   -101       C  
ATOM   4923  CG2 VAL C  31      61.334   4.717  -7.943  1.00 29.03           C  
ANISOU 4923  CG2 VAL C  31     3365   3537   4128      5    266   -122       C  
ATOM   4924  N   VAL C  32      65.880   5.412  -7.742  1.00 30.10           N  
ANISOU 4924  N   VAL C  32     3471   3688   4277    -26    266   -135       N  
ATOM   4925  CA  VAL C  32      67.072   5.881  -8.455  1.00 26.58           C  
ANISOU 4925  CA  VAL C  32     3015   3240   3842    -32    271   -125       C  
ATOM   4926  C   VAL C  32      67.241   4.849  -9.552  1.00 25.68           C  
ANISOU 4926  C   VAL C  32     2904   3141   3712    -19    270   -105       C  
ATOM   4927  O   VAL C  32      67.348   3.646  -9.264  1.00 24.84           O  
ANISOU 4927  O   VAL C  32     2800   3051   3585    -12    261   -108       O  
ATOM   4928  CB  VAL C  32      68.385   5.797  -7.657  1.00 27.39           C  
ANISOU 4928  CB  VAL C  32     3106   3356   3942    -45    266   -137       C  
ATOM   4929  CG1 VAL C  32      69.582   6.292  -8.538  1.00 26.00           C  
ANISOU 4929  CG1 VAL C  32     2919   3179   3779    -50    272   -122       C  
ATOM   4930  CG2 VAL C  32      68.330   6.520  -6.297  1.00 26.23           C  
ANISOU 4930  CG2 VAL C  32     2958   3205   3803    -61    264   -163       C  
ATOM   4931  N   LEU C  33      67.254   5.342 -10.784  1.00 24.35           N  
ANISOU 4931  N   LEU C  33     2735   2965   3552    -17    278    -86       N  
ATOM   4932  CA  LEU C  33      67.536   4.580 -11.950  1.00 23.54           C  
ANISOU 4932  CA  LEU C  33     2632   2875   3434     -8    281    -69       C  
ATOM   4933  C   LEU C  33      69.042   4.722 -12.150  1.00 24.66           C  
ANISOU 4933  C   LEU C  33     2761   3027   3581    -15    284    -67       C  
ATOM   4934  O   LEU C  33      69.560   5.800 -12.426  1.00 26.39           O  
ANISOU 4934  O   LEU C  33     2971   3237   3819    -26    291    -60       O  
ATOM   4935  CB  LEU C  33      66.773   5.124 -13.130  1.00 22.99           C  
ANISOU 4935  CB  LEU C  33     2567   2797   3370     -6    288    -47       C  
ATOM   4936  CG  LEU C  33      65.315   4.611 -13.088  1.00 24.17           C  
ANISOU 4936  CG  LEU C  33     2730   2944   3509      3    283    -46       C  
ATOM   4937  CD1 LEU C  33      64.419   5.549 -13.802  1.00 23.95           C  
ANISOU 4937  CD1 LEU C  33     2702   2899   3495      2    288    -27       C  
ATOM   4938  CD2 LEU C  33      65.232   3.196 -13.720  1.00 23.15           C  
ANISOU 4938  CD2 LEU C  33     2609   2835   3352     14    279    -42       C  
ATOM   4939  N   PHE C  34      69.778   3.649 -11.993  1.00 24.03           N  
ANISOU 4939  N   PHE C  34     2677   2965   3487    -10    280    -72       N  
ATOM   4940  CA  PHE C  34      71.203   3.781 -12.185  1.00 25.02           C  
ANISOU 4940  CA  PHE C  34     2786   3099   3618    -16    284    -69       C  
ATOM   4941  C   PHE C  34      71.661   3.047 -13.391  1.00 25.05           C  
ANISOU 4941  C   PHE C  34     2788   3119   3610     -6    292    -57       C  
ATOM   4942  O   PHE C  34      71.147   1.998 -13.670  1.00 26.87           O  
ANISOU 4942  O   PHE C  34     3027   3356   3824      5    290    -59       O  
ATOM   4943  CB  PHE C  34      71.961   3.261 -10.975  1.00 23.76           C  
ANISOU 4943  CB  PHE C  34     2618   2950   3457    -20    274    -83       C  
ATOM   4944  CG  PHE C  34      73.386   2.940 -11.273  1.00 24.37           C  
ANISOU 4944  CG  PHE C  34     2679   3042   3537    -21    278    -77       C  
ATOM   4945  CD1 PHE C  34      74.347   3.926 -11.214  1.00 24.62           C  
ANISOU 4945  CD1 PHE C  34     2697   3072   3584    -36    281    -74       C  
ATOM   4946  CD2 PHE C  34      73.759   1.662 -11.642  1.00 24.45           C  
ANISOU 4946  CD2 PHE C  34     2687   3066   3536     -6    277    -75       C  
ATOM   4947  CE1 PHE C  34      75.651   3.649 -11.484  1.00 26.49           C  
ANISOU 4947  CE1 PHE C  34     2916   3323   3823    -36    285    -67       C  
ATOM   4948  CE2 PHE C  34      75.059   1.390 -11.958  1.00 25.63           C  
ANISOU 4948  CE2 PHE C  34     2818   3229   3690     -6    283    -70       C  
ATOM   4949  CZ  PHE C  34      76.011   2.363 -11.865  1.00 26.75           C  
ANISOU 4949  CZ  PHE C  34     2945   3371   3845    -21    286    -65       C  
ATOM   4950  N   ASP C  35      72.691   3.535 -14.046  1.00 26.46           N  
ANISOU 4950  N   ASP C  35     2952   3304   3795    -13    301    -47       N  
ATOM   4951  CA  ASP C  35      73.288   2.843 -15.185  1.00 29.11           C  
ANISOU 4951  CA  ASP C  35     3283   3658   4119     -5    311    -39       C  
ATOM   4952  C   ASP C  35      74.601   3.495 -15.564  1.00 29.78           C  
ANISOU 4952  C   ASP C  35     3348   3751   4214    -15    320    -29       C  
ATOM   4953  O   ASP C  35      74.788   4.687 -15.349  1.00 28.85           O  
ANISOU 4953  O   ASP C  35     3224   3622   4113    -29    320    -23       O  
ATOM   4954  CB  ASP C  35      72.379   2.911 -16.411  1.00 30.32           C  
ANISOU 4954  CB  ASP C  35     3448   3813   4260     -1    319    -26       C  
ATOM   4955  CG  ASP C  35      72.534   1.666 -17.302  1.00 34.68           C  
ANISOU 4955  CG  ASP C  35     4002   4385   4790     10    326    -29       C  
ATOM   4956  OD1 ASP C  35      73.467   1.599 -18.159  1.00 32.15           O  
ANISOU 4956  OD1 ASP C  35     3669   4081   4465      9    338    -23       O  
ATOM   4957  OD2 ASP C  35      71.700   0.733 -17.124  1.00 37.21           O  
ANISOU 4957  OD2 ASP C  35     4337   4703   5099     21    319    -38       O  
ATOM   4958  N   ILE C  36      75.499   2.743 -16.167  1.00 30.08           N  
ANISOU 4958  N   ILE C  36     3375   3808   4244     -7    329    -28       N  
ATOM   4959  CA  ILE C  36      76.743   3.366 -16.605  1.00 32.52           C  
ANISOU 4959  CA  ILE C  36     3664   4128   4562    -17    338    -17       C  
ATOM   4960  C   ILE C  36      76.554   4.126 -17.917  1.00 35.70           C  
ANISOU 4960  C   ILE C  36     4066   4536   4960    -25    350      2       C  
ATOM   4961  O   ILE C  36      77.370   4.986 -18.259  1.00 37.02           O  
ANISOU 4961  O   ILE C  36     4218   4708   5139    -37    356     16       O  
ATOM   4962  CB  ILE C  36      77.842   2.328 -16.777  1.00 34.79           C  
ANISOU 4962  CB  ILE C  36     3936   4434   4845     -6    345    -23       C  
ATOM   4963  CG1 ILE C  36      77.544   1.433 -17.981  1.00 34.65           C  
ANISOU 4963  CG1 ILE C  36     3925   4431   4807      6    358    -25       C  
ATOM   4964  CG2 ILE C  36      78.085   1.554 -15.471  1.00 31.18           C  
ANISOU 4964  CG2 ILE C  36     3477   3973   4395      0    331    -37       C  
ATOM   4965  CD1 ILE C  36      78.463   0.238 -18.022  1.00 36.84           C  
ANISOU 4965  CD1 ILE C  36     4191   4723   5084     21    365    -36       C  
ATOM   4966  N   VAL C  37      75.463   3.845 -18.637  1.00 35.35           N  
ANISOU 4966  N   VAL C  37     4037   4492   4899    -19    352      5       N  
ATOM   4967  CA  VAL C  37      75.213   4.523 -19.898  1.00 37.66           C  
ANISOU 4967  CA  VAL C  37     4329   4794   5185    -28    362     27       C  
ATOM   4968  C   VAL C  37      74.821   5.941 -19.521  1.00 41.35           C  
ANISOU 4968  C   VAL C  37     4795   5238   5677    -42    355     42       C  
ATOM   4969  O   VAL C  37      73.998   6.105 -18.642  1.00 41.51           O  
ANISOU 4969  O   VAL C  37     4827   5236   5707    -40    344     32       O  
ATOM   4970  CB  VAL C  37      74.083   3.809 -20.662  1.00 37.73           C  
ANISOU 4970  CB  VAL C  37     4355   4810   5169    -19    363     27       C  
ATOM   4971  CG1 VAL C  37      73.431   4.721 -21.696  1.00 38.04           C  
ANISOU 4971  CG1 VAL C  37     4395   4852   5205    -32    367     54       C  
ATOM   4972  CG2 VAL C  37      74.604   2.511 -21.288  1.00 37.71           C  
ANISOU 4972  CG2 VAL C  37     4350   4831   5144     -7    374     13       C  
ATOM   4973  N   LYS C  38      75.398   6.961 -20.165  1.00 41.18           N  
ANISOU 4973  N   LYS C  38     4759   5219   5666    -57    361     64       N  
ATOM   4974  CA  LYS C  38      75.222   8.359 -19.735  1.00 41.00           C  
ANISOU 4974  CA  LYS C  38     4732   5171   5674    -72    355     77       C  
ATOM   4975  C   LYS C  38      73.871   8.910 -20.125  1.00 40.89           C  
ANISOU 4975  C   LYS C  38     4729   5140   5664    -74    351     92       C  
ATOM   4976  O   LYS C  38      73.374   8.536 -21.175  1.00 41.33           O  
ANISOU 4976  O   LYS C  38     4790   5214   5699    -71    356    106       O  
ATOM   4977  CB  LYS C  38      76.293   9.254 -20.385  1.00 43.06           C  
ANISOU 4977  CB  LYS C  38     4972   5441   5947    -89    363    100       C  
ATOM   4978  CG  LYS C  38      77.707   9.060 -19.864  1.00 44.52           C  
ANISOU 4978  CG  LYS C  38     5140   5636   6137    -91    365     89       C  
ATOM   4979  CD  LYS C  38      77.799   9.532 -18.417  1.00 50.80           C  
ANISOU 4979  CD  LYS C  38     5937   6405   6957    -97    352     71       C  
ATOM   4980  CE  LYS C  38      78.813   8.729 -17.633  1.00 53.03           C  
ANISOU 4980  CE  LYS C  38     6212   6702   7235    -92    350     51       C  
ATOM   4981  NZ  LYS C  38      80.163   8.916 -18.233  1.00 49.82           N  
ANISOU 4981  NZ  LYS C  38     5782   6316   6830   -100    360     67       N  
ATOM   4982  N   ASN C  39      73.296   9.820 -19.312  1.00 41.08           N  
ANISOU 4982  N   ASN C  39     4757   5131   5717    -79    343     89       N  
ATOM   4983  CA  ASN C  39      72.060  10.585 -19.686  1.00 43.24           C  
ANISOU 4983  CA  ASN C  39     5036   5385   6005    -82    340    109       C  
ATOM   4984  C   ASN C  39      70.705   9.824 -19.783  1.00 40.63           C  
ANISOU 4984  C   ASN C  39     4724   5055   5656    -68    336    104       C  
ATOM   4985  O   ASN C  39      69.684  10.344 -19.387  1.00 39.04           O  
ANISOU 4985  O   ASN C  39     4529   4829   5473    -67    331    106       O  
ATOM   4986  CB  ASN C  39      72.226  11.340 -21.032  1.00 47.53           C  
ANISOU 4986  CB  ASN C  39     5567   5939   6553    -95    346    148       C  
ATOM   4987  CG  ASN C  39      73.543  12.077 -21.149  1.00 55.25           C  
ANISOU 4987  CG  ASN C  39     6525   6920   7547   -110    350    159       C  
ATOM   4988  OD1 ASN C  39      74.002  12.708 -20.181  1.00 56.96           O  
ANISOU 4988  OD1 ASN C  39     6736   7112   7791   -117    346    145       O  
ATOM   4989  ND2 ASN C  39      74.155  12.026 -22.354  1.00 54.77           N  
ANISOU 4989  ND2 ASN C  39     6451   6889   7467   -118    359    184       N  
ATOM   4990  N   MET C  40      70.695   8.634 -20.381  1.00 39.96           N  
ANISOU 4990  N   MET C  40     4647   4999   5537    -59    340    100       N  
ATOM   4991  CA  MET C  40      69.442   7.871 -20.561  1.00 38.76           C  
ANISOU 4991  CA  MET C  40     4512   4851   5365    -48    335     97       C  
ATOM   4992  C   MET C  40      68.691   7.649 -19.206  1.00 35.39           C  
ANISOU 4992  C   MET C  40     4097   4400   4949    -38    326     72       C  
ATOM   4993  O   MET C  40      67.487   7.907 -19.129  1.00 35.51           O  
ANISOU 4993  O   MET C  40     4120   4400   4971    -35    321     79       O  
ATOM   4994  CB  MET C  40      69.730   6.603 -21.377  1.00 38.93           C  
ANISOU 4994  CB  MET C  40     4538   4905   5349    -41    341     92       C  
ATOM   4995  CG  MET C  40      68.659   5.518 -21.422  1.00 39.66           C  
ANISOU 4995  CG  MET C  40     4648   5003   5417    -29    336     81       C  
ATOM   4996  SD  MET C  40      68.542   4.648 -19.850  1.00 41.83           S  
ANISOU 4996  SD  MET C  40     4934   5263   5696    -14    326     45       S  
ATOM   4997  CE  MET C  40      69.614   3.214 -20.130  1.00 36.90           C  
ANISOU 4997  CE  MET C  40     4308   4665   5047     -5    333     25       C  
ATOM   4998  N   PRO C  41      69.394   7.270 -18.118  1.00 34.44           N  
ANISOU 4998  N   PRO C  41     3976   4277   4832    -34    323     45       N  
ATOM   4999  CA  PRO C  41      68.644   7.129 -16.865  1.00 32.61           C  
ANISOU 4999  CA  PRO C  41     3755   4028   4608    -28    315     23       C  
ATOM   5000  C   PRO C  41      68.007   8.440 -16.389  1.00 33.22           C  
ANISOU 5000  C   PRO C  41     3829   4074   4718    -36    314     28       C  
ATOM   5001  O   PRO C  41      66.873   8.430 -15.904  1.00 30.88           O  
ANISOU 5001  O   PRO C  41     3542   3764   4425    -29    309     21       O  
ATOM   5002  CB  PRO C  41      69.678   6.611 -15.872  1.00 32.10           C  
ANISOU 5002  CB  PRO C  41     3685   3969   4540    -28    312      0       C  
ATOM   5003  CG  PRO C  41      70.986   6.819 -16.519  1.00 31.54           C  
ANISOU 5003  CG  PRO C  41     3600   3913   4471    -35    319     10       C  
ATOM   5004  CD  PRO C  41      70.755   6.724 -17.977  1.00 35.28           C  
ANISOU 5004  CD  PRO C  41     4073   4401   4929    -35    327     33       C  
ATOM   5005  N   HIS C  42      68.716   9.562 -16.560  1.00 32.77           N  
ANISOU 5005  N   HIS C  42     3759   4006   4686    -49    318     39       N  
ATOM   5006  CA  HIS C  42      68.143  10.843 -16.227  1.00 32.71           C  
ANISOU 5006  CA  HIS C  42     3747   3965   4715    -56    318     44       C  
ATOM   5007  C   HIS C  42      66.908  11.129 -17.047  1.00 30.78           C  
ANISOU 5007  C   HIS C  42     3506   3712   4475    -52    318     70       C  
ATOM   5008  O   HIS C  42      65.935  11.646 -16.508  1.00 29.74           O  
ANISOU 5008  O   HIS C  42     3377   3555   4365    -48    317     65       O  
ATOM   5009  CB  HIS C  42      69.185  11.949 -16.384  1.00 33.33           C  
ANISOU 5009  CB  HIS C  42     3810   4033   4821    -72    322     54       C  
ATOM   5010  CG  HIS C  42      70.373  11.771 -15.496  1.00 34.33           C  
ANISOU 5010  CG  HIS C  42     3932   4167   4946    -79    321     29       C  
ATOM   5011  ND1 HIS C  42      70.347  12.061 -14.164  1.00 34.81           N  
ANISOU 5011  ND1 HIS C  42     3995   4209   5019    -83    317      0       N  
ATOM   5012  CD2 HIS C  42      71.636  11.294 -15.771  1.00 33.72           C  
ANISOU 5012  CD2 HIS C  42     3845   4113   4851    -82    323     31       C  
ATOM   5013  CE1 HIS C  42      71.546  11.804 -13.623  1.00 34.16           C  
ANISOU 5013  CE1 HIS C  42     3906   4142   4931    -90    315    -14       C  
ATOM   5014  NE2 HIS C  42      72.338  11.330 -14.600  1.00 37.47           N  
ANISOU 5014  NE2 HIS C  42     4317   4585   5333    -89    318      5       N  
ATOM   5015  N   GLY C  43      66.935  10.829 -18.359  1.00 30.70           N  
ANISOU 5015  N   GLY C  43     3494   3724   4446    -53    320     98       N  
ATOM   5016  CA  GLY C  43      65.759  11.048 -19.209  1.00 27.57           C  
ANISOU 5016  CA  GLY C  43     3099   3324   4050    -51    319    127       C  
ATOM   5017  C   GLY C  43      64.533  10.212 -18.823  1.00 28.63           C  
ANISOU 5017  C   GLY C  43     3249   3460   4168    -37    313    115       C  
ATOM   5018  O   GLY C  43      63.400  10.739 -18.734  1.00 28.39           O  
ANISOU 5018  O   GLY C  43     3219   3408   4158    -34    311    126       O  
ATOM   5019  N   LYS C  44      64.751   8.897 -18.650  1.00 26.81           N  
ANISOU 5019  N   LYS C  44     3030   3254   3903    -29    311     95       N  
ATOM   5020  CA  LYS C  44      63.758   7.974 -18.174  1.00 26.96           C  
ANISOU 5020  CA  LYS C  44     3063   3275   3903    -16    305     80       C  
ATOM   5021  C   LYS C  44      63.242   8.396 -16.817  1.00 25.84           C  
ANISOU 5021  C   LYS C  44     2924   3107   3785    -12    303     57       C  
ATOM   5022  O   LYS C  44      62.071   8.295 -16.589  1.00 25.34           O  
ANISOU 5022  O   LYS C  44     2867   3035   3724     -5    299     59       O  
ATOM   5023  CB  LYS C  44      64.283   6.527 -18.041  1.00 27.78           C  
ANISOU 5023  CB  LYS C  44     3176   3404   3973     -9    303     59       C  
ATOM   5024  CG  LYS C  44      64.686   5.900 -19.344  1.00 30.59           C  
ANISOU 5024  CG  LYS C  44     3532   3788   4300    -11    307     73       C  
ATOM   5025  CD  LYS C  44      64.743   4.358 -19.194  1.00 30.68           C  
ANISOU 5025  CD  LYS C  44     3555   3818   4281     -1    304     51       C  
ATOM   5026  CE  LYS C  44      65.142   3.722 -20.528  1.00 31.09           C  
ANISOU 5026  CE  LYS C  44     3608   3899   4305     -4    310     61       C  
ATOM   5027  NZ  LYS C  44      65.318   2.226 -20.410  1.00 30.48           N  
ANISOU 5027  NZ  LYS C  44     3540   3836   4203      6    308     37       N  
ATOM   5028  N   ALA C  45      64.109   8.795 -15.908  1.00 26.13           N  
ANISOU 5028  N   ALA C  45     2955   3134   3837    -17    305     36       N  
ATOM   5029  CA  ALA C  45      63.628   9.118 -14.582  1.00 27.11           C  
ANISOU 5029  CA  ALA C  45     3082   3239   3979    -15    303     10       C  
ATOM   5030  C   ALA C  45      62.812  10.403 -14.715  1.00 28.45           C  
ANISOU 5030  C   ALA C  45     3244   3377   4186    -18    308     25       C  
ATOM   5031  O   ALA C  45      61.817  10.559 -14.003  1.00 29.81           O  
ANISOU 5031  O   ALA C  45     3421   3534   4370    -11    308     12       O  
ATOM   5032  CB  ALA C  45      64.811   9.317 -13.607  1.00 27.96           C  
ANISOU 5032  CB  ALA C  45     3185   3346   4093    -24    304    -15       C  
ATOM   5033  N   LEU C  46      63.196  11.314 -15.631  1.00 27.44           N  
ANISOU 5033  N   LEU C  46     3105   3240   4080    -26    312     52       N  
ATOM   5034  CA  LEU C  46      62.412  12.529 -15.736  1.00 28.26           C  
ANISOU 5034  CA  LEU C  46     3200   3310   4225    -28    316     68       C  
ATOM   5035  C   LEU C  46      60.973  12.289 -16.342  1.00 28.49           C  
ANISOU 5035  C   LEU C  46     3233   3341   4251    -18    312     93       C  
ATOM   5036  O   LEU C  46      59.967  12.842 -15.883  1.00 26.87           O  
ANISOU 5036  O   LEU C  46     3025   3109   4073    -12    314     91       O  
ATOM   5037  CB  LEU C  46      63.220  13.581 -16.488  1.00 28.88           C  
ANISOU 5037  CB  LEU C  46     3263   3378   4331    -42    319     94       C  
ATOM   5038  CG  LEU C  46      62.569  14.931 -16.672  1.00 32.06           C  
ANISOU 5038  CG  LEU C  46     3654   3743   4784    -45    322    115       C  
ATOM   5039  CD1 LEU C  46      62.314  15.573 -15.297  1.00 31.10           C  
ANISOU 5039  CD1 LEU C  46     3532   3587   4695    -43    328     77       C  
ATOM   5040  CD2 LEU C  46      63.405  15.820 -17.647  1.00 32.20           C  
ANISOU 5040  CD2 LEU C  46     3654   3755   4823    -60    323    149       C  
ATOM   5041  N   ASP C  47      60.876  11.435 -17.345  1.00 28.94           N  
ANISOU 5041  N   ASP C  47     3295   3427   4273    -17    307    114       N  
ATOM   5042  CA  ASP C  47      59.583  11.041 -17.887  1.00 30.27           C  
ANISOU 5042  CA  ASP C  47     3468   3602   4431    -10    302    136       C  
ATOM   5043  C   ASP C  47      58.743  10.324 -16.807  1.00 30.54           C  
ANISOU 5043  C   ASP C  47     3515   3634   4454      2    299    106       C  
ATOM   5044  O   ASP C  47      57.519  10.531 -16.665  1.00 29.04           O  
ANISOU 5044  O   ASP C  47     3323   3430   4278      9    298    115       O  
ATOM   5045  CB  ASP C  47      59.841  10.113 -19.090  1.00 30.19           C  
ANISOU 5045  CB  ASP C  47     3463   3628   4378    -14    298    156       C  
ATOM   5046  CG  ASP C  47      58.567   9.656 -19.818  1.00 31.33           C  
ANISOU 5046  CG  ASP C  47     3611   3784   4506    -10    291    181       C  
ATOM   5047  OD1 ASP C  47      57.483  10.328 -19.730  1.00 28.21           O  
ANISOU 5047  OD1 ASP C  47     3211   3368   4140     -7    289    198       O  
ATOM   5048  OD2 ASP C  47      58.682   8.583 -20.529  1.00 32.22           O  
ANISOU 5048  OD2 ASP C  47     3734   3930   4577    -12    287    184       O  
ATOM   5049  N   THR C  48      59.402   9.477 -16.024  1.00 30.26           N  
ANISOU 5049  N   THR C  48     3488   3613   4394      4    298     74       N  
ATOM   5050  CA  THR C  48      58.631   8.704 -15.043  1.00 28.81           C  
ANISOU 5050  CA  THR C  48     3316   3433   4197     14    294     49       C  
ATOM   5051  C   THR C  48      58.133   9.577 -13.893  1.00 29.38           C  
ANISOU 5051  C   THR C  48     3382   3477   4302     16    300     29       C  
ATOM   5052  O   THR C  48      57.024   9.348 -13.379  1.00 29.35           O  
ANISOU 5052  O   THR C  48     3382   3469   4298     24    299     23       O  
ATOM   5053  CB  THR C  48      59.430   7.528 -14.506  1.00 27.22           C  
ANISOU 5053  CB  THR C  48     3123   3255   3961     15    289     24       C  
ATOM   5054  OG1 THR C  48      59.889   6.767 -15.621  1.00 28.24           O  
ANISOU 5054  OG1 THR C  48     3256   3408   4063     14    286     41       O  
ATOM   5055  CG2 THR C  48      58.585   6.652 -13.616  1.00 26.01           C  
ANISOU 5055  CG2 THR C  48     2980   3109   3791     24    283      6       C  
ATOM   5056  N   SER C  49      58.916  10.595 -13.533  1.00 28.77           N  
ANISOU 5056  N   SER C  49     3296   3380   4254      8    308     18       N  
ATOM   5057  CA  SER C  49      58.565  11.501 -12.395  1.00 27.09           C  
ANISOU 5057  CA  SER C  49     3078   3138   4075      7    316     -8       C  
ATOM   5058  C   SER C  49      57.205  12.197 -12.520  1.00 26.16           C  
ANISOU 5058  C   SER C  49     2954   2995   3990     16    321      6       C  
ATOM   5059  O   SER C  49      56.460  12.351 -11.531  1.00 23.94           O  
ANISOU 5059  O   SER C  49     2673   2702   3720     22    326    -18       O  
ATOM   5060  CB  SER C  49      59.647  12.532 -12.172  1.00 28.70           C  
ANISOU 5060  CB  SER C  49     3272   3323   4308     -4    322    -18       C  
ATOM   5061  OG  SER C  49      59.755  13.401 -13.321  1.00 28.27           O  
ANISOU 5061  OG  SER C  49     3206   3251   4281     -8    324     17       O  
ATOM   5062  N   HIS C  50      56.872  12.576 -13.752  1.00 26.16           N  
ANISOU 5062  N   HIS C  50     2947   2990   4003     16    319     48       N  
ATOM   5063  CA  HIS C  50      55.588  13.177 -14.098  1.00 26.10           C  
ANISOU 5063  CA  HIS C  50     2930   2961   4027     24    321     72       C  
ATOM   5064  C   HIS C  50      54.400  12.360 -13.789  1.00 25.44           C  
ANISOU 5064  C   HIS C  50     2853   2890   3922     36    317     70       C  
ATOM   5065  O   HIS C  50      53.339  12.920 -13.493  1.00 25.30           O  
ANISOU 5065  O   HIS C  50     2827   2849   3935     44    323     73       O  
ATOM   5066  CB  HIS C  50      55.552  13.554 -15.601  1.00 28.38           C  
ANISOU 5066  CB  HIS C  50     3208   3250   4323     19    316    124       C  
ATOM   5067  CG  HIS C  50      56.724  14.406 -16.031  1.00 28.50           C  
ANISOU 5067  CG  HIS C  50     3213   3253   4360      6    319    134       C  
ATOM   5068  ND1 HIS C  50      57.280  14.317 -17.261  1.00 28.91           N  
ANISOU 5068  ND1 HIS C  50     3261   3324   4396     -3    313    169       N  
ATOM   5069  CD2 HIS C  50      57.437  15.396 -15.332  1.00 29.36           C  
ANISOU 5069  CD2 HIS C  50     3315   3333   4506      0    328    110       C  
ATOM   5070  CE1 HIS C  50      58.311  15.208 -17.347  1.00 28.74           C  
ANISOU 5070  CE1 HIS C  50     3230   3287   4402    -14    318    171       C  
ATOM   5071  NE2 HIS C  50      58.404  15.856 -16.154  1.00 30.05           N  
ANISOU 5071  NE2 HIS C  50     3395   3422   4600    -12    326    134       N  
ATOM   5072  N   THR C  51      54.521  11.033 -13.864  1.00 24.71           N  
ANISOU 5072  N   THR C  51     2775   2832   3780     37    308     65       N  
ATOM   5073  CA  THR C  51      53.414  10.188 -13.515  1.00 24.32           C  
ANISOU 5073  CA  THR C  51     2733   2796   3710     46    303     62       C  
ATOM   5074  C   THR C  51      53.042  10.316 -12.048  1.00 24.84           C  
ANISOU 5074  C   THR C  51     2799   2852   3785     51    311     23       C  
ATOM   5075  O   THR C  51      51.925   9.889 -11.667  1.00 24.52           O  
ANISOU 5075  O   THR C  51     2761   2817   3739     60    309     22       O  
ATOM   5076  CB  THR C  51      53.579   8.668 -13.911  1.00 24.04           C  
ANISOU 5076  CB  THR C  51     2714   2799   3622     46    290     65       C  
ATOM   5077  OG1 THR C  51      54.545   8.049 -13.067  1.00 22.48           O  
ANISOU 5077  OG1 THR C  51     2524   2614   3401     43    289     31       O  
ATOM   5078  CG2 THR C  51      54.011   8.531 -15.352  1.00 23.60           C  
ANISOU 5078  CG2 THR C  51     2657   2757   3552     39    284     99       C  
ATOM   5079  N   ASN C  52      53.891  10.876 -11.190  1.00 25.81           N  
ANISOU 5079  N   ASN C  52     2920   2963   3922     45    319     -9       N  
ATOM   5080  CA  ASN C  52      53.337  11.047  -9.803  1.00 26.70           C  
ANISOU 5080  CA  ASN C  52     3032   3068   4044     49    328    -46       C  
ATOM   5081  C   ASN C  52      51.989  11.797  -9.807  1.00 26.77           C  
ANISOU 5081  C   ASN C  52     3028   3050   4089     60    337    -35       C  
ATOM   5082  O   ASN C  52      51.201  11.712  -8.858  1.00 26.35           O  
ANISOU 5082  O   ASN C  52     2975   2998   4038     66    344    -59       O  
ATOM   5083  CB  ASN C  52      54.215  11.860  -8.913  1.00 26.82           C  
ANISOU 5083  CB  ASN C  52     3044   3067   4079     39    338    -82       C  
ATOM   5084  CG  ASN C  52      55.350  11.069  -8.352  1.00 27.64           C  
ANISOU 5084  CG  ASN C  52     3157   3198   4145     29    330   -105       C  
ATOM   5085  OD1 ASN C  52      55.191  10.239  -7.414  1.00 26.67           O  
ANISOU 5085  OD1 ASN C  52     3040   3098   3992     29    326   -128       O  
ATOM   5086  ND2 ASN C  52      56.531  11.327  -8.909  1.00 28.47           N  
ANISOU 5086  ND2 ASN C  52     3260   3301   4253     20    328    -97       N  
ATOM   5087  N   VAL C  53      51.759  12.594 -10.827  1.00 26.15           N  
ANISOU 5087  N   VAL C  53     2940   2950   4046     62    338      0       N  
ATOM   5088  CA  VAL C  53      50.594  13.463 -10.767  1.00 28.20           C  
ANISOU 5088  CA  VAL C  53     3183   3179   4350     72    349      8       C  
ATOM   5089  C   VAL C  53      49.344  12.615 -11.109  1.00 28.40           C  
ANISOU 5089  C   VAL C  53     3211   3224   4353     82    340     33       C  
ATOM   5090  O   VAL C  53      48.375  12.619 -10.360  1.00 27.50           O  
ANISOU 5090  O   VAL C  53     3093   3106   4248     91    348     18       O  
ATOM   5091  CB  VAL C  53      50.684  14.694 -11.674  1.00 27.59           C  
ANISOU 5091  CB  VAL C  53     3091   3068   4325     70    353     41       C  
ATOM   5092  CG1 VAL C  53      49.320  15.371 -11.752  1.00 27.05           C  
ANISOU 5092  CG1 VAL C  53     3005   2971   4301     84    361     60       C  
ATOM   5093  CG2 VAL C  53      51.782  15.632 -11.219  1.00 26.03           C  
ANISOU 5093  CG2 VAL C  53     2890   2845   4156     61    363     14       C  
ATOM   5094  N   MET C  54      49.393  11.940 -12.245  1.00 28.59           N  
ANISOU 5094  N   MET C  54     3240   3270   4350     79    325     71       N  
ATOM   5095  CA  MET C  54      48.422  10.915 -12.592  1.00 31.93           C  
ANISOU 5095  CA  MET C  54     3670   3719   4742     84    314     92       C  
ATOM   5096  C   MET C  54      48.151   9.879 -11.506  1.00 30.63           C  
ANISOU 5096  C   MET C  54     3518   3578   4541     87    312     59       C  
ATOM   5097  O   MET C  54      46.996   9.522 -11.327  1.00 30.72           O  
ANISOU 5097  O   MET C  54     3527   3596   4550     95    310     67       O  
ATOM   5098  CB  MET C  54      48.806  10.168 -13.871  1.00 33.21           C  
ANISOU 5098  CB  MET C  54     3840   3907   4868     76    298    125       C  
ATOM   5099  CG  MET C  54      48.613  10.961 -15.134  1.00 33.72           C  
ANISOU 5099  CG  MET C  54     3892   3959   4961     72    295    172       C  
ATOM   5100  SD  MET C  54      49.823  12.274 -15.278  1.00 39.07           S  
ANISOU 5100  SD  MET C  54     4559   4607   5679     64    306    169       S  
ATOM   5101  CE  MET C  54      51.167  11.452 -16.104  1.00 35.43           C  
ANISOU 5101  CE  MET C  54     4111   4180   5168     50    296    174       C  
ATOM   5102  N   ALA C  55      49.180   9.440 -10.776  1.00 30.57           N  
ANISOU 5102  N   ALA C  55     3521   3584   4509     80    312     24       N  
ATOM   5103  CA  ALA C  55      49.060   8.342  -9.807  1.00 28.61           C  
ANISOU 5103  CA  ALA C  55     3284   3363   4223     81    306     -2       C  
ATOM   5104  C   ALA C  55      48.648   8.801  -8.445  1.00 28.54           C  
ANISOU 5104  C   ALA C  55     3269   3344   4229     84    320    -38       C  
ATOM   5105  O   ALA C  55      48.355   7.988  -7.594  1.00 25.87           O  
ANISOU 5105  O   ALA C  55     2936   3028   3862     84    316    -57       O  
ATOM   5106  CB  ALA C  55      50.375   7.629  -9.679  1.00 32.38           C  
ANISOU 5106  CB  ALA C  55     3774   3859   4668     71    298    -18       C  
ATOM   5107  N   TYR C  56      48.624  10.107  -8.219  1.00 27.28           N  
ANISOU 5107  N   TYR C  56     3096   3152   4115     86    336    -49       N  
ATOM   5108  CA  TYR C  56      48.422  10.610  -6.882  1.00 29.84           C  
ANISOU 5108  CA  TYR C  56     3415   3468   4454     86    352    -92       C  
ATOM   5109  C   TYR C  56      49.537  10.140  -5.897  1.00 29.92           C  
ANISOU 5109  C   TYR C  56     3436   3500   4431     73    350   -130       C  
ATOM   5110  O   TYR C  56      49.297  10.001  -4.676  1.00 28.74           O  
ANISOU 5110  O   TYR C  56     3285   3362   4269     70    357   -165       O  
ATOM   5111  CB  TYR C  56      47.014  10.293  -6.333  1.00 30.30           C  
ANISOU 5111  CB  TYR C  56     3467   3534   4508     97    357    -94       C  
ATOM   5112  CG  TYR C  56      46.432  11.489  -5.595  1.00 35.17           C  
ANISOU 5112  CG  TYR C  56     4068   4121   5171    103    380   -120       C  
ATOM   5113  CD1 TYR C  56      47.226  12.235  -4.671  1.00 36.43           C  
ANISOU 5113  CD1 TYR C  56     4227   4268   5346     94    395   -166       C  
ATOM   5114  CD2 TYR C  56      45.091  11.863  -5.741  1.00 36.47           C  
ANISOU 5114  CD2 TYR C  56     4218   4270   5366    118    389   -103       C  
ATOM   5115  CE1 TYR C  56      46.718  13.333  -3.986  1.00 36.42           C  
ANISOU 5115  CE1 TYR C  56     4212   4238   5389     99    418   -196       C  
ATOM   5116  CE2 TYR C  56      44.552  12.990  -5.037  1.00 38.73           C  
ANISOU 5116  CE2 TYR C  56     4488   4526   5700    125    414   -132       C  
ATOM   5117  CZ  TYR C  56      45.355  13.718  -4.144  1.00 38.68           C  
ANISOU 5117  CZ  TYR C  56     4483   4506   5708    116    429   -180       C  
ATOM   5118  OH  TYR C  56      44.865  14.875  -3.461  1.00 36.27           O  
ANISOU 5118  OH  TYR C  56     4161   4167   5453    123    456   -213       O  
ATOM   5119  N   SER C  57      50.754   9.975  -6.422  1.00 28.42           N  
ANISOU 5119  N   SER C  57     3253   3315   4230     64    341   -124       N  
ATOM   5120  CA  SER C  57      51.884   9.527  -5.628  1.00 28.88           C  
ANISOU 5120  CA  SER C  57     3319   3394   4260     51    336   -153       C  
ATOM   5121  C   SER C  57      52.845  10.626  -5.274  1.00 31.27           C  
ANISOU 5121  C   SER C  57     3616   3674   4589     40    347   -178       C  
ATOM   5122  O   SER C  57      52.840  11.677  -5.905  1.00 32.83           O  
ANISOU 5122  O   SER C  57     3805   3838   4828     43    356   -166       O  
ATOM   5123  CB  SER C  57      52.649   8.479  -6.411  1.00 28.19           C  
ANISOU 5123  CB  SER C  57     3242   3329   4139     48    318   -130       C  
ATOM   5124  OG  SER C  57      51.752   7.377  -6.579  1.00 30.84           O  
ANISOU 5124  OG  SER C  57     3584   3686   4446     56    307   -112       O  
ATOM   5125  N   ASN C  58      53.736  10.351  -4.325  1.00 29.96           N  
ANISOU 5125  N   ASN C  58     3454   3526   4400     27    345   -210       N  
ATOM   5126  CA  ASN C  58      54.843  11.216  -4.106  1.00 29.22           C  
ANISOU 5126  CA  ASN C  58     3357   3417   4327     14    351   -230       C  
ATOM   5127  C   ASN C  58      56.190  10.496  -3.974  1.00 28.73           C  
ANISOU 5127  C   ASN C  58     3302   3382   4232      1    338   -233       C  
ATOM   5128  O   ASN C  58      56.853  10.489  -2.915  1.00 27.33           O  
ANISOU 5128  O   ASN C  58     3125   3219   4040    -13    338   -265       O  
ATOM   5129  CB  ASN C  58      54.571  12.077  -2.897  1.00 30.50           C  
ANISOU 5129  CB  ASN C  58     3513   3567   4508      7    368   -274       C  
ATOM   5130  CG  ASN C  58      55.527  13.272  -2.807  1.00 32.44           C  
ANISOU 5130  CG  ASN C  58     3753   3783   4788     -5    377   -294       C  
ATOM   5131  OD1 ASN C  58      56.142  13.694  -3.791  1.00 33.04           O  
ANISOU 5131  OD1 ASN C  58     3826   3841   4884     -5    374   -268       O  
ATOM   5132  ND2 ASN C  58      55.660  13.799  -1.618  1.00 31.80           N  
ANISOU 5132  ND2 ASN C  58     3670   3702   4711    -18    389   -340       N  
ATOM   5133  N   CYS C  59      56.627   9.939  -5.076  1.00 27.25           N  
ANISOU 5133  N   CYS C  59     3118   3200   4033      5    326   -199       N  
ATOM   5134  CA  CYS C  59      57.963   9.369  -5.148  1.00 29.57           C  
ANISOU 5134  CA  CYS C  59     3415   3514   4304     -4    315   -198       C  
ATOM   5135  C   CYS C  59      58.936  10.166  -5.998  1.00 29.29           C  
ANISOU 5135  C   CYS C  59     3374   3459   4294     -9    318   -185       C  
ATOM   5136  O   CYS C  59      58.656  10.369  -7.202  1.00 29.27           O  
ANISOU 5136  O   CYS C  59     3371   3444   4306     -1    319   -152       O  
ATOM   5137  CB  CYS C  59      57.902   7.961  -5.741  1.00 29.35           C  
ANISOU 5137  CB  CYS C  59     3395   3512   4241      4    301   -173       C  
ATOM   5138  SG  CYS C  59      56.887   6.902  -4.693  1.00 38.49           S  
ANISOU 5138  SG  CYS C  59     4559   4697   5368      8    294   -186       S  
ATOM   5139  N   LYS C  60      60.120  10.468  -5.440  1.00 28.92           N  
ANISOU 5139  N   LYS C  60     3324   3416   4247    -25    318   -205       N  
ATOM   5140  CA  LYS C  60      61.239  11.066  -6.245  1.00 32.21           C  
ANISOU 5140  CA  LYS C  60     3735   3820   4682    -32    318   -190       C  
ATOM   5141  C   LYS C  60      61.700  10.025  -7.254  1.00 32.95           C  
ANISOU 5141  C   LYS C  60     3832   3936   4749    -25    308   -159       C  
ATOM   5142  O   LYS C  60      61.823   8.858  -6.920  1.00 30.74           O  
ANISOU 5142  O   LYS C  60     3558   3684   4435    -23    298   -162       O  
ATOM   5143  CB  LYS C  60      62.439  11.450  -5.385  1.00 34.44           C  
ANISOU 5143  CB  LYS C  60     4013   4107   4965    -52    318   -217       C  
ATOM   5144  CG  LYS C  60      62.348  12.894  -4.905  1.00 42.87           C  
ANISOU 5144  CG  LYS C  60     5074   5141   6073    -62    331   -241       C  
ATOM   5145  CD  LYS C  60      63.035  13.156  -3.567  1.00 49.02           C  
ANISOU 5145  CD  LYS C  60     5850   5929   6844    -82    332   -282       C  
ATOM   5146  CE  LYS C  60      62.156  14.081  -2.735  1.00 52.54           C  
ANISOU 5146  CE  LYS C  60     6295   6351   7316    -85    347   -317       C  
ATOM   5147  NZ  LYS C  60      62.706  14.370  -1.382  1.00 57.31           N  
ANISOU 5147  NZ  LYS C  60     6897   6966   7909   -107    349   -361       N  
ATOM   5148  N   VAL C  61      61.924  10.437  -8.489  1.00 33.80           N  
ANISOU 5148  N   VAL C  61     3936   4032   4873    -23    310   -130       N  
ATOM   5149  CA  VAL C  61      62.537   9.570  -9.444  1.00 33.08           C  
ANISOU 5149  CA  VAL C  61     3847   3962   4757    -19    303   -106       C  
ATOM   5150  C   VAL C  61      63.727  10.263 -10.095  1.00 34.60           C  
ANISOU 5150  C   VAL C  61     4030   4149   4966    -30    306    -94       C  
ATOM   5151  O   VAL C  61      63.555  11.200 -10.876  1.00 35.24           O  
ANISOU 5151  O   VAL C  61     4104   4208   5075    -31    312    -73       O  
ATOM   5152  CB  VAL C  61      61.547   9.177 -10.536  1.00 34.50           C  
ANISOU 5152  CB  VAL C  61     4032   4144   4931     -6    301    -76       C  
ATOM   5153  CG1 VAL C  61      62.117   8.022 -11.368  1.00 33.06           C  
ANISOU 5153  CG1 VAL C  61     3855   3990   4716     -3    294    -59       C  
ATOM   5154  CG2 VAL C  61      60.238   8.750  -9.875  1.00 36.06           C  
ANISOU 5154  CG2 VAL C  61     4237   4343   5121      2    299    -86       C  
ATOM   5155  N   SER C  62      64.892   9.695  -9.827  1.00 32.37           N  
ANISOU 5155  N   SER C  62     3745   3886   4664    -36    301   -102       N  
ATOM   5156  CA  SER C  62      66.232  10.201 -10.179  1.00 31.75           C  
ANISOU 5156  CA  SER C  62     3656   3808   4596    -48    302    -96       C  
ATOM   5157  C   SER C  62      66.992   9.301 -11.121  1.00 28.88           C  
ANISOU 5157  C   SER C  62     3292   3471   4210    -44    299    -76       C  
ATOM   5158  O   SER C  62      66.945   8.055 -11.004  1.00 27.76           O  
ANISOU 5158  O   SER C  62     3156   3350   4038    -35    293    -79       O  
ATOM   5159  CB  SER C  62      67.085  10.100  -8.907  1.00 31.43           C  
ANISOU 5159  CB  SER C  62     3613   3778   4550    -61    298   -126       C  
ATOM   5160  OG  SER C  62      66.690  11.097  -8.060  1.00 38.25           O  
ANISOU 5160  OG  SER C  62     4476   4619   5438    -70    303   -148       O  
ATOM   5161  N   GLY C  63      67.795   9.909 -11.967  1.00 28.75           N  
ANISOU 5161  N   GLY C  63     3265   3451   4206    -51    304    -57       N  
ATOM   5162  CA  GLY C  63      68.798   9.156 -12.724  1.00 30.53           C  
ANISOU 5162  CA  GLY C  63     3485   3701   4410    -50    304    -44       C  
ATOM   5163  C   GLY C  63      70.135   9.197 -12.012  1.00 30.78           C  
ANISOU 5163  C   GLY C  63     3507   3742   4444    -61    301    -58       C  
ATOM   5164  O   GLY C  63      70.420  10.101 -11.180  1.00 33.16           O  
ANISOU 5164  O   GLY C  63     3804   4027   4767    -75    301    -74       O  
ATOM   5165  N   SER C  64      70.994   8.233 -12.318  1.00 30.31           N  
ANISOU 5165  N   SER C  64     3443   3708   4364    -56    300    -55       N  
ATOM   5166  CA  SER C  64      72.321   8.272 -11.778  1.00 30.29           C  
ANISOU 5166  CA  SER C  64     3428   3715   4364    -67    297    -63       C  
ATOM   5167  C   SER C  64      73.316   7.479 -12.543  1.00 31.84           C  
ANISOU 5167  C   SER C  64     3616   3937   4546    -62    300    -50       C  
ATOM   5168  O   SER C  64      72.985   6.391 -13.040  1.00 31.78           O  
ANISOU 5168  O   SER C  64     3615   3943   4517    -47    301    -47       O  
ATOM   5169  CB  SER C  64      72.336   7.744 -10.334  1.00 30.95           C  
ANISOU 5169  CB  SER C  64     3515   3806   4439    -70    287    -89       C  
ATOM   5170  OG  SER C  64      73.675   7.534  -9.891  1.00 30.72           O  
ANISOU 5170  OG  SER C  64     3472   3793   4408    -79    282    -92       O  
ATOM   5171  N   ASN C  65      74.557   7.996 -12.566  1.00 30.06           N  
ANISOU 5171  N   ASN C  65     3374   3716   4332    -75    302    -45       N  
ATOM   5172  CA  ASN C  65      75.643   7.273 -13.140  1.00 30.64           C  
ANISOU 5172  CA  ASN C  65     3434   3812   4393    -70    306    -36       C  
ATOM   5173  C   ASN C  65      76.706   6.993 -12.093  1.00 30.07           C  
ANISOU 5173  C   ASN C  65     3350   3751   4323    -78    298    -48       C  
ATOM   5174  O   ASN C  65      77.801   6.623 -12.443  1.00 30.75           O  
ANISOU 5174  O   ASN C  65     3421   3855   4407    -77    302    -40       O  
ATOM   5175  CB  ASN C  65      76.249   8.030 -14.336  1.00 33.24           C  
ANISOU 5175  CB  ASN C  65     3752   4145   4732    -77    317    -12       C  
ATOM   5176  CG  ASN C  65      75.246   8.264 -15.469  1.00 35.46           C  
ANISOU 5176  CG  ASN C  65     4042   4420   5008    -72    324      5       C  
ATOM   5177  OD1 ASN C  65      75.119   9.377 -15.968  1.00 37.80           O  
ANISOU 5177  OD1 ASN C  65     4334   4702   5323    -83    328     22       O  
ATOM   5178  ND2 ASN C  65      74.552   7.215 -15.891  1.00 34.97           N  
ANISOU 5178  ND2 ASN C  65     3993   4370   4923    -56    325      2       N  
ATOM   5179  N   THR C  66      76.396   7.093 -10.803  1.00 29.44           N  
ANISOU 5179  N   THR C  66     3275   3663   4245    -85    287    -68       N  
ATOM   5180  CA  THR C  66      77.436   6.761  -9.816  1.00 28.10           C  
ANISOU 5180  CA  THR C  66     3091   3508   4074    -95    278    -77       C  
ATOM   5181  C   THR C  66      76.897   5.838  -8.745  1.00 27.77           C  
ANISOU 5181  C   THR C  66     3058   3474   4017    -89    265    -92       C  
ATOM   5182  O   THR C  66      75.820   6.084  -8.187  1.00 26.24           O  
ANISOU 5182  O   THR C  66     2878   3268   3821    -90    262   -106       O  
ATOM   5183  CB  THR C  66      77.990   8.004  -9.126  1.00 28.66           C  
ANISOU 5183  CB  THR C  66     3154   3569   4165   -120    274    -84       C  
ATOM   5184  OG1 THR C  66      78.724   7.603  -7.938  1.00 30.63           O  
ANISOU 5184  OG1 THR C  66     3393   3834   4408   -131    261    -96       O  
ATOM   5185  CG2 THR C  66      76.825   8.939  -8.692  1.00 27.52           C  
ANISOU 5185  CG2 THR C  66     3026   3398   4032   -127    275   -100       C  
ATOM   5186  N   TYR C  67      77.667   4.797  -8.440  1.00 28.86           N  
ANISOU 5186  N   TYR C  67     3184   3632   4146    -84    259    -89       N  
ATOM   5187  CA  TYR C  67      77.308   3.819  -7.397  1.00 30.98           C  
ANISOU 5187  CA  TYR C  67     3457   3912   4401    -80    245    -99       C  
ATOM   5188  C   TYR C  67      77.235   4.480  -6.043  1.00 30.07           C  
ANISOU 5188  C   TYR C  67     3342   3797   4287   -102    234   -116       C  
ATOM   5189  O   TYR C  67      76.781   3.897  -5.094  1.00 28.24           O  
ANISOU 5189  O   TYR C  67     3114   3574   4042   -104    222   -125       O  
ATOM   5190  CB  TYR C  67      78.322   2.695  -7.332  1.00 32.12           C  
ANISOU 5190  CB  TYR C  67     3584   4076   4543    -72    239    -88       C  
ATOM   5191  CG  TYR C  67      78.214   1.736  -8.467  1.00 33.81           C  
ANISOU 5191  CG  TYR C  67     3801   4292   4753    -48    249    -78       C  
ATOM   5192  CD1 TYR C  67      77.083   0.965  -8.615  1.00 35.11           C  
ANISOU 5192  CD1 TYR C  67     3982   4451   4905    -32    248    -83       C  
ATOM   5193  CD2 TYR C  67      79.259   1.567  -9.372  1.00 36.32           C  
ANISOU 5193  CD2 TYR C  67     4102   4618   5078    -41    260    -66       C  
ATOM   5194  CE1 TYR C  67      76.953   0.058  -9.642  1.00 37.86           C  
ANISOU 5194  CE1 TYR C  67     4335   4801   5249    -12    256    -77       C  
ATOM   5195  CE2 TYR C  67      79.154   0.672 -10.429  1.00 38.22           C  
ANISOU 5195  CE2 TYR C  67     4345   4862   5313    -20    271    -62       C  
ATOM   5196  CZ  TYR C  67      77.982  -0.087 -10.563  1.00 40.58           C  
ANISOU 5196  CZ  TYR C  67     4664   5154   5600     -5    269    -68       C  
ATOM   5197  OH  TYR C  67      77.828  -1.002 -11.574  1.00 40.56           O  
ANISOU 5197  OH  TYR C  67     4664   5153   5591     13    279    -67       O  
ATOM   5198  N   ASP C  68      77.613   5.743  -5.979  1.00 31.03           N  
ANISOU 5198  N   ASP C  68     3459   3907   4423   -121    238   -121       N  
ATOM   5199  CA  ASP C  68      77.480   6.513  -4.754  1.00 31.57           C  
ANISOU 5199  CA  ASP C  68     3528   3972   4492   -144    230   -143       C  
ATOM   5200  C   ASP C  68      76.032   6.680  -4.357  1.00 31.22           C  
ANISOU 5200  C   ASP C  68     3504   3915   4442   -140    232   -160       C  
ATOM   5201  O   ASP C  68      75.720   6.908  -3.159  1.00 31.17           O  
ANISOU 5201  O   ASP C  68     3501   3914   4428   -156    225   -181       O  
ATOM   5202  CB  ASP C  68      78.091   7.901  -4.940  1.00 33.99           C  
ANISOU 5202  CB  ASP C  68     3828   4264   4821   -164    237   -145       C  
ATOM   5203  CG  ASP C  68      79.616   7.892  -4.896  1.00 38.06           C  
ANISOU 5203  CG  ASP C  68     4321   4797   5342   -177    231   -133       C  
ATOM   5204  OD1 ASP C  68      80.278   6.822  -4.721  1.00 40.91           O  
ANISOU 5204  OD1 ASP C  68     4669   5181   5691   -170    223   -121       O  
ATOM   5205  OD2 ASP C  68      80.170   8.992  -5.042  1.00 40.24           O  
ANISOU 5205  OD2 ASP C  68     4590   5062   5637   -194    235   -133       O  
ATOM   5206  N   ASP C  69      75.137   6.564  -5.329  1.00 29.59           N  
ANISOU 5206  N   ASP C  69     3310   3694   4237   -121    242   -151       N  
ATOM   5207  CA  ASP C  69      73.705   6.771  -5.043  1.00 30.96           C  
ANISOU 5207  CA  ASP C  69     3501   3853   4408   -115    245   -166       C  
ATOM   5208  C   ASP C  69      73.032   5.579  -4.383  1.00 31.59           C  
ANISOU 5208  C   ASP C  69     3587   3950   4464   -106    235   -170       C  
ATOM   5209  O   ASP C  69      71.826   5.624  -4.098  1.00 30.54           O  
ANISOU 5209  O   ASP C  69     3468   3809   4326   -101    236   -180       O  
ATOM   5210  CB  ASP C  69      72.943   7.198  -6.303  1.00 34.78           C  
ANISOU 5210  CB  ASP C  69     3994   4315   4904   -101    258   -152       C  
ATOM   5211  CG  ASP C  69      73.213   8.663  -6.672  1.00 38.14           C  
ANISOU 5211  CG  ASP C  69     4415   4717   5358   -114    267   -152       C  
ATOM   5212  OD1 ASP C  69      73.539   9.450  -5.768  1.00 35.14           O  
ANISOU 5212  OD1 ASP C  69     4031   4331   4989   -134    265   -172       O  
ATOM   5213  OD2 ASP C  69      73.127   9.008  -7.871  1.00 41.23           O  
ANISOU 5213  OD2 ASP C  69     4806   5096   5760   -106    276   -132       O  
ATOM   5214  N   LEU C  70      73.805   4.515  -4.179  1.00 30.48           N  
ANISOU 5214  N   LEU C  70     3436   3832   4311   -103    224   -159       N  
ATOM   5215  CA  LEU C  70      73.435   3.401  -3.254  1.00 31.13           C  
ANISOU 5215  CA  LEU C  70     3520   3934   4373   -100    210   -162       C  
ATOM   5216  C   LEU C  70      73.441   3.829  -1.797  1.00 30.47           C  
ANISOU 5216  C   LEU C  70     3433   3863   4280   -125    201   -182       C  
ATOM   5217  O   LEU C  70      72.982   3.090  -0.928  1.00 31.17           O  
ANISOU 5217  O   LEU C  70     3523   3969   4351   -127    189   -186       O  
ATOM   5218  CB  LEU C  70      74.405   2.203  -3.419  1.00 29.41           C  
ANISOU 5218  CB  LEU C  70     3287   3734   4151    -92    201   -143       C  
ATOM   5219  CG  LEU C  70      74.305   1.566  -4.795  1.00 28.77           C  
ANISOU 5219  CG  LEU C  70     3211   3644   4074    -67    210   -127       C  
ATOM   5220  CD1 LEU C  70      75.516   0.686  -5.125  1.00 28.58           C  
ANISOU 5220  CD1 LEU C  70     3169   3634   4055    -59    207   -111       C  
ATOM   5221  CD2 LEU C  70      73.033   0.725  -4.782  1.00 26.37           C  
ANISOU 5221  CD2 LEU C  70     2922   3338   3756    -52    207   -128       C  
ATOM   5222  N   ALA C  71      73.963   5.003  -1.494  1.00 30.31           N  
ANISOU 5222  N   ALA C  71     3407   3836   4272   -145    205   -196       N  
ATOM   5223  CA  ALA C  71      73.992   5.380  -0.100  1.00 30.87           C  
ANISOU 5223  CA  ALA C  71     3475   3922   4331   -171    197   -219       C  
ATOM   5224  C   ALA C  71      72.557   5.478   0.453  1.00 34.76           C  
ANISOU 5224  C   ALA C  71     3983   4410   4813   -169    200   -239       C  
ATOM   5225  O   ALA C  71      71.711   6.198  -0.102  1.00 37.44           O  
ANISOU 5225  O   ALA C  71     4334   4723   5167   -159    215   -247       O  
ATOM   5226  CB  ALA C  71      74.679   6.710   0.054  1.00 32.46           C  
ANISOU 5226  CB  ALA C  71     3670   4112   4550   -193    202   -234       C  
ATOM   5227  N   GLY C  72      72.290   4.754   1.541  1.00 36.60           N  
ANISOU 5227  N   GLY C  72     4214   4671   5021   -177    187   -244       N  
ATOM   5228  CA  GLY C  72      70.968   4.674   2.168  1.00 32.26           C  
ANISOU 5228  CA  GLY C  72     3676   4123   4456   -176    190   -261       C  
ATOM   5229  C   GLY C  72      69.895   3.919   1.385  1.00 31.51           C  
ANISOU 5229  C   GLY C  72     3593   4017   4360   -148    193   -245       C  
ATOM   5230  O   GLY C  72      68.737   4.057   1.686  1.00 29.37           O  
ANISOU 5230  O   GLY C  72     3333   3743   4084   -144    199   -258       O  
ATOM   5231  N   ALA C  73      70.243   3.075   0.424  1.00 31.12           N  
ANISOU 5231  N   ALA C  73     3543   3965   4316   -128    190   -218       N  
ATOM   5232  CA  ALA C  73      69.195   2.345  -0.309  1.00 29.85           C  
ANISOU 5232  CA  ALA C  73     3394   3794   4152   -103    192   -205       C  
ATOM   5233  C   ALA C  73      68.534   1.383   0.673  1.00 30.60           C  
ANISOU 5233  C   ALA C  73     3490   3913   4223   -106    179   -205       C  
ATOM   5234  O   ALA C  73      69.224   0.928   1.605  1.00 31.40           O  
ANISOU 5234  O   ALA C  73     3578   4040   4311   -122    164   -203       O  
ATOM   5235  CB  ALA C  73      69.807   1.588  -1.486  1.00 28.37           C  
ANISOU 5235  CB  ALA C  73     3204   3602   3974    -84    192   -180       C  
ATOM   5236  N   ASP C  74      67.211   1.162   0.562  1.00 26.99           N  
ANISOU 5236  N   ASP C  74     3045   3448   3760    -94    182   -206       N  
ATOM   5237  CA  ASP C  74      66.562   0.099   1.350  1.00 26.74           C  
ANISOU 5237  CA  ASP C  74     3013   3440   3706    -94    168   -200       C  
ATOM   5238  C   ASP C  74      66.452  -1.188   0.584  1.00 25.55           C  
ANISOU 5238  C   ASP C  74     2865   3287   3555    -73    159   -174       C  
ATOM   5239  O   ASP C  74      66.408  -2.274   1.162  1.00 24.80           O  
ANISOU 5239  O   ASP C  74     2764   3211   3446    -74    143   -161       O  
ATOM   5240  CB  ASP C  74      65.159   0.519   1.771  1.00 29.17           C  
ANISOU 5240  CB  ASP C  74     3332   3745   4006    -95    176   -216       C  
ATOM   5241  CG  ASP C  74      65.188   1.705   2.677  1.00 34.60           C  
ANISOU 5241  CG  ASP C  74     4016   4436   4692   -116    185   -247       C  
ATOM   5242  OD1 ASP C  74      65.496   1.497   3.855  1.00 38.00           O  
ANISOU 5242  OD1 ASP C  74     4438   4897   5102   -137    175   -256       O  
ATOM   5243  OD2 ASP C  74      64.985   2.869   2.241  1.00 39.86           O  
ANISOU 5243  OD2 ASP C  74     4688   5078   5380   -115    203   -263       O  
ATOM   5244  N   VAL C  75      66.320  -1.051  -0.745  1.00 25.75           N  
ANISOU 5244  N   VAL C  75     2899   3287   3596    -55    171   -166       N  
ATOM   5245  CA  VAL C  75      66.212  -2.173  -1.633  1.00 24.12           C  
ANISOU 5245  CA  VAL C  75     2697   3076   3391    -35    166   -146       C  
ATOM   5246  C   VAL C  75      67.072  -1.880  -2.871  1.00 23.92           C  
ANISOU 5246  C   VAL C  75     2669   3034   3382    -26    177   -139       C  
ATOM   5247  O   VAL C  75      67.118  -0.742  -3.371  1.00 23.99           O  
ANISOU 5247  O   VAL C  75     2682   3029   3403    -28    191   -147       O  
ATOM   5248  CB  VAL C  75      64.759  -2.321  -2.043  1.00 24.74           C  
ANISOU 5248  CB  VAL C  75     2791   3144   3464    -23    170   -144       C  
ATOM   5249  CG1 VAL C  75      64.617  -3.269  -3.215  1.00 24.35           C  
ANISOU 5249  CG1 VAL C  75     2748   3084   3418     -4    169   -127       C  
ATOM   5250  CG2 VAL C  75      63.902  -2.698  -0.819  1.00 24.03           C  
ANISOU 5250  CG2 VAL C  75     2701   3073   3357    -33    159   -149       C  
ATOM   5251  N   VAL C  76      67.797  -2.884  -3.346  1.00 22.87           N  
ANISOU 5251  N   VAL C  76     2531   2905   3253    -16    171   -125       N  
ATOM   5252  CA  VAL C  76      68.556  -2.732  -4.586  1.00 21.68           C  
ANISOU 5252  CA  VAL C  76     2378   2743   3116     -6    183   -119       C  
ATOM   5253  C   VAL C  76      68.145  -3.799  -5.532  1.00 21.23           C  
ANISOU 5253  C   VAL C  76     2329   2678   3056     13    183   -108       C  
ATOM   5254  O   VAL C  76      68.089  -4.980  -5.179  1.00 23.45           O  
ANISOU 5254  O   VAL C  76     2607   2966   3334     18    170   -101       O  
ATOM   5255  CB  VAL C  76      70.088  -2.954  -4.327  1.00 22.03           C  
ANISOU 5255  CB  VAL C  76     2402   2798   3168    -11    178   -113       C  
ATOM   5256  CG1 VAL C  76      70.903  -2.769  -5.584  1.00 20.95           C  
ANISOU 5256  CG1 VAL C  76     2262   2653   3045     -2    192   -108       C  
ATOM   5257  CG2 VAL C  76      70.618  -2.121  -3.141  1.00 21.62           C  
ANISOU 5257  CG2 VAL C  76     2340   2759   3115    -35    173   -123       C  
ATOM   5258  N   ILE C  77      67.952  -3.466  -6.781  1.00 21.75           N  
ANISOU 5258  N   ILE C  77     2404   2733   3127     22    197   -106       N  
ATOM   5259  CA  ILE C  77      67.501  -4.489  -7.685  1.00 20.94           C  
ANISOU 5259  CA  ILE C  77     2309   2625   3019     38    197    -99       C  
ATOM   5260  C   ILE C  77      68.438  -4.495  -8.855  1.00 20.98           C  
ANISOU 5260  C   ILE C  77     2310   2628   3032     45    210    -96       C  
ATOM   5261  O   ILE C  77      68.662  -3.428  -9.493  1.00 20.56           O  
ANISOU 5261  O   ILE C  77     2257   2571   2984     40    223    -96       O  
ATOM   5262  CB  ILE C  77      66.083  -4.159  -8.129  1.00 21.08           C  
ANISOU 5262  CB  ILE C  77     2345   2634   3029     40    201    -99       C  
ATOM   5263  CG1 ILE C  77      65.185  -4.388  -6.922  1.00 21.95           C  
ANISOU 5263  CG1 ILE C  77     2459   2750   3131     35    187   -102       C  
ATOM   5264  CG2 ILE C  77      65.691  -5.066  -9.302  1.00 21.30           C  
ANISOU 5264  CG2 ILE C  77     2383   2658   3051     54    203    -93       C  
ATOM   5265  CD1 ILE C  77      63.917  -3.587  -6.870  1.00 21.72           C  
ANISOU 5265  CD1 ILE C  77     2440   2713   3097     32    192   -105       C  
ATOM   5266  N   VAL C  78      69.002  -5.664  -9.146  1.00 20.91           N  
ANISOU 5266  N   VAL C  78     2295   2621   3026     56    207    -94       N  
ATOM   5267  CA  VAL C  78      70.101  -5.666 -10.057  1.00 21.85           C  
ANISOU 5267  CA  VAL C  78     2405   2743   3155     61    220    -93       C  
ATOM   5268  C   VAL C  78      69.700  -6.322 -11.324  1.00 23.38           C  
ANISOU 5268  C   VAL C  78     2609   2932   3341     74    230    -95       C  
ATOM   5269  O   VAL C  78      69.568  -7.563 -11.366  1.00 23.42           O  
ANISOU 5269  O   VAL C  78     2616   2934   3348     85    223    -96       O  
ATOM   5270  CB  VAL C  78      71.339  -6.392  -9.505  1.00 22.08           C  
ANISOU 5270  CB  VAL C  78     2413   2778   3197     64    214    -91       C  
ATOM   5271  CG1 VAL C  78      72.463  -6.321 -10.542  1.00 22.44           C  
ANISOU 5271  CG1 VAL C  78     2447   2827   3252     71    231    -91       C  
ATOM   5272  CG2 VAL C  78      71.776  -5.773  -8.170  1.00 21.24           C  
ANISOU 5272  CG2 VAL C  78     2294   2681   3094     48    203    -89       C  
ATOM   5273  N   THR C  79      69.521  -5.508 -12.349  1.00 25.25           N  
ANISOU 5273  N   THR C  79     2852   3168   3571     71    244    -93       N  
ATOM   5274  CA  THR C  79      69.249  -5.983 -13.740  1.00 26.54           C  
ANISOU 5274  CA  THR C  79     3026   3333   3725     79    256    -95       C  
ATOM   5275  C   THR C  79      70.342  -5.752 -14.750  1.00 28.76           C  
ANISOU 5275  C   THR C  79     3294   3622   4008     81    274    -96       C  
ATOM   5276  O   THR C  79      70.198  -6.152 -15.893  1.00 31.10           O  
ANISOU 5276  O   THR C  79     3597   3923   4293     86    285   -100       O  
ATOM   5277  CB  THR C  79      68.044  -5.291 -14.375  1.00 26.41           C  
ANISOU 5277  CB  THR C  79     3025   3314   3695     74    259    -89       C  
ATOM   5278  OG1 THR C  79      68.198  -3.841 -14.433  1.00 27.25           O  
ANISOU 5278  OG1 THR C  79     3126   3419   3806     62    266    -81       O  
ATOM   5279  CG2 THR C  79      66.832  -5.642 -13.639  1.00 27.25           C  
ANISOU 5279  CG2 THR C  79     3143   3413   3796     74    244    -88       C  
ATOM   5280  N   ALA C  80      71.418  -5.093 -14.357  1.00 29.00           N  
ANISOU 5280  N   ALA C  80     3308   3657   4051     75    277    -93       N  
ATOM   5281  CA  ALA C  80      72.459  -4.742 -15.271  1.00 28.27           C  
ANISOU 5281  CA  ALA C  80     3204   3576   3962     74    294    -91       C  
ATOM   5282  C   ALA C  80      73.238  -6.024 -15.563  1.00 28.58           C  
ANISOU 5282  C   ALA C  80     3233   3619   4007     89    300   -101       C  
ATOM   5283  O   ALA C  80      73.281  -6.926 -14.740  1.00 27.56           O  
ANISOU 5283  O   ALA C  80     3101   3483   3887     97    287   -105       O  
ATOM   5284  CB  ALA C  80      73.349  -3.727 -14.631  1.00 28.14           C  
ANISOU 5284  CB  ALA C  80     3171   3561   3959     63    294    -85       C  
ATOM   5285  N   GLY C  81      73.807  -6.111 -16.762  1.00 28.58           N  
ANISOU 5285  N   GLY C  81     3227   3629   4000     93    319   -105       N  
ATOM   5286  CA  GLY C  81      74.662  -7.239 -17.128  1.00 27.73           C  
ANISOU 5286  CA  GLY C  81     3108   3525   3902    108    329   -117       C  
ATOM   5287  C   GLY C  81      74.552  -7.431 -18.638  1.00 29.24           C  
ANISOU 5287  C   GLY C  81     3306   3729   4075    110    349   -126       C  
ATOM   5288  O   GLY C  81      73.724  -6.832 -19.296  1.00 27.49           O  
ANISOU 5288  O   GLY C  81     3099   3512   3833    100    352   -121       O  
ATOM   5289  N   PHE C  82      75.445  -8.274 -19.149  1.00 33.20           N  
ANISOU 5289  N   PHE C  82     3795   4236   4584    122    364   -140       N  
ATOM   5290  CA  PHE C  82      75.600  -8.633 -20.534  1.00 32.48           C  
ANISOU 5290  CA  PHE C  82     3705   4159   4476    126    387   -154       C  
ATOM   5291  C   PHE C  82      74.694  -9.819 -20.766  1.00 32.84           C  
ANISOU 5291  C   PHE C  82     3769   4193   4515    135    382   -172       C  
ATOM   5292  O   PHE C  82      74.686 -10.763 -20.008  1.00 32.57           O  
ANISOU 5292  O   PHE C  82     3733   4141   4501    147    371   -179       O  
ATOM   5293  CB  PHE C  82      77.031  -9.082 -20.737  1.00 33.95           C  
ANISOU 5293  CB  PHE C  82     3864   4352   4680    137    404   -163       C  
ATOM   5294  CG  PHE C  82      78.047  -7.971 -20.633  1.00 33.58           C  
ANISOU 5294  CG  PHE C  82     3798   4320   4640    127    410   -146       C  
ATOM   5295  CD1 PHE C  82      78.336  -7.174 -21.735  1.00 33.51           C  
ANISOU 5295  CD1 PHE C  82     3785   4334   4611    116    429   -141       C  
ATOM   5296  CD2 PHE C  82      78.742  -7.751 -19.421  1.00 33.58           C  
ANISOU 5296  CD2 PHE C  82     3781   4311   4666    128    397   -134       C  
ATOM   5297  CE1 PHE C  82      79.289  -6.161 -21.642  1.00 34.49           C  
ANISOU 5297  CE1 PHE C  82     3890   4471   4744    106    434   -124       C  
ATOM   5298  CE2 PHE C  82      79.705  -6.744 -19.318  1.00 34.64           C  
ANISOU 5298  CE2 PHE C  82     3895   4457   4807    117    402   -118       C  
ATOM   5299  CZ  PHE C  82      79.961  -5.948 -20.427  1.00 35.28           C  
ANISOU 5299  CZ  PHE C  82     3973   4559   4870    107    420   -114       C  
ATOM   5300  N   THR C  83      73.955  -9.747 -21.844  1.00 33.57           N  
ANISOU 5300  N   THR C  83     3878   4298   4580    127    391   -178       N  
ATOM   5301  CA  THR C  83      73.039 -10.772 -22.235  1.00 37.04           C  
ANISOU 5301  CA  THR C  83     4335   4728   5007    132    388   -195       C  
ATOM   5302  C   THR C  83      73.395 -11.284 -23.613  1.00 38.74           C  
ANISOU 5302  C   THR C  83     4551   4963   5206    133    414   -218       C  
ATOM   5303  O   THR C  83      72.813 -12.233 -24.085  1.00 40.56           O  
ANISOU 5303  O   THR C  83     4795   5188   5427    137    415   -239       O  
ATOM   5304  CB  THR C  83      71.636 -10.177 -22.360  1.00 36.70           C  
ANISOU 5304  CB  THR C  83     4316   4688   4941    117    374   -181       C  
ATOM   5305  OG1 THR C  83      71.753  -8.978 -23.125  1.00 37.14           O  
ANISOU 5305  OG1 THR C  83     4367   4765   4977    102    385   -166       O  
ATOM   5306  CG2 THR C  83      71.043  -9.865 -20.951  1.00 34.08           C  
ANISOU 5306  CG2 THR C  83     3988   4336   4625    116    349   -164       C  
ATOM   5307  N   LYS C  84      74.328 -10.640 -24.293  1.00 39.14           N  
ANISOU 5307  N   LYS C  84     4585   5036   5249    128    434   -216       N  
ATOM   5308  CA  LYS C  84      74.677 -11.125 -25.637  1.00 39.27           C  
ANISOU 5308  CA  LYS C  84     4600   5075   5244    127    461   -240       C  
ATOM   5309  C   LYS C  84      76.138 -10.826 -25.850  1.00 39.52           C  
ANISOU 5309  C   LYS C  84     4604   5122   5288    133    482   -241       C  
ATOM   5310  O   LYS C  84      76.780 -10.195 -24.988  1.00 38.71           O  
ANISOU 5310  O   LYS C  84     4485   5012   5208    134    474   -221       O  
ATOM   5311  CB  LYS C  84      73.778 -10.538 -26.758  1.00 36.04           C  
ANISOU 5311  CB  LYS C  84     4208   4691   4792    106    465   -234       C  
ATOM   5312  CG  LYS C  84      73.406  -9.045 -26.697  1.00 36.17           C  
ANISOU 5312  CG  LYS C  84     4225   4719   4797     88    455   -197       C  
ATOM   5313  CD  LYS C  84      74.603  -8.126 -26.872  1.00 36.13           C  
ANISOU 5313  CD  LYS C  84     4196   4732   4798     83    469   -183       C  
ATOM   5314  CE  LYS C  84      74.283  -6.693 -27.295  1.00 33.98           C  
ANISOU 5314  CE  LYS C  84     3924   4478   4508     61    466   -150       C  
ATOM   5315  NZ  LYS C  84      75.575  -5.929 -27.440  1.00 33.01           N  
ANISOU 5315  NZ  LYS C  84     3776   4371   4395     58    481   -138       N  
ATOM   5316  N   ALA C  85      76.659 -11.264 -26.990  1.00 37.52           N  
ANISOU 5316  N   ALA C  85     4344   4890   5020    134    509   -265       N  
ATOM   5317  CA  ALA C  85      78.013 -10.957 -27.336  1.00 38.55           C  
ANISOU 5317  CA  ALA C  85     4448   5040   5158    137    532   -266       C  
ATOM   5318  C   ALA C  85      78.134  -9.408 -27.346  1.00 37.38           C  
ANISOU 5318  C   ALA C  85     4293   4910   4996    117    527   -230       C  
ATOM   5319  O   ALA C  85      77.365  -8.749 -28.008  1.00 37.73           O  
ANISOU 5319  O   ALA C  85     4351   4972   5009     99    525   -217       O  
ATOM   5320  CB  ALA C  85      78.335 -11.580 -28.697  1.00 40.70           C  
ANISOU 5320  CB  ALA C  85     4717   5339   5406    137    564   -299       C  
ATOM   5321  N   PRO C  86      79.070  -8.823 -26.566  1.00 37.11           N  
ANISOU 5321  N   PRO C  86     4237   4871   4990    121    523   -211       N  
ATOM   5322  CA  PRO C  86      79.066  -7.373 -26.425  1.00 37.37           C  
ANISOU 5322  CA  PRO C  86     4266   4914   5016    102    514   -177       C  
ATOM   5323  C   PRO C  86      79.121  -6.580 -27.719  1.00 39.21           C  
ANISOU 5323  C   PRO C  86     4496   5184   5215     82    532   -166       C  
ATOM   5324  O   PRO C  86      78.516  -5.507 -27.825  1.00 37.38           O  
ANISOU 5324  O   PRO C  86     4273   4957   4970     64    520   -139       O  
ATOM   5325  CB  PRO C  86      80.310  -7.121 -25.588  1.00 38.04           C  
ANISOU 5325  CB  PRO C  86     4325   4993   5135    110    513   -167       C  
ATOM   5326  CG  PRO C  86      80.290  -8.306 -24.658  1.00 39.30           C  
ANISOU 5326  CG  PRO C  86     4486   5123   5323    131    502   -184       C  
ATOM   5327  CD  PRO C  86      79.938  -9.455 -25.555  1.00 37.59           C  
ANISOU 5327  CD  PRO C  86     4280   4910   5092    141    519   -217       C  
ATOM   5328  N   GLY C  87      79.858  -7.109 -28.698  1.00 39.56           N  
ANISOU 5328  N   GLY C  87     4529   5255   5247     86    560   -188       N  
ATOM   5329  CA  GLY C  87      80.130  -6.362 -29.913  1.00 37.44           C  
ANISOU 5329  CA  GLY C  87     4251   5027   4945     66    579   -176       C  
ATOM   5330  C   GLY C  87      80.183  -7.233 -31.134  1.00 36.57           C  
ANISOU 5330  C   GLY C  87     4143   4945   4806     67    606   -209       C  
ATOM   5331  O   GLY C  87      80.300  -8.473 -31.061  1.00 35.98           O  
ANISOU 5331  O   GLY C  87     4070   4856   4742     87    615   -245       O  
ATOM   5332  N   LYS C  88      80.083  -6.588 -32.272  1.00 36.54           N  
ANISOU 5332  N   LYS C  88     4138   4981   4764     45    619   -197       N  
ATOM   5333  CA  LYS C  88      80.322  -7.298 -33.518  1.00 40.49           C  
ANISOU 5333  CA  LYS C  88     4635   5516   5231     42    649   -229       C  
ATOM   5334  C   LYS C  88      81.666  -8.050 -33.445  1.00 41.79           C  
ANISOU 5334  C   LYS C  88     4774   5682   5421     64    675   -258       C  
ATOM   5335  O   LYS C  88      81.780  -9.174 -33.889  1.00 40.56           O  
ANISOU 5335  O   LYS C  88     4621   5529   5261     77    695   -300       O  
ATOM   5336  CB  LYS C  88      80.387  -6.299 -34.646  1.00 40.36           C  
ANISOU 5336  CB  LYS C  88     4611   5549   5175     13    661   -204       C  
ATOM   5337  CG  LYS C  88      80.870  -6.945 -35.909  1.00 41.59           C  
ANISOU 5337  CG  LYS C  88     4757   5747   5295      8    696   -237       C  
ATOM   5338  CD  LYS C  88      79.690  -7.309 -36.780  1.00 40.72           C  
ANISOU 5338  CD  LYS C  88     4673   5656   5141     -8    694   -250       C  
ATOM   5339  CE  LYS C  88      80.208  -7.710 -38.160  1.00 39.88           C  
ANISOU 5339  CE  LYS C  88     4556   5604   4992    -20    730   -279       C  
ATOM   5340  NZ  LYS C  88      79.880  -9.133 -38.428  1.00 38.73           N  
ANISOU 5340  NZ  LYS C  88     4426   5449   4839     -7    744   -335       N  
ATOM   5341  N   SER C  89      82.672  -7.443 -32.826  1.00 43.51           N  
ANISOU 5341  N   SER C  89     4968   5895   5668     70    674   -236       N  
ATOM   5342  CA  SER C  89      83.993  -8.058 -32.834  1.00 44.71           C  
ANISOU 5342  CA  SER C  89     5092   6052   5844     89    700   -259       C  
ATOM   5343  C   SER C  89      84.053  -9.362 -32.044  1.00 45.96           C  
ANISOU 5343  C   SER C  89     5252   6169   6039    119    697   -291       C  
ATOM   5344  O   SER C  89      84.936 -10.185 -32.278  1.00 45.35           O  
ANISOU 5344  O   SER C  89     5156   6096   5979    138    723   -321       O  
ATOM   5345  CB  SER C  89      85.048  -7.082 -32.360  1.00 43.86           C  
ANISOU 5345  CB  SER C  89     4956   5950   5758     86    698   -225       C  
ATOM   5346  OG  SER C  89      84.997  -6.954 -30.975  1.00 44.02           O  
ANISOU 5346  OG  SER C  89     4978   5929   5818     96    670   -209       O  
ATOM   5347  N   ASP C  90      83.103  -9.572 -31.140  1.00 45.96           N  
ANISOU 5347  N   ASP C  90     5276   6132   6055    124    667   -285       N  
ATOM   5348  CA  ASP C  90      83.104 -10.793 -30.346  1.00 47.35           C  
ANISOU 5348  CA  ASP C  90     5454   6269   6268    150    660   -310       C  
ATOM   5349  C   ASP C  90      82.552 -11.999 -31.065  1.00 49.71           C  
ANISOU 5349  C   ASP C  90     5769   6566   6553    158    675   -354       C  
ATOM   5350  O   ASP C  90      81.369 -12.299 -30.981  1.00 51.50           O  
ANISOU 5350  O   ASP C  90     6024   6776   6766    153    657   -359       O  
ATOM   5351  CB  ASP C  90      82.431 -10.564 -29.007  1.00 46.35           C  
ANISOU 5351  CB  ASP C  90     5341   6105   6165    152    622   -285       C  
ATOM   5352  CG  ASP C  90      83.112  -9.510 -28.241  1.00 46.14           C  
ANISOU 5352  CG  ASP C  90     5295   6077   6157    147    610   -249       C  
ATOM   5353  OD1 ASP C  90      84.338  -9.610 -28.028  1.00 45.73           O  
ANISOU 5353  OD1 ASP C  90     5214   6028   6130    158    623   -249       O  
ATOM   5354  OD2 ASP C  90      82.442  -8.534 -27.887  1.00 48.95           O  
ANISOU 5354  OD2 ASP C  90     5665   6431   6503    129    588   -221       O  
ATOM   5355  N   LYS C  91      83.450 -12.714 -31.745  1.00 52.27           N  
ANISOU 5355  N   LYS C  91     6073   6903   6881    171    709   -388       N  
ATOM   5356  CA  LYS C  91      83.067 -13.814 -32.603  1.00 52.56           C  
ANISOU 5356  CA  LYS C  91     6124   6944   6903    176    730   -436       C  
ATOM   5357  C   LYS C  91      83.012 -15.105 -31.845  1.00 52.75           C  
ANISOU 5357  C   LYS C  91     6149   6920   6973    204    723   -461       C  
ATOM   5358  O   LYS C  91      83.773 -15.324 -30.912  1.00 55.69           O  
ANISOU 5358  O   LYS C  91     6500   7266   7393    224    717   -451       O  
ATOM   5359  CB  LYS C  91      84.063 -13.966 -33.743  1.00 56.79           C  
ANISOU 5359  CB  LYS C  91     6636   7520   7421    176    773   -464       C  
ATOM   5360  CG  LYS C  91      84.134 -12.785 -34.688  1.00 54.54           C  
ANISOU 5360  CG  LYS C  91     6347   7288   7085    146    784   -441       C  
ATOM   5361  CD  LYS C  91      85.215 -13.015 -35.732  1.00 59.74           C  
ANISOU 5361  CD  LYS C  91     6979   7987   7730    148    829   -469       C  
ATOM   5362  CE  LYS C  91      86.567 -13.344 -35.099  1.00 63.31           C  
ANISOU 5362  CE  LYS C  91     7396   8423   8236    177    842   -473       C  
ATOM   5363  NZ  LYS C  91      87.045 -12.295 -34.148  1.00 66.66           N  
ANISOU 5363  NZ  LYS C  91     7804   8838   8683    174    818   -420       N  
ATOM   5364  N   GLU C  92      82.097 -15.959 -32.261  1.00 53.30           N  
ANISOU 5364  N   GLU C  92     6244   6979   7028    203    723   -493       N  
ATOM   5365  CA  GLU C  92      81.931 -17.291 -31.686  1.00 56.95           C  
ANISOU 5365  CA  GLU C  92     6710   7394   7532    227    717   -521       C  
ATOM   5366  C   GLU C  92      81.710 -17.303 -30.149  1.00 57.56           C  
ANISOU 5366  C   GLU C  92     6787   7428   7653    239    679   -487       C  
ATOM   5367  O   GLU C  92      82.129 -18.232 -29.463  1.00 62.88           O  
ANISOU 5367  O   GLU C  92     7448   8065   8376    264    676   -498       O  
ATOM   5368  CB  GLU C  92      83.075 -18.219 -32.129  1.00 54.99           C  
ANISOU 5368  CB  GLU C  92     6435   7144   7315    251    755   -563       C  
ATOM   5369  N   TRP C  93      81.036 -16.275 -29.623  1.00 57.97           N  
ANISOU 5369  N   TRP C  93     6854   7485   7687    221    650   -446       N  
ATOM   5370  CA  TRP C  93      80.607 -16.238 -28.217  1.00 58.80           C  
ANISOU 5370  CA  TRP C  93     6965   7554   7823    227    613   -416       C  
ATOM   5371  C   TRP C  93      79.503 -17.228 -27.963  1.00 57.50           C  
ANISOU 5371  C   TRP C  93     6824   7357   7663    232    595   -433       C  
ATOM   5372  O   TRP C  93      78.598 -17.396 -28.784  1.00 54.14           O  
ANISOU 5372  O   TRP C  93     6424   6944   7202    218    599   -452       O  
ATOM   5373  CB  TRP C  93      80.103 -14.840 -27.830  1.00 62.56           C  
ANISOU 5373  CB  TRP C  93     7451   8046   8274    205    590   -373       C  
ATOM   5374  CG  TRP C  93      81.001 -14.058 -26.881  1.00 67.87           C  
ANISOU 5374  CG  TRP C  93     8099   8716   8973    208    580   -339       C  
ATOM   5375  CD1 TRP C  93      80.651 -13.516 -25.632  1.00 68.67           C  
ANISOU 5375  CD1 TRP C  93     8203   8797   9089    204    547   -306       C  
ATOM   5376  CD2 TRP C  93      82.430 -13.686 -27.073  1.00 71.79           C  
ANISOU 5376  CD2 TRP C  93     8561   9231   9483    214    602   -335       C  
ATOM   5377  NE1 TRP C  93      81.726 -12.872 -25.051  1.00 68.58           N  
ANISOU 5377  NE1 TRP C  93     8164   8791   9099    206    547   -283       N  
ATOM   5378  CE2 TRP C  93      82.826 -12.934 -25.863  1.00 73.45           C  
ANISOU 5378  CE2 TRP C  93     8758   9431   9717    211    578   -297       C  
ATOM   5379  CE3 TRP C  93      83.385 -13.898 -28.085  1.00 73.95           C  
ANISOU 5379  CE3 TRP C  93     8815   9531   9752    219    639   -358       C  
ATOM   5380  CZ2 TRP C  93      84.124 -12.422 -25.703  1.00 78.96           C  
ANISOU 5380  CZ2 TRP C  93     9423  10142  10433    214    589   -282       C  
ATOM   5381  CZ3 TRP C  93      84.691 -13.385 -27.908  1.00 79.29           C  
ANISOU 5381  CZ3 TRP C  93     9457  10222  10448    224    651   -342       C  
ATOM   5382  CH2 TRP C  93      85.050 -12.666 -26.748  1.00 84.94           C  
ANISOU 5382  CH2 TRP C  93    10160  10925  11186    221    626   -304       C  
ATOM   5383  N   ASN C  94      79.549 -17.903 -26.821  1.00 54.37           N  
ANISOU 5383  N   ASN C  94     6422   6923   7313    249    575   -426       N  
ATOM   5384  CA  ASN C  94      78.338 -18.570 -26.335  1.00 53.34           C  
ANISOU 5384  CA  ASN C  94     6317   6762   7186    249    549   -427       C  
ATOM   5385  C   ASN C  94      77.985 -17.992 -24.992  1.00 48.14           C  
ANISOU 5385  C   ASN C  94     5660   6089   6540    245    513   -385       C  
ATOM   5386  O   ASN C  94      78.716 -17.144 -24.473  1.00 45.37           O  
ANISOU 5386  O   ASN C  94     5290   5750   6198    243    510   -358       O  
ATOM   5387  CB  ASN C  94      78.470 -20.108 -26.280  1.00 53.78           C  
ANISOU 5387  CB  ASN C  94     6369   6783   7282    271    555   -461       C  
ATOM   5388  CG  ASN C  94      79.646 -20.575 -25.439  1.00 55.96           C  
ANISOU 5388  CG  ASN C  94     6610   7035   7614    295    556   -453       C  
ATOM   5389  OD1 ASN C  94      80.127 -19.873 -24.537  1.00 54.67           O  
ANISOU 5389  OD1 ASN C  94     6430   6874   7464    295    540   -416       O  
ATOM   5390  ND2 ASN C  94      80.115 -21.771 -25.733  1.00 57.76           N  
ANISOU 5390  ND2 ASN C  94     6826   7240   7878    316    574   -487       N  
ATOM   5391  N   ARG C  95      76.882 -18.480 -24.444  1.00 46.86           N  
ANISOU 5391  N   ARG C  95     5518   5903   6380    243    487   -381       N  
ATOM   5392  CA  ARG C  95      76.351 -18.040 -23.147  1.00 49.76           C  
ANISOU 5392  CA  ARG C  95     5891   6258   6758    237    453   -344       C  
ATOM   5393  C   ARG C  95      77.383 -18.083 -22.014  1.00 44.16           C  
ANISOU 5393  C   ARG C  95     5152   5534   6091    251    444   -323       C  
ATOM   5394  O   ARG C  95      77.530 -17.115 -21.269  1.00 42.12           O  
ANISOU 5394  O   ARG C  95     4887   5286   5829    242    429   -292       O  
ATOM   5395  CB  ARG C  95      75.123 -18.872 -22.755  1.00 52.69           C  
ANISOU 5395  CB  ARG C  95     6284   6602   7131    237    430   -348       C  
ATOM   5396  CG  ARG C  95      74.623 -18.589 -21.339  1.00 64.50           C  
ANISOU 5396  CG  ARG C  95     7782   8085   8640    233    395   -313       C  
ATOM   5397  CD  ARG C  95      73.113 -18.805 -21.173  1.00 74.72           C  
ANISOU 5397  CD  ARG C  95     9105   9369   9915    222    373   -308       C  
ATOM   5398  NE  ARG C  95      72.340 -18.549 -22.400  1.00 76.97           N  
ANISOU 5398  NE  ARG C  95     9413   9673  10157    208    386   -326       N  
ATOM   5399  CZ  ARG C  95      71.907 -17.357 -22.808  1.00 77.06           C  
ANISOU 5399  CZ  ARG C  95     9435   9712  10131    189    387   -311       C  
ATOM   5400  NH1 ARG C  95      72.155 -16.258 -22.093  1.00 82.35           N  
ANISOU 5400  NH1 ARG C  95    10096  10391  10802    184    378   -281       N  
ATOM   5401  NH2 ARG C  95      71.214 -17.273 -23.940  1.00 77.29           N  
ANISOU 5401  NH2 ARG C  95     9484   9759  10124    176    397   -325       N  
ATOM   5402  N   ASP C  96      78.083 -19.198 -21.881  1.00 40.95           N  
ANISOU 5402  N   ASP C  96     4727   5106   5726    273    452   -339       N  
ATOM   5403  CA  ASP C  96      79.136 -19.313 -20.853  1.00 41.95           C  
ANISOU 5403  CA  ASP C  96     4822   5221   5896    286    443   -317       C  
ATOM   5404  C   ASP C  96      80.128 -18.156 -20.826  1.00 39.24           C  
ANISOU 5404  C   ASP C  96     4457   4905   5545    279    453   -298       C  
ATOM   5405  O   ASP C  96      80.591 -17.784 -19.758  1.00 39.26           O  
ANISOU 5405  O   ASP C  96     4443   4906   5567    278    435   -269       O  
ATOM   5406  CB  ASP C  96      79.894 -20.651 -20.982  1.00 43.30           C  
ANISOU 5406  CB  ASP C  96     4971   5365   6116    311    458   -340       C  
ATOM   5407  CG  ASP C  96      79.012 -21.865 -20.643  1.00 45.86           C  
ANISOU 5407  CG  ASP C  96     5309   5653   6461    319    440   -350       C  
ATOM   5408  OD1 ASP C  96      77.840 -21.674 -20.212  1.00 46.39           O  
ANISOU 5408  OD1 ASP C  96     5402   5717   6506    304    414   -336       O  
ATOM   5409  OD2 ASP C  96      79.482 -23.010 -20.810  1.00 50.06           O  
ANISOU 5409  OD2 ASP C  96     5827   6158   7035    340    451   -371       O  
ATOM   5410  N   ASP C  97      80.441 -17.589 -21.984  1.00 37.85           N  
ANISOU 5410  N   ASP C  97     4283   4758   5341    272    481   -315       N  
ATOM   5411  CA  ASP C  97      81.416 -16.492 -22.068  1.00 40.07           C  
ANISOU 5411  CA  ASP C  97     4543   5066   5614    265    493   -297       C  
ATOM   5412  C   ASP C  97      80.943 -15.245 -21.310  1.00 38.60           C  
ANISOU 5412  C   ASP C  97     4367   4890   5407    244    468   -263       C  
ATOM   5413  O   ASP C  97      81.747 -14.414 -20.929  1.00 42.10           O  
ANISOU 5413  O   ASP C  97     4792   5348   5856    238    467   -241       O  
ATOM   5414  CB  ASP C  97      81.651 -16.118 -23.542  1.00 42.43           C  
ANISOU 5414  CB  ASP C  97     4845   5396   5879    259    527   -320       C  
ATOM   5415  CG  ASP C  97      82.577 -17.094 -24.265  1.00 46.14           C  
ANISOU 5415  CG  ASP C  97     5294   5864   6373    280    559   -354       C  
ATOM   5416  OD1 ASP C  97      83.540 -17.536 -23.616  1.00 47.10           O  
ANISOU 5416  OD1 ASP C  97     5386   5969   6539    297    559   -346       O  
ATOM   5417  OD2 ASP C  97      82.365 -17.398 -25.479  1.00 45.78           O  
ANISOU 5417  OD2 ASP C  97     5258   5831   6301    278    585   -387       O  
ATOM   5418  N   LEU C  98      79.642 -15.091 -21.102  1.00 36.55           N  
ANISOU 5418  N   LEU C  98     4138   4624   5125    232    448   -258       N  
ATOM   5419  CA  LEU C  98      79.106 -13.925 -20.368  1.00 35.66           C  
ANISOU 5419  CA  LEU C  98     4034   4518   4994    213    425   -229       C  
ATOM   5420  C   LEU C  98      79.455 -14.087 -18.896  1.00 35.08           C  
ANISOU 5420  C   LEU C  98     3945   4428   4953    217    401   -206       C  
ATOM   5421  O   LEU C  98      79.539 -13.105 -18.138  1.00 33.82           O  
ANISOU 5421  O   LEU C  98     3783   4277   4790    203    386   -183       O  
ATOM   5422  CB  LEU C  98      77.573 -13.814 -20.543  1.00 35.30           C  
ANISOU 5422  CB  LEU C  98     4023   4469   4919    201    412   -230       C  
ATOM   5423  CG  LEU C  98      77.156 -13.819 -22.037  1.00 37.38           C  
ANISOU 5423  CG  LEU C  98     4302   4750   5149    195    435   -253       C  
ATOM   5424  CD1 LEU C  98      75.646 -13.741 -22.290  1.00 36.28           C  
ANISOU 5424  CD1 LEU C  98     4195   4609   4980    182    422   -253       C  
ATOM   5425  CD2 LEU C  98      77.933 -12.806 -22.887  1.00 37.84           C  
ANISOU 5425  CD2 LEU C  98     4348   4839   5188    185    458   -248       C  
ATOM   5426  N   LEU C  99      79.636 -15.321 -18.469  1.00 33.97           N  
ANISOU 5426  N   LEU C  99     3796   4265   4846    234    395   -213       N  
ATOM   5427  CA  LEU C  99      79.793 -15.521 -17.035  1.00 34.00           C  
ANISOU 5427  CA  LEU C  99     3786   4255   4876    235    367   -189       C  
ATOM   5428  C   LEU C  99      80.920 -14.678 -16.419  1.00 35.82           C  
ANISOU 5428  C   LEU C  99     3990   4502   5118    229    365   -166       C  
ATOM   5429  O   LEU C  99      80.662 -13.996 -15.410  1.00 37.30           O  
ANISOU 5429  O   LEU C  99     4180   4693   5299    213    342   -144       O  
ATOM   5430  CB  LEU C  99      79.942 -16.985 -16.686  1.00 33.92           C  
ANISOU 5430  CB  LEU C  99     3765   4218   4905    255    361   -195       C  
ATOM   5431  CG  LEU C  99      78.661 -17.783 -16.965  1.00 34.26           C  
ANISOU 5431  CG  LEU C  99     3836   4243   4938    258    354   -212       C  
ATOM   5432  CD1 LEU C  99      78.946 -19.277 -17.060  1.00 33.21           C  
ANISOU 5432  CD1 LEU C  99     3691   4081   4846    280    358   -228       C  
ATOM   5433  CD2 LEU C  99      77.599 -17.479 -15.932  1.00 33.50           C  
ANISOU 5433  CD2 LEU C  99     3757   4143   4828    243    322   -190       C  
ATOM   5434  N   PRO C 100      82.156 -14.691 -17.006  1.00 34.24           N  
ANISOU 5434  N   PRO C 100     3764   4311   4933    238    389   -172       N  
ATOM   5435  CA  PRO C 100      83.174 -13.850 -16.333  1.00 34.14           C  
ANISOU 5435  CA  PRO C 100     3726   4314   4930    229    383   -147       C  
ATOM   5436  C   PRO C 100      82.877 -12.367 -16.371  1.00 33.01           C  
ANISOU 5436  C   PRO C 100     3597   4191   4754    205    380   -136       C  
ATOM   5437  O   PRO C 100      83.079 -11.678 -15.379  1.00 31.20           O  
ANISOU 5437  O   PRO C 100     3359   3966   4526    191    361   -115       O  
ATOM   5438  CB  PRO C 100      84.493 -14.143 -17.094  1.00 35.07           C  
ANISOU 5438  CB  PRO C 100     3814   4440   5069    244    412   -157       C  
ATOM   5439  CG  PRO C 100      84.233 -15.332 -17.962  1.00 34.53           C  
ANISOU 5439  CG  PRO C 100     3752   4356   5010    265    431   -188       C  
ATOM   5440  CD  PRO C 100      82.768 -15.712 -17.877  1.00 34.42           C  
ANISOU 5440  CD  PRO C 100     3773   4326   4978    261    415   -197       C  
ATOM   5441  N   LEU C 101      82.383 -11.873 -17.496  1.00 32.44           N  
ANISOU 5441  N   LEU C 101     3544   4131   4651    199    398   -151       N  
ATOM   5442  CA  LEU C 101      81.982 -10.471 -17.544  1.00 32.99           C  
ANISOU 5442  CA  LEU C 101     3627   4215   4692    176    394   -138       C  
ATOM   5443  C   LEU C 101      80.969 -10.100 -16.449  1.00 33.14           C  
ANISOU 5443  C   LEU C 101     3664   4222   4703    163    365   -126       C  
ATOM   5444  O   LEU C 101      81.085  -9.014 -15.822  1.00 32.90           O  
ANISOU 5444  O   LEU C 101     3632   4199   4669    146    354   -109       O  
ATOM   5445  CB  LEU C 101      81.382 -10.127 -18.911  1.00 34.14           C  
ANISOU 5445  CB  LEU C 101     3792   4373   4806    171    414   -153       C  
ATOM   5446  CG  LEU C 101      82.421 -10.255 -20.006  1.00 35.42           C  
ANISOU 5446  CG  LEU C 101     3934   4552   4968    179    445   -165       C  
ATOM   5447  CD1 LEU C 101      81.828  -9.821 -21.340  1.00 35.64           C  
ANISOU 5447  CD1 LEU C 101     3981   4600   4961    170    464   -176       C  
ATOM   5448  CD2 LEU C 101      83.542  -9.333 -19.563  1.00 35.93           C  
ANISOU 5448  CD2 LEU C 101     3972   4630   5045    170    445   -143       C  
ATOM   5449  N   ASN C 102      79.982 -10.973 -16.216  1.00 29.33           N  
ANISOU 5449  N   ASN C 102     3200   3723   4220    171    353   -134       N  
ATOM   5450  CA  ASN C 102      78.891 -10.542 -15.378  1.00 27.78           C  
ANISOU 5450  CA  ASN C 102     3023   3519   4010    158    329   -124       C  
ATOM   5451  C   ASN C 102      79.358 -10.703 -13.966  1.00 28.67           C  
ANISOU 5451  C   ASN C 102     3119   3629   4145    155    307   -108       C  
ATOM   5452  O   ASN C 102      78.955  -9.950 -13.109  1.00 29.50           O  
ANISOU 5452  O   ASN C 102     3231   3737   4241    139    290    -96       O  
ATOM   5453  CB  ASN C 102      77.569 -11.256 -15.701  1.00 26.83           C  
ANISOU 5453  CB  ASN C 102     2930   3386   3876    163    324   -137       C  
ATOM   5454  CG  ASN C 102      76.885 -10.680 -16.957  1.00 26.57           C  
ANISOU 5454  CG  ASN C 102     2919   3364   3813    156    341   -147       C  
ATOM   5455  OD1 ASN C 102      76.984  -9.468 -17.255  1.00 26.45           O  
ANISOU 5455  OD1 ASN C 102     2903   3362   3782    142    347   -138       O  
ATOM   5456  ND2 ASN C 102      76.157 -11.511 -17.656  1.00 24.64           N  
ANISOU 5456  ND2 ASN C 102     2690   3112   3558    164    346   -164       N  
ATOM   5457  N   ASN C 103      80.255 -11.639 -13.728  1.00 29.60           N  
ANISOU 5457  N   ASN C 103     3212   3740   4291    170    308   -106       N  
ATOM   5458  CA  ASN C 103      80.922 -11.716 -12.429  1.00 31.06           C  
ANISOU 5458  CA  ASN C 103     3375   3927   4498    165    287    -85       C  
ATOM   5459  C   ASN C 103      81.651 -10.446 -12.040  1.00 31.34           C  
ANISOU 5459  C   ASN C 103     3397   3981   4528    146    286    -71       C  
ATOM   5460  O   ASN C 103      81.600 -10.055 -10.875  1.00 33.54           O  
ANISOU 5460  O   ASN C 103     3673   4264   4806    130    264    -57       O  
ATOM   5461  CB  ASN C 103      81.869 -12.885 -12.330  1.00 30.34           C  
ANISOU 5461  CB  ASN C 103     3255   3827   4443    184    289    -82       C  
ATOM   5462  CG  ASN C 103      82.436 -13.047 -10.924  1.00 33.11           C  
ANISOU 5462  CG  ASN C 103     3583   4181   4815    177    264    -55       C  
ATOM   5463  OD1 ASN C 103      81.750 -12.880  -9.914  1.00 33.30           O  
ANISOU 5463  OD1 ASN C 103     3617   4206   4829    163    240    -44       O  
ATOM   5464  ND2 ASN C 103      83.691 -13.399 -10.852  1.00 36.75           N  
ANISOU 5464  ND2 ASN C 103     4010   4644   5306    186    269    -45       N  
ATOM   5465  N   LYS C 104      82.331  -9.803 -12.987  1.00 32.38           N  
ANISOU 5465  N   LYS C 104     3522   4124   4655    145    309    -76       N  
ATOM   5466  CA  LYS C 104      83.058  -8.542 -12.703  1.00 33.53           C  
ANISOU 5466  CA  LYS C 104     3655   4286   4797    126    308    -63       C  
ATOM   5467  C   LYS C 104      82.100  -7.421 -12.280  1.00 31.04           C  
ANISOU 5467  C   LYS C 104     3364   3971   4458    104    297    -62       C  
ATOM   5468  O   LYS C 104      82.233  -6.769 -11.196  1.00 30.39           O  
ANISOU 5468  O   LYS C 104     3276   3893   4375     86    279    -51       O  
ATOM   5469  CB  LYS C 104      83.910  -8.117 -13.886  1.00 36.14           C  
ANISOU 5469  CB  LYS C 104     3973   4630   5127    130    336    -68       C  
ATOM   5470  CG  LYS C 104      85.190  -8.925 -14.086  1.00 43.04           C  
ANISOU 5470  CG  LYS C 104     4814   5507   6031    147    348    -65       C  
ATOM   5471  CD  LYS C 104      86.147  -8.241 -15.092  1.00 48.02           C  
ANISOU 5471  CD  LYS C 104     5429   6157   6659    145    374    -65       C  
ATOM   5472  CE  LYS C 104      85.875  -6.716 -15.134  1.00 55.25           C  
ANISOU 5472  CE  LYS C 104     6358   7084   7551    119    371    -57       C  
ATOM   5473  NZ  LYS C 104      86.990  -5.783 -15.498  1.00 56.44           N  
ANISOU 5473  NZ  LYS C 104     6485   7253   7705    107    383    -44       N  
ATOM   5474  N   ILE C 105      81.072  -7.249 -13.087  1.00 29.51           N  
ANISOU 5474  N   ILE C 105     3196   3772   4243    106    306    -74       N  
ATOM   5475  CA  ILE C 105      79.921  -6.463 -12.650  1.00 27.21           C  
ANISOU 5475  CA  ILE C 105     2929   3475   3932     91    293    -74       C  
ATOM   5476  C   ILE C 105      79.455  -6.717 -11.217  1.00 25.80           C  
ANISOU 5476  C   ILE C 105     2752   3291   3757     84    267    -68       C  
ATOM   5477  O   ILE C 105      79.279  -5.766 -10.506  1.00 25.06           O  
ANISOU 5477  O   ILE C 105     2662   3201   3657     65    258    -65       O  
ATOM   5478  CB  ILE C 105      78.763  -6.634 -13.580  1.00 26.73           C  
ANISOU 5478  CB  ILE C 105     2894   3407   3852     97    302    -86       C  
ATOM   5479  CG1 ILE C 105      79.210  -6.146 -14.965  1.00 27.31           C  
ANISOU 5479  CG1 ILE C 105     2965   3493   3919     98    327    -89       C  
ATOM   5480  CG2 ILE C 105      77.601  -5.856 -12.987  1.00 25.03           C  
ANISOU 5480  CG2 ILE C 105     2699   3185   3622     83    288    -84       C  
ATOM   5481  CD1 ILE C 105      78.087  -6.145 -15.985  1.00 29.51           C  
ANISOU 5481  CD1 ILE C 105     3268   3769   4174    100    336    -97       C  
ATOM   5482  N   MET C 106      79.276  -7.974 -10.810  1.00 25.04           N  
ANISOU 5482  N   MET C 106     2653   3188   3670     97    257    -68       N  
ATOM   5483  CA  MET C 106      78.818  -8.288  -9.467  1.00 26.17           C  
ANISOU 5483  CA  MET C 106     2797   3330   3814     89    232    -60       C  
ATOM   5484  C   MET C 106      79.847  -7.955  -8.423  1.00 27.13           C  
ANISOU 5484  C   MET C 106     2894   3464   3948     75    219    -46       C  
ATOM   5485  O   MET C 106      79.464  -7.528  -7.332  1.00 29.15           O  
ANISOU 5485  O   MET C 106     3153   3726   4194     57    201    -41       O  
ATOM   5486  CB  MET C 106      78.408  -9.795  -9.275  1.00 26.71           C  
ANISOU 5486  CB  MET C 106     2867   3386   3895    106    221    -59       C  
ATOM   5487  CG  MET C 106      77.315 -10.265 -10.220  1.00 27.44           C  
ANISOU 5487  CG  MET C 106     2985   3466   3975    118    231    -74       C  
ATOM   5488  SD  MET C 106      75.807  -9.269 -10.006  1.00 30.37           S  
ANISOU 5488  SD  MET C 106     3387   3837   4315    102    225    -79       S  
ATOM   5489  CE  MET C 106      75.026  -9.323 -11.655  1.00 28.28           C  
ANISOU 5489  CE  MET C 106     3145   3565   4035    113    246    -95       C  
ATOM   5490  N   ILE C 107      81.149  -8.175  -8.723  1.00 26.66           N  
ANISOU 5490  N   ILE C 107     2807   3410   3908     82    227    -38       N  
ATOM   5491  CA  ILE C 107      82.238  -7.733  -7.788  1.00 26.23           C  
ANISOU 5491  CA  ILE C 107     2728   3373   3866     66    215    -22       C  
ATOM   5492  C   ILE C 107      82.141  -6.199  -7.607  1.00 26.15           C  
ANISOU 5492  C   ILE C 107     2727   3371   3838     41    216    -26       C  
ATOM   5493  O   ILE C 107      82.207  -5.671  -6.484  1.00 25.59           O  
ANISOU 5493  O   ILE C 107     2651   3309   3761     20    199    -21       O  
ATOM   5494  CB  ILE C 107      83.665  -8.136  -8.295  1.00 25.03           C  
ANISOU 5494  CB  ILE C 107     2544   3226   3740     78    228    -13       C  
ATOM   5495  CG1 ILE C 107      83.904  -9.639  -8.110  1.00 24.62           C  
ANISOU 5495  CG1 ILE C 107     2475   3164   3713     99    221     -5       C  
ATOM   5496  CG2 ILE C 107      84.783  -7.312  -7.664  1.00 24.64           C  
ANISOU 5496  CG2 ILE C 107     2470   3194   3697     58    221      1       C  
ATOM   5497  CD1 ILE C 107      84.969 -10.191  -9.039  1.00 24.24           C  
ANISOU 5497  CD1 ILE C 107     2404   3114   3690    121    243     -6       C  
ATOM   5498  N   GLU C 108      81.911  -5.498  -8.696  1.00 26.56           N  
ANISOU 5498  N   GLU C 108     2792   3417   3881     43    237    -37       N  
ATOM   5499  CA  GLU C 108      81.881  -4.048  -8.561  1.00 28.63           C  
ANISOU 5499  CA  GLU C 108     3061   3683   4133     21    238    -39       C  
ATOM   5500  C   GLU C 108      80.688  -3.590  -7.741  1.00 28.71           C  
ANISOU 5500  C   GLU C 108     3093   3688   4126      7    224    -48       C  
ATOM   5501  O   GLU C 108      80.855  -2.818  -6.783  1.00 28.67           O  
ANISOU 5501  O   GLU C 108     3085   3690   4119    -14    212    -47       O  
ATOM   5502  CB  GLU C 108      81.890  -3.400  -9.884  1.00 30.45           C  
ANISOU 5502  CB  GLU C 108     3298   3910   4359     25    261    -44       C  
ATOM   5503  CG  GLU C 108      81.666  -1.943  -9.723  1.00 34.56           C  
ANISOU 5503  CG  GLU C 108     3828   4430   4873      3    261    -46       C  
ATOM   5504  CD  GLU C 108      82.173  -1.208 -10.914  1.00 41.50           C  
ANISOU 5504  CD  GLU C 108     4702   5311   5754      2    281    -42       C  
ATOM   5505  OE1 GLU C 108      82.266  -1.834 -12.014  1.00 47.92           O  
ANISOU 5505  OE1 GLU C 108     5515   6127   6565     20    297    -43       O  
ATOM   5506  OE2 GLU C 108      82.501  -0.012 -10.740  1.00 47.37           O  
ANISOU 5506  OE2 GLU C 108     5441   6055   6500    -17    280    -38       O  
ATOM   5507  N   ILE C 109      79.488  -4.119  -8.073  1.00 28.51           N  
ANISOU 5507  N   ILE C 109     3090   3651   4090     20    225    -56       N  
ATOM   5508  CA  ILE C 109      78.252  -3.776  -7.320  1.00 26.35           C  
ANISOU 5508  CA  ILE C 109     2837   3372   3800     10    214    -64       C  
ATOM   5509  C   ILE C 109      78.327  -4.170  -5.831  1.00 26.22           C  
ANISOU 5509  C   ILE C 109     2811   3367   3782     -2    190    -59       C  
ATOM   5510  O   ILE C 109      77.978  -3.371  -4.928  1.00 26.48           O  
ANISOU 5510  O   ILE C 109     2850   3405   3806    -22    181    -65       O  
ATOM   5511  CB  ILE C 109      77.040  -4.437  -7.936  1.00 25.00           C  
ANISOU 5511  CB  ILE C 109     2688   3189   3619     26    218    -70       C  
ATOM   5512  CG1 ILE C 109      76.887  -3.999  -9.383  1.00 24.30           C  
ANISOU 5512  CG1 ILE C 109     2610   3094   3528     35    239    -74       C  
ATOM   5513  CG2 ILE C 109      75.795  -4.138  -7.105  1.00 25.13           C  
ANISOU 5513  CG2 ILE C 109     2723   3202   3621     16    206    -77       C  
ATOM   5514  CD1 ILE C 109      75.649  -4.580  -9.995  1.00 23.73           C  
ANISOU 5514  CD1 ILE C 109     2560   3011   3444     48    242    -80       C  
ATOM   5515  N   GLY C 110      78.819  -5.365  -5.574  1.00 25.77           N  
ANISOU 5515  N   GLY C 110     2739   3315   3737      8    181    -47       N  
ATOM   5516  CA  GLY C 110      78.855  -5.833  -4.219  1.00 28.08           C  
ANISOU 5516  CA  GLY C 110     3020   3620   4027     -3    158    -38       C  
ATOM   5517  C   GLY C 110      79.838  -5.117  -3.341  1.00 30.59           C  
ANISOU 5517  C   GLY C 110     3318   3957   4347    -27    148    -31       C  
ATOM   5518  O   GLY C 110      79.624  -4.991  -2.129  1.00 34.97           O  
ANISOU 5518  O   GLY C 110     3870   4526   4889    -47    130    -30       O  
ATOM   5519  N   GLY C 111      80.942  -4.653  -3.935  1.00 29.25           N  
ANISOU 5519  N   GLY C 111     3133   3789   4191    -27    160    -27       N  
ATOM   5520  CA  GLY C 111      81.837  -3.811  -3.202  1.00 29.44           C  
ANISOU 5520  CA  GLY C 111     3139   3829   4215    -52    152    -23       C  
ATOM   5521  C   GLY C 111      81.103  -2.543  -2.774  1.00 30.15           C  
ANISOU 5521  C   GLY C 111     3249   3917   4287    -75    153    -42       C  
ATOM   5522  O   GLY C 111      81.240  -2.064  -1.662  1.00 30.39           O  
ANISOU 5522  O   GLY C 111     3275   3963   4308   -100    138    -45       O  
ATOM   5523  N   HIS C 112      80.377  -1.936  -3.683  1.00 30.30           N  
ANISOU 5523  N   HIS C 112     3290   3917   4303    -66    170    -55       N  
ATOM   5524  CA  HIS C 112      79.678  -0.684  -3.295  1.00 32.06           C  
ANISOU 5524  CA  HIS C 112     3531   4136   4515    -86    172    -74       C  
ATOM   5525  C   HIS C 112      78.531  -0.853  -2.296  1.00 29.62           C  
ANISOU 5525  C   HIS C 112     3236   3829   4187    -94    160    -85       C  
ATOM   5526  O   HIS C 112      78.194   0.091  -1.597  1.00 28.30           O  
ANISOU 5526  O   HIS C 112     3076   3664   4011   -115    157   -101       O  
ATOM   5527  CB  HIS C 112      79.157   0.004  -4.514  1.00 32.01           C  
ANISOU 5527  CB  HIS C 112     3540   4108   4512    -75    192    -81       C  
ATOM   5528  CG  HIS C 112      80.233   0.622  -5.367  1.00 33.82           C  
ANISOU 5528  CG  HIS C 112     3756   4336   4756    -77    205    -73       C  
ATOM   5529  ND1 HIS C 112      80.840   1.781  -5.036  1.00 33.79           N  
ANISOU 5529  ND1 HIS C 112     3745   4334   4759   -100    205    -77       N  
ATOM   5530  CD2 HIS C 112      80.718   0.265  -6.651  1.00 32.97           C  
ANISOU 5530  CD2 HIS C 112     3642   4225   4657    -58    221    -63       C  
ATOM   5531  CE1 HIS C 112      81.705   2.123  -6.031  1.00 34.41           C  
ANISOU 5531  CE1 HIS C 112     3810   4411   4850    -96    219    -66       C  
ATOM   5532  NE2 HIS C 112      81.617   1.201  -7.010  1.00 33.29           N  
ANISOU 5532  NE2 HIS C 112     3671   4268   4709    -70    229    -58       N  
ATOM   5533  N   ILE C 113      77.952  -2.053  -2.230  1.00 27.92           N  
ANISOU 5533  N   ILE C 113     3025   3615   3967    -77    152    -78       N  
ATOM   5534  CA  ILE C 113      76.849  -2.289  -1.343  1.00 28.87           C  
ANISOU 5534  CA  ILE C 113     3158   3741   4069    -84    141    -86       C  
ATOM   5535  C   ILE C 113      77.425  -2.392   0.066  1.00 32.17           C  
ANISOU 5535  C   ILE C 113     3557   4185   4478   -109    120    -80       C  
ATOM   5536  O   ILE C 113      76.878  -1.810   1.029  1.00 31.95           O  
ANISOU 5536  O   ILE C 113     3537   4169   4433   -130    114    -96       O  
ATOM   5537  CB  ILE C 113      76.155  -3.566  -1.759  1.00 29.63           C  
ANISOU 5537  CB  ILE C 113     3261   3830   4165    -60    138    -76       C  
ATOM   5538  CG1 ILE C 113      75.393  -3.287  -3.069  1.00 28.61           C  
ANISOU 5538  CG1 ILE C 113     3154   3678   4039    -41    158    -85       C  
ATOM   5539  CG2 ILE C 113      75.291  -4.146  -0.624  1.00 29.11           C  
ANISOU 5539  CG2 ILE C 113     3199   3777   4081    -68    120    -75       C  
ATOM   5540  CD1 ILE C 113      74.565  -4.468  -3.511  1.00 30.81           C  
ANISOU 5540  CD1 ILE C 113     3442   3947   4314    -19    156    -79       C  
ATOM   5541  N   LYS C 114      78.573  -3.066   0.155  1.00 32.69           N  
ANISOU 5541  N   LYS C 114     3599   4263   4556   -107    111    -59       N  
ATOM   5542  CA  LYS C 114      79.248  -3.280   1.417  1.00 35.48           C  
ANISOU 5542  CA  LYS C 114     3931   4645   4903   -131     89    -47       C  
ATOM   5543  C   LYS C 114      79.564  -1.916   1.987  1.00 33.86           C  
ANISOU 5543  C   LYS C 114     3726   4450   4689   -161     91    -66       C  
ATOM   5544  O   LYS C 114      79.409  -1.666   3.189  1.00 32.43           O  
ANISOU 5544  O   LYS C 114     3542   4291   4488   -188     77    -73       O  
ATOM   5545  CB  LYS C 114      80.525  -4.120   1.207  1.00 36.31           C  
ANISOU 5545  CB  LYS C 114     4007   4757   5030   -121     82    -20       C  
ATOM   5546  CG  LYS C 114      81.139  -4.665   2.484  1.00 40.51           C  
ANISOU 5546  CG  LYS C 114     4514   5319   5557   -142     56      0       C  
ATOM   5547  CD  LYS C 114      82.414  -5.499   2.263  1.00 41.43           C  
ANISOU 5547  CD  LYS C 114     4598   5440   5701   -131     49     31       C  
ATOM   5548  CE  LYS C 114      82.875  -6.060   3.602  1.00 45.09           C  
ANISOU 5548  CE  LYS C 114     5037   5936   6158   -153     20     55       C  
ATOM   5549  NZ  LYS C 114      84.365  -6.229   3.764  1.00 48.13           N  
ANISOU 5549  NZ  LYS C 114     5386   6336   6564   -160     11     82       N  
ATOM   5550  N   LYS C 115      80.024  -1.034   1.115  1.00 34.36           N  
ANISOU 5550  N   LYS C 115     3792   4496   4766   -158    108    -74       N  
ATOM   5551  CA  LYS C 115      80.348   0.330   1.525  1.00 33.57           C  
ANISOU 5551  CA  LYS C 115     3692   4399   4662   -186    111    -92       C  
ATOM   5552  C   LYS C 115      79.198   1.308   1.900  1.00 33.24           C  
ANISOU 5552  C   LYS C 115     3675   4347   4606   -199    119   -124       C  
ATOM   5553  O   LYS C 115      79.313   1.971   2.898  1.00 33.78           O  
ANISOU 5553  O   LYS C 115     3740   4430   4662   -228    111   -139       O  
ATOM   5554  CB  LYS C 115      81.262   0.967   0.494  1.00 33.80           C  
ANISOU 5554  CB  LYS C 115     3714   4415   4713   -181    126    -87       C  
ATOM   5555  CG  LYS C 115      81.574   2.438   0.750  1.00 35.33           C  
ANISOU 5555  CG  LYS C 115     3910   4605   4909   -208    131   -106       C  
ATOM   5556  CD  LYS C 115      82.809   2.838  -0.067  1.00 40.19           C  
ANISOU 5556  CD  LYS C 115     4508   5215   5545   -207    139    -92       C  
ATOM   5557  CE  LYS C 115      82.411   3.208  -1.504  1.00 40.78           C  
ANISOU 5557  CE  LYS C 115     4597   5262   5634   -184    162    -93       C  
ATOM   5558  NZ  LYS C 115      81.812   4.590  -1.518  1.00 45.01           N  
ANISOU 5558  NZ  LYS C 115     5150   5778   6172   -200    171   -116       N  
ATOM   5559  N   ASN C 116      78.130   1.384   1.101  1.00 32.58           N  
ANISOU 5559  N   ASN C 116     3614   4239   4526   -177    134   -133       N  
ATOM   5560  CA  ASN C 116      77.080   2.401   1.184  1.00 33.24           C  
ANISOU 5560  CA  ASN C 116     3718   4306   4605   -184    146   -160       C  
ATOM   5561  C   ASN C 116      75.745   1.949   1.749  1.00 32.26           C  
ANISOU 5561  C   ASN C 116     3609   4185   4461   -179    142   -170       C  
ATOM   5562  O   ASN C 116      75.023   2.780   2.212  1.00 31.65           O  
ANISOU 5562  O   ASN C 116     3544   4103   4379   -191    149   -195       O  
ATOM   5563  CB  ASN C 116      76.729   2.893  -0.222  1.00 35.12           C  
ANISOU 5563  CB  ASN C 116     3969   4513   4861   -162    166   -159       C  
ATOM   5564  CG  ASN C 116      77.917   3.477  -0.950  1.00 38.98           C  
ANISOU 5564  CG  ASN C 116     4445   4995   5370   -166    173   -150       C  
ATOM   5565  OD1 ASN C 116      78.581   2.803  -1.739  1.00 37.08           O  
ANISOU 5565  OD1 ASN C 116     4194   4757   5138   -149    175   -129       O  
ATOM   5566  ND2 ASN C 116      78.147   4.751  -0.739  1.00 40.61           N  
ANISOU 5566  ND2 ASN C 116     4651   5192   5585   -187    179   -166       N  
ATOM   5567  N   CYS C 117      75.404   0.651   1.657  1.00 31.28           N  
ANISOU 5567  N   CYS C 117     3484   4068   4330   -161    133   -152       N  
ATOM   5568  CA  CYS C 117      74.079   0.139   2.059  1.00 31.60           C  
ANISOU 5568  CA  CYS C 117     3538   4111   4354   -154    130   -157       C  
ATOM   5569  C   CYS C 117      74.152  -1.336   2.481  1.00 31.46           C  
ANISOU 5569  C   CYS C 117     3510   4114   4327   -147    111   -133       C  
ATOM   5570  O   CYS C 117      73.460  -2.177   1.927  1.00 29.66           O  
ANISOU 5570  O   CYS C 117     3291   3875   4101   -124    112   -123       O  
ATOM   5571  CB  CYS C 117      73.011   0.330   0.937  1.00 30.49           C  
ANISOU 5571  CB  CYS C 117     3420   3941   4223   -129    148   -162       C  
ATOM   5572  SG  CYS C 117      73.378  -0.318  -0.724  1.00 32.03           S  
ANISOU 5572  SG  CYS C 117     3616   4116   4437    -98    158   -140       S  
ATOM   5573  N   PRO C 118      75.002  -1.635   3.475  1.00 31.69           N  
ANISOU 5573  N   PRO C 118     3519   4171   4348   -168     93   -123       N  
ATOM   5574  CA  PRO C 118      75.127  -2.974   3.964  1.00 32.20           C  
ANISOU 5574  CA  PRO C 118     3570   4254   4408   -164     73    -97       C  
ATOM   5575  C   PRO C 118      73.810  -3.546   4.500  1.00 33.25           C  
ANISOU 5575  C   PRO C 118     3716   4396   4522   -162     67    -99       C  
ATOM   5576  O   PRO C 118      73.731  -4.755   4.648  1.00 33.26           O  
ANISOU 5576  O   PRO C 118     3708   4404   4523   -152     52    -75       O  
ATOM   5577  CB  PRO C 118      76.148  -2.843   5.111  1.00 32.23           C  
ANISOU 5577  CB  PRO C 118     3550   4292   4402   -195     55    -90       C  
ATOM   5578  CG  PRO C 118      76.255  -1.384   5.400  1.00 31.11           C  
ANISOU 5578  CG  PRO C 118     3415   4150   4253   -219     66   -120       C  
ATOM   5579  CD  PRO C 118      76.021  -0.749   4.072  1.00 31.44           C  
ANISOU 5579  CD  PRO C 118     3473   4154   4316   -196     90   -132       C  
ATOM   5580  N   ASN C 119      72.792  -2.737   4.783  1.00 31.35           N  
ANISOU 5580  N   ASN C 119     3492   4152   4266   -170     77   -126       N  
ATOM   5581  CA  ASN C 119      71.579  -3.353   5.311  1.00 31.44           C  
ANISOU 5581  CA  ASN C 119     3513   4174   4258   -168     70   -125       C  
ATOM   5582  C   ASN C 119      70.460  -3.388   4.340  1.00 28.99           C  
ANISOU 5582  C   ASN C 119     3223   3834   3955   -142     86   -131       C  
ATOM   5583  O   ASN C 119      69.325  -3.643   4.697  1.00 28.38           O  
ANISOU 5583  O   ASN C 119     3156   3762   3864   -141     84   -135       O  
ATOM   5584  CB  ASN C 119      71.127  -2.717   6.609  1.00 35.28           C  
ANISOU 5584  CB  ASN C 119     3998   4688   4716   -198     67   -147       C  
ATOM   5585  CG  ASN C 119      72.243  -2.649   7.600  1.00 41.94           C  
ANISOU 5585  CG  ASN C 119     4820   5565   5549   -228     51   -140       C  
ATOM   5586  OD1 ASN C 119      72.925  -3.634   7.816  1.00 43.22           O  
ANISOU 5586  OD1 ASN C 119     4963   5742   5713   -229     31   -109       O  
ATOM   5587  ND2 ASN C 119      72.485  -1.474   8.157  1.00 44.85           N  
ANISOU 5587  ND2 ASN C 119     5190   5942   5908   -254     58   -169       N  
ATOM   5588  N   ALA C 120      70.767  -3.132   3.094  1.00 28.00           N  
ANISOU 5588  N   ALA C 120     3104   3680   3852   -122    100   -130       N  
ATOM   5589  CA  ALA C 120      69.716  -3.236   2.116  1.00 26.52           C  
ANISOU 5589  CA  ALA C 120     2937   3468   3671    -99    113   -133       C  
ATOM   5590  C   ALA C 120      69.336  -4.670   1.854  1.00 26.78           C  
ANISOU 5590  C   ALA C 120     2970   3500   3705    -81    101   -110       C  
ATOM   5591  O   ALA C 120      70.095  -5.639   2.139  1.00 25.91           O  
ANISOU 5591  O   ALA C 120     2843   3402   3599    -81     85    -89       O  
ATOM   5592  CB  ALA C 120      70.144  -2.594   0.820  1.00 29.30           C  
ANISOU 5592  CB  ALA C 120     3295   3793   4044    -85    131   -136       C  
ATOM   5593  N   PHE C 121      68.181  -4.775   1.210  1.00 27.47           N  
ANISOU 5593  N   PHE C 121     3075   3571   3791    -65    109   -113       N  
ATOM   5594  CA  PHE C 121      67.657  -5.994   0.737  1.00 28.02           C  
ANISOU 5594  CA  PHE C 121     3149   3632   3863    -47    102    -96       C  
ATOM   5595  C   PHE C 121      67.846  -5.992  -0.796  1.00 28.34           C  
ANISOU 5595  C   PHE C 121     3199   3646   3921    -25    117    -95       C  
ATOM   5596  O   PHE C 121      67.543  -4.978  -1.473  1.00 27.98           O  
ANISOU 5596  O   PHE C 121     3164   3585   3878    -22    134   -108       O  
ATOM   5597  CB  PHE C 121      66.154  -6.068   1.164  1.00 27.58           C  
ANISOU 5597  CB  PHE C 121     3106   3581   3789    -48    100   -101       C  
ATOM   5598  CG  PHE C 121      65.491  -7.323   0.705  1.00 28.01           C  
ANISOU 5598  CG  PHE C 121     3167   3627   3846    -31     91    -83       C  
ATOM   5599  CD1 PHE C 121      65.720  -8.524   1.364  1.00 28.49           C  
ANISOU 5599  CD1 PHE C 121     3216   3703   3906    -34     69    -63       C  
ATOM   5600  CD2 PHE C 121      64.717  -7.334  -0.455  1.00 28.42           C  
ANISOU 5600  CD2 PHE C 121     3236   3656   3903    -13    102    -85       C  
ATOM   5601  CE1 PHE C 121      65.112  -9.697   0.945  1.00 27.51           C  
ANISOU 5601  CE1 PHE C 121     3097   3569   3787    -19     60    -47       C  
ATOM   5602  CE2 PHE C 121      64.110  -8.517  -0.892  1.00 29.85           C  
ANISOU 5602  CE2 PHE C 121     3424   3829   4087      0     93    -71       C  
ATOM   5603  CZ  PHE C 121      64.316  -9.694  -0.197  1.00 27.51           C  
ANISOU 5603  CZ  PHE C 121     3116   3545   3791     -2     73    -53       C  
ATOM   5604  N   ILE C 122      68.355  -7.104  -1.350  1.00 26.79           N  
ANISOU 5604  N   ILE C 122     2997   3444   3738    -10    111    -79       N  
ATOM   5605  CA  ILE C 122      68.894  -7.132  -2.698  1.00 26.06           C  
ANISOU 5605  CA  ILE C 122     2907   3332   3661      6    125    -79       C  
ATOM   5606  C   ILE C 122      68.191  -8.186  -3.481  1.00 25.02           C  
ANISOU 5606  C   ILE C 122     2787   3187   3532     25    124    -73       C  
ATOM   5607  O   ILE C 122      68.022  -9.303  -3.016  1.00 24.19           O  
ANISOU 5607  O   ILE C 122     2677   3086   3428     28    108    -60       O  
ATOM   5608  CB  ILE C 122      70.385  -7.655  -2.760  1.00 27.86           C  
ANISOU 5608  CB  ILE C 122     3114   3565   3907      9    122    -68       C  
ATOM   5609  CG1 ILE C 122      71.232  -7.078  -1.621  1.00 28.64           C  
ANISOU 5609  CG1 ILE C 122     3195   3684   4003    -12    113    -67       C  
ATOM   5610  CG2 ILE C 122      71.003  -7.368  -4.122  1.00 26.53           C  
ANISOU 5610  CG2 ILE C 122     2947   3380   3751     23    141    -73       C  
ATOM   5611  CD1 ILE C 122      71.227  -5.554  -1.656  1.00 31.00           C  
ANISOU 5611  CD1 ILE C 122     3500   3981   4295    -25    127    -86       C  
ATOM   5612  N   ILE C 123      67.819  -7.821  -4.683  1.00 24.39           N  
ANISOU 5612  N   ILE C 123     2721   3092   3453     36    141    -80       N  
ATOM   5613  CA  ILE C 123      67.106  -8.736  -5.531  1.00 23.47           C  
ANISOU 5613  CA  ILE C 123     2617   2963   3336     51    141    -77       C  
ATOM   5614  C   ILE C 123      67.901  -8.728  -6.807  1.00 23.53           C  
ANISOU 5614  C   ILE C 123     2624   2961   3355     63    157    -80       C  
ATOM   5615  O   ILE C 123      68.151  -7.631  -7.374  1.00 23.75           O  
ANISOU 5615  O   ILE C 123     2654   2988   3382     59    172    -87       O  
ATOM   5616  CB  ILE C 123      65.707  -8.240  -5.802  1.00 23.53           C  
ANISOU 5616  CB  ILE C 123     2644   2965   3330     50    145    -81       C  
ATOM   5617  CG1 ILE C 123      64.857  -8.466  -4.561  1.00 24.06           C  
ANISOU 5617  CG1 ILE C 123     2711   3043   3385     40    130    -77       C  
ATOM   5618  CG2 ILE C 123      65.080  -8.971  -7.004  1.00 23.04           C  
ANISOU 5618  CG2 ILE C 123     2597   2891   3267     65    150    -80       C  
ATOM   5619  CD1 ILE C 123      63.681  -7.537  -4.478  1.00 25.82           C  
ANISOU 5619  CD1 ILE C 123     2947   3266   3596     35    136    -85       C  
ATOM   5620  N   VAL C 124      68.333  -9.923  -7.259  1.00 23.42           N  
ANISOU 5620  N   VAL C 124     2605   2940   3352     76    155    -77       N  
ATOM   5621  CA  VAL C 124      69.158  -9.975  -8.481  1.00 23.42           C  
ANISOU 5621  CA  VAL C 124     2602   2934   3363     87    172    -83       C  
ATOM   5622  C   VAL C 124      68.370 -10.594  -9.577  1.00 23.85           C  
ANISOU 5622  C   VAL C 124     2673   2977   3410     98    179    -89       C  
ATOM   5623  O   VAL C 124      67.659 -11.555  -9.341  1.00 25.59           O  
ANISOU 5623  O   VAL C 124     2900   3191   3630    103    166    -85       O  
ATOM   5624  CB  VAL C 124      70.372 -10.850  -8.231  1.00 24.34           C  
ANISOU 5624  CB  VAL C 124     2697   3050   3500     95    168    -77       C  
ATOM   5625  CG1 VAL C 124      71.211 -11.061  -9.539  1.00 24.01           C  
ANISOU 5625  CG1 VAL C 124     2651   3002   3469    108    188    -86       C  
ATOM   5626  CG2 VAL C 124      71.124 -10.338  -7.000  1.00 23.29           C  
ANISOU 5626  CG2 VAL C 124     2545   2931   3371     81    157    -68       C  
ATOM   5627  N   VAL C 125      68.532 -10.114 -10.780  1.00 24.47           N  
ANISOU 5627  N   VAL C 125     2758   3054   3484    102    197    -96       N  
ATOM   5628  CA  VAL C 125      67.726 -10.552 -11.919  1.00 26.49           C  
ANISOU 5628  CA  VAL C 125     3032   3304   3729    108    205   -103       C  
ATOM   5629  C   VAL C 125      68.661 -10.994 -13.051  1.00 29.56           C  
ANISOU 5629  C   VAL C 125     3415   3693   4124    119    222   -113       C  
ATOM   5630  O   VAL C 125      68.286 -11.763 -13.899  1.00 33.91           O  
ANISOU 5630  O   VAL C 125     3976   4238   4671    126    227   -122       O  
ATOM   5631  CB  VAL C 125      66.837  -9.391 -12.422  1.00 25.27           C  
ANISOU 5631  CB  VAL C 125     2891   3153   3555     99    212   -100       C  
ATOM   5632  CG1 VAL C 125      66.005  -9.769 -13.642  1.00 24.22           C  
ANISOU 5632  CG1 VAL C 125     2776   3018   3408    102    219   -104       C  
ATOM   5633  CG2 VAL C 125      65.961  -8.847 -11.297  1.00 24.51           C  
ANISOU 5633  CG2 VAL C 125     2799   3057   3454     89    198    -93       C  
ATOM   5634  N   THR C 126      69.906 -10.542 -13.040  1.00 32.90           N  
ANISOU 5634  N   THR C 126     3819   4121   4558    119    232   -113       N  
ATOM   5635  CA  THR C 126      70.855 -10.824 -14.131  1.00 32.52           C  
ANISOU 5635  CA  THR C 126     3763   4077   4516    128    252   -123       C  
ATOM   5636  C   THR C 126      71.042 -12.324 -14.340  1.00 35.39           C  
ANISOU 5636  C   THR C 126     4123   4428   4894    143    251   -134       C  
ATOM   5637  O   THR C 126      71.314 -13.077 -13.379  1.00 34.21           O  
ANISOU 5637  O   THR C 126     3963   4271   4765    149    236   -127       O  
ATOM   5638  CB  THR C 126      72.210 -10.156 -13.867  1.00 30.48           C  
ANISOU 5638  CB  THR C 126     3482   3827   4270    125    260   -118       C  
ATOM   5639  OG1 THR C 126      72.002  -8.744 -13.723  1.00 29.25           O  
ANISOU 5639  OG1 THR C 126     3330   3679   4104    110    261   -110       O  
ATOM   5640  CG2 THR C 126      73.175 -10.370 -15.015  1.00 30.68           C  
ANISOU 5640  CG2 THR C 126     3497   3859   4300    134    282   -129       C  
ATOM   5641  N   ASN C 127      70.868 -12.747 -15.595  1.00 35.94           N  
ANISOU 5641  N   ASN C 127     4203   4498   4954    149    266   -149       N  
ATOM   5642  CA  ASN C 127      71.052 -14.148 -15.941  1.00 39.87           C  
ANISOU 5642  CA  ASN C 127     4698   4981   5467    164    269   -164       C  
ATOM   5643  C   ASN C 127      72.515 -14.649 -16.105  1.00 38.66           C  
ANISOU 5643  C   ASN C 127     4521   4826   5340    177    283   -172       C  
ATOM   5644  O   ASN C 127      73.405 -13.846 -16.372  1.00 36.71           O  
ANISOU 5644  O   ASN C 127     4260   4594   5092    174    297   -170       O  
ATOM   5645  CB  ASN C 127      70.163 -14.516 -17.131  1.00 44.99           C  
ANISOU 5645  CB  ASN C 127     5370   5631   6094    163    278   -180       C  
ATOM   5646  CG  ASN C 127      68.682 -14.604 -16.725  1.00 50.05           C  
ANISOU 5646  CG  ASN C 127     6031   6264   6720    154    258   -171       C  
ATOM   5647  OD1 ASN C 127      68.339 -15.097 -15.625  1.00 48.40           O  
ANISOU 5647  OD1 ASN C 127     5820   6044   6525    156    237   -161       O  
ATOM   5648  ND2 ASN C 127      67.796 -14.087 -17.594  1.00 50.46           N  
ANISOU 5648  ND2 ASN C 127     6101   6327   6743    144    264   -173       N  
ATOM   5649  N   PRO C 128      72.761 -15.962 -15.838  1.00 37.74           N  
ANISOU 5649  N   PRO C 128     4396   4691   5252    192    278   -179       N  
ATOM   5650  CA  PRO C 128      71.861 -16.959 -15.155  1.00 36.00           C  
ANISOU 5650  CA  PRO C 128     4184   4451   5042    195    255   -174       C  
ATOM   5651  C   PRO C 128      71.690 -16.640 -13.674  1.00 34.06           C  
ANISOU 5651  C   PRO C 128     3931   4207   4802    186    229   -148       C  
ATOM   5652  O   PRO C 128      72.668 -16.538 -12.924  1.00 34.27           O  
ANISOU 5652  O   PRO C 128     3934   4237   4849    188    224   -135       O  
ATOM   5653  CB  PRO C 128      72.632 -18.276 -15.290  1.00 38.66           C  
ANISOU 5653  CB  PRO C 128     4504   4767   5415    214    260   -186       C  
ATOM   5654  CG  PRO C 128      74.086 -17.841 -15.472  1.00 37.63           C  
ANISOU 5654  CG  PRO C 128     4349   4648   5299    220    278   -187       C  
ATOM   5655  CD  PRO C 128      74.054 -16.549 -16.222  1.00 36.88           C  
ANISOU 5655  CD  PRO C 128     4263   4577   5169    208    295   -191       C  
ATOM   5656  N   VAL C 129      70.465 -16.505 -13.233  1.00 31.60           N  
ANISOU 5656  N   VAL C 129     3638   3896   4473    176    212   -139       N  
ATOM   5657  CA  VAL C 129      70.231 -15.735 -12.008  1.00 29.54           C  
ANISOU 5657  CA  VAL C 129     3373   3646   4204    162    194   -118       C  
ATOM   5658  C   VAL C 129      70.672 -16.462 -10.756  1.00 27.95           C  
ANISOU 5658  C   VAL C 129     3151   3438   4028    165    173   -100       C  
ATOM   5659  O   VAL C 129      71.104 -15.829  -9.820  1.00 26.64           O  
ANISOU 5659  O   VAL C 129     2973   3286   3863    155    164    -86       O  
ATOM   5660  CB  VAL C 129      68.761 -15.221 -11.937  1.00 29.21           C  
ANISOU 5660  CB  VAL C 129     3355   3608   4133    150    186   -115       C  
ATOM   5661  CG1 VAL C 129      67.837 -16.397 -12.013  1.00 29.34           C  
ANISOU 5661  CG1 VAL C 129     3384   3609   4153    155    173   -117       C  
ATOM   5662  CG2 VAL C 129      68.499 -14.448 -10.678  1.00 27.04           C  
ANISOU 5662  CG2 VAL C 129     3077   3346   3851    136    170    -98       C  
ATOM   5663  N   ASP C 130      70.591 -17.792 -10.754  1.00 28.14           N  
ANISOU 5663  N   ASP C 130     3172   3443   4076    176    165   -101       N  
ATOM   5664  CA  ASP C 130      70.973 -18.602  -9.618  1.00 29.03           C  
ANISOU 5664  CA  ASP C 130     3264   3548   4216    179    143    -80       C  
ATOM   5665  C   ASP C 130      72.527 -18.558  -9.332  1.00 29.14           C  
ANISOU 5665  C   ASP C 130     3247   3566   4258    185    149    -73       C  
ATOM   5666  O   ASP C 130      72.997 -18.629  -8.168  1.00 29.13           O  
ANISOU 5666  O   ASP C 130     3225   3573   4270    179    130    -49       O  
ATOM   5667  CB  ASP C 130      70.473 -20.035  -9.846  1.00 31.56           C  
ANISOU 5667  CB  ASP C 130     3589   3842   4559    190    135    -84       C  
ATOM   5668  CG  ASP C 130      68.920 -20.123  -9.929  1.00 34.76           C  
ANISOU 5668  CG  ASP C 130     4021   4245   4938    181    124    -86       C  
ATOM   5669  OD1 ASP C 130      68.222 -20.205  -8.844  1.00 38.30           O  
ANISOU 5669  OD1 ASP C 130     4470   4700   5380    170    100    -64       O  
ATOM   5670  OD2 ASP C 130      68.406 -20.132 -11.078  1.00 32.58           O  
ANISOU 5670  OD2 ASP C 130     3766   3964   4647    184    140   -108       O  
ATOM   5671  N   VAL C 131      73.299 -18.409 -10.398  1.00 28.21           N  
ANISOU 5671  N   VAL C 131     3125   3446   4145    196    175    -92       N  
ATOM   5672  CA  VAL C 131      74.732 -18.113 -10.278  1.00 29.89           C  
ANISOU 5672  CA  VAL C 131     3310   3667   4378    201    184    -86       C  
ATOM   5673  C   VAL C 131      74.930 -16.645  -9.854  1.00 29.83           C  
ANISOU 5673  C   VAL C 131     3303   3686   4345    182    185    -78       C  
ATOM   5674  O   VAL C 131      75.584 -16.336  -8.832  1.00 29.66           O  
ANISOU 5674  O   VAL C 131     3261   3677   4332    173    171    -58       O  
ATOM   5675  CB  VAL C 131      75.455 -18.438 -11.608  1.00 28.58           C  
ANISOU 5675  CB  VAL C 131     3140   3492   4226    218    214   -111       C  
ATOM   5676  CG1 VAL C 131      76.849 -17.876 -11.647  1.00 30.34           C  
ANISOU 5676  CG1 VAL C 131     3336   3728   4461    221    228   -107       C  
ATOM   5677  CG2 VAL C 131      75.532 -19.936 -11.764  1.00 28.90           C  
ANISOU 5677  CG2 VAL C 131     3172   3504   4303    237    212   -118       C  
ATOM   5678  N   MET C 132      74.314 -15.730 -10.585  1.00 29.50           N  
ANISOU 5678  N   MET C 132     3284   3653   4272    174    198    -92       N  
ATOM   5679  CA  MET C 132      74.548 -14.297 -10.261  1.00 28.76           C  
ANISOU 5679  CA  MET C 132     3188   3580   4158    157    201    -86       C  
ATOM   5680  C   MET C 132      74.173 -13.864  -8.862  1.00 28.02           C  
ANISOU 5680  C   MET C 132     3093   3497   4056    140    177    -68       C  
ATOM   5681  O   MET C 132      74.858 -13.068  -8.297  1.00 30.89           O  
ANISOU 5681  O   MET C 132     3443   3875   4419    128    175    -59       O  
ATOM   5682  CB  MET C 132      73.944 -13.401 -11.309  1.00 29.18           C  
ANISOU 5682  CB  MET C 132     3264   3638   4183    152    219   -101       C  
ATOM   5683  CG  MET C 132      74.501 -13.645 -12.727  1.00 29.98           C  
ANISOU 5683  CG  MET C 132     3365   3738   4288    166    245   -119       C  
ATOM   5684  SD  MET C 132      76.256 -13.153 -12.783  1.00 32.95           S  
ANISOU 5684  SD  MET C 132     3709   4126   4683    168    260   -114       S  
ATOM   5685  CE  MET C 132      76.918 -14.536 -13.690  1.00 30.34           C  
ANISOU 5685  CE  MET C 132     3366   3781   4379    193    278   -132       C  
ATOM   5686  N   VAL C 133      73.098 -14.377  -8.282  1.00 27.05           N  
ANISOU 5686  N   VAL C 133     2982   3368   3925    137    159    -62       N  
ATOM   5687  CA  VAL C 133      72.708 -13.955  -6.925  1.00 26.01           C  
ANISOU 5687  CA  VAL C 133     2849   3252   3782    118    137    -46       C  
ATOM   5688  C   VAL C 133      73.768 -14.378  -5.866  1.00 26.95           C  
ANISOU 5688  C   VAL C 133     2937   3379   3923    114    121    -26       C  
ATOM   5689  O   VAL C 133      74.072 -13.643  -4.931  1.00 28.49           O  
ANISOU 5689  O   VAL C 133     3121   3592   4108     96    111    -16       O  
ATOM   5690  CB  VAL C 133      71.266 -14.438  -6.574  1.00 24.77           C  
ANISOU 5690  CB  VAL C 133     2710   3088   3610    115    122    -44       C  
ATOM   5691  CG1 VAL C 133      71.126 -15.968  -6.690  1.00 24.31           C  
ANISOU 5691  CG1 VAL C 133     2648   3011   3575    130    112    -38       C  
ATOM   5692  CG2 VAL C 133      70.809 -13.989  -5.194  1.00 25.31           C  
ANISOU 5692  CG2 VAL C 133     2776   3176   3664     95    103    -30       C  
ATOM   5693  N   GLN C 134      74.305 -15.586  -6.028  1.00 26.72           N  
ANISOU 5693  N   GLN C 134     2891   3334   3924    131    118    -18       N  
ATOM   5694  CA  GLN C 134      75.311 -16.109  -5.158  1.00 27.81           C  
ANISOU 5694  CA  GLN C 134     2999   3478   4089    129    102      4       C  
ATOM   5695  C   GLN C 134      76.623 -15.357  -5.318  1.00 28.64           C  
ANISOU 5695  C   GLN C 134     3084   3595   4201    127    115      4       C  
ATOM   5696  O   GLN C 134      77.246 -15.059  -4.318  1.00 28.72           O  
ANISOU 5696  O   GLN C 134     3074   3623   4214    112    100     22       O  
ATOM   5697  CB  GLN C 134      75.557 -17.656  -5.292  1.00 26.95           C  
ANISOU 5697  CB  GLN C 134     2875   3345   4019    150     95     13       C  
ATOM   5698  CG  GLN C 134      76.617 -18.114  -4.272  1.00 26.45           C  
ANISOU 5698  CG  GLN C 134     2775   3289   3984    146     76     44       C  
ATOM   5699  CD  GLN C 134      76.686 -19.656  -4.083  1.00 27.80           C  
ANISOU 5699  CD  GLN C 134     2929   3436   4195    162     62     61       C  
ATOM   5700  OE1 GLN C 134      76.497 -20.393  -5.032  1.00 27.64           O  
ANISOU 5700  OE1 GLN C 134     2918   3389   4195    182     76     43       O  
ATOM   5701  NE2 GLN C 134      76.946 -20.122  -2.847  1.00 26.92           N  
ANISOU 5701  NE2 GLN C 134     2793   3334   4098    151     33     96       N  
ATOM   5702  N   LEU C 135      77.038 -15.088  -6.552  1.00 27.44           N  
ANISOU 5702  N   LEU C 135     2936   3435   4052    140    142    -15       N  
ATOM   5703  CA  LEU C 135      78.163 -14.181  -6.761  1.00 29.73           C  
ANISOU 5703  CA  LEU C 135     3210   3739   4344    135    156    -16       C  
ATOM   5704  C   LEU C 135      77.924 -12.804  -6.048  1.00 29.68           C  
ANISOU 5704  C   LEU C 135     3213   3755   4308    109    149    -14       C  
ATOM   5705  O   LEU C 135      78.810 -12.304  -5.350  1.00 30.59           O  
ANISOU 5705  O   LEU C 135     3308   3887   4428     95    141     -1       O  
ATOM   5706  CB  LEU C 135      78.420 -13.975  -8.272  1.00 28.78           C  
ANISOU 5706  CB  LEU C 135     3099   3611   4224    150    187    -39       C  
ATOM   5707  CG  LEU C 135      78.774 -15.192  -9.137  1.00 30.63           C  
ANISOU 5707  CG  LEU C 135     3326   3825   4486    176    200    -49       C  
ATOM   5708  CD1 LEU C 135      78.829 -14.870 -10.658  1.00 30.47           C  
ANISOU 5708  CD1 LEU C 135     3318   3803   4455    186    232    -75       C  
ATOM   5709  CD2 LEU C 135      80.072 -15.884  -8.661  1.00 31.88           C  
ANISOU 5709  CD2 LEU C 135     3446   3981   4684    186    195    -31       C  
ATOM   5710  N   LEU C 136      76.742 -12.197  -6.169  1.00 28.01           N  
ANISOU 5710  N   LEU C 136     3030   3543   4068    100    150    -26       N  
ATOM   5711  CA  LEU C 136      76.619 -10.889  -5.512  1.00 26.81           C  
ANISOU 5711  CA  LEU C 136     2882   3408   3894     77    146    -27       C  
ATOM   5712  C   LEU C 136      76.619 -11.054  -3.989  1.00 28.38           C  
ANISOU 5712  C   LEU C 136     3068   3623   4090     59    120    -10       C  
ATOM   5713  O   LEU C 136      77.098 -10.176  -3.307  1.00 29.91           O  
ANISOU 5713  O   LEU C 136     3253   3834   4275     39    115     -7       O  
ATOM   5714  CB  LEU C 136      75.366 -10.167  -5.911  1.00 25.20           C  
ANISOU 5714  CB  LEU C 136     2709   3201   3665     72    154    -43       C  
ATOM   5715  CG  LEU C 136      75.252  -8.702  -5.468  1.00 24.19           C  
ANISOU 5715  CG  LEU C 136     2586   3084   3518     50    156    -49       C  
ATOM   5716  CD1 LEU C 136      76.468  -7.880  -5.822  1.00 24.32           C  
ANISOU 5716  CD1 LEU C 136     2588   3107   3544     45    168    -50       C  
ATOM   5717  CD2 LEU C 136      74.049  -8.174  -6.195  1.00 23.30           C  
ANISOU 5717  CD2 LEU C 136     2502   2962   3389     53    167    -63       C  
ATOM   5718  N   HIS C 137      76.129 -12.199  -3.487  1.00 28.46           N  
ANISOU 5718  N   HIS C 137     3076   3628   4107     65    102      2       N  
ATOM   5719  CA  HIS C 137      76.120 -12.515  -2.060  1.00 29.73           C  
ANISOU 5719  CA  HIS C 137     3222   3807   4265     47     75     23       C  
ATOM   5720  C   HIS C 137      77.506 -12.633  -1.571  1.00 31.29           C  
ANISOU 5720  C   HIS C 137     3387   4017   4483     42     67     42       C  
ATOM   5721  O   HIS C 137      77.836 -12.216  -0.493  1.00 33.09           O  
ANISOU 5721  O   HIS C 137     3601   4269   4700     19     51     54       O  
ATOM   5722  CB  HIS C 137      75.350 -13.814  -1.771  1.00 28.42           C  
ANISOU 5722  CB  HIS C 137     3059   3631   4108     57     59     36       C  
ATOM   5723  CG  HIS C 137      75.338 -14.204  -0.286  1.00 27.82           C  
ANISOU 5723  CG  HIS C 137     2965   3577   4027     37     29     62       C  
ATOM   5724  ND1 HIS C 137      75.520 -15.481   0.138  1.00 29.62           N  
ANISOU 5724  ND1 HIS C 137     3173   3799   4279     44     10     88       N  
ATOM   5725  CD2 HIS C 137      75.123 -13.443   0.855  1.00 26.71           C  
ANISOU 5725  CD2 HIS C 137     2823   3466   3858      8     16     65       C  
ATOM   5726  CE1 HIS C 137      75.440 -15.540   1.497  1.00 28.24           C  
ANISOU 5726  CE1 HIS C 137     2985   3652   4092     20    -15    111       C  
ATOM   5727  NE2 HIS C 137      75.212 -14.287   1.944  1.00 27.15           N  
ANISOU 5727  NE2 HIS C 137     2858   3537   3919     -1    -10     95       N  
ATOM   5728  N   GLN C 138      78.339 -13.234  -2.383  1.00 36.45           N  
ANISOU 5728  N   GLN C 138     4026   4655   5166     63     79     44       N  
ATOM   5729  CA  GLN C 138      79.720 -13.490  -2.037  1.00 37.80           C  
ANISOU 5729  CA  GLN C 138     4162   4834   5363     63     73     65       C  
ATOM   5730  C   GLN C 138      80.427 -12.156  -2.037  1.00 36.34           C  
ANISOU 5730  C   GLN C 138     3974   4668   5165     45     83     57       C  
ATOM   5731  O   GLN C 138      81.145 -11.835  -1.102  1.00 38.23           O  
ANISOU 5731  O   GLN C 138     4191   4929   5403     25     67     74       O  
ATOM   5732  CB  GLN C 138      80.364 -14.273  -3.161  1.00 43.45           C  
ANISOU 5732  CB  GLN C 138     4867   5527   6113     92     91     61       C  
ATOM   5733  CG  GLN C 138      80.851 -15.660  -2.859  1.00 55.01           C  
ANISOU 5733  CG  GLN C 138     6305   6979   7616    108     78     85       C  
ATOM   5734  CD  GLN C 138      81.832 -16.120  -3.926  1.00 60.87           C  
ANISOU 5734  CD  GLN C 138     7030   7704   8393    134    101     78       C  
ATOM   5735  OE1 GLN C 138      82.786 -15.396  -4.287  1.00 61.10           O  
ANISOU 5735  OE1 GLN C 138     7047   7744   8425    132    116     74       O  
ATOM   5736  NE2 GLN C 138      81.601 -17.325  -4.449  1.00 70.10           N  
ANISOU 5736  NE2 GLN C 138     8198   8845   9590    158    105     74       N  
ATOM   5737  N   HIS C 139      80.274 -11.412  -3.113  1.00 30.92           N  
ANISOU 5737  N   HIS C 139     3306   3972   4470     53    108     34       N  
ATOM   5738  CA  HIS C 139      80.973 -10.115  -3.215  1.00 31.18           C  
ANISOU 5738  CA  HIS C 139     3334   4018   4492     37    118     27       C  
ATOM   5739  C   HIS C 139      80.369  -8.947  -2.455  1.00 29.72           C  
ANISOU 5739  C   HIS C 139     3165   3848   4277      9    111     17       C  
ATOM   5740  O   HIS C 139      80.951  -7.898  -2.466  1.00 30.52           O  
ANISOU 5740  O   HIS C 139     3262   3958   4373     -5    117     12       O  
ATOM   5741  CB  HIS C 139      81.128  -9.713  -4.679  1.00 31.11           C  
ANISOU 5741  CB  HIS C 139     3337   3996   4487     53    148      8       C  
ATOM   5742  CG  HIS C 139      81.672 -10.815  -5.578  1.00 32.47           C  
ANISOU 5742  CG  HIS C 139     3496   4153   4688     82    161     10       C  
ATOM   5743  ND1 HIS C 139      82.725 -11.568  -5.232  1.00 32.24           N  
ANISOU 5743  ND1 HIS C 139     3434   4126   4688     89    153     30       N  
ATOM   5744  CD2 HIS C 139      81.272 -11.259  -6.875  1.00 31.62           C  
ANISOU 5744  CD2 HIS C 139     3403   4026   4582    104    183     -7       C  
ATOM   5745  CE1 HIS C 139      82.998 -12.457  -6.248  1.00 33.99           C  
ANISOU 5745  CE1 HIS C 139     3651   4330   4934    117    171     22       C  
ATOM   5746  NE2 HIS C 139      82.097 -12.272  -7.233  1.00 31.30           N  
ANISOU 5746  NE2 HIS C 139     3339   3977   4574    125    189     -1       N  
ATOM   5747  N   SER C 140      79.182  -9.064  -1.852  1.00 27.94           N  
ANISOU 5747  N   SER C 140     2959   3624   4032      2     99     12       N  
ATOM   5748  CA  SER C 140      78.610  -7.938  -1.124  1.00 27.48           C  
ANISOU 5748  CA  SER C 140     2914   3579   3946    -23     95      0       C  
ATOM   5749  C   SER C 140      78.752  -8.135   0.378  1.00 27.75           C  
ANISOU 5749  C   SER C 140     2933   3640   3971    -47     68     15       C  
ATOM   5750  O   SER C 140      78.709  -7.171   1.109  1.00 29.60           O  
ANISOU 5750  O   SER C 140     3170   3891   4185    -73     64      6       O  
ATOM   5751  CB  SER C 140      77.088  -7.785  -1.385  1.00 26.81           C  
ANISOU 5751  CB  SER C 140     2861   3481   3841    -18    101    -17       C  
ATOM   5752  OG  SER C 140      76.404  -8.895  -0.775  1.00 27.01           O  
ANISOU 5752  OG  SER C 140     2887   3509   3865    -14     83     -5       O  
ATOM   5753  N   GLY C 141      78.754  -9.373   0.842  1.00 28.64           N  
ANISOU 5753  N   GLY C 141     3031   3755   4093    -40     51     38       N  
ATOM   5754  CA  GLY C 141      78.860  -9.647   2.290  1.00 27.84           C  
ANISOU 5754  CA  GLY C 141     2913   3683   3981    -65     23     57       C  
ATOM   5755  C   GLY C 141      77.538  -9.510   3.033  1.00 28.43           C  
ANISOU 5755  C   GLY C 141     3008   3768   4025    -80     14     47       C  
ATOM   5756  O   GLY C 141      77.527  -9.454   4.289  1.00 28.74           O  
ANISOU 5756  O   GLY C 141     3035   3837   4045   -107     -5     58       O  
ATOM   5757  N   VAL C 142      76.410  -9.410   2.320  1.00 26.56           N  
ANISOU 5757  N   VAL C 142     2799   3510   3780    -64     29     28       N  
ATOM   5758  CA  VAL C 142      75.159  -9.244   3.079  1.00 26.81           C  
ANISOU 5758  CA  VAL C 142     2848   3555   3783    -78     21     19       C  
ATOM   5759  C   VAL C 142      74.647 -10.594   3.590  1.00 27.43           C  
ANISOU 5759  C   VAL C 142     2919   3637   3865    -73      0     43       C  
ATOM   5760  O   VAL C 142      74.924 -11.616   2.963  1.00 27.67           O  
ANISOU 5760  O   VAL C 142     2942   3647   3922    -50      0     59       O  
ATOM   5761  CB  VAL C 142      74.045  -8.597   2.272  1.00 26.18           C  
ANISOU 5761  CB  VAL C 142     2800   3454   3693    -67     42     -8       C  
ATOM   5762  CG1 VAL C 142      74.471  -7.207   1.758  1.00 25.40           C  
ANISOU 5762  CG1 VAL C 142     2707   3348   3593    -73     63    -30       C  
ATOM   5763  CG2 VAL C 142      73.604  -9.528   1.162  1.00 26.12           C  
ANISOU 5763  CG2 VAL C 142     2803   3418   3703    -37     50     -4       C  
ATOM   5764  N   PRO C 143      73.912 -10.598   4.729  1.00 28.01           N  
ANISOU 5764  N   PRO C 143     2994   3736   3911    -95    -15     47       N  
ATOM   5765  CA  PRO C 143      73.250 -11.803   5.290  1.00 28.56           C  
ANISOU 5765  CA  PRO C 143     3058   3812   3980    -94    -36     71       C  
ATOM   5766  C   PRO C 143      72.406 -12.528   4.215  1.00 30.34           C  
ANISOU 5766  C   PRO C 143     3303   4002   4220    -63    -26     68       C  
ATOM   5767  O   PRO C 143      71.762 -11.892   3.366  1.00 27.11           O  
ANISOU 5767  O   PRO C 143     2919   3575   3806    -52     -4     41       O  
ATOM   5768  CB  PRO C 143      72.263 -11.249   6.283  1.00 27.68           C  
ANISOU 5768  CB  PRO C 143     2958   3729   3831   -119    -41     60       C  
ATOM   5769  CG  PRO C 143      72.507  -9.746   6.364  1.00 27.82           C  
ANISOU 5769  CG  PRO C 143     2984   3755   3831   -135    -24     28       C  
ATOM   5770  CD  PRO C 143      73.623  -9.371   5.491  1.00 26.53           C  
ANISOU 5770  CD  PRO C 143     2814   3572   3692   -123    -11     24       C  
ATOM   5771  N   LYS C 144      72.371 -13.852   4.324  1.00 32.14           N  
ANISOU 5771  N   LYS C 144     3518   4223   4468    -53    -43     95       N  
ATOM   5772  CA  LYS C 144      71.724 -14.691   3.343  1.00 32.89           C  
ANISOU 5772  CA  LYS C 144     3628   4285   4582    -26    -36     93       C  
ATOM   5773  C   LYS C 144      70.191 -14.522   3.302  1.00 31.05           C  
ANISOU 5773  C   LYS C 144     3422   4050   4323    -27    -32     79       C  
ATOM   5774  O   LYS C 144      69.527 -14.878   2.321  1.00 32.02           O  
ANISOU 5774  O   LYS C 144     3564   4146   4454     -6    -22     69       O  
ATOM   5775  CB  LYS C 144      72.094 -16.122   3.661  1.00 33.69           C  
ANISOU 5775  CB  LYS C 144     3707   4381   4713    -18    -59    128       C  
ATOM   5776  CG  LYS C 144      72.250 -16.338   5.160  1.00 39.42           C  
ANISOU 5776  CG  LYS C 144     4409   5144   5424    -47    -87    158       C  
ATOM   5777  CD  LYS C 144      71.001 -16.864   5.807  1.00 40.59           C  
ANISOU 5777  CD  LYS C 144     4565   5303   5552    -56   -103    170       C  
ATOM   5778  CE  LYS C 144      71.369 -17.820   6.926  1.00 46.05           C  
ANISOU 5778  CE  LYS C 144     5226   6017   6254    -72   -136    214       C  
ATOM   5779  NZ  LYS C 144      70.162 -18.675   7.115  1.00 48.53           N  
ANISOU 5779  NZ  LYS C 144     5548   6326   6564    -70   -149    228       N  
ATOM   5780  N   ASN C 145      69.627 -13.982   4.354  1.00 31.14           N  
ANISOU 5780  N   ASN C 145     3435   4092   4303    -51    -41     77       N  
ATOM   5781  CA  ASN C 145      68.189 -13.744   4.355  1.00 32.80           C  
ANISOU 5781  CA  ASN C 145     3668   4303   4490    -53    -36     63       C  
ATOM   5782  C   ASN C 145      67.894 -12.384   3.714  1.00 30.47           C  
ANISOU 5782  C   ASN C 145     3395   4000   4182    -50     -9     28       C  
ATOM   5783  O   ASN C 145      66.751 -11.964   3.705  1.00 27.95           O  
ANISOU 5783  O   ASN C 145     3093   3681   3844    -52     -1     14       O  
ATOM   5784  CB  ASN C 145      67.639 -13.770   5.817  1.00 34.79           C  
ANISOU 5784  CB  ASN C 145     3911   4595   4712    -81    -55     76       C  
ATOM   5785  CG  ASN C 145      68.261 -12.688   6.666  1.00 38.37           C  
ANISOU 5785  CG  ASN C 145     4355   5080   5144   -107    -53     64       C  
ATOM   5786  OD1 ASN C 145      69.470 -12.630   6.756  1.00 40.94           O  
ANISOU 5786  OD1 ASN C 145     4662   5409   5483   -112    -57     72       O  
ATOM   5787  ND2 ASN C 145      67.447 -11.834   7.298  1.00 37.70           N  
ANISOU 5787  ND2 ASN C 145     4280   5016   5026   -125    -46     43       N  
ATOM   5788  N   LYS C 146      68.918 -11.671   3.239  1.00 28.54           N  
ANISOU 5788  N   LYS C 146     3145   3748   3948    -48      4     17       N  
ATOM   5789  CA  LYS C 146      68.650 -10.358   2.689  1.00 28.47           C  
ANISOU 5789  CA  LYS C 146     3155   3731   3930    -48     27    -12       C  
ATOM   5790  C   LYS C 146      68.988 -10.358   1.186  1.00 27.92           C  
ANISOU 5790  C   LYS C 146     3095   3630   3883    -23     46    -20       C  
ATOM   5791  O   LYS C 146      69.058  -9.301   0.574  1.00 29.69           O  
ANISOU 5791  O   LYS C 146     3329   3845   4105    -22     65    -39       O  
ATOM   5792  CB  LYS C 146      69.339  -9.206   3.440  1.00 27.55           C  
ANISOU 5792  CB  LYS C 146     3029   3636   3800    -72     30    -25       C  
ATOM   5793  CG  LYS C 146      69.085  -9.115   4.951  1.00 27.63           C  
ANISOU 5793  CG  LYS C 146     3029   3684   3784   -101     14    -21       C  
ATOM   5794  CD  LYS C 146      67.836  -8.372   5.429  1.00 28.87           C  
ANISOU 5794  CD  LYS C 146     3202   3852   3915   -112     22    -44       C  
ATOM   5795  CE  LYS C 146      67.929  -6.853   5.230  1.00 29.51           C  
ANISOU 5795  CE  LYS C 146     3293   3925   3992   -120     44    -77       C  
ATOM   5796  NZ  LYS C 146      69.318  -6.311   5.165  1.00 30.01           N  
ANISOU 5796  NZ  LYS C 146     3344   3991   4068   -129     46    -79       N  
ATOM   5797  N   ILE C 147      69.207 -11.517   0.587  1.00 25.90           N  
ANISOU 5797  N   ILE C 147     2834   3357   3647     -4     41     -5       N  
ATOM   5798  CA  ILE C 147      69.491 -11.508  -0.890  1.00 26.16           C  
ANISOU 5798  CA  ILE C 147     2877   3362   3697     17     61    -16       C  
ATOM   5799  C   ILE C 147      68.825 -12.609  -1.613  1.00 26.23           C  
ANISOU 5799  C   ILE C 147     2897   3351   3717     36     59    -11       C  
ATOM   5800  O   ILE C 147      68.987 -13.747  -1.216  1.00 28.19           O  
ANISOU 5800  O   ILE C 147     3132   3598   3979     40     42      7       O  
ATOM   5801  CB  ILE C 147      71.004 -11.418  -1.290  1.00 25.38           C  
ANISOU 5801  CB  ILE C 147     2760   3261   3620     22     68    -13       C  
ATOM   5802  CG1 ILE C 147      71.217 -11.540  -2.830  1.00 24.36           C  
ANISOU 5802  CG1 ILE C 147     2640   3107   3506     45     89    -25       C  
ATOM   5803  CG2 ILE C 147      71.878 -12.420  -0.533  1.00 26.09           C  
ANISOU 5803  CG2 ILE C 147     2823   3360   3728     20     48     11       C  
ATOM   5804  CD1 ILE C 147      72.562 -10.961  -3.312  1.00 25.13           C  
ANISOU 5804  CD1 ILE C 147     2723   3205   3617     46    103    -28       C  
ATOM   5805  N   ILE C 148      68.061 -12.289  -2.663  1.00 26.03           N  
ANISOU 5805  N   ILE C 148     2894   3310   3685     46     75    -27       N  
ATOM   5806  CA  ILE C 148      67.338 -13.314  -3.366  1.00 24.95           C  
ANISOU 5806  CA  ILE C 148     2769   3155   3554     62     73    -25       C  
ATOM   5807  C   ILE C 148      67.423 -13.017  -4.856  1.00 25.06           C  
ANISOU 5807  C   ILE C 148     2796   3151   3572     76     96    -41       C  
ATOM   5808  O   ILE C 148      67.779 -11.904  -5.290  1.00 24.65           O  
ANISOU 5808  O   ILE C 148     2747   3102   3514     73    112    -53       O  
ATOM   5809  CB  ILE C 148      65.855 -13.379  -2.937  1.00 25.31           C  
ANISOU 5809  CB  ILE C 148     2830   3205   3580     55     64    -22       C  
ATOM   5810  CG1 ILE C 148      65.177 -12.016  -3.088  1.00 24.09           C  
ANISOU 5810  CG1 ILE C 148     2690   3056   3405     47     79    -38       C  
ATOM   5811  CG2 ILE C 148      65.695 -13.902  -1.499  1.00 24.99           C  
ANISOU 5811  CG2 ILE C 148     2774   3184   3534     40     40     -3       C  
ATOM   5812  CD1 ILE C 148      63.677 -12.127  -2.806  1.00 23.57           C  
ANISOU 5812  CD1 ILE C 148     2639   2994   3322     43     72    -36       C  
ATOM   5813  N   GLY C 149      67.163 -14.026  -5.651  1.00 24.33           N  
ANISOU 5813  N   GLY C 149     2711   3041   3491     91     96    -42       N  
ATOM   5814  CA  GLY C 149      67.184 -13.826  -7.099  1.00 25.72           C  
ANISOU 5814  CA  GLY C 149     2900   3205   3666    103    118    -59       C  
ATOM   5815  C   GLY C 149      65.803 -14.068  -7.620  1.00 25.29           C  
ANISOU 5815  C   GLY C 149     2869   3143   3597    104    117    -62       C  
ATOM   5816  O   GLY C 149      65.027 -14.813  -7.004  1.00 26.18           O  
ANISOU 5816  O   GLY C 149     2983   3253   3708    102     99    -52       O  
ATOM   5817  N   LEU C 150      65.498 -13.500  -8.773  1.00 27.83           N  
ANISOU 5817  N   LEU C 150     3205   3461   3907    107    134    -75       N  
ATOM   5818  CA  LEU C 150      64.181 -13.658  -9.381  1.00 27.34           C  
ANISOU 5818  CA  LEU C 150     3163   3393   3829    107    134    -77       C  
ATOM   5819  C   LEU C 150      64.165 -14.908 -10.156  1.00 30.57           C  
ANISOU 5819  C   LEU C 150     3578   3787   4249    119    133    -83       C  
ATOM   5820  O   LEU C 150      65.004 -15.101 -11.048  1.00 30.54           O  
ANISOU 5820  O   LEU C 150     3570   3778   4254    127    148    -96       O  
ATOM   5821  CB  LEU C 150      63.903 -12.561 -10.358  1.00 27.19           C  
ANISOU 5821  CB  LEU C 150     3156   3378   3795    104    152    -85       C  
ATOM   5822  CG  LEU C 150      62.698 -12.825 -11.306  1.00 27.67           C  
ANISOU 5822  CG  LEU C 150     3237   3434   3841    105    154    -87       C  
ATOM   5823  CD1 LEU C 150      61.447 -12.437 -10.540  1.00 26.80           C  
ANISOU 5823  CD1 LEU C 150     3134   3328   3718     96    141    -76       C  
ATOM   5824  CD2 LEU C 150      62.825 -11.941 -12.523  1.00 27.06           C  
ANISOU 5824  CD2 LEU C 150     3167   3361   3753    104    173    -94       C  
ATOM   5825  N   GLY C 151      63.201 -15.768  -9.848  1.00 30.83           N  
ANISOU 5825  N   GLY C 151     3619   3814   4281    118    117    -76       N  
ATOM   5826  CA  GLY C 151      63.088 -17.034 -10.556  1.00 29.72           C  
ANISOU 5826  CA  GLY C 151     3484   3655   4152    127    115    -84       C  
ATOM   5827  C   GLY C 151      61.628 -17.427 -10.661  1.00 31.35           C  
ANISOU 5827  C   GLY C 151     3708   3859   4344    122    103    -79       C  
ATOM   5828  O   GLY C 151      60.948 -17.171 -11.696  1.00 33.02           O  
ANISOU 5828  O   GLY C 151     3937   4071   4538    120    112    -88       O  
ATOM   5829  N   GLY C 152      61.132 -17.984  -9.576  1.00 26.19           N  
ANISOU 5829  N   GLY C 152     3049   3204   3696    117     81    -62       N  
ATOM   5830  CA  GLY C 152      59.924 -18.725  -9.597  1.00 25.37           C  
ANISOU 5830  CA  GLY C 152     2957   3093   3586    114     66    -55       C  
ATOM   5831  C   GLY C 152      58.675 -17.901  -9.780  1.00 26.64           C  
ANISOU 5831  C   GLY C 152     3134   3267   3719    104     68    -51       C  
ATOM   5832  O   GLY C 152      57.715 -18.430 -10.383  1.00 25.79           O  
ANISOU 5832  O   GLY C 152     3041   3153   3604    102     63    -52       O  
ATOM   5833  N   VAL C 153      58.683 -16.624  -9.316  1.00 26.28           N  
ANISOU 5833  N   VAL C 153     3085   3239   3661     98     75    -48       N  
ATOM   5834  CA  VAL C 153      57.509 -15.786  -9.420  1.00 25.00           C  
ANISOU 5834  CA  VAL C 153     2934   3087   3478     90     78    -43       C  
ATOM   5835  C   VAL C 153      57.226 -15.572 -10.880  1.00 25.91           C  
ANISOU 5835  C   VAL C 153     3063   3197   3582     92     92    -53       C  
ATOM   5836  O   VAL C 153      56.062 -15.484 -11.258  1.00 27.83           O  
ANISOU 5836  O   VAL C 153     3319   3443   3811     87     88    -47       O  
ATOM   5837  CB  VAL C 153      57.607 -14.430  -8.696  1.00 25.93           C  
ANISOU 5837  CB  VAL C 153     3044   3220   3587     84     85    -41       C  
ATOM   5838  CG1 VAL C 153      56.275 -13.671  -8.821  1.00 25.29           C  
ANISOU 5838  CG1 VAL C 153     2973   3145   3489     78     87    -35       C  
ATOM   5839  CG2 VAL C 153      57.901 -14.587  -7.203  1.00 24.94           C  
ANISOU 5839  CG2 VAL C 153     2903   3104   3467     78     72    -32       C  
ATOM   5840  N   LEU C 154      58.268 -15.399 -11.685  1.00 25.53           N  
ANISOU 5840  N   LEU C 154     3013   3146   3539     98    108    -68       N  
ATOM   5841  CA  LEU C 154      58.112 -15.100 -13.137  1.00 24.42           C  
ANISOU 5841  CA  LEU C 154     2885   3006   3385     97    123    -78       C  
ATOM   5842  C   LEU C 154      57.704 -16.362 -13.865  1.00 24.35           C  
ANISOU 5842  C   LEU C 154     2888   2986   3376     99    117    -86       C  
ATOM   5843  O   LEU C 154      56.757 -16.375 -14.619  1.00 26.28           O  
ANISOU 5843  O   LEU C 154     3147   3234   3604     92    116    -84       O  
ATOM   5844  CB  LEU C 154      59.421 -14.532 -13.745  1.00 23.53           C  
ANISOU 5844  CB  LEU C 154     2765   2896   3278    102    143    -90       C  
ATOM   5845  CG  LEU C 154      59.504 -14.458 -15.285  1.00 24.72           C  
ANISOU 5845  CG  LEU C 154     2926   3050   3415    101    160   -102       C  
ATOM   5846  CD1 LEU C 154      58.223 -13.772 -15.779  1.00 25.27           C  
ANISOU 5846  CD1 LEU C 154     3008   3129   3463     91    158    -90       C  
ATOM   5847  CD2 LEU C 154      60.815 -13.872 -15.858  1.00 23.87           C  
ANISOU 5847  CD2 LEU C 154     2808   2949   3312    105    181   -113       C  
ATOM   5848  N   ASP C 155      58.461 -17.431 -13.681  1.00 25.15           N  
ANISOU 5848  N   ASP C 155     2983   3073   3498    107    113    -95       N  
ATOM   5849  CA  ASP C 155      58.158 -18.687 -14.301  1.00 24.80           C  
ANISOU 5849  CA  ASP C 155     2948   3014   3459    109    107   -106       C  
ATOM   5850  C   ASP C 155      56.774 -19.209 -13.931  1.00 24.68           C  
ANISOU 5850  C   ASP C 155     2943   2996   3436    101     86    -91       C  
ATOM   5851  O   ASP C 155      56.024 -19.654 -14.819  1.00 23.50           O  
ANISOU 5851  O   ASP C 155     2809   2844   3275     95     85    -98       O  
ATOM   5852  CB  ASP C 155      59.226 -19.686 -13.944  1.00 27.27           C  
ANISOU 5852  CB  ASP C 155     3247   3309   3803    121    105   -115       C  
ATOM   5853  CG  ASP C 155      60.599 -19.380 -14.635  1.00 30.79           C  
ANISOU 5853  CG  ASP C 155     3684   3756   4256    130    129   -134       C  
ATOM   5854  OD1 ASP C 155      60.647 -18.927 -15.829  1.00 30.17           O  
ANISOU 5854  OD1 ASP C 155     3615   3687   4159    127    147   -149       O  
ATOM   5855  OD2 ASP C 155      61.632 -19.663 -13.971  1.00 31.66           O  
ANISOU 5855  OD2 ASP C 155     3777   3860   4393    139    128   -132       O  
ATOM   5856  N   THR C 156      56.438 -19.167 -12.645  1.00 23.31           N  
ANISOU 5856  N   THR C 156     2760   2825   3269     99     70    -71       N  
ATOM   5857  CA  THR C 156      55.124 -19.600 -12.182  1.00 23.81           C  
ANISOU 5857  CA  THR C 156     2831   2890   3325     90     50    -54       C  
ATOM   5858  C   THR C 156      53.996 -18.733 -12.730  1.00 23.73           C  
ANISOU 5858  C   THR C 156     2833   2894   3288     81     54    -48       C  
ATOM   5859  O   THR C 156      52.919 -19.257 -12.935  1.00 22.07           O  
ANISOU 5859  O   THR C 156     2633   2682   3070     74     42    -40       O  
ATOM   5860  CB  THR C 156      55.020 -19.799 -10.623  1.00 24.34           C  
ANISOU 5860  CB  THR C 156     2883   2961   3403     88     31    -33       C  
ATOM   5861  OG1 THR C 156      55.113 -18.571  -9.936  1.00 27.49           O  
ANISOU 5861  OG1 THR C 156     3273   3378   3791     85     38    -26       O  
ATOM   5862  CG2 THR C 156      56.163 -20.625 -10.066  1.00 24.90           C  
ANISOU 5862  CG2 THR C 156     2938   3018   3503     97     26    -35       C  
ATOM   5863  N   SER C 157      54.232 -17.436 -13.049  1.00 23.00           N  
ANISOU 5863  N   SER C 157     2739   2815   3184     80     71    -49       N  
ATOM   5864  CA  SER C 157      53.164 -16.627 -13.534  1.00 23.66           C  
ANISOU 5864  CA  SER C 157     2831   2910   3246     72     74    -39       C  
ATOM   5865  C   SER C 157      52.779 -17.014 -15.004  1.00 24.87           C  
ANISOU 5865  C   SER C 157     3000   3062   3385     66     79    -48       C  
ATOM   5866  O   SER C 157      51.581 -16.861 -15.463  1.00 23.52           O  
ANISOU 5866  O   SER C 157     2839   2900   3198     57     72    -36       O  
ATOM   5867  CB  SER C 157      53.516 -15.089 -13.397  1.00 26.24           C  
ANISOU 5867  CB  SER C 157     3151   3249   3570     73     90    -36       C  
ATOM   5868  OG  SER C 157      54.336 -14.665 -14.486  1.00 29.59           O  
ANISOU 5868  OG  SER C 157     3577   3675   3991     75    108    -49       O  
ATOM   5869  N   ARG C 158      53.764 -17.517 -15.736  1.00 23.93           N  
ANISOU 5869  N   ARG C 158     2883   2936   3272     71     89    -70       N  
ATOM   5870  CA  ARG C 158      53.442 -18.077 -17.046  1.00 25.87           C  
ANISOU 5870  CA  ARG C 158     3143   3182   3503     64     93    -83       C  
ATOM   5871  C   ARG C 158      52.660 -19.401 -16.943  1.00 26.34           C  
ANISOU 5871  C   ARG C 158     3211   3227   3567     60     73    -83       C  
ATOM   5872  O   ARG C 158      51.686 -19.666 -17.721  1.00 27.23           O  
ANISOU 5872  O   ARG C 158     3338   3346   3661     47     67    -81       O  
ATOM   5873  CB  ARG C 158      54.719 -18.254 -17.843  1.00 26.88           C  
ANISOU 5873  CB  ARG C 158     3270   3307   3636     71    112   -109       C  
ATOM   5874  CG  ARG C 158      55.242 -16.889 -18.173  1.00 25.43           C  
ANISOU 5874  CG  ARG C 158     3079   3139   3442     71    130   -104       C  
ATOM   5875  CD  ARG C 158      56.667 -16.781 -17.870  1.00 28.04           C  
ANISOU 5875  CD  ARG C 158     3395   3465   3791     83    143   -117       C  
ATOM   5876  NE  ARG C 158      57.163 -15.501 -18.412  1.00 29.42           N  
ANISOU 5876  NE  ARG C 158     3566   3656   3955     80    161   -114       N  
ATOM   5877  CZ  ARG C 158      58.424 -15.336 -18.773  1.00 30.09           C  
ANISOU 5877  CZ  ARG C 158     3641   3743   4046     86    179   -128       C  
ATOM   5878  NH1 ARG C 158      59.239 -16.371 -18.658  1.00 32.23           N  
ANISOU 5878  NH1 ARG C 158     3908   4001   4337     97    180   -147       N  
ATOM   5879  NH2 ARG C 158      58.874 -14.170 -19.255  1.00 31.44           N  
ANISOU 5879  NH2 ARG C 158     3807   3930   4209     83    194   -123       N  
ATOM   5880  N   LEU C 159      52.995 -20.200 -15.965  1.00 24.36           N  
ANISOU 5880  N   LEU C 159     2952   2960   3340     67     61    -82       N  
ATOM   5881  CA  LEU C 159      52.245 -21.451 -15.888  1.00 25.76           C  
ANISOU 5881  CA  LEU C 159     3138   3124   3525     62     41    -81       C  
ATOM   5882  C   LEU C 159      50.828 -21.249 -15.249  1.00 26.26           C  
ANISOU 5882  C   LEU C 159     3203   3197   3576     52     22    -52       C  
ATOM   5883  O   LEU C 159      49.880 -21.899 -15.633  1.00 25.69           O  
ANISOU 5883  O   LEU C 159     3142   3121   3496     41      9    -48       O  
ATOM   5884  CB  LEU C 159      53.051 -22.515 -15.202  1.00 25.51           C  
ANISOU 5884  CB  LEU C 159     3096   3069   3526     73     33    -88       C  
ATOM   5885  CG  LEU C 159      52.389 -23.819 -14.756  1.00 25.74           C  
ANISOU 5885  CG  LEU C 159     3128   3078   3572     69      9    -80       C  
ATOM   5886  CD1 LEU C 159      52.277 -24.664 -16.006  1.00 26.15           C  
ANISOU 5886  CD1 LEU C 159     3195   3116   3621     64     14   -106       C  
ATOM   5887  CD2 LEU C 159      53.212 -24.474 -13.619  1.00 24.65           C  
ANISOU 5887  CD2 LEU C 159     2971   2924   3468     80      0    -72       C  
ATOM   5888  N   LYS C 160      50.692 -20.279 -14.344  1.00 27.03           N  
ANISOU 5888  N   LYS C 160     3289   3307   3670     54     23    -34       N  
ATOM   5889  CA  LYS C 160      49.434 -20.027 -13.697  1.00 24.24           C  
ANISOU 5889  CA  LYS C 160     2935   2965   3307     46      8     -8       C  
ATOM   5890  C   LYS C 160      48.536 -19.461 -14.765  1.00 24.80           C  
ANISOU 5890  C   LYS C 160     3018   3048   3354     36     13     -4       C  
ATOM   5891  O   LYS C 160      47.369 -19.865 -14.867  1.00 23.04           O  
ANISOU 5891  O   LYS C 160     2802   2829   3123     26     -1      9       O  
ATOM   5892  CB  LYS C 160      49.620 -19.050 -12.575  1.00 23.21           C  
ANISOU 5892  CB  LYS C 160     2790   2847   3179     51     13      3       C  
ATOM   5893  CG  LYS C 160      50.444 -19.628 -11.453  1.00 22.62           C  
ANISOU 5893  CG  LYS C 160     2703   2765   3126     57      5      3       C  
ATOM   5894  CD  LYS C 160      50.840 -18.524 -10.512  1.00 22.97           C  
ANISOU 5894  CD  LYS C 160     2733   2823   3169     60     13      8       C  
ATOM   5895  CE  LYS C 160      51.390 -19.108  -9.203  1.00 24.24           C  
ANISOU 5895  CE  LYS C 160     2878   2983   3346     62      0     16       C  
ATOM   5896  NZ  LYS C 160      52.284 -18.148  -8.507  1.00 24.92           N  
ANISOU 5896  NZ  LYS C 160     2952   3080   3434     65     12     12       N  
ATOM   5897  N   TYR C 161      49.107 -18.539 -15.547  1.00 25.34           N  
ANISOU 5897  N   TYR C 161     3087   3125   3413     38     33    -14       N  
ATOM   5898  CA  TYR C 161      48.413 -17.930 -16.699  1.00 26.43           C  
ANISOU 5898  CA  TYR C 161     3235   3277   3529     27     40     -8       C  
ATOM   5899  C   TYR C 161      47.902 -18.905 -17.700  1.00 26.49           C  
ANISOU 5899  C   TYR C 161     3257   3282   3524     15     31    -17       C  
ATOM   5900  O   TYR C 161      46.728 -18.929 -17.971  1.00 29.16           O  
ANISOU 5900  O   TYR C 161     3601   3629   3848      3     19      0       O  
ATOM   5901  CB  TYR C 161      49.202 -16.794 -17.446  1.00 25.33           C  
ANISOU 5901  CB  TYR C 161     3092   3148   3382     30     62    -16       C  
ATOM   5902  CG  TYR C 161      48.276 -16.003 -18.352  1.00 25.29           C  
ANISOU 5902  CG  TYR C 161     3092   3160   3356     18     65      1       C  
ATOM   5903  CD1 TYR C 161      47.315 -15.196 -17.783  1.00 25.47           C  
ANISOU 5903  CD1 TYR C 161     3107   3189   3379     16     59     27       C  
ATOM   5904  CD2 TYR C 161      48.288 -16.157 -19.780  1.00 26.68           C  
ANISOU 5904  CD2 TYR C 161     3278   3346   3510      6     71     -7       C  
ATOM   5905  CE1 TYR C 161      46.401 -14.496 -18.552  1.00 28.33           C  
ANISOU 5905  CE1 TYR C 161     3471   3566   3726      6     59     47       C  
ATOM   5906  CE2 TYR C 161      47.368 -15.453 -20.584  1.00 26.20           C  
ANISOU 5906  CE2 TYR C 161     3220   3304   3431     -7     69     14       C  
ATOM   5907  CZ  TYR C 161      46.455 -14.635 -19.956  1.00 28.55           C  
ANISOU 5907  CZ  TYR C 161     3508   3605   3733     -6     63     42       C  
ATOM   5908  OH  TYR C 161      45.536 -13.902 -20.592  1.00 33.36           O  
ANISOU 5908  OH  TYR C 161     4116   4229   4330    -17     61     68       O  
ATOM   5909  N   TYR C 162      48.768 -19.680 -18.320  1.00 29.30           N  
ANISOU 5909  N   TYR C 162     3619   3627   3884     18     38    -44       N  
ATOM   5910  CA  TYR C 162      48.292 -20.602 -19.391  1.00 27.79           C  
ANISOU 5910  CA  TYR C 162     3445   3435   3680      4     32    -58       C  
ATOM   5911  C   TYR C 162      47.221 -21.593 -18.879  1.00 25.82           C  
ANISOU 5911  C   TYR C 162     3200   3174   3436     -3      6    -45       C  
ATOM   5912  O   TYR C 162      46.253 -21.924 -19.593  1.00 23.12           O  
ANISOU 5912  O   TYR C 162     2869   2839   3075    -20     -3    -41       O  
ATOM   5913  CB  TYR C 162      49.466 -21.354 -20.028  1.00 29.10           C  
ANISOU 5913  CB  TYR C 162     3615   3587   3854      9     45    -94       C  
ATOM   5914  CG  TYR C 162      50.522 -20.429 -20.611  1.00 30.57           C  
ANISOU 5914  CG  TYR C 162     3795   3786   4033     15     71   -106       C  
ATOM   5915  CD1 TYR C 162      50.187 -19.470 -21.556  1.00 32.07           C  
ANISOU 5915  CD1 TYR C 162     3989   4002   4195      3     80    -98       C  
ATOM   5916  CD2 TYR C 162      51.876 -20.591 -20.272  1.00 32.46           C  
ANISOU 5916  CD2 TYR C 162     4024   4012   4295     32     84   -125       C  
ATOM   5917  CE1 TYR C 162      51.153 -18.631 -22.102  1.00 34.70           C  
ANISOU 5917  CE1 TYR C 162     4315   4346   4520      7    103   -106       C  
ATOM   5918  CE2 TYR C 162      52.862 -19.796 -20.814  1.00 32.26           C  
ANISOU 5918  CE2 TYR C 162     3994   4000   4264     36    107   -136       C  
ATOM   5919  CZ  TYR C 162      52.492 -18.803 -21.716  1.00 36.29           C  
ANISOU 5919  CZ  TYR C 162     4507   4534   4744     24    116   -126       C  
ATOM   5920  OH  TYR C 162      53.460 -18.018 -22.264  1.00 36.64           O  
ANISOU 5920  OH  TYR C 162     4545   4592   4783     27    138   -134       O  
ATOM   5921  N   ILE C 163      47.379 -22.029 -17.644  1.00 24.53           N  
ANISOU 5921  N   ILE C 163     3027   2996   3297      6     -4    -37       N  
ATOM   5922  CA  ILE C 163      46.416 -22.977 -17.079  1.00 24.94           C  
ANISOU 5922  CA  ILE C 163     3081   3039   3356     -1    -28    -22       C  
ATOM   5923  C   ILE C 163      45.056 -22.280 -16.944  1.00 24.76           C  
ANISOU 5923  C   ILE C 163     3057   3036   3313    -12    -38      8       C  
ATOM   5924  O   ILE C 163      43.993 -22.885 -17.257  1.00 23.66           O  
ANISOU 5924  O   ILE C 163     2927   2898   3165    -26    -55     18       O  
ATOM   5925  CB  ILE C 163      46.926 -23.571 -15.730  1.00 27.40           C  
ANISOU 5925  CB  ILE C 163     3378   3332   3697     10    -39    -16       C  
ATOM   5926  CG1 ILE C 163      47.898 -24.734 -16.000  1.00 27.41           C  
ANISOU 5926  CG1 ILE C 163     3383   3307   3724     17    -38    -44       C  
ATOM   5927  CG2 ILE C 163      45.810 -24.234 -14.904  1.00 25.94           C  
ANISOU 5927  CG2 ILE C 163     3191   3145   3517      2    -65      9       C  
ATOM   5928  CD1 ILE C 163      48.773 -25.088 -14.824  1.00 26.12           C  
ANISOU 5928  CD1 ILE C 163     3203   3129   3592     31    -42    -39       C  
ATOM   5929  N   SER C 164      45.084 -20.981 -16.573  1.00 24.06           N  
ANISOU 5929  N   SER C 164     2958   2964   3219     -5    -26     22       N  
ATOM   5930  CA  SER C 164      43.876 -20.342 -16.119  1.00 23.20           C  
ANISOU 5930  CA  SER C 164     2843   2871   3100    -11    -35     52       C  
ATOM   5931  C   SER C 164      43.066 -20.117 -17.401  1.00 23.95           C  
ANISOU 5931  C   SER C 164     2948   2978   3170    -26    -35     58       C  
ATOM   5932  O   SER C 164      41.828 -20.136 -17.391  1.00 25.37           O  
ANISOU 5932  O   SER C 164     3128   3168   3340    -37    -49     82       O  
ATOM   5933  CB  SER C 164      44.153 -19.038 -15.430  1.00 21.91           C  
ANISOU 5933  CB  SER C 164     2666   2718   2941      0    -20     61       C  
ATOM   5934  OG  SER C 164      44.465 -17.993 -16.388  1.00 20.85           O  
ANISOU 5934  OG  SER C 164     2533   2593   2794      0     -2     57       O  
ATOM   5935  N   GLN C 165      43.764 -19.875 -18.504  1.00 25.61           N  
ANISOU 5935  N   GLN C 165     3167   3193   3371    -29    -20     38       N  
ATOM   5936  CA  GLN C 165      43.100 -19.645 -19.767  1.00 25.09           C  
ANISOU 5936  CA  GLN C 165     3110   3143   3279    -46    -20     44       C  
ATOM   5937  C   GLN C 165      42.454 -20.913 -20.074  1.00 26.88           C  
ANISOU 5937  C   GLN C 165     3349   3363   3501    -60    -39     39       C  
ATOM   5938  O   GLN C 165      41.255 -20.904 -20.278  1.00 30.51           O  
ANISOU 5938  O   GLN C 165     3810   3834   3947    -75    -54     62       O  
ATOM   5939  CB  GLN C 165      44.038 -19.162 -20.847  1.00 26.88           C  
ANISOU 5939  CB  GLN C 165     3341   3378   3492    -47      0     24       C  
ATOM   5940  CG  GLN C 165      44.561 -17.743 -20.616  1.00 27.48           C  
ANISOU 5940  CG  GLN C 165     3403   3462   3573    -35     18     35       C  
ATOM   5941  CD  GLN C 165      43.461 -16.817 -20.049  1.00 31.09           C  
ANISOU 5941  CD  GLN C 165     3849   3930   4032    -36     11     71       C  
ATOM   5942  OE1 GLN C 165      43.289 -16.663 -18.771  1.00 29.32           O  
ANISOU 5942  OE1 GLN C 165     3615   3698   3827    -24      7     80       O  
ATOM   5943  NE2 GLN C 165      42.637 -16.258 -20.973  1.00 30.75           N  
ANISOU 5943  NE2 GLN C 165     3807   3906   3970    -50      9     92       N  
ATOM   5944  N   LYS C 166      43.168 -22.047 -20.018  1.00 26.41           N  
ANISOU 5944  N   LYS C 166     3296   3281   3455    -57    -41     11       N  
ATOM   5945  CA  LYS C 166      42.490 -23.309 -20.263  1.00 26.59           C  
ANISOU 5945  CA  LYS C 166     3331   3294   3477    -71    -61      6       C  
ATOM   5946  C   LYS C 166      41.265 -23.556 -19.382  1.00 27.54           C  
ANISOU 5946  C   LYS C 166     3445   3414   3603    -77    -85     39       C  
ATOM   5947  O   LYS C 166      40.207 -23.919 -19.862  1.00 27.77           O  
ANISOU 5947  O   LYS C 166     3482   3452   3617    -96   -101     51       O  
ATOM   5948  CB  LYS C 166      43.499 -24.451 -20.188  1.00 27.42           C  
ANISOU 5948  CB  LYS C 166     3441   3370   3605    -63    -59    -28       C  
ATOM   5949  CG  LYS C 166      42.935 -25.823 -20.458  1.00 28.99           C  
ANISOU 5949  CG  LYS C 166     3653   3552   3810    -78    -79    -38       C  
ATOM   5950  CD  LYS C 166      42.703 -26.007 -21.971  1.00 30.19           C  
ANISOU 5950  CD  LYS C 166     3822   3716   3932    -99    -74    -60       C  
ATOM   5951  CE  LYS C 166      41.873 -27.262 -22.170  1.00 32.36           C  
ANISOU 5951  CE  LYS C 166     4109   3976   4209   -118    -97    -64       C  
ATOM   5952  NZ  LYS C 166      41.311 -27.376 -23.558  1.00 30.98           N  
ANISOU 5952  NZ  LYS C 166     3950   3820   4000   -144    -97    -78       N  
ATOM   5953  N   LEU C 167      41.395 -23.404 -18.069  1.00 28.63           N  
ANISOU 5953  N   LEU C 167     3569   3546   3761    -62    -88     53       N  
ATOM   5954  CA  LEU C 167      40.263 -23.700 -17.182  1.00 28.22           C  
ANISOU 5954  CA  LEU C 167     3510   3497   3714    -68   -110     84       C  
ATOM   5955  C   LEU C 167      39.234 -22.531 -17.012  1.00 29.00           C  
ANISOU 5955  C   LEU C 167     3598   3622   3797    -71   -108    117       C  
ATOM   5956  O   LEU C 167      38.249 -22.703 -16.270  1.00 26.37           O  
ANISOU 5956  O   LEU C 167     3258   3295   3467    -75   -124    143       O  
ATOM   5957  CB  LEU C 167      40.830 -24.137 -15.816  1.00 29.16           C  
ANISOU 5957  CB  LEU C 167     3617   3601   3860    -54   -115     86       C  
ATOM   5958  CG  LEU C 167      41.691 -25.404 -15.921  1.00 30.15           C  
ANISOU 5958  CG  LEU C 167     3749   3697   4006    -51   -120     59       C  
ATOM   5959  CD1 LEU C 167      42.219 -25.743 -14.534  1.00 31.38           C  
ANISOU 5959  CD1 LEU C 167     3890   3842   4189    -38   -126     68       C  
ATOM   5960  CD2 LEU C 167      40.861 -26.541 -16.462  1.00 29.08           C  
ANISOU 5960  CD2 LEU C 167     3627   3551   3870    -70   -141     59       C  
ATOM   5961  N   ASN C 168      39.492 -21.344 -17.637  1.00 28.53           N  
ANISOU 5961  N   ASN C 168     3537   3577   3725    -67    -89    116       N  
ATOM   5962  CA  ASN C 168      38.573 -20.166 -17.573  1.00 29.09           C  
ANISOU 5962  CA  ASN C 168     3597   3669   3787    -68    -86    147       C  
ATOM   5963  C   ASN C 168      38.296 -19.704 -16.169  1.00 25.79           C  
ANISOU 5963  C   ASN C 168     3162   3253   3384    -56    -85    165       C  
ATOM   5964  O   ASN C 168      37.156 -19.475 -15.827  1.00 25.02           O  
ANISOU 5964  O   ASN C 168     3055   3168   3283    -61    -95    192       O  
ATOM   5965  CB  ASN C 168      37.222 -20.444 -18.278  1.00 31.51           C  
ANISOU 5965  CB  ASN C 168     3907   3989   4075    -90   -103    170       C  
ATOM   5966  CG  ASN C 168      36.442 -19.176 -18.601  1.00 41.10           C  
ANISOU 5966  CG  ASN C 168     5110   5224   5280    -92    -97    199       C  
ATOM   5967  OD1 ASN C 168      37.020 -18.087 -18.876  1.00 48.36           O  
ANISOU 5967  OD1 ASN C 168     6024   6148   6200    -82    -77    197       O  
ATOM   5968  ND2 ASN C 168      35.098 -19.290 -18.584  1.00 46.31           N  
ANISOU 5968  ND2 ASN C 168     5764   5896   5933   -104   -114    230       N  
ATOM   5969  N   VAL C 169      39.341 -19.607 -15.365  1.00 24.62           N  
ANISOU 5969  N   VAL C 169     3007   3094   3250    -40    -75    148       N  
ATOM   5970  CA  VAL C 169      39.293 -19.009 -14.053  1.00 25.55           C  
ANISOU 5970  CA  VAL C 169     3108   3217   3380    -28    -70    159       C  
ATOM   5971  C   VAL C 169      40.225 -17.776 -13.948  1.00 27.89           C  
ANISOU 5971  C   VAL C 169     3398   3515   3682    -14    -46    146       C  
ATOM   5972  O   VAL C 169      41.003 -17.451 -14.883  1.00 26.65           O  
ANISOU 5972  O   VAL C 169     3249   3354   3521    -13    -33    130       O  
ATOM   5973  CB  VAL C 169      39.657 -19.988 -12.941  1.00 23.70           C  
ANISOU 5973  CB  VAL C 169     2870   2972   3159    -25    -83    155       C  
ATOM   5974  CG1 VAL C 169      38.796 -21.259 -13.031  1.00 24.53           C  
ANISOU 5974  CG1 VAL C 169     2982   3073   3263    -40   -108    167       C  
ATOM   5975  CG2 VAL C 169      41.113 -20.340 -12.999  1.00 23.89           C  
ANISOU 5975  CG2 VAL C 169     2900   2981   3196    -16    -74    126       C  
ATOM   5976  N   CYS C 170      40.156 -17.112 -12.791  1.00 29.32           N  
ANISOU 5976  N   CYS C 170     3565   3703   3873     -5    -39    153       N  
ATOM   5977  CA  CYS C 170      41.080 -16.023 -12.448  1.00 28.85           C  
ANISOU 5977  CA  CYS C 170     3497   3642   3822      6    -18    140       C  
ATOM   5978  C   CYS C 170      42.534 -16.548 -12.469  1.00 26.97           C  
ANISOU 5978  C   CYS C 170     3265   3391   3591     12    -14    114       C  
ATOM   5979  O   CYS C 170      42.839 -17.377 -11.627  1.00 28.34           O  
ANISOU 5979  O   CYS C 170     3435   3559   3772     13    -25    110       O  
ATOM   5980  CB  CYS C 170      40.825 -15.533 -11.018  1.00 27.21           C  
ANISOU 5980  CB  CYS C 170     3273   3443   3621     12    -15    146       C  
ATOM   5981  SG  CYS C 170      41.407 -13.827 -10.770  1.00 34.46           S  
ANISOU 5981  SG  CYS C 170     4180   4362   4549     24     12    136       S  
ATOM   5982  N   PRO C 171      43.428 -15.954 -13.303  1.00 24.24           N  
ANISOU 5982  N   PRO C 171     2923   3040   3244     16      2     98       N  
ATOM   5983  CA  PRO C 171      44.825 -16.318 -13.467  1.00 25.27           C  
ANISOU 5983  CA  PRO C 171     3058   3160   3382     22      9     74       C  
ATOM   5984  C   PRO C 171      45.463 -16.511 -12.073  1.00 24.65           C  
ANISOU 5984  C   PRO C 171     2969   3079   3319     30      7     69       C  
ATOM   5985  O   PRO C 171      46.142 -17.526 -11.826  1.00 22.31           O  
ANISOU 5985  O   PRO C 171     2673   2771   3031     32     -1     59       O  
ATOM   5986  CB  PRO C 171      45.439 -15.088 -14.175  1.00 24.76           C  
ANISOU 5986  CB  PRO C 171     2991   3098   3315     26     30     67       C  
ATOM   5987  CG  PRO C 171      44.277 -14.589 -14.985  1.00 24.57           C  
ANISOU 5987  CG  PRO C 171     2970   3084   3279     17     29     87       C  
ATOM   5988  CD  PRO C 171      43.165 -14.660 -13.945  1.00 24.75           C  
ANISOU 5988  CD  PRO C 171     2985   3112   3305     17     17    107       C  
ATOM   5989  N   ARG C 172      45.137 -15.658 -11.143  1.00 24.91           N  
ANISOU 5989  N   ARG C 172     2989   3121   3353     33     12     78       N  
ATOM   5990  CA  ARG C 172      45.794 -15.849  -9.786  1.00 26.91           C  
ANISOU 5990  CA  ARG C 172     3231   3377   3616     37      9     73       C  
ATOM   5991  C   ARG C 172      45.169 -16.872  -8.823  1.00 27.03           C  
ANISOU 5991  C   ARG C 172     3241   3396   3631     31    -11     87       C  
ATOM   5992  O   ARG C 172      45.679 -17.121  -7.678  1.00 27.00           O  
ANISOU 5992  O   ARG C 172     3226   3398   3634     31    -17     87       O  
ATOM   5993  CB  ARG C 172      45.940 -14.527  -9.046  1.00 28.23           C  
ANISOU 5993  CB  ARG C 172     3385   3553   3785     41     25     70       C  
ATOM   5994  CG  ARG C 172      47.113 -14.568  -8.051  1.00 28.83           C  
ANISOU 5994  CG  ARG C 172     3452   3630   3869     44     27     57       C  
ATOM   5995  CD  ARG C 172      47.067 -13.372  -7.136  1.00 30.37           C  
ANISOU 5995  CD  ARG C 172     3635   3837   4065     45     40     53       C  
ATOM   5996  NE  ARG C 172      48.023 -13.487  -6.009  1.00 32.05           N  
ANISOU 5996  NE  ARG C 172     3837   4057   4281     44     38     44       N  
ATOM   5997  CZ  ARG C 172      49.263 -12.995  -5.969  1.00 30.82           C  
ANISOU 5997  CZ  ARG C 172     3678   3897   4133     47     49     28       C  
ATOM   5998  NH1 ARG C 172      49.807 -12.337  -7.024  1.00 30.78           N  
ANISOU 5998  NH1 ARG C 172     3679   3880   4134     53     64     19       N  
ATOM   5999  NH2 ARG C 172      49.951 -13.162  -4.849  1.00 29.14           N  
ANISOU 5999  NH2 ARG C 172     3454   3695   3922     43     44     25       N  
ATOM   6000  N   ASP C 173      44.018 -17.401  -9.207  1.00 28.34           N  
ANISOU 6000  N   ASP C 173     3412   3563   3789     23    -25    103       N  
ATOM   6001  CA  ASP C 173      43.462 -18.519  -8.463  1.00 29.67           C  
ANISOU 6001  CA  ASP C 173     3577   3734   3959     16    -47    118       C  
ATOM   6002  C   ASP C 173      44.097 -19.900  -8.870  1.00 28.09           C  
ANISOU 6002  C   ASP C 173     3386   3514   3771     15    -61    110       C  
ATOM   6003  O   ASP C 173      43.754 -20.923  -8.275  1.00 29.42           O  
ANISOU 6003  O   ASP C 173     3552   3681   3946      9    -81    124       O  
ATOM   6004  CB  ASP C 173      41.940 -18.529  -8.552  1.00 34.81           C  
ANISOU 6004  CB  ASP C 173     4229   4397   4600      8    -56    140       C  
ATOM   6005  CG  ASP C 173      41.278 -17.429  -7.661  1.00 39.92           C  
ANISOU 6005  CG  ASP C 173     4860   5064   5240      9    -45    150       C  
ATOM   6006  OD1 ASP C 173      41.941 -16.845  -6.738  1.00 44.57           O  
ANISOU 6006  OD1 ASP C 173     5439   5660   5832     14    -35    140       O  
ATOM   6007  OD2 ASP C 173      40.073 -17.184  -7.883  1.00 40.40           O  
ANISOU 6007  OD2 ASP C 173     4921   5135   5295      5    -48    167       O  
ATOM   6008  N   VAL C 174      44.978 -19.894  -9.882  1.00 24.96           N  
ANISOU 6008  N   VAL C 174     3000   3104   3380     20    -50     89       N  
ATOM   6009  CA  VAL C 174      45.927 -21.011 -10.154  1.00 25.44           C  
ANISOU 6009  CA  VAL C 174     3065   3142   3456     24    -56     75       C  
ATOM   6010  C   VAL C 174      47.186 -20.847  -9.291  1.00 25.52           C  
ANISOU 6010  C   VAL C 174     3062   3151   3481     33    -50     67       C  
ATOM   6011  O   VAL C 174      47.777 -19.780  -9.260  1.00 25.96           O  
ANISOU 6011  O   VAL C 174     3114   3216   3534     39    -32     58       O  
ATOM   6012  CB  VAL C 174      46.317 -21.103 -11.624  1.00 24.22           C  
ANISOU 6012  CB  VAL C 174     2926   2976   3299     25    -45     54       C  
ATOM   6013  CG1 VAL C 174      47.161 -22.371 -11.867  1.00 24.93           C  
ANISOU 6013  CG1 VAL C 174     3019   3042   3410     28    -52     37       C  
ATOM   6014  CG2 VAL C 174      45.046 -21.221 -12.451  1.00 23.25           C  
ANISOU 6014  CG2 VAL C 174     2815   2859   3159     12    -53     63       C  
ATOM   6015  N   ASN C 175      47.555 -21.858  -8.530  1.00 25.85           N  
ANISOU 6015  N   ASN C 175     3095   3184   3540     32    -66     74       N  
ATOM   6016  CA  ASN C 175      48.862 -21.835  -7.859  1.00 28.11           C  
ANISOU 6016  CA  ASN C 175     3368   3467   3842     40    -62     67       C  
ATOM   6017  C   ASN C 175      49.733 -23.008  -8.338  1.00 27.55           C  
ANISOU 6017  C   ASN C 175     3299   3369   3797     47    -67     55       C  
ATOM   6018  O   ASN C 175      49.250 -24.148  -8.486  1.00 25.94           O  
ANISOU 6018  O   ASN C 175     3101   3150   3605     42    -85     62       O  
ATOM   6019  CB  ASN C 175      48.720 -21.945  -6.336  1.00 30.17           C  
ANISOU 6019  CB  ASN C 175     3611   3745   4104     34    -77     89       C  
ATOM   6020  CG  ASN C 175      49.640 -20.979  -5.606  1.00 35.47           C  
ANISOU 6020  CG  ASN C 175     4270   4432   4774     38    -63     83       C  
ATOM   6021  OD1 ASN C 175      50.736 -20.601  -6.112  1.00 37.28           O  
ANISOU 6021  OD1 ASN C 175     4499   4652   5011     47    -47     64       O  
ATOM   6022  ND2 ASN C 175      49.170 -20.495  -4.434  1.00 38.11           N  
ANISOU 6022  ND2 ASN C 175     4593   4792   5095     30    -67     97       N  
ATOM   6023  N   ALA C 176      51.019 -22.755  -8.559  1.00 27.52           N  
ANISOU 6023  N   ALA C 176     3291   3358   3805     57    -53     38       N  
ATOM   6024  CA  ALA C 176      51.851 -23.811  -9.066  1.00 26.88           C  
ANISOU 6024  CA  ALA C 176     3211   3251   3751     65    -54     24       C  
ATOM   6025  C   ALA C 176      53.220 -23.500  -8.539  1.00 27.84           C  
ANISOU 6025  C   ALA C 176     3316   3373   3888     74    -45     19       C  
ATOM   6026  O   ALA C 176      53.503 -22.333  -8.164  1.00 27.26           O  
ANISOU 6026  O   ALA C 176     3237   3320   3800     74    -33     19       O  
ATOM   6027  CB  ALA C 176      51.818 -23.778 -10.600  1.00 29.08           C  
ANISOU 6027  CB  ALA C 176     3507   3518   4021     67    -38     -1       C  
ATOM   6028  N   HIS C 177      54.047 -24.533  -8.447  1.00 26.22           N  
ANISOU 6028  N   HIS C 177     3101   3145   3715     82    -52     17       N  
ATOM   6029  CA  HIS C 177      55.440 -24.386  -8.015  1.00 26.87           C  
ANISOU 6029  CA  HIS C 177     3165   3226   3816     91    -45     13       C  
ATOM   6030  C   HIS C 177      56.413 -24.821  -9.017  1.00 26.44           C  
ANISOU 6030  C   HIS C 177     3114   3149   3783    105    -29    -12       C  
ATOM   6031  O   HIS C 177      56.416 -26.008  -9.431  1.00 27.12           O  
ANISOU 6031  O   HIS C 177     3202   3206   3894    109    -37    -18       O  
ATOM   6032  CB  HIS C 177      55.723 -25.137  -6.734  1.00 26.73           C  
ANISOU 6032  CB  HIS C 177     3127   3206   3821     89    -68     41       C  
ATOM   6033  CG  HIS C 177      54.967 -24.595  -5.605  1.00 29.44           C  
ANISOU 6033  CG  HIS C 177     3464   3579   4142     75    -81     65       C  
ATOM   6034  ND1 HIS C 177      55.564 -23.950  -4.587  1.00 29.86           N  
ANISOU 6034  ND1 HIS C 177     3500   3655   4190     71    -81     76       N  
ATOM   6035  CD2 HIS C 177      53.586 -24.486  -5.398  1.00 30.00           C  
ANISOU 6035  CD2 HIS C 177     3544   3664   4190     63    -91     78       C  
ATOM   6036  CE1 HIS C 177      54.630 -23.498  -3.740  1.00 28.31           C  
ANISOU 6036  CE1 HIS C 177     3302   3485   3968     58    -90     93       C  
ATOM   6037  NE2 HIS C 177      53.414 -23.822  -4.241  1.00 29.12           N  
ANISOU 6037  NE2 HIS C 177     3420   3582   4060     54    -96     95       N  
ATOM   6038  N   ILE C 178      57.296 -23.908  -9.353  1.00 24.53           N  
ANISOU 6038  N   ILE C 178     2868   2916   3534    111     -8    -27       N  
ATOM   6039  CA  ILE C 178      58.469 -24.242 -10.132  1.00 26.35           C  
ANISOU 6039  CA  ILE C 178     3094   3129   3786    125      8    -50       C  
ATOM   6040  C   ILE C 178      59.744 -23.955  -9.322  1.00 26.23           C  
ANISOU 6040  C   ILE C 178     3055   3119   3790    132     11    -42       C  
ATOM   6041  O   ILE C 178      59.946 -22.842  -8.871  1.00 25.55           O  
ANISOU 6041  O   ILE C 178     2964   3057   3684    127     17    -36       O  
ATOM   6042  CB  ILE C 178      58.483 -23.476 -11.454  1.00 25.63           C  
ANISOU 6042  CB  ILE C 178     3021   3046   3672    126     34    -77       C  
ATOM   6043  CG1 ILE C 178      57.305 -23.961 -12.288  1.00 26.05           C  
ANISOU 6043  CG1 ILE C 178     3095   3092   3710    118     29    -85       C  
ATOM   6044  CG2 ILE C 178      59.857 -23.615 -12.115  1.00 26.84           C  
ANISOU 6044  CG2 ILE C 178     3164   3187   3845    140     55   -100       C  
ATOM   6045  CD1 ILE C 178      56.964 -23.115 -13.497  1.00 26.88           C  
ANISOU 6045  CD1 ILE C 178     3217   3211   3782    113     49   -103       C  
ATOM   6046  N   VAL C 179      60.616 -24.957  -9.195  1.00 25.83           N  
ANISOU 6046  N   VAL C 179     2988   3045   3778    143      6    -42       N  
ATOM   6047  CA  VAL C 179      61.786 -24.872  -8.317  1.00 26.29           C  
ANISOU 6047  CA  VAL C 179     3021   3109   3859    148      3    -27       C  
ATOM   6048  C   VAL C 179      63.072 -25.307  -9.042  1.00 27.03           C  
ANISOU 6048  C   VAL C 179     3104   3182   3985    166     21    -48       C  
ATOM   6049  O   VAL C 179      63.058 -25.701 -10.242  1.00 27.87           O  
ANISOU 6049  O   VAL C 179     3223   3269   4094    174     38    -77       O  
ATOM   6050  CB  VAL C 179      61.585 -25.723  -7.033  1.00 25.30           C  
ANISOU 6050  CB  VAL C 179     2878   2979   3755    142    -27      7       C  
ATOM   6051  CG1 VAL C 179      60.343 -25.306  -6.261  1.00 25.64           C  
ANISOU 6051  CG1 VAL C 179     2929   3046   3765    124    -44     27       C  
ATOM   6052  CG2 VAL C 179      61.523 -27.215  -7.362  1.00 25.84           C  
ANISOU 6052  CG2 VAL C 179     2944   3009   3863    151    -38      5       C  
ATOM   6053  N   GLY C 180      64.145 -25.314  -8.263  1.00 26.96           N  
ANISOU 6053  N   GLY C 180     3069   3175   3999    170     17    -32       N  
ATOM   6054  CA  GLY C 180      65.490 -25.694  -8.679  1.00 28.43           C  
ANISOU 6054  CA  GLY C 180     3237   3345   4220    188     32    -45       C  
ATOM   6055  C   GLY C 180      66.323 -24.519  -9.184  1.00 29.81           C  
ANISOU 6055  C   GLY C 180     3409   3539   4375    190     58    -62       C  
ATOM   6056  O   GLY C 180      67.267 -24.024  -8.531  1.00 28.68           O  
ANISOU 6056  O   GLY C 180     3246   3411   4240    190     58    -48       O  
ATOM   6057  N   ALA C 181      65.964 -24.094 -10.385  1.00 29.92           N  
ANISOU 6057  N   ALA C 181     3447   3556   4366    191     79    -90       N  
ATOM   6058  CA  ALA C 181      66.641 -23.041 -11.081  1.00 29.94           C  
ANISOU 6058  CA  ALA C 181     3449   3575   4349    193    105   -108       C  
ATOM   6059  C   ALA C 181      65.668 -22.362 -12.030  1.00 29.87           C  
ANISOU 6059  C   ALA C 181     3469   3578   4299    184    117   -125       C  
ATOM   6060  O   ALA C 181      64.676 -22.965 -12.460  1.00 27.86           O  
ANISOU 6060  O   ALA C 181     3233   3313   4038    181    111   -132       O  
ATOM   6061  CB  ALA C 181      67.799 -23.641 -11.883  1.00 32.47           C  
ANISOU 6061  CB  ALA C 181     3757   3878   4701    211    126   -130       C  
ATOM   6062  N   HIS C 182      65.967 -21.092 -12.347  1.00 30.06           N  
ANISOU 6062  N   HIS C 182     3496   3626   4299    179    134   -130       N  
ATOM   6063  CA  HIS C 182      65.328 -20.351 -13.372  1.00 30.39           C  
ANISOU 6063  CA  HIS C 182     3559   3680   4306    171    149   -144       C  
ATOM   6064  C   HIS C 182      65.961 -20.795 -14.687  1.00 31.41           C  
ANISOU 6064  C   HIS C 182     3690   3801   4442    182    173   -174       C  
ATOM   6065  O   HIS C 182      67.093 -21.182 -14.690  1.00 31.79           O  
ANISOU 6065  O   HIS C 182     3720   3841   4517    194    183   -181       O  
ATOM   6066  CB  HIS C 182      65.561 -18.860 -13.045  1.00 33.12           C  
ANISOU 6066  CB  HIS C 182     3901   4051   4630    162    156   -134       C  
ATOM   6067  CG  HIS C 182      64.898 -17.908 -14.019  1.00 37.51           C  
ANISOU 6067  CG  HIS C 182     4476   4621   5152    153    170   -142       C  
ATOM   6068  ND1 HIS C 182      63.607 -18.048 -14.414  1.00 37.51           N  
ANISOU 6068  ND1 HIS C 182     4497   4622   5133    145    163   -142       N  
ATOM   6069  CD2 HIS C 182      65.393 -16.785 -14.685  1.00 37.69           C  
ANISOU 6069  CD2 HIS C 182     4498   4661   5159    150    190   -148       C  
ATOM   6070  CE1 HIS C 182      63.295 -17.074 -15.295  1.00 38.39           C  
ANISOU 6070  CE1 HIS C 182     4619   4748   5216    138    177   -147       C  
ATOM   6071  NE2 HIS C 182      64.382 -16.298 -15.450  1.00 39.06           N  
ANISOU 6071  NE2 HIS C 182     4691   4844   5305    140    194   -150       N  
ATOM   6072  N   GLY C 183      65.273 -20.773 -15.829  1.00 33.74           N  
ANISOU 6072  N   GLY C 183     4007   4100   4712    176    185   -193       N  
ATOM   6073  CA  GLY C 183      65.912 -21.245 -17.120  1.00 33.72           C  
ANISOU 6073  CA  GLY C 183     4005   4092   4713    184    210   -226       C  
ATOM   6074  C   GLY C 183      65.552 -22.702 -17.499  1.00 36.29           C  
ANISOU 6074  C   GLY C 183     4338   4390   5058    191    205   -246       C  
ATOM   6075  O   GLY C 183      64.630 -23.297 -16.931  1.00 35.29           O  
ANISOU 6075  O   GLY C 183     4220   4251   4937    186    182   -233       O  
ATOM   6076  N   ASN C 184      66.267 -23.257 -18.475  1.00 38.81           N  
ANISOU 6076  N   ASN C 184     4654   4702   5387    200    229   -278       N  
ATOM   6077  CA  ASN C 184      65.999 -24.563 -19.112  1.00 39.36           C  
ANISOU 6077  CA  ASN C 184     4734   4747   5474    205    231   -307       C  
ATOM   6078  C   ASN C 184      65.752 -25.709 -18.167  1.00 36.19           C  
ANISOU 6078  C   ASN C 184     4325   4311   5114    213    207   -294       C  
ATOM   6079  O   ASN C 184      65.080 -26.641 -18.500  1.00 37.14           O  
ANISOU 6079  O   ASN C 184     4459   4411   5241    210    200   -309       O  
ATOM   6080  CB  ASN C 184      67.235 -24.988 -19.920  1.00 46.15           C  
ANISOU 6080  CB  ASN C 184     5579   5599   6354    221    261   -340       C  
ATOM   6081  CG  ASN C 184      67.115 -24.661 -21.387  1.00 56.42           C  
ANISOU 6081  CG  ASN C 184     6896   6922   7616    211    288   -372       C  
ATOM   6082  OD1 ASN C 184      66.140 -24.028 -21.818  1.00 64.07           O  
ANISOU 6082  OD1 ASN C 184     7886   7913   8542    192    283   -366       O  
ATOM   6083  ND2 ASN C 184      68.107 -25.100 -22.178  1.00 60.80           N  
ANISOU 6083  ND2 ASN C 184     7440   7473   8186    223    316   -407       N  
ATOM   6084  N   LYS C 185      66.395 -25.681 -17.017  1.00 36.77           N  
ANISOU 6084  N   LYS C 185     4376   4378   5217    222    194   -267       N  
ATOM   6085  CA  LYS C 185      66.363 -26.805 -16.101  1.00 34.60           C  
ANISOU 6085  CA  LYS C 185     4088   4071   4985    230    171   -252       C  
ATOM   6086  C   LYS C 185      65.329 -26.587 -15.008  1.00 33.03           C  
ANISOU 6086  C   LYS C 185     3894   3879   4773    216    139   -215       C  
ATOM   6087  O   LYS C 185      65.271 -27.379 -14.091  1.00 32.44           O  
ANISOU 6087  O   LYS C 185     3807   3784   4731    219    116   -193       O  
ATOM   6088  CB  LYS C 185      67.741 -27.019 -15.433  1.00 35.93           C  
ANISOU 6088  CB  LYS C 185     4223   4229   5198    247    174   -240       C  
ATOM   6089  CG  LYS C 185      68.924 -27.119 -16.381  1.00 37.62           C  
ANISOU 6089  CG  LYS C 185     4426   4440   5428    263    207   -273       C  
ATOM   6090  CD  LYS C 185      68.998 -28.498 -16.993  1.00 39.96           C  
ANISOU 6090  CD  LYS C 185     4721   4697   5761    276    215   -305       C  
ATOM   6091  CE  LYS C 185      70.448 -28.914 -17.168  1.00 42.13           C  
ANISOU 6091  CE  LYS C 185     4967   4957   6081    298    237   -319       C  
ATOM   6092  NZ  LYS C 185      70.569 -29.382 -18.582  1.00 42.26           N  
ANISOU 6092  NZ  LYS C 185     4996   4966   6094    304    268   -372       N  
ATOM   6093  N   MET C 186      64.562 -25.498 -15.052  1.00 32.45           N  
ANISOU 6093  N   MET C 186     3837   3835   4654    200    137   -205       N  
ATOM   6094  CA  MET C 186      63.481 -25.305 -14.029  1.00 32.42           C  
ANISOU 6094  CA  MET C 186     3840   3840   4637    187    109   -172       C  
ATOM   6095  C   MET C 186      62.725 -26.601 -13.769  1.00 31.76           C  
ANISOU 6095  C   MET C 186     3762   3729   4577    186     87   -167       C  
ATOM   6096  O   MET C 186      62.498 -27.385 -14.689  1.00 31.34           O  
ANISOU 6096  O   MET C 186     3720   3655   4530    188     94   -194       O  
ATOM   6097  CB  MET C 186      62.495 -24.203 -14.413  1.00 30.73           C  
ANISOU 6097  CB  MET C 186     3647   3655   4374    171    112   -170       C  
ATOM   6098  CG  MET C 186      61.654 -24.472 -15.671  1.00 31.76           C  
ANISOU 6098  CG  MET C 186     3803   3783   4481    163    120   -194       C  
ATOM   6099  SD  MET C 186      60.598 -23.064 -16.074  1.00 35.23           S  
ANISOU 6099  SD  MET C 186     4260   4256   4867    145    123   -184       S  
ATOM   6100  CE  MET C 186      61.683 -21.858 -16.803  1.00 30.17           C  
ANISOU 6100  CE  MET C 186     3613   3638   4210    149    154   -197       C  
ATOM   6101  N   VAL C 187      62.341 -26.844 -12.525  1.00 30.83           N  
ANISOU 6101  N   VAL C 187     3633   3609   4470    181     60   -133       N  
ATOM   6102  CA  VAL C 187      61.580 -28.046 -12.287  1.00 31.13           C  
ANISOU 6102  CA  VAL C 187     3676   3622   4530    178     37   -126       C  
ATOM   6103  C   VAL C 187      60.065 -27.773 -12.187  1.00 29.58           C  
ANISOU 6103  C   VAL C 187     3500   3440   4297    159     22   -113       C  
ATOM   6104  O   VAL C 187      59.626 -27.175 -11.234  1.00 29.07           O  
ANISOU 6104  O   VAL C 187     3431   3397   4216    150      7    -84       O  
ATOM   6105  CB  VAL C 187      62.164 -28.761 -11.063  1.00 32.00           C  
ANISOU 6105  CB  VAL C 187     3757   3715   4683    184     16    -96       C  
ATOM   6106  CG1 VAL C 187      61.325 -29.964 -10.703  1.00 32.33           C  
ANISOU 6106  CG1 VAL C 187     3803   3732   4749    179     -9    -81       C  
ATOM   6107  CG2 VAL C 187      63.571 -29.207 -11.432  1.00 33.58           C  
ANISOU 6107  CG2 VAL C 187     3939   3895   4924    204     34   -114       C  
ATOM   6108  N   LEU C 188      59.271 -28.170 -13.186  1.00 31.22           N  
ANISOU 6108  N   LEU C 188     3731   3639   4492    153     26   -135       N  
ATOM   6109  CA  LEU C 188      57.782 -27.964 -13.114  1.00 31.23           C  
ANISOU 6109  CA  LEU C 188     3751   3654   4461    136      9   -120       C  
ATOM   6110  C   LEU C 188      57.065 -29.061 -12.324  1.00 31.37           C  
ANISOU 6110  C   LEU C 188     3764   3651   4502    130    -20    -96       C  
ATOM   6111  O   LEU C 188      56.966 -30.151 -12.803  1.00 34.78           O  
ANISOU 6111  O   LEU C 188     4201   4054   4959    132    -24   -111       O  
ATOM   6112  CB  LEU C 188      57.179 -27.903 -14.518  1.00 32.30           C  
ANISOU 6112  CB  LEU C 188     3910   3791   4568    128     24   -150       C  
ATOM   6113  CG  LEU C 188      57.834 -26.851 -15.406  1.00 33.90           C  
ANISOU 6113  CG  LEU C 188     4118   4017   4746    131     54   -172       C  
ATOM   6114  CD1 LEU C 188      58.678 -27.517 -16.497  1.00 34.05           C  
ANISOU 6114  CD1 LEU C 188     4138   4016   4782    141     76   -212       C  
ATOM   6115  CD2 LEU C 188      56.770 -25.984 -16.027  1.00 32.37           C  
ANISOU 6115  CD2 LEU C 188     3943   3850   4505    115     57   -169       C  
ATOM   6116  N   LEU C 189      56.633 -28.784 -11.100  1.00 30.98           N  
ANISOU 6116  N   LEU C 189     3703   3618   4447    122    -41    -59       N  
ATOM   6117  CA  LEU C 189      56.004 -29.772 -10.188  1.00 31.95           C  
ANISOU 6117  CA  LEU C 189     3819   3727   4593    115    -72    -30       C  
ATOM   6118  C   LEU C 189      54.486 -30.036 -10.406  1.00 32.43           C  
ANISOU 6118  C   LEU C 189     3899   3790   4631     99    -87    -22       C  
ATOM   6119  O   LEU C 189      53.615 -29.345  -9.835  1.00 29.19           O  
ANISOU 6119  O   LEU C 189     3490   3408   4189     87    -96      0       O  
ATOM   6120  CB  LEU C 189      56.276 -29.351  -8.718  1.00 30.55           C  
ANISOU 6120  CB  LEU C 189     3618   3571   4416    112    -86      6       C  
ATOM   6121  CG  LEU C 189      57.759 -29.385  -8.346  1.00 30.73           C  
ANISOU 6121  CG  LEU C 189     3618   3587   4470    127    -79      6       C  
ATOM   6122  CD1 LEU C 189      57.852 -28.757  -6.976  1.00 31.34           C  
ANISOU 6122  CD1 LEU C 189     3677   3694   4535    118    -92     40       C  
ATOM   6123  CD2 LEU C 189      58.318 -30.842  -8.319  1.00 29.90           C  
ANISOU 6123  CD2 LEU C 189     3498   3439   4421    137    -90      8       C  
ATOM   6124  N   LYS C 190      54.177 -31.038 -11.227  1.00 34.02           N  
ANISOU 6124  N   LYS C 190     4112   3961   4849     98    -90    -42       N  
ATOM   6125  CA  LYS C 190      52.802 -31.346 -11.610  1.00 36.38           C  
ANISOU 6125  CA  LYS C 190     4431   4262   5129     81   -103    -39       C  
ATOM   6126  C   LYS C 190      51.983 -31.577 -10.333  1.00 37.01           C  
ANISOU 6126  C   LYS C 190     4500   4352   5210     70   -133      5       C  
ATOM   6127  O   LYS C 190      50.785 -31.190 -10.223  1.00 34.31           O  
ANISOU 6127  O   LYS C 190     4167   4031   4835     55   -143     21       O  
ATOM   6128  CB  LYS C 190      52.838 -32.579 -12.506  1.00 41.63           C  
ANISOU 6128  CB  LYS C 190     5106   4887   5822     83   -104    -67       C  
ATOM   6129  CG  LYS C 190      51.550 -33.052 -13.181  1.00 45.03           C  
ANISOU 6129  CG  LYS C 190     5560   5313   6237     65   -115    -74       C  
ATOM   6130  CD  LYS C 190      51.855 -34.399 -13.888  1.00 49.58           C  
ANISOU 6130  CD  LYS C 190     6141   5843   6853     69   -116   -104       C  
ATOM   6131  CE  LYS C 190      50.787 -35.477 -13.640  1.00 51.62           C  
ANISOU 6131  CE  LYS C 190     6405   6079   7129     53   -146    -87       C  
ATOM   6132  NZ  LYS C 190      49.486 -35.344 -14.396  1.00 49.86           N  
ANISOU 6132  NZ  LYS C 190     6206   5872   6866     32   -151    -93       N  
ATOM   6133  N   ARG C 191      52.658 -32.135  -9.339  1.00 35.31           N  
ANISOU 6133  N   ARG C 191     4261   4124   5030     77   -147     27       N  
ATOM   6134  CA  ARG C 191      51.982 -32.570  -8.146  1.00 36.66           C  
ANISOU 6134  CA  ARG C 191     4419   4302   5208     65   -177     70       C  
ATOM   6135  C   ARG C 191      51.472 -31.409  -7.330  1.00 37.27           C  
ANISOU 6135  C   ARG C 191     4491   4424   5243     56   -178     93       C  
ATOM   6136  O   ARG C 191      50.529 -31.581  -6.547  1.00 36.00           O  
ANISOU 6136  O   ARG C 191     4326   4279   5073     41   -200    125       O  
ATOM   6137  CB  ARG C 191      52.904 -33.410  -7.277  1.00 39.58           C  
ANISOU 6137  CB  ARG C 191     4762   4650   5626     73   -192     91       C  
ATOM   6138  CG  ARG C 191      52.160 -34.419  -6.420  1.00 43.51           C  
ANISOU 6138  CG  ARG C 191     5249   5137   6145     60   -227    130       C  
ATOM   6139  CD  ARG C 191      53.064 -35.414  -5.683  1.00 42.47           C  
ANISOU 6139  CD  ARG C 191     5089   4977   6069     67   -244    153       C  
ATOM   6140  NE  ARG C 191      54.402 -34.920  -5.332  1.00 43.51           N  
ANISOU 6140  NE  ARG C 191     5202   5117   6212     82   -230    151       N  
ATOM   6141  CZ  ARG C 191      54.849 -34.705  -4.095  1.00 43.29           C  
ANISOU 6141  CZ  ARG C 191     5149   5112   6187     77   -244    188       C  
ATOM   6142  NH1 ARG C 191      54.056 -34.893  -3.052  1.00 44.10           N  
ANISOU 6142  NH1 ARG C 191     5241   5237   6279     59   -271    230       N  
ATOM   6143  NH2 ARG C 191      56.095 -34.304  -3.899  1.00 44.23           N  
ANISOU 6143  NH2 ARG C 191     5251   5236   6318     90   -230    183       N  
ATOM   6144  N   TYR C 192      52.104 -30.241  -7.471  1.00 35.84           N  
ANISOU 6144  N   TYR C 192     4311   4266   5041     63   -154     78       N  
ATOM   6145  CA  TYR C 192      51.785 -29.095  -6.606  1.00 34.12           C  
ANISOU 6145  CA  TYR C 192     4086   4089   4788     56   -153     97       C  
ATOM   6146  C   TYR C 192      50.755 -28.110  -7.156  1.00 34.76           C  
ANISOU 6146  C   TYR C 192     4185   4194   4827     48   -141     88       C  
ATOM   6147  O   TYR C 192      50.324 -27.244  -6.411  1.00 39.80           O  
ANISOU 6147  O   TYR C 192     4818   4864   5440     42   -141    104       O  
ATOM   6148  CB  TYR C 192      53.059 -28.379  -6.117  1.00 34.66           C  
ANISOU 6148  CB  TYR C 192     4137   4169   4860     66   -139     93       C  
ATOM   6149  CG  TYR C 192      53.775 -29.180  -5.047  1.00 35.38           C  
ANISOU 6149  CG  TYR C 192     4203   4252   4986     67   -159    120       C  
ATOM   6150  CD1 TYR C 192      54.629 -30.244  -5.391  1.00 34.53           C  
ANISOU 6150  CD1 TYR C 192     4088   4107   4925     79   -162    113       C  
ATOM   6151  CD2 TYR C 192      53.549 -28.925  -3.687  1.00 34.40           C  
ANISOU 6151  CD2 TYR C 192     4061   4158   4849     54   -175    154       C  
ATOM   6152  CE1 TYR C 192      55.257 -30.999  -4.425  1.00 35.75           C  
ANISOU 6152  CE1 TYR C 192     4216   4253   5114     79   -182    142       C  
ATOM   6153  CE2 TYR C 192      54.189 -29.672  -2.713  1.00 36.92           C  
ANISOU 6153  CE2 TYR C 192     4355   4473   5198     52   -196    183       C  
ATOM   6154  CZ  TYR C 192      55.027 -30.717  -3.082  1.00 37.43           C  
ANISOU 6154  CZ  TYR C 192     4411   4498   5311     65   -200    179       C  
ATOM   6155  OH  TYR C 192      55.636 -31.463  -2.105  1.00 37.62           O  
ANISOU 6155  OH  TYR C 192     4407   4517   5368     63   -222    212       O  
ATOM   6156  N   ILE C 193      50.314 -28.278  -8.413  1.00 29.85           N  
ANISOU 6156  N   ILE C 193     3584   3557   4198     48   -132     65       N  
ATOM   6157  CA  ILE C 193      49.402 -27.358  -9.024  1.00 26.03           C  
ANISOU 6157  CA  ILE C 193     3117   3095   3677     41   -121     59       C  
ATOM   6158  C   ILE C 193      47.980 -27.388  -8.417  1.00 26.41           C  
ANISOU 6158  C   ILE C 193     3165   3161   3707     26   -141     89       C  
ATOM   6159  O   ILE C 193      47.404 -28.438  -8.178  1.00 25.24           O  
ANISOU 6159  O   ILE C 193     3016   2999   3573     17   -163    105       O  
ATOM   6160  CB  ILE C 193      49.328 -27.623 -10.520  1.00 25.01           C  
ANISOU 6160  CB  ILE C 193     3008   2949   3544     41   -109     29       C  
ATOM   6161  CG1 ILE C 193      50.735 -27.552 -11.154  1.00 24.44           C  
ANISOU 6161  CG1 ILE C 193     2935   2862   3488     57    -87     -1       C  
ATOM   6162  CG2 ILE C 193      48.409 -26.598 -11.182  1.00 23.86           C  
ANISOU 6162  CG2 ILE C 193     2876   2827   3359     33    -99     27       C  
ATOM   6163  CD1 ILE C 193      50.757 -27.987 -12.620  1.00 23.39           C  
ANISOU 6163  CD1 ILE C 193     2821   2712   3353     56    -75    -34       C  
ATOM   6164  N   THR C 194      47.401 -26.221  -8.185  1.00 25.90           N  
ANISOU 6164  N   THR C 194     3100   3126   3612     22   -131     96       N  
ATOM   6165  CA  THR C 194      46.072 -26.135  -7.588  1.00 26.45           C  
ANISOU 6165  CA  THR C 194     3168   3216   3664      9   -146    123       C  
ATOM   6166  C   THR C 194      45.358 -25.033  -8.296  1.00 26.02           C  
ANISOU 6166  C   THR C 194     3125   3180   3580      7   -130    116       C  
ATOM   6167  O   THR C 194      46.002 -24.043  -8.629  1.00 26.70           O  
ANISOU 6167  O   THR C 194     3212   3272   3658     16   -108     99       O  
ATOM   6168  CB  THR C 194      46.019 -25.844  -6.030  1.00 26.14           C  
ANISOU 6168  CB  THR C 194     3107   3202   3620      5   -155    150       C  
ATOM   6169  OG1 THR C 194      46.769 -24.674  -5.651  1.00 27.55           O  
ANISOU 6169  OG1 THR C 194     3279   3399   3790     12   -135    139       O  
ATOM   6170  CG2 THR C 194      46.538 -27.006  -5.272  1.00 27.00           C  
ANISOU 6170  CG2 THR C 194     3202   3297   3758      3   -177    166       C  
ATOM   6171  N   VAL C 195      44.034 -25.184  -8.401  1.00 24.22           N  
ANISOU 6171  N   VAL C 195     2902   2961   3339     -4   -142    134       N  
ATOM   6172  CA  VAL C 195      43.114 -24.242  -8.942  1.00 24.08           C  
ANISOU 6172  CA  VAL C 195     2891   2961   3295     -8   -132    136       C  
ATOM   6173  C   VAL C 195      42.062 -23.901  -7.915  1.00 25.28           C  
ANISOU 6173  C   VAL C 195     3031   3139   3435    -15   -141    165       C  
ATOM   6174  O   VAL C 195      41.217 -24.745  -7.525  1.00 26.31           O  
ANISOU 6174  O   VAL C 195     3158   3270   3568    -27   -163    187       O  
ATOM   6175  CB  VAL C 195      42.448 -24.836 -10.196  1.00 24.29           C  
ANISOU 6175  CB  VAL C 195     2935   2974   3316    -17   -139    130       C  
ATOM   6176  CG1 VAL C 195      41.407 -23.904 -10.775  1.00 23.60           C  
ANISOU 6176  CG1 VAL C 195     2854   2908   3205    -23   -131    139       C  
ATOM   6177  CG2 VAL C 195      43.539 -25.121 -11.209  1.00 25.04           C  
ANISOU 6177  CG2 VAL C 195     3043   3048   3423    -10   -126     98       C  
ATOM   6178  N   GLY C 196      42.044 -22.635  -7.532  1.00 25.00           N  
ANISOU 6178  N   GLY C 196     2987   3123   3386    -10   -123    164       N  
ATOM   6179  CA  GLY C 196      41.333 -22.224  -6.333  1.00 26.00           C  
ANISOU 6179  CA  GLY C 196     3098   3276   3504    -15   -127    185       C  
ATOM   6180  C   GLY C 196      41.448 -23.188  -5.159  1.00 27.69           C  
ANISOU 6180  C   GLY C 196     3299   3494   3728    -21   -148    203       C  
ATOM   6181  O   GLY C 196      40.430 -23.523  -4.531  1.00 26.94           O  
ANISOU 6181  O   GLY C 196     3196   3415   3625    -32   -162    227       O  
ATOM   6182  N   GLY C 197      42.652 -23.683  -4.879  1.00 26.29           N  
ANISOU 6182  N   GLY C 197     3117   3302   3567    -16   -150    194       N  
ATOM   6183  CA  GLY C 197      42.915 -24.390  -3.610  1.00 25.81           C  
ANISOU 6183  CA  GLY C 197     3039   3250   3515    -23   -169    214       C  
ATOM   6184  C   GLY C 197      42.717 -25.914  -3.770  1.00 27.30           C  
ANISOU 6184  C   GLY C 197     3231   3416   3725    -30   -195    229       C  
ATOM   6185  O   GLY C 197      42.917 -26.690  -2.812  1.00 28.41           O  
ANISOU 6185  O   GLY C 197     3356   3559   3878    -37   -215    251       O  
ATOM   6186  N   ILE C 198      42.278 -26.318  -4.954  1.00 25.47           N  
ANISOU 6186  N   ILE C 198     3017   3163   3497    -31   -197    220       N  
ATOM   6187  CA  ILE C 198      41.892 -27.697  -5.253  1.00 24.88           C  
ANISOU 6187  CA  ILE C 198     2947   3064   3442    -40   -222    231       C  
ATOM   6188  C   ILE C 198      42.952 -28.283  -6.178  1.00 25.80           C  
ANISOU 6188  C   ILE C 198     3075   3144   3582    -30   -217    203       C  
ATOM   6189  O   ILE C 198      43.340 -27.629  -7.189  1.00 25.31           O  
ANISOU 6189  O   ILE C 198     3026   3076   3511    -21   -195    175       O  
ATOM   6190  CB  ILE C 198      40.529 -27.670  -6.046  1.00 23.71           C  
ANISOU 6190  CB  ILE C 198     2812   2919   3275    -50   -226    237       C  
ATOM   6191  CG1 ILE C 198      39.534 -26.748  -5.334  1.00 23.20           C  
ANISOU 6191  CG1 ILE C 198     2736   2892   3184    -55   -221    257       C  
ATOM   6192  CG2 ILE C 198      39.947 -29.058  -6.230  1.00 23.07           C  
ANISOU 6192  CG2 ILE C 198     2735   2817   3211    -63   -254    252       C  
ATOM   6193  CD1 ILE C 198      38.180 -26.575  -6.009  1.00 23.08           C  
ANISOU 6193  CD1 ILE C 198     2730   2886   3152    -64   -225    268       C  
ATOM   6194  N   PRO C 199      43.357 -29.551  -5.926  1.00 25.87           N  
ANISOU 6194  N   PRO C 199     3079   3127   3623    -32   -237    211       N  
ATOM   6195  CA  PRO C 199      44.369 -30.105  -6.794  1.00 25.28           C  
ANISOU 6195  CA  PRO C 199     3013   3016   3574    -21   -229    182       C  
ATOM   6196  C   PRO C 199      43.962 -30.086  -8.292  1.00 24.84           C  
ANISOU 6196  C   PRO C 199     2982   2947   3507    -23   -218    154       C  
ATOM   6197  O   PRO C 199      42.827 -30.396  -8.677  1.00 24.59           O  
ANISOU 6197  O   PRO C 199     2960   2918   3465    -36   -231    164       O  
ATOM   6198  CB  PRO C 199      44.565 -31.549  -6.272  1.00 27.37           C  
ANISOU 6198  CB  PRO C 199     3267   3253   3877    -25   -256    201       C  
ATOM   6199  CG  PRO C 199      43.918 -31.593  -4.955  1.00 28.28           C  
ANISOU 6199  CG  PRO C 199     3363   3395   3984    -37   -276    242       C  
ATOM   6200  CD  PRO C 199      42.879 -30.502  -4.911  1.00 25.56           C  
ANISOU 6200  CD  PRO C 199     3024   3089   3598    -44   -266    247       C  
ATOM   6201  N   LEU C 200      44.913 -29.770  -9.138  1.00 23.65           N  
ANISOU 6201  N   LEU C 200     2840   2784   3360    -10   -197    121       N  
ATOM   6202  CA  LEU C 200      44.660 -29.745 -10.557  1.00 24.92           C  
ANISOU 6202  CA  LEU C 200     3023   2936   3508    -14   -185     93       C  
ATOM   6203  C   LEU C 200      44.189 -31.168 -10.996  1.00 25.63           C  
ANISOU 6203  C   LEU C 200     3122   2994   3620    -24   -206     91       C  
ATOM   6204  O   LEU C 200      43.355 -31.321 -11.905  1.00 25.03           O  
ANISOU 6204  O   LEU C 200     3063   2919   3528    -37   -209     82       O  
ATOM   6205  CB  LEU C 200      45.961 -29.326 -11.253  1.00 24.56           C  
ANISOU 6205  CB  LEU C 200     2981   2881   3468      1   -159     58       C  
ATOM   6206  CG  LEU C 200      45.821 -29.433 -12.800  1.00 24.91           C  
ANISOU 6206  CG  LEU C 200     3048   2917   3500     -3   -146     26       C  
ATOM   6207  CD1 LEU C 200      44.942 -28.306 -13.311  1.00 24.65           C  
ANISOU 6207  CD1 LEU C 200     3023   2915   3426    -12   -137     33       C  
ATOM   6208  CD2 LEU C 200      47.147 -29.482 -13.564  1.00 23.80           C  
ANISOU 6208  CD2 LEU C 200     2910   2759   3373     10   -124    -10       C  
ATOM   6209  N   GLN C 201      44.712 -32.212 -10.345  1.00 25.97           N  
ANISOU 6209  N   GLN C 201     3153   3011   3702    -21   -222     99       N  
ATOM   6210  CA  GLN C 201      44.211 -33.592 -10.642  1.00 27.19           C  
ANISOU 6210  CA  GLN C 201     3314   3132   3882    -32   -245    100       C  
ATOM   6211  C   GLN C 201      42.706 -33.693 -10.631  1.00 26.79           C  
ANISOU 6211  C   GLN C 201     3271   3098   3810    -53   -264    124       C  
ATOM   6212  O   GLN C 201      42.186 -34.480 -11.418  1.00 28.78           O  
ANISOU 6212  O   GLN C 201     3537   3329   4068    -65   -274    111       O  
ATOM   6213  CB  GLN C 201      44.765 -34.657  -9.700  1.00 28.66           C  
ANISOU 6213  CB  GLN C 201     3482   3292   4116    -28   -265    119       C  
ATOM   6214  CG  GLN C 201      44.476 -36.087 -10.154  1.00 28.46           C  
ANISOU 6214  CG  GLN C 201     3464   3224   4125    -37   -284    112       C  
ATOM   6215  CD  GLN C 201      45.270 -36.437 -11.391  1.00 29.74           C  
ANISOU 6215  CD  GLN C 201     3641   3354   4303    -27   -263     61       C  
ATOM   6216  OE1 GLN C 201      46.528 -36.377 -11.371  1.00 30.27           O  
ANISOU 6216  OE1 GLN C 201     3699   3407   4392     -8   -246     43       O  
ATOM   6217  NE2 GLN C 201      44.569 -36.737 -12.492  1.00 27.41           N  
ANISOU 6217  NE2 GLN C 201     3369   3050   3993    -41   -263     37       N  
ATOM   6218  N   GLU C 202      41.979 -32.928  -9.796  1.00 25.48           N  
ANISOU 6218  N   GLU C 202     3093   2968   3617    -58   -269    157       N  
ATOM   6219  CA  GLU C 202      40.507 -33.097  -9.851  1.00 24.33           C  
ANISOU 6219  CA  GLU C 202     2953   2837   3453    -78   -287    181       C  
ATOM   6220  C   GLU C 202      39.899 -32.686 -11.190  1.00 24.48           C  
ANISOU 6220  C   GLU C 202     2994   2863   3443    -86   -276    158       C  
ATOM   6221  O   GLU C 202      38.965 -33.325 -11.656  1.00 26.54           O  
ANISOU 6221  O   GLU C 202     3265   3116   3701   -104   -293    164       O  
ATOM   6222  CB  GLU C 202      39.811 -32.389  -8.731  1.00 23.62           C  
ANISOU 6222  CB  GLU C 202     2846   2785   3341    -82   -293    218       C  
ATOM   6223  CG  GLU C 202      40.271 -32.765  -7.310  1.00 24.29           C  
ANISOU 6223  CG  GLU C 202     2907   2872   3448    -78   -307    246       C  
ATOM   6224  CD  GLU C 202      39.120 -32.663  -6.317  1.00 25.57           C  
ANISOU 6224  CD  GLU C 202     3055   3066   3593    -93   -324    288       C  
ATOM   6225  OE1 GLU C 202      37.973 -32.371  -6.789  1.00 27.03           O  
ANISOU 6225  OE1 GLU C 202     3249   3267   3754   -104   -326    294       O  
ATOM   6226  OE2 GLU C 202      39.300 -32.874  -5.075  1.00 26.30           O  
ANISOU 6226  OE2 GLU C 202     3126   3170   3694    -95   -336    316       O  
ATOM   6227  N   PHE C 203      40.402 -31.605 -11.787  1.00 24.27           N  
ANISOU 6227  N   PHE C 203     2973   2851   3394    -76   -249    136       N  
ATOM   6228  CA  PHE C 203      40.022 -31.109 -13.150  1.00 23.47           C  
ANISOU 6228  CA  PHE C 203     2892   2760   3265    -83   -235    114       C  
ATOM   6229  C   PHE C 203      40.515 -31.960 -14.267  1.00 23.78           C  
ANISOU 6229  C   PHE C 203     2949   2768   3317    -87   -232     76       C  
ATOM   6230  O   PHE C 203      39.911 -32.042 -15.316  1.00 25.30           O  
ANISOU 6230  O   PHE C 203     3158   2965   3490   -102   -232     63       O  
ATOM   6231  CB  PHE C 203      40.647 -29.699 -13.379  1.00 22.25           C  
ANISOU 6231  CB  PHE C 203     2736   2628   3089    -69   -206    101       C  
ATOM   6232  CG  PHE C 203      40.150 -28.662 -12.390  1.00 22.16           C  
ANISOU 6232  CG  PHE C 203     2708   2648   3062    -65   -204    133       C  
ATOM   6233  CD1 PHE C 203      40.688 -28.580 -11.084  1.00 21.39           C  
ANISOU 6233  CD1 PHE C 203     2592   2554   2980    -55   -206    147       C  
ATOM   6234  CD2 PHE C 203      39.088 -27.825 -12.727  1.00 21.71           C  
ANISOU 6234  CD2 PHE C 203     2654   2619   2976    -74   -201    148       C  
ATOM   6235  CE1 PHE C 203      40.189 -27.677 -10.165  1.00 21.03           C  
ANISOU 6235  CE1 PHE C 203     2532   2538   2920    -53   -203    172       C  
ATOM   6236  CE2 PHE C 203      38.579 -26.897 -11.819  1.00 21.44           C  
ANISOU 6236  CE2 PHE C 203     2603   2610   2930    -70   -198    174       C  
ATOM   6237  CZ  PHE C 203      39.149 -26.800 -10.524  1.00 20.69           C  
ANISOU 6237  CZ  PHE C 203     2491   2519   2849    -60   -197    184       C  
ATOM   6238  N   ILE C 204      41.694 -32.484 -14.127  1.00 24.62           N  
ANISOU 6238  N   ILE C 204     3051   2847   3455    -72   -225     55       N  
ATOM   6239  CA  ILE C 204      42.154 -33.580 -15.029  1.00 26.52           C  
ANISOU 6239  CA  ILE C 204     3305   3051   3718    -76   -224     18       C  
ATOM   6240  C   ILE C 204      41.190 -34.810 -14.952  1.00 26.31           C  
ANISOU 6240  C   ILE C 204     3284   3003   3709    -95   -255     31       C  
ATOM   6241  O   ILE C 204      40.690 -35.260 -15.957  1.00 26.26           O  
ANISOU 6241  O   ILE C 204     3296   2989   3692   -111   -258     11       O  
ATOM   6242  CB  ILE C 204      43.610 -34.029 -14.734  1.00 26.32           C  
ANISOU 6242  CB  ILE C 204     3271   2996   3733    -54   -213     -2       C  
ATOM   6243  CG1 ILE C 204      44.567 -32.860 -14.976  1.00 26.42           C  
ANISOU 6243  CG1 ILE C 204     3280   3029   3728    -38   -183    -19       C  
ATOM   6244  CG2 ILE C 204      44.004 -35.214 -15.614  1.00 25.78           C  
ANISOU 6244  CG2 ILE C 204     3214   2887   3692    -57   -213    -41       C  
ATOM   6245  CD1 ILE C 204      46.014 -33.151 -14.540  1.00 26.81           C  
ANISOU 6245  CD1 ILE C 204     3315   3055   3815    -16   -172    -33       C  
ATOM   6246  N   ASN C 205      40.920 -35.319 -13.764  1.00 25.91           N  
ANISOU 6246  N   ASN C 205     3217   2945   3682    -95   -278     67       N  
ATOM   6247  CA  ASN C 205      39.902 -36.374 -13.645  1.00 26.67           C  
ANISOU 6247  CA  ASN C 205     3316   3024   3791   -116   -309     86       C  
ATOM   6248  C   ASN C 205      38.626 -35.935 -14.305  1.00 27.41           C  
ANISOU 6248  C   ASN C 205     3422   3146   3843   -137   -314     95       C  
ATOM   6249  O   ASN C 205      37.906 -36.801 -14.753  1.00 29.02           O  
ANISOU 6249  O   ASN C 205     3637   3334   4053   -156   -333     93       O  
ATOM   6250  CB  ASN C 205      39.514 -36.674 -12.179  1.00 25.04           C  
ANISOU 6250  CB  ASN C 205     3086   2823   3603   -117   -333    136       C  
ATOM   6251  CG  ASN C 205      40.661 -37.211 -11.373  1.00 25.42           C  
ANISOU 6251  CG  ASN C 205     3118   2845   3695   -100   -335    138       C  
ATOM   6252  OD1 ASN C 205      41.685 -37.573 -11.920  1.00 25.80           O  
ANISOU 6252  OD1 ASN C 205     3170   2862   3767    -87   -321    102       O  
ATOM   6253  ND2 ASN C 205      40.502 -37.263 -10.041  1.00 25.99           N  
ANISOU 6253  ND2 ASN C 205     3167   2929   3777   -100   -352    182       N  
ATOM   6254  N   ASN C 206      38.282 -34.629 -14.307  1.00 26.46           N  
ANISOU 6254  N   ASN C 206     3300   3068   3684   -134   -299    108       N  
ATOM   6255  CA  ASN C 206      36.998 -34.242 -14.830  1.00 27.89           C  
ANISOU 6255  CA  ASN C 206     3489   3275   3830   -154   -307    123       C  
ATOM   6256  C   ASN C 206      37.041 -34.010 -16.297  1.00 28.51           C  
ANISOU 6256  C   ASN C 206     3588   3357   3883   -163   -292     88       C  
ATOM   6257  O   ASN C 206      36.053 -33.598 -16.840  1.00 29.09           O  
ANISOU 6257  O   ASN C 206     3669   3457   3927   -180   -297    100       O  
ATOM   6258  CB  ASN C 206      36.410 -33.023 -14.136  1.00 28.78           C  
ANISOU 6258  CB  ASN C 206     3587   3429   3916   -150   -302    158       C  
ATOM   6259  CG  ASN C 206      35.704 -33.387 -12.840  1.00 30.33           C  
ANISOU 6259  CG  ASN C 206     3766   3633   4125   -154   -326    202       C  
ATOM   6260  OD1 ASN C 206      35.270 -34.522 -12.663  1.00 31.80           O  
ANISOU 6260  OD1 ASN C 206     3952   3798   4331   -168   -351    213       O  
ATOM   6261  ND2 ASN C 206      35.605 -32.452 -11.936  1.00 28.51           N  
ANISOU 6261  ND2 ASN C 206     3518   3432   3882   -144   -318    226       N  
ATOM   6262  N   LYS C 207      38.165 -34.366 -16.914  1.00 28.34           N  
ANISOU 6262  N   LYS C 207     3577   3311   3878   -153   -275     45       N  
ATOM   6263  CA  LYS C 207      38.496 -34.084 -18.325  1.00 29.81           C  
ANISOU 6263  CA  LYS C 207     3781   3503   4039   -159   -255      4       C  
ATOM   6264  C   LYS C 207      38.323 -32.638 -18.733  1.00 30.12           C  
ANISOU 6264  C   LYS C 207     3820   3584   4037   -157   -236     13       C  
ATOM   6265  O   LYS C 207      37.850 -32.342 -19.836  1.00 30.92           O  
ANISOU 6265  O   LYS C 207     3935   3705   4107   -175   -232      2       O  
ATOM   6266  CB  LYS C 207      37.762 -35.016 -19.259  1.00 30.30           C  
ANISOU 6266  CB  LYS C 207     3862   3552   4095   -186   -270    -12       C  
ATOM   6267  CG  LYS C 207      38.309 -36.432 -19.140  1.00 32.03           C  
ANISOU 6267  CG  LYS C 207     4085   3722   4362   -185   -280    -38       C  
ATOM   6268  CD  LYS C 207      37.300 -37.436 -19.593  1.00 34.98           C  
ANISOU 6268  CD  LYS C 207     4471   4081   4737   -213   -306    -39       C  
ATOM   6269  CE  LYS C 207      35.960 -37.141 -18.945  1.00 41.37           C  
ANISOU 6269  CE  LYS C 207     5271   4917   5528   -228   -331     15       C  
ATOM   6270  NZ  LYS C 207      34.802 -37.589 -19.782  1.00 44.82           N  
ANISOU 6270  NZ  LYS C 207     5723   5361   5942   -261   -349     15       N  
ATOM   6271  N   LEU C 208      38.675 -31.722 -17.852  1.00 29.34           N  
ANISOU 6271  N   LEU C 208     3705   3502   3941   -138   -226     34       N  
ATOM   6272  CA  LEU C 208      38.577 -30.273 -18.222  1.00 30.89           C  
ANISOU 6272  CA  LEU C 208     3899   3734   4103   -134   -206     43       C  
ATOM   6273  C   LEU C 208      39.893 -29.765 -18.805  1.00 31.78           C  
ANISOU 6273  C   LEU C 208     4015   3845   4214   -119   -177      7       C  
ATOM   6274  O   LEU C 208      39.928 -28.762 -19.549  1.00 32.77           O  
ANISOU 6274  O   LEU C 208     4144   3996   4311   -121   -160      4       O  
ATOM   6275  CB  LEU C 208      38.162 -29.409 -17.028  1.00 29.91           C  
ANISOU 6275  CB  LEU C 208     3755   3631   3977   -124   -209     83       C  
ATOM   6276  CG  LEU C 208      36.771 -29.727 -16.461  1.00 31.30           C  
ANISOU 6276  CG  LEU C 208     3925   3817   4150   -139   -235    122       C  
ATOM   6277  CD1 LEU C 208      36.562 -29.143 -15.070  1.00 29.99           C  
ANISOU 6277  CD1 LEU C 208     3737   3666   3990   -127   -237    155       C  
ATOM   6278  CD2 LEU C 208      35.667 -29.202 -17.384  1.00 32.93           C  
ANISOU 6278  CD2 LEU C 208     4139   4051   4323   -159   -239    135       C  
ATOM   6279  N   ILE C 209      40.958 -30.490 -18.445  1.00 33.11           N  
ANISOU 6279  N   ILE C 209     4181   3983   4416   -104   -173    -14       N  
ATOM   6280  CA  ILE C 209      42.291 -30.356 -18.985  1.00 33.61           C  
ANISOU 6280  CA  ILE C 209     4247   4037   4486    -90   -147    -52       C  
ATOM   6281  C   ILE C 209      42.906 -31.769 -18.973  1.00 34.97           C  
ANISOU 6281  C   ILE C 209     4423   4166   4697    -86   -153    -80       C  
ATOM   6282  O   ILE C 209      42.636 -32.573 -18.075  1.00 40.69           O  
ANISOU 6282  O   ILE C 209     5139   4869   5451    -85   -175    -61       O  
ATOM   6283  CB  ILE C 209      43.101 -29.318 -18.180  1.00 34.23           C  
ANISOU 6283  CB  ILE C 209     4308   4126   4569    -67   -130    -40       C  
ATOM   6284  CG1 ILE C 209      44.472 -29.104 -18.818  1.00 34.21           C  
ANISOU 6284  CG1 ILE C 209     4308   4118   4571    -53   -103    -78       C  
ATOM   6285  CG2 ILE C 209      43.142 -29.688 -16.681  1.00 32.57           C  
ANISOU 6285  CG2 ILE C 209     4080   3903   4389    -56   -147    -13       C  
ATOM   6286  CD1 ILE C 209      45.234 -27.896 -18.286  1.00 38.35           C  
ANISOU 6286  CD1 ILE C 209     4817   4659   5093    -35    -84    -68       C  
ATOM   6287  N   SER C 210      43.702 -32.079 -19.980  1.00 34.12           N  
ANISOU 6287  N   SER C 210     4325   4046   4590    -85   -134   -124       N  
ATOM   6288  CA  SER C 210      44.288 -33.386 -20.104  1.00 34.46           C  
ANISOU 6288  CA  SER C 210     4372   4048   4672    -81   -137   -156       C  
ATOM   6289  C   SER C 210      45.766 -33.399 -19.633  1.00 35.70           C  
ANISOU 6289  C   SER C 210     4515   4185   4864    -53   -118   -172       C  
ATOM   6290  O   SER C 210      46.467 -32.361 -19.602  1.00 33.87           O  
ANISOU 6290  O   SER C 210     4276   3975   4618    -39    -97   -171       O  
ATOM   6291  CB  SER C 210      44.205 -33.783 -21.585  1.00 34.97           C  
ANISOU 6291  CB  SER C 210     4459   4113   4715    -99   -126   -200       C  
ATOM   6292  OG  SER C 210      45.407 -33.462 -22.271  1.00 34.43           O  
ANISOU 6292  OG  SER C 210     4390   4045   4643    -86    -94   -238       O  
ATOM   6293  N   ASP C 211      46.283 -34.574 -19.324  1.00 37.12           N  
ANISOU 6293  N   ASP C 211     4690   4322   5090    -45   -125   -186       N  
ATOM   6294  CA  ASP C 211      47.716 -34.680 -19.008  1.00 39.31           C  
ANISOU 6294  CA  ASP C 211     4952   4579   5403    -19   -107   -204       C  
ATOM   6295  C   ASP C 211      48.587 -34.190 -20.159  1.00 38.08           C  
ANISOU 6295  C   ASP C 211     4804   4435   5227    -13    -73   -248       C  
ATOM   6296  O   ASP C 211      49.612 -33.568 -19.895  1.00 36.24           O  
ANISOU 6296  O   ASP C 211     4558   4209   5000      5    -54   -249       O  
ATOM   6297  CB  ASP C 211      48.101 -36.116 -18.621  1.00 48.14           C  
ANISOU 6297  CB  ASP C 211     6063   5645   6580    -12   -120   -214       C  
ATOM   6298  CG  ASP C 211      47.575 -36.520 -17.229  1.00 57.59           C  
ANISOU 6298  CG  ASP C 211     7244   6831   7803    -12   -152   -164       C  
ATOM   6299  OD1 ASP C 211      48.011 -35.902 -16.229  1.00 61.99           O  
ANISOU 6299  OD1 ASP C 211     7783   7404   8366      1   -153   -133       O  
ATOM   6300  OD2 ASP C 211      46.731 -37.461 -17.124  1.00 67.11           O  
ANISOU 6300  OD2 ASP C 211     8456   8016   9026    -27   -178   -154       O  
ATOM   6301  N   ALA C 212      48.191 -34.459 -21.423  1.00 36.41           N  
ANISOU 6301  N   ALA C 212     4614   4229   4990    -32    -65   -283       N  
ATOM   6302  CA  ALA C 212      48.987 -34.019 -22.573  1.00 33.96           C  
ANISOU 6302  CA  ALA C 212     4311   3934   4656    -30    -32   -325       C  
ATOM   6303  C   ALA C 212      48.953 -32.464 -22.704  1.00 32.34           C  
ANISOU 6303  C   ALA C 212     4103   3778   4405    -30    -19   -303       C  
ATOM   6304  O   ALA C 212      49.989 -31.822 -22.915  1.00 31.41           O  
ANISOU 6304  O   ALA C 212     3977   3671   4284    -15      6   -316       O  
ATOM   6305  CB  ALA C 212      48.525 -34.696 -23.855  1.00 31.58           C  
ANISOU 6305  CB  ALA C 212     4032   3630   4336    -53    -28   -367       C  
ATOM   6306  N   GLU C 213      47.778 -31.866 -22.553  1.00 30.81           N  
ANISOU 6306  N   GLU C 213     3914   3611   4179    -47    -36   -267       N  
ATOM   6307  CA  GLU C 213      47.701 -30.417 -22.582  1.00 30.06           C  
ANISOU 6307  CA  GLU C 213     3814   3557   4048    -47    -26   -242       C  
ATOM   6308  C   GLU C 213      48.560 -29.792 -21.479  1.00 29.00           C  
ANISOU 6308  C   GLU C 213     3659   3421   3938    -21    -19   -222       C  
ATOM   6309  O   GLU C 213      49.175 -28.740 -21.694  1.00 30.46           O  
ANISOU 6309  O   GLU C 213     3838   3628   4105    -14      0   -222       O  
ATOM   6310  CB  GLU C 213      46.258 -29.958 -22.463  1.00 31.65           C  
ANISOU 6310  CB  GLU C 213     4021   3783   4220    -66    -48   -204       C  
ATOM   6311  CG  GLU C 213      45.421 -30.044 -23.728  1.00 34.96           C  
ANISOU 6311  CG  GLU C 213     4460   4223   4600    -95    -50   -218       C  
ATOM   6312  CD  GLU C 213      43.922 -30.237 -23.444  1.00 38.56           C  
ANISOU 6312  CD  GLU C 213     4920   4685   5043   -115    -80   -183       C  
ATOM   6313  OE1 GLU C 213      43.464 -30.201 -22.267  1.00 38.32           O  
ANISOU 6313  OE1 GLU C 213     4877   4648   5032   -107    -98   -147       O  
ATOM   6314  OE2 GLU C 213      43.183 -30.462 -24.425  1.00 43.01           O  
ANISOU 6314  OE2 GLU C 213     5499   5263   5578   -140    -85   -193       O  
ATOM   6315  N   LEU C 214      48.573 -30.385 -20.303  1.00 27.69           N  
ANISOU 6315  N   LEU C 214     3482   3230   3809    -11    -38   -202       N  
ATOM   6316  CA  LEU C 214      49.428 -29.893 -19.210  1.00 29.85           C  
ANISOU 6316  CA  LEU C 214     3734   3501   4104     10    -33   -183       C  
ATOM   6317  C   LEU C 214      50.904 -29.927 -19.625  1.00 29.58           C  
ANISOU 6317  C   LEU C 214     3693   3456   4089     28     -6   -217       C  
ATOM   6318  O   LEU C 214      51.595 -28.913 -19.553  1.00 27.85           O  
ANISOU 6318  O   LEU C 214     3464   3256   3858     38     10   -214       O  
ATOM   6319  CB  LEU C 214      49.181 -30.670 -17.892  1.00 29.96           C  
ANISOU 6319  CB  LEU C 214     3735   3491   4155     15    -60   -155       C  
ATOM   6320  CG  LEU C 214      50.057 -30.187 -16.717  1.00 32.04           C  
ANISOU 6320  CG  LEU C 214     3976   3756   4440     34    -58   -134       C  
ATOM   6321  CD1 LEU C 214      49.756 -28.704 -16.463  1.00 31.95           C  
ANISOU 6321  CD1 LEU C 214     3961   3784   4393     32    -50   -111       C  
ATOM   6322  CD2 LEU C 214      49.725 -31.008 -15.493  1.00 31.38           C  
ANISOU 6322  CD2 LEU C 214     3879   3653   4388     34    -86   -104       C  
ATOM   6323  N   GLU C 215      51.345 -31.080 -20.139  1.00 30.63           N  
ANISOU 6323  N   GLU C 215     3831   3558   4249     30     -2   -252       N  
ATOM   6324  CA  GLU C 215      52.683 -31.222 -20.627  1.00 34.15           C  
ANISOU 6324  CA  GLU C 215     4270   3992   4713     47     24   -288       C  
ATOM   6325  C   GLU C 215      53.023 -30.166 -21.651  1.00 32.27           C  
ANISOU 6325  C   GLU C 215     4039   3789   4433     42     51   -306       C  
ATOM   6326  O   GLU C 215      54.136 -29.667 -21.618  1.00 33.75           O  
ANISOU 6326  O   GLU C 215     4213   3981   4627     58     72   -314       O  
ATOM   6327  CB  GLU C 215      52.999 -32.636 -21.226  1.00 40.06           C  
ANISOU 6327  CB  GLU C 215     5024   4699   5494     48     27   -330       C  
ATOM   6328  CG  GLU C 215      52.698 -33.905 -20.374  1.00 48.93           C  
ANISOU 6328  CG  GLU C 215     6142   5780   6668     51      0   -317       C  
ATOM   6329  CD  GLU C 215      53.572 -34.102 -19.109  1.00 57.57           C  
ANISOU 6329  CD  GLU C 215     7209   6852   7810     74     -6   -292       C  
ATOM   6330  OE1 GLU C 215      53.485 -33.286 -18.151  1.00 62.35           O  
ANISOU 6330  OE1 GLU C 215     7803   7481   8406     77    -16   -252       O  
ATOM   6331  OE2 GLU C 215      54.315 -35.115 -19.042  1.00 62.56           O  
ANISOU 6331  OE2 GLU C 215     7832   7445   8494     88     -3   -312       O  
ATOM   6332  N   ALA C 216      52.106 -29.852 -22.566  1.00 30.01           N  
ANISOU 6332  N   ALA C 216     3770   3527   4102     20     50   -310       N  
ATOM   6333  CA  ALA C 216      52.406 -28.907 -23.611  1.00 31.61           C  
ANISOU 6333  CA  ALA C 216     3979   3766   4265     13     75   -325       C  
ATOM   6334  C   ALA C 216      52.459 -27.472 -23.000  1.00 32.34           C  
ANISOU 6334  C   ALA C 216     4060   3887   4341     19     77   -287       C  
ATOM   6335  O   ALA C 216      53.218 -26.580 -23.465  1.00 29.93           O  
ANISOU 6335  O   ALA C 216     3748   3603   4018     23    100   -294       O  
ATOM   6336  CB  ALA C 216      51.369 -29.008 -24.742  1.00 31.97           C  
ANISOU 6336  CB  ALA C 216     4046   3831   4268    -15     71   -337       C  
ATOM   6337  N   ILE C 217      51.682 -27.254 -21.928  1.00 31.48           N  
ANISOU 6337  N   ILE C 217     3945   3776   4238     18     53   -247       N  
ATOM   6338  CA  ILE C 217      51.687 -25.959 -21.260  1.00 30.73           C  
ANISOU 6338  CA  ILE C 217     3839   3704   4132     24     54   -213       C  
ATOM   6339  C   ILE C 217      53.055 -25.797 -20.561  1.00 30.91           C  
ANISOU 6339  C   ILE C 217     3842   3715   4185     47     67   -218       C  
ATOM   6340  O   ILE C 217      53.601 -24.686 -20.474  1.00 29.86           O  
ANISOU 6340  O   ILE C 217     3701   3602   4042     53     81   -209       O  
ATOM   6341  CB  ILE C 217      50.491 -25.813 -20.285  1.00 29.56           C  
ANISOU 6341  CB  ILE C 217     3688   3558   3981     17     27   -173       C  
ATOM   6342  CG1 ILE C 217      49.229 -25.347 -21.082  1.00 29.99           C  
ANISOU 6342  CG1 ILE C 217     3758   3640   3997     -5     20   -161       C  
ATOM   6343  CG2 ILE C 217      50.820 -24.878 -19.126  1.00 29.88           C  
ANISOU 6343  CG2 ILE C 217     3713   3608   4032     30     27   -145       C  
ATOM   6344  CD1 ILE C 217      47.891 -25.517 -20.378  1.00 28.79           C  
ANISOU 6344  CD1 ILE C 217     3607   3488   3842    -15     -6   -127       C  
ATOM   6345  N   PHE C 218      53.569 -26.920 -20.086  1.00 31.82           N  
ANISOU 6345  N   PHE C 218     3951   3797   4340     58     61   -230       N  
ATOM   6346  CA  PHE C 218      54.858 -26.985 -19.379  1.00 34.83           C  
ANISOU 6346  CA  PHE C 218     4313   4164   4756     80     70   -233       C  
ATOM   6347  C   PHE C 218      55.947 -26.604 -20.358  1.00 34.64           C  
ANISOU 6347  C   PHE C 218     4287   4149   4723     87    101   -264       C  
ATOM   6348  O   PHE C 218      56.889 -25.931 -19.977  1.00 33.04           O  
ANISOU 6348  O   PHE C 218     4068   3954   4529     99    113   -259       O  
ATOM   6349  CB  PHE C 218      55.154 -28.405 -18.878  1.00 35.17           C  
ANISOU 6349  CB  PHE C 218     4349   4166   4846     89     57   -241       C  
ATOM   6350  CG  PHE C 218      54.571 -28.734 -17.518  1.00 38.81           C  
ANISOU 6350  CG  PHE C 218     4801   4617   5327     89     27   -203       C  
ATOM   6351  CD1 PHE C 218      53.615 -27.934 -16.925  1.00 39.30           C  
ANISOU 6351  CD1 PHE C 218     4864   4703   5362     78     13   -169       C  
ATOM   6352  CD2 PHE C 218      54.968 -29.894 -16.852  1.00 40.86           C  
ANISOU 6352  CD2 PHE C 218     5048   4841   5634     99     13   -201       C  
ATOM   6353  CE1 PHE C 218      53.104 -28.262 -15.673  1.00 41.84           C  
ANISOU 6353  CE1 PHE C 218     5176   5019   5700     77    -12   -135       C  
ATOM   6354  CE2 PHE C 218      54.476 -30.227 -15.597  1.00 40.83           C  
ANISOU 6354  CE2 PHE C 218     5034   4831   5648     97    -13   -164       C  
ATOM   6355  CZ  PHE C 218      53.524 -29.425 -15.016  1.00 42.16           C  
ANISOU 6355  CZ  PHE C 218     5204   5027   5785     86    -27   -132       C  
ATOM   6356  N   ASP C 219      55.814 -27.045 -21.618  1.00 35.69           N  
ANISOU 6356  N   ASP C 219     4435   4284   4840     77    114   -298       N  
ATOM   6357  CA  ASP C 219      56.842 -26.761 -22.634  1.00 35.84           C  
ANISOU 6357  CA  ASP C 219     4452   4315   4848     81    145   -332       C  
ATOM   6358  C   ASP C 219      56.845 -25.272 -22.910  1.00 33.18           C  
ANISOU 6358  C   ASP C 219     4114   4018   4474     74    156   -313       C  
ATOM   6359  O   ASP C 219      57.889 -24.652 -22.959  1.00 32.42           O  
ANISOU 6359  O   ASP C 219     4005   3931   4382     85    176   -317       O  
ATOM   6360  CB  ASP C 219      56.603 -27.536 -23.924  1.00 41.56           C  
ANISOU 6360  CB  ASP C 219     5195   5038   5558     68    156   -373       C  
ATOM   6361  CG  ASP C 219      56.779 -29.056 -23.739  1.00 54.05           C  
ANISOU 6361  CG  ASP C 219     6776   6576   7184     77    150   -399       C  
ATOM   6362  OD1 ASP C 219      57.451 -29.465 -22.751  1.00 55.80           O  
ANISOU 6362  OD1 ASP C 219     6980   6770   7452     97    144   -388       O  
ATOM   6363  OD2 ASP C 219      56.239 -29.845 -24.576  1.00 58.51           O  
ANISOU 6363  OD2 ASP C 219     7358   7133   7739     63    150   -428       O  
ATOM   6364  N   ARG C 220      55.658 -24.704 -23.013  1.00 30.84           N  
ANISOU 6364  N   ARG C 220     3830   3742   4146     57    142   -289       N  
ATOM   6365  CA  ARG C 220      55.477 -23.273 -23.250  1.00 30.54           C  
ANISOU 6365  CA  ARG C 220     3790   3737   4075     49    149   -266       C  
ATOM   6366  C   ARG C 220      56.007 -22.440 -22.133  1.00 28.04           C  
ANISOU 6366  C   ARG C 220     3455   3420   3777     63    148   -240       C  
ATOM   6367  O   ARG C 220      56.644 -21.421 -22.330  1.00 28.24           O  
ANISOU 6367  O   ARG C 220     3472   3464   3792     66    164   -235       O  
ATOM   6368  CB  ARG C 220      54.011 -22.985 -23.384  1.00 31.59           C  
ANISOU 6368  CB  ARG C 220     3936   3885   4181     29    130   -241       C  
ATOM   6369  CG  ARG C 220      53.682 -21.936 -24.399  1.00 32.09           C  
ANISOU 6369  CG  ARG C 220     4005   3985   4203     13    141   -233       C  
ATOM   6370  CD  ARG C 220      52.176 -21.731 -24.505  1.00 32.21           C  
ANISOU 6370  CD  ARG C 220     4030   4012   4194     -6    120   -206       C  
ATOM   6371  NE  ARG C 220      52.079 -20.439 -25.144  1.00 33.31           N  
ANISOU 6371  NE  ARG C 220     4166   4184   4304    -16    131   -188       N  
ATOM   6372  CZ  ARG C 220      50.989 -19.733 -25.339  1.00 32.58           C  
ANISOU 6372  CZ  ARG C 220     4077   4111   4189    -31    120   -157       C  
ATOM   6373  NH1 ARG C 220      49.795 -20.113 -24.923  1.00 30.18           N  
ANISOU 6373  NH1 ARG C 220     3780   3801   3886    -38     96   -138       N  
ATOM   6374  NH2 ARG C 220      51.146 -18.593 -25.942  1.00 33.31           N  
ANISOU 6374  NH2 ARG C 220     4164   4229   4261    -37    132   -142       N  
ATOM   6375  N   THR C 221      55.751 -22.870 -20.929  1.00 27.50           N  
ANISOU 6375  N   THR C 221     3381   3332   3735     71    128   -222       N  
ATOM   6376  CA  THR C 221      56.371 -22.180 -19.789  1.00 25.58           C  
ANISOU 6376  CA  THR C 221     3119   3088   3509     84    126   -200       C  
ATOM   6377  C   THR C 221      57.895 -22.146 -19.866  1.00 25.55           C  
ANISOU 6377  C   THR C 221     3100   3079   3525     99    147   -219       C  
ATOM   6378  O   THR C 221      58.482 -21.074 -19.827  1.00 26.04           O  
ANISOU 6378  O   THR C 221     3154   3159   3580    102    160   -212       O  
ATOM   6379  CB  THR C 221      55.931 -22.838 -18.494  1.00 25.83           C  
ANISOU 6379  CB  THR C 221     3146   3101   3567     88    101   -180       C  
ATOM   6380  OG1 THR C 221      54.489 -22.827 -18.452  1.00 26.00           O  
ANISOU 6380  OG1 THR C 221     3180   3129   3569     73     83   -162       O  
ATOM   6381  CG2 THR C 221      56.482 -22.090 -17.319  1.00 25.45           C  
ANISOU 6381  CG2 THR C 221     3079   3057   3532     98     99   -159       C  
ATOM   6382  N   VAL C 222      58.556 -23.293 -19.976  1.00 25.94           N  
ANISOU 6382  N   VAL C 222     3146   3105   3604    110    151   -244       N  
ATOM   6383  CA  VAL C 222      59.970 -23.306 -20.264  1.00 26.91           C  
ANISOU 6383  CA  VAL C 222     3255   3225   3744    124    174   -265       C  
ATOM   6384  C   VAL C 222      60.412 -22.405 -21.436  1.00 29.11           C  
ANISOU 6384  C   VAL C 222     3537   3532   3991    118    201   -280       C  
ATOM   6385  O   VAL C 222      61.448 -21.753 -21.316  1.00 29.82           O  
ANISOU 6385  O   VAL C 222     3611   3631   4087    127    216   -279       O  
ATOM   6386  CB  VAL C 222      60.438 -24.739 -20.605  1.00 27.87           C  
ANISOU 6386  CB  VAL C 222     3375   3315   3896    134    179   -297       C  
ATOM   6387  CG1 VAL C 222      61.976 -24.790 -20.667  1.00 27.18           C  
ANISOU 6387  CG1 VAL C 222     3268   3222   3836    153    201   -314       C  
ATOM   6388  CG2 VAL C 222      59.875 -25.700 -19.586  1.00 26.89           C  
ANISOU 6388  CG2 VAL C 222     3249   3163   3803    137    151   -280       C  
ATOM   6389  N   ASN C 223      59.660 -22.352 -22.563  1.00 28.41           N  
ANISOU 6389  N   ASN C 223     3466   3460   3866    101    206   -292       N  
ATOM   6390  CA  ASN C 223      60.171 -21.581 -23.709  1.00 29.60           C  
ANISOU 6390  CA  ASN C 223     3617   3640   3987     94    232   -306       C  
ATOM   6391  C   ASN C 223      59.583 -20.190 -23.961  1.00 28.47           C  
ANISOU 6391  C   ASN C 223     3477   3528   3809     79    230   -277       C  
ATOM   6392  O   ASN C 223      59.617 -19.703 -25.103  1.00 28.30           O  
ANISOU 6392  O   ASN C 223     3462   3534   3757     66    246   -286       O  
ATOM   6393  CB  ASN C 223      60.052 -22.403 -24.972  1.00 29.66           C  
ANISOU 6393  CB  ASN C 223     3639   3651   3978     84    245   -343       C  
ATOM   6394  CG  ASN C 223      60.775 -23.726 -24.839  1.00 33.65           C  
ANISOU 6394  CG  ASN C 223     4139   4124   4523    101    251   -376       C  
ATOM   6395  OD1 ASN C 223      60.193 -24.793 -25.052  1.00 34.03           O  
ANISOU 6395  OD1 ASN C 223     4199   4152   4578     96    242   -395       O  
ATOM   6396  ND2 ASN C 223      62.024 -23.670 -24.382  1.00 34.67           N  
ANISOU 6396  ND2 ASN C 223     4247   4243   4682    121    264   -380       N  
ATOM   6397  N   THR C 224      58.973 -19.604 -22.934  1.00 25.96           N  
ANISOU 6397  N   THR C 224     3157   3207   3497     79    211   -244       N  
ATOM   6398  CA  THR C 224      58.192 -18.381 -23.155  1.00 25.32           C  
ANISOU 6398  CA  THR C 224     3080   3151   3388     65    207   -216       C  
ATOM   6399  C   THR C 224      59.066 -17.203 -23.590  1.00 26.44           C  
ANISOU 6399  C   THR C 224     3210   3313   3520     64    228   -211       C  
ATOM   6400  O   THR C 224      58.752 -16.529 -24.598  1.00 26.19           O  
ANISOU 6400  O   THR C 224     3184   3307   3457     49    237   -205       O  
ATOM   6401  CB  THR C 224      57.277 -18.072 -21.973  1.00 24.89           C  
ANISOU 6401  CB  THR C 224     3025   3087   3343     65    184   -185       C  
ATOM   6402  OG1 THR C 224      56.217 -19.044 -21.966  1.00 23.02           O  
ANISOU 6402  OG1 THR C 224     2803   2840   3104     58    166   -186       O  
ATOM   6403  CG2 THR C 224      56.719 -16.632 -22.044  1.00 24.25           C  
ANISOU 6403  CG2 THR C 224     2943   3027   3243     55    184   -155       C  
ATOM   6404  N   ALA C 225      60.204 -17.038 -22.923  1.00 26.50           N  
ANISOU 6404  N   ALA C 225     3202   3312   3554     80    236   -214       N  
ATOM   6405  CA  ALA C 225      61.155 -16.023 -23.293  1.00 28.44           C  
ANISOU 6405  CA  ALA C 225     3434   3575   3794     80    256   -211       C  
ATOM   6406  C   ALA C 225      61.529 -16.145 -24.777  1.00 29.96           C  
ANISOU 6406  C   ALA C 225     3632   3790   3961     71    277   -233       C  
ATOM   6407  O   ALA C 225      61.493 -15.142 -25.511  1.00 31.15           O  
ANISOU 6407  O   ALA C 225     3781   3967   4086     58    287   -220       O  
ATOM   6408  CB  ALA C 225      62.414 -16.097 -22.409  1.00 29.89           C  
ANISOU 6408  CB  ALA C 225     3599   3744   4011     98    261   -215       C  
ATOM   6409  N   LEU C 226      61.870 -17.354 -25.217  1.00 30.02           N  
ANISOU 6409  N   LEU C 226     3643   3787   3973     76    286   -267       N  
ATOM   6410  CA  LEU C 226      62.231 -17.567 -26.588  1.00 31.48           C  
ANISOU 6410  CA  LEU C 226     3831   3994   4132     67    308   -293       C  
ATOM   6411  C   LEU C 226      61.060 -17.339 -27.543  1.00 31.79           C  
ANISOU 6411  C   LEU C 226     3889   4058   4130     42    302   -286       C  
ATOM   6412  O   LEU C 226      61.255 -16.859 -28.644  1.00 35.01           O  
ANISOU 6412  O   LEU C 226     4296   4497   4506     28    318   -290       O  
ATOM   6413  CB  LEU C 226      62.772 -18.994 -26.771  1.00 35.66           C  
ANISOU 6413  CB  LEU C 226     4363   4504   4682     79    317   -335       C  
ATOM   6414  CG  LEU C 226      62.760 -19.417 -28.237  1.00 36.87           C  
ANISOU 6414  CG  LEU C 226     4526   4680   4802     64    337   -368       C  
ATOM   6415  CD1 LEU C 226      64.076 -18.984 -28.898  1.00 40.08           C  
ANISOU 6415  CD1 LEU C 226     4916   5108   5204     69    368   -383       C  
ATOM   6416  CD2 LEU C 226      62.616 -20.920 -28.321  1.00 42.34           C  
ANISOU 6416  CD2 LEU C 226     5229   5346   5513     71    336   -404       C  
ATOM   6417  N   GLU C 227      59.846 -17.686 -27.133  1.00 31.69           N  
ANISOU 6417  N   GLU C 227     3890   4034   4117     36    278   -273       N  
ATOM   6418  CA  GLU C 227      58.656 -17.514 -27.985  1.00 31.11           C  
ANISOU 6418  CA  GLU C 227     3832   3983   4005     12    269   -262       C  
ATOM   6419  C   GLU C 227      58.299 -16.010 -28.163  1.00 30.08           C  
ANISOU 6419  C   GLU C 227     3694   3877   3855      0    267   -222       C  
ATOM   6420  O   GLU C 227      57.935 -15.530 -29.276  1.00 29.49           O  
ANISOU 6420  O   GLU C 227     3625   3836   3744    -21    273   -215       O  
ATOM   6421  CB  GLU C 227      57.520 -18.276 -27.364  1.00 32.11           C  
ANISOU 6421  CB  GLU C 227     3971   4087   4141     11    244   -256       C  
ATOM   6422  CG  GLU C 227      56.109 -17.951 -27.854  1.00 35.96           C  
ANISOU 6422  CG  GLU C 227     4471   4593   4597    -11    227   -232       C  
ATOM   6423  CD  GLU C 227      54.977 -18.619 -26.999  1.00 38.65           C  
ANISOU 6423  CD  GLU C 227     4822   4911   4952    -10    199   -220       C  
ATOM   6424  OE1 GLU C 227      55.198 -18.998 -25.812  1.00 42.80           O  
ANISOU 6424  OE1 GLU C 227     5342   5407   5513      7    190   -218       O  
ATOM   6425  OE2 GLU C 227      53.828 -18.736 -27.509  1.00 38.92           O  
ANISOU 6425  OE2 GLU C 227     4868   4957   4961    -30    186   -209       O  
ATOM   6426  N   ILE C 228      58.470 -15.258 -27.104  1.00 28.27           N  
ANISOU 6426  N   ILE C 228     3455   3635   3651     13    260   -198       N  
ATOM   6427  CA  ILE C 228      58.301 -13.792 -27.167  1.00 29.04           C  
ANISOU 6427  CA  ILE C 228     3543   3749   3740      5    261   -162       C  
ATOM   6428  C   ILE C 228      59.338 -13.191 -28.135  1.00 30.23           C  
ANISOU 6428  C   ILE C 228     3684   3927   3874     -1    285   -168       C  
ATOM   6429  O   ILE C 228      58.930 -12.573 -29.101  1.00 32.26           O  
ANISOU 6429  O   ILE C 228     3942   4213   4102    -20    288   -152       O  
ATOM   6430  CB  ILE C 228      58.308 -13.129 -25.775  1.00 27.87           C  
ANISOU 6430  CB  ILE C 228     3385   3580   3624     19    250   -139       C  
ATOM   6431  CG1 ILE C 228      57.025 -13.519 -25.011  1.00 26.53           C  
ANISOU 6431  CG1 ILE C 228     3225   3393   3460     19    225   -126       C  
ATOM   6432  CG2 ILE C 228      58.379 -11.593 -25.892  1.00 25.73           C  
ANISOU 6432  CG2 ILE C 228     3102   3323   3349     12    255   -108       C  
ATOM   6433  CD1 ILE C 228      57.148 -13.399 -23.495  1.00 27.14           C  
ANISOU 6433  CD1 ILE C 228     3294   3446   3570     35    215   -117       C  
ATOM   6434  N   VAL C 229      60.636 -13.464 -27.938  1.00 31.08           N  
ANISOU 6434  N   VAL C 229     3780   4027   4000     14    302   -191       N  
ATOM   6435  CA  VAL C 229      61.686 -12.927 -28.817  1.00 30.81           C  
ANISOU 6435  CA  VAL C 229     3734   4019   3952      8    326   -198       C  
ATOM   6436  C   VAL C 229      61.478 -13.342 -30.289  1.00 31.94           C  
ANISOU 6436  C   VAL C 229     3886   4195   4053    -11    339   -216       C  
ATOM   6437  O   VAL C 229      61.702 -12.557 -31.186  1.00 31.04           O  
ANISOU 6437  O   VAL C 229     3766   4113   3913    -27    350   -203       O  
ATOM   6438  CB  VAL C 229      63.096 -13.355 -28.402  1.00 31.28           C  
ANISOU 6438  CB  VAL C 229     3780   4066   4039     29    343   -223       C  
ATOM   6439  CG1 VAL C 229      64.086 -12.924 -29.459  1.00 29.69           C  
ANISOU 6439  CG1 VAL C 229     3566   3895   3817     21    369   -233       C  
ATOM   6440  CG2 VAL C 229      63.519 -12.785 -27.047  1.00 29.74           C  
ANISOU 6440  CG2 VAL C 229     3572   3846   3880     45    334   -204       C  
ATOM   6441  N   ASN C 230      61.079 -14.577 -30.533  1.00 33.28           N  
ANISOU 6441  N   ASN C 230     4071   4356   4217    -12    336   -247       N  
ATOM   6442  CA  ASN C 230      60.715 -14.981 -31.872  1.00 35.39           C  
ANISOU 6442  CA  ASN C 230     4348   4655   4441    -35    345   -265       C  
ATOM   6443  C   ASN C 230      59.578 -14.185 -32.504  1.00 36.60           C  
ANISOU 6443  C   ASN C 230     4508   4837   4560    -61    331   -228       C  
ATOM   6444  O   ASN C 230      59.395 -14.246 -33.702  1.00 34.73           O  
ANISOU 6444  O   ASN C 230     4277   4636   4283    -84    339   -236       O  
ATOM   6445  CB  ASN C 230      60.343 -16.472 -31.891  1.00 37.98           C  
ANISOU 6445  CB  ASN C 230     4692   4962   4773    -32    340   -303       C  
ATOM   6446  CG  ASN C 230      61.556 -17.371 -31.707  1.00 40.03           C  
ANISOU 6446  CG  ASN C 230     4945   5203   5061    -10    361   -346       C  
ATOM   6447  OD1 ASN C 230      62.678 -16.919 -31.889  1.00 43.07           O  
ANISOU 6447  OD1 ASN C 230     5313   5599   5450     -2    382   -351       O  
ATOM   6448  ND2 ASN C 230      61.342 -18.641 -31.361  1.00 39.98           N  
ANISOU 6448  ND2 ASN C 230     4948   5165   5075      0    354   -375       N  
ATOM   6449  N   LEU C 231      58.782 -13.465 -31.717  1.00 35.00           N  
ANISOU 6449  N   LEU C 231     4304   4619   4372    -59    309   -189       N  
ATOM   6450  CA  LEU C 231      57.705 -12.690 -32.313  1.00 33.69           C  
ANISOU 6450  CA  LEU C 231     4141   4479   4178    -83    296   -151       C  
ATOM   6451  C   LEU C 231      58.128 -11.218 -32.494  1.00 34.10           C  
ANISOU 6451  C   LEU C 231     4175   4548   4230    -88    303   -114       C  
ATOM   6452  O   LEU C 231      57.272 -10.337 -32.602  1.00 36.61           O  
ANISOU 6452  O   LEU C 231     4490   4876   4542   -101    289    -73       O  
ATOM   6453  CB  LEU C 231      56.441 -12.801 -31.434  1.00 33.79           C  
ANISOU 6453  CB  LEU C 231     4163   4466   4207    -79    269   -129       C  
ATOM   6454  CG  LEU C 231      55.722 -14.155 -31.444  1.00 32.86           C  
ANISOU 6454  CG  LEU C 231     4063   4336   4083    -82    257   -155       C  
ATOM   6455  CD1 LEU C 231      54.898 -14.382 -30.181  1.00 32.59           C  
ANISOU 6455  CD1 LEU C 231     4034   4268   4079    -69    234   -140       C  
A