CNRS Nantes University UFIP UFIP
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***  4m8  ***

elNémo ID: 22092722260083457

Job options:

ID        	=	 22092722260083457
JOBID     	=	 4m8
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4m8

ATOM      1  N   LYS A 554      33.795 162.960-218.133  1.00201.45           N  
ANISOU    1  N   LYS A 554    21843  21502  33198   8967   3861  -7570       N  
ATOM      2  CA  LYS A 554      33.423 162.305-216.886  1.00199.04           C  
ANISOU    2  CA  LYS A 554    21553  20750  33324   8696   3132  -7480       C  
ATOM      3  C   LYS A 554      33.439 163.288-215.722  1.00196.21           C  
ANISOU    3  C   LYS A 554    20898  20414  33239   8310   2904  -7076       C  
ATOM      4  O   LYS A 554      32.881 163.016-214.661  1.00190.93           O  
ANISOU    4  O   LYS A 554    20306  19459  32780   8044   2326  -6923       O  
ATOM      5  CB  LYS A 554      34.353 161.134-216.605  1.00204.35           C  
ANISOU    5  CB  LYS A 554    21992  21120  34530   8932   2921  -7652       C  
ATOM      6  N   GLN A 555      34.079 164.434-215.930  1.00201.23           N  
ANISOU    6  N   GLN A 555    21186  21394  33879   8284   3367  -6900       N  
ATOM      7  CA  GLN A 555      34.210 165.442-214.882  1.00202.24           C  
ANISOU    7  CA  GLN A 555    20978  21551  34311   7919   3189  -6556       C  
ATOM      8  C   GLN A 555      32.887 166.150-214.586  1.00198.22           C  
ANISOU    8  C   GLN A 555    20811  21075  33428   7584   3008  -6379       C  
ATOM      9  O   GLN A 555      32.656 166.606-213.466  1.00193.38           O  
ANISOU    9  O   GLN A 555    20067  20352  33058   7264   2617  -6139       O  
ATOM     10  CB  GLN A 555      35.288 166.453-215.253  1.00205.89           C  
ANISOU   10  CB  GLN A 555    20939  22342  34946   7963   3752  -6430       C  
ATOM     11  N   MET A 556      32.022 166.236-215.593  1.00201.02           N  
ANISOU   11  N   MET A 556    21604  21596  33179   7679   3285  -6510       N  
ATOM     12  CA  MET A 556      30.734 166.909-215.443  1.00198.54           C  
ANISOU   12  CA  MET A 556    21628  21334  32474   7391   3154  -6365       C  
ATOM     13  C   MET A 556      29.765 166.091-214.593  1.00197.49           C  
ANISOU   13  C   MET A 556    21813  20826  32399   7198   2462  -6373       C  
ATOM     14  O   MET A 556      28.862 166.642-213.953  1.00190.04           O  
ANISOU   14  O   MET A 556    21012  19848  31345   6887   2190  -6169       O  
ATOM     15  CB  MET A 556      30.128 167.202-216.809  1.00199.90           C  
ANISOU   15  CB  MET A 556    22171  21816  31966   7583   3648  -6516       C  
ATOM     16  N   SER A 557      29.961 164.776-214.595  1.00205.65           N  
ANISOU   16  N   SER A 557    22940  21574  33623   7388   2192  -6594       N  
ATOM     17  CA  SER A 557      29.107 163.861-213.844  1.00205.61           C  
ANISOU   17  CA  SER A 557    23209  21187  33726   7230   1557  -6582       C  
ATOM     18  C   SER A 557      29.135 164.170-212.349  1.00203.73           C  
ANISOU   18  C   SER A 557    22733  20801  33875   6940   1095  -6229       C  
ATOM     19  O   SER A 557      28.117 164.055-211.663  1.00200.37           O  
ANISOU   19  O   SER A 557    22553  20205  33373   6701    668  -6071       O  
ATOM     20  CB  SER A 557      29.521 162.415-214.101  1.00209.73           C  
ANISOU   20  CB  SER A 557    23780  21414  34492   7502   1394  -6863       C  
ATOM     21  N   LYS A 558      30.304 164.565-211.855  1.00204.76           N  
ANISOU   21  N   LYS A 558    22376  21012  34410   6973   1181  -6111       N  
ATOM     22  CA  LYS A 558      30.468 164.925-210.453  1.00199.64           C  
ANISOU   22  CA  LYS A 558    21463  20278  34114   6737    755  -5809       C  
ATOM     23  C   LYS A 558      29.583 166.113-210.096  1.00190.59           C  
ANISOU   23  C   LYS A 558    20425  19305  32685   6418    742  -5586       C  
ATOM     24  O   LYS A 558      28.773 166.039-209.170  1.00185.73           O  
ANISOU   24  O   LYS A 558    19981  18542  32047   6210    276  -5393       O  
ATOM     25  CB  LYS A 558      31.927 165.241-210.154  1.00204.05           C  
ANISOU   25  CB  LYS A 558    21453  20936  35140   6835    900  -5779       C  
ATOM     26  N   LYS A 559      29.741 167.201-210.843  1.00188.13           N  
ANISOU   26  N   LYS A 559    20009  19308  32165   6394   1273  -5598       N  
ATOM     27  CA  LYS A 559      28.959 168.412-210.626  1.00181.07           C  
ANISOU   27  CA  LYS A 559    19192  18586  31020   6106   1335  -5401       C  
ATOM     28  C   LYS A 559      27.466 168.136-210.746  1.00177.07           C  
ANISOU   28  C   LYS A 559    19230  17984  30064   5994   1109  -5408       C  
ATOM     29  O   LYS A 559      26.673 168.650-209.960  1.00170.48           O  
ANISOU   29  O   LYS A 559    18495  17124  29155   5731    815  -5201       O  
ATOM     30  CB  LYS A 559      29.378 169.498-211.605  1.00180.97           C  
ANISOU   30  CB  LYS A 559    19002  18908  30852   6143   2013  -5408       C  
ATOM     31  N   MET A 560      27.090 167.319-211.727  1.00181.15           N  
ANISOU   31  N   MET A 560    20088  18450  30290   6197   1233  -5662       N  
ATOM     32  CA  MET A 560      25.685 166.973-211.935  1.00176.90           C  
ANISOU   32  CA  MET A 560    20056  17807  29352   6092   1004  -5713       C  
ATOM     33  C   MET A 560      25.114 166.232-210.730  1.00172.41           C  
ANISOU   33  C   MET A 560    19591  16897  29019   5918    346  -5538       C  
ATOM     34  O   MET A 560      24.062 166.602-210.200  1.00168.56           O  
ANISOU   34  O   MET A 560    19315  16379  28350   5670     90  -5353       O  
ATOM     35  CB  MET A 560      25.523 166.143-213.199  1.00180.07           C  
ANISOU   35  CB  MET A 560    20758  18205  29456   6363   1219  -6071       C  
ATOM     36  N   ASN A 561      25.824 165.193-210.298  1.00171.73           N  
ANISOU   36  N   ASN A 561    19347  16563  29341   6064     95  -5574       N  
ATOM     37  CA  ASN A 561      25.411 164.395-209.149  1.00167.73           C  
ANISOU   37  CA  ASN A 561    18907  15728  29093   5949   -497  -5363       C  
ATOM     38  C   ASN A 561      25.293 165.239-207.880  1.00162.06           C  
ANISOU   38  C   ASN A 561    18012  15090  28475   5715   -763  -5006       C  
ATOM     39  O   ASN A 561      24.295 165.154-207.159  1.00157.33           O  
ANISOU   39  O   ASN A 561    17638  14364  27775   5522  -1130  -4781       O  
ATOM     40  CB  ASN A 561      26.379 163.237-208.934  1.00171.90           C  
ANISOU   40  CB  ASN A 561    19235  16007  30073   6183   -659  -5448       C  
ATOM     41  N   ASP A 562      26.312 166.053-207.616  1.00161.46           N  
ANISOU   41  N   ASP A 562    17519  15225  28605   5735   -578  -4961       N  
ATOM     42  CA  ASP A 562      26.311 166.933-206.451  1.00156.39           C  
ANISOU   42  CA  ASP A 562    16665  14691  28065   5534   -824  -4685       C  
ATOM     43  C   ASP A 562      25.131 167.892-206.497  1.00151.37           C  
ANISOU   43  C   ASP A 562    16287  14200  27025   5287   -763  -4576       C  
ATOM     44  O   ASP A 562      24.441 168.094-205.495  1.00148.50           O  
ANISOU   44  O   ASP A 562    16018  13794  26610   5117  -1146  -4332       O  
ATOM     45  CB  ASP A 562      27.612 167.730-206.379  1.00159.20           C  
ANISOU   45  CB  ASP A 562    16505  15259  28724   5580   -572  -4724       C  
ATOM     46  CG  ASP A 562      28.817 166.856-206.114  1.00167.39           C  
ANISOU   46  CG  ASP A 562    17236  16158  30206   5810   -704  -4797       C  
ATOM     47  OD1 ASP A 562      28.754 165.646-206.421  1.00171.70           O  
ANISOU   47  OD1 ASP A 562    17978  16468  30793   5987   -808  -4899       O  
ATOM     48  OD2 ASP A 562      29.827 167.383-205.600  1.00169.42           O1-
ANISOU   48  OD2 ASP A 562    17045  16533  30795   5811   -715  -4764       O1-
ATOM     49  N   GLN A 563      24.910 168.479-207.669  1.00152.82           N  
ANISOU   49  N   GLN A 563    16587  14570  26909   5295   -271  -4748       N  
ATOM     50  CA  GLN A 563      23.807 169.410-207.872  1.00152.17           C  
ANISOU   50  CA  GLN A 563    16754  14635  26430   5085   -157  -4668       C  
ATOM     51  C   GLN A 563      22.469 168.764-207.553  1.00151.84           C  
ANISOU   51  C   GLN A 563    17152  14386  26153   4968   -560  -4576       C  
ATOM     52  O   GLN A 563      21.704 169.274-206.731  1.00147.60           O  
ANISOU   52  O   GLN A 563    16702  13857  25522   4760   -825  -4345       O  
ATOM     53  CB  GLN A 563      23.805 169.943-209.305  1.00155.17           C  
ANISOU   53  CB  GLN A 563    17223  15243  26492   5181    448  -4871       C  
ATOM     54  CG  GLN A 563      24.694 171.161-209.509  1.00157.71           C  
ANISOU   54  CG  GLN A 563    17131  15826  26964   5154    905  -4818       C  
ATOM     55  CD  GLN A 563      24.668 171.667-210.937  1.00160.27           C  
ANISOU   55  CD  GLN A 563    17559  16399  26938   5281   1541  -4953       C  
ATOM     56  OE1 GLN A 563      24.918 170.914-211.879  1.00164.98           O  
ANISOU   56  OE1 GLN A 563    18293  17009  27384   5544   1753  -5182       O  
ATOM     57  NE2 GLN A 563      24.357 172.948-211.106  1.00157.09           N  
ANISOU   57  NE2 GLN A 563    17094  16202  26392   5112   1854  -4803       N  
ATOM     58  N   LEU A 564      22.195 167.636-208.198  1.00156.93           N  
ANISOU   58  N   LEU A 564    18059  14842  26728   5101   -607  -4759       N  
ATOM     59  CA  LEU A 564      20.939 166.928-207.982  1.00157.90           C  
ANISOU   59  CA  LEU A 564    18571  14731  26693   4974   -976  -4681       C  
ATOM     60  C   LEU A 564      20.778 166.503-206.526  1.00159.12           C  
ANISOU   60  C   LEU A 564    18660  14672  27124   4866  -1497  -4336       C  
ATOM     61  O   LEU A 564      19.665 166.465-206.003  1.00155.18           O  
ANISOU   61  O   LEU A 564    18408  14073  26481   4677  -1780  -4122       O  
ATOM     62  CB  LEU A 564      20.845 165.712-208.902  1.00161.80           C  
ANISOU   62  CB  LEU A 564    19280  15027  27168   5147   -956  -4975       C  
ATOM     63  CG  LEU A 564      20.906 166.029-210.396  1.00163.28           C  
ANISOU   63  CG  LEU A 564    19594  15455  26990   5305   -463  -5330       C  
ATOM     64  CD1 LEU A 564      20.710 164.765-211.220  1.00168.55           C  
ANISOU   64  CD1 LEU A 564    20494  15915  27633   5473   -527  -5651       C  
ATOM     65  CD2 LEU A 564      19.877 167.085-210.760  1.00157.93           C  
ANISOU   65  CD2 LEU A 564    19148  15015  25846   5128   -312  -5287       C  
ATOM     66  N   GLU A 565      21.898 166.191-205.879  1.00163.70           N  
ANISOU   66  N   GLU A 565    18904  15203  28090   5004  -1614  -4269       N  
ATOM     67  CA  GLU A 565      21.903 165.821-204.468  1.00163.35           C  
ANISOU   67  CA  GLU A 565    18769  15013  28284   4964  -2095  -3925       C  
ATOM     68  C   GLU A 565      21.454 166.974-203.570  1.00156.15           C  
ANISOU   68  C   GLU A 565    17806  14314  27207   4774  -2229  -3670       C  
ATOM     69  O   GLU A 565      20.478 166.843-202.824  1.00151.80           O  
ANISOU   69  O   GLU A 565    17476  13670  26531   4639  -2551  -3386       O  
ATOM     70  CB  GLU A 565      23.296 165.342-204.051  1.00170.22           C  
ANISOU   70  CB  GLU A 565    19263  15837  29577   5182  -2172  -3948       C  
ATOM     71  CG  GLU A 565      23.473 165.149-202.553  1.00174.12           C  
ANISOU   71  CG  GLU A 565    19613  16272  30271   5185  -2651  -3588       C  
ATOM     72  CD  GLU A 565      22.790 163.901-202.030  1.00179.25           C  
ANISOU   72  CD  GLU A 565    20524  16576  31009   5194  -3023  -3333       C  
ATOM     73  OE1 GLU A 565      22.239 163.130-202.845  1.00181.62           O  
ANISOU   73  OE1 GLU A 565    21081  16646  31281   5186  -2929  -3483       O  
ATOM     74  OE2 GLU A 565      22.809 163.687-200.799  1.00181.33           O1-
ANISOU   74  OE2 GLU A 565    20724  16802  31369   5215  -3407  -2976       O1-
ATOM     75  N   LEU A 566      22.174 168.094-203.642  1.00156.21           N  
ANISOU   75  N   LEU A 566    17507  14603  27240   4766  -1974  -3769       N  
ATOM     76  CA  LEU A 566      21.845 169.280-202.850  1.00155.36           C  
ANISOU   76  CA  LEU A 566    17306  14713  27010   4597  -2078  -3594       C  
ATOM     77  C   LEU A 566      20.415 169.720-203.112  1.00152.33           C  
ANISOU   77  C   LEU A 566    17308  14347  26225   4398  -2042  -3517       C  
ATOM     78  O   LEU A 566      19.684 170.094-202.189  1.00149.95           O  
ANISOU   78  O   LEU A 566    17129  14160  25685   4199  -2308  -3216       O  
ATOM     79  CB  LEU A 566      22.796 170.438-203.172  1.00159.04           C  
ANISOU   79  CB  LEU A 566    17379  15445  27606   4587  -1713  -3766       C  
ATOM     80  CG  LEU A 566      22.360 171.826-202.682  1.00157.91           C  
ANISOU   80  CG  LEU A 566    17154  15525  27320   4385  -1703  -3673       C  
ATOM     81  CD1 LEU A 566      22.450 171.936-201.163  1.00158.38           C  
ANISOU   81  CD1 LEU A 566    17068  15651  27457   4359  -2223  -3448       C  
ATOM     82  CD2 LEU A 566      23.158 172.936-203.358  1.00159.30           C  
ANISOU   82  CD2 LEU A 566    16985  15908  27636   4337  -1210  -3850       C  
ATOM     83  N   MET A 567      20.022 169.668-204.381  1.00152.06           N  
ANISOU   83  N   MET A 567    17494  14307  25975   4391  -1686  -3741       N  
ATOM     84  CA  MET A 567      18.673 170.044-204.773  1.00147.12           C  
ANISOU   84  CA  MET A 567    17259  13777  24864   4148  -1620  -3654       C  
ATOM     85  C   MET A 567      17.661 169.139-204.095  1.00145.05           C  
ANISOU   85  C   MET A 567    17287  13266  24558   4055  -2060  -3407       C  
ATOM     86  O   MET A 567      16.685 169.610-203.511  1.00141.59           O  
ANISOU   86  O   MET A 567    17028  12969  23801   3795  -2200  -3118       O  
ATOM     87  CB  MET A 567      18.513 169.953-206.289  1.00148.29           C  
ANISOU   87  CB  MET A 567    17587  13945  24811   4246  -1217  -3986       C  
ATOM     88  CG  MET A 567      17.194 170.503-206.788  1.00145.02           C  
ANISOU   88  CG  MET A 567    17540  13708  23851   3995  -1117  -3904       C  
ATOM     89  SD  MET A 567      17.057 170.382-208.576  1.00206.80           S  
ANISOU   89  SD  MET A 567    25584  21621  31371   4176   -678  -4312       S  
ATOM     90  CE  MET A 567      17.193 168.610-208.793  1.00158.40           C  
ANISOU   90  CE  MET A 567    19559  15055  25570   4420   -972  -4577       C  
ATOM     91  N   GLU A 568      17.911 167.836-204.169  1.00146.05           N  
ANISOU   91  N   GLU A 568    17441  13044  25006   4247  -2247  -3490       N  
ATOM     92  CA  GLU A 568      17.022 166.852-203.576  1.00144.85           C  
ANISOU   92  CA  GLU A 568    17528  12600  24909   4161  -2632  -3226       C  
ATOM     93  C   GLU A 568      16.844 167.095-202.088  1.00144.33           C  
ANISOU   93  C   GLU A 568    17385  12583  24871   4085  -2984  -2780       C  
ATOM     94  O   GLU A 568      15.721 167.184-201.602  1.00142.12           O  
ANISOU   94  O   GLU A 568    17335  12346  24319   3849  -3132  -2471       O  
ATOM     95  CB  GLU A 568      17.555 165.441-203.790  1.00149.16           C  
ANISOU   95  CB  GLU A 568    18044  12846  25783   4327  -2732  -3317       C  
ATOM     96  CG  GLU A 568      16.617 164.366-203.273  1.00149.84           C  
ANISOU   96  CG  GLU A 568    18354  12590  25990   4218  -3081  -3033       C  
ATOM     97  CD  GLU A 568      17.330 163.072-202.957  1.00153.53           C  
ANISOU   97  CD  GLU A 568    18695  12756  26883   4396  -3266  -2975       C  
ATOM     98  OE1 GLU A 568      18.579 163.061-202.982  1.00155.30           O  
ANISOU   98  OE1 GLU A 568    18648  13060  27300   4608  -3169  -3123       O  
ATOM     99  OE2 GLU A 568      16.637 162.071-202.681  1.00154.98           O1-
ANISOU   99  OE2 GLU A 568    19034  12614  27236   4317  -3499  -2770       O1-
ATOM    100  N   SER A 569      17.959 167.200-201.370  1.00147.70           N  
ANISOU  100  N   SER A 569    17481  13088  25550   4259  -3094  -2728       N  
ATOM    101  CA  SER A 569      17.916 167.399-199.925  1.00148.18           C  
ANISOU  101  CA  SER A 569    17457  13289  25554   4224  -3442  -2315       C  
ATOM    102  C   SER A 569      17.210 168.700-199.577  1.00141.28           C  
ANISOU  102  C   SER A 569    16665  12843  24172   3930  -3343  -2173       C  
ATOM    103  O   SER A 569      16.529 168.800-198.552  1.00140.91           O  
ANISOU  103  O   SER A 569    16732  12923  23886   3812  -3591  -1795       O  
ATOM    104  CB  SER A 569      19.325 167.403-199.334  1.00154.30           C  
ANISOU  104  CB  SER A 569    17828  14133  26667   4477  -3572  -2371       C  
ATOM    105  OG  SER A 569      19.279 167.587-197.930  1.00155.83           O  
ANISOU  105  OG  SER A 569    17951  14497  26758   4495  -3950  -1999       O  
ATOM    106  N   ASN A 570      17.382 169.696-200.438  1.00136.88           N  
ANISOU  106  N   ASN A 570    16042  12507  23458   3831  -2960  -2464       N  
ATOM    107  CA  ASN A 570      16.706 170.969-200.263  1.00130.70           C  
ANISOU  107  CA  ASN A 570    15335  12086  22241   3557  -2826  -2368       C  
ATOM    108  C   ASN A 570      15.202 170.753-200.337  1.00125.02           C  
ANISOU  108  C   ASN A 570    15009  11324  21169   3331  -2875  -2146       C  
ATOM    109  O   ASN A 570      14.459 171.203-199.466  1.00122.19           O  
ANISOU  109  O   ASN A 570    14745  11162  20518   3163  -3030  -1850       O  
ATOM    110  CB  ASN A 570      17.155 171.953-201.319  1.00130.96           C  
ANISOU  110  CB  ASN A 570    15236  12292  22233   3514  -2369  -2685       C  
ATOM    111  N   ILE A 571      14.762 170.044-201.371  1.00123.44           N  
ANISOU  111  N   ILE A 571    15019  10869  21012   3345  -2754  -2313       N  
ATOM    112  CA  ILE A 571      13.346 169.747-201.543  1.00121.08           C  
ANISOU  112  CA  ILE A 571    15058  10484  20463   3136  -2820  -2149       C  
ATOM    113  C   ILE A 571      12.822 168.971-200.339  1.00122.56           C  
ANISOU  113  C   ILE A 571    15314  10508  20744   3108  -3204  -1712       C  
ATOM    114  O   ILE A 571      11.684 169.164-199.904  1.00120.18           O  
ANISOU  114  O   ILE A 571    15196  10302  20167   2886  -3280  -1421       O  
ATOM    115  CB  ILE A 571      13.095 168.962-202.840  1.00120.41           C  
ANISOU  115  CB  ILE A 571    15151  10114  20485   3209  -2697  -2474       C  
ATOM    116  CG1 ILE A 571      13.590 169.771-204.039  1.00118.41           C  
ANISOU  116  CG1 ILE A 571    14846  10087  20056   3269  -2272  -2853       C  
ATOM    117  CG2 ILE A 571      11.619 168.652-202.999  1.00119.19           C  
ANISOU  117  CG2 ILE A 571    15302   9853  20132   2982  -2810  -2330       C  
ATOM    118  CD1 ILE A 571      13.376 169.095-205.373  1.00120.47           C  
ANISOU  118  CD1 ILE A 571    15293  10159  20321   3389  -2136  -3228       C  
ATOM    119  N   ARG A 572      13.677 168.113-199.791  1.00126.92           N  
ANISOU  119  N   ARG A 572    15703  10830  21692   3350  -3429  -1641       N  
ATOM    120  CA  ARG A 572      13.351 167.362-198.586  1.00129.10           C  
ANISOU  120  CA  ARG A 572    16015  10965  22074   3381  -3781  -1165       C  
ATOM    121  C   ARG A 572      13.031 168.312-197.447  1.00126.33           C  
ANISOU  121  C   ARG A 572    15634  11057  21308   3261  -3866   -842       C  
ATOM    122  O   ARG A 572      11.942 168.259-196.877  1.00122.42           O  
ANISOU  122  O   ARG A 572    15322  10618  20575   3088  -3955   -472       O  
ATOM    123  CB  ARG A 572      14.508 166.447-198.181  1.00131.76           C  
ANISOU  123  CB  ARG A 572    16136  11035  22891   3709  -3999  -1152       C  
ATOM    124  CG  ARG A 572      14.757 165.297-199.133  1.00133.51           C  
ANISOU  124  CG  ARG A 572    16395  10750  23583   3864  -3978  -1432       C  
ATOM    125  CD  ARG A 572      15.924 164.442-198.671  1.00136.25           C  
ANISOU  125  CD  ARG A 572    16511  10941  24317   4136  -4141  -1384       C  
ATOM    126  NE  ARG A 572      16.132 163.316-199.572  1.00138.63           N  
ANISOU  126  NE  ARG A 572    16856  10901  24917   4187  -4040  -1642       N  
ATOM    127  CZ  ARG A 572      15.453 162.176-199.503  1.00141.78           C  
ANISOU  127  CZ  ARG A 572    17417  10940  25511   4108  -4177  -1430       C  
ATOM    128  NH1 ARG A 572      14.525 162.007-198.570  1.00140.91           N1+
ANISOU  128  NH1 ARG A 572    17439  10774  25325   3966  -4383   -906       N1+
ATOM    129  NH2 ARG A 572      15.704 161.206-200.369  1.00146.20           N  
ANISOU  129  NH2 ARG A 572    17991  11207  26353   4175  -4096  -1738       N  
ATOM    130  N   ARG A 573      13.986 169.182-197.131  1.00128.73           N  
ANISOU  130  N   ARG A 573    15687  11672  21552   3360  -3836  -1008       N  
ATOM    131  CA  ARG A 573      13.808 170.169-196.070  1.00130.38           C  
ANISOU  131  CA  ARG A 573    15838  12321  21380   3282  -3936   -810       C  
ATOM    132  C   ARG A 573      12.535 170.978-196.294  1.00131.85           C  
ANISOU  132  C   ARG A 573    16249  12718  21129   2972  -3742   -741       C  
ATOM    133  O   ARG A 573      11.805 171.291-195.350  1.00131.95           O  
ANISOU  133  O   ARG A 573    16354  12974  20808   2881  -3867   -416       O  
ATOM    134  CB  ARG A 573      15.017 171.092-195.999  1.00129.51           C  
ANISOU  134  CB  ARG A 573    15393  12459  21354   3394  -3886  -1134       C  
ATOM    135  N   ASP A 574      12.265 171.289-197.558  1.00132.20           N  
ANISOU  135  N   ASP A 574    16383  12683  21165   2839  -3435  -1043       N  
ATOM    136  CA  ASP A 574      11.126 172.121-197.916  1.00127.84           C  
ANISOU  136  CA  ASP A 574    16021  12328  20226   2567  -3239  -1019       C  
ATOM    137  C   ASP A 574       9.792 171.445-197.632  1.00115.92           C  
ANISOU  137  C   ASP A 574    14766  10685  18592   2415  -3363   -662       C  
ATOM    138  O   ASP A 574       9.027 171.906-196.786  1.00109.97           O  
ANISOU  138  O   ASP A 574    14078  10182  17525   2291  -3429   -365       O  
ATOM    139  CB  ASP A 574      11.215 172.530-199.382  1.00134.79           C  
ANISOU  139  CB  ASP A 574    16938  13161  21117   2512  -2894  -1405       C  
ATOM    140  CG  ASP A 574      12.360 173.490-199.645  1.00142.81           C  
ANISOU  140  CG  ASP A 574    17677  14365  22218   2598  -2686  -1694       C  
ATOM    141  OD1 ASP A 574      12.685 174.295-198.741  1.00142.92           O  
ANISOU  141  OD1 ASP A 574    17514  14637  22153   2584  -2777  -1627       O  
ATOM    142  OD2 ASP A 574      12.935 173.437-200.754  1.00147.13           O1-
ANISOU  142  OD2 ASP A 574    18172  14805  22928   2688  -2429  -1996       O1-
ATOM    143  N   ILE A 575       9.523 170.354-198.341  1.00112.04           N  
ANISOU  143  N   ILE A 575    14399   9793  18378   2432  -3388   -710       N  
ATOM    144  CA  ILE A 575       8.275 169.617-198.184  1.00105.70           C  
ANISOU  144  CA  ILE A 575    13795   8780  17586   2272  -3504   -397       C  
ATOM    145  C   ILE A 575       8.072 169.165-196.744  1.00105.34           C  
ANISOU  145  C   ILE A 575    13723   8769  17531   2319  -3751    137       C  
ATOM    146  O   ILE A 575       6.950 169.175-196.223  1.00103.87           O  
ANISOU  146  O   ILE A 575    13654   8661  17152   2143  -3776    500       O  
ATOM    147  CB  ILE A 575       8.244 168.388-199.097  1.00105.37           C  
ANISOU  147  CB  ILE A 575    13835   8231  17971   2333  -3556   -588       C  
ATOM    148  CG1 ILE A 575       8.632 168.777-200.524  1.00103.58           C  
ANISOU  148  CG1 ILE A 575    13629   8018  17708   2373  -3306  -1138       C  
ATOM    149  CG2 ILE A 575       6.871 167.751-199.075  1.00105.29           C  
ANISOU  149  CG2 ILE A 575    13996   7984  18024   2120  -3656   -321       C  
ATOM    150  CD1 ILE A 575       8.482 167.657-201.517  1.00107.90           C  
ANISOU  150  CD1 ILE A 575    14282   8115  18600   2441  -3358  -1417       C  
ATOM    151  N   ARG A 576       9.168 168.775-196.101  1.00109.44           N  
ANISOU  151  N   ARG A 576    14079   9253  18251   2577  -3924    200       N  
ATOM    152  CA  ARG A 576       9.123 168.374-194.703  1.00114.47           C  
ANISOU  152  CA  ARG A 576    14686   9983  18824   2689  -4166    721       C  
ATOM    153  C   ARG A 576       8.625 169.533-193.861  1.00111.83           C  
ANISOU  153  C   ARG A 576    14363  10191  17935   2587  -4125    887       C  
ATOM    154  O   ARG A 576       7.716 169.369-193.042  1.00109.16           O  
ANISOU  154  O   ARG A 576    14130   9967  17379   2512  -4182   1352       O  
ATOM    155  CB  ARG A 576      10.506 167.940-194.224  1.00119.75           C  
ANISOU  155  CB  ARG A 576    15148  10592  19758   3018  -4371    687       C  
ATOM    156  CG  ARG A 576      10.590 167.659-192.740  1.00125.04           C  
ANISOU  156  CG  ARG A 576    15782  11459  20270   3195  -4638   1213       C  
ATOM    157  CD  ARG A 576       9.871 166.374-192.374  1.00127.98           C  
ANISOU  157  CD  ARG A 576    16289  11439  20899   3193  -4755   1754       C  
ATOM    158  NE  ARG A 576       9.745 166.229-190.928  1.00129.48           N  
ANISOU  158  NE  ARG A 576    16482  11907  20807   3349  -4949   2345       N  
ATOM    159  CZ  ARG A 576       9.149 165.203-190.334  1.00131.55           C  
ANISOU  159  CZ  ARG A 576    16837  11910  21237   3379  -5042   2956       C  
ATOM    160  NH1 ARG A 576       8.631 164.228-191.067  1.00131.82           N1+
ANISOU  160  NH1 ARG A 576    16946  11352  21789   3239  -4987   3011       N1+
ATOM    161  NH2 ARG A 576       9.076 165.152-189.011  1.00134.38           N  
ANISOU  161  NH2 ARG A 576    17203  12601  21254   3560  -5190   3510       N  
ATOM    162  N   GLN A 577       9.218 170.706-194.078  1.00115.99           N  
ANISOU  162  N   GLN A 577    14767  11040  18265   2591  -4010    501       N  
ATOM    163  CA  GLN A 577       8.802 171.911-193.364  1.00118.86           C  
ANISOU  163  CA  GLN A 577    15121  11898  18141   2502  -3970    553       C  
ATOM    164  C   GLN A 577       7.348 172.269-193.646  1.00113.66           C  
ANISOU  164  C   GLN A 577    14663  11306  17217   2217  -3784    695       C  
ATOM    165  O   GLN A 577       6.661 172.804-192.782  1.00111.56           O  
ANISOU  165  O   GLN A 577    14442  11379  16567   2162  -3799    947       O  
ATOM    166  CB  GLN A 577       9.715 173.095-193.695  1.00121.60           C  
ANISOU  166  CB  GLN A 577    15269  12478  18455   2532  -3863     75       C  
ATOM    167  CG  GLN A 577      11.030 173.092-192.933  1.00128.43           C  
ANISOU  167  CG  GLN A 577    15879  13467  19452   2813  -4110    -14       C  
ATOM    168  CD  GLN A 577      10.835 173.048-191.431  1.00131.77           C  
ANISOU  168  CD  GLN A 577    16314  14218  19536   2960  -4395    362       C  
ATOM    169  OE1 GLN A 577      11.533 172.316-190.726  1.00135.47           O  
ANISOU  169  OE1 GLN A 577    16688  14653  20130   3223  -4672    544       O  
ATOM    170  NE2 GLN A 577       9.888 173.838-190.930  1.00129.15           N  
ANISOU  170  NE2 GLN A 577    16095  14226  18749   2818  -4325    485       N  
ATOM    171  N   GLY A 578       6.889 171.964-194.856  1.00112.42           N  
ANISOU  171  N   GLY A 578    14614  10841  17259   2060  -3621    513       N  
ATOM    172  CA  GLY A 578       5.507 172.194-195.234  1.00112.17           C  
ANISOU  172  CA  GLY A 578    14751  10828  17042   1797  -3477    624       C  
ATOM    173  C   GLY A 578       4.543 171.333-194.438  1.00115.55           C  
ANISOU  173  C   GLY A 578    15270  11148  17486   1737  -3600   1167       C  
ATOM    174  O   GLY A 578       3.556 171.839-193.897  1.00115.66           O  
ANISOU  174  O   GLY A 578    15340  11429  17175   1599  -3532   1423       O  
ATOM    175  N   PHE A 579       4.827 170.032-194.364  1.00115.72           N  
ANISOU  175  N   PHE A 579    15289  10763  17917   1847  -3762   1360       N  
ATOM    176  CA  PHE A 579       4.010 169.115-193.563  1.00113.30           C  
ANISOU  176  CA  PHE A 579    15036  10296  17716   1807  -3865   1950       C  
ATOM    177  C   PHE A 579       4.030 169.484-192.078  1.00113.55           C  
ANISOU  177  C   PHE A 579    15029  10777  17336   1946  -3939   2385       C  
ATOM    178  O   PHE A 579       2.971 169.614-191.446  1.00113.31           O  
ANISOU  178  O   PHE A 579    15058  10940  17053   1825  -3863   2789       O  
ATOM    179  CB  PHE A 579       4.464 167.665-193.756  1.00115.14           C  
ANISOU  179  CB  PHE A 579    15249   9963  18536   1931  -4035   2063       C  
ATOM    180  CG  PHE A 579       3.774 166.683-192.840  1.00117.50           C  
ANISOU  180  CG  PHE A 579    15570  10060  19016   1920  -4134   2746       C  
ATOM    181  CD1 PHE A 579       2.460 166.309-193.068  1.00116.04           C  
ANISOU  181  CD1 PHE A 579    15448   9654  18990   1649  -4050   2986       C  
ATOM    182  CD2 PHE A 579       4.446 166.130-191.756  1.00119.05           C  
ANISOU  182  CD2 PHE A 579    15703  10286  19245   2190  -4307   3169       C  
ATOM    183  CE1 PHE A 579       1.826 165.409-192.234  1.00118.65           C  
ANISOU  183  CE1 PHE A 579    15765   9773  19544   1627  -4099   3660       C  
ATOM    184  CE2 PHE A 579       3.816 165.232-190.915  1.00121.64           C  
ANISOU  184  CE2 PHE A 579    16048  10431  19737   2196  -4359   3867       C  
ATOM    185  CZ  PHE A 579       2.506 164.870-191.155  1.00122.06           C  
ANISOU  185  CZ  PHE A 579    16151  10241  19986   1904  -4236   4125       C  
ATOM    186  N   VAL A 580       5.235 169.644-191.528  1.00114.15           N  
ANISOU  186  N   VAL A 580    14995  11036  17341   2219  -4091   2288       N  
ATOM    187  CA  VAL A 580       5.398 170.045-190.133  1.00116.55           C  
ANISOU  187  CA  VAL A 580    15259  11823  17200   2412  -4209   2609       C  
ATOM    188  C   VAL A 580       4.586 171.297-189.841  1.00117.60           C  
ANISOU  188  C   VAL A 580    15435  12444  16802   2261  -4042   2547       C  
ATOM    189  O   VAL A 580       3.866 171.363-188.843  1.00119.26           O  
ANISOU  189  O   VAL A 580    15700  12963  16651   2289  -4030   2989       O  
ATOM    190  CB  VAL A 580       6.867 170.339-189.791  1.00116.53           C  
ANISOU  190  CB  VAL A 580    15092  11997  17187   2705  -4409   2317       C  
ATOM    191  CG1 VAL A 580       6.968 170.938-188.400  1.00119.50           C  
ANISOU  191  CG1 VAL A 580    15433  12952  17019   2908  -4554   2540       C  
ATOM    192  CG2 VAL A 580       7.710 169.083-189.891  1.00118.63           C  
ANISOU  192  CG2 VAL A 580    15295  11818  17961   2912  -4600   2432       C  
ATOM    193  N   ASP A 581       4.699 172.284-190.725  1.00118.42           N  
ANISOU  193  N   ASP A 581    15511  12615  16869   2117  -3894   2012       N  
ATOM    194  CA  ASP A 581       3.944 173.525-190.589  1.00120.67           C  
ANISOU  194  CA  ASP A 581    15824  13301  16723   1969  -3727   1898       C  
ATOM    195  C   ASP A 581       2.446 173.257-190.566  1.00116.66           C  
ANISOU  195  C   ASP A 581    15445  12752  16129   1748  -3575   2285       C  
ATOM    196  O   ASP A 581       1.750 173.689-189.646  1.00118.14           O  
ANISOU  196  O   ASP A 581    15656  13321  15909   1760  -3528   2570       O  
ATOM    197  CB  ASP A 581       4.289 174.513-191.711  1.00123.77           C  
ANISOU  197  CB  ASP A 581    16166  13671  17190   1841  -3566   1314       C  
ATOM    198  CG  ASP A 581       5.532 175.339-191.403  1.00130.23           C  
ANISOU  198  CG  ASP A 581    16802  14731  17948   2024  -3664    940       C  
ATOM    199  OD1 ASP A 581       6.474 174.789-190.787  1.00136.75           O  
ANISOU  199  OD1 ASP A 581    17526  15550  18881   2267  -3895   1006       O  
ATOM    200  OD2 ASP A 581       5.561 176.535-191.770  1.00127.23           O1-
ANISOU  200  OD2 ASP A 581    16361  14530  17451   1928  -3520    587       O1-
ATOM    201  N   LEU A 582       1.962 172.534-191.573  1.00110.37           N  
ANISOU  201  N   LEU A 582    14710  11497  15726   1561  -3507   2274       N  
ATOM    202  CA  LEU A 582       0.535 172.260-191.704  1.00104.23           C  
ANISOU  202  CA  LEU A 582    14010  10620  14974   1321  -3378   2584       C  
ATOM    203  C   LEU A 582      -0.023 171.583-190.459  1.00108.12           C  
ANISOU  203  C   LEU A 582    14505  11211  15365   1394  -3416   3259       C  
ATOM    204  O   LEU A 582      -1.170 171.803-190.077  1.00105.45           O  
ANISOU  204  O   LEU A 582    14183  11055  14826   1254  -3269   3567       O  
ATOM    205  CB  LEU A 582       0.267 171.407-192.944  1.00 98.78           C  
ANISOU  205  CB  LEU A 582    13362   9372  14796   1155  -3381   2426       C  
ATOM    206  CG  LEU A 582      -1.171 170.927-193.157  1.00 97.92           C  
ANISOU  206  CG  LEU A 582    13287   9058  14859    897  -3304   2723       C  
ATOM    207  CD1 LEU A 582      -2.144 172.094-193.141  1.00 94.58           C  
ANISOU  207  CD1 LEU A 582    12875   9035  14026    735  -3118   2677       C  
ATOM    208  CD2 LEU A 582      -1.280 170.163-194.461  1.00 97.98           C  
ANISOU  208  CD2 LEU A 582    13329   8533  15368    771  -3365   2420       C  
ATOM    209  N   GLN A 583       0.802 170.767-189.818  1.00115.84           N  
ANISOU  209  N   GLN A 583    15454  12083  16477   1633  -3598   3512       N  
ATOM    210  CA  GLN A 583       0.351 170.042-188.638  1.00124.41           C  
ANISOU  210  CA  GLN A 583    16546  13253  17470   1742  -3621   4225       C  
ATOM    211  C   GLN A 583       0.458 170.876-187.357  1.00132.32           C  
ANISOU  211  C   GLN A 583    17546  14938  17792   1968  -3625   4390       C  
ATOM    212  O   GLN A 583      -0.339 170.712-186.434  1.00135.03           O  
ANISOU  212  O   GLN A 583    17914  15532  17860   2002  -3521   4948       O  
ATOM    213  CB  GLN A 583       1.109 168.718-188.500  1.00124.12           C  
ANISOU  213  CB  GLN A 583    16486  12772  17901   1921  -3820   4497       C  
ATOM    214  CG  GLN A 583       0.929 167.781-189.690  1.00116.64           C  
ANISOU  214  CG  GLN A 583    15539  11123  17656   1720  -3834   4340       C  
ATOM    215  CD  GLN A 583      -0.523 167.433-189.941  1.00110.84           C  
ANISOU  215  CD  GLN A 583    14816  10163  17134   1410  -3670   4644       C  
ATOM    216  OE1 GLN A 583      -1.081 167.782-190.978  1.00107.28           O  
ANISOU  216  OE1 GLN A 583    14383   9575  16805   1164  -3586   4240       O  
ATOM    217  NE2 GLN A 583      -1.143 166.741-188.989  1.00112.61           N  
ANISOU  217  NE2 GLN A 583    15016  10357  17414   1429  -3624   5378       N  
ATOM    218  N   THR A 584       1.428 171.782-187.312  1.00136.85           N  
ANISOU  218  N   THR A 584    18075  15817  18105   2128  -3738   3889       N  
ATOM    219  CA  THR A 584       1.700 172.538-186.093  1.00144.43           C  
ANISOU  219  CA  THR A 584    19017  17412  18448   2390  -3819   3943       C  
ATOM    220  C   THR A 584       1.129 173.954-186.114  1.00145.63           C  
ANISOU  220  C   THR A 584    19167  17984  18182   2271  -3655   3583       C  
ATOM    221  O   THR A 584       1.522 174.799-185.310  1.00146.30           O  
ANISOU  221  O   THR A 584    19214  18571  17803   2482  -3753   3397       O  
ATOM    222  CB  THR A 584       3.208 172.617-185.819  1.00147.69           C  
ANISOU  222  CB  THR A 584    19334  17916  18865   2688  -4112   3629       C  
ATOM    223  OG1 THR A 584       3.857 173.267-186.918  1.00145.98           O  
ANISOU  223  OG1 THR A 584    19034  17506  18925   2557  -4097   2952       O  
ATOM    224  CG2 THR A 584       3.788 171.224-185.647  1.00150.69           C  
ANISOU  224  CG2 THR A 584    19708  17917  19629   2861  -4292   4029       C  
ATOM    225  N   GLU A 585       0.201 174.209-187.030  1.00147.91           N  
ANISOU  225  N   GLU A 585    19487  18060  18653   1951  -3430   3468       N  
ATOM    226  CA  GLU A 585      -0.427 175.523-187.132  1.00147.06           C  
ANISOU  226  CA  GLU A 585    19373  18291  18212   1829  -3260   3157       C  
ATOM    227  C   GLU A 585      -1.546 175.693-186.107  1.00149.37           C  
ANISOU  227  C   GLU A 585    19701  19003  18051   1865  -3107   3616       C  
ATOM    228  O   GLU A 585      -2.601 175.068-186.215  1.00150.04           O  
ANISOU  228  O   GLU A 585    19812  18908  18289   1688  -2939   4053       O  
ATOM    229  CB  GLU A 585      -0.957 175.755-188.545  1.00142.50           C  
ANISOU  229  CB  GLU A 585    18811  17346  17985   1507  -3097   2854       C  
ATOM    230  N   LYS A 586      -1.304 176.542-185.113  1.00150.18           N  
ANISOU  230  N   LYS A 586    19785  19666  17611   2105  -3166   3495       N  
ATOM    231  CA  LYS A 586      -2.308 176.849-184.104  1.00153.72           C  
ANISOU  231  CA  LYS A 586    20263  20600  17543   2192  -2999   3860       C  
ATOM    232  C   LYS A 586      -3.295 177.873-184.648  1.00154.44           C  
ANISOU  232  C   LYS A 586    20333  20766  17581   1950  -2758   3585       C  
ATOM    233  O   LYS A 586      -3.089 178.427-185.729  1.00151.83           O  
ANISOU  233  O   LYS A 586    19974  20160  17554   1754  -2748   3102       O  
ATOM    234  CB  LYS A 586      -1.644 177.373-182.843  1.00156.05           C  
ANISOU  234  CB  LYS A 586    20553  21494  17247   2583  -3186   3766       C  
ATOM    235  N   SER A 587      -4.369 178.121-183.903  1.00159.06           N  
ANISOU  235  N   SER A 587    20926  21734  17777   1984  -2549   3917       N  
ATOM    236  CA  SER A 587      -5.360 179.117-184.305  1.00158.39           C  
ANISOU  236  CA  SER A 587    20802  21759  17620   1793  -2322   3683       C  
ATOM    237  C   SER A 587      -5.454 180.249-183.285  1.00160.24           C  
ANISOU  237  C   SER A 587    21021  22635  17229   2051  -2297   3455       C  
ATOM    238  O   SER A 587      -6.390 180.305-182.487  1.00163.66           O  
ANISOU  238  O   SER A 587    21452  23450  17282   2140  -2093   3817       O  
ATOM    239  CB  SER A 587      -6.733 178.470-184.508  1.00158.94           C  
ANISOU  239  CB  SER A 587    20847  21657  17885   1557  -2057   4220       C  
ATOM    240  OG  SER A 587      -7.665 179.407-185.021  1.00154.66           O  
ANISOU  240  OG  SER A 587    20250  21175  17338   1368  -1864   3971       O  
ATOM    241  N   ASP A 588      -4.478 181.149-183.322  1.00157.60           N  
ANISOU  241  N   ASP A 588    20656  22408  16819   2174  -2500   2837       N  
ATOM    242  CA  ASP A 588      -4.425 182.272-182.394  1.00157.84           C  
ANISOU  242  CA  ASP A 588    20655  23003  16315   2435  -2541   2490       C  
ATOM    243  C   ASP A 588      -5.075 183.518-182.992  1.00152.45           C  
ANISOU  243  C   ASP A 588    19909  22299  15717   2252  -2366   2055       C  
ATOM    244  O   ASP A 588      -4.613 184.639-182.774  1.00153.79           O  
ANISOU  244  O   ASP A 588    20014  22670  15750   2376  -2477   1493       O  
ATOM    245  CB  ASP A 588      -2.974 182.563-182.000  1.00159.53           C  
ANISOU  245  CB  ASP A 588    20828  23339  16448   2689  -2901   2041       C  
ATOM    246  CG  ASP A 588      -2.051 182.658-183.201  1.00155.32           C  
ANISOU  246  CG  ASP A 588    20225  22266  16523   2479  -3022   1628       C  
ATOM    247  OD1 ASP A 588      -2.399 182.103-184.264  1.00151.65           O  
ANISOU  247  OD1 ASP A 588    19791  21326  16502   2189  -2874   1810       O  
ATOM    248  OD2 ASP A 588      -0.975 183.281-183.081  1.00155.81           O1-
ANISOU  248  OD2 ASP A 588    20188  22389  16625   2616  -3263   1112       O1-
ATOM    249  N   LEU A 589      -6.151 183.311-183.745  1.00145.23           N  
ANISOU  249  N   LEU A 589    18996  21121  15065   1963  -2110   2315       N  
ATOM    250  CA  LEU A 589      -6.871 184.404-184.382  1.00136.62           C  
ANISOU  250  CA  LEU A 589    17845  19980  14085   1788  -1935   1983       C  
ATOM    251  C   LEU A 589      -7.764 185.131-183.379  1.00139.19           C  
ANISOU  251  C   LEU A 589    18136  20851  13899   1975  -1764   2012       C  
ATOM    252  O   LEU A 589      -7.903 184.691-182.238  1.00143.00           O  
ANISOU  252  O   LEU A 589    18653  21758  13921   2227  -1748   2351       O  
ATOM    253  CB  LEU A 589      -7.700 183.879-185.556  1.00129.68           C  
ANISOU  253  CB  LEU A 589    16968  18643  13661   1438  -1767   2236       C  
ATOM    254  CG  LEU A 589      -6.899 183.189-186.665  1.00124.65           C  
ANISOU  254  CG  LEU A 589    16373  17467  13523   1264  -1913   2155       C  
ATOM    255  CD1 LEU A 589      -7.810 182.676-187.770  1.00121.83           C  
ANISOU  255  CD1 LEU A 589    16018  16711  13559    953  -1778   2364       C  
ATOM    256  CD2 LEU A 589      -5.847 184.131-187.229  1.00121.16           C  
ANISOU  256  CD2 LEU A 589    15898  16905  13232   1284  -2042   1541       C  
ATOM    257  N   ILE A 590      -8.356 186.242-183.816  1.00137.72           N  
ANISOU  257  N   ILE A 590    17881  20658  13789   1874  -1628   1666       N  
ATOM    258  CA  ILE A 590      -9.221 187.078-182.979  1.00140.22           C  
ANISOU  258  CA  ILE A 590    18144  21460  13674   2053  -1453   1596       C  
ATOM    259  C   ILE A 590      -8.505 187.640-181.751  1.00144.68           C  
ANISOU  259  C   ILE A 590    18716  22537  13719   2446  -1639   1250       C  
ATOM    260  O   ILE A 590      -8.290 186.941-180.761  1.00149.29           O  
ANISOU  260  O   ILE A 590    19365  23481  13876   2696  -1703   1570       O  
ATOM    261  CB  ILE A 590     -10.517 186.342-182.555  1.00142.09           C  
ANISOU  261  CB  ILE A 590    18367  21893  13728   2020  -1160   2259       C  
ATOM    262  CG1 ILE A 590     -11.306 185.900-183.788  1.00139.12           C  
ANISOU  262  CG1 ILE A 590    17946  21014  13899   1632  -1017   2509       C  
ATOM    263  CG2 ILE A 590     -11.373 187.228-181.659  1.00144.42           C  
ANISOU  263  CG2 ILE A 590    18595  22731  13548   2245   -953   2163       C  
ATOM    264  CD1 ILE A 590     -11.576 187.021-184.779  1.00135.48           C  
ANISOU  264  CD1 ILE A 590    17424  20316  13738   1461   -983   2034       C  
ATOM    265  N   VAL A 593     -12.435 191.191-180.310  1.00150.36           N  
ANISOU  265  N   VAL A 593    19118  24452  13557   2837   -753    662       N  
ATOM    266  CA  VAL A 593     -12.905 192.066-181.379  1.00147.17           C  
ANISOU  266  CA  VAL A 593    18614  23632  13671   2585   -668    376       C  
ATOM    267  C   VAL A 593     -13.951 193.057-180.869  1.00150.90           C  
ANISOU  267  C   VAL A 593    18972  24453  13912   2766   -431    173       C  
ATOM    268  O   VAL A 593     -13.770 194.271-180.975  1.00152.30           O  
ANISOU  268  O   VAL A 593    19079  24559  14228   2844   -510   -432       O  
ATOM    269  CB  VAL A 593     -13.484 191.259-182.558  1.00142.57           C  
ANISOU  269  CB  VAL A 593    18024  22568  13579   2188   -539    872       C  
ATOM    270  CG1 VAL A 593     -14.129 192.190-183.566  1.00139.29           C  
ANISOU  270  CG1 VAL A 593    17505  21822  13595   1989   -433    629       C  
ATOM    271  CG2 VAL A 593     -12.395 190.424-183.217  1.00139.04           C  
ANISOU  271  CG2 VAL A 593    17683  21712  13435   2012   -781    954       C  
ATOM    272  N   GLY A 594     -15.045 192.534-180.325  1.00152.26           N  
ANISOU  272  N   GLY A 594    19100  24977  13775   2834   -126    689       N  
ATOM    273  CA  GLY A 594     -16.044 193.363-179.675  1.00152.79           C  
ANISOU  273  CA  GLY A 594    19048  25466  13540   3066    131    538       C  
ATOM    274  C   GLY A 594     -17.035 194.043-180.601  1.00146.89           C  
ANISOU  274  C   GLY A 594    18145  24389  13276   2837    316    477       C  
ATOM    275  O   GLY A 594     -17.730 193.385-181.376  1.00144.74           O  
ANISOU  275  O   GLY A 594    17814  23824  13356   2533    457    963       O  
ATOM    276  N   ALA A 595     -17.101 195.369-180.512  1.00143.91           N  
ANISOU  276  N   ALA A 595    17689  24051  12938   2999    293   -138       N  
ATOM    277  CA  ALA A 595     -18.083 196.155-181.257  1.00138.90           C  
ANISOU  277  CA  ALA A 595    16894  23163  12717   2860    472   -225       C  
ATOM    278  C   ALA A 595     -17.767 196.238-182.749  1.00132.06           C  
ANISOU  278  C   ALA A 595    16044  21605  12530   2482    320   -248       C  
ATOM    279  O   ALA A 595     -16.764 196.826-183.148  1.00130.73           O  
ANISOU  279  O   ALA A 595    15932  21131  12607   2455     77   -701       O  
ATOM    280  CB  ALA A 595     -18.196 197.551-180.662  1.00140.14           C  
ANISOU  280  CB  ALA A 595    16962  23549  12735   3178    483   -890       C  
ATOM    281  N   ILE A 596     -18.637 195.658-183.568  1.00128.33           N  
ANISOU  281  N   ILE A 596    15502  20897  12359   2204    467    237       N  
ATOM    282  CA  ILE A 596     -18.439 195.631-185.015  1.00121.47           C  
ANISOU  282  CA  ILE A 596    14662  19432  12058   1873    334    267       C  
ATOM    283  C   ILE A 596     -18.744 196.989-185.653  1.00119.26           C  
ANISOU  283  C   ILE A 596    14280  18902  12130   1884    349   -141       C  
ATOM    284  O   ILE A 596     -19.854 197.507-185.516  1.00121.44           O  
ANISOU  284  O   ILE A 596    14394  19331  12418   1967    553   -110       O  
ATOM    285  CB  ILE A 596     -19.312 194.546-185.687  1.00119.30           C  
ANISOU  285  CB  ILE A 596    14334  18999  11996   1591    443    879       C  
ATOM    286  CG1 ILE A 596     -19.038 193.166-185.081  1.00119.21           C  
ANISOU  286  CG1 ILE A 596    14406  19166  11721   1568    444   1336       C  
ATOM    287  CG2 ILE A 596     -19.063 194.512-187.179  1.00115.20           C  
ANISOU  287  CG2 ILE A 596    13869  17919  11982   1298    279    863       C  
ATOM    288  CD1 ILE A 596     -20.000 192.761-183.978  1.00121.91           C  
ANISOU  288  CD1 ILE A 596    14619  20016  11684   1734    740   1728       C  
ATOM    289  N   PRO A 597     -17.760 197.563-186.367  1.00115.22           N  
ANISOU  289  N   PRO A 597    13847  17990  11942   1805    147   -496       N  
ATOM    290  CA  PRO A 597     -17.878 198.891-186.988  1.00113.18           C  
ANISOU  290  CA  PRO A 597    13499  17434  12072   1823    152   -868       C  
ATOM    291  C   PRO A 597     -18.937 198.951-188.087  1.00109.61           C  
ANISOU  291  C   PRO A 597    12962  16729  11956   1634    266   -556       C  
ATOM    292  O   PRO A 597     -18.609 199.217-189.247  1.00105.63           O  
ANISOU  292  O   PRO A 597    12507  15795  11834   1466    177   -567       O  
ATOM    293  CB  PRO A 597     -16.489 199.114-187.595  1.00109.33           C  
ANISOU  293  CB  PRO A 597    13119  16550  11869   1723    -69  -1143       C  
ATOM    294  CG  PRO A 597     -15.951 197.751-187.815  1.00106.18           C  
ANISOU  294  CG  PRO A 597    12866  16124  11353   1552   -169   -781       C  
ATOM    295  CD  PRO A 597     -16.459 196.939-186.661  1.00110.68           C  
ANISOU  295  CD  PRO A 597    13433  17198  11424   1691    -79   -519       C  
ATOM    296  N   PHE A 598     -20.191 198.715-187.717  1.00109.46           N  
ANISOU  296  N   PHE A 598    12804  16997  11789   1679    463   -278       N  
ATOM    297  CA  PHE A 598     -21.286 198.750-188.674  1.00107.10           C  
ANISOU  297  CA  PHE A 598    12384  16506  11803   1523    544      6       C  
ATOM    298  C   PHE A 598     -21.507 200.140-189.249  1.00107.10           C  
ANISOU  298  C   PHE A 598    12295  16245  12152   1608    553   -313       C  
ATOM    299  O   PHE A 598     -21.178 201.150-188.626  1.00110.54           O  
ANISOU  299  O   PHE A 598    12692  16741  12567   1832    573   -757       O  
ATOM    300  CB  PHE A 598     -22.579 198.250-188.033  1.00109.08           C  
ANISOU  300  CB  PHE A 598    12448  17139  11859   1572    772    354       C  
ATOM    301  CG  PHE A 598     -22.724 196.763-188.057  1.00106.35           C  
ANISOU  301  CG  PHE A 598    12137  16850  11420   1366    768    859       C  
ATOM    302  CD1 PHE A 598     -23.097 196.114-189.221  1.00102.44           C  
ANISOU  302  CD1 PHE A 598    11631  16026  11266   1082    662   1161       C  
ATOM    303  CD2 PHE A 598     -22.488 196.011-186.917  1.00108.27           C  
ANISOU  303  CD2 PHE A 598    12420  17470  11246   1473    858   1029       C  
ATOM    304  CE1 PHE A 598     -23.231 194.741-189.247  1.00101.96           C  
ANISOU  304  CE1 PHE A 598    11581  15961  11200    886    641   1592       C  
ATOM    305  CE2 PHE A 598     -22.620 194.638-186.937  1.00107.03           C  
ANISOU  305  CE2 PHE A 598    12281  17311  11077   1281    864   1528       C  
ATOM    306  CZ  PHE A 598     -22.990 194.002-188.102  1.00103.93           C  
ANISOU  306  CZ  PHE A 598    11858  16537  11095    976    752   1793       C  
ATOM    307  N   LEU A 599     -22.071 200.175-190.449  1.00102.76           N  
ANISOU  307  N   LEU A 599    11709  15399  11936   1440    523    -87       N  
ATOM    308  CA  LEU A 599     -22.450 201.421-191.090  1.00 99.99           C  
ANISOU  308  CA  LEU A 599    11260  14793  11939   1523    547   -272       C  
ATOM    309  C   LEU A 599     -23.924 201.727-190.853  1.00110.53           C  
ANISOU  309  C   LEU A 599    12344  16343  13308   1633    720   -140       C  
ATOM    310  O   LEU A 599     -24.748 200.816-190.746  1.00111.15           O  
ANISOU  310  O   LEU A 599    12325  16638  13269   1535    787    224       O  
ATOM    311  CB  LEU A 599     -22.177 201.338-192.588  1.00 88.13           C  
ANISOU  311  CB  LEU A 599     9873  12869  10744   1323    403    -91       C  
ATOM    312  CG  LEU A 599     -20.769 201.748-192.986  1.00 81.19           C  
ANISOU  312  CG  LEU A 599     9167  11671  10010   1295    296   -339       C  
ATOM    313  CD1 LEU A 599     -20.601 201.701-194.490  1.00 73.40           C  
ANISOU  313  CD1 LEU A 599     8289  10325   9275   1141    205   -121       C  
ATOM    314  CD2 LEU A 599     -20.522 203.143-192.463  1.00 88.98           C  
ANISOU  314  CD2 LEU A 599    10053  12569  11188   1513    362   -775       C  
ATOM    315  N   ASP A 600     -24.249 203.014-190.764  1.00118.30           N  
ANISOU  315  N   ASP A 600    13199  17244  14504   1839    797   -439       N  
ATOM    316  CA  ASP A 600     -25.639 203.446-190.662  1.00123.92           C  
ANISOU  316  CA  ASP A 600    13649  18111  15324   1966    957   -342       C  
ATOM    317  C   ASP A 600     -26.330 203.175-191.989  1.00119.87           C  
ANISOU  317  C   ASP A 600    13089  17351  15106   1777    857     36       C  
ATOM    318  O   ASP A 600     -25.709 203.306-193.044  1.00116.89           O  
ANISOU  318  O   ASP A 600    12875  16608  14930   1657    691     70       O  
ATOM    319  CB  ASP A 600     -25.721 204.933-190.325  1.00130.12           C  
ANISOU  319  CB  ASP A 600    14318  18796  16328   2245   1035   -789       C  
ATOM    320  CG  ASP A 600     -25.107 205.260-188.978  1.00136.70           C  
ANISOU  320  CG  ASP A 600    15177  19908  16856   2474   1100  -1246       C  
ATOM    321  OD1 ASP A 600     -24.181 204.538-188.549  1.00137.10           O  
ANISOU  321  OD1 ASP A 600    15408  20083  16602   2398   1012  -1272       O  
ATOM    322  OD2 ASP A 600     -25.555 206.244-188.350  1.00141.51           O1-
ANISOU  322  OD2 ASP A 600    15622  20618  17528   2752   1221  -1601       O1-
ATOM    323  N   TYR A 601     -27.610 202.809-191.933  1.00118.57           N  
ANISOU  323  N   TYR A 601    12687  17403  14962   1768    957    313       N  
ATOM    324  CA  TYR A 601     -28.337 202.361-193.122  1.00116.39           C  
ANISOU  324  CA  TYR A 601    12338  16954  14930   1585    814    668       C  
ATOM    325  C   TYR A 601     -28.211 203.288-194.327  1.00113.96           C  
ANISOU  325  C   TYR A 601    12097  16250  14954   1624    664    609       C  
ATOM    326  O   TYR A 601     -28.234 202.833-195.470  1.00112.34           O  
ANISOU  326  O   TYR A 601    11982  15852  14851   1461    467    842       O  
ATOM    327  CB  TYR A 601     -29.820 202.128-192.828  1.00121.07           C  
ANISOU  327  CB  TYR A 601    12582  17816  15601   1619    954    903       C  
ATOM    328  CG  TYR A 601     -30.589 201.762-194.077  1.00123.43           C  
ANISOU  328  CG  TYR A 601    12777  17931  16191   1455    750   1203       C  
ATOM    329  CD1 TYR A 601     -30.456 200.503-194.646  1.00123.25           C  
ANISOU  329  CD1 TYR A 601    12846  17845  16139   1177    566   1469       C  
ATOM    330  CD2 TYR A 601     -31.420 202.681-194.705  1.00125.95           C  
ANISOU  330  CD2 TYR A 601    12906  18129  16821   1598    712   1193       C  
ATOM    331  CE1 TYR A 601     -31.141 200.163-195.793  1.00124.47           C  
ANISOU  331  CE1 TYR A 601    12904  17847  16542   1047    332   1678       C  
ATOM    332  CE2 TYR A 601     -32.109 202.348-195.854  1.00126.85           C  
ANISOU  332  CE2 TYR A 601    12925  18107  17164   1478    480   1444       C  
ATOM    333  CZ  TYR A 601     -31.965 201.088-196.392  1.00126.01           C  
ANISOU  333  CZ  TYR A 601    12914  17966  16999   1204    281   1664       C  
ATOM    334  OH  TYR A 601     -32.648 200.750-197.536  1.00127.42           O  
ANISOU  334  OH  TYR A 601    12995  18029  17392   1105      6   1852       O  
ATOM    335  N   LYS A 602     -28.090 204.585-194.075  1.00113.97           N  
ANISOU  335  N   LYS A 602    12051  16130  15124   1857    757    302       N  
ATOM    336  CA  LYS A 602     -27.928 205.528-195.169  1.00112.54           C  
ANISOU  336  CA  LYS A 602    11927  15547  15285   1916    650    294       C  
ATOM    337  C   LYS A 602     -26.640 205.241-195.939  1.00112.09           C  
ANISOU  337  C   LYS A 602    12183  15208  15197   1751    503    322       C  
ATOM    338  O   LYS A 602     -26.659 205.120-197.162  1.00112.31           O  
ANISOU  338  O   LYS A 602    12309  15033  15331   1666    357    568       O  
ATOM    339  CB  LYS A 602     -27.971 206.974-194.661  1.00112.71           C  
ANISOU  339  CB  LYS A 602    11823  15440  15563   2197    788    -61       C  
ATOM    340  CG  LYS A 602     -27.254 207.199-193.346  1.00114.24           C  
ANISOU  340  CG  LYS A 602    12048  15794  15563   2311    911   -490       C  
ATOM    341  CD  LYS A 602     -27.400 208.634-192.861  1.00118.09           C  
ANISOU  341  CD  LYS A 602    12381  16134  16356   2605   1022   -896       C  
ATOM    342  CE  LYS A 602     -26.660 208.840-191.546  1.00120.73           C  
ANISOU  342  CE  LYS A 602    12750  16658  16464   2742   1095  -1392       C  
ATOM    343  NZ  LYS A 602     -26.899 210.183-190.952  1.00125.77           N1+
ANISOU  343  NZ  LYS A 602    13207  17188  17390   3054   1195  -1862       N1+
ATOM    344  N   HIS A 603     -25.534 205.103-195.215  1.00111.74           N  
ANISOU  344  N   HIS A 603    12286  15185  14986   1725    540     68       N  
ATOM    345  CA  HIS A 603     -24.224 204.903-195.831  1.00110.49           C  
ANISOU  345  CA  HIS A 603    12388  14759  14833   1590    434     52       C  
ATOM    346  C   HIS A 603     -24.105 203.533-196.496  1.00107.39           C  
ANISOU  346  C   HIS A 603    12149  14432  14222   1352    288    366       C  
ATOM    347  O   HIS A 603     -23.536 203.393-197.582  1.00107.13           O  
ANISOU  347  O   HIS A 603    12293  14160  14251   1258    181    500       O  
ATOM    348  CB  HIS A 603     -23.119 205.083-194.788  1.00111.03           C  
ANISOU  348  CB  HIS A 603    12527  14861  14800   1638    483   -334       C  
ATOM    349  CG  HIS A 603     -23.064 206.457-194.197  1.00112.94           C  
ANISOU  349  CG  HIS A 603    12630  14972  15311   1871    584   -729       C  
ATOM    350  ND1 HIS A 603     -22.123 207.390-194.572  1.00113.37           N  
ANISOU  350  ND1 HIS A 603    12737  14613  15727   1903    571   -940       N  
ATOM    351  CD2 HIS A 603     -23.836 207.057-193.259  1.00115.13           C  
ANISOU  351  CD2 HIS A 603    12701  15461  15584   2090    705   -967       C  
ATOM    352  CE1 HIS A 603     -22.314 208.505-193.890  1.00116.24           C  
ANISOU  352  CE1 HIS A 603    12931  14904  16332   2123    652  -1314       C  
ATOM    353  NE2 HIS A 603     -23.348 208.329-193.087  1.00117.57           N  
ANISOU  353  NE2 HIS A 603    12950  15462  16257   2253    733  -1354       N  
ATOM    354  N   PHE A 604     -24.643 202.526-195.821  1.00104.03           N  
ANISOU  354  N   PHE A 604    11646  14330  13551   1269    299    481       N  
ATOM    355  CA  PHE A 604     -24.715 201.171-196.344  1.00 98.68           C  
ANISOU  355  CA  PHE A 604    11058  13704  12731   1045    154    766       C  
ATOM    356  C   PHE A 604     -25.469 201.154-197.668  1.00 96.26           C  
ANISOU  356  C   PHE A 604    10720  13256  12597   1000      2   1007       C  
ATOM    357  O   PHE A 604     -24.914 200.795-198.710  1.00 94.50           O  
ANISOU  357  O   PHE A 604    10698  12846  12364    903   -151   1096       O  
ATOM    358  CB  PHE A 604     -25.414 200.292-195.303  1.00100.49           C  
ANISOU  358  CB  PHE A 604    11126  14288  12769    998    244    889       C  
ATOM    359  CG  PHE A 604     -25.946 198.990-195.835  1.00 97.91           C  
ANISOU  359  CG  PHE A 604    10773  13990  12438    775    102   1214       C  
ATOM    360  CD1 PHE A 604     -25.120 197.888-195.956  1.00 95.21           C  
ANISOU  360  CD1 PHE A 604    10630  13584  11961    598    -13   1288       C  
ATOM    361  CD2 PHE A 604     -27.286 198.858-196.163  1.00 98.29           C  
ANISOU  361  CD2 PHE A 604    10567  14118  12660    748     76   1423       C  
ATOM    362  CE1 PHE A 604     -25.610 196.685-196.421  1.00 96.39           C  
ANISOU  362  CE1 PHE A 604    10738  13716  12170    394   -159   1546       C  
ATOM    363  CE2 PHE A 604     -27.784 197.660-196.632  1.00 98.95           C  
ANISOU  363  CE2 PHE A 604    10590  14195  12811    533    -82   1678       C  
ATOM    364  CZ  PHE A 604     -26.945 196.571-196.758  1.00 99.00           C  
ANISOU  364  CZ  PHE A 604    10807  14109  12701    354   -200   1732       C  
ATOM    365  N   ALA A 605     -26.732 201.568-197.619  1.00 97.09           N  
ANISOU  365  N   ALA A 605    10567  13476  12849   1097     41   1096       N  
ATOM    366  CA  ALA A 605     -27.590 201.567-198.797  1.00 94.45           C  
ANISOU  366  CA  ALA A 605    10157  13058  12672   1087   -138   1314       C  
ATOM    367  C   ALA A 605     -26.980 202.381-199.925  1.00 94.70           C  
ANISOU  367  C   ALA A 605    10385  12793  12802   1182   -216   1310       C  
ATOM    368  O   ALA A 605     -27.004 201.962-201.076  1.00 93.05           O  
ANISOU  368  O   ALA A 605    10297  12502  12554   1122   -419   1476       O  
ATOM    369  CB  ALA A 605     -28.976 202.083-198.453  1.00 93.84           C  
ANISOU  369  CB  ALA A 605     9733  13141  12780   1221    -59   1371       C  
ATOM    370  N   SER A 606     -26.419 203.538-199.589  1.00 98.33           N  
ANISOU  370  N   SER A 606    10872  13093  13396   1342    -51   1118       N  
ATOM    371  CA  SER A 606     -25.806 204.398-200.597  1.00 99.94           C  
ANISOU  371  CA  SER A 606    11236  12983  13753   1441    -66   1164       C  
ATOM    372  C   SER A 606     -24.582 203.743-201.238  1.00 97.09           C  
ANISOU  372  C   SER A 606    11174  12499  13217   1296   -136   1198       C  
ATOM    373  O   SER A 606     -24.345 203.908-202.435  1.00 95.68           O  
ANISOU  373  O   SER A 606    11146  12166  13042   1333   -214   1379       O  
ATOM    374  CB  SER A 606     -25.450 205.773-200.014  1.00102.17           C  
ANISOU  374  CB  SER A 606    11440  13065  14314   1625    132    929       C  
ATOM    375  OG  SER A 606     -24.570 205.663-198.908  1.00101.17           O  
ANISOU  375  OG  SER A 606    11354  12983  14103   1577    242    621       O  
ATOM    376  N   ARG A 607     -23.814 202.996-200.448  1.00 96.93           N  
ANISOU  376  N   ARG A 607    11235  12568  13026   1157   -102   1038       N  
ATOM    377  CA  ARG A 607     -22.653 202.285-200.985  1.00 97.30           C  
ANISOU  377  CA  ARG A 607    11539  12510  12920   1025   -165   1052       C  
ATOM    378  C   ARG A 607     -23.056 201.106-201.867  1.00 96.47           C  
ANISOU  378  C   ARG A 607    11527  12506  12623    899   -385   1259       C  
ATOM    379  O   ARG A 607     -22.379 200.795-202.847  1.00 99.61           O  
ANISOU  379  O   ARG A 607    12137  12787  12922    870   -460   1331       O  
ATOM    380  CB  ARG A 607     -21.703 201.829-199.873  1.00 98.62           C  
ANISOU  380  CB  ARG A 607    11753  12741  12978    937    -93    819       C  
ATOM    381  CG  ARG A 607     -20.737 202.912-199.430  1.00103.48           C  
ANISOU  381  CG  ARG A 607    12370  13149  13798   1039     60    562       C  
ATOM    382  CD  ARG A 607     -19.398 202.350-198.963  1.00106.65           C  
ANISOU  382  CD  ARG A 607    12904  13523  14093    938     56    382       C  
ATOM    383  NE  ARG A 607     -18.779 201.440-199.931  1.00108.19           N  
ANISOU  383  NE  ARG A 607    13306  13645  14156    808    -39    553       N  
ATOM    384  CZ  ARG A 607     -18.119 201.819-201.024  1.00108.76           C  
ANISOU  384  CZ  ARG A 607    13505  13474  14346    827      3    649       C  
ATOM    385  NH1 ARG A 607     -17.992 203.105-201.326  1.00111.38           N1+
ANISOU  385  NH1 ARG A 607    13771  13569  14977    951    142    639       N1+
ATOM    386  NH2 ARG A 607     -17.591 200.904-201.828  1.00106.14           N  
ANISOU  386  NH2 ARG A 607    13358  13129  13842    734    -78    768       N  
ATOM    387  N   ILE A 608     -24.164 200.459-201.523  1.00 92.99           N  
ANISOU  387  N   ILE A 608    10907  12276  12150    833   -483   1340       N  
ATOM    388  CA  ILE A 608     -24.685 199.359-202.333  1.00 91.50           C  
ANISOU  388  CA  ILE A 608    10749  12156  11862    710   -733   1492       C  
ATOM    389  C   ILE A 608     -25.309 199.828-203.653  1.00 94.78           C  
ANISOU  389  C   ILE A 608    11178  12521  12312    840   -896   1642       C  
ATOM    390  O   ILE A 608     -25.109 199.208-204.699  1.00 94.53           O  
ANISOU  390  O   ILE A 608    11320  12466  12133    808  -1095   1699       O  
ATOM    391  CB  ILE A 608     -25.713 198.515-201.550  1.00 90.76           C  
ANISOU  391  CB  ILE A 608    10406  12272  11808    583   -781   1557       C  
ATOM    392  CG1 ILE A 608     -25.008 197.694-200.467  1.00 90.14           C  
ANISOU  392  CG1 ILE A 608    10378  12262  11611    445   -677   1483       C  
ATOM    393  CG2 ILE A 608     -26.490 197.606-202.488  1.00 89.44           C  
ANISOU  393  CG2 ILE A 608    10191  12130  11663    479  -1077   1688       C  
ATOM    394  CD1 ILE A 608     -25.757 196.441-200.059  1.00 90.59           C  
ANISOU  394  CD1 ILE A 608    10268  12453  11699    262   -768   1631       C  
ATOM    395  N   PHE A 609     -26.061 200.925-203.602  1.00 98.63           N  
ANISOU  395  N   PHE A 609    11487  13007  12981   1014   -820   1696       N  
ATOM    396  CA  PHE A 609     -26.755 201.432-204.786  1.00100.41           C  
ANISOU  396  CA  PHE A 609    11699  13211  13239   1177   -986   1872       C  
ATOM    397  C   PHE A 609     -25.772 202.086-205.745  1.00103.65           C  
ANISOU  397  C   PHE A 609    12387  13428  13566   1310   -920   1949       C  
ATOM    398  O   PHE A 609     -25.878 201.926-206.962  1.00104.42           O  
ANISOU  398  O   PHE A 609    12626  13551  13498   1397  -1107   2096       O  
ATOM    399  CB  PHE A 609     -27.848 202.443-204.417  1.00 98.91           C  
ANISOU  399  CB  PHE A 609    11216  13056  13310   1346   -915   1923       C  
ATOM    400  CG  PHE A 609     -28.814 201.956-203.376  1.00 97.79           C  
ANISOU  400  CG  PHE A 609    10761  13120  13276   1246   -894   1869       C  
ATOM    401  CD1 PHE A 609     -29.028 200.604-203.173  1.00 98.44           C  
ANISOU  401  CD1 PHE A 609    10800  13341  13264   1018  -1033   1874       C  
ATOM    402  CD2 PHE A 609     -29.508 202.859-202.596  1.00 99.58           C  
ANISOU  402  CD2 PHE A 609    10723  13389  13725   1390   -713   1823       C  
ATOM    403  CE1 PHE A 609     -29.913 200.165-202.207  1.00100.95           C  
ANISOU  403  CE1 PHE A 609    10808  13843  13707    927   -964   1887       C  
ATOM    404  CE2 PHE A 609     -30.394 202.427-201.633  1.00102.31           C  
ANISOU  404  CE2 PHE A 609    10768  13955  14150   1321   -643   1802       C  
ATOM    405  CZ  PHE A 609     -30.597 201.078-201.436  1.00102.49           C  
ANISOU  405  CZ  PHE A 609    10742  14122  14076   1084   -755   1860       C  
ATOM    406  N   PHE A 610     -24.820 202.830-205.189  1.00106.52           N  
ANISOU  406  N   PHE A 610    12813  13608  14051   1340   -651   1849       N  
ATOM    407  CA  PHE A 610     -23.808 203.496-206.001  1.00112.26           C  
ANISOU  407  CA  PHE A 610    13761  14114  14779   1449   -523   1950       C  
ATOM    408  C   PHE A 610     -22.393 203.253-205.498  1.00113.04           C  
ANISOU  408  C   PHE A 610    14003  14085  14862   1319   -352   1769       C  
ATOM    409  O   PHE A 610     -21.798 204.124-204.866  1.00114.31           O  
ANISOU  409  O   PHE A 610    14103  14052  15278   1355   -137   1648       O  
ATOM    410  CB  PHE A 610     -24.065 205.001-206.063  1.00114.83           C  
ANISOU  410  CB  PHE A 610    13970  14237  15424   1665   -357   2058       C  
ATOM    411  CG  PHE A 610     -25.421 205.364-206.579  1.00117.49           C  
ANISOU  411  CG  PHE A 610    14149  14682  15810   1833   -524   2252       C  
ATOM    412  CD1 PHE A 610     -25.646 205.491-207.939  1.00119.49           C  
ANISOU  412  CD1 PHE A 610    14541  14959  15901   1996   -667   2541       C  
ATOM    413  CD2 PHE A 610     -26.472 205.581-205.704  1.00118.28           C  
ANISOU  413  CD2 PHE A 610    13953  14885  16105   1852   -536   2146       C  
ATOM    414  CE1 PHE A 610     -26.896 205.826-208.418  1.00122.33           C  
ANISOU  414  CE1 PHE A 610    14740  15432  16308   2172   -860   2713       C  
ATOM    415  CE2 PHE A 610     -27.724 205.916-206.175  1.00121.05           C  
ANISOU  415  CE2 PHE A 610    14121  15331  16540   2013   -699   2318       C  
ATOM    416  CZ  PHE A 610     -27.937 206.041-207.535  1.00123.32           C  
ANISOU  416  CZ  PHE A 610    14543  15629  16683   2171   -880   2599       C  
ATOM    417  N   PRO A 611     -21.843 202.066-205.787  1.00111.27           N  
ANISOU  417  N   PRO A 611    13953  13953  14373   1175   -468   1727       N  
ATOM    418  CA  PRO A 611     -20.431 201.815-205.503  1.00113.57           C  
ANISOU  418  CA  PRO A 611    14386  14116  14649   1078   -323   1584       C  
ATOM    419  C   PRO A 611     -19.553 202.367-206.619  1.00123.83           C  
ANISOU  419  C   PRO A 611    15873  15235  15942   1196   -184   1751       C  
ATOM    420  O   PRO A 611     -18.395 201.975-206.739  1.00127.58           O  
ANISOU  420  O   PRO A 611    16486  15629  16358   1126    -93   1679       O  
ATOM    421  CB  PRO A 611     -20.357 200.292-205.487  1.00107.17           C  
ANISOU  421  CB  PRO A 611    13670  13471  13577    906   -522   1507       C  
ATOM    422  CG  PRO A 611     -21.403 199.877-206.453  1.00106.68           C  
ANISOU  422  CG  PRO A 611    13621  13554  13358    960   -769   1662       C  
ATOM    423  CD  PRO A 611     -22.524 200.862-206.294  1.00108.04           C  
ANISOU  423  CD  PRO A 611    13578  13752  13719   1091   -755   1769       C  
ATOM    424  N   GLU A 612     -20.104 203.263-207.432  1.00130.06           N  
ANISOU  424  N   GLU A 612    16653  15967  16796   1388   -155   1999       N  
ATOM    425  CA  GLU A 612     -19.354 203.860-208.530  1.00135.46           C  
ANISOU  425  CA  GLU A 612    17504  16496  17467   1534     20   2244       C  
ATOM    426  C   GLU A 612     -18.560 205.068-208.052  1.00132.19           C  
ANISOU  426  C   GLU A 612    16983  15740  17502   1561    331   2230       C  
ATOM    427  O   GLU A 612     -17.336 205.015-207.946  1.00131.56           O  
ANISOU  427  O   GLU A 612    16961  15507  17519   1478    506   2143       O  
ATOM    428  CB  GLU A 612     -20.299 204.258-209.667  1.00144.77           C  
ANISOU  428  CB  GLU A 612    18732  17782  18490   1761    -99   2566       C  
ATOM    429  CG  GLU A 612     -21.033 203.081-210.284  1.00148.72           C  
ANISOU  429  CG  GLU A 612    19332  18603  18573   1750   -448   2545       C  
ATOM    430  CD  GLU A 612     -20.086 202.068-210.900  1.00150.22           C  
ANISOU  430  CD  GLU A 612    19772  18877  18428   1692   -472   2473       C  
ATOM    431  OE1 GLU A 612     -19.204 202.482-211.683  1.00152.13           O  
ANISOU  431  OE1 GLU A 612    20184  19032  18586   1821   -251   2659       O  
ATOM    432  OE2 GLU A 612     -20.223 200.863-210.597  1.00149.07           O1-
ANISOU  432  OE2 GLU A 612    19638  18872  18131   1524   -693   2242       O1-
ATOM    433  N   ALA A 613     -19.266 206.158-207.771  1.00128.53           N  
ANISOU  433  N   ALA A 613    16339  15140  17357   1681    387   2298       N  
ATOM    434  CA  ALA A 613     -18.640 207.354-207.230  1.00123.77           C  
ANISOU  434  CA  ALA A 613    15589  14168  17270   1707    646   2227       C  
ATOM    435  C   ALA A 613     -18.828 207.362-205.725  1.00116.63           C  
ANISOU  435  C   ALA A 613    14480  13283  16549   1597    598   1806       C  
ATOM    436  O   ALA A 613     -19.751 207.986-205.211  1.00115.15           O  
ANISOU  436  O   ALA A 613    14110  13087  16553   1692    566   1742       O  
ATOM    437  CB  ALA A 613     -19.248 208.593-207.848  1.00128.56           C  
ANISOU  437  CB  ALA A 613    16119  14570  18158   1935    746   2550       C  
ATOM    438  N   GLY A 614     -17.943 206.660-205.028  1.00115.30           N  
ANISOU  438  N   GLY A 614    14345  13163  16302   1424    594   1522       N  
ATOM    439  CA  GLY A 614     -18.090 206.422-203.605  1.00116.82           C  
ANISOU  439  CA  GLY A 614    14389  13479  16517   1338    521   1136       C  
ATOM    440  C   GLY A 614     -18.299 207.663-202.762  1.00118.65           C  
ANISOU  440  C   GLY A 614    14391  13500  17192   1443    626    911       C  
ATOM    441  O   GLY A 614     -19.149 207.684-201.872  1.00119.18           O  
ANISOU  441  O   GLY A 614    14314  13752  17218   1484    553    721       O  
ATOM    442  N   THR A 615     -17.528 208.704-203.050  1.00120.62           N  
ANISOU  442  N   THR A 615    14588  13350  17892   1496    811    932       N  
ATOM    443  CA  THR A 615     -17.559 209.916-202.242  1.00125.86           C  
ANISOU  443  CA  THR A 615    15019  13736  19066   1592    900    648       C  
ATOM    444  C   THR A 615     -18.746 210.823-202.584  1.00129.22           C  
ANISOU  444  C   THR A 615    15330  14063  19704   1790    925    851       C  
ATOM    445  O   THR A 615     -19.293 211.497-201.709  1.00130.80           O  
ANISOU  445  O   THR A 615    15330  14215  20151   1894    920    561       O  
ATOM    446  CB  THR A 615     -16.233 210.697-202.358  1.00129.83           C  
ANISOU  446  CB  THR A 615    15457  13781  20090   1551   1082    563       C  
ATOM    447  OG1 THR A 615     -16.343 211.939-201.654  1.00133.03           O  
ANISOU  447  OG1 THR A 615    15620  13864  21063   1658   1144    270       O  
ATOM    448  CG2 THR A 615     -15.891 210.970-203.820  1.00132.83           C  
ANISOU  448  CG2 THR A 615    15964  13936  20569   1588   1257   1090       C  
ATOM    449  N   LEU A 616     -19.144 210.826-203.855  1.00130.32           N  
ANISOU  449  N   LEU A 616    15596  14194  19728   1868    940   1336       N  
ATOM    450  CA  LEU A 616     -20.261 211.651-204.318  1.00132.06           C  
ANISOU  450  CA  LEU A 616    15716  14326  20135   2081    940   1593       C  
ATOM    451  C   LEU A 616     -21.600 211.166-203.769  1.00130.60           C  
ANISOU  451  C   LEU A 616    15431  14528  19664   2125    749   1480       C  
ATOM    452  O   LEU A 616     -22.581 211.910-203.755  1.00131.82           O  
ANISOU  452  O   LEU A 616    15421  14621  20043   2307    740   1548       O  
ATOM    453  CB  LEU A 616     -20.309 211.684-205.848  1.00132.31           C  
ANISOU  453  CB  LEU A 616    15930  14318  20024   2181    976   2157       C  
ATOM    454  CG  LEU A 616     -19.149 212.398-206.543  1.00134.23           C  
ANISOU  454  CG  LEU A 616    16231  14141  20629   2195   1241   2403       C  
ATOM    455  CD1 LEU A 616     -19.327 212.370-208.052  1.00136.17           C  
ANISOU  455  CD1 LEU A 616    16678  14450  20609   2348   1279   2995       C  
ATOM    456  CD2 LEU A 616     -19.031 213.829-206.043  1.00137.57           C  
ANISOU  456  CD2 LEU A 616    16407  14058  21805   2290   1413   2285       C  
ATOM    457  N   THR A 617     -21.630 209.918-203.309  1.00127.46           N  
ANISOU  457  N   THR A 617    15109  14509  18811   1960    610   1324       N  
ATOM    458  CA  THR A 617     -22.850 209.311-202.783  1.00125.34           C  
ANISOU  458  CA  THR A 617    14726  14618  18281   1967    455   1256       C  
ATOM    459  C   THR A 617     -23.382 210.008-201.535  1.00126.59           C  
ANISOU  459  C   THR A 617    14626  14778  18694   2074    527    901       C  
ATOM    460  O   THR A 617     -24.509 209.760-201.113  1.00128.75           O  
ANISOU  460  O   THR A 617    14746  15328  18844   2130    457    880       O  
ATOM    461  CB  THR A 617     -22.636 207.828-202.461  1.00121.06           C  
ANISOU  461  CB  THR A 617    14304  14421  17272   1753    325   1171       C  
ATOM    462  OG1 THR A 617     -21.516 207.689-201.578  1.00119.17           O  
ANISOU  462  OG1 THR A 617    14098  14122  17060   1642    410    842       O  
ATOM    463  CG2 THR A 617     -22.364 207.056-203.729  1.00119.89           C  
ANISOU  463  CG2 THR A 617    14392  14326  16835   1683    215   1487       C  
ATOM    464  N   ALA A 618     -22.572 210.880-200.948  1.00126.92           N  
ANISOU  464  N   ALA A 618    14603  14512  19109   2113    666    604       N  
ATOM    465  CA  ALA A 618     -23.005 211.654-199.794  1.00130.62           C  
ANISOU  465  CA  ALA A 618    14833  14959  19837   2259    730    203       C  
ATOM    466  C   ALA A 618     -23.961 212.768-200.211  1.00131.97           C  
ANISOU  466  C   ALA A 618    14829  14904  20410   2495    778    361       C  
ATOM    467  O   ALA A 618     -24.498 213.485-199.365  1.00132.62           O  
ANISOU  467  O   ALA A 618    14693  14958  20739   2662    833     45       O  
ATOM    468  CB  ALA A 618     -21.803 212.230-199.062  1.00134.37           C  
ANISOU  468  CB  ALA A 618    15280  15156  20621   2233    814   -224       C  
ATOM    469  N   VAL A 619     -24.169 212.911-201.518  1.00132.68           N  
ANISOU  469  N   VAL A 619    15017  14847  20549   2537    752    846       N  
ATOM    470  CA  VAL A 619     -25.058 213.944-202.040  1.00137.37           C  
ANISOU  470  CA  VAL A 619    15459  15217  21520   2782    777   1075       C  
ATOM    471  C   VAL A 619     -26.511 213.482-201.993  1.00133.26           C  
ANISOU  471  C   VAL A 619    14800  15092  20740   2868    637   1181       C  
ATOM    472  O   VAL A 619     -27.435 214.281-202.153  1.00135.27           O  
ANISOU  472  O   VAL A 619    14864  15237  21295   3094    638   1285       O  
ATOM    473  CB  VAL A 619     -24.692 214.333-203.491  1.00141.87           C  
ANISOU  473  CB  VAL A 619    16193  15492  22219   2836    810   1602       C  
ATOM    474  CG1 VAL A 619     -25.279 213.331-204.481  1.00140.96           C  
ANISOU  474  CG1 VAL A 619    16238  15751  21567   2804    618   2001       C  
ATOM    475  CG2 VAL A 619     -25.173 215.744-203.806  1.00145.94           C  
ANISOU  475  CG2 VAL A 619    16534  15585  23331   3103    906   1766       C  
ATOM    476  N   MET A 620     -26.706 212.189-201.760  1.00126.48           N  
ANISOU  476  N   MET A 620    14012  14672  19374   2687    517   1160       N  
ATOM    477  CA  MET A 620     -28.040 211.607-201.774  1.00124.92           C  
ANISOU  477  CA  MET A 620    13658  14846  18959   2723    377   1288       C  
ATOM    478  C   MET A 620     -28.629 211.475-200.375  1.00128.03           C  
ANISOU  478  C   MET A 620    13814  15512  19317   2747    463    915       C  
ATOM    479  O   MET A 620     -29.783 211.076-200.214  1.00132.90           O  
ANISOU  479  O   MET A 620    14232  16430  19833   2784    399    995       O  
ATOM    480  CB  MET A 620     -28.014 210.246-202.466  1.00119.94           C  
ANISOU  480  CB  MET A 620    13214  14500  17855   2517    183   1530       C  
ATOM    481  CG  MET A 620     -27.635 210.318-203.936  1.00120.62           C  
ANISOU  481  CG  MET A 620    13530  14418  17883   2551     84   1921       C  
ATOM    482  SD  MET A 620     -28.816 211.251-204.932  1.00200.59           S  
ANISOU  482  SD  MET A 620    23509  24445  28262   2862    -26   2296       S  
ATOM    483  CE  MET A 620     -27.976 211.267-206.513  1.00114.91           C  
ANISOU  483  CE  MET A 620    13006  13432  17224   2902    -73   2730       C  
ATOM    484  N   ILE A 621     -27.840 211.819-199.365  1.00125.74           N  
ANISOU  484  N   ILE A 621    13530  15134  19113   2741    610    506       N  
ATOM    485  CA  ILE A 621     -28.294 211.731-197.983  1.00124.99           C  
ANISOU  485  CA  ILE A 621    13237  15339  18913   2807    715    127       C  
ATOM    486  C   ILE A 621     -28.802 213.074-197.468  1.00129.30           C  
ANISOU  486  C   ILE A 621    13536  15679  19913   3102    842   -148       C  
ATOM    487  O   ILE A 621     -28.072 214.064-197.459  1.00129.03           O  
ANISOU  487  O   ILE A 621    13528  15224  20272   3192    904   -355       O  
ATOM    488  CB  ILE A 621     -27.175 211.225-197.060  1.00122.16           C  
ANISOU  488  CB  ILE A 621    13026  15092  18296   2665    763   -214       C  
ATOM    489  CG1 ILE A 621     -26.661 209.871-197.551  1.00117.88           C  
ANISOU  489  CG1 ILE A 621    12721  14729  17341   2386    638     49       C  
ATOM    490  CG2 ILE A 621     -27.675 211.132-195.626  1.00124.99           C  
ANISOU  490  CG2 ILE A 621    13198  15828  18466   2782    883   -579       C  
ATOM    491  CD1 ILE A 621     -25.562 209.286-196.702  1.00116.59           C  
ANISOU  491  CD1 ILE A 621    12701  14684  16913   2253    659   -235       C  
ATOM    492  N   ARG A 622     -30.058 213.101-197.041  1.00134.45           N  
ANISOU  492  N   ARG A 622    13922  16606  20555   3254    887   -159       N  
ATOM    493  CA  ARG A 622     -30.644 214.316-196.488  1.00141.61           C  
ANISOU  493  CA  ARG A 622    14567  17357  21880   3564   1015   -455       C  
ATOM    494  C   ARG A 622     -30.011 214.662-195.143  1.00145.73           C  
ANISOU  494  C   ARG A 622    15068  17936  22367   3651   1152  -1059       C  
ATOM    495  O   ARG A 622     -30.710 214.945-194.171  1.00151.03           O  
ANISOU  495  O   ARG A 622    15511  18860  23015   3863   1284  -1375       O  
ATOM    496  CB  ARG A 622     -32.156 214.168-196.350  1.00143.48           C  
ANISOU  496  CB  ARG A 622    14499  17922  22094   3707   1042   -313       C  
ATOM    497  N   GLU A 629     -40.290 221.198-197.594  1.00197.94           N  
ANISOU  497  N   GLU A 629    18904  23674  32631   6220   1198    -31       N  
ATOM    498  CA  GLU A 629     -39.790 222.554-197.794  1.00201.31           C  
ANISOU  498  CA  GLU A 629    19448  23466  33576   6408   1211   -165       C  
ATOM    499  C   GLU A 629     -39.337 222.761-199.236  1.00200.19           C  
ANISOU  499  C   GLU A 629    19565  22917  33580   6331    980    426       C  
ATOM    500  O   GLU A 629     -40.028 223.402-200.028  1.00203.88           O  
ANISOU  500  O   GLU A 629    19976  23201  34287   6498    834    764       O  
ATOM    501  CB  GLU A 629     -38.649 222.845-196.829  1.00199.95           C  
ANISOU  501  CB  GLU A 629    19472  23130  33372   6333   1389   -744       C  
ATOM    502  N   GLN A 630     -38.172 222.214-199.568  1.00194.76           N  
ANISOU  502  N   GLN A 630    19199  22135  32667   6068    949    551       N  
ATOM    503  CA  GLN A 630     -37.637 222.314-200.919  1.00192.52           C  
ANISOU  503  CA  GLN A 630    19192  21528  32430   5994    773   1128       C  
ATOM    504  C   GLN A 630     -38.444 221.452-201.886  1.00189.17           C  
ANISOU  504  C   GLN A 630    18753  21506  31618   5938    506   1661       C  
ATOM    505  O   GLN A 630     -38.543 221.762-203.074  1.00190.16           O  
ANISOU  505  O   GLN A 630    18973  21419  31861   6054    325   2185       O  
ATOM    506  CB  GLN A 630     -36.169 221.910-200.939  1.00188.92           C  
ANISOU  506  CB  GLN A 630    19129  20948  31705   5671    825   1062       C  
ATOM    507  N   THR A 631     -39.015 220.369-201.366  1.00184.90           N  
ANISOU  507  N   THR A 631    18084  21546  30622   5769    478   1524       N  
ATOM    508  CA  THR A 631     -39.834 219.463-202.165  1.00181.06           C  
ANISOU  508  CA  THR A 631    17526  21459  29809   5690    198   1935       C  
ATOM    509  C   THR A 631     -41.074 220.182-202.687  1.00183.17           C  
ANISOU  509  C   THR A 631    17440  21645  30512   6058     53   2186       C  
ATOM    510  O   THR A 631     -41.447 220.031-203.851  1.00182.54           O  
ANISOU  510  O   THR A 631    17403  21597  30357   6121   -246   2663       O  
ATOM    511  CB  THR A 631     -40.261 218.221-201.351  1.00178.16           C  
ANISOU  511  CB  THR A 631    17015  21678  29001   5440    242   1711       C  
ATOM    512  OG1 THR A 631     -39.098 217.542-200.859  1.00174.05           O  
ANISOU  512  OG1 THR A 631    16825  21233  28073   5121    361   1497       O  
ATOM    513  CG2 THR A 631     -41.070 217.264-202.214  1.00177.10           C  
ANISOU  513  CG2 THR A 631    16783  21900  28609   5332    -83   2102       C  
ATOM    514  N   THR A 632     -41.699 220.974-201.821  1.00186.17           N  
ANISOU  514  N   THR A 632    17468  21932  31338   6326    257   1845       N  
ATOM    515  CA  THR A 632     -42.873 221.752-202.196  1.00190.83           C  
ANISOU  515  CA  THR A 632    17818  22468  32223   6604    132   1974       C  
ATOM    516  C   THR A 632     -42.503 222.851-203.185  1.00195.15           C  
ANISOU  516  C   THR A 632    18645  22487  33017   6750     21   2287       C  
ATOM    517  O   THR A 632     -43.341 223.309-203.965  1.00198.59           O  
ANISOU  517  O   THR A 632    18990  22889  33575   6948   -192   2595       O  
ATOM    518  CB  THR A 632     -43.532 222.345-200.962  1.00192.63           C  
ANISOU  518  CB  THR A 632    17732  22767  32693   6782    400   1447       C  
ATOM    519  N   VAL A 633     -41.242 223.271-203.145  1.00195.08           N  
ANISOU  519  N   VAL A 633    18963  22072  33087   6647    173   2213       N  
ATOM    520  CA  VAL A 633     -40.736 224.287-204.061  1.00198.02           C  
ANISOU  520  CA  VAL A 633    19613  21924  33702   6735    127   2546       C  
ATOM    521  C   VAL A 633     -40.564 223.708-205.461  1.00194.87           C  
ANISOU  521  C   VAL A 633    19463  21638  32941   6676   -146   3182       C  
ATOM    522  O   VAL A 633     -41.073 224.257-206.439  1.00198.82           O  
ANISOU  522  O   VAL A 633    20007  22034  33500   6864   -334   3590       O  
ATOM    523  CB  VAL A 633     -39.419 224.852-203.549  1.00197.19           C  
ANISOU  523  CB  VAL A 633    19745  21366  33811   6600    380   2252       C  
ATOM    524  N   ASP A 634     -39.841 222.596-205.549  1.00186.77           N  
ANISOU  524  N   ASP A 634    18608  20848  31507   6430   -173   3250       N  
ATOM    525  CA  ASP A 634     -39.661 221.900-206.816  1.00181.89           C  
ANISOU  525  CA  ASP A 634    18242  20423  30443   6369   -445   3789       C  
ATOM    526  C   ASP A 634     -40.933 221.150-207.193  1.00177.82           C  
ANISOU  526  C   ASP A 634    17467  20419  29678   6443   -780   3934       C  
ATOM    527  O   ASP A 634     -41.069 219.958-206.915  1.00174.05           O  
ANISOU  527  O   ASP A 634    16874  20361  28895   6260   -878   3843       O  
ATOM    528  CB  ASP A 634     -38.480 220.931-206.735  1.00177.76           C  
ANISOU  528  CB  ASP A 634    17986  19998  29556   6077   -369   3767       C  
ATOM    529  CG  ASP A 634     -37.141 221.641-206.728  1.00178.38           C  
ANISOU  529  CG  ASP A 634    18363  19556  29858   5999   -102   3754       C  
ATOM    530  OD1 ASP A 634     -36.968 222.592-207.518  1.00182.30           O  
ANISOU  530  OD1 ASP A 634    19032  19702  30533   6119    -90   4076       O  
ATOM    531  OD2 ASP A 634     -36.262 221.248-205.931  1.00175.22           O1-
ANISOU  531  OD2 ASP A 634    18073  19150  29354   5735     87   3364       O1-
ATOM    532  N   GLU A 635     -41.865 221.859-207.823  1.00178.45           N  
ANISOU  532  N   GLU A 635    17437  20451  29914   6702   -964   4152       N  
ATOM    533  CA  GLU A 635     -43.121 221.260-208.258  1.00175.57           C  
ANISOU  533  CA  GLU A 635    16804  20536  29366   6788  -1321   4273       C  
ATOM    534  C   GLU A 635     -42.874 220.231-209.353  1.00169.26           C  
ANISOU  534  C   GLU A 635    16260  20060  27989   6670  -1663   4627       C  
ATOM    535  O   GLU A 635     -43.660 219.299-209.532  1.00167.79           O  
ANISOU  535  O   GLU A 635    15861  20317  27574   6607  -1966   4617       O  
ATOM    536  CB  GLU A 635     -44.082 222.335-208.744  1.00181.35           C  
ANISOU  536  CB  GLU A 635    17395  21108  30403   7121  -1450   4432       C  
ATOM    537  N   LYS A 636     -41.782 220.415-210.088  1.00165.92           N  
ANISOU  537  N   LYS A 636    16289  19413  27339   6634  -1611   4918       N  
ATOM    538  CA  LYS A 636     -41.389 219.481-211.134  1.00162.79           C  
ANISOU  538  CA  LYS A 636    16203  19318  26331   6535  -1896   5219       C  
ATOM    539  C   LYS A 636     -41.176 218.102-210.525  1.00156.91           C  
ANISOU  539  C   LYS A 636    15357  18931  25329   6232  -1935   4972       C  
ATOM    540  O   LYS A 636     -41.632 217.092-211.064  1.00156.42           O  
ANISOU  540  O   LYS A 636    15265  19292  24877   6152  -2302   5032       O  
ATOM    541  CB  LYS A 636     -40.121 219.961-211.823  1.00161.58           C  
ANISOU  541  CB  LYS A 636    16536  18839  26017   6525  -1710   5525       C  
ATOM    542  N   CYS A 637     -40.489 218.082-209.387  1.00152.04           N  
ANISOU  542  N   CYS A 637    14750  18151  24868   5999  -1558   4590       N  
ATOM    543  CA  CYS A 637     -40.221 216.856-208.652  1.00146.01           C  
ANISOU  543  CA  CYS A 637    14014  17712  23751   5584  -1510   4203       C  
ATOM    544  C   CYS A 637     -41.515 216.218-208.153  1.00148.68           C  
ANISOU  544  C   CYS A 637    13893  18439  24160   5540  -1682   4002       C  
ATOM    545  O   CYS A 637     -41.639 214.996-208.116  1.00146.82           O  
ANISOU  545  O   CYS A 637    13653  18563  23568   5253  -1848   3885       O  
ATOM    546  CB  CYS A 637     -39.286 217.141-207.476  1.00142.05           C  
ANISOU  546  CB  CYS A 637    13602  16954  23418   5400  -1070   3815       C  
ATOM    547  SG  CYS A 637     -37.639 217.716-207.954  1.00170.25           S  
ANISOU  547  SG  CYS A 637    17671  20064  26951   5359   -843   3997       S  
ATOM    548  N   LEU A 638     -42.474 217.055-207.770  1.00154.42           N  
ANISOU  548  N   LEU A 638    14210  19069  25393   5828  -1630   3967       N  
ATOM    549  CA  LEU A 638     -43.773 216.579-207.310  1.00158.16           C  
ANISOU  549  CA  LEU A 638    14179  19890  26024   5828  -1758   3813       C  
ATOM    550  C   LEU A 638     -44.511 215.886-208.450  1.00163.19           C  
ANISOU  550  C   LEU A 638    14738  20841  26426   5864  -2285   4099       C  
ATOM    551  O   LEU A 638     -45.087 214.810-208.273  1.00163.29           O  
ANISOU  551  O   LEU A 638    14526  21216  26303   5628  -2461   3960       O  
ATOM    552  CB  LEU A 638     -44.609 217.747-206.780  1.00161.31           C  
ANISOU  552  CB  LEU A 638    14161  20084  27043   6191  -1592   3740       C  
ATOM    553  CG  LEU A 638     -45.990 217.410-206.213  1.00162.32           C  
ANISOU  553  CG  LEU A 638    13740  20554  27382   6207  -1644   3550       C  
ATOM    554  CD1 LEU A 638     -45.855 216.690-204.884  1.00158.30           C  
ANISOU  554  CD1 LEU A 638    13073  20273  26801   5921  -1301   3160       C  
ATOM    555  CD2 LEU A 638     -46.848 218.658-206.068  1.00167.28           C  
ANISOU  555  CD2 LEU A 638    14147  20980  28430   6540  -1561   3468       C  
ATOM    556  N   ALA A 639     -44.485 216.512-209.623  1.00167.01           N  
ANISOU  556  N   ALA A 639    15424  21180  26852   6154  -2535   4480       N  
ATOM    557  CA  ALA A 639     -45.149 215.968-210.801  1.00169.06           C  
ANISOU  557  CA  ALA A 639    15708  21746  26781   6213  -3064   4675       C  
ATOM    558  C   ALA A 639     -44.510 214.654-211.219  1.00163.89           C  
ANISOU  558  C   ALA A 639    15295  21363  25613   5923  -3284   4691       C  
ATOM    559  O   ALA A 639     -45.206 213.674-211.482  1.00164.02           O  
ANISOU  559  O   ALA A 639    15098  21729  25493   5787  -3655   4597       O  
ATOM    560  CB  ALA A 639     -45.101 216.967-211.944  1.00174.14           C  
ANISOU  560  CB  ALA A 639    16667  22185  27315   6546  -3210   5014       C  
ATOM    561  N   PHE A 640     -43.182 214.645-211.278  1.00160.40           N  
ANISOU  561  N   PHE A 640    15350  20733  24860   5774  -3035   4715       N  
ATOM    562  CA  PHE A 640     -42.435 213.446-211.643  1.00157.33           C  
ANISOU  562  CA  PHE A 640    15310  20558  23910   5449  -3168   4625       C  
ATOM    563  C   PHE A 640     -42.733 212.314-210.665  1.00154.16           C  
ANISOU  563  C   PHE A 640    14655  20387  23533   5046  -3118   4227       C  
ATOM    564  O   PHE A 640     -42.939 211.171-211.072  1.00152.53           O  
ANISOU  564  O   PHE A 640    14446  20465  23042   4843  -3453   4145       O  
ATOM    565  CB  PHE A 640     -40.932 213.733-211.659  1.00155.18           C  
ANISOU  565  CB  PHE A 640    15548  20003  23410   5355  -2817   4688       C  
ATOM    566  CG  PHE A 640     -40.147 212.820-212.562  1.00154.41           C  
ANISOU  566  CG  PHE A 640    15883  20093  22691   5208  -3026   4769       C  
ATOM    567  CD1 PHE A 640     -39.827 211.532-212.169  1.00150.86           C  
ANISOU  567  CD1 PHE A 640    15498  19854  21968   4810  -3065   4451       C  
ATOM    568  CD2 PHE A 640     -39.724 213.258-213.806  1.00157.51           C  
ANISOU  568  CD2 PHE A 640    16619  20455  22774   5493  -3165   5177       C  
ATOM    569  CE1 PHE A 640     -39.104 210.697-213.003  1.00149.32           C  
ANISOU  569  CE1 PHE A 640    15693  19817  21223   4698  -3259   4488       C  
ATOM    570  CE2 PHE A 640     -39.000 212.428-214.642  1.00155.98           C  
ANISOU  570  CE2 PHE A 640    16823  20465  21976   5395  -3337   5227       C  
ATOM    571  CZ  PHE A 640     -38.691 211.147-214.240  1.00151.68           C  
ANISOU  571  CZ  PHE A 640    16332  20113  21187   4997  -3392   4856       C  
ATOM    572  N   ALA A 641     -42.757 212.646-209.377  1.00154.15           N  
ANISOU  572  N   ALA A 641    14436  20255  23878   4950  -2696   3983       N  
ATOM    573  CA  ALA A 641     -43.042 211.676-208.323  1.00152.52           C  
ANISOU  573  CA  ALA A 641    13972  20265  23713   4603  -2561   3661       C  
ATOM    574  C   ALA A 641     -44.437 211.083-208.469  1.00157.41           C  
ANISOU  574  C   ALA A 641    14081  21184  24542   4600  -2908   3655       C  
ATOM    575  O   ALA A 641     -44.609 209.864-208.441  1.00157.91           O  
ANISOU  575  O   ALA A 641    14063  21478  24457   4293  -3091   3539       O  
ATOM    576  CB  ALA A 641     -42.889 212.320-206.956  1.00150.72           C  
ANISOU  576  CB  ALA A 641    13594  19878  23794   4604  -2046   3420       C  
ATOM    577  N   GLU A 642     -45.432 211.952-208.620  1.00160.98           N  
ANISOU  577  N   GLU A 642    14164  21607  25394   4944  -3003   3778       N  
ATOM    578  CA  GLU A 642     -46.809 211.514-208.810  1.00164.44           C  
ANISOU  578  CA  GLU A 642    14058  22311  26110   4983  -3354   3783       C  
ATOM    579  C   GLU A 642     -46.937 210.695-210.091  1.00165.20           C  
ANISOU  579  C   GLU A 642    14289  22608  25872   4942  -3956   3902       C  
ATOM    580  O   GLU A 642     -47.850 209.881-210.233  1.00168.66           O  
ANISOU  580  O   GLU A 642    14332  23290  26462   4816  -4296   3818       O  
ATOM    581  CB  GLU A 642     -47.746 212.714-208.849  1.00169.05           C  
ANISOU  581  CB  GLU A 642    14262  22794  27176   5417  -3362   3917       C  
ATOM    582  N   LEU A 643     -46.011 210.917-211.020  1.00161.46           N  
ANISOU  582  N   LEU A 643    14360  22032  24955   5058  -4081   4084       N  
ATOM    583  CA  LEU A 643     -46.014 210.208-212.293  1.00159.93           C  
ANISOU  583  CA  LEU A 643    14369  22052  24346   5079  -4644   4173       C  
ATOM    584  C   LEU A 643     -45.420 208.806-212.156  1.00155.04           C  
ANISOU  584  C   LEU A 643    13944  21559  23404   4630  -4696   3922       C  
ATOM    585  O   LEU A 643     -45.889 207.862-212.793  1.00157.11           O  
ANISOU  585  O   LEU A 643    14092  22053  23549   4529  -5187   3821       O  
ATOM    586  CB  LEU A 643     -45.255 211.016-213.350  1.00158.38           C  
ANISOU  586  CB  LEU A 643    14680  21727  23770   5419  -4710   4507       C  
ATOM    587  CG  LEU A 643     -45.178 210.448-214.768  1.00158.29           C  
ANISOU  587  CG  LEU A 643    14984  21964  23195   5528  -5253   4587       C  
ATOM    588  CD1 LEU A 643     -46.564 210.099-215.284  1.00163.96           C  
ANISOU  588  CD1 LEU A 643    15327  22951  24018   5622  -5772   4420       C  
ATOM    589  CD2 LEU A 643     -44.489 211.435-215.700  1.00158.31           C  
ANISOU  589  CD2 LEU A 643    15507  21807  22835   5874  -5174   4921       C  
ATOM    590  N   ILE A 644     -44.395 208.676-211.318  1.00149.81           N  
ANISOU  590  N   ILE A 644    13559  20731  22631   4373  -4211   3802       N  
ATOM    591  CA  ILE A 644     -43.718 207.396-211.108  1.00146.67           C  
ANISOU  591  CA  ILE A 644    13373  20408  21947   3958  -4206   3586       C  
ATOM    592  C   ILE A 644     -44.626 206.366-210.434  1.00147.95           C  
ANISOU  592  C   ILE A 644    13028  20739  22447   3648  -4301   3376       C  
ATOM    593  O   ILE A 644     -44.523 205.164-210.688  1.00146.90           O  
ANISOU  593  O   ILE A 644    12937  20713  22165   3367  -4563   3229       O  
ATOM    594  CB  ILE A 644     -42.413 207.580-210.294  1.00141.31           C  
ANISOU  594  CB  ILE A 644    13077  19510  21106   3786  -3657   3517       C  
ATOM    595  CG1 ILE A 644     -41.394 208.375-211.108  1.00141.13           C  
ANISOU  595  CG1 ILE A 644    13570  19308  20744   4029  -3594   3736       C  
ATOM    596  CG2 ILE A 644     -41.808 206.244-209.913  1.00137.01           C  
ANISOU  596  CG2 ILE A 644    12681  19036  20340   3361  -3626   3298       C  
ATOM    597  CD1 ILE A 644     -41.095 207.762-212.458  1.00142.41           C  
ANISOU  597  CD1 ILE A 644    14061  19635  20415   4087  -4042   3826       C  
ATOM    598  N   ARG A 645     -45.539 206.848-209.597  1.00150.03           N  
ANISOU  598  N   ARG A 645    12790  21013  23202   3713  -4084   3372       N  
ATOM    599  CA  ARG A 645     -46.467 205.984-208.874  1.00151.59           C  
ANISOU  599  CA  ARG A 645    12439  21363  23795   3441  -4088   3235       C  
ATOM    600  C   ARG A 645     -47.397 205.196-209.810  1.00155.46           C  
ANISOU  600  C   ARG A 645    12614  22034  24419   3406  -4739   3201       C  
ATOM    601  O   ARG A 645     -48.097 204.281-209.375  1.00157.54           O  
ANISOU  601  O   ARG A 645    12432  22395  25031   3123  -4813   3090       O  
ATOM    602  CB  ARG A 645     -47.283 206.817-207.878  1.00156.04           C  
ANISOU  602  CB  ARG A 645    12521  21926  24840   3601  -3705   3257       C  
ATOM    603  CG  ARG A 645     -47.929 206.024-206.749  1.00158.84           C  
ANISOU  603  CG  ARG A 645    12382  22419  25550   3295  -3440   3150       C  
ATOM    604  CD  ARG A 645     -46.907 205.170-206.008  1.00154.73           C  
ANISOU  604  CD  ARG A 645    12191  21867  24730   2925  -3112   3046       C  
ATOM    605  NE  ARG A 645     -47.416 204.691-204.725  1.00155.93           N  
ANISOU  605  NE  ARG A 645    11916  22148  25182   2713  -2698   3010       N  
ATOM    606  CZ  ARG A 645     -48.304 203.710-204.585  1.00157.76           C  
ANISOU  606  CZ  ARG A 645    11655  22512  25776   2465  -2840   3035       C  
ATOM    607  NH1 ARG A 645     -48.795 203.097-205.655  1.00159.71           N1+
ANISOU  607  NH1 ARG A 645    11761  22769  26150   2393  -3439   3031       N1+
ATOM    608  NH2 ARG A 645     -48.704 203.343-203.374  1.00157.85           N  
ANISOU  608  NH2 ARG A 645    11297  22648  26030   2300  -2383   3062       N  
ATOM    609  N   ASP A 646     -47.399 205.548-211.094  1.00157.15           N  
ANISOU  609  N   ASP A 646    13050  22295  24367   3701  -5214   3300       N  
ATOM    610  CA  ASP A 646     -48.206 204.837-212.085  1.00162.22           C  
ANISOU  610  CA  ASP A 646    13441  23129  25066   3716  -5908   3215       C  
ATOM    611  C   ASP A 646     -47.528 203.544-212.529  1.00161.10           C  
ANISOU  611  C   ASP A 646    13616  23019  24574   3398  -6171   3007       C  
ATOM    612  O   ASP A 646     -46.337 203.532-212.833  1.00157.42           O  
ANISOU  612  O   ASP A 646    13751  22478  23582   3396  -6042   3023       O  
ATOM    613  CB  ASP A 646     -48.484 205.731-213.284  1.00166.56           C  
ANISOU  613  CB  ASP A 646    14208  23761  25316   4182  -6242   3340       C  
ATOM    614  N   LYS A 647     -48.295 202.458-212.570  1.00165.05           N  
ANISOU  614  N   LYS A 647    13725  23610  25378   3125  -6500   2781       N  
ATOM    615  CA  LYS A 647     -47.755 201.143-212.909  1.00163.54           C  
ANISOU  615  CA  LYS A 647    13741  23406  24990   2802  -6775   2547       C  
ATOM    616  C   LYS A 647     -47.443 201.005-214.396  1.00166.00           C  
ANISOU  616  C   LYS A 647    14512  23867  24694   3038  -7300   2419       C  
ATOM    617  O   LYS A 647     -46.337 200.612-214.770  1.00163.72           O  
ANISOU  617  O   LYS A 647    14721  23537  23949   2993  -7352   2374       O  
ATOM    618  CB  LYS A 647     -48.707 200.042-212.462  1.00165.91           C  
ANISOU  618  CB  LYS A 647    13501  23705  25831   2417  -6869   2325       C  
ATOM    619  N   GLN A 648     -48.425 201.319-215.237  1.00170.41           N  
ANISOU  619  N   GLN A 648    14895  24628  25225   3300  -7667   2365       N  
ATOM    620  CA  GLN A 648     -48.246 201.257-216.682  1.00172.60           C  
ANISOU  620  CA  GLN A 648    15566  25133  24880   3572  -8136   2280       C  
ATOM    621  C   GLN A 648     -47.099 202.156-217.127  1.00168.62           C  
ANISOU  621  C   GLN A 648    15674  24616  23776   3912  -7952   2573       C  
ATOM    622  O   GLN A 648     -46.211 201.722-217.868  1.00169.01           O  
ANISOU  622  O   GLN A 648    16218  24738  23260   3938  -8099   2500       O  
ATOM    623  CB  GLN A 648     -49.531 201.644-217.394  1.00179.32           C  
ANISOU  623  CB  GLN A 648    16076  26227  25831   3833  -8495   2268       C  
ATOM    624  N   PHE A 649     -47.119 203.404-216.661  1.00165.08           N  
ANISOU  624  N   PHE A 649    15186  24055  23483   4166  -7598   2903       N  
ATOM    625  CA  PHE A 649     -46.090 204.374-217.027  1.00160.04           C  
ANISOU  625  CA  PHE A 649    15084  23338  22387   4490  -7367   3234       C  
ATOM    626  C   PHE A 649     -44.693 203.880-216.697  1.00152.98           C  
ANISOU  626  C   PHE A 649    14630  22274  21223   4241  -7102   3219       C  
ATOM    627  O   PHE A 649     -43.809 203.907-217.543  1.00153.21           O  
ANISOU  627  O   PHE A 649    15195  22373  20644   4413  -7166   3292       O  
ATOM    628  CB  PHE A 649     -46.313 205.729-216.348  1.00158.30           C  
ANISOU  628  CB  PHE A 649    14695  22919  22533   4712  -6941   3551       C  
ATOM    629  CG  PHE A 649     -45.119 206.647-216.439  1.00153.42           C  
ANISOU  629  CG  PHE A 649    14585  22111  21595   4919  -6557   3900       C  
ATOM    630  CD1 PHE A 649     -44.846 207.334-217.610  1.00155.02           C  
ANISOU  630  CD1 PHE A 649    15218  22391  21291   5340  -6708   4122       C  
ATOM    631  CD2 PHE A 649     -44.260 206.805-215.362  1.00149.43           C  
ANISOU  631  CD2 PHE A 649    14227  21336  21213   4657  -5921   3891       C  
ATOM    632  CE1 PHE A 649     -43.744 208.170-217.704  1.00152.59           C  
ANISOU  632  CE1 PHE A 649    15374  21869  20733   5490  -6286   4450       C  
ATOM    633  CE2 PHE A 649     -43.155 207.638-215.451  1.00147.26           C  
ANISOU  633  CE2 PHE A 649    14431  20859  20664   4808  -5509   4135       C  
ATOM    634  CZ  PHE A 649     -42.900 208.323-216.625  1.00148.88           C  
ANISOU  634  CZ  PHE A 649    14969  21128  20471   5229  -5696   4466       C  
ATOM    635  N   LEU A 650     -44.496 203.441-215.460  1.00146.54           N  
ANISOU  635  N   LEU A 650    13645  21265  20768   3828  -6661   3085       N  
ATOM    636  CA  LEU A 650     -43.182 203.000-215.022  1.00139.82           C  
ANISOU  636  CA  LEU A 650    13245  20256  19625   3558  -6248   3011       C  
ATOM    637  C   LEU A 650     -42.777 201.713-215.730  1.00143.98           C  
ANISOU  637  C   LEU A 650    14005  20896  19807   3381  -6657   2722       C  
ATOM    638  O   LEU A 650     -41.593 201.461-215.942  1.00138.71           O  
ANISOU  638  O   LEU A 650    13842  20171  18691   3326  -6474   2696       O  
ATOM    639  CB  LEU A 650     -43.150 202.814-213.506  1.00134.45           C  
ANISOU  639  CB  LEU A 650    12302  19387  19396   3195  -5716   2943       C  
ATOM    640  CG  LEU A 650     -41.763 202.556-212.919  1.00127.75           C  
ANISOU  640  CG  LEU A 650    11903  18363  18274   2960  -5240   2900       C  
ATOM    641  CD1 LEU A 650     -40.762 203.562-213.461  1.00126.97           C  
ANISOU  641  CD1 LEU A 650    12318  18178  17748   3260  -5019   3127       C  
ATOM    642  CD2 LEU A 650     -41.802 202.615-211.406  1.00124.66           C  
ANISOU  642  CD2 LEU A 650    11249  17835  18279   2708  -4707   2877       C  
ATOM    643  N   SER A 651     -43.767 200.903-216.095  1.00154.27           N  
ANISOU  643  N   SER A 651    14914  22344  21359   3298  -7218   2482       N  
ATOM    644  CA  SER A 651     -43.517 199.682-216.854  1.00160.69           C  
ANISOU  644  CA  SER A 651    15898  23257  21900   3166  -7700   2142       C  
ATOM    645  C   SER A 651     -42.924 200.028-218.217  1.00161.49           C  
ANISOU  645  C   SER A 651    16552  23582  21225   3563  -7918   2200       C  
ATOM    646  O   SER A 651     -41.867 199.510-218.601  1.00159.53           O  
ANISOU  646  O   SER A 651    16775  23330  20510   3523  -7899   2082       O  
ATOM    647  CB  SER A 651     -44.813 198.886-217.028  1.00172.70           C  
ANISOU  647  CB  SER A 651    16892  24885  23841   2992  -8116   1843       C  
ATOM    648  OG  SER A 651     -44.595 197.712-217.793  1.00178.39           O  
ANISOU  648  OG  SER A 651    17807  25679  24296   2842  -8482   1464       O  
ATOM    649  N   CYS A 652     -43.607 200.914-218.939  1.00162.14           N  
ANISOU  649  N   CYS A 652    16573  23872  21161   3936  -8055   2411       N  
ATOM    650  CA  CYS A 652     -43.112 201.392-220.224  1.00162.05           C  
ANISOU  650  CA  CYS A 652    17058  24081  20432   4298  -8152   2597       C  
ATOM    651  C   CYS A 652     -41.757 202.069-220.054  1.00156.19           C  
ANISOU  651  C   CYS A 652    16833  23172  19340   4443  -7687   2901       C  
ATOM    652  O   CYS A 652     -40.888 201.964-220.914  1.00156.89           O  
ANISOU  652  O   CYS A 652    17432  23361  18819   4558  -7659   2937       O  
ATOM    653  CB  CYS A 652     -44.109 202.368-220.852  1.00167.00           C  
ANISOU  653  CB  CYS A 652    17476  24892  21085   4647  -8325   2884       C  
ATOM    654  SG  CYS A 652     -45.746 201.670-221.147  1.00218.89           S  
ANISOU  654  SG  CYS A 652    23432  31685  28052   4531  -8877   2535       S  
ATOM    655  N   PHE A 653     -41.588 202.751-218.926  1.00150.98           N  
ANISOU  655  N   PHE A 653    16029  22235  19101   4388  -7249   3100       N  
ATOM    656  CA  PHE A 653     -40.362 203.478-218.621  1.00145.52           C  
ANISOU  656  CA  PHE A 653    15769  21330  18193   4417  -6614   3378       C  
ATOM    657  C   PHE A 653     -39.189 202.525-218.406  1.00139.95           C  
ANISOU  657  C   PHE A 653    15415  20533  17224   4090  -6399   3134       C  
ATOM    658  O   PHE A 653     -38.041 202.867-218.690  1.00138.06           O  
ANISOU  658  O   PHE A 653    15641  20231  16583   4189  -6064   3308       O  
ATOM    659  CB  PHE A 653     -40.560 204.360-217.383  1.00142.12           C  
ANISOU  659  CB  PHE A 653    15049  20608  18343   4309  -6085   3556       C  
ATOM    660  CG  PHE A 653     -39.431 205.323-217.136  1.00138.99           C  
ANISOU  660  CG  PHE A 653    15030  19965  17814   4402  -5489   3852       C  
ATOM    661  CD1 PHE A 653     -39.324 206.486-217.877  1.00142.82           C  
ANISOU  661  CD1 PHE A 653    15710  20445  18109   4842  -5433   4270       C  
ATOM    662  CD2 PHE A 653     -38.479 205.068-216.163  1.00133.20           C  
ANISOU  662  CD2 PHE A 653    14435  18993  17182   4057  -4995   3724       C  
ATOM    663  CE1 PHE A 653     -38.288 207.373-217.657  1.00139.73           C  
ANISOU  663  CE1 PHE A 653    15624  19776  17690   4908  -4884   4545       C  
ATOM    664  CE2 PHE A 653     -37.439 205.953-215.938  1.00129.68           C  
ANISOU  664  CE2 PHE A 653    14294  18301  16678   4133  -4480   3958       C  
ATOM    665  CZ  PHE A 653     -37.344 207.105-216.683  1.00132.18           C  
ANISOU  665  CZ  PHE A 653    14780  18576  16868   4543  -4418   4364       C  
ATOM    666  N   VAL A 654     -39.477 201.330-217.904  1.00137.45           N  
ANISOU  666  N   VAL A 654    14854  20192  17177   3703  -6583   2751       N  
ATOM    667  CA  VAL A 654     -38.428 200.354-217.641  1.00132.21           C  
ANISOU  667  CA  VAL A 654    14482  19418  16333   3385  -6405   2508       C  
ATOM    668  C   VAL A 654     -38.116 199.533-218.887  1.00138.07           C  
ANISOU  668  C   VAL A 654    15544  20403  16513   3529  -6892   2264       C  
ATOM    669  O   VAL A 654     -36.965 199.166-219.122  1.00135.58           O  
ANISOU  669  O   VAL A 654    15662  20057  15797   3489  -6696   2199       O  
ATOM    670  CB  VAL A 654     -38.815 199.448-216.483  1.00125.73           C  
ANISOU  670  CB  VAL A 654    13266  18424  16082   2910  -6330   2257       C  
ATOM    671  N   HIS A 655     -39.140 199.254-219.690  1.00144.77           N  
ANISOU  671  N   HIS A 655    16167  21505  17335   3717  -7537   2103       N  
ATOM    672  CA  HIS A 655     -38.956 198.430-220.887  1.00147.41           C  
ANISOU  672  CA  HIS A 655    16774  22075  17161   3766  -7881   1805       C  
ATOM    673  C   HIS A 655     -38.380 199.195-222.078  1.00151.72           C  
ANISOU  673  C   HIS A 655    17809  22839  16999   4164  -7765   2091       C  
ATOM    674  O   HIS A 655     -37.472 198.707-222.752  1.00151.92           O  
ANISOU  674  O   HIS A 655    18265  22951  16506   4199  -7718   1950       O  
ATOM    675  CB  HIS A 655     -40.265 197.745-221.284  1.00150.33           C  
ANISOU  675  CB  HIS A 655    16708  22586  17825   3652  -8404   1479       C  
ATOM    676  CG  HIS A 655     -40.616 196.575-220.421  1.00147.64           C  
ANISOU  676  CG  HIS A 655    15983  22022  18090   3194  -8538   1103       C  
ATOM    677  ND1 HIS A 655     -41.895 196.069-220.336  1.00150.76           N  
ANISOU  677  ND1 HIS A 655    15841  22429  19012   3016  -8882    877       N  
ATOM    678  CD2 HIS A 655     -39.853 195.810-219.605  1.00144.36           C  
ANISOU  678  CD2 HIS A 655    15636  21342  17873   2864  -8352    948       C  
ATOM    679  CE1 HIS A 655     -41.905 195.044-219.503  1.00149.61           C  
ANISOU  679  CE1 HIS A 655    15443  22018  19383   2586  -8872    624       C  
ATOM    680  NE2 HIS A 655     -40.679 194.865-219.046  1.00145.68           N  
ANISOU  680  NE2 HIS A 655    15307  21352  18694   2486  -8565    670       N  
ATOM    681  N   ALA A 656     -38.914 200.386-222.339  1.00155.73           N  
ANISOU  681  N   ALA A 656    18238  23411  17523   4455  -7704   2500       N  
ATOM    682  CA  ALA A 656     -38.491 201.183-223.489  1.00160.73           C  
ANISOU  682  CA  ALA A 656    19295  24208  17567   4818  -7597   2830       C  
ATOM    683  C   ALA A 656     -37.001 201.502-223.455  1.00159.54           C  
ANISOU  683  C   ALA A 656    19645  23928  17043   4877  -7060   3048       C  
ATOM    684  O   ALA A 656     -36.341 201.526-224.493  1.00162.03           O  
ANISOU  684  O   ALA A 656    20381  24412  16769   5063  -6991   3112       O  
ATOM    685  CB  ALA A 656     -39.306 202.464-223.582  1.00162.74           C  
ANISOU  685  CB  ALA A 656    19345  24447  18043   5087  -7585   3266       C  
ATOM    686  N   LEU A 657     -36.479 201.751-222.260  1.00158.07           N  
ANISOU  686  N   LEU A 657    19392  23459  17208   4729  -6664   3158       N  
ATOM    687  CA  LEU A 657     -35.060 202.041-222.098  1.00157.46           C  
ANISOU  687  CA  LEU A 657    19730  23236  16864   4751  -6121   3360       C  
ATOM    688  C   LEU A 657     -34.222 200.832-222.494  1.00157.88           C  
ANISOU  688  C   LEU A 657    20084  23393  16511   4596  -6200   2972       C  
ATOM    689  O   LEU A 657     -33.316 200.941-223.321  1.00160.19           O  
ANISOU  689  O   LEU A 657    20797  23783  16286   4751  -5976   3086       O  
ATOM    690  CB  LEU A 657     -34.748 202.458-220.657  1.00151.56           C  
ANISOU  690  CB  LEU A 657    18787  22130  16669   4514  -5646   3472       C  
ATOM    691  CG  LEU A 657     -35.331 203.795-220.196  1.00151.08           C  
ANISOU  691  CG  LEU A 657    18471  21894  17037   4668  -5410   3867       C  
ATOM    692  CD1 LEU A 657     -34.903 204.118-218.773  1.00144.62           C  
ANISOU  692  CD1 LEU A 657    17494  20677  16779   4312  -4854   3856       C  
ATOM    693  CD2 LEU A 657     -34.922 204.908-221.143  1.00153.98           C  
ANISOU  693  CD2 LEU A 657    19163  22304  17040   5089  -5218   4361       C  
ATOM    694  N   GLU A 658     -34.546 199.680-221.909  1.00155.08           N  
ANISOU  694  N   GLU A 658    19491  22997  16437   4289  -6510   2510       N  
ATOM    695  CA  GLU A 658     -33.849 198.430-222.198  1.00152.57           C  
ANISOU  695  CA  GLU A 658    19403  22720  15846   4112  -6630   2080       C  
ATOM    696  C   GLU A 658     -33.963 198.053-223.670  1.00155.68           C  
ANISOU  696  C   GLU A 658    20024  23435  15693   4311  -6927   1899       C  
ATOM    697  O   GLU A 658     -33.097 197.367-224.212  1.00157.74           O  
ANISOU  697  O   GLU A 658    20617  23773  15544   4315  -6875   1666       O  
ATOM    698  CB  GLU A 658     -34.407 197.293-221.340  1.00151.53           C  
ANISOU  698  CB  GLU A 658    18895  22429  16248   3723  -6964   1636       C  
ATOM    699  CG  GLU A 658     -34.237 197.484-219.842  1.00146.22           C  
ANISOU  699  CG  GLU A 658    17980  21371  16204   3312  -6443   1763       C  
ATOM    700  CD  GLU A 658     -34.831 196.339-219.039  1.00145.42           C  
ANISOU  700  CD  GLU A 658    17485  21095  16672   2871  -6667   1394       C  
ATOM    701  OE1 GLU A 658     -35.312 195.362-219.654  1.00149.14           O  
ANISOU  701  OE1 GLU A 658    17869  21690  17106   2853  -7231   1009       O  
ATOM    702  OE2 GLU A 658     -34.816 196.414-217.793  1.00140.69           O1-
ANISOU  702  OE2 GLU A 658    16656  20234  16565   2552  -6278   1490       O1-
ATOM    703  N   GLU A 659     -35.037 198.503-224.311  1.00155.45           N  
ANISOU  703  N   GLU A 659    19806  23598  15661   4497  -7242   1994       N  
ATOM    704  CA  GLU A 659     -35.276 198.193-225.711  1.00159.03           C  
ANISOU  704  CA  GLU A 659    20446  24383  15594   4724  -7573   1814       C  
ATOM    705  C   GLU A 659     -34.225 198.825-226.620  1.00159.05           C  
ANISOU  705  C   GLU A 659    20961  24531  14937   5042  -7184   2136       C  
ATOM    706  O   GLU A 659     -33.930 198.298-227.691  1.00165.17           O  
ANISOU  706  O   GLU A 659    22009  25569  15181   5205  -7334   1901       O  
ATOM    707  CB  GLU A 659     -36.671 198.640-226.120  1.00165.34           C  
ANISOU  707  CB  GLU A 659    20911  25345  16565   4867  -7984   1893       C  
ATOM    708  N   GLN A 660     -33.658 199.949-226.189  1.00153.25           N  
ANISOU  708  N   GLN A 660    20341  23617  14271   5135  -6666   2664       N  
ATOM    709  CA  GLN A 660     -32.695 200.680-227.012  1.00154.23           C  
ANISOU  709  CA  GLN A 660    20895  23837  13870   5425  -6233   3049       C  
ATOM    710  C   GLN A 660     -31.245 200.261-226.758  1.00149.14           C  
ANISOU  710  C   GLN A 660    20558  23074  13033   5313  -5783   2984       C  
ATOM    711  O   GLN A 660     -30.830 200.099-225.614  1.00143.19           O  
ANISOU  711  O   GLN A 660    19699  22033  12672   5051  -5567   2946       O  
ATOM    712  CB  GLN A 660     -32.858 202.194-226.826  1.00154.02           C  
ANISOU  712  CB  GLN A 660    20818  23644  14059   5606  -5898   3676       C  
ATOM    713  CG  GLN A 660     -34.183 202.754-227.340  1.00159.29           C  
ANISOU  713  CG  GLN A 660    21251  24464  14806   5810  -6308   3815       C  
ATOM    714  CD  GLN A 660     -34.376 202.560-228.837  1.00166.97           C  
ANISOU  714  CD  GLN A 660    22460  25852  15129   6113  -6601   3745       C  
ATOM    715  OE1 GLN A 660     -35.500 202.394-229.311  1.00171.96           O  
ANISOU  715  OE1 GLN A 660    22880  26695  15763   6206  -7126   3585       O  
ATOM    716  NE2 GLN A 660     -33.280 202.593-229.590  1.00168.61           N  
ANISOU  716  NE2 GLN A 660    23089  26192  14782   6286  -6251   3867       N  
ATOM    717  N   LYS A 661     -30.482 200.105-227.837  1.00153.30           N  
ANISOU  717  N   LYS A 661    21456  23839  12951   5535  -5638   2980       N  
ATOM    718  CA  LYS A 661     -29.105 199.606-227.769  1.00150.14           C  
ANISOU  718  CA  LYS A 661    21346  23378  12323   5462  -5241   2875       C  
ATOM    719  C   LYS A 661     -28.118 200.619-227.192  1.00143.62           C  
ANISOU  719  C   LYS A 661    20627  22269  11675   5453  -4558   3402       C  
ATOM    720  O   LYS A 661     -26.986 200.271-226.858  1.00136.05           O  
ANISOU  720  O   LYS A 661    19836  21185  10673   5338  -4199   3344       O  
ATOM    721  CB  LYS A 661     -28.621 199.145-229.150  1.00158.63           C  
ANISOU  721  CB  LYS A 661    22756  24825  12692   5745  -5280   2704       C  
ATOM    722  CG  LYS A 661     -29.169 197.797-229.609  1.00165.17           C  
ANISOU  722  CG  LYS A 661    23532  25865  13360   5693  -5881   2020       C  
ATOM    723  CD  LYS A 661     -30.610 197.897-230.089  1.00174.50           C  
ANISOU  723  CD  LYS A 661    24476  27242  14585   5803  -6450   1928       C  
ATOM    724  CE  LYS A 661     -31.155 196.542-230.511  1.00180.85           C  
ANISOU  724  CE  LYS A 661    25190  28203  15322   5727  -7044   1218       C  
ATOM    725  NZ  LYS A 661     -30.474 196.010-231.725  1.00187.61           N1+
ANISOU  725  NZ  LYS A 661    26412  29383  15489   6019  -7031    967       N1+
ATOM    726  N   ASN A 662     -28.545 201.873-227.087  1.00148.15           N  
ANISOU  726  N   ASN A 662    21087  22719  12484   5577  -4383   3905       N  
ATOM    727  CA  ASN A 662     -27.711 202.921-226.509  1.00148.46           C  
ANISOU  727  CA  ASN A 662    21169  22427  12813   5555  -3749   4399       C  
ATOM    728  C   ASN A 662     -27.702 202.805-224.991  1.00143.21           C  
ANISOU  728  C   ASN A 662    20253  21405  12754   5234  -3669   4295       C  
ATOM    729  O   ASN A 662     -26.884 203.423-224.309  1.00139.40           O  
ANISOU  729  O   ASN A 662    19787  20611  12568   5147  -3157   4575       O  
ATOM    730  CB  ASN A 662     -28.215 204.309-226.919  1.00154.80           C  
ANISOU  730  CB  ASN A 662    21916  23175  13724   5803  -3606   4947       C  
ATOM    731  CG  ASN A 662     -28.298 204.487-228.427  1.00165.15           C  
ANISOU  731  CG  ASN A 662    23468  24868  14414   6159  -3696   5097       C  
ATOM    732  OD1 ASN A 662     -28.766 203.606-229.150  1.00169.14           O  
ANISOU  732  OD1 ASN A 662    24034  25732  14499   6246  -4163   4708       O  
ATOM    733  ND2 ASN A 662     -27.841 205.637-228.907  1.00169.95           N  
ANISOU  733  ND2 ASN A 662    24199  25392  14982   6374  -3242   5659       N  
ATOM    734  N   PHE A 663     -28.626 202.003-224.476  1.00144.46           N  
ANISOU  734  N   PHE A 663    20157  21613  13117   5061  -4179   3884       N  
ATOM    735  CA  PHE A 663     -28.802 201.825-223.042  1.00142.18           C  
ANISOU  735  CA  PHE A 663    19589  21048  13386   4785  -4169   3764       C  
ATOM    736  C   PHE A 663     -27.922 200.690-222.525  1.00138.78           C  
ANISOU  736  C   PHE A 663    19274  20547  12909   4525  -4112   3374       C  
ATOM    737  O   PHE A 663     -28.282 199.517-222.637  1.00139.03           O  
ANISOU  737  O   PHE A 663    19259  20718  12847   4397  -4561   2890       O  
ATOM    738  CB  PHE A 663     -30.273 201.529-222.747  1.00146.86           C  
ANISOU  738  CB  PHE A 663    19796  21721  14280   4720  -4730   3531       C  
ATOM    739  CG  PHE A 663     -30.683 201.828-221.340  1.00146.87           C  
ANISOU  739  CG  PHE A 663    19422  21396  14987   4435  -4581   3539       C  
ATOM    740  CD1 PHE A 663     -30.695 203.132-220.874  1.00148.01           C  
ANISOU  740  CD1 PHE A 663    19457  21294  15485   4513  -4181   3970       C  
ATOM    741  CD2 PHE A 663     -31.072 200.810-220.486  1.00145.64           C  
ANISOU  741  CD2 PHE A 663    18994  21128  15214   4024  -4784   3085       C  
ATOM    742  CE1 PHE A 663     -31.076 203.413-219.578  1.00144.90           C  
ANISOU  742  CE1 PHE A 663    18706  20588  15760   4206  -3995   3899       C  
ATOM    743  CE2 PHE A 663     -31.456 201.086-219.190  1.00142.75           C  
ANISOU  743  CE2 PHE A 663    18273  20467  15498   3717  -4570   3078       C  
ATOM    744  CZ  PHE A 663     -31.456 202.387-218.737  1.00142.08           C  
ANISOU  744  CZ  PHE A 663    18098  20180  15706   3819  -4180   3460       C  
ATOM    745  N   SER A 664     -26.774 201.051-221.954  1.00136.41           N  
ANISOU  745  N   SER A 664    19077  19950  12801   4357  -3526   3536       N  
ATOM    746  CA  SER A 664     -25.764 200.081-221.525  1.00133.85           C  
ANISOU  746  CA  SER A 664    18869  19496  12492   4058  -3358   3185       C  
ATOM    747  C   SER A 664     -26.022 199.523-220.127  1.00129.15           C  
ANISOU  747  C   SER A 664    17953  18596  12524   3576  -3383   2860       C  
ATOM    748  O   SER A 664     -27.042 199.823-219.513  1.00131.65           O  
ANISOU  748  O   SER A 664    17945  18832  13243   3471  -3544   2875       O  
ATOM    749  CB  SER A 664     -24.373 200.716-221.572  1.00132.90           C  
ANISOU  749  CB  SER A 664    18981  19209  12306   4112  -2727   3507       C  
ATOM    750  OG  SER A 664     -24.279 201.786-220.650  1.00129.88           O  
ANISOU  750  OG  SER A 664    18392  18459  12497   3968  -2332   3798       O  
ATOM    751  N   ILE A 665     -25.088 198.711-219.633  1.00124.18           N  
ANISOU  751  N   ILE A 665    17409  17813  11961   3306  -3210   2589       N  
ATOM    752  CA  ILE A 665     -25.198 198.110-218.301  1.00118.89           C  
ANISOU  752  CA  ILE A 665    16472  16875  11826   2869  -3197   2318       C  
ATOM    753  C   ILE A 665     -25.148 199.168-217.199  1.00115.85           C  
ANISOU  753  C   ILE A 665    15876  16203  11937   2732  -2791   2572       C  
ATOM    754  O   ILE A 665     -25.995 199.181-216.303  1.00112.64           O  
ANISOU  754  O   ILE A 665    15152  15702  11944   2538  -2894   2498       O  
ATOM    755  CB  ILE A 665     -24.076 197.079-218.034  1.00114.92           C  
ANISOU  755  CB  ILE A 665    16132  16261  11272   2654  -3067   2022       C  
ATOM    756  CG1 ILE A 665     -23.982 196.066-219.173  1.00119.24           C  
ANISOU  756  CG1 ILE A 665    16917  17076  11312   2828  -3432   1730       C  
ATOM    757  CG2 ILE A 665     -24.318 196.351-216.719  1.00109.62           C  
ANISOU  757  CG2 ILE A 665    15186  15359  11107   2237  -3117   1770       C  
ATOM    758  CD1 ILE A 665     -25.009 194.966-219.094  1.00119.95           C  
ANISOU  758  CD1 ILE A 665    16800  17216  11558   2664  -3998   1332       C  
ATOM    759  N   LYS A 666     -24.146 200.044-217.268  1.00116.82           N  
ANISOU  759  N   LYS A 666    16163  16188  12037   2838  -2325   2854       N  
ATOM    760  CA  LYS A 666     -23.997 201.136-216.310  1.00116.03           C  
ANISOU  760  CA  LYS A 666    15878  15791  12416   2746  -1944   3060       C  
ATOM    761  C   LYS A 666     -25.260 201.992-216.253  1.00122.12           C  
ANISOU  761  C   LYS A 666    16408  16588  13404   2890  -2096   3261       C  
ATOM    762  O   LYS A 666     -25.684 202.417-215.177  1.00124.38           O  
ANISOU  762  O   LYS A 666    16418  16688  14152   2728  -1992   3223       O  
ATOM    763  CB  LYS A 666     -22.791 201.989-216.662  1.00115.47           C  
ANISOU  763  CB  LYS A 666    16010  15566  12297   2888  -1467   3363       C  
ATOM    764  N   ASP A 667     -25.858 202.234-217.417  1.00126.03           N  
ANISOU  764  N   ASP A 667    17005  17337  13543   3223  -2349   3464       N  
ATOM    765  CA  ASP A 667     -27.137 202.929-217.492  1.00129.58           C  
ANISOU  765  CA  ASP A 667    17215  17851  14166   3395  -2573   3640       C  
ATOM    766  C   ASP A 667     -28.206 202.169-216.708  1.00124.72           C  
ANISOU  766  C   ASP A 667    16262  17277  13847   3138  -2921   3299       C  
ATOM    767  O   ASP A 667     -29.063 202.771-216.059  1.00126.18           O  
ANISOU  767  O   ASP A 667    16136  17371  14435   3118  -2922   3367       O  
ATOM    768  CB  ASP A 667     -27.584 203.092-218.949  1.00138.76           C  
ANISOU  768  CB  ASP A 667    18567  19350  14804   3815  -2873   3870       C  
ATOM    769  CG  ASP A 667     -26.598 203.893-219.779  1.00145.28           C  
ANISOU  769  CG  ASP A 667    19714  20163  15325   4108  -2489   4301       C  
ATOM    770  OD1 ASP A 667     -25.878 204.736-219.204  1.00145.82           O  
ANISOU  770  OD1 ASP A 667    19756  19889  15759   4028  -2002   4518       O  
ATOM    771  OD2 ASP A 667     -26.547 203.681-221.009  1.00150.20           O1-
ANISOU  771  OD2 ASP A 667    20602  21119  15347   4429  -2673   4421       O1-
ATOM    772  N   LYS A 668     -28.141 200.842-216.764  1.00117.67           N  
ANISOU  772  N   LYS A 668    15416  16507  12787   2946  -3194   2940       N  
ATOM    773  CA  LYS A 668     -29.141 199.994-216.125  1.00109.63           C  
ANISOU  773  CA  LYS A 668    14068  15521  12066   2693  -3531   2644       C  
ATOM    774  C   LYS A 668     -29.015 200.024-214.606  1.00106.32           C  
ANISOU  774  C   LYS A 668    13412  14845  12138   2362  -3211   2563       C  
ATOM    775  O   LYS A 668     -30.014 200.173-213.896  1.00108.08           O  
ANISOU  775  O   LYS A 668    13279  15052  12736   2268  -3284   2548       O  
ATOM    776  CB  LYS A 668     -29.043 198.563-216.656  1.00104.38           C  
ANISOU  776  CB  LYS A 668    13521  15004  11133   2588  -3911   2284       C  
ATOM    777  CG  LYS A 668     -29.493 198.428-218.101  1.00107.57           C  
ANISOU  777  CG  LYS A 668    14084  15733  11055   2933  -4356   2270       C  
ATOM    778  CD  LYS A 668     -28.908 197.192-218.750  1.00105.88           C  
ANISOU  778  CD  LYS A 668    14122  15636  10472   2901  -4596   1915       C  
ATOM    779  CE  LYS A 668     -29.280 197.100-220.220  1.00109.72           C  
ANISOU  779  CE  LYS A 668    14803  16497  10389   3301  -5038   1867       C  
ATOM    780  NZ  LYS A 668     -28.617 195.930-220.860  1.00109.80           N1+
ANISOU  780  NZ  LYS A 668    15083  16619  10017   3304  -5242   1475       N1+
ATOM    781  N   CYS A 669     -27.786 199.884-214.117  1.00102.71           N  
ANISOU  781  N   CYS A 669    13146  14216  11663   2210  -2858   2509       N  
ATOM    782  CA  CYS A 669     -27.509 199.993-212.690  1.00100.98           C  
ANISOU  782  CA  CYS A 669    12750  13786  11831   1948  -2538   2434       C  
ATOM    783  C   CYS A 669     -27.953 201.358-212.180  1.00103.93           C  
ANISOU  783  C   CYS A 669    12927  14046  12514   2080  -2300   2650       C  
ATOM    784  O   CYS A 669     -28.706 201.450-211.203  1.00107.15           O  
ANISOU  784  O   CYS A 669    13019  14431  13262   1958  -2275   2583       O  
ATOM    785  CB  CYS A 669     -26.015 199.797-212.419  1.00 98.88           C  
ANISOU  785  CB  CYS A 669    12743  13363  11462   1836  -2213   2365       C  
ATOM    786  SG  CYS A 669     -25.349 198.190-212.948  1.00146.00           S  
ANISOU  786  SG  CYS A 669    18949  19418  17107   1694  -2448   2082       S  
ATOM    787  N   THR A 670     -27.478 202.405-212.857  1.00104.80           N  
ANISOU  787  N   THR A 670    13217  14081  12521   2342  -2111   2917       N  
ATOM    788  CA  THR A 670     -27.884 203.780-212.580  1.00104.46           C  
ANISOU  788  CA  THR A 670    13009  13888  12795   2520  -1909   3147       C  
ATOM    789  C   THR A 670     -29.393 203.867-212.414  1.00101.15           C  
ANISOU  789  C   THR A 670    12247  13605  12579   2578  -2192   3145       C  
ATOM    790  O   THR A 670     -29.874 204.174-211.329  1.00 98.16           O  
ANISOU  790  O   THR A 670    11582  13139  12576   2472  -2059   3051       O  
ATOM    791  CB  THR A 670     -27.453 204.737-213.712  1.00114.39           C  
ANISOU  791  CB  THR A 670    14500  15097  13865   2851  -1789   3519       C  
ATOM    792  OG1 THR A 670     -26.027 204.715-213.853  1.00116.73           O  
ANISOU  792  OG1 THR A 670    15072  15251  14029   2796  -1476   3544       O  
ATOM    793  CG2 THR A 670     -27.892 206.160-213.418  1.00117.66           C  
ANISOU  793  CG2 THR A 670    14723  15295  14686   3037  -1589   3762       C  
ATOM    794  N   VAL A 671     -30.129 203.571-213.484  1.00101.59           N  
ANISOU  794  N   VAL A 671    12322  13899  12380   2760  -2590   3228       N  
ATOM    795  CA  VAL A 671     -31.591 203.649-213.465  1.00103.63           C  
ANISOU  795  CA  VAL A 671    12227  14300  12848   2839  -2906   3235       C  
ATOM    796  C   VAL A 671     -32.200 202.896-212.294  1.00102.90           C  
ANISOU  796  C   VAL A 671    11795  14217  13085   2518  -2939   2963       C  
ATOM    797  O   VAL A 671     -33.054 203.425-211.591  1.00105.31           O  
ANISOU  797  O   VAL A 671    11756  14493  13762   2535  -2873   2989       O  
ATOM    798  CB  VAL A 671     -32.221 203.131-214.769  1.00103.19           C  
ANISOU  798  CB  VAL A 671    12240  14537  12430   3038  -3419   3258       C  
ATOM    799  CG1 VAL A 671     -33.688 202.783-214.550  1.00103.42           C  
ANISOU  799  CG1 VAL A 671    11835  14713  12746   2993  -3798   3136       C  
ATOM    800  CG2 VAL A 671     -32.079 204.170-215.861  1.00107.35           C  
ANISOU  800  CG2 VAL A 671    12987  15107  12695   3454  -3399   3638       C  
ATOM    801  N   ALA A 672     -31.745 201.666-212.084  1.00103.59           N  
ANISOU  801  N   ALA A 672    11974  14341  13045   2243  -3018   2723       N  
ATOM    802  CA  ALA A 672     -32.269 200.832-211.012  1.00104.89           C  
ANISOU  802  CA  ALA A 672    11831  14515  13507   1932  -3033   2521       C  
ATOM    803  C   ALA A 672     -32.115 201.502-209.650  1.00104.48           C  
ANISOU  803  C   ALA A 672    11617  14319  13761   1849  -2591   2529       C  
ATOM    804  O   ALA A 672     -33.051 201.525-208.842  1.00105.70           O  
ANISOU  804  O   ALA A 672    11398  14527  14235   1777  -2561   2502       O  
ATOM    805  CB  ALA A 672     -31.583 199.479-211.016  1.00103.27           C  
ANISOU  805  CB  ALA A 672    11806  14309  13124   1672  -3134   2303       C  
ATOM    806  N   SER A 673     -30.937 202.065-209.407  1.00103.23           N  
ANISOU  806  N   SER A 673    11723  13988  13509   1876  -2249   2551       N  
ATOM    807  CA  SER A 673     -30.653 202.660-208.111  1.00104.69           C  
ANISOU  807  CA  SER A 673    11787  14044  13948   1810  -1862   2482       C  
ATOM    808  C   SER A 673     -31.346 204.006-207.922  1.00107.21           C  
ANISOU  808  C   SER A 673    11885  14291  14558   2056  -1732   2608       C  
ATOM    809  O   SER A 673     -31.850 204.294-206.839  1.00109.86           O  
ANISOU  809  O   SER A 673    11943  14639  15161   2021  -1554   2512       O  
ATOM    810  CB  SER A 673     -29.146 202.801-207.903  1.00105.94           C  
ANISOU  810  CB  SER A 673    12263  14022  13969   1750  -1578   2419       C  
ATOM    811  OG  SER A 673     -28.519 201.530-207.837  1.00106.25           O  
ANISOU  811  OG  SER A 673    12458  14113  13797   1514  -1663   2273       O  
ATOM    812  N   LEU A 674     -31.362 204.827-208.969  1.00104.71           N  
ANISOU  812  N   LEU A 674    11695  13907  14184   2327  -1809   2833       N  
ATOM    813  CA  LEU A 674     -32.033 206.118-208.920  1.00102.55           C  
ANISOU  813  CA  LEU A 674    11217  13526  14220   2592  -1716   2986       C  
ATOM    814  C   LEU A 674     -33.510 205.901-208.675  1.00108.80           C  
ANISOU  814  C   LEU A 674    11602  14518  15221   2611  -1940   2962       C  
ATOM    815  O   LEU A 674     -34.152 206.660-207.949  1.00114.07           O  
ANISOU  815  O   LEU A 674    11976  15132  16233   2715  -1779   2939       O  
ATOM    816  CB  LEU A 674     -31.853 206.870-210.236  1.00101.54           C  
ANISOU  816  CB  LEU A 674    11306  13322  13951   2892  -1807   3306       C  
ATOM    817  CG  LEU A 674     -30.473 207.438-210.554  1.00 96.62           C  
ANISOU  817  CG  LEU A 674    11025  12449  13239   2943  -1512   3427       C  
ATOM    818  CD1 LEU A 674     -30.485 208.062-211.940  1.00 97.32           C  
ANISOU  818  CD1 LEU A 674    11302  12533  13142   3266  -1620   3820       C  
ATOM    819  CD2 LEU A 674     -30.038 208.453-209.502  1.00 94.89           C  
ANISOU  819  CD2 LEU A 674    10690  11914  13449   2938  -1122   3328       C  
ATOM    820  N   LEU A 675     -34.042 204.854-209.293  1.00108.20           N  
ANISOU  820  N   LEU A 675    11487  14662  14963   2517  -2317   2943       N  
ATOM    821  CA  LEU A 675     -35.445 204.511-209.151  1.00108.33           C  
ANISOU  821  CA  LEU A 675    11080  14865  15216   2504  -2572   2917       C  
ATOM    822  C   LEU A 675     -35.702 203.965-207.757  1.00103.60           C  
ANISOU  822  C   LEU A 675    10204  14311  14849   2237  -2345   2729       C  
ATOM    823  O   LEU A 675     -36.787 204.144-207.204  1.00106.14           O  
ANISOU  823  O   LEU A 675    10110  14728  15493   2268  -2331   2728       O  
ATOM    824  CB  LEU A 675     -35.859 203.491-210.211  1.00110.41           C  
ANISOU  824  CB  LEU A 675    11374  15322  15254   2462  -3070   2899       C  
ATOM    825  CG  LEU A 675     -37.334 203.109-210.248  1.00115.38           C  
ANISOU  825  CG  LEU A 675    11533  16133  16175   2452  -3410   2870       C  
ATOM    826  CD1 LEU A 675     -38.207 204.344-210.104  1.00119.37           C  
ANISOU  826  CD1 LEU A 675    11739  16617  16998   2742  -3331   3034       C  
ATOM    827  CD2 LEU A 675     -37.636 202.398-211.552  1.00118.97           C  
ANISOU  827  CD2 LEU A 675    12077  16755  16373   2516  -3959   2840       C  
ATOM    828  N   THR A 676     -34.697 203.307-207.188  1.00 96.87           N  
ANISOU  828  N   THR A 676     9576  13406  13823   1997  -2153   2592       N  
ATOM    829  CA  THR A 676     -34.811 202.795-205.827  1.00 95.99           C  
ANISOU  829  CA  THR A 676     9251  13359  13861   1773  -1902   2455       C  
ATOM    830  C   THR A 676     -34.824 203.939-204.804  1.00 97.39           C  
ANISOU  830  C   THR A 676     9294  13469  14242   1928  -1510   2403       C  
ATOM    831  O   THR A 676     -35.613 203.929-203.855  1.00 95.91           O  
ANISOU  831  O   THR A 676     8754  13415  14273   1904  -1354   2355       O  
ATOM    832  CB  THR A 676     -33.701 201.759-205.514  1.00 93.41           C  
ANISOU  832  CB  THR A 676     9210  12999  13281   1502  -1832   2337       C  
ATOM    833  OG1 THR A 676     -34.023 200.512-206.141  1.00 93.71           O  
ANISOU  833  OG1 THR A 676     9226  13121  13259   1319  -2189   2327       O  
ATOM    834  CG2 THR A 676     -33.573 201.524-204.022  1.00 91.08           C  
ANISOU  834  CG2 THR A 676     8771  12762  13072   1351  -1490   2234       C  
ATOM    835  N   LEU A 677     -33.968 204.933-205.018  1.00100.40           N  
ANISOU  835  N   LEU A 677     9937  13638  14573   2099  -1348   2408       N  
ATOM    836  CA  LEU A 677     -33.893 206.096-204.134  1.00105.44           C  
ANISOU  836  CA  LEU A 677    10465  14153  15443   2268  -1012   2302       C  
ATOM    837  C   LEU A 677     -35.137 206.977-204.246  1.00111.80           C  
ANISOU  837  C   LEU A 677    10919  14978  16582   2529  -1056   2398       C  
ATOM    838  O   LEU A 677     -35.643 207.484-203.242  1.00113.07           O  
ANISOU  838  O   LEU A 677    10802  15184  16974   2617   -820   2262       O  
ATOM    839  CB  LEU A 677     -32.640 206.922-204.436  1.00102.87           C  
ANISOU  839  CB  LEU A 677    10482  13532  15071   2368   -855   2291       C  
ATOM    840  CG  LEU A 677     -31.703 207.160-203.253  1.00100.35           C  
ANISOU  840  CG  LEU A 677    10242  13119  14766   2291   -530   2017       C  
ATOM    841  CD1 LEU A 677     -31.221 205.837-202.699  1.00 95.42           C  
ANISOU  841  CD1 LEU A 677     9719  12683  13854   1998   -537   1903       C  
ATOM    842  CD2 LEU A 677     -30.528 208.025-203.660  1.00102.84           C  
ANISOU  842  CD2 LEU A 677    10835  13097  15144   2384   -400   2021       C  
ATOM    843  N   ALA A 678     -35.620 207.167-205.471  1.00116.13           N  
ANISOU  843  N   ALA A 678    11479  15510  17137   2682  -1362   2625       N  
ATOM    844  CA  ALA A 678     -36.867 207.890-205.688  1.00122.85           C  
ANISOU  844  CA  ALA A 678    11973  16397  18307   2938  -1470   2743       C  
ATOM    845  C   ALA A 678     -38.010 207.155-204.997  1.00127.81           C  
ANISOU  845  C   ALA A 678    12162  17300  19101   2805  -1513   2663       C  
ATOM    846  O   ALA A 678     -38.778 207.745-204.238  1.00131.02           O  
ANISOU  846  O   ALA A 678    12216  17751  19815   2941  -1322   2598       O  
ATOM    847  CB  ALA A 678     -37.146 208.028-207.174  1.00124.96           C  
ANISOU  847  CB  ALA A 678    12354  16658  18466   3121  -1850   3012       C  
ATOM    848  N   LEU A 679     -38.105 205.858-205.263  1.00128.88           N  
ANISOU  848  N   LEU A 679    12306  17604  19060   2541  -1749   2667       N  
ATOM    849  CA  LEU A 679     -39.152 205.036-204.683  1.00131.83           C  
ANISOU  849  CA  LEU A 679    12245  18207  19639   2371  -1793   2636       C  
ATOM    850  C   LEU A 679     -38.744 204.431-203.347  1.00131.80           C  
ANISOU  850  C   LEU A 679    12216  18290  19573   2134  -1430   2495       C  
ATOM    851  O   LEU A 679     -39.165 203.322-203.021  1.00134.56           O  
ANISOU  851  O   LEU A 679    12363  18791  19972   1883  -1486   2514       O  
ATOM    852  CB  LEU A 679     -39.539 203.910-205.641  1.00132.04           C  
ANISOU  852  CB  LEU A 679    12241  18335  19593   2201  -2261   2699       C  
ATOM    853  CG  LEU A 679     -40.327 204.310-206.885  1.00136.13           C  
ANISOU  853  CG  LEU A 679    12645  18884  20195   2446  -2697   2833       C  
ATOM    854  CD1 LEU A 679     -40.674 203.074-207.689  1.00137.76           C  
ANISOU  854  CD1 LEU A 679    12802  19209  20331   2254  -3176   2799       C  
ATOM    855  CD2 LEU A 679     -41.580 205.060-206.476  1.00139.98           C  
ANISOU  855  CD2 LEU A 679    12621  19445  21120   2651  -2632   2889       C  
ATOM    856  N   HIS A 680     -37.927 205.144-202.575  1.00129.27           N  
ANISOU  856  N   HIS A 680    12088  17868  19160   2221  -1072   2359       N  
ATOM    857  CA  HIS A 680     -37.515 204.633-201.268  1.00126.93           C  
ANISOU  857  CA  HIS A 680    11785  17699  18743   2051   -736   2221       C  
ATOM    858  C   HIS A 680     -38.436 205.100-200.141  1.00129.92           C  
ANISOU  858  C   HIS A 680    11738  18269  19357   2191   -421   2154       C  
ATOM    859  O   HIS A 680     -38.340 204.624-199.010  1.00129.75           O  
ANISOU  859  O   HIS A 680    11637  18438  19223   2084   -134   2082       O  
ATOM    860  CB  HIS A 680     -36.061 204.989-200.956  1.00122.08           C  
ANISOU  860  CB  HIS A 680    11601  16915  17867   2051   -547   2056       C  
ATOM    861  CG  HIS A 680     -35.416 204.060-199.975  1.00118.94           C  
ANISOU  861  CG  HIS A 680    11310  16656  17227   1819   -358   1962       C  
ATOM    862  ND1 HIS A 680     -35.572 204.191-198.611  1.00118.87           N  
ANISOU  862  ND1 HIS A 680    11123  16843  17198   1868    -12   1829       N  
ATOM    863  CD2 HIS A 680     -34.626 202.975-200.159  1.00115.69           C  
ANISOU  863  CD2 HIS A 680    11160  16227  16569   1562   -471   1993       C  
ATOM    864  CE1 HIS A 680     -34.901 203.233-197.998  1.00116.11           C  
ANISOU  864  CE1 HIS A 680    10930  16600  16586   1655     75   1814       C  
ATOM    865  NE2 HIS A 680     -34.318 202.482-198.916  1.00114.09           N  
ANISOU  865  NE2 HIS A 680    10934  16196  16219   1459   -201   1911       N  
ATOM    866  N   GLY A 681     -39.333 206.027-200.458  1.00133.45           N  
ANISOU  866  N   GLY A 681    11909  18683  20113   2455   -469   2191       N  
ATOM    867  CA  GLY A 681     -40.337 206.461-199.506  1.00136.74           C  
ANISOU  867  CA  GLY A 681    11873  19296  20786   2617   -187   2131       C  
ATOM    868  C   GLY A 681     -41.524 205.517-199.518  1.00138.49           C  
ANISOU  868  C   GLY A 681    11645  19752  21222   2454   -298   2319       C  
ATOM    869  O   GLY A 681     -42.072 205.179-198.471  1.00139.10           O  
ANISOU  869  O   GLY A 681    11404  20081  21368   2411     13   2318       O  
ATOM    870  N   ASP A 682     -41.917 205.092-200.716  1.00139.20           N  
ANISOU  870  N   ASP A 682    11698  19768  21424   2372   -743   2479       N  
ATOM    871  CA  ASP A 682     -43.022 204.151-200.891  1.00140.51           C  
ANISOU  871  CA  ASP A 682    11418  20100  21871   2189   -937   2634       C  
ATOM    872  C   ASP A 682     -42.502 202.796-201.376  1.00134.31           C  
ANISOU  872  C   ASP A 682    10852  19274  20904   1830  -1209   2692       C  
ATOM    873  O   ASP A 682     -42.466 202.545-202.577  1.00135.15           O  
ANISOU  873  O   ASP A 682    11098  19271  20983   1803  -1665   2723       O  
ATOM    874  CB  ASP A 682     -44.028 204.703-201.907  1.00146.66           C  
ANISOU  874  CB  ASP A 682    11906  20838  22978   2403  -1310   2722       C  
ATOM    875  CG  ASP A 682     -45.309 203.884-201.976  1.00153.80           C  
ANISOU  875  CG  ASP A 682    12235  21914  24289   2247  -1495   2843       C  
ATOM    876  OD1 ASP A 682     -45.369 202.789-201.376  1.00153.86           O  
ANISOU  876  OD1 ASP A 682    12099  22028  24332   1935  -1364   2894       O  
ATOM    877  OD2 ASP A 682     -46.266 204.336-202.640  1.00159.55           O1-
ANISOU  877  OD2 ASP A 682    12631  22655  25337   2439  -1780   2901       O1-
ATOM    878  N   LEU A 683     -42.122 201.917-200.452  1.00128.77           N  
ANISOU  878  N   LEU A 683    10177  18671  20078   1580   -939   2707       N  
ATOM    879  CA  LEU A 683     -41.482 200.651-200.816  1.00122.91           C  
ANISOU  879  CA  LEU A 683     9682  17844  19174   1251  -1159   2742       C  
ATOM    880  C   LEU A 683     -42.501 199.578-201.172  1.00123.81           C  
ANISOU  880  C   LEU A 683     9360  17997  19684   1009  -1441   2875       C  
ATOM    881  O   LEU A 683     -42.138 198.550-201.744  1.00119.35           O  
ANISOU  881  O   LEU A 683     8953  17315  19080    760  -1744   2870       O  
ATOM    882  CB  LEU A 683     -40.571 200.165-199.685  1.00118.37           C  
ANISOU  882  CB  LEU A 683     9340  17331  18305   1104   -768   2725       C  
ATOM    883  CG  LEU A 683     -39.371 201.087-199.435  1.00112.40           C  
ANISOU  883  CG  LEU A 683     9053  16489  17166   1298   -573   2537       C  
ATOM    884  CD1 LEU A 683     -38.730 200.825-198.084  1.00110.59           C  
ANISOU  884  CD1 LEU A 683     8931  16409  16679   1242   -147   2494       C  
ATOM    885  CD2 LEU A 683     -38.342 200.968-200.556  1.00106.92           C  
ANISOU  885  CD2 LEU A 683     8843  15553  16227   1247   -907   2470       C  
ATOM    886  N   LEU A 684     -43.764 199.813-200.792  1.00129.86           N  
ANISOU  886  N   LEU A 684     9554  18918  20870   1084  -1329   2974       N  
ATOM    887  CA  LEU A 684     -44.920 198.973-201.180  1.00136.21           C  
ANISOU  887  CA  LEU A 684     9825  19743  22186    886  -1622   3089       C  
ATOM    888  C   LEU A 684     -44.972 198.905-202.701  1.00138.34           C  
ANISOU  888  C   LEU A 684    10232  19865  22467    921  -2275   2978       C  
ATOM    889  O   LEU A 684     -44.709 197.851-203.332  1.00141.71           O  
ANISOU  889  O   LEU A 684    10777  20168  22899    668  -2640   2929       O  
ATOM    890  CB  LEU A 684     -46.240 199.615-200.694  1.00142.12           C  
ANISOU  890  CB  LEU A 684     9948  20679  23374   1071  -1414   3180       C  
ATOM    891  CG  LEU A 684     -47.636 199.048-200.984  1.00148.78           C  
ANISOU  891  CG  LEU A 684    10099  21569  24862    937  -1658   3297       C  
ATOM    892  CD1 LEU A 684     -47.855 197.731-200.260  1.00150.35           C  
ANISOU  892  CD1 LEU A 684    10002  21786  25337    548  -1450   3488       C  
ATOM    893  CD2 LEU A 684     -48.599 200.088-200.495  1.00152.15           C  
ANISOU  893  CD2 LEU A 684    10074  22180  25558   1245  -1378   3336       C  
ATOM    894  N   TYR A 685     -45.331 200.053-203.273  1.00136.10           N  
ANISOU  894  N   TYR A 685     9925  19602  22183   1265  -2418   2936       N  
ATOM    895  CA  TYR A 685     -45.310 200.238-204.709  1.00133.63           C  
ANISOU  895  CA  TYR A 685     9808  19204  21762   1405  -2997   2857       C  
ATOM    896  C   TYR A 685     -44.043 199.740-205.384  1.00131.24           C  
ANISOU  896  C   TYR A 685    10130  18762  20974   1299  -3202   2753       C  
ATOM    897  O   TYR A 685     -44.113 199.185-206.476  1.00133.57           O  
ANISOU  897  O   TYR A 685    10501  19020  21230   1255  -3727   2668       O  
ATOM    898  CB  TYR A 685     -45.486 201.703-205.050  1.00131.86           C  
ANISOU  898  CB  TYR A 685     9636  18989  21475   1831  -2981   2878       C  
ATOM    899  CG  TYR A 685     -45.308 202.001-206.519  1.00130.22           C  
ANISOU  899  CG  TYR A 685     9719  18720  21038   2035  -3521   2854       C  
ATOM    900  CD1 TYR A 685     -46.106 201.382-207.461  1.00133.58           C  
ANISOU  900  CD1 TYR A 685     9873  19210  21671   1993  -4102   2815       C  
ATOM    901  CD2 TYR A 685     -44.329 202.890-206.965  1.00127.14           C  
ANISOU  901  CD2 TYR A 685     9867  18216  20223   2279  -3452   2873       C  
ATOM    902  CE1 TYR A 685     -45.950 201.630-208.793  1.00133.90           C  
ANISOU  902  CE1 TYR A 685    10193  19255  21427   2218  -4602   2792       C  
ATOM    903  CE2 TYR A 685     -44.170 203.145-208.307  1.00127.19           C  
ANISOU  903  CE2 TYR A 685    10144  18206  19977   2492  -3908   2906       C  
ATOM    904  CZ  TYR A 685     -44.986 202.510-209.212  1.00129.60           C  
ANISOU  904  CZ  TYR A 685    10197  18629  20417   2475  -4485   2863       C  
ATOM    905  OH  TYR A 685     -44.843 202.750-210.552  1.00129.16           O  
ANISOU  905  OH  TYR A 685    10423  18616  20038   2729  -4952   2892       O  
ATOM    906  N   LEU A 686     -42.895 199.946-204.744  1.00127.43           N  
ANISOU  906  N   LEU A 686    10078  18216  20123   1280  -2803   2736       N  
ATOM    907  CA  LEU A 686     -41.626 199.488-205.293  1.00124.48           C  
ANISOU  907  CA  LEU A 686    10281  17711  19306   1183  -2934   2642       C  
ATOM    908  C   LEU A 686     -41.594 197.963-205.379  1.00124.14           C  
ANISOU  908  C   LEU A 686    10177  17617  19373    815  -3159   2591       C  
ATOM    909  O   LEU A 686     -41.177 197.403-206.388  1.00122.18           O  
ANISOU  909  O   LEU A 686    10197  17289  18936    767  -3568   2471       O  
ATOM    910  CB  LEU A 686     -40.455 199.990-204.454  1.00122.44           C  
ANISOU  910  CB  LEU A 686    10413  17395  18714   1220  -2449   2621       C  
ATOM    911  CG  LEU A 686     -39.120 199.508-205.023  1.00121.76           C  
ANISOU  911  CG  LEU A 686    10889  17170  18203   1122  -2569   2530       C  
ATOM    912  CD1 LEU A 686     -38.922 200.046-206.434  1.00124.21           C  
ANISOU  912  CD1 LEU A 686    11473  17428  18291   1362  -2943   2519       C  
ATOM    913  CD2 LEU A 686     -37.946 199.887-204.135  1.00119.13           C  
ANISOU  913  CD2 LEU A 686    10893  16776  17594   1125  -2118   2486       C  
ATOM    914  N   THR A 687     -42.042 197.307-204.313  1.00127.24           N  
ANISOU  914  N   THR A 687    10208  18053  20083    575  -2874   2688       N  
ATOM    915  CA  THR A 687     -42.193 195.861-204.304  1.00129.25           C  
ANISOU  915  CA  THR A 687    10297  18216  20597    214  -3063   2686       C  
ATOM    916  C   THR A 687     -43.111 195.423-205.462  1.00130.98           C  
ANISOU  916  C   THR A 687    10216  18404  21148    186  -3690   2574       C  
ATOM    917  O   THR A 687     -42.715 194.572-206.266  1.00131.95           O  
ANISOU  917  O   THR A 687    10548  18396  21190     49  -4099   2406       O  
ATOM    918  CB  THR A 687     -42.744 195.336-202.960  1.00132.95           C  
ANISOU  918  CB  THR A 687    10327  18757  21430     -3  -2619   2896       C  
ATOM    919  OG1 THR A 687     -41.887 195.753-201.899  1.00131.12           O  
ANISOU  919  OG1 THR A 687    10389  18601  20830     64  -2083   2961       O  
ATOM    920  CG2 THR A 687     -42.791 193.821-202.951  1.00134.19           C  
ANISOU  920  CG2 THR A 687    10337  18748  21900   -390  -2794   2932       C  
ATOM    921  N   GLU A 688     -44.304 196.015-205.558  1.00130.92           N  
ANISOU  921  N   GLU A 688     9723  18520  21501    341  -3784   2634       N  
ATOM    922  CA  GLU A 688     -45.270 195.549-206.539  1.00134.77           C  
ANISOU  922  CA  GLU A 688     9841  18998  22370    306  -4396   2513       C  
ATOM    923  C   GLU A 688     -44.743 195.781-207.984  1.00156.23           C  
ANISOU  923  C   GLU A 688    13025  21708  24627    533  -4937   2302       C  
ATOM    924  O   GLU A 688     -44.812 194.890-208.851  1.00160.82           O  
ANISOU  924  O   GLU A 688    13615  22218  25271    410  -5470   2090       O  
ATOM    925  CB  GLU A 688     -46.679 196.109-206.269  1.00140.65           C  
ANISOU  925  CB  GLU A 688     9914  19885  23643    424  -4368   2633       C  
ATOM    926  CG  GLU A 688     -47.352 195.526-204.968  1.00154.71           C  
ANISOU  926  CG  GLU A 688    11133  21681  25969    140  -3903   2846       C  
ATOM    927  CD  GLU A 688     -47.510 193.998-205.006  1.00155.93           C  
ANISOU  927  CD  GLU A 688    11050  21644  26552   -291  -4133   2818       C  
ATOM    928  OE1 GLU A 688     -48.003 193.464-206.025  1.00159.45           O  
ANISOU  928  OE1 GLU A 688    11306  21998  27278   -360  -4767   2613       O  
ATOM    929  OE2 GLU A 688     -47.156 193.326-204.016  1.00153.60           O1-
ANISOU  929  OE2 GLU A 688    10745  21283  26333   -549  -3694   2997       O1-
ATOM    930  N   ILE A 689     -44.115 196.931-208.215  1.00150.51           N  
ANISOU  930  N   ILE A 689    12721  21048  23418    864  -4772   2355       N  
ATOM    931  CA  ILE A 689     -43.584 197.254-209.544  1.00147.13           C  
ANISOU  931  CA  ILE A 689    12749  20648  22504   1123  -5196   2234       C  
ATOM    932  C   ILE A 689     -42.395 196.373-209.904  1.00140.59           C  
ANISOU  932  C   ILE A 689    12432  19701  21284    951  -5281   2072       C  
ATOM    933  O   ILE A 689     -42.220 196.022-211.068  1.00141.74           O  
ANISOU  933  O   ILE A 689    12803  19880  21171   1048  -5779   1887       O  
ATOM    934  CB  ILE A 689     -43.250 198.764-209.740  1.00125.15           C  
ANISOU  934  CB  ILE A 689    10249  17926  19376   1533  -4978   2392       C  
ATOM    935  CG1 ILE A 689     -42.909 199.043-211.209  1.00126.12           C  
ANISOU  935  CG1 ILE A 689    10763  18121  19036   1826  -5451   2332       C  
ATOM    936  CG2 ILE A 689     -42.086 199.206-208.875  1.00120.86           C  
ANISOU  936  CG2 ILE A 689    10101  17277  18543   1503  -4379   2473       C  
ATOM    937  CD1 ILE A 689     -43.991 198.648-212.206  1.00131.55           C  
ANISOU  937  CD1 ILE A 689    11112  18953  19920   1918  -6138   2199       C  
ATOM    938  N   MET A 690     -41.586 196.014-208.911  1.00134.05           N  
ANISOU  938  N   MET A 690    11780  18754  20397    723  -4807   2128       N  
ATOM    939  CA  MET A 690     -40.517 195.052-209.138  1.00129.66           C  
ANISOU  939  CA  MET A 690    11636  18063  19566    529  -4876   1974       C  
ATOM    940  C   MET A 690     -41.108 193.682-209.458  1.00135.31           C  
ANISOU  940  C   MET A 690    12041  18681  20690    240  -5323   1786       C  
ATOM    941  O   MET A 690     -40.536 192.918-210.236  1.00138.13           O  
ANISOU  941  O   MET A 690    12691  18956  20835    186  -5666   1552       O  
ATOM    942  CB  MET A 690     -39.590 194.963-207.928  1.00120.98           C  
ANISOU  942  CB  MET A 690    10741  16868  18358    361  -4288   2090       C  
ATOM    943  CG  MET A 690     -38.422 194.020-208.130  1.00114.84           C  
ANISOU  943  CG  MET A 690    10390  15939  17304    186  -4338   1944       C  
ATOM    944  SD  MET A 690     -37.488 193.783-206.613  1.00155.46           S  
ANISOU  944  SD  MET A 690    15679  20994  22393    -21  -3703   2092       S  
ATOM    945  CE  MET A 690     -38.770 193.150-205.532  1.00136.24           C  
ANISOU  945  CE  MET A 690    12566  18579  20619   -290  -3551   2277       C  
ATOM    946  N   GLU A 691     -42.259 193.374-208.868  1.00137.70           N  
ANISOU  946  N   GLU A 691    11728  18979  21613     62  -5315   1876       N  
ATOM    947  CA  GLU A 691     -42.936 192.118-209.171  1.00141.20           C  
ANISOU  947  CA  GLU A 691    11787  19285  22579   -226  -5756   1701       C  
ATOM    948  C   GLU A 691     -43.411 192.061-210.617  1.00143.06           C  
ANISOU  948  C   GLU A 691    12007  19604  22747    -33  -6493   1401       C  
ATOM    949  O   GLU A 691     -43.197 191.061-211.304  1.00143.72           O  
ANISOU  949  O   GLU A 691    12188  19561  22857   -165  -6939   1102       O  
ATOM    950  CB  GLU A 691     -44.108 191.877-208.227  1.00145.84           C  
ANISOU  950  CB  GLU A 691    11664  19853  23895   -448  -5550   1906       C  
ATOM    951  CG  GLU A 691     -43.688 191.445-206.850  1.00144.71           C  
ANISOU  951  CG  GLU A 691    11491  19611  23881   -710  -4925   2165       C  
ATOM    952  CD  GLU A 691     -44.829 190.838-206.082  1.00151.17           C  
ANISOU  952  CD  GLU A 691    11588  20371  25477   -988  -4791   2361       C  
ATOM    953  OE1 GLU A 691     -45.991 190.981-206.529  1.00156.23           O  
ANISOU  953  OE1 GLU A 691    11718  21073  26571   -947  -5127   2304       O  
ATOM    954  OE2 GLU A 691     -44.561 190.211-205.037  1.00151.35           O1-
ANISOU  954  OE2 GLU A 691    11544  20295  25669  -1240  -4348   2591       O1-
ATOM    955  N   ASP A 692     -44.050 193.126-211.089  1.00144.30           N  
ANISOU  955  N   ASP A 692    12044  19978  22806    302  -6638   1465       N  
ATOM    956  CA  ASP A 692     -44.481 193.143-212.483  1.00148.17           C  
ANISOU  956  CA  ASP A 692    12551  20606  23142    548  -7355   1198       C  
ATOM    957  C   ASP A 692     -43.314 193.223-213.469  1.00144.05           C  
ANISOU  957  C   ASP A 692    12746  20151  21835    783  -7529   1035       C  
ATOM    958  O   ASP A 692     -43.371 192.643-214.559  1.00146.90           O  
ANISOU  958  O   ASP A 692    13231  20570  22013    862  -8092    700       O  
ATOM    959  CB  ASP A 692     -45.488 194.262-212.736  1.00154.01           C  
ANISOU  959  CB  ASP A 692    12973  21565  23979    873  -7463   1343       C  
ATOM    960  CG  ASP A 692     -46.880 193.900-212.261  1.00161.59           C  
ANISOU  960  CG  ASP A 692    13254  22490  25653    662  -7445   1327       C  
ATOM    961  OD1 ASP A 692     -47.126 192.696-212.025  1.00163.47           O  
ANISOU  961  OD1 ASP A 692    13269  22531  26311    287  -7513   1161       O  
ATOM    962  OD2 ASP A 692     -47.728 194.809-212.131  1.00165.18           O1-
ANISOU  962  OD2 ASP A 692    13400  23091  26270    876  -7351   1486       O1-
ATOM    963  N   LEU A 693     -42.258 193.931-213.077  1.00138.34           N  
ANISOU  963  N   LEU A 693    12502  19427  20634    898  -6992   1249       N  
ATOM    964  CA  LEU A 693     -41.068 194.077-213.912  1.00135.30           C  
ANISOU  964  CA  LEU A 693    12786  19100  19524   1117  -7039   1159       C  
ATOM    965  C   LEU A 693     -40.314 192.755-214.023  1.00133.47           C  
ANISOU  965  C   LEU A 693    12778  18690  19244    843  -7169    871       C  
ATOM    966  O   LEU A 693     -39.655 192.482-215.027  1.00134.95           O  
ANISOU  966  O   LEU A 693    13387  18952  18934   1012  -7465    645       O  
ATOM    967  CB  LEU A 693     -40.147 195.157-213.336  1.00129.41           C  
ANISOU  967  CB  LEU A 693    12411  18341  18416   1262  -6396   1466       C  
ATOM    968  CG  LEU A 693     -39.939 196.431-214.158  1.00130.99           C  
ANISOU  968  CG  LEU A 693    12923  18723  18125   1723  -6411   1643       C  
ATOM    969  CD1 LEU A 693     -41.253 197.156-214.392  1.00136.60           C  
ANISOU  969  CD1 LEU A 693    13188  19587  19127   1948  -6669   1759       C  
ATOM    970  CD2 LEU A 693     -38.943 197.354-213.479  1.00126.45           C  
ANISOU  970  CD2 LEU A 693    12676  18047  17322   1788  -5761   1901       C  
ATOM    971  N   LEU A 694     -40.421 191.939-212.981  1.00130.99           N  
ANISOU  971  N   LEU A 694    12174  18144  19452    440  -6932    896       N  
ATOM    972  CA  LEU A 694     -39.734 190.656-212.927  1.00128.11           C  
ANISOU  972  CA  LEU A 694    11973  17549  19154    154  -7009    665       C  
ATOM    973  C   LEU A 694     -40.552 189.585-213.634  1.00134.41           C  
ANISOU  973  C   LEU A 694    12424  18264  20380     16  -7693    290       C  
ATOM    974  O   LEU A 694     -40.005 188.669-214.252  1.00134.56           O  
ANISOU  974  O   LEU A 694    12687  18170  20269    -42  -8017    -52       O  
ATOM    975  CB  LEU A 694     -39.508 190.257-211.472  1.00122.55           C  
ANISOU  975  CB  LEU A 694    11099  16629  18834   -198  -6447    909       C  
ATOM    976  CG  LEU A 694     -38.397 189.256-211.176  1.00118.61           C  
ANISOU  976  CG  LEU A 694    10924  15892  18250   -428  -6299    806       C  
ATOM    977  CD1 LEU A 694     -37.586 189.748-209.994  1.00114.53           C  
ANISOU  977  CD1 LEU A 694    10609  15356  17551   -475  -5604   1127       C  
ATOM    978  CD2 LEU A 694     -38.974 187.887-210.888  1.00121.53           C  
ANISOU  978  CD2 LEU A 694    10870  15983  19321   -810  -6540    680       C  
ATOM    979  N   GLN A 695     -41.870 189.700-213.532  1.00139.68           N  
ANISOU  979  N   GLN A 695    12496  18977  21598    -31  -7922    329       N  
ATOM    980  CA  GLN A 695     -42.753 188.751-214.188  1.00146.94           C  
ANISOU  980  CA  GLN A 695    13137  19807  22886   -160  -8379    -47       C  
ATOM    981  C   GLN A 695     -42.785 189.002-215.694  1.00153.48           C  
ANISOU  981  C   GLN A 695    14313  20905  23096    223  -8842   -377       C  
ATOM    982  O   GLN A 695     -42.993 188.077-216.484  1.00158.85           O  
ANISOU  982  O   GLN A 695    15026  21513  23815    168  -9229   -795       O  
ATOM    983  CB  GLN A 695     -44.158 188.829-213.591  1.00149.29           C  
ANISOU  983  CB  GLN A 695    12756  20076  23892   -323  -8298    113       C  
ATOM    984  CG  GLN A 695     -45.131 187.823-214.171  1.00155.74           C  
ANISOU  984  CG  GLN A 695    13254  20751  25171   -491  -8711   -255       C  
ATOM    985  CD  GLN A 695     -46.284 187.539-213.238  1.00159.76           C  
ANISOU  985  CD  GLN A 695    13081  21093  26528   -795  -8490    -46       C  
ATOM    986  OE1 GLN A 695     -46.420 188.179-212.194  1.00156.61           O  
ANISOU  986  OE1 GLN A 695    12443  20744  26318   -841  -8017    373       O  
ATOM    987  NE2 GLN A 695     -47.119 186.573-213.603  1.00167.20           N  
ANISOU  987  NE2 GLN A 695    13704  21834  27989   -995  -8808   -333       N  
ATOM    988  N   SER A 696     -42.572 190.255-216.088  1.00152.81           N  
ANISOU  988  N   SER A 696    14489  21125  22445    623  -8779   -168       N  
ATOM    989  CA  SER A 696     -42.507 190.596-217.507  1.00155.53           C  
ANISOU  989  CA  SER A 696    15207  21776  22111   1025  -9138   -381       C  
ATOM    990  C   SER A 696     -41.167 190.176-218.121  1.00152.55           C  
ANISOU  990  C   SER A 696    15460  21404  21099   1128  -9155   -584       C  
ATOM    991  O   SER A 696     -41.076 189.909-219.321  1.00157.43           O  
ANISOU  991  O   SER A 696    16362  22206  21249   1349  -9484   -891       O  
ATOM    992  CB  SER A 696     -42.765 192.088-217.717  1.00154.15           C  
ANISOU  992  CB  SER A 696    15083  21898  21589   1427  -9026    -25       C  
ATOM    993  OG  SER A 696     -44.093 192.427-217.349  1.00155.62           O  
ANISOU  993  OG  SER A 696    14682  22114  22332   1380  -9072     91       O  
ATOM    994  N   LEU A 697     -40.135 190.108-217.286  1.00144.53           N  
ANISOU  994  N   LEU A 697    14647  20194  20073    971  -8788   -410       N  
ATOM    995  CA  LEU A 697     -38.831 189.600-217.700  1.00142.31           C  
ANISOU  995  CA  LEU A 697    14916  19866  19287   1018  -8754   -606       C  
ATOM    996  C   LEU A 697     -38.862 188.068-217.752  1.00148.38           C  
ANISOU  996  C   LEU A 697    15571  20346  20461    684  -8986  -1037       C  
ATOM    997  O   LEU A 697     -37.869 187.416-218.076  1.00146.83           O  
ANISOU  997  O   LEU A 697    15765  20058  19965    680  -8991  -1274       O  
ATOM    998  CB  LEU A 697     -37.749 190.086-216.727  1.00132.77           C  
ANISOU  998  CB  LEU A 697    13969  18531  17945    940  -8145   -244       C  
ATOM    999  CG  LEU A 697     -36.275 189.743-216.985  1.00126.71           C  
ANISOU  999  CG  LEU A 697    13790  17710  16643    989  -7918   -352       C  
ATOM   1000  CD1 LEU A 697     -35.754 190.456-218.222  1.00128.24           C  
ANISOU 1000  CD1 LEU A 697    14464  18244  16017   1474  -8049   -375       C  
ATOM   1001  CD2 LEU A 697     -35.408 190.051-215.772  1.00119.40           C  
ANISOU 1001  CD2 LEU A 697    12998  16592  15776    790  -7189     -8       C  
ATOM   1002  N   MET A 698     -40.022 187.498-217.442  1.00156.34           N  
ANISOU 1002  N   MET A 698    16030  21191  22183    417  -9164  -1134       N  
ATOM   1003  CA  MET A 698     -40.158 186.054-217.308  1.00162.30           C  
ANISOU 1003  CA  MET A 698    16593  21580  23493     60  -9332  -1470       C  
ATOM   1004  C   MET A 698     -41.255 185.492-218.209  1.00172.25           C  
ANISOU 1004  C   MET A 698    17591  22868  24989     87  -9822  -1866       C  
ATOM   1005  O   MET A 698     -40.985 184.695-219.111  1.00174.03           O  
ANISOU 1005  O   MET A 698    18053  23053  25015    158 -10139  -2318       O  
ATOM   1006  CB  MET A 698     -40.454 185.708-215.848  1.00160.95           C  
ANISOU 1006  CB  MET A 698    15960  21075  24117   -375  -8993  -1151       C  
ATOM   1007  CG  MET A 698     -40.263 184.249-215.498  1.00163.49           C  
ANISOU 1007  CG  MET A 698    16171  20952  24997   -754  -9026  -1368       C  
ATOM   1008  SD  MET A 698     -40.848 183.875-213.837  1.00219.63           S  
ANISOU 1008  SD  MET A 698    22669  27722  33058  -1239  -8591   -904       S  
ATOM   1009  CE  MET A 698     -39.915 185.056-212.872  1.00126.02           C  
ANISOU 1009  CE  MET A 698    11031  16070  20782  -1145  -8069   -376       C  
ATOM   1010  N   ASP A 699     -42.493 185.910-217.952  1.00179.75           N  
ANISOU 1010  N   ASP A 699    18038  23883  26376     41  -9881  -1706       N  
ATOM   1011  CA  ASP A 699     -43.652 185.434-218.704  1.00192.65           C  
ANISOU 1011  CA  ASP A 699    19347  25532  28321     47 -10350  -2050       C  
ATOM   1012  C   ASP A 699     -43.567 185.811-220.178  1.00199.45           C  
ANISOU 1012  C   ASP A 699    20596  26786  28400    495 -10742  -2340       C  
ATOM   1013  O   ASP A 699     -43.690 184.956-221.057  1.00205.54           O  
ANISOU 1013  O   ASP A 699    21444  27506  29146    526 -11148  -2822       O  
ATOM   1014  CB  ASP A 699     -44.950 185.993-218.106  1.00196.09           C  
ANISOU 1014  CB  ASP A 699    19177  26008  29319    -46 -10281  -1763       C  
ATOM   1015  CG  ASP A 699     -45.252 185.435-216.728  1.00194.53           C  
ANISOU 1015  CG  ASP A 699    18515  25420  29979   -507  -9914  -1503       C  
ATOM   1016  OD1 ASP A 699     -44.297 185.098-215.998  1.00188.38           O  
ANISOU 1016  OD1 ASP A 699    17932  24428  29216   -694  -9577  -1349       O  
ATOM   1017  OD2 ASP A 699     -46.447 185.339-216.373  1.00199.61           O1-
ANISOU 1017  OD2 ASP A 699    18591  25978  31272   -673  -9945  -1428       O1-
ATOM   1018  N   GLN A 700     -43.360 187.098-220.442  1.00198.00           N  
ANISOU 1018  N   GLN A 700    20652  26987  27590    855 -10605  -2027       N  
ATOM   1019  CA  GLN A 700     -43.313 187.601-221.811  1.00200.70           C  
ANISOU 1019  CA  GLN A 700    21355  27743  27157   1309 -10911  -2181       C  
ATOM   1020  C   GLN A 700     -41.880 187.859-222.275  1.00193.95           C  
ANISOU 1020  C   GLN A 700    21178  27044  25471   1565 -10701  -2145       C  
ATOM   1021  O   GLN A 700     -41.651 188.623-223.214  1.00197.00           O  
ANISOU 1021  O   GLN A 700    21917  27810  25124   1980 -10762  -2059       O  
ATOM   1022  CB  GLN A 700     -44.157 188.866-221.940  1.00202.17           C  
ANISOU 1022  CB  GLN A 700    21336  28254  27227   1577 -10924  -1830       C  
ATOM   1023  N   SER A 701     -40.924 187.212-221.613  1.00183.56           N  
ANISOU 1023  N   SER A 701    20030  25426  24287   1318 -10435  -2185       N  
ATOM   1024  CA  SER A 701     -39.514 187.340-221.966  1.00174.95           C  
ANISOU 1024  CA  SER A 701    19553  24437  22482   1522 -10205  -2173       C  
ATOM   1025  C   SER A 701     -39.242 186.779-223.358  1.00178.64           C  
ANISOU 1025  C   SER A 701    20375  25096  22405   1788 -10551  -2639       C  
ATOM   1026  O   SER A 701     -39.676 185.676-223.689  1.00184.05           O  
ANISOU 1026  O   SER A 701    20882  25592  23457   1633 -10910  -3111       O  
ATOM   1027  CB  SER A 701     -38.647 186.637-220.936  1.00168.44           C  
ANISOU 1027  CB  SER A 701    18771  23219  22010   1172  -9899  -2156       C  
ATOM   1028  N   SER A 702     -38.532 187.548-224.177  1.00176.96           N  
ANISOU 1028  N   SER A 702    20653  25248  21335   2201 -10425  -2494       N  
ATOM   1029  CA  SER A 702     -38.184 187.102-225.520  1.00181.29           C  
ANISOU 1029  CA  SER A 702    21572  26030  21281   2503 -10693  -2898       C  
ATOM   1030  C   SER A 702     -37.158 185.972-225.464  1.00178.14           C  
ANISOU 1030  C   SER A 702    21425  25362  20897   2354 -10619  -3273       C  
ATOM   1031  O   SER A 702     -37.427 184.859-225.914  1.00184.52           O  
ANISOU 1031  O   SER A 702    22139  26014  21956   2267 -10983  -3803       O  
ATOM   1032  CB  SER A 702     -37.662 188.267-226.363  1.00181.71           C  
ANISOU 1032  CB  SER A 702    22074  26536  20431   2982 -10497  -2559       C  
ATOM   1033  OG  SER A 702     -36.624 188.956-225.688  1.00175.04           O  
ANISOU 1033  OG  SER A 702    21496  25643  19370   2988  -9951  -2117       O  
ATOM   1034  N   ASN A 703     -35.986 186.260-224.908  1.00168.42           N  
ANISOU 1034  N   ASN A 703    20504  24061  19429   2334 -10152  -3004       N  
ATOM   1035  CA  ASN A 703     -34.941 185.249-224.764  1.00165.44           C  
ANISOU 1035  CA  ASN A 703    20362  23417  19083   2195 -10040  -3312       C  
ATOM   1036  C   ASN A 703     -35.040 184.537-223.418  1.00162.97           C  
ANISOU 1036  C   ASN A 703    19686  22594  19639   1691  -9949  -3291       C  
ATOM   1037  O   ASN A 703     -34.314 184.857-222.474  1.00156.17           O  
ANISOU 1037  O   ASN A 703    18908  21589  18841   1547  -9552  -2957       O  
ATOM   1038  CB  ASN A 703     -33.556 185.871-224.950  1.00159.22           C  
ANISOU 1038  CB  ASN A 703    20110  22823  17562   2458  -9586  -3056       C  
ATOM   1039  CG  ASN A 703     -33.354 187.110-224.099  1.00151.11           C  
ANISOU 1039  CG  ASN A 703    19082  21845  16489   2453  -9164  -2427       C  
ATOM   1040  OD1 ASN A 703     -34.309 187.811-223.767  1.00149.91           O  
ANISOU 1040  OD1 ASN A 703    18611  21755  16595   2423  -9231  -2147       O  
ATOM   1041  ND2 ASN A 703     -32.105 187.383-223.738  1.00145.49           N  
ANISOU 1041  ND2 ASN A 703    18715  21092  15472   2495  -8726  -2213       N  
ATOM   1042  N   ALA A 704     -35.942 183.564-223.336  1.00167.73           N  
ANISOU 1042  N   ALA A 704    19883  22917  20930   1428 -10312  -3634       N  
ATOM   1043  CA  ALA A 704     -36.253 182.930-222.060  1.00164.08           C  
ANISOU 1043  CA  ALA A 704    18998  21972  21374    939 -10217  -3536       C  
ATOM   1044  C   ALA A 704     -35.918 181.443-222.011  1.00163.90           C  
ANISOU 1044  C   ALA A 704    18945  21508  21819    699 -10361  -3978       C  
ATOM   1045  O   ALA A 704     -36.705 180.600-222.446  1.00171.20           O  
ANISOU 1045  O   ALA A 704    19606  22264  23180    614 -10753  -4372       O  
ATOM   1046  CB  ALA A 704     -37.718 183.154-221.703  1.00167.64           C  
ANISOU 1046  CB  ALA A 704    18877  22388  22430    766 -10412  -3403       C  
ATOM   1047  N   ASN A 705     -34.739 181.135-221.484  1.00154.78           N  
ANISOU 1047  N   ASN A 705    18060  20156  20594    603 -10045  -3909       N  
ATOM   1048  CA  ASN A 705     -34.408 179.776-221.078  1.00151.41           C  
ANISOU 1048  CA  ASN A 705    17536  19219  20774    302 -10086  -4185       C  
ATOM   1049  C   ASN A 705     -34.354 179.749-219.561  1.00143.41           C  
ANISOU 1049  C   ASN A 705    16240  17857  20393   -114  -9743  -3729       C  
ATOM   1050  O   ASN A 705     -33.312 180.031-218.976  1.00132.36           O  
ANISOU 1050  O   ASN A 705    15104  16435  18751   -134  -9390  -3479       O  
ATOM   1051  CB  ASN A 705     -33.066 179.334-221.657  1.00149.40           C  
ANISOU 1051  CB  ASN A 705    17796  18987  19982    522  -9994  -4474       C  
ATOM   1052  CG  ASN A 705     -32.745 177.885-221.339  1.00150.33           C  
ANISOU 1052  CG  ASN A 705    17812  18561  20745    253 -10070  -4789       C  
ATOM   1053  OD1 ASN A 705     -32.111 177.584-220.327  1.00142.22           O  
ANISOU 1053  OD1 ASN A 705    16770  17209  20058    -13  -9772  -4547       O  
ATOM   1054  ND2 ASN A 705     -33.189 176.976-222.204  1.00160.03           N  
ANISOU 1054  ND2 ASN A 705    18962  19680  22161    335 -10479  -5324       N  
ATOM   1055  N   PRO A 706     -35.480 179.395-218.926  1.00145.46           N  
ANISOU 1055  N   PRO A 706    15952  17849  21467   -441  -9837  -3613       N  
ATOM   1056  CA  PRO A 706     -35.791 179.568-217.500  1.00143.69           C  
ANISOU 1056  CA  PRO A 706    15348  17392  21857   -812  -9506  -3092       C  
ATOM   1057  C   PRO A 706     -34.636 179.308-216.532  1.00140.54           C  
ANISOU 1057  C   PRO A 706    15136  16739  21525  -1004  -9117  -2834       C  
ATOM   1058  O   PRO A 706     -34.522 180.003-215.522  1.00137.08           O  
ANISOU 1058  O   PRO A 706    14592  16349  21144  -1135  -8771  -2339       O  
ATOM   1059  CB  PRO A 706     -36.927 178.562-217.261  1.00149.98           C  
ANISOU 1059  CB  PRO A 706    15603  17789  23595  -1131  -9721  -3217       C  
ATOM   1060  CG  PRO A 706     -36.968 177.692-218.488  1.00156.44           C  
ANISOU 1060  CG  PRO A 706    16570  18542  24327   -953 -10170  -3856       C  
ATOM   1061  CD  PRO A 706     -36.490 178.563-219.595  1.00154.87           C  
ANISOU 1061  CD  PRO A 706    16844  18885  23113   -482 -10285  -4040       C  
ATOM   1062  N   LYS A 707     -33.790 178.330-216.837  1.00142.37           N  
ANISOU 1062  N   LYS A 707    15632  16712  21750  -1004  -9176  -3166       N  
ATOM   1063  CA  LYS A 707     -32.678 177.983-215.955  1.00135.64           C  
ANISOU 1063  CA  LYS A 707    14954  15592  20990  -1182  -8837  -2948       C  
ATOM   1064  C   LYS A 707     -31.463 178.882-216.184  1.00127.58           C  
ANISOU 1064  C   LYS A 707    14464  14922  19087   -881  -8624  -2875       C  
ATOM   1065  O   LYS A 707     -30.385 178.636-215.649  1.00122.36           O  
ANISOU 1065  O   LYS A 707    14032  14089  18369   -956  -8380  -2773       O  
ATOM   1066  CB  LYS A 707     -32.303 176.513-216.139  1.00140.03           C  
ANISOU 1066  CB  LYS A 707    15536  15679  21988  -1304  -8976  -3317       C  
ATOM   1067  CG  LYS A 707     -33.472 175.572-215.925  1.00147.69           C  
ANISOU 1067  CG  LYS A 707    15984  16257  23875  -1591  -9175  -3376       C  
ATOM   1068  CD  LYS A 707     -33.292 174.254-216.657  1.00157.04           C  
ANISOU 1068  CD  LYS A 707    17234  17094  25340  -1549  -9480  -3921       C  
ATOM   1069  CE  LYS A 707     -32.670 173.190-215.770  1.00157.96           C  
ANISOU 1069  CE  LYS A 707    17289  16661  26068  -1832  -9254  -3754       C  
ATOM   1070  NZ  LYS A 707     -32.754 171.842-216.406  1.00164.68           N1+
ANISOU 1070  NZ  LYS A 707    18078  17110  27383  -1820  -9578  -4257       N1+
ATOM   1071  N   LEU A 708     -31.648 179.926-216.984  1.00128.50           N  
ANISOU 1071  N   LEU A 708    14771  15523  18532   -529  -8707  -2902       N  
ATOM   1072  CA  LEU A 708     -30.567 180.842-217.326  1.00125.98           C  
ANISOU 1072  CA  LEU A 708    14956  15555  17355   -196  -8487  -2807       C  
ATOM   1073  C   LEU A 708     -31.000 182.265-217.000  1.00127.61           C  
ANISOU 1073  C   LEU A 708    15100  16104  17283    -80  -8219  -2323       C  
ATOM   1074  O   LEU A 708     -30.297 183.229-217.296  1.00125.90           O  
ANISOU 1074  O   LEU A 708    15263  16197  16375    216  -7896  -2129       O  
ATOM   1075  CB  LEU A 708     -30.229 180.715-218.812  1.00126.37           C  
ANISOU 1075  CB  LEU A 708    15386  15881  16746    213  -8702  -3273       C  
ATOM   1076  CG  LEU A 708     -28.811 181.039-219.278  1.00121.69           C  
ANISOU 1076  CG  LEU A 708    15353  15497  15384    523  -8451  -3322       C  
ATOM   1077  CD1 LEU A 708     -27.788 180.335-218.412  1.00117.06           C  
ANISOU 1077  CD1 LEU A 708    14856  14521  15102    280  -8225  -3291       C  
ATOM   1078  CD2 LEU A 708     -28.649 180.623-220.728  1.00126.98           C  
ANISOU 1078  CD2 LEU A 708    16294  16388  15564    876  -8686  -3819       C  
ATOM   1079  N   LEU A 709     -32.171 182.378-216.383  1.00131.36           N  
ANISOU 1079  N   LEU A 709    15071  16494  18344   -316  -8288  -2107       N  
ATOM   1080  CA  LEU A 709     -32.745 183.666-216.029  1.00132.40           C  
ANISOU 1080  CA  LEU A 709    15073  16912  18323   -216  -8014  -1663       C  
ATOM   1081  C   LEU A 709     -31.932 184.342-214.926  1.00125.45           C  
ANISOU 1081  C   LEU A 709    14361  16012  17293   -288  -7278  -1159       C  
ATOM   1082  O   LEU A 709     -31.268 183.666-214.140  1.00123.37           O  
ANISOU 1082  O   LEU A 709    14134  15459  17282   -528  -7004  -1081       O  
ATOM   1083  CB  LEU A 709     -34.195 183.478-215.582  1.00140.41           C  
ANISOU 1083  CB  LEU A 709    15455  17808  20086   -472  -8260  -1586       C  
ATOM   1084  CG  LEU A 709     -35.084 184.720-215.498  1.00145.66           C  
ANISOU 1084  CG  LEU A 709    15900  18787  20657   -316  -8174  -1263       C  
ATOM   1085  CD1 LEU A 709     -35.257 185.352-216.872  1.00151.11           C  
ANISOU 1085  CD1 LEU A 709    16832  19873  20710    130  -8581  -1507       C  
ATOM   1086  CD2 LEU A 709     -36.435 184.374-214.891  1.00150.35           C  
ANISOU 1086  CD2 LEU A 709    15819  19209  22100   -623  -8342  -1170       C  
ATOM   1087  N   LEU A 710     -31.977 185.675-214.895  1.00123.72           N  
ANISOU 1087  N   LEU A 710    14242  16096  16672    -61  -6988   -836       N  
ATOM   1088  CA  LEU A 710     -31.303 186.487-213.872  1.00120.90           C  
ANISOU 1088  CA  LEU A 710    14010  15747  16179    -94  -6328   -396       C  
ATOM   1089  C   LEU A 710     -29.767 186.449-213.906  1.00116.00           C  
ANISOU 1089  C   LEU A 710    13876  15087  15111      0  -5997   -417       C  
ATOM   1090  O   LEU A 710     -29.112 187.056-213.060  1.00107.63           O  
ANISOU 1090  O   LEU A 710    12921  14013  13959    -31  -5485   -108       O  
ATOM   1091  CB  LEU A 710     -31.809 186.131-212.468  1.00123.38           C  
ANISOU 1091  CB  LEU A 710    13910  15829  17141   -465  -6061   -119       C  
ATOM   1092  CG  LEU A 710     -33.265 186.461-212.138  1.00128.46           C  
ANISOU 1092  CG  LEU A 710    14029  16539  18241   -557  -6182     42       C  
ATOM   1093  CD1 LEU A 710     -33.649 185.868-210.794  1.00127.52           C  
ANISOU 1093  CD1 LEU A 710    13522  16179  18751   -928  -5901    305       C  
ATOM   1094  CD2 LEU A 710     -33.485 187.969-212.143  1.00127.99           C  
ANISOU 1094  CD2 LEU A 710    14018  16783  17828   -284  -5934    311       C  
ATOM   1095  N   ARG A 711     -29.200 185.749-214.883  1.00121.23           N  
ANISOU 1095  N   ARG A 711    14817  15739  15504    131  -6299   -805       N  
ATOM   1096  CA  ARG A 711     -27.751 185.566-214.966  1.00118.27           C  
ANISOU 1096  CA  ARG A 711    14864  15310  14762    216  -6012   -865       C  
ATOM   1097  C   ARG A 711     -27.109 186.672-215.802  1.00117.36           C  
ANISOU 1097  C   ARG A 711    15133  15526  13933    611  -5826   -771       C  
ATOM   1098  O   ARG A 711     -26.238 187.403-215.330  1.00112.25           O  
ANISOU 1098  O   ARG A 711    14673  14896  13082    658  -5329   -489       O  
ATOM   1099  CB  ARG A 711     -27.432 184.192-215.563  1.00119.22           C  
ANISOU 1099  CB  ARG A 711    15076  15232  14991    167  -6403  -1349       C  
ATOM   1100  CG  ARG A 711     -26.268 183.465-214.909  1.00113.38           C  
ANISOU 1100  CG  ARG A 711    14499  14202  14378      4  -6104  -1354       C  
ATOM   1101  CD  ARG A 711     -26.250 182.003-215.326  1.00115.53           C  
ANISOU 1101  CD  ARG A 711    14733  14185  14978   -108  -6541  -1828       C  
ATOM   1102  NE  ARG A 711     -24.950 181.379-215.108  1.00111.14           N  
ANISOU 1102  NE  ARG A 711    14443  13423  14360   -125  -6308  -1917       N  
ATOM   1103  CZ  ARG A 711     -24.635 180.151-215.506  1.00112.34           C  
ANISOU 1103  CZ  ARG A 711    14644  13306  14732   -167  -6617  -2348       C  
ATOM   1104  NH1 ARG A 711     -23.425 179.665-215.268  1.00109.75           N1+
ANISOU 1104  NH1 ARG A 711    14549  12801  14350   -160  -6371  -2395       N1+
ATOM   1105  NH2 ARG A 711     -25.529 179.409-216.144  1.00116.63           N  
ANISOU 1105  NH2 ARG A 711    14984  13743  15585   -207  -7190  -2756       N  
ATOM   1106  N   ARG A 712     -27.545 186.781-217.051  1.00122.27           N  
ANISOU 1106  N   ARG A 712    15858  16410  14191    903  -6235  -1004       N  
ATOM   1107  CA  ARG A 712     -27.150 187.890-217.906  1.00124.08           C  
ANISOU 1107  CA  ARG A 712    16407  16985  13754   1307  -6078   -838       C  
ATOM   1108  C   ARG A 712     -27.860 189.152-217.433  1.00124.19           C  
ANISOU 1108  C   ARG A 712    16215  17106  13864   1339  -5866   -400       C  
ATOM   1109  O   ARG A 712     -29.073 189.145-217.220  1.00129.98           O  
ANISOU 1109  O   ARG A 712    16580  17841  14967   1232  -6150   -393       O  
ATOM   1110  CB  ARG A 712     -27.504 187.592-219.367  1.00131.95           C  
ANISOU 1110  CB  ARG A 712    17562  18273  14299   1643  -6619  -1213       C  
ATOM   1111  CG  ARG A 712     -28.907 187.023-219.570  1.00137.18           C  
ANISOU 1111  CG  ARG A 712    17839  18925  15359   1540  -7246  -1493       C  
ATOM   1112  CD  ARG A 712     -29.150 186.583-221.005  1.00143.43           C  
ANISOU 1112  CD  ARG A 712    18801  20000  15697   1874  -7800  -1958       C  
ATOM   1113  NE  ARG A 712     -29.801 185.275-221.067  1.00148.57           N  
ANISOU 1113  NE  ARG A 712    19158  20393  16897   1611  -8209  -2427       N  
ATOM   1114  CZ  ARG A 712     -31.095 185.068-220.839  1.00153.76           C  
ANISOU 1114  CZ  ARG A 712    19353  20954  18117   1408  -8518  -2474       C  
ATOM   1115  NH1 ARG A 712     -31.889 186.083-220.524  1.00154.24           N1+
ANISOU 1115  NH1 ARG A 712    19184  21171  18250   1446  -8478  -2095       N1+
ATOM   1116  NH2 ARG A 712     -31.595 183.842-220.921  1.00158.12           N  
ANISOU 1116  NH2 ARG A 712    19655  21228  19195   1175  -8848  -2894       N  
ATOM   1117  N   THR A 713     -27.107 190.232-217.256  1.00117.24           N  
ANISOU 1117  N   THR A 713    15546  16294  12707   1484  -5364    -45       N  
ATOM   1118  CA  THR A 713     -27.692 191.493-216.817  1.00112.29           C  
ANISOU 1118  CA  THR A 713    14743  15736  12187   1543  -5137    353       C  
ATOM   1119  C   THR A 713     -28.220 192.247-218.023  1.00120.69           C  
ANISOU 1119  C   THR A 713    15917  17133  12808   1949  -5386    436       C  
ATOM   1120  O   THR A 713     -27.588 193.181-218.507  1.00122.74           O  
ANISOU 1120  O   THR A 713    16451  17528  12656   2229  -5089    701       O  
ATOM   1121  CB  THR A 713     -26.666 192.372-216.094  1.00102.78           C  
ANISOU 1121  CB  THR A 713    13687  14417  10949   1525  -4511    677       C  
ATOM   1122  OG1 THR A 713     -25.895 191.569-215.192  1.00100.94           O  
ANISOU 1122  OG1 THR A 713    13457  13928  10968   1227  -4306    560       O  
ATOM   1123  CG2 THR A 713     -27.367 193.480-215.320  1.00 97.13           C  
ANISOU 1123  CG2 THR A 713    12700  13678  10526   1498  -4291   1010       C  
ATOM   1124  N   GLU A 714     -29.380 191.829-218.510  1.00127.46           N  
ANISOU 1124  N   GLU A 714    16543  18116  13771   1985  -5940    220       N  
ATOM   1125  CA  GLU A 714     -29.950 192.415-219.712  1.00134.62           C  
ANISOU 1125  CA  GLU A 714    17545  19378  14225   2400  -6275    257       C  
ATOM   1126  C   GLU A 714     -31.146 193.285-219.363  1.00135.75           C  
ANISOU 1126  C   GLU A 714    17322  19567  14691   2425  -6346    533       C  
ATOM   1127  O   GLU A 714     -31.827 193.807-220.250  1.00142.05           O  
ANISOU 1127  O   GLU A 714    18117  20652  15206   2761  -6671    597       O  
ATOM   1128  CB  GLU A 714     -30.385 191.314-220.676  1.00142.07           C  
ANISOU 1128  CB  GLU A 714    18503  20477  15000   2493  -6938   -260       C  
ATOM   1129  CG  GLU A 714     -31.562 190.499-220.176  1.00145.17           C  
ANISOU 1129  CG  GLU A 714    18400  20694  16064   2172  -7384   -529       C  
ATOM   1130  CD  GLU A 714     -32.044 189.502-221.204  1.00152.68           C  
ANISOU 1130  CD  GLU A 714    19329  21769  16915   2248  -7973  -1057       C  
ATOM   1131  OE1 GLU A 714     -31.195 188.934-221.922  1.00154.26           O  
ANISOU 1131  OE1 GLU A 714    19888  22032  16693   2373  -7953  -1330       O  
ATOM   1132  OE2 GLU A 714     -33.271 189.296-221.300  1.00157.58           O1-
ANISOU 1132  OE2 GLU A 714    19553  22398  17920   2151  -8327  -1185       O1-
ATOM   1133  N   SER A 715     -31.401 193.438-218.067  1.00129.09           N  
ANISOU 1133  N   SER A 715    16166  18462  14423   2095  -6043    696       N  
ATOM   1134  CA  SER A 715     -32.556 194.202-217.611  1.00127.27           C  
ANISOU 1134  CA  SER A 715    15538  18253  14565   2097  -6077    929       C  
ATOM   1135  C   SER A 715     -32.211 195.173-216.488  1.00118.93           C  
ANISOU 1135  C   SER A 715    14422  17018  13749   1996  -5461   1295       C  
ATOM   1136  O   SER A 715     -31.119 195.117-215.923  1.00113.50           O  
ANISOU 1136  O   SER A 715    13948  16161  13017   1858  -5039   1337       O  
ATOM   1137  CB  SER A 715     -33.669 193.258-217.151  1.00129.07           C  
ANISOU 1137  CB  SER A 715    15285  18378  15379   1792  -6468    672       C  
ATOM   1138  OG  SER A 715     -33.199 192.381-216.142  1.00123.70           O  
ANISOU 1138  OG  SER A 715    14527  17408  15064   1392  -6232    569       O  
ATOM   1139  N   ILE A 716     -33.148 196.069-216.183  1.00116.82           N  
ANISOU 1139  N   ILE A 716    13851  16791  13744   2085  -5436   1530       N  
ATOM   1140  CA  ILE A 716     -33.023 196.959-215.033  1.00111.93           C  
ANISOU 1140  CA  ILE A 716    13098  16001  13430   1989  -4910   1804       C  
ATOM   1141  C   ILE A 716     -33.459 196.220-213.773  1.00111.75           C  
ANISOU 1141  C   ILE A 716    12705  15813  13943   1589  -4821   1687       C  
ATOM   1142  O   ILE A 716     -32.817 196.320-212.723  1.00108.30           O  
ANISOU 1142  O   ILE A 716    12297  15210  13643   1404  -4374   1758       O  
ATOM   1143  CB  ILE A 716     -33.882 198.228-215.200  1.00112.98           C  
ANISOU 1143  CB  ILE A 716    13036  16232  13658   2272  -4911   2090       C  
ATOM   1144  CG1 ILE A 716     -33.428 199.026-216.423  1.00117.36           C  
ANISOU 1144  CG1 ILE A 716    13965  16945  13681   2694  -4947   2299       C  
ATOM   1145  CG2 ILE A 716     -33.812 199.096-213.952  1.00107.48           C  
ANISOU 1145  CG2 ILE A 716    12169  15345  13324   2173  -4392   2293       C  
ATOM   1146  CD1 ILE A 716     -34.407 200.106-216.839  1.00122.72           C  
ANISOU 1146  CD1 ILE A 716    14451  17750  14428   3022  -5093   2570       C  
ATOM   1147  N   VAL A 717     -34.540 195.456-213.906  1.00116.15           N  
ANISOU 1147  N   VAL A 717    12908  16423  14799   1467  -5258   1510       N  
ATOM   1148  CA  VAL A 717     -35.128 194.687-212.810  1.00116.92           C  
ANISOU 1148  CA  VAL A 717    12594  16379  15453   1097  -5205   1447       C  
ATOM   1149  C   VAL A 717     -34.122 193.915-211.955  1.00116.42           C  
ANISOU 1149  C   VAL A 717    12694  16112  15429    801  -4877   1388       C  
ATOM   1150  O   VAL A 717     -34.341 193.738-210.766  1.00116.66           O  
ANISOU 1150  O   VAL A 717    12462  16040  15824    564  -4589   1490       O  
ATOM   1151  CB  VAL A 717     -36.172 193.676-213.335  1.00121.53           C  
ANISOU 1151  CB  VAL A 717    12839  16998  16339    980  -5796   1192       C  
ATOM   1152  CG1 VAL A 717     -37.153 193.303-212.231  1.00121.45           C  
ANISOU 1152  CG1 VAL A 717    12267  16882  16996    676  -5700   1267       C  
ATOM   1153  CG2 VAL A 717     -36.909 194.243-214.539  1.00126.71           C  
ANISOU 1153  CG2 VAL A 717    13463  17899  16780   1336  -6260   1161       C  
ATOM   1154  N   GLU A 718     -33.029 193.452-212.551  1.00118.16           N  
ANISOU 1154  N   GLU A 718    13338  16293  15263    838  -4914   1234       N  
ATOM   1155  CA  GLU A 718     -32.079 192.615-211.820  1.00118.71           C  
ANISOU 1155  CA  GLU A 718    13553  16165  15388    572  -4668   1157       C  
ATOM   1156  C   GLU A 718     -31.322 193.396-210.755  1.00118.55           C  
ANISOU 1156  C   GLU A 718    13636  16077  15332    551  -4088   1383       C  
ATOM   1157  O   GLU A 718     -31.296 193.013-209.570  1.00120.36           O  
ANISOU 1157  O   GLU A 718    13686  16196  15847    307  -3835   1448       O  
ATOM   1158  CB  GLU A 718     -31.106 191.944-212.786  1.00119.69           C  
ANISOU 1158  CB  GLU A 718    14090  16274  15114    652  -4863    910       C  
ATOM   1159  CG  GLU A 718     -31.794 190.989-213.745  1.00127.77           C  
ANISOU 1159  CG  GLU A 718    15006  17340  16200    651  -5474    588       C  
ATOM   1160  CD  GLU A 718     -30.902 190.551-214.888  1.00130.21           C  
ANISOU 1160  CD  GLU A 718    15753  17720  16003    845  -5680    322       C  
ATOM   1161  OE1 GLU A 718     -29.855 189.922-214.616  1.00127.28           O  
ANISOU 1161  OE1 GLU A 718    15611  17184  15567    718  -5486    222       O  
ATOM   1162  OE2 GLU A 718     -31.253 190.839-216.055  1.00133.16           O1-
ANISOU 1162  OE2 GLU A 718    16235  18334  16028   1148  -6035    214       O1-
ATOM   1163  N   LYS A 719     -30.705 194.496-211.173  1.00117.85           N  
ANISOU 1163  N   LYS A 719    13824  16054  14900    819  -3883   1506       N  
ATOM   1164  CA  LYS A 719     -29.979 195.334-210.233  1.00114.29           C  
ANISOU 1164  CA  LYS A 719    13456  15521  14450    822  -3375   1669       C  
ATOM   1165  C   LYS A 719     -30.963 195.898-209.215  1.00105.61           C  
ANISOU 1165  C   LYS A 719    11956  14451  13722    770  -3206   1812       C  
ATOM   1166  O   LYS A 719     -30.644 196.030-208.028  1.00 99.31           O  
ANISOU 1166  O   LYS A 719    11086  13590  13058    646  -2851   1860       O  
ATOM   1167  CB  LYS A 719     -29.230 196.451-210.960  1.00120.46           C  
ANISOU 1167  CB  LYS A 719    14557  16326  14887   1121  -3203   1795       C  
ATOM   1168  CG  LYS A 719     -28.211 197.159-210.086  1.00122.16           C  
ANISOU 1168  CG  LYS A 719    14897  16399  15120   1099  -2716   1880       C  
ATOM   1169  CD  LYS A 719     -27.254 196.166-209.435  1.00122.70           C  
ANISOU 1169  CD  LYS A 719    15089  16353  15178    853  -2595   1723       C  
ATOM   1170  CE  LYS A 719     -26.394 196.852-208.380  1.00122.12           C  
ANISOU 1170  CE  LYS A 719    15058  16163  15180    820  -2158   1768       C  
ATOM   1171  NZ  LYS A 719     -25.578 195.891-207.585  1.00120.38           N1+
ANISOU 1171  NZ  LYS A 719    14906  15856  14976    591  -2057   1638       N1+
ATOM   1172  N   LEU A 720     -32.169 196.199-209.689  1.00104.27           N  
ANISOU 1172  N   LEU A 720    11515  14401  13702    887  -3476   1862       N  
ATOM   1173  CA  LEU A 720     -33.262 196.622-208.825  1.00103.38           C  
ANISOU 1173  CA  LEU A 720    10964  14340  13977    849  -3359   1979       C  
ATOM   1174  C   LEU A 720     -33.445 195.583-207.724  1.00106.67           C  
ANISOU 1174  C   LEU A 720    11139  14699  14689    516  -3246   1944       C  
ATOM   1175  O   LEU A 720     -33.572 195.923-206.550  1.00105.11           O  
ANISOU 1175  O   LEU A 720    10762  14519  14658    457  -2884   2047       O  
ATOM   1176  CB  LEU A 720     -34.552 196.759-209.641  1.00103.51           C  
ANISOU 1176  CB  LEU A 720    10693  14490  14145    989  -3777   1993       C  
ATOM   1177  CG  LEU A 720     -35.563 197.868-209.326  1.00100.32           C  
ANISOU 1177  CG  LEU A 720     9951  14172  13996   1174  -3675   2163       C  
ATOM   1178  CD1 LEU A 720     -36.636 197.908-210.406  1.00101.08           C  
ANISOU 1178  CD1 LEU A 720     9842  14407  14155   1349  -4182   2151       C  
ATOM   1179  CD2 LEU A 720     -36.192 197.685-207.954  1.00 99.98           C  
ANISOU 1179  CD2 LEU A 720     9496  14129  14364    967  -3390   2212       C  
ATOM   1180  N   LEU A 721     -33.424 194.313-208.120  1.00111.76           N  
ANISOU 1180  N   LEU A 721    11795  15278  15392    319  -3553   1800       N  
ATOM   1181  CA  LEU A 721     -33.625 193.191-207.209  1.00115.07           C  
ANISOU 1181  CA  LEU A 721    11978  15602  16141     -5  -3486   1809       C  
ATOM   1182  C   LEU A 721     -32.516 193.116-206.170  1.00111.52           C  
ANISOU 1182  C   LEU A 721    11751  15081  15542    -99  -3053   1868       C  
ATOM   1183  O   LEU A 721     -32.758 192.760-205.012  1.00110.95           O  
ANISOU 1183  O   LEU A 721    11447  15012  15696   -270  -2797   2000       O  
ATOM   1184  CB  LEU A 721     -33.694 191.879-207.992  1.00119.89           C  
ANISOU 1184  CB  LEU A 721    12598  16094  16862   -171  -3939   1603       C  
ATOM   1185  CG  LEU A 721     -33.979 190.610-207.188  1.00125.77           C  
ANISOU 1185  CG  LEU A 721    13065  16677  18047   -520  -3922   1639       C  
ATOM   1186  CD1 LEU A 721     -35.258 190.779-206.381  1.00130.89           C  
ANISOU 1186  CD1 LEU A 721    13168  17405  19158   -618  -3790   1852       C  
ATOM   1187  CD2 LEU A 721     -34.079 189.405-208.112  1.00128.93           C  
ANISOU 1187  CD2 LEU A 721    13466  16915  18606   -652  -4432   1372       C  
ATOM   1188  N   THR A 722     -31.296 193.444-206.587  1.00108.82           N  
ANISOU 1188  N   THR A 722    11846  14690  14812     26  -2971   1782       N  
ATOM   1189  CA  THR A 722     -30.195 193.519-205.632  1.00106.21           C  
ANISOU 1189  CA  THR A 722    11719  14303  14334    -25  -2586   1812       C  
ATOM   1190  C   THR A 722     -30.461 194.619-204.607  1.00103.63           C  
ANISOU 1190  C   THR A 722    11227  14088  14061     83  -2210   1939       C  
ATOM   1191  O   THR A 722     -30.308 194.416-203.394  1.00 99.30           O  
ANISOU 1191  O   THR A 722    10582  13575  13574    -23  -1927   2006       O  
ATOM   1192  CB  THR A 722     -28.858 193.798-206.329  1.00106.09           C  
ANISOU 1192  CB  THR A 722    12157  14211  13943    109  -2556   1697       C  
ATOM   1193  OG1 THR A 722     -28.543 192.714-207.212  1.00109.45           O  
ANISOU 1193  OG1 THR A 722    12748  14547  14291     27  -2882   1537       O  
ATOM   1194  CG2 THR A 722     -27.747 193.954-205.302  1.00100.41           C  
ANISOU 1194  CG2 THR A 722    11598  13435  13117     66  -2183   1705       C  
ATOM   1195  N   ASN A 723     -30.868 195.782-205.110  1.00105.37           N  
ANISOU 1195  N   ASN A 723    11418  14370  14247    320  -2217   1968       N  
ATOM   1196  CA  ASN A 723     -31.195 196.913-204.253  1.00104.18           C  
ANISOU 1196  CA  ASN A 723    11097  14301  14187    463  -1895   2041       C  
ATOM   1197  C   ASN A 723     -32.259 196.552-203.223  1.00109.45           C  
ANISOU 1197  C   ASN A 723    11337  15102  15148    339  -1775   2142       C  
ATOM   1198  O   ASN A 723     -32.104 196.841-202.037  1.00109.56           O  
ANISOU 1198  O   ASN A 723    11275  15198  15154    346  -1429   2163       O  
ATOM   1199  CB  ASN A 723     -31.660 198.106-205.091  1.00101.96           C  
ANISOU 1199  CB  ASN A 723    10800  14032  13909    738  -1985   2087       C  
ATOM   1200  CG  ASN A 723     -30.550 198.691-205.941  1.00 99.67           C  
ANISOU 1200  CG  ASN A 723    10917  13618  13334    898  -1975   2059       C  
ATOM   1201  OD1 ASN A 723     -29.370 198.450-205.693  1.00 96.92           O  
ANISOU 1201  OD1 ASN A 723    10837  13175  12814    822  -1820   1978       O  
ATOM   1202  ND2 ASN A 723     -30.925 199.475-206.945  1.00101.65           N  
ANISOU 1202  ND2 ASN A 723    11200  13876  13546   1135  -2129   2151       N  
ATOM   1203  N   TRP A 724     -33.325 195.903-203.685  1.00112.72           N  
ANISOU 1203  N   TRP A 724    11460  15549  15821    235  -2063   2198       N  
ATOM   1204  CA  TRP A 724     -34.458 195.546-202.836  1.00116.36           C  
ANISOU 1204  CA  TRP A 724    11450  16129  16632    114  -1952   2336       C  
ATOM   1205  C   TRP A 724     -34.088 194.492-201.805  1.00117.49           C  
ANISOU 1205  C   TRP A 724    11567  16264  16810   -132  -1743   2423       C  
ATOM   1206  O   TRP A 724     -34.512 194.565-200.644  1.00119.62           O  
ANISOU 1206  O   TRP A 724    11584  16685  17181   -149  -1407   2563       O  
ATOM   1207  CB  TRP A 724     -35.615 195.042-203.686  1.00120.10           C  
ANISOU 1207  CB  TRP A 724    11602  16597  17432     43  -2362   2351       C  
ATOM   1208  CG  TRP A 724     -36.827 194.674-202.897  1.00124.28           C  
ANISOU 1208  CG  TRP A 724    11591  17230  18398    -92  -2244   2517       C  
ATOM   1209  CD1 TRP A 724     -37.832 195.509-202.501  1.00126.22           C  
ANISOU 1209  CD1 TRP A 724    11463  17637  18856     62  -2082   2610       C  
ATOM   1210  CD2 TRP A 724     -37.176 193.371-202.419  1.00125.81           C  
ANISOU 1210  CD2 TRP A 724    11528  17360  18912   -403  -2255   2631       C  
ATOM   1211  NE1 TRP A 724     -38.782 194.807-201.804  1.00128.73           N  
ANISOU 1211  NE1 TRP A 724    11300  18023  19587   -133  -1972   2781       N  
ATOM   1212  CE2 TRP A 724     -38.405 193.489-201.740  1.00128.74           C  
ANISOU 1212  CE2 TRP A 724    11360  17876  19678   -429  -2072   2817       C  
ATOM   1213  CE3 TRP A 724     -36.569 192.114-202.499  1.00125.29           C  
ANISOU 1213  CE3 TRP A 724    11621  17108  18877   -657  -2391   2609       C  
ATOM   1214  CZ2 TRP A 724     -39.039 192.404-201.144  1.00132.12           C  
ANISOU 1214  CZ2 TRP A 724    11396  18267  20537   -712  -1998   3016       C  
ATOM   1215  CZ3 TRP A 724     -37.199 191.037-201.907  1.00129.41           C  
ANISOU 1215  CZ3 TRP A 724    11765  17562  19844   -936  -2343   2796       C  
ATOM   1216  CH2 TRP A 724     -38.421 191.188-201.238  1.00132.66           C  
ANISOU 1216  CH2 TRP A 724    11632  18119  20652   -968  -2137   3015       C  
ATOM   1217  N   MET A 725     -33.308 193.506-202.238  1.00117.14           N  
ANISOU 1217  N   MET A 725    11783  16053  16673   -297  -1937   2351       N  
ATOM   1218  CA  MET A 725     -32.767 192.516-201.317  1.00116.97           C  
ANISOU 1218  CA  MET A 725    11800  15987  16655   -503  -1750   2452       C  
ATOM   1219  C   MET A 725     -32.000 193.221-200.212  1.00110.43           C  
ANISOU 1219  C   MET A 725    11140  15296  15523   -366  -1329   2465       C  
ATOM   1220  O   MET A 725     -32.153 192.896-199.043  1.00108.52           O  
ANISOU 1220  O   MET A 725    10735  15184  15313   -430  -1039   2634       O  
ATOM   1221  CB  MET A 725     -31.847 191.537-202.045  1.00118.77           C  
ANISOU 1221  CB  MET A 725    12349  15990  16788   -637  -2024   2319       C  
ATOM   1222  CG  MET A 725     -32.583 190.474-202.827  1.00123.60           C  
ANISOU 1222  CG  MET A 725    12748  16446  17766   -833  -2431   2286       C  
ATOM   1223  SD  MET A 725     -33.600 189.470-201.744  1.00135.82           S  
ANISOU 1223  SD  MET A 725    13782  17979  19846  -1114  -2273   2593       S  
ATOM   1224  CE  MET A 725     -34.395 188.409-202.952  1.00138.36           C  
ANISOU 1224  CE  MET A 725    13867  18055  20649  -1316  -2857   2436       C  
ATOM   1225  N   SER A 726     -31.191 194.202-200.597  1.00106.95           N  
ANISOU 1225  N   SER A 726    11010  14829  14797   -164  -1302   2288       N  
ATOM   1226  CA  SER A 726     -30.369 194.955-199.653  1.00104.63           C  
ANISOU 1226  CA  SER A 726    10884  14628  14245    -20   -964   2217       C  
ATOM   1227  C   SER A 726     -31.214 195.739-198.645  1.00102.75           C  
ANISOU 1227  C   SER A 726    10333  14625  14082    122   -661   2282       C  
ATOM   1228  O   SER A 726     -31.001 195.646-197.426  1.00101.15           O  
ANISOU 1228  O   SER A 726    10092  14595  13748    139   -369   2325       O  
ATOM   1229  CB  SER A 726     -29.464 195.910-200.428  1.00106.40           C  
ANISOU 1229  CB  SER A 726    11436  14722  14270    158  -1020   2025       C  
ATOM   1230  OG  SER A 726     -29.071 195.325-201.660  1.00108.57           O  
ANISOU 1230  OG  SER A 726    11925  14825  14503     83  -1335   1978       O  
ATOM   1231  N   ILE A 727     -32.162 196.510-199.178  1.00101.04           N  
ANISOU 1231  N   ILE A 727     9900  14434  14055    252   -740   2282       N  
ATOM   1232  CA  ILE A 727     -33.124 197.274-198.394  1.00100.41           C  
ANISOU 1232  CA  ILE A 727     9477  14566  14108    410   -483   2328       C  
ATOM   1233  C   ILE A 727     -33.813 196.420-197.353  1.00103.75           C  
ANISOU 1233  C   ILE A 727     9581  15193  14648    268   -269   2546       C  
ATOM   1234  O   ILE A 727     -33.856 196.776-196.177  1.00105.42           O  
ANISOU 1234  O   ILE A 727     9698  15634  14722    390     86   2554       O  
ATOM   1235  CB  ILE A 727     -34.228 197.851-199.294  1.00101.94           C  
ANISOU 1235  CB  ILE A 727     9416  14732  14584    515   -692   2358       C  
ATOM   1236  CG1 ILE A 727     -33.677 198.973-200.175  1.00103.52           C  
ANISOU 1236  CG1 ILE A 727     9889  14771  14674    733   -809   2205       C  
ATOM   1237  CG2 ILE A 727     -35.404 198.350-198.458  1.00102.53           C  
ANISOU 1237  CG2 ILE A 727     9045  15036  14875    636   -431   2443       C  
ATOM   1238  CD1 ILE A 727     -34.704 199.555-201.132  1.00106.40           C  
ANISOU 1238  CD1 ILE A 727    10037  15112  15277    875  -1048   2263       C  
ATOM   1239  N   CYS A 728     -34.354 195.290-197.793  1.00106.45           N  
ANISOU 1239  N   CYS A 728     9747  15448  15253     20   -483   2723       N  
ATOM   1240  CA  CYS A 728     -35.162 194.458-196.910  1.00111.24           C  
ANISOU 1240  CA  CYS A 728     9976  16208  16084   -135   -273   3004       C  
ATOM   1241  C   CYS A 728     -34.338 193.587-195.959  1.00111.63           C  
ANISOU 1241  C   CYS A 728    10203  16305  15906   -254    -60   3139       C  
ATOM   1242  O   CYS A 728     -34.786 193.272-194.860  1.00114.58           O  
ANISOU 1242  O   CYS A 728    10334  16907  16295   -264    279   3381       O  
ATOM   1243  CB  CYS A 728     -36.143 193.607-197.723  1.00114.05           C  
ANISOU 1243  CB  CYS A 728    10003  16413  16917   -363   -595   3136       C  
ATOM   1244  SG  CYS A 728     -37.373 194.562-198.655  1.00146.87           S  
ANISOU 1244  SG  CYS A 728    13831  20593  21381   -197   -834   3042       S  
ATOM   1245  N   LEU A 729     -33.130 193.218-196.374  1.00110.94           N  
ANISOU 1245  N   LEU A 729    10534  16022  15597   -318   -242   3003       N  
ATOM   1246  CA  LEU A 729     -32.292 192.306-195.589  1.00112.44           C  
ANISOU 1246  CA  LEU A 729    10904  16220  15599   -430   -105   3137       C  
ATOM   1247  C   LEU A 729     -31.253 193.004-194.716  1.00108.94           C  
ANISOU 1247  C   LEU A 729    10753  15957  14684   -209    142   2975       C  
ATOM   1248  O   LEU A 729     -30.524 192.325-193.984  1.00107.92           O  
ANISOU 1248  O   LEU A 729    10777  15877  14349   -256    255   3085       O  
ATOM   1249  CB  LEU A 729     -31.586 191.278-196.488  1.00112.18           C  
ANISOU 1249  CB  LEU A 729    11113  15853  15656   -646   -459   3092       C  
ATOM   1250  CG  LEU A 729     -32.414 190.192-197.179  1.00116.16           C  
ANISOU 1250  CG  LEU A 729    11347  16138  16650   -914   -736   3239       C  
ATOM   1251  CD1 LEU A 729     -31.674 189.654-198.397  1.00114.29           C  
ANISOU 1251  CD1 LEU A 729    11417  15589  16420  -1013  -1154   3009       C  
ATOM   1252  CD2 LEU A 729     -32.735 189.064-196.216  1.00118.40           C  
ANISOU 1252  CD2 LEU A 729    11392  16438  17158  -1109   -523   3619       C  
ATOM   1253  N   TYR A 730     -31.172 194.336-194.794  1.00105.53           N  
ANISOU 1253  N   TYR A 730    10385  15602  14109     35    202   2711       N  
ATOM   1254  CA  TYR A 730     -30.235 195.068-193.939  1.00102.07           C  
ANISOU 1254  CA  TYR A 730    10178  15320  13284    252    409   2494       C  
ATOM   1255  C   TYR A 730     -30.357 194.645-192.482  1.00104.41           C  
ANISOU 1255  C   TYR A 730    10354  15962  13354    311    745   2688       C  
ATOM   1256  O   TYR A 730     -29.352 194.343-191.819  1.00105.10           O  
ANISOU 1256  O   TYR A 730    10684  16126  13123    351    805   2646       O  
ATOM   1257  CB  TYR A 730     -30.415 196.586-194.010  1.00100.94           C  
ANISOU 1257  CB  TYR A 730    10005  15225  13122    518    487   2211       C  
ATOM   1258  CG  TYR A 730     -29.504 197.285-193.017  1.00 99.40           C  
ANISOU 1258  CG  TYR A 730     9998  15191  12578    738    684   1945       C  
ATOM   1259  CD1 TYR A 730     -28.156 197.470-193.304  1.00 97.29           C  
ANISOU 1259  CD1 TYR A 730    10080  14726  12160    743    545   1709       C  
ATOM   1260  CD2 TYR A 730     -29.973 197.713-191.779  1.00 99.59           C  
ANISOU 1260  CD2 TYR A 730     9835  15582  12424    948   1003   1914       C  
ATOM   1261  CE1 TYR A 730     -27.305 198.083-192.407  1.00 95.47           C  
ANISOU 1261  CE1 TYR A 730     9990  14626  11657    936    676   1426       C  
ATOM   1262  CE2 TYR A 730     -29.122 198.324-190.866  1.00 98.82           C  
ANISOU 1262  CE2 TYR A 730     9909  15649  11990   1168   1133   1609       C  
ATOM   1263  CZ  TYR A 730     -27.791 198.507-191.190  1.00 95.79           C  
ANISOU 1263  CZ  TYR A 730     9855  15032  11508   1152    948   1356       C  
ATOM   1264  OH  TYR A 730     -26.940 199.118-190.298  1.00 93.78           O  
ANISOU 1264  OH  TYR A 730     9739  14924  10970   1366   1031   1012       O  
ATOM   1265  N   GLY A 731     -31.593 194.639-191.991  1.00105.24           N  
ANISOU 1265  N   GLY A 731    10075  16295  13617    340    970   2911       N  
ATOM   1266  CA  GLY A 731     -31.867 194.256-190.620  1.00107.87           C  
ANISOU 1266  CA  GLY A 731    10254  17009  13722    427   1344   3157       C  
ATOM   1267  C   GLY A 731     -31.257 192.912-190.287  1.00107.26           C  
ANISOU 1267  C   GLY A 731    10315  16876  13562    232   1323   3458       C  
ATOM   1268  O   GLY A 731     -30.617 192.746-189.245  1.00108.31           O  
ANISOU 1268  O   GLY A 731    10600  17267  13286    370   1518   3505       O  
ATOM   1269  N   PHE A 732     -31.435 191.961-191.198  1.00105.76           N  
ANISOU 1269  N   PHE A 732    10077  16341  13768    -71   1059   3638       N  
ATOM   1270  CA  PHE A 732     -30.946 190.602-191.007  1.00106.05           C  
ANISOU 1270  CA  PHE A 732    10207  16237  13851   -283   1009   3941       C  
ATOM   1271  C   PHE A 732     -29.427 190.545-191.010  1.00103.00           C  
ANISOU 1271  C   PHE A 732    10274  15747  13113   -225    851   3705       C  
ATOM   1272  O   PHE A 732     -28.829 189.699-190.343  1.00101.87           O  
ANISOU 1272  O   PHE A 732    10250  15648  12807   -258    925   3932       O  
ATOM   1273  CB  PHE A 732     -31.509 189.675-192.084  1.00104.92           C  
ANISOU 1273  CB  PHE A 732     9891  15702  14274   -609    711   4090       C  
ATOM   1274  CG  PHE A 732     -31.077 188.250-191.933  1.00102.05           C  
ANISOU 1274  CG  PHE A 732     9587  15124  14064   -837    647   4397       C  
ATOM   1275  CD1 PHE A 732     -31.220 187.603-190.724  1.00105.04           C  
ANISOU 1275  CD1 PHE A 732     9834  15728  14350   -825    997   4839       C  
ATOM   1276  CD2 PHE A 732     -30.529 187.558-192.999  1.00 99.79           C  
ANISOU 1276  CD2 PHE A 732     9487  14414  14014  -1038    248   4253       C  
ATOM   1277  CE1 PHE A 732     -30.822 186.293-190.577  1.00108.15           C  
ANISOU 1277  CE1 PHE A 732    10274  15887  14930  -1024    943   5160       C  
ATOM   1278  CE2 PHE A 732     -30.131 186.246-192.857  1.00100.88           C  
ANISOU 1278  CE2 PHE A 732     9669  14314  14346  -1236    182   4517       C  
ATOM   1279  CZ  PHE A 732     -30.276 185.613-191.643  1.00105.85           C  
ANISOU 1279  CZ  PHE A 732    10158  15129  14929  -1236    527   4985       C  
ATOM   1280  N   LEU A 733     -28.811 191.447-191.769  1.00103.65           N  
ANISOU 1280  N   LEU A 733    10590  15683  13108   -131    641   3277       N  
ATOM   1281  CA  LEU A 733     -27.354 191.546-191.809  1.00103.54           C  
ANISOU 1281  CA  LEU A 733    10968  15568  12802    -62    505   3014       C  
ATOM   1282  C   LEU A 733     -26.812 192.022-190.469  1.00108.06           C  
ANISOU 1282  C   LEU A 733    11631  16519  12907    202    760   2934       C  
ATOM   1283  O   LEU A 733     -25.983 191.355-189.852  1.00109.32           O  
ANISOU 1283  O   LEU A 733    11963  16741  12833    214    770   3035       O  
ATOM   1284  CB  LEU A 733     -26.904 192.500-192.915  1.00 98.39           C  
ANISOU 1284  CB  LEU A 733    10496  14683  12205    -10    279   2618       C  
ATOM   1285  CG  LEU A 733     -26.319 191.864-194.174  1.00 95.09           C  
ANISOU 1285  CG  LEU A 733    10278  13876  11975   -204    -56   2553       C  
ATOM   1286  CD1 LEU A 733     -27.396 191.185-194.995  1.00 97.69           C  
ANISOU 1286  CD1 LEU A 733    10375  14038  12704   -413   -224   2748       C  
ATOM   1287  CD2 LEU A 733     -25.600 192.909-195.002  1.00 92.34           C  
ANISOU 1287  CD2 LEU A 733    10154  13374  11557    -84   -184   2192       C  
ATOM   1288  N   ARG A 734     -27.297 193.174-190.017  1.00110.29           N  
ANISOU 1288  N   ARG A 734    11789  17060  13056    435    949   2734       N  
ATOM   1289  CA  ARG A 734     -26.868 193.736-188.736  1.00111.04           C  
ANISOU 1289  CA  ARG A 734    11951  17554  12686    731   1172   2574       C  
ATOM   1290  C   ARG A 734     -27.209 192.819-187.553  1.00116.21           C  
ANISOU 1290  C   ARG A 734    12488  18572  13095    770   1446   3011       C  
ATOM   1291  O   ARG A 734     -26.587 192.898-186.488  1.00116.85           O  
ANISOU 1291  O   ARG A 734    12702  18985  12710   1000   1567   2942       O  
ATOM   1292  CB  ARG A 734     -27.498 195.119-188.548  1.00111.66           C  
ANISOU 1292  CB  ARG A 734    11872  17809  12745    975   1322   2267       C  
ATOM   1293  CG  ARG A 734     -27.082 195.826-187.279  1.00115.15           C  
ANISOU 1293  CG  ARG A 734    12376  18661  12714   1317   1516   1987       C  
ATOM   1294  CD  ARG A 734     -26.612 197.238-187.564  1.00113.71           C  
ANISOU 1294  CD  ARG A 734    12288  18340  12577   1499   1408   1424       C  
ATOM   1295  NE  ARG A 734     -26.242 197.916-186.327  1.00118.24           N  
ANISOU 1295  NE  ARG A 734    12900  19305  12720   1842   1557   1085       N  
ATOM   1296  CZ  ARG A 734     -25.829 199.176-186.257  1.00120.36           C  
ANISOU 1296  CZ  ARG A 734    13216  19510  13006   2054   1498    547       C  
ATOM   1297  NH1 ARG A 734     -25.727 199.904-187.360  1.00119.39           N1+
ANISOU 1297  NH1 ARG A 734    13111  18939  13313   1955   1327    354       N1+
ATOM   1298  NH2 ARG A 734     -25.518 199.708-185.082  1.00123.97           N  
ANISOU 1298  NH2 ARG A 734    13697  20349  13057   2378   1605    202       N  
ATOM   1299  N   GLU A 735     -28.191 191.940-187.753  1.00120.23           N  
ANISOU 1299  N   GLU A 735    12736  19014  13933    553   1534   3471       N  
ATOM   1300  CA  GLU A 735     -28.672 191.067-186.682  1.00126.87           C  
ANISOU 1300  CA  GLU A 735    13406  20175  14624    575   1852   3985       C  
ATOM   1301  C   GLU A 735     -27.959 189.715-186.577  1.00127.37           C  
ANISOU 1301  C   GLU A 735    13631  20062  14704    396   1745   4336       C  
ATOM   1302  O   GLU A 735     -27.566 189.301-185.485  1.00130.81           O  
ANISOU 1302  O   GLU A 735    14150  20821  14733    561   1938   4573       O  
ATOM   1303  CB  GLU A 735     -30.179 190.853-186.815  1.00131.81           C  
ANISOU 1303  CB  GLU A 735    13591  20831  15660    443   2061   4337       C  
ATOM   1304  N   SER A 736     -27.801 189.024-187.702  1.00124.16           N  
ANISOU 1304  N   SER A 736    13266  19152  14755     86   1434   4368       N  
ATOM   1305  CA  SER A 736     -27.383 187.627-187.651  1.00123.49           C  
ANISOU 1305  CA  SER A 736    13248  18841  14832   -114   1355   4759       C  
ATOM   1306  C   SER A 736     -26.210 187.270-188.553  1.00115.06           C  
ANISOU 1306  C   SER A 736    12504  17350  13865   -242    957   4482       C  
ATOM   1307  O   SER A 736     -25.633 186.192-188.421  1.00118.98           O  
ANISOU 1307  O   SER A 736    13109  17667  14431   -348    875   4736       O  
ATOM   1308  CB  SER A 736     -28.563 186.712-187.989  1.00128.64           C  
ANISOU 1308  CB  SER A 736    13530  19275  16074   -407   1421   5218       C  
ATOM   1309  OG  SER A 736     -29.636 186.895-187.082  1.00134.90           O  
ANISOU 1309  OG  SER A 736    13986  20467  16802   -295   1844   5561       O  
ATOM   1310  N   VAL A 737     -25.859 188.154-189.475  1.00105.35           N  
ANISOU 1310  N   VAL A 737    11415  15951  12660   -221    727   3987       N  
ATOM   1311  CA  VAL A 737     -24.840 187.808-190.452  1.00102.83           C  
ANISOU 1311  CA  VAL A 737    11368  15231  12471   -347    380   3741       C  
ATOM   1312  C   VAL A 737     -23.605 188.702-190.359  1.00104.73           C  
ANISOU 1312  C   VAL A 737    11907  15553  12332   -130    299   3294       C  
ATOM   1313  O   VAL A 737     -22.527 188.322-190.808  1.00102.82           O  
ANISOU 1313  O   VAL A 737    11904  15068  12097   -178     83   3144       O  
ATOM   1314  CB  VAL A 737     -25.394 187.860-191.884  1.00101.50           C  
ANISOU 1314  CB  VAL A 737    11119  14708  12739   -549    129   3582       C  
ATOM   1315  CG1 VAL A 737     -24.589 186.948-192.787  1.00100.32           C  
ANISOU 1315  CG1 VAL A 737    11178  14141  12800   -726   -186   3505       C  
ATOM   1316  CG2 VAL A 737     -26.858 187.456-191.896  1.00105.15           C  
ANISOU 1316  CG2 VAL A 737    11190  15178  13583   -706    237   3918       C  
ATOM   1317  N   GLY A 738     -23.768 189.882-189.770  1.00109.45           N  
ANISOU 1317  N   GLY A 738    12466  16478  12645    109    472   3069       N  
ATOM   1318  CA  GLY A 738     -22.697 190.855-189.700  1.00107.69           C  
ANISOU 1318  CA  GLY A 738    12464  16296  12158    305    389   2604       C  
ATOM   1319  C   GLY A 738     -21.499 190.401-188.895  1.00110.53           C  
ANISOU 1319  C   GLY A 738    13029  16775  12192    423    346   2587       C  
ATOM   1320  O   GLY A 738     -20.355 190.497-189.359  1.00109.16           O  
ANISOU 1320  O   GLY A 738    13066  16382  12029    417    138   2306       O  
ATOM   1321  N   GLN A 739     -21.758 189.904-187.689  1.00116.01           N  
ANISOU 1321  N   GLN A 739    13651  17834  12595    547    549   2906       N  
ATOM   1322  CA  GLN A 739     -20.689 189.438-186.807  1.00119.64           C  
ANISOU 1322  CA  GLN A 739    14293  18473  12693    705    502   2937       C  
ATOM   1323  C   GLN A 739     -19.775 188.379-187.444  1.00115.98           C  
ANISOU 1323  C   GLN A 739    14000  17607  12459    513    249   3041       C  
ATOM   1324  O   GLN A 739     -18.564 188.579-187.486  1.00112.99           O  
ANISOU 1324  O   GLN A 739    13813  17155  11962    602     62   2726       O  
ATOM   1325  CB  GLN A 739     -21.237 188.964-185.448  1.00128.35           C  
ANISOU 1325  CB  GLN A 739    15285  20057  13425    882    789   3370       C  
ATOM   1326  CG  GLN A 739     -20.158 188.391-184.536  1.00134.86           C  
ANISOU 1326  CG  GLN A 739    16303  21090  13848   1070    716   3463       C  
ATOM   1327  CD  GLN A 739     -20.645 188.139-183.119  1.00145.06           C  
ANISOU 1327  CD  GLN A 739    17514  22959  14645   1334   1022   3852       C  
ATOM   1328  OE1 GLN A 739     -21.802 188.409-182.791  1.00149.38           O  
ANISOU 1328  OE1 GLN A 739    17842  23758  15156   1374   1324   4048       O  
ATOM   1329  NE2 GLN A 739     -19.761 187.623-182.269  1.00147.74           N  
ANISOU 1329  NE2 GLN A 739    18020  23532  14583   1539    953   3978       N  
ATOM   1330  N   PRO A 740     -20.340 187.266-187.962  1.00115.51           N  
ANISOU 1330  N   PRO A 740    13849  17265  12774    254    232   3449       N  
ATOM   1331  CA  PRO A 740     -19.429 186.280-188.552  1.00114.02           C  
ANISOU 1331  CA  PRO A 740    13826  16685  12810    105    -16   3490       C  
ATOM   1332  C   PRO A 740     -18.693 186.790-189.793  1.00109.91           C  
ANISOU 1332  C   PRO A 740    13459  15818  12483     25   -263   3012       C  
ATOM   1333  O   PRO A 740     -17.584 186.328-190.058  1.00110.59           O  
ANISOU 1333  O   PRO A 740    13722  15697  12601     18   -448   2896       O  
ATOM   1334  CB  PRO A 740     -20.354 185.116-188.923  1.00113.90           C  
ANISOU 1334  CB  PRO A 740    13636  16407  13235   -163     12   3959       C  
ATOM   1335  CG  PRO A 740     -21.679 185.735-189.097  1.00114.23           C  
ANISOU 1335  CG  PRO A 740    13430  16571  13400   -217    181   3993       C  
ATOM   1336  CD  PRO A 740     -21.738 186.812-188.051  1.00116.00           C  
ANISOU 1336  CD  PRO A 740    13640  17312  13123     85    410   3855       C  
ATOM   1337  N   LEU A 741     -19.293 187.716-190.539  1.00103.95           N  
ANISOU 1337  N   LEU A 741    12630  15010  11858    -16   -251   2767       N  
ATOM   1338  CA  LEU A 741     -18.637 188.279-191.716  1.00 98.90           C  
ANISOU 1338  CA  LEU A 741    12132  14078  11368    -62   -437   2368       C  
ATOM   1339  C   LEU A 741     -17.443 189.145-191.325  1.00 97.27           C  
ANISOU 1339  C   LEU A 741    12070  13984  10904    144   -464   1987       C  
ATOM   1340  O   LEU A 741     -16.363 189.056-191.927  1.00 95.30           O  
ANISOU 1340  O   LEU A 741    11978  13494  10739    122   -622   1772       O  
ATOM   1341  CB  LEU A 741     -19.611 189.091-192.566  1.00 98.73           C  
ANISOU 1341  CB  LEU A 741    11989  13993  11530   -123   -412   2252       C  
ATOM   1342  CG  LEU A 741     -18.968 189.830-193.745  1.00 96.95           C  
ANISOU 1342  CG  LEU A 741    11911  13517  11407   -123   -553   1885       C  
ATOM   1343  CD1 LEU A 741     -18.325 188.850-194.714  1.00 95.81           C  
ANISOU 1343  CD1 LEU A 741    11920  13031  11454   -273   -766   1885       C  
ATOM   1344  CD2 LEU A 741     -19.976 190.712-194.469  1.00 97.03           C  
ANISOU 1344  CD2 LEU A 741    11796  13514  11558   -132   -520   1815       C  
ATOM   1345  N   PHE A 742     -17.634 189.987-190.316  1.00 98.70           N  
ANISOU 1345  N   PHE A 742    12177  14529  10794    352   -310   1880       N  
ATOM   1346  CA  PHE A 742     -16.539 190.818-189.836  1.00 98.93           C  
ANISOU 1346  CA  PHE A 742    12302  14669  10616    554   -363   1477       C  
ATOM   1347  C   PHE A 742     -15.473 189.954-189.185  1.00 95.77           C  
ANISOU 1347  C   PHE A 742    12024  14325  10039    624   -484   1554       C  
ATOM   1348  O   PHE A 742     -14.278 190.246-189.267  1.00 93.22           O  
ANISOU 1348  O   PHE A 742    11802  13900   9716    695   -630   1236       O  
ATOM   1349  CB  PHE A 742     -17.024 191.864-188.835  1.00103.99           C  
ANISOU 1349  CB  PHE A 742    12829  15707  10975    791   -196   1299       C  
ATOM   1350  CG  PHE A 742     -15.939 192.796-188.379  1.00103.68           C  
ANISOU 1350  CG  PHE A 742    12854  15745  10794    994   -290    810       C  
ATOM   1351  CD1 PHE A 742     -15.356 193.679-189.274  1.00100.60           C  
ANISOU 1351  CD1 PHE A 742    12493  15031  10699    945   -378    446       C  
ATOM   1352  CD2 PHE A 742     -15.495 192.787-187.067  1.00104.86           C  
ANISOU 1352  CD2 PHE A 742    13021  16289  10532   1243   -298    719       C  
ATOM   1353  CE1 PHE A 742     -14.354 194.540-188.873  1.00100.05           C  
ANISOU 1353  CE1 PHE A 742    12436  14978  10600   1107   -472    -14       C  
ATOM   1354  CE2 PHE A 742     -14.494 193.648-186.659  1.00105.43           C  
ANISOU 1354  CE2 PHE A 742    13121  16415  10524   1427   -433    211       C  
ATOM   1355  CZ  PHE A 742     -13.924 194.524-187.564  1.00103.18           C  
ANISOU 1355  CZ  PHE A 742    12832  15752  10619   1342   -520   -162       C  
ATOM   1356  N   LEU A 743     -15.924 188.890-188.534  1.00 96.09           N  
ANISOU 1356  N   LEU A 743    12032  14516   9962    608   -415   2004       N  
ATOM   1357  CA  LEU A 743     -15.029 187.947-187.885  1.00 98.70           C  
ANISOU 1357  CA  LEU A 743    12471  14900  10132    688   -524   2176       C  
ATOM   1358  C   LEU A 743     -14.187 187.194-188.908  1.00 97.15           C  
ANISOU 1358  C   LEU A 743    12394  14240  10280    510   -735   2140       C  
ATOM   1359  O   LEU A 743     -13.031 186.875-188.643  1.00 99.24           O  
ANISOU 1359  O   LEU A 743    12763  14473  10470    608   -889   2034       O  
ATOM   1360  CB  LEU A 743     -15.812 186.969-187.000  1.00100.13           C  
ANISOU 1360  CB  LEU A 743    12571  15318  10157    707   -359   2752       C  
ATOM   1361  CG  LEU A 743     -16.256 187.497-185.632  1.00 98.82           C  
ANISOU 1361  CG  LEU A 743    12332  15733   9481    994   -152   2818       C  
ATOM   1362  CD1 LEU A 743     -17.047 186.444-184.866  1.00101.52           C  
ANISOU 1362  CD1 LEU A 743    12581  16278   9715    995     61   3483       C  
ATOM   1363  CD2 LEU A 743     -15.056 187.969-184.828  1.00 97.15           C  
ANISOU 1363  CD2 LEU A 743    12248  15792   8872   1288   -307   2456       C  
ATOM   1364  N   LEU A 744     -14.763 186.923-190.076  1.00 93.88           N  
ANISOU 1364  N   LEU A 744    11954  13483  10231    272   -753   2203       N  
ATOM   1365  CA  LEU A 744     -14.028 186.253-191.145  1.00 95.72           C  
ANISOU 1365  CA  LEU A 744    12304  13292  10773    126   -942   2118       C  
ATOM   1366  C   LEU A 744     -13.045 187.191-191.845  1.00 91.41           C  
ANISOU 1366  C   LEU A 744    11847  12613  10269    179  -1023   1639       C  
ATOM   1367  O   LEU A 744     -11.901 186.816-192.106  1.00 89.12           O  
ANISOU 1367  O   LEU A 744    11659  12143  10058    201  -1158   1500       O  
ATOM   1368  CB  LEU A 744     -14.973 185.631-192.176  1.00 98.36           C  
ANISOU 1368  CB  LEU A 744    12583  13331  11459   -118   -967   2301       C  
ATOM   1369  CG  LEU A 744     -14.262 185.021-193.390  1.00 96.59           C  
ANISOU 1369  CG  LEU A 744    12490  12691  11521   -237  -1164   2137       C  
ATOM   1370  CD1 LEU A 744     -13.408 183.829-192.981  1.00 95.18           C  
ANISOU 1370  CD1 LEU A 744    12388  12371  11404   -216  -1280   2305       C  
ATOM   1371  CD2 LEU A 744     -15.256 184.626-194.468  1.00 97.77           C  
ANISOU 1371  CD2 LEU A 744    12576  12595  11975   -442  -1227   2205       C  
ATOM   1372  N   VAL A 745     -13.495 188.402-192.163  1.00 89.44           N  
ANISOU 1372  N   VAL A 745    11540  12433  10010    203   -926   1410       N  
ATOM   1373  CA  VAL A 745     -12.605 189.398-192.757  1.00 85.12           C  
ANISOU 1373  CA  VAL A 745    11044  11753   9545    258   -957   1002       C  
ATOM   1374  C   VAL A 745     -11.411 189.649-191.839  1.00 86.49           C  
ANISOU 1374  C   VAL A 745    11235  12074   9555    440  -1029    774       C  
ATOM   1375  O   VAL A 745     -10.258 189.714-192.287  1.00 85.88           O  
ANISOU 1375  O   VAL A 745    11212  11797   9622    450  -1123    544       O  
ATOM   1376  CB  VAL A 745     -13.342 190.719-193.015  1.00 81.12           C  
ANISOU 1376  CB  VAL A 745    10447  11316   9061    290   -825    835       C  
ATOM   1377  CG1 VAL A 745     -12.366 191.809-193.431  1.00 76.48           C  
ANISOU 1377  CG1 VAL A 745     9880  10586   8595    363   -829    446       C  
ATOM   1378  CG2 VAL A 745     -14.424 190.518-194.064  1.00 82.50           C  
ANISOU 1378  CG2 VAL A 745    10599  11331   9415    126   -803   1020       C  
ATOM   1379  N   SER A 746     -11.693 189.770-190.545  1.00 88.99           N  
ANISOU 1379  N   SER A 746    11489  12761   9561    601   -986    834       N  
ATOM   1380  CA  SER A 746     -10.637 189.982-189.572  1.00 90.43           C  
ANISOU 1380  CA  SER A 746    11678  13145   9536    809  -1099    600       C  
ATOM   1381  C   SER A 746      -9.752 188.757-189.487  1.00 89.07           C  
ANISOU 1381  C   SER A 746    11595  12860   9388    803  -1260    776       C  
ATOM   1382  O   SER A 746      -8.536 188.876-189.345  1.00 88.62           O  
ANISOU 1382  O   SER A 746    11550  12755   9366    900  -1411    507       O  
ATOM   1383  CB  SER A 746     -11.210 190.288-188.194  1.00 98.21           C  
ANISOU 1383  CB  SER A 746    12598  14615  10104   1024  -1021    647       C  
ATOM   1384  OG  SER A 746     -10.162 190.424-187.247  1.00104.26           O  
ANISOU 1384  OG  SER A 746    13376  15605  10632   1254  -1184    398       O  
ATOM   1385  N   ALA A 747     -10.367 187.579-189.567  1.00 88.72           N  
ANISOU 1385  N   ALA A 747    11588  12749   9374    689  -1233   1224       N  
ATOM   1386  CA  ALA A 747      -9.628 186.325-189.454  1.00 86.19           C  
ANISOU 1386  CA  ALA A 747    11345  12287   9117    689  -1380   1441       C  
ATOM   1387  C   ALA A 747      -8.616 186.204-190.579  1.00 81.82           C  
ANISOU 1387  C   ALA A 747    10852  11335   8900    595  -1501   1182       C  
ATOM   1388  O   ALA A 747      -7.439 185.939-190.337  1.00 83.28           O  
ANISOU 1388  O   ALA A 747    11061  11481   9102    705  -1651   1045       O  
ATOM   1389  CB  ALA A 747     -10.571 185.140-189.462  1.00 85.21           C  
ANISOU 1389  CB  ALA A 747    11217  12078   9080    551  -1315   1963       C  
ATOM   1390  N   LEU A 748      -9.080 186.407-191.807  1.00 76.49           N  
ANISOU 1390  N   LEU A 748    10193  10391   8478    412  -1433   1116       N  
ATOM   1391  CA  LEU A 748      -8.219 186.338-192.977  1.00 76.50           C  
ANISOU 1391  CA  LEU A 748    10258  10049   8760    340  -1495    885       C  
ATOM   1392  C   LEU A 748      -7.106 187.368-192.889  1.00 80.05           C  
ANISOU 1392  C   LEU A 748    10659  10532   9224    464  -1510    482       C  
ATOM   1393  O   LEU A 748      -5.934 187.046-193.074  1.00 80.05           O  
ANISOU 1393  O   LEU A 748    10669  10382   9363    512  -1612    335       O  
ATOM   1394  CB  LEU A 748      -9.037 186.570-194.245  1.00 74.79           C  
ANISOU 1394  CB  LEU A 748    10068   9634   8713    173  -1408    879       C  
ATOM   1395  CG  LEU A 748      -9.705 185.337-194.834  1.00 80.15           C  
ANISOU 1395  CG  LEU A 748    10798  10099   9558     19  -1475   1150       C  
ATOM   1396  CD1 LEU A 748     -10.528 185.708-196.049  1.00 81.09           C  
ANISOU 1396  CD1 LEU A 748    10933  10087   9792   -105  -1428   1087       C  
ATOM   1397  CD2 LEU A 748      -8.639 184.339-195.217  1.00 83.21           C  
ANISOU 1397  CD2 LEU A 748    11271  10224  10122     32  -1613   1102       C  
ATOM   1398  N   THR A 749      -7.488 188.607-192.596  1.00 83.02           N  
ANISOU 1398  N   THR A 749    10954  11086   9503    515  -1410    296       N  
ATOM   1399  CA  THR A 749      -6.530 189.699-192.493  1.00 82.59           C  
ANISOU 1399  CA  THR A 749    10810  11024   9545    614  -1422   -109       C  
ATOM   1400  C   THR A 749      -5.419 189.389-191.505  1.00 84.77           C  
ANISOU 1400  C   THR A 749    11041  11440   9728    782  -1611   -245       C  
ATOM   1401  O   THR A 749      -4.242 189.585-191.798  1.00 86.18           O  
ANISOU 1401  O   THR A 749    11159  11450  10136    811  -1682   -504       O  
ATOM   1402  CB  THR A 749      -7.230 190.988-192.069  1.00 85.61           C  
ANISOU 1402  CB  THR A 749    11100  11597   9833    673  -1313   -278       C  
ATOM   1403  OG1 THR A 749      -7.958 191.509-193.187  1.00 86.79           O  
ANISOU 1403  OG1 THR A 749    11266  11551  10157    538  -1155   -230       O  
ATOM   1404  CG2 THR A 749      -6.216 192.017-191.601  1.00 87.77           C  
ANISOU 1404  CG2 THR A 749    11244  11891  10214    803  -1381   -718       C  
ATOM   1405  N   GLN A 750      -5.810 188.890-190.339  1.00 90.83           N  
ANISOU 1405  N   GLN A 750    11825  12530  10157    907  -1685    -46       N  
ATOM   1406  CA  GLN A 750      -4.865 188.561-189.286  1.00 99.67           C  
ANISOU 1406  CA  GLN A 750    12911  13856  11102   1113  -1893   -136       C  
ATOM   1407  C   GLN A 750      -3.987 187.400-189.728  1.00 97.38           C  
ANISOU 1407  C   GLN A 750    12676  13306  11016   1078  -2018      4       C  
ATOM   1408  O   GLN A 750      -2.773 187.406-189.515  1.00 95.14           O  
ANISOU 1408  O   GLN A 750    12320  12988  10839   1192  -2187   -238       O  
ATOM   1409  CB  GLN A 750      -5.620 188.198-188.011  1.00109.63           C  
ANISOU 1409  CB  GLN A 750    14204  15551  11898   1273  -1900    145       C  
ATOM   1410  CG  GLN A 750      -4.812 188.282-186.731  1.00119.38           C  
ANISOU 1410  CG  GLN A 750    15395  17144  12821   1563  -2118    -36       C  
ATOM   1411  CD  GLN A 750      -5.692 188.123-185.504  1.00130.18           C  
ANISOU 1411  CD  GLN A 750    16800  19008  13655   1755  -2059    238       C  
ATOM   1412  OE1 GLN A 750      -6.921 188.153-185.602  1.00132.08           O  
ANISOU 1412  OE1 GLN A 750    17059  19316  13809   1656  -1830    505       O  
ATOM   1413  NE2 GLN A 750      -5.070 187.950-184.342  1.00136.54           N  
ANISOU 1413  NE2 GLN A 750    17604  20185  14089   2047  -2262    183       N  
ATOM   1414  N   GLN A 751      -4.612 186.418-190.368  1.00 95.88           N  
ANISOU 1414  N   GLN A 751    12592  12915  10921    923  -1944    367       N  
ATOM   1415  CA  GLN A 751      -3.927 185.203-190.792  1.00 96.51           C  
ANISOU 1415  CA  GLN A 751    12732  12723  11213    896  -2057    519       C  
ATOM   1416  C   GLN A 751      -2.848 185.474-191.830  1.00 92.94           C  
ANISOU 1416  C   GLN A 751    12242  11959  11110    850  -2065    182       C  
ATOM   1417  O   GLN A 751      -1.766 184.894-191.770  1.00 98.93           O  
ANISOU 1417  O   GLN A 751    12971  12606  12010    942  -2209    115       O  
ATOM   1418  CB  GLN A 751      -4.920 184.168-191.327  1.00 99.23           C  
ANISOU 1418  CB  GLN A 751    13176  12877  11651    725  -1984    919       C  
ATOM   1419  CG  GLN A 751      -4.262 182.937-191.954  1.00102.84           C  
ANISOU 1419  CG  GLN A 751    13695  12976  12404    685  -2097   1015       C  
ATOM   1420  CD  GLN A 751      -3.339 182.200-190.994  1.00107.09           C  
ANISOU 1420  CD  GLN A 751    14215  13596  12877    884  -2289   1133       C  
ATOM   1421  OE1 GLN A 751      -3.644 182.054-189.810  1.00110.04           O  
ANISOU 1421  OE1 GLN A 751    14580  14283  12946   1017  -2329   1388       O  
ATOM   1422  NE2 GLN A 751      -2.200 181.738-191.503  1.00106.50           N  
ANISOU 1422  NE2 GLN A 751    14132  13262  13073    930  -2403    958       N  
ATOM   1423  N   ILE A 752      -3.136 186.357-192.780  1.00 83.52           N  
ANISOU 1423  N   ILE A 752    11037  10636  10062    726  -1894     -5       N  
ATOM   1424  CA  ILE A 752      -2.179 186.649-193.841  1.00 76.75           C  
ANISOU 1424  CA  ILE A 752    10139   9499   9523    687  -1834   -268       C  
ATOM   1425  C   ILE A 752      -0.983 187.429-193.297  1.00 83.97           C  
ANISOU 1425  C   ILE A 752    10874  10480  10550    819  -1918   -619       C  
ATOM   1426  O   ILE A 752       0.121 187.346-193.833  1.00 86.00           O  
ANISOU 1426  O   ILE A 752    11051  10533  11092    838  -1924   -798       O  
ATOM   1427  CB  ILE A 752      -2.840 187.413-195.002  1.00 64.22           C  
ANISOU 1427  CB  ILE A 752     8592   7777   8031    546  -1614   -316       C  
ATOM   1428  CG1 ILE A 752      -4.109 186.696-195.443  1.00 58.47           C  
ANISOU 1428  CG1 ILE A 752     8005   7015   7196    424  -1583    -10       C  
ATOM   1429  CG2 ILE A 752      -1.905 187.508-196.183  1.00 56.62           C  
ANISOU 1429  CG2 ILE A 752     7614   6541   7356    524  -1510   -494       C  
ATOM   1430  CD1 ILE A 752      -4.929 187.472-196.428  1.00 58.14           C  
ANISOU 1430  CD1 ILE A 752     7999   6915   7175    319  -1409    -29       C  
ATOM   1431  N   SER A 753      -1.209 188.162-192.211  1.00 90.07           N  
ANISOU 1431  N   SER A 753    11565  11546  11111    922  -1991   -736       N  
ATOM   1432  CA  SER A 753      -0.161 188.962-191.593  1.00 99.95           C  
ANISOU 1432  CA  SER A 753    12619  12876  12482   1054  -2123  -1128       C  
ATOM   1433  C   SER A 753       0.788 188.135-190.734  1.00103.82           C  
ANISOU 1433  C   SER A 753    13059  13486  12901   1235  -2401  -1137       C  
ATOM   1434  O   SER A 753       1.736 188.673-190.159  1.00106.79           O  
ANISOU 1434  O   SER A 753    13250  13942  13385   1366  -2574  -1483       O  
ATOM   1435  CB  SER A 753      -0.773 190.081-190.756  1.00107.89           C  
ANISOU 1435  CB  SER A 753    13555  14156  13281   1126  -2125  -1318       C  
ATOM   1436  OG  SER A 753      -1.495 190.980-191.580  1.00111.41           O  
ANISOU 1436  OG  SER A 753    14007  14451  13873    978  -1880  -1347       O  
ATOM   1437  N   LYS A 754       0.524 186.834-190.642  1.00103.31           N  
ANISOU 1437  N   LYS A 754    13145  13420  12689   1250  -2460   -759       N  
ATOM   1438  CA  LYS A 754       1.392 185.915-189.913  1.00104.28           C  
ANISOU 1438  CA  LYS A 754    13238  13619  12763   1435  -2720   -688       C  
ATOM   1439  C   LYS A 754       2.621 185.604-190.745  1.00104.39           C  
ANISOU 1439  C   LYS A 754    13147  13298  13219   1415  -2743   -870       C  
ATOM   1440  O   LYS A 754       3.737 185.544-190.229  1.00108.95           O  
ANISOU 1440  O   LYS A 754    13565  13921  13909   1578  -2962  -1075       O  
ATOM   1441  CB  LYS A 754       0.663 184.607-189.594  1.00104.09           C  
ANISOU 1441  CB  LYS A 754    13397  13639  12514   1447  -2745   -173       C  
ATOM   1442  CG  LYS A 754      -0.383 184.697-188.494  1.00105.01           C  
ANISOU 1442  CG  LYS A 754    13587  14159  12153   1537  -2741     80       C  
ATOM   1443  CD  LYS A 754      -1.051 183.341-188.290  1.00106.12           C  
ANISOU 1443  CD  LYS A 754    13871  14261  12188   1519  -2728    645       C  
ATOM   1444  CE  LYS A 754      -2.177 183.412-187.273  1.00107.36           C  
ANISOU 1444  CE  LYS A 754    14084  14820  11887   1596  -2647    962       C  
ATOM   1445  NZ  LYS A 754      -2.868 182.103-187.102  1.00107.47           N1+
ANISOU 1445  NZ  LYS A 754    14200  14749  11883   1551  -2596   1562       N1+
ATOM   1446  N   GLY A 755       2.407 185.404-192.040  1.00100.23           N  
ANISOU 1446  N   GLY A 755    12699  12453  12932   1235  -2519   -805       N  
ATOM   1447  CA  GLY A 755       3.490 185.073-192.947  1.00 99.13           C  
ANISOU 1447  CA  GLY A 755    12473  12006  13186   1226  -2478   -957       C  
ATOM   1448  C   GLY A 755       3.859 186.224-193.851  1.00 97.40           C  
ANISOU 1448  C   GLY A 755    12120  11632  13255   1121  -2245  -1251       C  
ATOM   1449  O   GLY A 755       3.123 187.200-193.947  1.00 97.83           O  
ANISOU 1449  O   GLY A 755    12190  11762  13220   1027  -2102  -1297       O  
ATOM   1450  N   PRO A 756       5.009 186.109-194.521  1.00 97.78           N  
ANISOU 1450  N   PRO A 756    12023  11455  13674   1147  -2188  -1428       N  
ATOM   1451  CA  PRO A 756       5.552 187.161-195.382  1.00 96.43           C  
ANISOU 1451  CA  PRO A 756    11681  11115  13844   1065  -1933  -1667       C  
ATOM   1452  C   PRO A 756       4.590 187.591-196.482  1.00 92.04           C  
ANISOU 1452  C   PRO A 756    11300  10465  13205    909  -1622  -1525       C  
ATOM   1453  O   PRO A 756       3.810 186.776-196.994  1.00 88.24           O  
ANISOU 1453  O   PRO A 756    11059   9951  12516    864  -1586  -1287       O  
ATOM   1454  CB  PRO A 756       6.781 186.495-196.006  1.00 98.61           C  
ANISOU 1454  CB  PRO A 756    11832  11172  14465   1138  -1898  -1755       C  
ATOM   1455  CG  PRO A 756       7.183 185.456-195.026  1.00 99.71           C  
ANISOU 1455  CG  PRO A 756    11965  11411  14509   1300  -2244  -1695       C  
ATOM   1456  CD  PRO A 756       5.894 184.933-194.467  1.00 99.42           C  
ANISOU 1456  CD  PRO A 756    12199  11548  14027   1275  -2351  -1386       C  
ATOM   1457  N   VAL A 757       4.647 188.881-196.815  1.00 89.89           N  
ANISOU 1457  N   VAL A 757    10889  10141  13123    837  -1422  -1676       N  
ATOM   1458  CA  VAL A 757       3.920 189.443-197.947  1.00 83.37           C  
ANISOU 1458  CA  VAL A 757    10191   9217  12268    722  -1109  -1546       C  
ATOM   1459  C   VAL A 757       4.911 190.224-198.784  1.00 80.33           C  
ANISOU 1459  C   VAL A 757     9590   8620  12314    706   -830  -1686       C  
ATOM   1460  O   VAL A 757       5.768 190.913-198.242  1.00 82.71           O  
ANISOU 1460  O   VAL A 757     9600   8871  12956    726   -880  -1926       O  
ATOM   1461  CB  VAL A 757       2.826 190.421-197.506  1.00 82.08           C  
ANISOU 1461  CB  VAL A 757    10068   9191  11929    654  -1093  -1519       C  
ATOM   1462  CG1 VAL A 757       1.863 190.671-198.656  1.00 80.54           C  
ANISOU 1462  CG1 VAL A 757    10066   8932  11604    563   -837  -1304       C  
ATOM   1463  CG2 VAL A 757       2.084 189.889-196.292  1.00 82.24           C  
ANISOU 1463  CG2 VAL A 757    10192   9472  11584    703  -1375  -1437       C  
ATOM   1464  N   ASP A 758       4.805 190.114-200.101  1.00 78.68           N  
ANISOU 1464  N   ASP A 758     9507   8292  12098    681   -537  -1537       N  
ATOM   1465  CA  ASP A 758       5.676 190.873-200.985  1.00 82.33           C  
ANISOU 1465  CA  ASP A 758     9771   8569  12943    676   -197  -1588       C  
ATOM   1466  C   ASP A 758       5.158 192.306-201.101  1.00 86.38           C  
ANISOU 1466  C   ASP A 758    10207   9033  13580    585     -7  -1553       C  
ATOM   1467  O   ASP A 758       4.033 192.525-201.544  1.00 87.13           O  
ANISOU 1467  O   ASP A 758    10528   9197  13380    545     77  -1358       O  
ATOM   1468  CB  ASP A 758       5.742 190.207-202.355  1.00 80.44           C  
ANISOU 1468  CB  ASP A 758     9715   8273  12575    731     59  -1433       C  
ATOM   1469  CG  ASP A 758       6.577 190.987-203.339  1.00 85.70           C  
ANISOU 1469  CG  ASP A 758    10193   8785  13585    748    479  -1409       C  
ATOM   1470  OD1 ASP A 758       7.434 191.778-202.898  1.00 86.49           O  
ANISOU 1470  OD1 ASP A 758     9952   8761  14151    715    536  -1556       O  
ATOM   1471  OD2 ASP A 758       6.377 190.807-204.557  1.00 90.52           O1-
ANISOU 1471  OD2 ASP A 758    10984   9404  14006    806    755  -1244       O1-
ATOM   1472  N   SER A 759       5.981 193.274-200.699  1.00 85.96           N  
ANISOU 1472  N   SER A 759     9814   8839  14008    557     44  -1752       N  
ATOM   1473  CA  SER A 759       5.562 194.676-200.616  1.00 86.99           C  
ANISOU 1473  CA  SER A 759     9822   8870  14360    474    177  -1769       C  
ATOM   1474  C   SER A 759       5.201 195.281-201.976  1.00 90.98           C  
ANISOU 1474  C   SER A 759    10428   9250  14891    444    610  -1468       C  
ATOM   1475  O   SER A 759       4.481 196.279-202.048  1.00 91.99           O  
ANISOU 1475  O   SER A 759    10564   9321  15066    392    716  -1382       O  
ATOM   1476  CB  SER A 759       6.662 195.512-199.947  1.00 88.80           C  
ANISOU 1476  CB  SER A 759     9619   8919  15204    449    122  -2090       C  
ATOM   1477  OG  SER A 759       6.216 196.816-199.616  1.00 87.86           O  
ANISOU 1477  OG  SER A 759     9367   8688  15328    378    159  -2183       O  
ATOM   1478  N   VAL A 760       5.691 194.662-203.047  1.00 92.40           N  
ANISOU 1478  N   VAL A 760    10689   9403  15017    506    856  -1308       N  
ATOM   1479  CA  VAL A 760       5.562 195.219-204.391  1.00 92.38           C  
ANISOU 1479  CA  VAL A 760    10759   9314  15027    527   1300  -1009       C  
ATOM   1480  C   VAL A 760       4.496 194.515-205.230  1.00 93.21           C  
ANISOU 1480  C   VAL A 760    11280   9621  14514    596   1315   -776       C  
ATOM   1481  O   VAL A 760       3.935 195.105-206.153  1.00 99.07           O  
ANISOU 1481  O   VAL A 760    12151  10367  15125    625   1582   -513       O  
ATOM   1482  CB  VAL A 760       6.911 195.183-205.122  1.00 94.60           C  
ANISOU 1482  CB  VAL A 760    10806   9442  15696    581   1640   -988       C  
ATOM   1483  CG1 VAL A 760       6.821 195.880-206.466  1.00 96.55           C  
ANISOU 1483  CG1 VAL A 760    11107   9620  15956    627   2145   -632       C  
ATOM   1484  CG2 VAL A 760       7.966 195.845-204.264  1.00 97.55           C  
ANISOU 1484  CG2 VAL A 760    10722   9598  16744    501   1578  -1256       C  
ATOM   1485  N   THR A 761       4.204 193.261-204.907  1.00 88.24           N  
ANISOU 1485  N   THR A 761    10849   9150  13528    630   1010   -869       N  
ATOM   1486  CA  THR A 761       3.166 192.540-205.632  1.00 86.38           C  
ANISOU 1486  CA  THR A 761    10975   9081  12766    682    960   -708       C  
ATOM   1487  C   THR A 761       1.992 192.185-204.737  1.00 80.54           C  
ANISOU 1487  C   THR A 761    10384   8476  11743    606    588   -731       C  
ATOM   1488  O   THR A 761       0.976 191.697-205.219  1.00 81.76           O  
ANISOU 1488  O   THR A 761    10795   8749  11519    619    506   -607       O  
ATOM   1489  CB  THR A 761       3.701 191.246-206.263  1.00 93.49           C  
ANISOU 1489  CB  THR A 761    12004  10020  13497    799    954   -768       C  
ATOM   1490  OG1 THR A 761       4.066 190.330-205.227  1.00 97.35           O  
ANISOU 1490  OG1 THR A 761    12428  10501  14059    779    614   -968       O  
ATOM   1491  CG2 THR A 761       4.911 191.533-207.140  1.00 98.52           C  
ANISOU 1491  CG2 THR A 761    12475  10556  14403    899   1360   -741       C  
ATOM   1492  N   GLU A 762       2.144 192.422-203.437  1.00 80.12           N  
ANISOU 1492  N   GLU A 762    10151   8416  11873    541    365   -896       N  
ATOM   1493  CA  GLU A 762       1.147 192.038-202.433  1.00 84.38           C  
ANISOU 1493  CA  GLU A 762    10798   9116  12148    492     38   -908       C  
ATOM   1494  C   GLU A 762       0.883 190.534-202.367  1.00 78.68           C  
ANISOU 1494  C   GLU A 762    10271   8478  11146    517   -196   -876       C  
ATOM   1495  O   GLU A 762      -0.013 190.091-201.643  1.00 78.72           O  
ANISOU 1495  O   GLU A 762    10374   8610  10927    474   -430   -816       O  
ATOM   1496  CB  GLU A 762      -0.166 192.804-202.609  1.00 97.63           C  
ANISOU 1496  CB  GLU A 762    12587  10869  13639    443     88   -747       C  
ATOM   1497  CG  GLU A 762      -0.279 194.047-201.746  1.00112.99           C  
ANISOU 1497  CG  GLU A 762    14327  12786  15817    402     86   -859       C  
ATOM   1498  CD  GLU A 762      -1.685 194.615-201.733  1.00125.25           C  
ANISOU 1498  CD  GLU A 762    15992  14440  17159    373     78   -714       C  
ATOM   1499  OE1 GLU A 762      -2.623 193.891-202.136  1.00128.92           O  
ANISOU 1499  OE1 GLU A 762    16675  15031  17276    366     -3   -545       O  
ATOM   1500  OE2 GLU A 762      -1.849 195.785-201.321  1.00129.33           O1-
ANISOU 1500  OE2 GLU A 762    16354  14891  17894    359    143   -789       O1-
ATOM   1501  N   LYS A 763       1.649 189.755-203.124  1.00 72.36           N  
ANISOU 1501  N   LYS A 763     9513   7593  10388    593   -116   -908       N  
ATOM   1502  CA  LYS A 763       1.602 188.307-203.000  1.00 70.34           C  
ANISOU 1502  CA  LYS A 763     9396   7345   9985    627   -350   -922       C  
ATOM   1503  C   LYS A 763       2.070 187.924-201.601  1.00 77.99           C  
ANISOU 1503  C   LYS A 763    10219   8341  11073    630   -620  -1017       C  
ATOM   1504  O   LYS A 763       3.046 188.473-201.084  1.00 82.25           O  
ANISOU 1504  O   LYS A 763    10519   8843  11889    661   -599  -1172       O  
ATOM   1505  CB  LYS A 763       2.478 187.640-204.059  1.00 68.90           C  
ANISOU 1505  CB  LYS A 763     9253   7055   9871    742   -193   -995       C  
ATOM   1506  CG  LYS A 763       1.918 187.710-205.464  1.00 73.70           C  
ANISOU 1506  CG  LYS A 763    10070   7699  10233    791     14   -902       C  
ATOM   1507  CD  LYS A 763       2.966 187.328-206.498  1.00 80.30           C  
ANISOU 1507  CD  LYS A 763    10899   8469  11142    946    255   -998       C  
ATOM   1508  CE  LYS A 763       2.485 187.610-207.921  1.00 83.63           C  
ANISOU 1508  CE  LYS A 763    11523   8990  11264   1042    503   -897       C  
ATOM   1509  NZ  LYS A 763       3.600 187.575-208.924  1.00 86.80           N1+
ANISOU 1509  NZ  LYS A 763    11874   9374  11733   1219    852   -953       N1+
ATOM   1510  N   ALA A 764       1.359 186.992-200.983  1.00 79.08           N  
ANISOU 1510  N   ALA A 764    10488   8548  11012    606   -881   -914       N  
ATOM   1511  CA  ALA A 764       1.712 186.548-199.644  1.00 83.09           C  
ANISOU 1511  CA  ALA A 764    10892   9127  11554    645  -1143   -940       C  
ATOM   1512  C   ALA A 764       1.884 185.032-199.585  1.00 83.89           C  
ANISOU 1512  C   ALA A 764    11095   9131  11647    700  -1336   -866       C  
ATOM   1513  O   ALA A 764       1.451 184.314-200.488  1.00 82.27           O  
ANISOU 1513  O   ALA A 764    11061   8814  11384    680  -1305   -807       O  
ATOM   1514  CB  ALA A 764       0.672 187.016-198.640  1.00 84.52           C  
ANISOU 1514  CB  ALA A 764    11087   9513  11513    586  -1260   -831       C  
ATOM   1515  N   LEU A 765       2.539 184.559-198.528  1.00 84.01           N  
ANISOU 1515  N   LEU A 765    10998   9182  11739    787  -1551   -886       N  
ATOM   1516  CA  LEU A 765       2.739 183.131-198.320  1.00 81.23           C  
ANISOU 1516  CA  LEU A 765    10721   8712  11431    856  -1751   -779       C  
ATOM   1517  C   LEU A 765       1.437 182.449-197.913  1.00 77.45           C  
ANISOU 1517  C   LEU A 765    10413   8280  10735    768  -1884   -489       C  
ATOM   1518  O   LEU A 765       1.062 181.445-198.504  1.00 79.84           O  
ANISOU 1518  O   LEU A 765    10850   8396  11090    737  -1929   -400       O  
ATOM   1519  CB  LEU A 765       3.808 182.895-197.257  1.00 85.50           C  
ANISOU 1519  CB  LEU A 765    11079   9303  12103   1001  -1956   -849       C  
ATOM   1520  CG  LEU A 765       4.123 181.442-196.905  1.00 88.57           C  
ANISOU 1520  CG  LEU A 765    11518   9556  12578   1106  -2180   -704       C  
ATOM   1521  CD1 LEU A 765       4.853 180.754-198.055  1.00 90.71           C  
ANISOU 1521  CD1 LEU A 765    11801   9544  13119   1163  -2080   -855       C  
ATOM   1522  CD2 LEU A 765       4.931 181.365-195.611  1.00 90.50           C  
ANISOU 1522  CD2 LEU A 765    11594   9950  12843   1268  -2427   -712       C  
ATOM   1523  N   TYR A 766       0.754 182.992-196.904  1.00 75.63           N  
ANISOU 1523  N   TYR A 766    10157   8292  10288    736  -1943   -357       N  
ATOM   1524  CA  TYR A 766      -0.575 182.507-196.523  1.00 76.00           C  
ANISOU 1524  CA  TYR A 766    10325   8409  10141    639  -2006    -53       C  
ATOM   1525  C   TYR A 766      -1.654 183.166-197.376  1.00 73.33           C  
ANISOU 1525  C   TYR A 766    10071   8087   9705    494  -1834    -52       C  
ATOM   1526  O   TYR A 766      -1.733 184.384-197.443  1.00 75.99           O  
ANISOU 1526  O   TYR A 766    10346   8557   9971    480  -1695   -182       O  
ATOM   1527  CB  TYR A 766      -0.840 182.762-195.039  1.00 81.28           C  
ANISOU 1527  CB  TYR A 766    10927   9377  10579    707  -2119    103       C  
ATOM   1528  CG  TYR A 766       0.107 182.010-194.140  1.00 94.22           C  
ANISOU 1528  CG  TYR A 766    12501  11036  12262    880  -2330    162       C  
ATOM   1529  CD1 TYR A 766      -0.073 180.656-193.881  1.00100.78           C  
ANISOU 1529  CD1 TYR A 766    13411  11724  13158    901  -2464    472       C  
ATOM   1530  CD2 TYR A 766       1.191 182.648-193.563  1.00 99.25           C  
ANISOU 1530  CD2 TYR A 766    12979  11812  12918   1028  -2413    -93       C  
ATOM   1531  CE1 TYR A 766       0.802 179.963-193.064  1.00105.24           C  
ANISOU 1531  CE1 TYR A 766    13918  12304  13766   1086  -2665    563       C  
ATOM   1532  CE2 TYR A 766       2.069 181.968-192.745  1.00103.75           C  
ANISOU 1532  CE2 TYR A 766    13479  12423  13518   1212  -2640    -45       C  
ATOM   1533  CZ  TYR A 766       1.873 180.626-192.499  1.00108.40           C  
ANISOU 1533  CZ  TYR A 766    14169  12887  14133   1251  -2761    301       C  
ATOM   1534  OH  TYR A 766       2.755 179.952-191.683  1.00114.50           O  
ANISOU 1534  OH  TYR A 766    14872  13698  14934   1462  -2996    384       O  
ATOM   1535  N   THR A 767      -2.477 182.355-198.032  1.00 70.79           N  
ANISOU 1535  N   THR A 767     9874   7610   9412    396  -1864     85       N  
ATOM   1536  CA  THR A 767      -3.504 182.861-198.942  1.00 70.47           C  
ANISOU 1536  CA  THR A 767     9911   7580   9283    280  -1747     77       C  
ATOM   1537  C   THR A 767      -4.487 181.739-199.325  1.00 72.69           C  
ANISOU 1537  C   THR A 767    10287   7695   9636    171  -1876    247       C  
ATOM   1538  O   THR A 767      -4.236 180.571-199.034  1.00 74.91           O  
ANISOU 1538  O   THR A 767    10581   7796  10086    186  -2027    348       O  
ATOM   1539  CB  THR A 767      -2.862 183.511-200.206  1.00 76.40           C  
ANISOU 1539  CB  THR A 767    10694   8255  10081    328  -1569   -188       C  
ATOM   1540  OG1 THR A 767      -3.881 184.021-201.078  1.00 77.31           O  
ANISOU 1540  OG1 THR A 767    10893   8412  10068    250  -1477   -168       O  
ATOM   1541  CG2 THR A 767      -2.004 182.510-200.958  1.00 77.00           C  
ANISOU 1541  CG2 THR A 767    10830   8095  10332    410  -1614   -330       C  
ATOM   1542  N   LEU A 768      -5.609 182.093-199.952  1.00 69.43           N  
ANISOU 1542  N   LEU A 768     9919   7324   9137     64  -1833    279       N  
ATOM   1543  CA  LEU A 768      -6.538 181.084-200.465  1.00 71.71           C  
ANISOU 1543  CA  LEU A 768    10265   7427   9554    -49  -1981    370       C  
ATOM   1544  C   LEU A 768      -6.512 181.007-201.994  1.00 81.31           C  
ANISOU 1544  C   LEU A 768    11602   8514  10777    -22  -1984    100       C  
ATOM   1545  O   LEU A 768      -7.201 180.182-202.597  1.00 82.56           O  
ANISOU 1545  O   LEU A 768    11809   8502  11059    -95  -2145     75       O  
ATOM   1546  CB  LEU A 768      -7.969 181.340-199.982  1.00 64.75           C  
ANISOU 1546  CB  LEU A 768     9310   6690   8602   -188  -1984    621       C  
ATOM   1547  CG  LEU A 768      -8.197 181.464-198.475  1.00 65.13           C  
ANISOU 1547  CG  LEU A 768     9245   6939   8563   -190  -1948    913       C  
ATOM   1548  CD1 LEU A 768      -9.668 181.603-198.163  1.00 65.30           C  
ANISOU 1548  CD1 LEU A 768     9177   7082   8551   -323  -1924   1159       C  
ATOM   1549  CD2 LEU A 768      -7.625 180.278-197.729  1.00 68.47           C  
ANISOU 1549  CD2 LEU A 768     9656   7208   9151   -152  -2073   1094       C  
ATOM   1550  N   SER A 769      -5.711 181.867-202.615  1.00 87.77           N  
ANISOU 1550  N   SER A 769    12459   9420  11469     95  -1806   -102       N  
ATOM   1551  CA  SER A 769      -5.651 181.934-204.070  1.00 96.80           C  
ANISOU 1551  CA  SER A 769    13732  10522  12527    170  -1759   -329       C  
ATOM   1552  C   SER A 769      -4.270 181.563-204.604  1.00104.43           C  
ANISOU 1552  C   SER A 769    14741  11366  13571    330  -1682   -556       C  
ATOM   1553  O   SER A 769      -3.258 182.089-204.139  1.00104.19           O  
ANISOU 1553  O   SER A 769    14620  11384  13584    401  -1532   -574       O  
ATOM   1554  CB  SER A 769      -6.035 183.335-204.549  1.00 98.12           C  
ANISOU 1554  CB  SER A 769    13907  10909  12465    190  -1560   -316       C  
ATOM   1555  OG  SER A 769      -6.003 183.408-205.962  1.00102.63           O  
ANISOU 1555  OG  SER A 769    14619  11488  12888    298  -1505   -490       O  
ATOM   1556  N   GLU A 770      -4.240 180.659-205.582  1.00110.80           N  
ANISOU 1556  N   GLU A 770    15668  12015  14417    396  -1792   -757       N  
ATOM   1557  CA  GLU A 770      -2.988 180.224-206.197  1.00114.58           C  
ANISOU 1557  CA  GLU A 770    16189  12383  14965    575  -1705   -999       C  
ATOM   1558  C   GLU A 770      -2.336 181.379-206.949  1.00110.08           C  
ANISOU 1558  C   GLU A 770    15635  12006  14186    707  -1379  -1078       C  
ATOM   1559  O   GLU A 770      -1.107 181.480-207.017  1.00109.31           O  
ANISOU 1559  O   GLU A 770    15470  11880  14184    831  -1203  -1180       O  
ATOM   1560  CB  GLU A 770      -3.227 179.034-207.137  1.00123.95           C  
ANISOU 1560  CB  GLU A 770    17509  13373  16213    639  -1906  -1246       C  
ATOM   1561  CG  GLU A 770      -1.958 178.463-207.781  1.00132.14           C  
ANISOU 1561  CG  GLU A 770    18587  14291  17331    854  -1818  -1529       C  
ATOM   1562  CD  GLU A 770      -2.186 177.130-208.494  1.00139.49           C  
ANISOU 1562  CD  GLU A 770    19628  14972  18400    920  -2074  -1813       C  
ATOM   1563  OE1 GLU A 770      -3.199 176.451-208.205  1.00141.25           O  
ANISOU 1563  OE1 GLU A 770    19847  15027  18795    761  -2359  -1748       O  
ATOM   1564  OE2 GLU A 770      -1.345 176.761-209.342  1.00142.32           O1-
ANISOU 1564  OE2 GLU A 770    20058  15292  18724   1137  -1984  -2114       O1-
ATOM   1565  N   ASP A 771      -3.172 182.251-207.507  1.00105.61           N  
ANISOU 1565  N   ASP A 771    15135  11625  13367    682  -1294  -1005       N  
ATOM   1566  CA  ASP A 771      -2.697 183.413-208.249  1.00100.80           C  
ANISOU 1566  CA  ASP A 771    14540  11188  12573    802   -963  -1000       C  
ATOM   1567  C   ASP A 771      -1.980 184.362-207.307  1.00 92.11           C  
ANISOU 1567  C   ASP A 771    13242  10113  11643    752   -772   -873       C  
ATOM   1568  O   ASP A 771      -0.985 184.982-207.665  1.00 92.48           O  
ANISOU 1568  O   ASP A 771    13217  10179  11742    857   -491   -911       O  
ATOM   1569  CB  ASP A 771      -3.867 184.137-208.913  1.00105.32           C  
ANISOU 1569  CB  ASP A 771    15214  11940  12862    786   -955   -897       C  
ATOM   1570  CG  ASP A 771      -4.687 183.227-209.808  1.00115.38           C  
ANISOU 1570  CG  ASP A 771    16661  13206  13974    833  -1212  -1064       C  
ATOM   1571  OD1 ASP A 771      -4.125 182.244-210.345  1.00120.73           O1+
ANISOU 1571  OD1 ASP A 771    17421  13770  14681    952  -1287  -1313       O1+
ATOM   1572  OD2 ASP A 771      -5.895 183.498-209.978  1.00117.26           O1-
ANISOU 1572  OD2 ASP A 771    16933  13544  14077    760  -1355   -976       O1-
ATOM   1573  N   TRP A 772      -2.498 184.454-206.089  1.00 87.16           N  
ANISOU 1573  N   TRP A 772    12512   9487  11117    600   -929   -732       N  
ATOM   1574  CA  TRP A 772      -1.984 185.377-205.090  1.00 84.81           C  
ANISOU 1574  CA  TRP A 772    12025   9239  10959    558   -815   -659       C  
ATOM   1575  C   TRP A 772      -0.845 184.785-204.270  1.00 83.20           C  
ANISOU 1575  C   TRP A 772    11690   8925  10997    598   -891   -748       C  
ATOM   1576  O   TRP A 772      -0.218 185.473-203.474  1.00 80.36           O  
ANISOU 1576  O   TRP A 772    11154   8602  10778    594   -829   -759       O  
ATOM   1577  CB  TRP A 772      -3.117 185.820-204.165  1.00 86.22           C  
ANISOU 1577  CB  TRP A 772    12160   9531  11069    420   -938   -485       C  
ATOM   1578  CG  TRP A 772      -3.855 187.002-204.688  1.00 87.18           C  
ANISOU 1578  CG  TRP A 772    12303   9775  11047    406   -776   -396       C  
ATOM   1579  CD1 TRP A 772      -5.113 187.026-205.211  1.00 88.14           C  
ANISOU 1579  CD1 TRP A 772    12532   9974  10982    363   -856   -299       C  
ATOM   1580  CD2 TRP A 772      -3.366 188.340-204.754  1.00 84.28           C  
ANISOU 1580  CD2 TRP A 772    11825   9441  10758    443   -516   -389       C  
ATOM   1581  NE1 TRP A 772      -5.439 188.304-205.593  1.00 85.51           N  
ANISOU 1581  NE1 TRP A 772    12177   9736  10575    390   -660   -214       N  
ATOM   1582  CE2 TRP A 772      -4.380 189.127-205.323  1.00 83.42           C  
ANISOU 1582  CE2 TRP A 772    11781   9427  10488    433   -440   -259       C  
ATOM   1583  CE3 TRP A 772      -2.167 188.948-204.383  1.00 84.55           C  
ANISOU 1583  CE3 TRP A 772    11685   9408  11032    482   -353   -483       C  
ATOM   1584  CZ2 TRP A 772      -4.230 190.490-205.530  1.00 85.33           C  
ANISOU 1584  CZ2 TRP A 772    11935   9676  10810    466   -189   -193       C  
ATOM   1585  CZ3 TRP A 772      -2.019 190.299-204.590  1.00 85.75           C  
ANISOU 1585  CZ3 TRP A 772    11731   9555  11296    493   -108   -441       C  
ATOM   1586  CH2 TRP A 772      -3.044 191.059-205.157  1.00 86.33           C  
ANISOU 1586  CH2 TRP A 772    11887   9701  11213    486    -19   -284       C  
ATOM   1587  N   LEU A 773      -0.584 183.502-204.475  1.00 88.57           N  
ANISOU 1587  N   LEU A 773    12446   9460  11746    649  -1048   -833       N  
ATOM   1588  CA  LEU A 773       0.405 182.779-203.685  1.00 90.79           C  
ANISOU 1588  CA  LEU A 773    12610   9621  12263    705  -1168   -888       C  
ATOM   1589  C   LEU A 773       1.822 183.280-203.964  1.00 92.35           C  
ANISOU 1589  C   LEU A 773    12655   9797  12637    831   -940  -1049       C  
ATOM   1590  O   LEU A 773       2.185 183.549-205.109  1.00 95.00           O  
ANISOU 1590  O   LEU A 773    13038  10131  12928    921   -699  -1151       O  
ATOM   1591  CB  LEU A 773       0.283 181.270-203.944  1.00 89.48           C  
ANISOU 1591  CB  LEU A 773    12561   9254  12183    738  -1386   -938       C  
ATOM   1592  CG  LEU A 773       1.048 180.273-203.065  1.00 85.93           C  
ANISOU 1592  CG  LEU A 773    12018   8643  11989    798  -1579   -925       C  
ATOM   1593  CD1 LEU A 773       1.038 180.694-201.609  1.00 82.04           C  
ANISOU 1593  CD1 LEU A 773    11386   8286  11498    743  -1676   -732       C  
ATOM   1594  CD2 LEU A 773       0.441 178.889-203.216  1.00 85.63           C  
ANISOU 1594  CD2 LEU A 773    12103   8377  12057    769  -1821   -893       C  
ATOM   1595  N   LEU A 774       2.604 183.431-202.900  1.00 91.98           N  
ANISOU 1595  N   LEU A 774    12411   9752  12787    847  -1015  -1064       N  
ATOM   1596  CA  LEU A 774       3.999 183.837-203.012  1.00 92.30           C  
ANISOU 1596  CA  LEU A 774    12240   9745  13087    952   -841  -1227       C  
ATOM   1597  C   LEU A 774       4.878 182.597-203.117  1.00 96.37           C  
ANISOU 1597  C   LEU A 774    12733  10091  13791   1090   -951  -1346       C  
ATOM   1598  O   LEU A 774       5.496 182.170-202.138  1.00100.79           O  
ANISOU 1598  O   LEU A 774    13150  10612  14533   1138  -1155  -1358       O  
ATOM   1599  CB  LEU A 774       4.405 184.683-201.800  1.00 87.86           C  
ANISOU 1599  CB  LEU A 774    11443   9274  12665    914   -914  -1239       C  
ATOM   1600  CG  LEU A 774       5.847 185.185-201.708  1.00 87.31           C  
ANISOU 1600  CG  LEU A 774    11078   9143  12953    998   -788  -1426       C  
ATOM   1601  CD1 LEU A 774       6.247 185.898-202.978  1.00 89.32           C  
ANISOU 1601  CD1 LEU A 774    11292   9343  13304   1019   -384  -1466       C  
ATOM   1602  CD2 LEU A 774       6.023 186.092-200.499  1.00 85.73           C  
ANISOU 1602  CD2 LEU A 774    10661   9050  12861    953   -919  -1487       C  
ATOM   1603  N   CYS A 775       4.935 182.014-204.311  1.00113.50           N  
ANISOU 1603  N   CYS A 775    12411  15412  15300    219  -1164  -3305       N  
ATOM   1604  CA  CYS A 775       5.668 180.767-204.508  1.00112.76           C  
ANISOU 1604  CA  CYS A 775    12285  14877  15683    353  -1025  -3583       C  
ATOM   1605  C   CYS A 775       7.169 181.000-204.553  1.00112.69           C  
ANISOU 1605  C   CYS A 775    12155  14893  15767    626   -813  -3430       C  
ATOM   1606  O   CYS A 775       7.887 180.364-205.323  1.00115.62           O  
ANISOU 1606  O   CYS A 775    12487  15153  16291    830   -593  -3803       O  
ATOM   1607  CB  CYS A 775       5.198 180.055-205.777  1.00114.31           C  
ANISOU 1607  CB  CYS A 775    12571  15096  15767    345   -985  -4270       C  
ATOM   1608  SG  CYS A 775       3.428 179.672-205.778  1.00147.28           S  
ANISOU 1608  SG  CYS A 775    16762  19253  19946    -20  -1273  -4558       S  
ATOM   1609  N   GLN A 776       7.632 181.914-203.710  1.00112.75           N  
ANISOU 1609  N   GLN A 776    12077  15052  15709    618   -868  -2917       N  
ATOM   1610  CA  GLN A 776       9.030 182.292-203.653  1.00119.39           C  
ANISOU 1610  CA  GLN A 776    12713  15980  16669    816   -702  -2753       C  
ATOM   1611  C   GLN A 776       9.680 181.661-202.436  1.00122.23           C  
ANISOU 1611  C   GLN A 776    12919  15932  17590    920   -865  -2422       C  
ATOM   1612  O   GLN A 776       9.057 181.544-201.380  1.00120.89           O  
ANISOU 1612  O   GLN A 776    12869  15565  17499    771  -1108  -2100       O  
ATOM   1613  CB  GLN A 776       9.149 183.811-203.555  1.00120.11           C  
ANISOU 1613  CB  GLN A 776    12813  16516  16307    704   -680  -2437       C  
ATOM   1614  CG  GLN A 776      10.571 184.329-203.537  1.00124.42           C  
ANISOU 1614  CG  GLN A 776    13092  17193  16988    821   -483  -2299       C  
ATOM   1615  CD  GLN A 776      11.118 184.547-204.930  1.00131.22           C  
ANISOU 1615  CD  GLN A 776    13941  18323  17592    932    -69  -2643       C  
ATOM   1616  OE1 GLN A 776      10.359 184.688-205.891  1.00131.89           O  
ANISOU 1616  OE1 GLN A 776    14304  18608  17201    901     16  -2896       O  
ATOM   1617  NE2 GLN A 776      12.442 184.575-205.050  1.00135.62           N  
ANISOU 1617  NE2 GLN A 776    14167  18916  18448   1068    191  -2661       N  
ATOM   1618  N   ALA A 777      10.933 181.254-202.587  1.00127.12           N  
ANISOU 1618  N   ALA A 777    13273  16440  18586   1199   -726  -2495       N  
ATOM   1619  CA  ALA A 777      11.705 180.760-201.462  1.00133.15           C  
ANISOU 1619  CA  ALA A 777    13850  16884  19857   1380   -943  -2145       C  
ATOM   1620  C   ALA A 777      12.100 181.933-200.574  1.00137.43           C  
ANISOU 1620  C   ALA A 777    14271  17751  20195   1249  -1138  -1693       C  
ATOM   1621  O   ALA A 777      12.716 182.888-201.044  1.00140.18           O  
ANISOU 1621  O   ALA A 777    14426  18493  20343   1209   -959  -1737       O  
ATOM   1622  CB  ALA A 777      12.936 180.030-201.955  1.00137.59           C  
ANISOU 1622  CB  ALA A 777    14084  17275  20920   1765   -742  -2400       C  
ATOM   1623  N   GLN A 778      11.740 181.866-199.294  1.00139.78           N  
ANISOU 1623  N   GLN A 778    14717  17869  20525   1158  -1476  -1273       N  
ATOM   1624  CA  GLN A 778      12.053 182.947-198.360  1.00140.61           C  
ANISOU 1624  CA  GLN A 778    14764  18261  20401   1011  -1698   -891       C  
ATOM   1625  C   GLN A 778      12.122 182.473-196.909  1.00144.58           C  
ANISOU 1625  C   GLN A 778    15379  18487  21068   1070  -2093   -449       C  
ATOM   1626  O   GLN A 778      11.145 181.950-196.370  1.00145.71           O  
ANISOU 1626  O   GLN A 778    15875  18349  21139    955  -2166   -292       O  
ATOM   1627  CB  GLN A 778      11.040 184.083-198.501  1.00134.92           C  
ANISOU 1627  CB  GLN A 778    14301  17856  19108    678  -1619   -870       C  
ATOM   1628  N   ASP A 779      13.279 182.664-196.281  1.00147.15           N  
ANISOU 1628  N   ASP A 779    15400  18912  21598   1239  -2346   -248       N  
ATOM   1629  CA  ASP A 779      13.464 182.290-194.882  1.00149.04           C  
ANISOU 1629  CA  ASP A 779    15771  18959  21899   1337  -2791    203       C  
ATOM   1630  C   ASP A 779      13.086 183.438-193.950  1.00144.25           C  
ANISOU 1630  C   ASP A 779    15380  18666  20765   1009  -2990    465       C  
ATOM   1631  O   ASP A 779      13.694 184.509-193.985  1.00146.05           O  
ANISOU 1631  O   ASP A 779    15355  19278  20860    879  -3024    398       O  
ATOM   1632  CB  ASP A 779      14.901 181.846-194.632  1.00154.54           C  
ANISOU 1632  CB  ASP A 779    16000  19623  23096   1738  -3058    270       C  
ATOM   1633  N   PHE A 780      12.076 183.210-193.117  1.00137.48           N  
ANISOU 1633  N   PHE A 780    14997  17616  19624    854  -3074    739       N  
ATOM   1634  CA  PHE A 780      11.615 184.231-192.188  1.00128.78           C  
ANISOU 1634  CA  PHE A 780    14162  16772  17995    559  -3211    954       C  
ATOM   1635  C   PHE A 780      11.548 183.704-190.759  1.00132.22           C  
ANISOU 1635  C   PHE A 780    14951  17005  18281    622  -3568   1418       C  
ATOM   1636  O   PHE A 780      11.568 182.496-190.524  1.00135.77           O  
ANISOU 1636  O   PHE A 780    15533  17035  19017    857  -3646   1617       O  
ATOM   1637  CB  PHE A 780      10.248 184.764-192.617  1.00118.79           C  
ANISOU 1637  CB  PHE A 780    13165  15581  16389    250  -2857    798       C  
ATOM   1638  CG  PHE A 780       9.131 183.770-192.464  1.00116.33           C  
ANISOU 1638  CG  PHE A 780    13175  14892  16134    197  -2710    881       C  
ATOM   1639  CD1 PHE A 780       8.896 182.817-193.440  1.00117.14           C  
ANISOU 1639  CD1 PHE A 780    13181  14717  16609    304  -2501    613       C  
ATOM   1640  CD2 PHE A 780       8.308 183.796-191.348  1.00115.23           C  
ANISOU 1640  CD2 PHE A 780    13437  14669  15676      5  -2742   1192       C  
ATOM   1641  CE1 PHE A 780       7.863 181.903-193.304  1.00118.18           C  
ANISOU 1641  CE1 PHE A 780    13578  14467  16856    186  -2351    647       C  
ATOM   1642  CE2 PHE A 780       7.276 182.886-191.205  1.00115.90           C  
ANISOU 1642  CE2 PHE A 780    13782  14390  15865   -106  -2540   1265       C  
ATOM   1643  CZ  PHE A 780       7.053 181.939-192.185  1.00117.49           C  
ANISOU 1643  CZ  PHE A 780    13849  14291  16499    -34  -2356    988       C  
ATOM   1644  N   GLU A 781      11.469 184.623-189.805  1.00130.06           N  
ANISOU 1644  N   GLU A 781    14881  17006  17531    415  -3766   1591       N  
ATOM   1645  CA  GLU A 781      11.358 184.255-188.403  1.00130.36           C  
ANISOU 1645  CA  GLU A 781    15346  16923  17263    447  -4091   2039       C  
ATOM   1646  C   GLU A 781      10.677 185.371-187.625  1.00126.80           C  
ANISOU 1646  C   GLU A 781    15247  16754  16176     95  -4049   2082       C  
ATOM   1647  O   GLU A 781      11.088 186.528-187.706  1.00125.28           O  
ANISOU 1647  O   GLU A 781    14862  16918  15821    -60  -4116   1866       O  
ATOM   1648  CB  GLU A 781      12.727 183.961-187.825  1.00135.78           C  
ANISOU 1648  CB  GLU A 781    15783  17675  18133    777  -4656   2233       C  
ATOM   1649  N   PRO A 782       9.619 185.025-186.878  1.00126.26           N  
ANISOU 1649  N   PRO A 782    15704  16495  15774    -47  -3882   2342       N  
ATOM   1650  CA  PRO A 782       8.844 185.965-186.059  1.00124.36           C  
ANISOU 1650  CA  PRO A 782    15853  16476  14920   -354  -3759   2381       C  
ATOM   1651  C   PRO A 782       9.701 186.713-185.039  1.00126.87           C  
ANISOU 1651  C   PRO A 782    16274  17112  14818   -365  -4240   2479       C  
ATOM   1652  O   PRO A 782      10.250 186.100-184.123  1.00132.63           O  
ANISOU 1652  O   PRO A 782    17224  17776  15391   -177  -4659   2836       O  
ATOM   1653  CB  PRO A 782       7.852 185.053-185.333  1.00128.50           C  
ANISOU 1653  CB  PRO A 782    16891  16664  15270   -419  -3535   2736       C  
ATOM   1654  CG  PRO A 782       7.698 183.876-186.235  1.00129.02           C  
ANISOU 1654  CG  PRO A 782    16760  16321  15942   -272  -3347   2698       C  
ATOM   1655  CD  PRO A 782       9.043 183.669-186.862  1.00129.05           C  
ANISOU 1655  CD  PRO A 782    16297  16358  16378     57  -3705   2577       C  
ATOM   1656  N   LEU A 783       9.801 188.030-185.205  1.00122.84           N  
ANISOU 1656  N   LEU A 783    15628  16924  14121   -581  -4196   2160       N  
ATOM   1657  CA  LEU A 783      10.576 188.883-184.310  1.00124.41           C  
ANISOU 1657  CA  LEU A 783    15897  17435  13937   -675  -4636   2132       C  
ATOM   1658  C   LEU A 783       9.675 189.637-183.338  1.00123.93           C  
ANISOU 1658  C   LEU A 783    16412  17482  13193   -945  -4458   2146       C  
ATOM   1659  O   LEU A 783       8.751 190.347-183.754  1.00121.70           O  
ANISOU 1659  O   LEU A 783    16197  17201  12844  -1139  -3976   1919       O  
ATOM   1660  CB  LEU A 783      11.389 189.894-185.119  1.00123.12           C  
ANISOU 1660  CB  LEU A 783    15207  17504  14071   -781  -4677   1732       C  
ATOM   1661  CG  LEU A 783      12.342 189.338-186.176  1.00125.07           C  
ANISOU 1661  CG  LEU A 783    14821  17704  14994   -543  -4753   1630       C  
ATOM   1662  CD1 LEU A 783      12.980 190.466-186.979  1.00123.74           C  
ANISOU 1662  CD1 LEU A 783    14209  17754  15054   -738  -4634   1246       C  
ATOM   1663  CD2 LEU A 783      13.406 188.473-185.522  1.00132.70           C  
ANISOU 1663  CD2 LEU A 783    15621  18682  16119   -234  -5358   1884       C  
ATOM   1664  N   LYS A 784       9.945 189.477-182.045  1.00126.13           N  
ANISOU 1664  N   LYS A 784    17116  17860  12950   -923  -4849   2409       N  
ATOM   1665  CA  LYS A 784       9.269 190.260-181.018  1.00125.46           C  
ANISOU 1665  CA  LYS A 784    17602  17926  12139  -1174  -4714   2371       C  
ATOM   1666  C   LYS A 784      10.009 191.582-180.833  1.00124.66           C  
ANISOU 1666  C   LYS A 784    17357  18139  11869  -1374  -5012   1976       C  
ATOM   1667  O   LYS A 784      11.197 191.598-180.505  1.00130.34           O  
ANISOU 1667  O   LYS A 784    17854  19056  12615  -1301  -5638   1963       O  
ATOM   1668  CB  LYS A 784       9.206 189.500-179.687  1.00132.44           C  
ANISOU 1668  CB  LYS A 784    19106  18789  12424  -1074  -4978   2836       C  
ATOM   1669  CG  LYS A 784       8.204 188.347-179.641  1.00134.61           C  
ANISOU 1669  CG  LYS A 784    19705  18695  12745  -1004  -4522   3233       C  
ATOM   1670  CD  LYS A 784       8.769 187.065-180.248  1.00137.51           C  
ANISOU 1670  CD  LYS A 784    19754  18753  13740   -677  -4736   3508       C  
ATOM   1671  CE  LYS A 784       7.883 185.858-179.949  1.00140.65           C  
ANISOU 1671  CE  LYS A 784    20595  18725  14122   -643  -4352   3958       C  
ATOM   1672  NZ  LYS A 784       8.465 184.595-180.486  1.00142.06           N1+
ANISOU 1672  NZ  LYS A 784    20528  18522  14926   -302  -4566   4212       N1+
ATOM   1673  N   LEU A 785       9.306 192.688-181.050  1.00117.29           N  
ANISOU 1673  N   LEU A 785    16526  17230  10808  -1624  -4568   1640       N  
ATOM   1674  CA  LEU A 785       9.930 194.005-181.008  1.00114.01           C  
ANISOU 1674  CA  LEU A 785    15986  17006  10327  -1862  -4745   1223       C  
ATOM   1675  C   LEU A 785       9.310 194.892-179.937  1.00118.72           C  
ANISOU 1675  C   LEU A 785    17205  17696  10205  -2093  -4606   1050       C  
ATOM   1676  O   LEU A 785       8.094 195.111-179.923  1.00115.56           O  
ANISOU 1676  O   LEU A 785    17115  17167   9625  -2135  -4021   1029       O  
ATOM   1677  CB  LEU A 785       9.832 194.687-182.375  1.00102.92           C  
ANISOU 1677  CB  LEU A 785    14129  15486   9490  -1931  -4342    932       C  
ATOM   1678  CG  LEU A 785      10.346 193.838-183.539  1.00 97.63           C  
ANISOU 1678  CG  LEU A 785    12879  14724   9491  -1706  -4363   1043       C  
ATOM   1679  CD1 LEU A 785      10.099 194.524-184.871  1.00 96.15           C  
ANISOU 1679  CD1 LEU A 785    12380  14439   9712  -1769  -3908    792       C  
ATOM   1680  CD2 LEU A 785      11.820 193.521-183.361  1.00 97.84           C  
ANISOU 1680  CD2 LEU A 785    12495  14924   9756  -1627  -4993   1060       C  
ATOM   1681  N   LYS A 786      10.157 195.386-179.038  1.00126.94           N  
ANISOU 1681  N   LYS A 786    18401  18980  10850  -2234  -5155    892       N  
ATOM   1682  CA  LYS A 786       9.734 196.329-178.012  1.00133.27           C  
ANISOU 1682  CA  LYS A 786    19806  19888  10944  -2478  -5071    622       C  
ATOM   1683  C   LYS A 786       9.661 197.726-178.614  1.00132.86           C  
ANISOU 1683  C   LYS A 786    19594  19721  11165  -2735  -4746    116       C  
ATOM   1684  O   LYS A 786      10.671 198.280-179.053  1.00135.15           O  
ANISOU 1684  O   LYS A 786    19445  20060  11845  -2889  -5063   -146       O  
ATOM   1685  CB  LYS A 786      10.696 196.303-176.838  1.00141.49           C  
ANISOU 1685  CB  LYS A 786    21004  21195  11560  -2453  -5722    578       C  
ATOM   1686  N   VAL A 787       8.461 198.294-178.638  1.00129.40           N  
ANISOU 1686  N   VAL A 787    19501  19107  10558  -2774  -4090    -12       N  
ATOM   1687  CA  VAL A 787       8.247 199.565-179.312  1.00125.08           C  
ANISOU 1687  CA  VAL A 787    18847  18357  10322  -2934  -3708   -416       C  
ATOM   1688  C   VAL A 787       8.143 200.727-178.335  1.00129.50           C  
ANISOU 1688  C   VAL A 787    19946  18924  10333  -3198  -3677   -854       C  
ATOM   1689  O   VAL A 787       7.353 200.700-177.396  1.00132.64           O  
ANISOU 1689  O   VAL A 787    20910  19376  10109  -3177  -3446   -855       O  
ATOM   1690  CB  VAL A 787       6.997 199.519-180.200  1.00120.74           C  
ANISOU 1690  CB  VAL A 787    18215  17573  10087  -2737  -3011   -309       C  
ATOM   1691  CG1 VAL A 787       6.815 200.836-180.920  1.00120.26           C  
ANISOU 1691  CG1 VAL A 787    18085  17269  10338  -2834  -2660   -659       C  
ATOM   1692  CG2 VAL A 787       7.108 198.380-181.197  1.00116.54           C  
ANISOU 1692  CG2 VAL A 787    17176  17024  10080  -2507  -3050     46       C  
ATOM   1693  N   VAL A 788       8.956 201.746-178.578  1.00131.77           N  
ANISOU 1693  N   VAL A 788    20058  19134  10873  -3468  -3869  -1249       N  
ATOM   1694  CA  VAL A 788       9.029 202.928-177.740  1.00137.54           C  
ANISOU 1694  CA  VAL A 788    21263  19815  11182  -3774  -3888  -1761       C  
ATOM   1695  C   VAL A 788       8.479 204.131-178.505  1.00134.22           C  
ANISOU 1695  C   VAL A 788    20869  18965  11165  -3839  -3276  -2055       C  
ATOM   1696  O   VAL A 788       8.727 204.275-179.702  1.00128.23           O  
ANISOU 1696  O   VAL A 788    19635  18016  11069  -3802  -3128  -1960       O  
ATOM   1697  CB  VAL A 788      10.490 203.173-177.305  1.00145.30           C  
ANISOU 1697  CB  VAL A 788    22030  21025  12155  -4096  -4663  -2033       C  
ATOM   1698  CG1 VAL A 788      10.801 204.656-177.223  1.00152.39           C  
ANISOU 1698  CG1 VAL A 788    23083  21673  13144  -4505  -4572  -2649       C  
ATOM   1699  CG2 VAL A 788      10.780 202.466-175.985  1.00150.34           C  
ANISOU 1699  CG2 VAL A 788    22892  22000  12230  -3894  -5100  -1891       C  
ATOM   1700  N   PHE A 789       7.715 204.979-177.819  1.00137.41           N  
ANISOU 1700  N   PHE A 789    21860  19203  11147  -3899  -2897  -2394       N  
ATOM   1701  CA  PHE A 789       7.141 206.170-178.443  1.00137.65           C  
ANISOU 1701  CA  PHE A 789    21995  18767  11537  -3899  -2317  -2668       C  
ATOM   1702  C   PHE A 789       7.725 207.464-177.886  1.00146.38           C  
ANISOU 1702  C   PHE A 789    23445  19648  12526  -4309  -2430  -3277       C  
ATOM   1703  O   PHE A 789       7.773 207.666-176.670  1.00154.56           O  
ANISOU 1703  O   PHE A 789    24979  20845  12901  -4487  -2626  -3608       O  
ATOM   1704  CB  PHE A 789       5.620 206.174-178.297  1.00134.99           C  
ANISOU 1704  CB  PHE A 789    21988  18315  10986  -3559  -1649  -2591       C  
ATOM   1705  CG  PHE A 789       4.927 205.224-179.222  1.00127.97           C  
ANISOU 1705  CG  PHE A 789    20672  17487  10464  -3192  -1406  -2090       C  
ATOM   1706  CD1 PHE A 789       4.926 203.863-178.962  1.00124.93           C  
ANISOU 1706  CD1 PHE A 789    20141  17446   9879  -3084  -1644  -1689       C  
ATOM   1707  CD2 PHE A 789       4.279 205.689-180.354  1.00124.14           C  
ANISOU 1707  CD2 PHE A 789    19955  16697  10516  -2951   -963  -2024       C  
ATOM   1708  CE1 PHE A 789       4.292 202.984-179.810  1.00118.06           C  
ANISOU 1708  CE1 PHE A 789    18883  16599   9373  -2796  -1424  -1294       C  
ATOM   1709  CE2 PHE A 789       3.641 204.813-181.207  1.00118.12           C  
ANISOU 1709  CE2 PHE A 789    18792  16027  10063  -2636   -798  -1625       C  
ATOM   1710  CZ  PHE A 789       3.649 203.458-180.935  1.00115.48           C  
ANISOU 1710  CZ  PHE A 789    18295  16021   9561  -2586  -1019  -1291       C  
ATOM   1711  N   ALA A 790       8.158 208.343-178.784  1.00144.80           N  
ANISOU 1711  N   ALA A 790    23014  19053  12948  -4477  -2282  -3433       N  
ATOM   1712  CA  ALA A 790       8.807 209.587-178.383  1.00149.68           C  
ANISOU 1712  CA  ALA A 790    23902  19371  13600  -4939  -2373  -4027       C  
ATOM   1713  C   ALA A 790       7.814 210.727-178.174  1.00149.32           C  
ANISOU 1713  C   ALA A 790    24463  18812  13461  -4848  -1727  -4380       C  
ATOM   1714  O   ALA A 790       6.718 210.726-178.741  1.00145.12           O  
ANISOU 1714  O   ALA A 790    23972  18076  13091  -4409  -1167  -4117       O  
ATOM   1715  CB  ALA A 790       9.869 209.980-179.401  1.00148.84           C  
ANISOU 1715  CB  ALA A 790    23263  19053  14237  -5238  -2503  -4023       C  
ATOM   1716  N   VAL A 791       8.216 211.698-177.357  1.00153.25           N  
ANISOU 1716  N   VAL A 791    25406  19102  13722  -5255  -1833  -5009       N  
ATOM   1717  CA  VAL A 791       7.396 212.866-177.055  1.00154.03           C  
ANISOU 1717  CA  VAL A 791    26130  18650  13745  -5198  -1237  -5448       C  
ATOM   1718  C   VAL A 791       8.258 214.001-176.503  1.00161.15           C  
ANISOU 1718  C   VAL A 791    27328  19221  14682  -5778  -1447  -6149       C  
ATOM   1719  O   VAL A 791       8.638 214.920-177.230  1.00160.99           O  
ANISOU 1719  O   VAL A 791    27265  18618  15287  -6030  -1233  -6312       O  
ATOM   1720  CB  VAL A 791       6.296 212.505-176.062  1.00153.81           C  
ANISOU 1720  CB  VAL A 791    26594  18873  12973  -4870   -963  -5507       C  
ATOM   1721  N   GLY A 794      11.602 217.534-177.809  1.00193.35           N  
ANISOU 1721  N   GLY A 794    30843  21600  21022  -7519  -1562  -7251       N  
ATOM   1722  CA  GLY A 794      12.580 216.893-176.950  1.00196.26           C  
ANISOU 1722  CA  GLY A 794    30745  22705  21122  -7707  -2384  -7394       C  
ATOM   1723  C   GLY A 794      13.345 215.795-177.663  1.00189.52           C  
ANISOU 1723  C   GLY A 794    29110  22372  20526  -7760  -2803  -6920       C  
ATOM   1724  O   GLY A 794      13.313 215.698-178.890  1.00184.24           O  
ANISOU 1724  O   GLY A 794    28219  21444  20341  -7795  -2449  -6554       O  
ATOM   1725  N   GLU A 795      14.033 214.961-176.888  1.00188.99           N  
ANISOU 1725  N   GLU A 795    28641  23028  20138  -7723  -3551  -6921       N  
ATOM   1726  CA  GLU A 795      14.849 213.892-177.450  1.00181.80           C  
ANISOU 1726  CA  GLU A 795    26934  22634  19509  -7712  -4005  -6505       C  
ATOM   1727  C   GLU A 795      14.481 212.521-176.890  1.00176.72           C  
ANISOU 1727  C   GLU A 795    26256  22685  18204  -7216  -4407  -6103       C  
ATOM   1728  O   GLU A 795      14.106 211.618-177.639  1.00169.11           O  
ANISOU 1728  O   GLU A 795    25089  21893  17273  -6948  -4285  -5568       O  
ATOM   1729  CB  GLU A 795      16.327 214.181-177.223  1.00187.89           C  
ANISOU 1729  CB  GLU A 795    27063  23552  20776  -8139  -4577  -6853       C  
ATOM   1730  N   GLU A 796      14.583 212.369-175.574  1.00182.35           N  
ANISOU 1730  N   GLU A 796    27197  23772  18314  -7091  -4869  -6355       N  
ATOM   1731  CA  GLU A 796      14.407 211.062-174.945  1.00180.83           C  
ANISOU 1731  CA  GLU A 796    26966  24223  17519  -6637  -5288  -5952       C  
ATOM   1732  C   GLU A 796      13.097 210.906-174.172  1.00179.29           C  
ANISOU 1732  C   GLU A 796    27552  24059  16509  -6275  -4916  -5873       C  
ATOM   1733  O   GLU A 796      13.002 211.290-173.006  1.00187.62           O  
ANISOU 1733  O   GLU A 796    29046  25222  17019  -6268  -5056  -6256       O  
ATOM   1734  CB  GLU A 796      15.594 210.751-174.043  1.00190.19           C  
ANISOU 1734  CB  GLU A 796    27752  25915  18598  -6685  -6151  -6188       C  
ATOM   1735  N   ILE A 797      12.092 210.340-174.835  1.00169.60           N  
ANISOU 1735  N   ILE A 797    26472  22750  15219  -5979  -4427  -5396       N  
ATOM   1736  CA  ILE A 797      10.837 209.961-174.187  1.00167.70           C  
ANISOU 1736  CA  ILE A 797    26836  22605  14278  -5594  -4042  -5222       C  
ATOM   1737  C   ILE A 797      10.445 208.560-174.662  1.00162.04           C  
ANISOU 1737  C   ILE A 797    25869  22211  13488  -5230  -4064  -4523       C  
ATOM   1738  O   ILE A 797      10.422 208.288-175.863  1.00154.02           O  
ANISOU 1738  O   ILE A 797    24486  21053  12980  -5234  -3911  -4232       O  
ATOM   1739  CB  ILE A 797       9.698 210.956-174.501  1.00163.37           C  
ANISOU 1739  CB  ILE A 797    26835  21467  13770  -5578  -3211  -5474       C  
ATOM   1740  CG1 ILE A 797      10.037 212.358-173.981  1.00170.86           C  
ANISOU 1740  CG1 ILE A 797    28087  22018  14812  -5913  -3147  -6174       C  
ATOM   1741  CG2 ILE A 797       8.385 210.476-173.898  1.00160.70           C  
ANISOU 1741  CG2 ILE A 797    26993  21270  12794  -5156  -2755  -5272       C  
ATOM   1742  CD1 ILE A 797      10.042 212.476-172.467  1.00179.67           C  
ANISOU 1742  CD1 ILE A 797    29611  23443  15211  -5860  -3401  -6528       C  
ATOM   1743  N   SER A 798      10.143 207.669-173.721  1.00165.12           N  
ANISOU 1743  N   SER A 798    26478  23013  13247  -4923  -4240  -4256       N  
ATOM   1744  CA  SER A 798       9.922 206.267-174.057  1.00158.47           C  
ANISOU 1744  CA  SER A 798    25384  22457  12371  -4595  -4335  -3590       C  
ATOM   1745  C   SER A 798       8.787 205.607-173.279  1.00160.07           C  
ANISOU 1745  C   SER A 798    26109  22813  11899  -4264  -3960  -3301       C  
ATOM   1746  O   SER A 798       8.658 205.783-172.070  1.00168.14           O  
ANISOU 1746  O   SER A 798    27581  24002  12303  -4227  -4001  -3505       O  
ATOM   1747  CB  SER A 798      11.211 205.472-173.840  1.00161.54           C  
ANISOU 1747  CB  SER A 798    25241  23251  12887  -4555  -5150  -3400       C  
ATOM   1748  OG  SER A 798      11.631 205.545-172.489  1.00172.41           O  
ANISOU 1748  OG  SER A 798    26898  24934  13676  -4532  -5572  -3643       O  
ATOM   1749  N   GLU A 799       7.972 204.838-173.986  1.00155.36           N  
ANISOU 1749  N   GLU A 799    25431  22168  11431  -4043  -3577  -2837       N  
ATOM   1750  CA  GLU A 799       6.973 203.991-173.351  1.00159.49           C  
ANISOU 1750  CA  GLU A 799    26320  22849  11428  -3755  -3224  -2470       C  
ATOM   1751  C   GLU A 799       6.874 202.694-174.145  1.00154.47           C  
ANISOU 1751  C   GLU A 799    25293  22304  11095  -3555  -3293  -1847       C  
ATOM   1752  O   GLU A 799       6.744 202.722-175.368  1.00148.88           O  
ANISOU 1752  O   GLU A 799    24226  21416  10924  -3584  -3139  -1769       O  
ATOM   1753  CB  GLU A 799       5.618 204.692-173.295  1.00161.99           C  
ANISOU 1753  CB  GLU A 799    27078  22900  11571  -3703  -2374  -2712       C  
ATOM   1754  CG  GLU A 799       4.660 204.090-172.280  1.00168.06           C  
ANISOU 1754  CG  GLU A 799    28293  23853  11710  -3489  -1960  -2495       C  
ATOM   1755  CD  GLU A 799       3.225 204.514-172.508  1.00167.54           C  
ANISOU 1755  CD  GLU A 799    28444  23548  11666  -3363  -1050  -2624       C  
ATOM   1756  OE1 GLU A 799       2.770 204.463-173.673  1.00161.78           O  
ANISOU 1756  OE1 GLU A 799    27405  22629  11436  -3300   -765  -2505       O  
ATOM   1757  OE2 GLU A 799       2.555 204.898-171.524  1.00171.20           O1-
ANISOU 1757  OE2 GLU A 799    29361  24035  11652  -3303   -617  -2859       O1-
ATOM   1758  N   SER A 800       6.934 201.564-173.447  1.00156.53           N  
ANISOU 1758  N   SER A 800    25655  22824  10996  -3349  -3519  -1411       N  
ATOM   1759  CA  SER A 800       7.076 200.261-174.098  1.00151.86           C  
ANISOU 1759  CA  SER A 800    24686  22290  10724  -3159  -3710   -831       C  
ATOM   1760  C   SER A 800       5.797 199.701-174.715  1.00146.20           C  
ANISOU 1760  C   SER A 800    24024  21420  10105  -3051  -3045   -518       C  
ATOM   1761  O   SER A 800       4.692 199.964-174.242  1.00148.46           O  
ANISOU 1761  O   SER A 800    24730  21647  10031  -3037  -2411   -609       O  
ATOM   1762  CB  SER A 800       7.658 199.236-173.124  1.00159.19           C  
ANISOU 1762  CB  SER A 800    25739  23488  11258  -2957  -4204   -459       C  
ATOM   1763  OG  SER A 800       7.721 197.955-173.728  1.00156.30           O  
ANISOU 1763  OG  SER A 800    25071  23094  11221  -2752  -4329    102       O  
ATOM   1764  N   LEU A 801       5.975 198.914-175.773  1.00139.64           N  
ANISOU 1764  N   LEU A 801    22644  20511   9901  -2915  -3144   -176       N  
ATOM   1765  CA  LEU A 801       4.874 198.247-176.459  1.00132.61           C  
ANISOU 1765  CA  LEU A 801    21543  19441   9402  -2718  -2534    120       C  
ATOM   1766  C   LEU A 801       5.394 197.013-177.188  1.00132.21           C  
ANISOU 1766  C   LEU A 801    21005  19366   9862  -2542  -2864    561       C  
ATOM   1767  O   LEU A 801       6.480 197.036-177.766  1.00130.66           O  
ANISOU 1767  O   LEU A 801    20370  19201  10072  -2537  -3367    515       O  
ATOM   1768  CB  LEU A 801       4.212 199.188-177.464  1.00123.31           C  
ANISOU 1768  CB  LEU A 801    20050  18024   8778  -2687  -2014   -199       C  
ATOM   1769  CG  LEU A 801       2.911 198.666-178.078  1.00116.95           C  
ANISOU 1769  CG  LEU A 801    19034  17086   8318  -2497  -1377      0       C  
ATOM   1770  CD1 LEU A 801       1.728 199.035-177.199  1.00119.58           C  
ANISOU 1770  CD1 LEU A 801    19846  17429   8158  -2517   -752   -145       C  
ATOM   1771  CD2 LEU A 801       2.714 199.175-179.498  1.00110.92           C  
ANISOU 1771  CD2 LEU A 801    17723  16129   8291  -2371  -1196   -140       C  
ATOM   1772  N   GLU A 802       4.614 195.937-177.162  1.00134.30           N  
ANISOU 1772  N   GLU A 802    21337  19551  10140  -2412  -2538    960       N  
ATOM   1773  CA  GLU A 802       5.015 194.691-177.805  1.00132.33           C  
ANISOU 1773  CA  GLU A 802    20697  19205  10376  -2235  -2790   1363       C  
ATOM   1774  C   GLU A 802       4.398 194.571-179.188  1.00125.46           C  
ANISOU 1774  C   GLU A 802    19265  18134  10272  -2140  -2382   1300       C  
ATOM   1775  O   GLU A 802       3.174 194.587-179.329  1.00126.14           O  
ANISOU 1775  O   GLU A 802    19389  18125  10412  -2149  -1777   1269       O  
ATOM   1776  CB  GLU A 802       4.622 193.499-176.948  1.00136.74           C  
ANISOU 1776  CB  GLU A 802    21707  19732  10515  -2176  -2715   1861       C  
ATOM   1777  N   VAL A 803       5.245 194.457-180.208  1.00119.71           N  
ANISOU 1777  N   VAL A 803    17997  17367  10120  -2046  -2713   1260       N  
ATOM   1778  CA  VAL A 803       4.761 194.289-181.576  1.00110.85           C  
ANISOU 1778  CA  VAL A 803    16374  16090   9653  -1938  -2398   1199       C  
ATOM   1779  C   VAL A 803       5.525 193.191-182.302  1.00110.15           C  
ANISOU 1779  C   VAL A 803    15878  15920  10054  -1772  -2726   1423       C  
ATOM   1780  O   VAL A 803       6.752 193.168-182.291  1.00112.91           O  
ANISOU 1780  O   VAL A 803    16048  16361  10493  -1734  -3233   1428       O  
ATOM   1781  CB  VAL A 803       4.862 195.593-182.387  1.00107.75           C  
ANISOU 1781  CB  VAL A 803    15738  15697   9505  -1987  -2281    808       C  
ATOM   1782  CG1 VAL A 803       4.647 195.316-183.863  1.00102.97           C  
ANISOU 1782  CG1 VAL A 803    14626  14984   9514  -1837  -2108    790       C  
ATOM   1783  CG2 VAL A 803       3.852 196.608-181.887  1.00109.66           C  
ANISOU 1783  CG2 VAL A 803    16331  15926   9409  -2071  -1826    569       C  
ATOM   1784  N   ILE A 804       4.791 192.284-182.937  1.00106.83           N  
ANISOU 1784  N   ILE A 804    15282  15325   9984  -1675  -2427   1567       N  
ATOM   1785  CA  ILE A 804       5.408 191.170-183.642  1.00105.62           C  
ANISOU 1785  CA  ILE A 804    14784  15031  10314  -1500  -2665   1740       C  
ATOM   1786  C   ILE A 804       5.515 191.426-185.146  1.00102.11           C  
ANISOU 1786  C   ILE A 804    13815  14570  10411  -1420  -2555   1472       C  
ATOM   1787  O   ILE A 804       4.521 191.737-185.809  1.00100.46           O  
ANISOU 1787  O   ILE A 804    13506  14338  10328  -1444  -2158   1302       O  
ATOM   1788  CB  ILE A 804       4.646 189.850-183.393  1.00103.19           C  
ANISOU 1788  CB  ILE A 804    14653  14477  10079  -1468  -2435   2062       C  
ATOM   1789  CG1 ILE A 804       4.667 189.486-181.908  1.00106.13           C  
ANISOU 1789  CG1 ILE A 804    15619  14848   9857  -1521  -2553   2418       C  
ATOM   1790  CG2 ILE A 804       5.240 188.718-184.224  1.00102.74           C  
ANISOU 1790  CG2 ILE A 804    14245  14202  10588  -1269  -2634   2174       C  
ATOM   1791  CD1 ILE A 804       3.455 189.971-181.137  1.00107.28           C  
ANISOU 1791  CD1 ILE A 804    16175  15055   9531  -1731  -2035   2386       C  
ATOM   1792  N   ALA A 805       6.729 191.292-185.676  1.00100.82           N  
ANISOU 1792  N   ALA A 805    13314  14443  10553  -1309  -2909   1436       N  
ATOM   1793  CA  ALA A 805       6.953 191.444-187.112  1.00 96.50           C  
ANISOU 1793  CA  ALA A 805    12314  13889  10464  -1226  -2784   1209       C  
ATOM   1794  C   ALA A 805       7.749 190.273-187.676  1.00 94.46           C  
ANISOU 1794  C   ALA A 805    11732  13508  10652  -1013  -2994   1307       C  
ATOM   1795  O   ALA A 805       7.937 189.266-187.003  1.00 97.68           O  
ANISOU 1795  O   ALA A 805    12280  13771  11063   -906  -3203   1583       O  
ATOM   1796  CB  ALA A 805       7.665 192.755-187.401  1.00 98.51           C  
ANISOU 1796  CB  ALA A 805    12429  14310  10689  -1339  -2852    965       C  
ATOM   1797  N   LEU A 806       8.215 190.412-188.913  1.00 88.29           N  
ANISOU 1797  N   LEU A 806    10550  12761  10233   -933  -2910   1089       N  
ATOM   1798  CA  LEU A 806       9.008 189.372-189.557  1.00 87.67           C  
ANISOU 1798  CA  LEU A 806    10130  12567  10613   -706  -3043   1102       C  
ATOM   1799  C   LEU A 806      10.363 189.924-189.976  1.00 96.28           C  
ANISOU 1799  C   LEU A 806    10815  13841  11925   -680  -3224    949       C  
ATOM   1800  O   LEU A 806      10.537 191.135-190.111  1.00 96.46           O  
ANISOU 1800  O   LEU A 806    10812  14039  11801   -873  -3141    788       O  
ATOM   1801  CB  LEU A 806       8.280 188.832-190.783  1.00 77.85           C  
ANISOU 1801  CB  LEU A 806     8757  11195   9625   -627  -2699    927       C  
ATOM   1802  CG  LEU A 806       6.838 188.409-190.522  1.00 72.75           C  
ANISOU 1802  CG  LEU A 806     8401  10401   8839   -721  -2462    994       C  
ATOM   1803  CD1 LEU A 806       6.189 187.895-191.791  1.00 70.15           C  
ANISOU 1803  CD1 LEU A 806     7885   9992   8778   -662  -2208    746       C  
ATOM   1804  CD2 LEU A 806       6.801 187.355-189.438  1.00 76.83           C  
ANISOU 1804  CD2 LEU A 806     9177  10668   9348   -688  -2621   1328       C  
ATOM   1805  N   THR A 807      11.319 189.027-190.188  1.00103.66           N  
ANISOU 1805  N   THR A 807    11419  14706  13263   -442  -3438    990       N  
ATOM   1806  CA  THR A 807      12.666 189.421-190.578  1.00106.35           C  
ANISOU 1806  CA  THR A 807    11263  15233  13911   -408  -3585    830       C  
ATOM   1807  C   THR A 807      12.668 190.014-191.975  1.00 98.46           C  
ANISOU 1807  C   THR A 807    10037  14313  13059   -484  -3135    538       C  
ATOM   1808  O   THR A 807      13.550 190.797-192.325  1.00101.27           O  
ANISOU 1808  O   THR A 807    10073  14851  13555   -608  -3094    380       O  
ATOM   1809  CB  THR A 807      13.630 188.217-190.563  1.00114.28           C  
ANISOU 1809  CB  THR A 807    11913  16123  15387    -55  -3874    926       C  
ATOM   1810  OG1 THR A 807      13.163 187.213-191.477  1.00114.75           O  
ANISOU 1810  OG1 THR A 807    11960  15916  15722    151  -3567    857       O  
ATOM   1811  CG2 THR A 807      13.721 187.623-189.172  1.00118.15           C  
ANISOU 1811  CG2 THR A 807    12674  16530  15688     71  -4371   1284       C  
ATOM   1812  N   CYS A 808      11.675 189.630-192.768  1.00 89.32           N  
ANISOU 1812  N   CYS A 808     9056  13025  11858   -424  -2800    469       N  
ATOM   1813  CA  CYS A 808      11.593 190.051-194.156  1.00 89.90           C  
ANISOU 1813  CA  CYS A 808     8995  13180  11982   -437  -2396    221       C  
ATOM   1814  C   CYS A 808      10.659 191.241-194.350  1.00 93.92           C  
ANISOU 1814  C   CYS A 808     9825  13778  12083   -646  -2162    187       C  
ATOM   1815  O   CYS A 808      10.470 191.706-195.475  1.00 90.42           O  
ANISOU 1815  O   CYS A 808     9372  13408  11578   -644  -1847     38       O  
ATOM   1816  CB  CYS A 808      11.107 188.890-195.010  1.00 87.24           C  
ANISOU 1816  CB  CYS A 808     8641  12672  11835   -217  -2224    104       C  
ATOM   1817  SG  CYS A 808       9.588 188.152-194.382  1.00131.35           S  
ANISOU 1817  SG  CYS A 808    14645  18025  17238   -243  -2270    249       S  
ATOM   1818  N   ASP A 809      10.061 191.725-193.265  1.00102.30           N  
ANISOU 1818  N   ASP A 809    11200  14825  12846   -793  -2306    331       N  
ATOM   1819  CA  ASP A 809       9.133 192.852-193.355  1.00106.92           C  
ANISOU 1819  CA  ASP A 809    12088  15451  13088   -935  -2085    295       C  
ATOM   1820  C   ASP A 809       9.844 194.143-193.744  1.00106.76           C  
ANISOU 1820  C   ASP A 809    12004  15516  13042  -1105  -1945    201       C  
ATOM   1821  O   ASP A 809      10.852 194.512-193.145  1.00110.92           O  
ANISOU 1821  O   ASP A 809    12378  16093  13672  -1261  -2139    194       O  
ATOM   1822  CB  ASP A 809       8.377 193.048-192.036  1.00113.64           C  
ANISOU 1822  CB  ASP A 809    13288  16256  13634  -1044  -2216    434       C  
ATOM   1823  CG  ASP A 809       7.261 192.025-191.838  1.00119.30           C  
ANISOU 1823  CG  ASP A 809    14145  16855  14327   -944  -2165    522       C  
ATOM   1824  OD1 ASP A 809       6.677 191.559-192.844  1.00118.89           O  
ANISOU 1824  OD1 ASP A 809    13986  16777  14409   -830  -1982    407       O  
ATOM   1825  OD2 ASP A 809       6.966 191.688-190.670  1.00122.60           O1-
ANISOU 1825  OD2 ASP A 809    14793  17210  14578  -1005  -2299    696       O1-
ATOM   1826  N   THR A 810       9.325 194.829-194.755  1.00101.42           N  
ANISOU 1826  N   THR A 810    11448  14849  12237  -1082  -1620    132       N  
ATOM   1827  CA  THR A 810       9.875 196.122-195.123  1.00 97.33           C  
ANISOU 1827  CA  THR A 810    10974  14329  11680  -1267  -1414     92       C  
ATOM   1828  C   THR A 810       9.502 197.119-194.045  1.00 98.91           C  
ANISOU 1828  C   THR A 810    11489  14437  11655  -1459  -1496    122       C  
ATOM   1829  O   THR A 810       8.653 196.835-193.195  1.00 98.03           O  
ANISOU 1829  O   THR A 810    11587  14303  11358  -1408  -1635    175       O  
ATOM   1830  CB  THR A 810       9.362 196.613-196.483  1.00 93.72           C  
ANISOU 1830  CB  THR A 810    10664  13876  11070  -1144  -1051     77       C  
ATOM   1831  OG1 THR A 810       7.936 196.514-196.527  1.00 91.48           O  
ANISOU 1831  OG1 THR A 810    10636  13581  10540   -961  -1056    108       O  
ATOM   1832  CG2 THR A 810       9.943 195.779-197.595  1.00 92.92           C  
ANISOU 1832  CG2 THR A 810    10277  13883  11146  -1000   -915    -14       C  
ATOM   1833  N   ILE A 811      10.140 198.284-194.087  1.00102.57           N  
ANISOU 1833  N   ILE A 811    12001  14826  12145  -1701  -1363     66       N  
ATOM   1834  CA  ILE A 811       9.975 199.297-193.052  1.00103.85           C  
ANISOU 1834  CA  ILE A 811    12466  14863  12129  -1926  -1434     17       C  
ATOM   1835  C   ILE A 811       8.519 199.707-192.899  1.00100.72           C  
ANISOU 1835  C   ILE A 811    12490  14356  11423  -1757  -1284     64       C  
ATOM   1836  O   ILE A 811       7.972 199.710-191.790  1.00102.25           O  
ANISOU 1836  O   ILE A 811    12898  14536  11415  -1786  -1427     42       O  
ATOM   1837  CB  ILE A 811      10.819 200.544-193.358  1.00107.96           C  
ANISOU 1837  CB  ILE A 811    12995  15239  12788  -2238  -1221    -76       C  
ATOM   1838  CG1 ILE A 811      12.266 200.140-193.653  1.00111.48           C  
ANISOU 1838  CG1 ILE A 811    12904  15830  13621  -2405  -1303   -152       C  
ATOM   1839  CG2 ILE A 811      10.743 201.532-192.210  1.00108.94           C  
ANISOU 1839  CG2 ILE A 811    13432  15204  12756  -2504  -1331   -207       C  
ATOM   1840  CD1 ILE A 811      12.869 199.220-192.606  1.00112.52           C  
ANISOU 1840  CD1 ILE A 811    12724  16161  13868  -2410  -1819   -198       C  
ATOM   1841  N   GLN A 812       7.889 200.038-194.020  1.00 96.95           N  
ANISOU 1841  N   GLN A 812    12122  13823  10893  -1557   -992    128       N  
ATOM   1842  CA  GLN A 812       6.493 200.444-193.996  1.00 95.27           C  
ANISOU 1842  CA  GLN A 812    12214  13532  10453  -1334   -866    163       C  
ATOM   1843  C   GLN A 812       5.618 199.347-193.404  1.00 90.00           C  
ANISOU 1843  C   GLN A 812    11464  13011   9722  -1188  -1037    168       C  
ATOM   1844  O   GLN A 812       4.745 199.630-192.598  1.00 89.49           O  
ANISOU 1844  O   GLN A 812    11609  12896   9497  -1157  -1004    142       O  
ATOM   1845  CB  GLN A 812       6.002 200.829-195.388  1.00 98.21           C  
ANISOU 1845  CB  GLN A 812    12674  13880  10763  -1081   -621    254       C  
ATOM   1846  CG  GLN A 812       4.578 201.354-195.395  1.00102.07           C  
ANISOU 1846  CG  GLN A 812    13413  14299  11068   -797   -532    285       C  
ATOM   1847  CD  GLN A 812       4.226 202.029-196.698  1.00111.37           C  
ANISOU 1847  CD  GLN A 812    14768  15416  12130   -534   -337    417       C  
ATOM   1848  OE1 GLN A 812       5.110 202.419-197.464  1.00115.70           O  
ANISOU 1848  OE1 GLN A 812    15378  15887  12694   -642   -172    503       O  
ATOM   1849  NE2 GLN A 812       2.931 202.171-196.964  1.00114.40           N  
ANISOU 1849  NE2 GLN A 812    15230  15847  12391   -180   -351    444       N  
ATOM   1850  N   GLN A 813       5.869 198.101-193.797  1.00 86.64           N  
ANISOU 1850  N   GLN A 813    10741  12732   9445  -1113  -1171    190       N  
ATOM   1851  CA  GLN A 813       5.130 196.963-193.263  1.00 84.07           C  
ANISOU 1851  CA  GLN A 813    10342  12479   9122  -1029  -1298    213       C  
ATOM   1852  C   GLN A 813       5.203 196.914-191.745  1.00 85.85           C  
ANISOU 1852  C   GLN A 813    10737  12668   9213  -1204  -1448    251       C  
ATOM   1853  O   GLN A 813       4.193 196.688-191.071  1.00 88.34           O  
ANISOU 1853  O   GLN A 813    11198  12981   9386  -1172  -1382    273       O  
ATOM   1854  CB  GLN A 813       5.669 195.660-193.834  1.00 84.64           C  
ANISOU 1854  CB  GLN A 813    10105  12623   9432   -959  -1424    214       C  
ATOM   1855  CG  GLN A 813       5.304 195.418-195.276  1.00 87.88           C  
ANISOU 1855  CG  GLN A 813    10393  13112   9886   -761  -1287    132       C  
ATOM   1856  CD  GLN A 813       5.659 194.015-195.718  1.00 93.84           C  
ANISOU 1856  CD  GLN A 813    10884  13891  10880   -685  -1388     68       C  
ATOM   1857  OE1 GLN A 813       5.661 193.705-196.908  1.00 95.30           O  
ANISOU 1857  OE1 GLN A 813    10961  14154  11095   -548  -1296    -51       O  
ATOM   1858  NE2 GLN A 813       5.956 193.153-194.754  1.00 98.33           N  
ANISOU 1858  NE2 GLN A 813    11393  14372  11597   -755  -1574    146       N  
ATOM   1859  N   VAL A 814       6.401 197.131-191.211  1.00 86.11           N  
ANISOU 1859  N   VAL A 814    10742  12700   9277  -1397  -1645    244       N  
ATOM   1860  CA  VAL A 814       6.591 197.190-189.766  1.00 89.59           C  
ANISOU 1860  CA  VAL A 814    11398  13148   9495  -1566  -1853    261       C  
ATOM   1861  C   VAL A 814       5.770 198.321-189.153  1.00 92.17           C  
ANISOU 1861  C   VAL A 814    12111  13382   9527  -1632  -1640    157       C  
ATOM   1862  O   VAL A 814       5.090 198.128-188.137  1.00 91.08           O  
ANISOU 1862  O   VAL A 814    12223  13262   9122  -1649  -1621    181       O  
ATOM   1863  CB  VAL A 814       8.067 197.393-189.396  1.00 90.86           C  
ANISOU 1863  CB  VAL A 814    11402  13364   9758  -1768  -2162    210       C  
ATOM   1864  CG1 VAL A 814       8.205 197.620-187.897  1.00 93.42           C  
ANISOU 1864  CG1 VAL A 814    12023  13731   9742  -1943  -2423    187       C  
ATOM   1865  CG2 VAL A 814       8.894 196.199-189.843  1.00 91.61           C  
ANISOU 1865  CG2 VAL A 814    11088  13544  10176  -1646  -2380    307       C  
ATOM   1866  N   LYS A 815       5.836 199.495-189.782  1.00 93.28           N  
ANISOU 1866  N   LYS A 815    12328  13395   9721  -1657  -1437     47       N  
ATOM   1867  CA  LYS A 815       5.091 200.663-189.311  1.00 93.67           C  
ANISOU 1867  CA  LYS A 815    12751  13280   9558  -1669  -1199    -78       C  
ATOM   1868  C   LYS A 815       3.607 200.332-189.216  1.00 93.39           C  
ANISOU 1868  C   LYS A 815    12782  13283   9419  -1420   -983    -39       C  
ATOM   1869  O   LYS A 815       2.945 200.608-188.212  1.00 95.21           O  
ANISOU 1869  O   LYS A 815    13280  13487   9406  -1446   -862   -121       O  
ATOM   1870  CB  LYS A 815       5.290 201.850-190.255  1.00 93.42           C  
ANISOU 1870  CB  LYS A 815    12795  13034   9668  -1658   -972   -128       C  
ATOM   1871  CG  LYS A 815       6.717 202.371-190.349  1.00 97.00           C  
ANISOU 1871  CG  LYS A 815    13166  13408  10283  -1980  -1083   -208       C  
ATOM   1872  CD  LYS A 815       6.791 203.553-191.305  1.00100.06           C  
ANISOU 1872  CD  LYS A 815    13710  13511  10797  -1979   -759   -201       C  
ATOM   1873  CE  LYS A 815       8.219 204.005-191.549  1.00102.42           C  
ANISOU 1873  CE  LYS A 815    13848  13728  11340  -2351   -785   -276       C  
ATOM   1874  NZ  LYS A 815       8.288 205.004-192.654  1.00103.40           N1+
ANISOU 1874  NZ  LYS A 815    14145  13554  11587  -2341   -395   -181       N1+
ATOM   1875  N   GLU A 816       3.104 199.721-190.278  1.00 92.47           N  
ANISOU 1875  N   GLU A 816    12395  13247   9491  -1193   -926     54       N  
ATOM   1876  CA  GLU A 816       1.719 199.311-190.370  1.00 95.81           C  
ANISOU 1876  CA  GLU A 816    12739  13747   9918   -974   -755     59       C  
ATOM   1877  C   GLU A 816       1.375 198.299-189.289  1.00 93.66           C  
ANISOU 1877  C   GLU A 816    12483  13565   9538  -1094   -790    113       C  
ATOM   1878  O   GLU A 816       0.254 198.286-188.782  1.00 93.03           O  
ANISOU 1878  O   GLU A 816    12457  13510   9379  -1029   -556     70       O  
ATOM   1879  CB  GLU A 816       1.443 198.735-191.759  1.00102.08           C  
ANISOU 1879  CB  GLU A 816    13214  14646  10926   -761   -788    102       C  
ATOM   1880  CG  GLU A 816       1.609 199.753-192.880  1.00112.25           C  
ANISOU 1880  CG  GLU A 816    14568  15850  12233   -595   -702    108       C  
ATOM   1881  CD  GLU A 816       1.814 199.113-194.248  1.00121.25           C  
ANISOU 1881  CD  GLU A 816    15459  17127  13483   -455   -792    147       C  
ATOM   1882  OE1 GLU A 816       2.092 197.892-194.307  1.00123.48           O  
ANISOU 1882  OE1 GLU A 816    15504  17526  13886   -529   -937    135       O  
ATOM   1883  OE2 GLU A 816       1.699 199.839-195.265  1.00124.52           O1-
ANISOU 1883  OE2 GLU A 816    15960  17511  13840   -257   -706    190       O1-
ATOM   1884  N   LYS A 817       2.333 197.453-188.926  1.00 94.29           N  
ANISOU 1884  N   LYS A 817    12518  13684   9625  -1253  -1059    223       N  
ATOM   1885  CA  LYS A 817       2.070 196.471-187.878  1.00102.95           C  
ANISOU 1885  CA  LYS A 817    13721  14819  10578  -1354  -1094    351       C  
ATOM   1886  C   LYS A 817       1.972 197.112-186.498  1.00111.37           C  
ANISOU 1886  C   LYS A 817    15213  15878  11226  -1504  -1020    304       C  
ATOM   1887  O   LYS A 817       1.062 196.795-185.727  1.00114.46           O  
ANISOU 1887  O   LYS A 817    15770  16292  11427  -1528   -777    344       O  
ATOM   1888  CB  LYS A 817       3.095 195.335-187.893  1.00103.74           C  
ANISOU 1888  CB  LYS A 817    13672  14927  10817  -1403  -1431    520       C  
ATOM   1889  CG  LYS A 817       2.870 194.341-189.027  1.00105.29           C  
ANISOU 1889  CG  LYS A 817    13511  15107  11387  -1262  -1420    544       C  
ATOM   1890  CD  LYS A 817       3.837 193.169-188.949  1.00106.70           C  
ANISOU 1890  CD  LYS A 817    13569  15229  11742  -1262  -1714    703       C  
ATOM   1891  CE  LYS A 817       3.739 192.289-190.186  1.00104.00           C  
ANISOU 1891  CE  LYS A 817    12894  14842  11781  -1123  -1687    638       C  
ATOM   1892  NZ  LYS A 817       4.690 191.150-190.105  1.00105.23           N1+
ANISOU 1892  NZ  LYS A 817    12937  14885  12163  -1071  -1942    775       N1+
ATOM   1893  N   ILE A 818       2.892 198.023-186.190  1.00117.19           N  
ANISOU 1893  N   ILE A 818    16128  16584  11815  -1631  -1195    188       N  
ATOM   1894  CA  ILE A 818       2.863 198.695-184.892  1.00121.77           C  
ANISOU 1894  CA  ILE A 818    17157  17163  11948  -1791  -1157     65       C  
ATOM   1895  C   ILE A 818       1.653 199.623-184.773  1.00121.95           C  
ANISOU 1895  C   ILE A 818    17365  17091  11878  -1682   -689   -128       C  
ATOM   1896  O   ILE A 818       1.140 199.849-183.674  1.00127.15           O  
ANISOU 1896  O   ILE A 818    18383  17772  12155  -1753   -488   -217       O  
ATOM   1897  CB  ILE A 818       4.171 199.472-184.604  1.00126.56           C  
ANISOU 1897  CB  ILE A 818    17873  17751  12464  -2004  -1495    -88       C  
ATOM   1898  CG1 ILE A 818       4.190 200.811-185.340  1.00126.15           C  
ANISOU 1898  CG1 ILE A 818    17824  17498  12611  -2001  -1289   -313       C  
ATOM   1899  CG2 ILE A 818       5.380 198.637-184.986  1.00127.30           C  
ANISOU 1899  CG2 ILE A 818    17622  17946  12801  -2041  -1935     72       C  
ATOM   1900  CD1 ILE A 818       5.451 201.599-185.112  1.00129.72           C  
ANISOU 1900  CD1 ILE A 818    18337  17889  13061  -2286  -1566   -504       C  
ATOM   1901  N   LEU A 819       1.191 200.147-185.905  1.00115.91           N  
ANISOU 1901  N   LEU A 819    16366  16229  11446  -1475   -510   -188       N  
ATOM   1902  CA  LEU A 819      -0.002 200.987-185.915  1.00114.44           C  
ANISOU 1902  CA  LEU A 819    16273  15946  11263  -1272    -95   -350       C  
ATOM   1903  C   LEU A 819      -1.259 200.147-185.743  1.00113.08           C  
ANISOU 1903  C   LEU A 819    15905  15918  11140  -1151    176   -281       C  
ATOM   1904  O   LEU A 819      -2.179 200.539-185.019  1.00117.56           O  
ANISOU 1904  O   LEU A 819    16636  16481  11550  -1095    547   -419       O  
ATOM   1905  CB  LEU A 819      -0.083 201.798-187.205  1.00110.84           C  
ANISOU 1905  CB  LEU A 819    15654  15340  11122  -1039    -46   -382       C  
ATOM   1906  CG  LEU A 819       0.794 203.047-187.240  1.00110.28           C  
ANISOU 1906  CG  LEU A 819    15875  15008  11018  -1162    -90   -517       C  
ATOM   1907  CD1 LEU A 819       0.701 203.724-188.593  1.00108.51           C  
ANISOU 1907  CD1 LEU A 819    15537  14615  11078   -915    -12   -448       C  
ATOM   1908  CD2 LEU A 819       0.361 203.991-186.140  1.00112.76           C  
ANISOU 1908  CD2 LEU A 819    16622  15155  11068  -1205    171   -777       C  
ATOM   1909  N   GLN A 820      -1.294 199.002-186.423  1.00109.41           N  
ANISOU 1909  N   GLN A 820    15075  15566  10929  -1128     25   -101       N  
ATOM   1910  CA  GLN A 820      -2.382 198.042-186.259  1.00105.98           C  
ANISOU 1910  CA  GLN A 820    14415  15245  10607  -1110    263    -39       C  
ATOM   1911  C   GLN A 820      -2.506 197.667-184.795  1.00102.87           C  
ANISOU 1911  C   GLN A 820    14390  14879   9819  -1334    450     28       C  
ATOM   1912  O   GLN A 820      -3.592 197.725-184.224  1.00101.30           O  
ANISOU 1912  O   GLN A 820    14210  14725   9553  -1318    885    -54       O  
ATOM   1913  CB  GLN A 820      -2.141 196.778-187.091  1.00106.47           C  
ANISOU 1913  CB  GLN A 820    14120  15357  10976  -1132     20    119       C  
ATOM   1914  CG  GLN A 820      -2.690 196.828-188.509  1.00110.59           C  
ANISOU 1914  CG  GLN A 820    14211  15941  11867   -887    -16     20       C  
ATOM   1915  CD  GLN A 820      -2.693 195.463-189.181  1.00117.74           C  
ANISOU 1915  CD  GLN A 820    14787  16890  13059   -944   -177     92       C  
ATOM   1916  OE1 GLN A 820      -2.627 194.430-188.514  1.00121.47           O  
ANISOU 1916  OE1 GLN A 820    15319  17307  13527  -1150   -150    230       O  
ATOM   1917  NE2 GLN A 820      -2.766 195.455-190.509  1.00119.30           N  
ANISOU 1917  NE2 GLN A 820    14685  17160  13483   -756   -336     -1       N  
ATOM   1918  N   THR A 821      -1.380 197.291-184.195  1.00103.60           N  
ANISOU 1918  N   THR A 821    14766  14961   9636  -1525    120    180       N  
ATOM   1919  CA  THR A 821      -1.341 196.912-182.786  1.00109.78           C  
ANISOU 1919  CA  THR A 821    15999  15789   9924  -1723    210    298       C  
ATOM   1920  C   THR A 821      -1.811 198.047-181.890  1.00114.84           C  
ANISOU 1920  C   THR A 821    17035  16436  10163  -1738    551     37       C  
ATOM   1921  O   THR A 821      -2.649 197.851-181.003  1.00119.99           O  
ANISOU 1921  O   THR A 821    17910  17147  10533  -1804    982     41       O  
ATOM   1922  CB  THR A 821       0.086 196.532-182.349  1.00111.05           C  
ANISOU 1922  CB  THR A 821    16388  15968   9839  -1858   -332    473       C  
ATOM   1923  OG1 THR A 821       0.651 195.617-183.294  1.00110.26           O  
ANISOU 1923  OG1 THR A 821    15895  15827  10172  -1792   -646    655       O  
ATOM   1924  CG2 THR A 821       0.078 195.899-180.959  1.00114.21           C  
ANISOU 1924  CG2 THR A 821    17279  16433   9683  -2017   -295    690       C  
ATOM   1925  N   PHE A 822      -1.256 199.232-182.123  1.00113.92           N  
ANISOU 1925  N   PHE A 822    17024  16230  10030  -1694    400   -205       N  
ATOM   1926  CA  PHE A 822      -1.589 200.392-181.315  1.00116.86           C  
ANISOU 1926  CA  PHE A 822    17812  16538  10050  -1703    702   -518       C  
ATOM   1927  C   PHE A 822      -3.087 200.648-181.336  1.00118.81           C  
ANISOU 1927  C   PHE A 822    17906  16779  10457  -1494   1320   -656       C  
ATOM   1928  O   PHE A 822      -3.697 200.847-180.291  1.00121.24           O  
ANISOU 1928  O   PHE A 822    18550  17135  10380  -1548   1736   -791       O  
ATOM   1929  CB  PHE A 822      -0.833 201.628-181.791  1.00117.14           C  
ANISOU 1929  CB  PHE A 822    17922  16381  10204  -1688    487   -760       C  
ATOM   1930  CG  PHE A 822      -1.086 202.845-180.951  1.00125.04           C  
ANISOU 1930  CG  PHE A 822    19402  17240  10868  -1716    779  -1136       C  
ATOM   1931  CD1 PHE A 822      -0.390 203.044-179.774  1.00129.81           C  
ANISOU 1931  CD1 PHE A 822    20522  17907  10891  -1994    592  -1288       C  
ATOM   1932  CD2 PHE A 822      -2.026 203.786-181.333  1.00127.17           C  
ANISOU 1932  CD2 PHE A 822    19617  17309  11392  -1437   1221  -1358       C  
ATOM   1933  CE1 PHE A 822      -0.624 204.159-178.998  1.00134.84           C  
ANISOU 1933  CE1 PHE A 822    21639  18396  11197  -2035    875  -1701       C  
ATOM   1934  CE2 PHE A 822      -2.263 204.901-180.561  1.00131.73           C  
ANISOU 1934  CE2 PHE A 822    20658  17698  11695  -1436   1529  -1741       C  
ATOM   1935  CZ  PHE A 822      -1.562 205.088-179.392  1.00135.98           C  
ANISOU 1935  CZ  PHE A 822    21737  18288  11643  -1756   1374  -1936       C  
ATOM   1936  N   GLN A 823      -3.680 200.631-182.524  1.00119.55           N  
ANISOU 1936  N   GLN A 823    17475  16844  11107  -1245   1376   -637       N  
ATOM   1937  CA  GLN A 823      -5.122 200.808-182.642  1.00127.28           C  
ANISOU 1937  CA  GLN A 823    18161  17864  12337  -1008   1895   -774       C  
ATOM   1938  C   GLN A 823      -5.860 199.666-181.954  1.00134.88           C  
ANISOU 1938  C   GLN A 823    19039  19005  13205  -1185   2231   -627       C  
ATOM   1939  O   GLN A 823      -6.935 199.862-181.386  1.00138.52           O  
ANISOU 1939  O   GLN A 823    19466  19527  13637  -1123   2794   -786       O  
ATOM   1940  CB  GLN A 823      -5.540 200.882-184.109  1.00125.50           C  
ANISOU 1940  CB  GLN A 823    17365  17630  12690   -702   1756   -755       C  
ATOM   1941  CG  GLN A 823      -7.026 201.113-184.302  1.00129.88           C  
ANISOU 1941  CG  GLN A 823    17511  18267  13571   -405   2202   -922       C  
ATOM   1942  CD  GLN A 823      -7.456 200.923-185.738  1.00130.36           C  
ANISOU 1942  CD  GLN A 823    16982  18408  14143   -123   1958   -872       C  
ATOM   1943  OE1 GLN A 823      -8.559 201.308-186.126  1.00133.98           O  
ANISOU 1943  OE1 GLN A 823    17046  18937  14922    209   2177  -1024       O  
ATOM   1944  NE2 GLN A 823      -6.584 200.321-186.539  1.00127.21           N  
ANISOU 1944  NE2 GLN A 823    16507  18021  13807   -233   1490   -678       N  
ATOM   1945  N   ARG A 824      -5.270 198.474-182.003  1.00138.11           N  
ANISOU 1945  N   ARG A 824    19417  19465  13593  -1405   1923   -319       N  
ATOM   1946  CA  ARG A 824      -5.852 197.292-181.370  1.00144.11           C  
ANISOU 1946  CA  ARG A 824    20166  20310  14278  -1622   2233   -107       C  
ATOM   1947  C   ARG A 824      -5.681 197.301-179.850  1.00146.84           C  
ANISOU 1947  C   ARG A 824    21194  20694  13906  -1841   2481    -47       C  
ATOM   1948  O   ARG A 824      -6.149 196.389-179.170  1.00152.85           O  
ANISOU 1948  O   ARG A 824    22081  21497  14498  -2043   2819    172       O  
ATOM   1949  CB  ARG A 824      -5.252 196.005-181.951  1.00146.84           C  
ANISOU 1949  CB  ARG A 824    20307  20616  14870  -1748   1821    211       C  
ATOM   1950  CG  ARG A 824      -5.756 195.630-183.342  1.00149.34           C  
ANISOU 1950  CG  ARG A 824    19940  20944  15858  -1597   1717    146       C  
ATOM   1951  CD  ARG A 824      -4.944 194.477-183.932  1.00150.51           C  
ANISOU 1951  CD  ARG A 824    19972  21003  16210  -1700   1274    395       C  
ATOM   1952  NE  ARG A 824      -5.330 194.160-185.305  1.00151.39           N  
ANISOU 1952  NE  ARG A 824    19494  21145  16884  -1560   1126    273       N  
ATOM   1953  CZ  ARG A 824      -4.651 193.342-186.105  1.00151.85           C  
ANISOU 1953  CZ  ARG A 824    19386  21124  17184  -1574    743    379       C  
ATOM   1954  NH1 ARG A 824      -3.542 192.758-185.671  1.00152.41           N1+
ANISOU 1954  NH1 ARG A 824    19785  21070  17054  -1688    463    630       N1+
ATOM   1955  NH2 ARG A 824      -5.074 193.109-187.342  1.00151.19           N  
ANISOU 1955  NH2 ARG A 824    18809  21101  17533  -1448    623    212       N  
ATOM   1956  N   LYS A 825      -5.010 198.319-179.316  1.00142.13           N  
ANISOU 1956  N   LYS A 825    21069  20070  12864  -1824   2323   -243       N  
ATOM   1957  CA  LYS A 825      -4.854 198.424-177.863  1.00141.63           C  
ANISOU 1957  CA  LYS A 825    21711  20084  12020  -2018   2525   -252       C  
ATOM   1958  C   LYS A 825      -5.430 199.718-177.280  1.00144.37           C  
ANISOU 1958  C   LYS A 825    22339  20412  12103  -1908   3002   -703       C  
ATOM   1959  O   LYS A 825      -5.746 199.789-176.090  1.00147.70           O  
ANISOU 1959  O   LYS A 825    23286  20929  11904  -2039   3417   -779       O  
ATOM   1960  CB  LYS A 825      -3.383 198.280-177.461  1.00136.23           C  
ANISOU 1960  CB  LYS A 825    21458  19418  10887  -2171   1831    -94       C  
ATOM   1961  CG  LYS A 825      -3.176 198.065-175.971  1.00138.65           C  
ANISOU 1961  CG  LYS A 825    22516  19860  10304  -2376   1920      3       C  
ATOM   1962  CD  LYS A 825      -1.718 198.201-175.580  1.00137.55           C  
ANISOU 1962  CD  LYS A 825    22748  19783   9732  -2479   1150     40       C  
ATOM   1963  CE  LYS A 825      -1.555 198.180-174.070  1.00144.97           C  
ANISOU 1963  CE  LYS A 825    24506  20903   9673  -2649   1198     64       C  
ATOM   1964  NZ  LYS A 825      -0.144 198.416-173.655  1.00145.99           N1+
ANISOU 1964  NZ  LYS A 825    24950  21147   9374  -2745    373     21       N1+
ATOM   1965  N   PHE A 826      -5.576 200.736-178.120  1.00143.00           N  
ANISOU 1965  N   PHE A 826    21857  20093  12384  -1649   2970   -996       N  
ATOM   1966  CA  PHE A 826      -5.989 202.055-177.652  1.00147.13           C  
ANISOU 1966  CA  PHE A 826    22674  20499  12729  -1497   3364  -1449       C  
ATOM   1967  C   PHE A 826      -7.227 202.582-178.379  1.00145.91           C  
ANISOU 1967  C   PHE A 826    21960  20270  13208  -1120   3834  -1651       C  
ATOM   1968  O   PHE A 826      -7.775 203.619-178.009  1.00146.21           O  
ANISOU 1968  O   PHE A 826    22174  20183  13195   -917   4269  -2029       O  
ATOM   1969  CB  PHE A 826      -4.835 203.055-177.790  1.00147.13           C  
ANISOU 1969  CB  PHE A 826    23002  20299  12603  -1532   2857  -1661       C  
ATOM   1970  CG  PHE A 826      -3.621 202.708-176.968  1.00148.17           C  
ANISOU 1970  CG  PHE A 826    23659  20544  12094  -1877   2356  -1559       C  
ATOM   1971  CD1 PHE A 826      -2.634 201.881-177.477  1.00144.27           C  
ANISOU 1971  CD1 PHE A 826    22951  20123  11742  -2003   1714  -1203       C  
ATOM   1972  CD2 PHE A 826      -3.460 203.223-175.691  1.00153.09           C  
ANISOU 1972  CD2 PHE A 826    24982  21217  11969  -2046   2503  -1847       C  
ATOM   1973  CE1 PHE A 826      -1.514 201.569-176.728  1.00146.48           C  
ANISOU 1973  CE1 PHE A 826    23646  20534  11477  -2261   1192  -1109       C  
ATOM   1974  CE2 PHE A 826      -2.341 202.912-174.937  1.00155.33           C  
ANISOU 1974  CE2 PHE A 826    25729  21655  11634  -2335   1949  -1764       C  
ATOM   1975  CZ  PHE A 826      -1.368 202.084-175.457  1.00152.06           C  
ANISOU 1975  CZ  PHE A 826    25035  21323  11417  -2427   1273  -1380       C  
ATOM   1976  N   GLY A 827      -7.656 201.872-179.420  1.00145.88           N  
ANISOU 1976  N   GLY A 827    21279  20342  13807  -1003   3717  -1424       N  
ATOM   1977  CA  GLY A 827      -8.857 202.237-180.154  1.00149.45           C  
ANISOU 1977  CA  GLY A 827    21110  20797  14875   -625   4061  -1589       C  
ATOM   1978  C   GLY A 827      -8.774 203.590-180.835  1.00150.25           C  
ANISOU 1978  C   GLY A 827    21208  20636  15246   -236   3929  -1831       C  
ATOM   1979  O   GLY A 827      -9.788 204.170-181.224  1.00154.35           O  
ANISOU 1979  O   GLY A 827    21341  21120  16187    165   4254  -2024       O  
ATOM   1980  N   PHE A 828      -7.556 204.096-180.973  1.00146.04           N  
ANISOU 1980  N   PHE A 828    21096  19898  14493   -352   3455  -1811       N  
ATOM   1981  CA  PHE A 828      -7.328 205.368-181.636  1.00142.43           C  
ANISOU 1981  CA  PHE A 828    20729  19107  14282    -51   3328  -1985       C  
ATOM   1982  C   PHE A 828      -6.054 205.280-182.454  1.00132.75           C  
ANISOU 1982  C   PHE A 828    19543  17781  13113   -215   2680  -1755       C  
ATOM   1983  O   PHE A 828      -5.014 204.859-181.952  1.00128.84           O  
ANISOU 1983  O   PHE A 828    19358  17348  12247   -603   2366  -1668       O  
ATOM   1984  CB  PHE A 828      -7.230 206.491-180.616  1.00148.28           C  
ANISOU 1984  CB  PHE A 828    22109  19591  14642    -69   3662  -2383       C  
ATOM   1985  N   ARG A 829      -6.143 205.665-183.720  1.00130.00           N  
ANISOU 1985  N   ARG A 829    18869  17301  13224    102   2486  -1650       N  
ATOM   1986  CA  ARG A 829      -4.981 205.662-184.589  1.00127.11           C  
ANISOU 1986  CA  ARG A 829    18526  16830  12938    -32   1973  -1443       C  
ATOM   1987  C   ARG A 829      -3.957 206.665-184.078  1.00128.29           C  
ANISOU 1987  C   ARG A 829    19263  16647  12835   -267   1894  -1639       C  
ATOM   1988  O   ARG A 829      -4.288 207.819-183.805  1.00133.50           O  
ANISOU 1988  O   ARG A 829    20235  16974  13515    -85   2195  -1908       O  
ATOM   1989  CB  ARG A 829      -5.383 205.995-186.026  1.00128.23           C  
ANISOU 1989  CB  ARG A 829    18296  16888  13537    392   1854  -1296       C  
ATOM   1990  CG  ARG A 829      -6.254 204.939-186.698  1.00128.79           C  
ANISOU 1990  CG  ARG A 829    17729  17321  13883    571   1795  -1138       C  
ATOM   1991  CD  ARG A 829      -6.639 205.371-188.108  1.00132.14           C  
ANISOU 1991  CD  ARG A 829    17856  17692  14659   1027   1613  -1015       C  
ATOM   1992  NE  ARG A 829      -7.344 204.328-188.852  1.00133.26           N  
ANISOU 1992  NE  ARG A 829    17378  18206  15048   1146   1448   -912       N  
ATOM   1993  CZ  ARG A 829      -8.657 204.127-188.800  1.00137.61           C  
ANISOU 1993  CZ  ARG A 829    17459  18968  15860   1413   1668  -1043       C  
ATOM   1994  NH1 ARG A 829      -9.420 204.893-188.030  1.00142.63           N1+
ANISOU 1994  NH1 ARG A 829    18171  19483  16540   1632   2108  -1266       N1+
ATOM   1995  NH2 ARG A 829      -9.207 203.156-189.515  1.00136.96           N  
ANISOU 1995  NH2 ARG A 829    16801  19217  16021   1449   1463   -992       N  
ATOM   1996  N   TYR A 830      -2.715 206.214-183.938  1.00125.51           N  
ANISOU 1996  N   TYR A 830    19032  16372  12282   -673   1484  -1534       N  
ATOM   1997  CA  TYR A 830      -1.632 207.079-183.491  1.00129.06           C  
ANISOU 1997  CA  TYR A 830    19947  16551  12539   -979   1328  -1749       C  
ATOM   1998  C   TYR A 830      -1.355 208.148-184.539  1.00129.37           C  
ANISOU 1998  C   TYR A 830    20021  16172  12960   -813   1333  -1739       C  
ATOM   1999  O   TYR A 830      -0.826 209.217-184.232  1.00132.37           O  
ANISOU 1999  O   TYR A 830    20819  16171  13303   -978   1392  -1996       O  
ATOM   2000  CB  TYR A 830      -0.368 206.260-183.218  1.00129.06           C  
ANISOU 2000  CB  TYR A 830    19922  16788  12326  -1406    830  -1615       C  
ATOM   2001  CG  TYR A 830       0.802 207.089-182.746  1.00135.99           C  
ANISOU 2001  CG  TYR A 830    21177  17450  13045  -1779    600  -1879       C  
ATOM   2002  CD1 TYR A 830       0.900 207.494-181.424  1.00143.81           C  
ANISOU 2002  CD1 TYR A 830    22662  18432  13549  -2009    654  -2230       C  
ATOM   2003  CD2 TYR A 830       1.807 207.471-183.623  1.00137.13           C  
ANISOU 2003  CD2 TYR A 830    21177  17407  13518  -1929    346  -1807       C  
ATOM   2004  CE1 TYR A 830       1.967 208.258-180.986  1.00149.37           C  
ANISOU 2004  CE1 TYR A 830    23678  18950  14124  -2392    396  -2541       C  
ATOM   2005  CE2 TYR A 830       2.880 208.233-183.197  1.00142.84           C  
ANISOU 2005  CE2 TYR A 830    22173  17928  14171  -2332    146  -2089       C  
ATOM   2006  CZ  TYR A 830       2.955 208.623-181.877  1.00149.16           C  
ANISOU 2006  CZ  TYR A 830    23434  18727  14512  -2568    138  -2474       C  
ATOM   2007  OH  TYR A 830       4.019 209.383-181.443  1.00154.67           O  
ANISOU 2007  OH  TYR A 830    24374  19237  15154  -3009   -109  -2822       O  
ATOM   2008  N   THR A 831      -1.720 207.850-185.781  1.00127.03           N  
ANISOU 2008  N   THR A 831    19319  15935  13013   -500   1276  -1442       N  
ATOM   2009  CA  THR A 831      -1.560 208.794-186.878  1.00129.35           C  
ANISOU 2009  CA  THR A 831    19680  15846  13620   -280   1306  -1337       C  
ATOM   2010  C   THR A 831      -2.593 208.534-187.971  1.00132.81           C  
ANISOU 2010  C   THR A 831    19718  16416  14330    250   1352  -1091       C  
ATOM   2011  O   THR A 831      -2.911 207.385-188.279  1.00130.92           O  
ANISOU 2011  O   THR A 831    19037  16597  14109    288   1188   -932       O  
ATOM   2012  CB  THR A 831      -0.144 208.723-187.482  1.00123.91           C  
ANISOU 2012  CB  THR A 831    18980  15105  12998   -651    981  -1185       C  
ATOM   2013  OG1 THR A 831      -0.078 209.546-188.651  1.00124.35           O  
ANISOU 2013  OG1 THR A 831    19116  14804  13326   -419   1074  -1004       O  
ATOM   2014  CG2 THR A 831       0.198 207.300-187.865  1.00117.53           C  
ANISOU 2014  CG2 THR A 831    17708  14774  12173   -759    655   -941       C  
ATOM   2015  N   GLN A 832      -3.126 209.605-188.547  1.00139.33           N  
ANISOU 2015  N   GLN A 832    20709  16861  15368    669   1554  -1072       N  
ATOM   2016  CA  GLN A 832      -4.055 209.479-189.661  1.00141.34           C  
ANISOU 2016  CA  GLN A 832    20604  17245  15855   1219   1508   -834       C  
ATOM   2017  C   GLN A 832      -3.322 208.907-190.871  1.00140.75           C  
ANISOU 2017  C   GLN A 832    20337  17344  15797   1125   1164   -506       C  
ATOM   2018  O   GLN A 832      -3.708 207.870-191.414  1.00138.26           O  
ANISOU 2018  O   GLN A 832    19559  17465  15507   1227    954   -382       O  
ATOM   2019  CB  GLN A 832      -4.676 210.825-189.992  1.00145.79           C  
ANISOU 2019  CB  GLN A 832    21463  17310  16623   1731   1761   -844       C  
ATOM   2020  N   GLN A 833      -2.255 209.585-191.281  1.00143.49           N  
ANISOU 2020  N   GLN A 833    21044  17335  16141    900   1146   -401       N  
ATOM   2021  CA  GLN A 833      -1.422 209.118-192.382  1.00142.11           C  
ANISOU 2021  CA  GLN A 833    20736  17301  15957    762    912   -119       C  
ATOM   2022  C   GLN A 833      -0.213 208.355-191.848  1.00141.36           C  
ANISOU 2022  C   GLN A 833    20538  17406  15765    156    735   -209       C  
ATOM   2023  O   GLN A 833       0.426 208.781-190.886  1.00142.96           O  
ANISOU 2023  O   GLN A 833    20999  17406  15912   -225    796   -433       O  
ATOM   2024  CB  GLN A 833      -0.981 210.286-193.249  1.00144.37           C  
ANISOU 2024  CB  GLN A 833    21447  17083  16325    880   1058     96       C  
ATOM   2025  N   ILE A 834       0.095 207.227-192.480  1.00138.96           N  
ANISOU 2025  N   ILE A 834    19851  17502  15446     93    489    -57       N  
ATOM   2026  CA  ILE A 834       1.176 206.355-192.030  1.00135.68           C  
ANISOU 2026  CA  ILE A 834    19256  17311  14986   -380    280   -114       C  
ATOM   2027  C   ILE A 834       2.545 206.930-192.403  1.00135.58           C  
ANISOU 2027  C   ILE A 834    19405  17054  15056   -734    295    -70       C  
ATOM   2028  O   ILE A 834       3.561 206.581-191.804  1.00137.23           O  
ANISOU 2028  O   ILE A 834    19520  17351  15272  -1157    134   -186       O  
ATOM   2029  CB  ILE A 834       1.002 204.924-192.600  1.00134.56           C  
ANISOU 2029  CB  ILE A 834    18651  17619  14857   -293     50      4       C  
ATOM   2030  CG1 ILE A 834      -0.429 204.434-192.356  1.00134.50           C  
ANISOU 2030  CG1 ILE A 834    18435  17823  14845     29     83    -51       C  
ATOM   2031  CG2 ILE A 834       2.009 203.955-191.989  1.00131.51           C  
ANISOU 2031  CG2 ILE A 834    18079  17435  14454   -696   -176    -45       C  
ATOM   2032  CD1 ILE A 834      -0.693 203.020-192.829  1.00131.63           C  
ANISOU 2032  CD1 ILE A 834    17633  17843  14539     63   -123      5       C  
ATOM   2033  N   ARG A 835       2.558 207.833-193.378  1.00135.34           N  
ANISOU 2033  N   ARG A 835    19614  16710  15098   -557    495    108       N  
ATOM   2034  CA  ARG A 835       3.797 208.445-193.851  1.00136.65           C  
ANISOU 2034  CA  ARG A 835    19934  16602  15384   -913    615    177       C  
ATOM   2035  C   ARG A 835       4.467 209.327-192.798  1.00139.54           C  
ANISOU 2035  C   ARG A 835    20583  16598  15837  -1361    705   -102       C  
ATOM   2036  O   ARG A 835       5.677 209.554-192.845  1.00139.72           O  
ANISOU 2036  O   ARG A 835    20566  16509  16011  -1823    717   -158       O  
ATOM   2037  CB  ARG A 835       3.528 209.279-195.103  1.00139.00           C  
ANISOU 2037  CB  ARG A 835    20536  16589  15687   -591    868    484       C  
ATOM   2038  CG  ARG A 835       2.670 210.511-194.852  1.00143.36           C  
ANISOU 2038  CG  ARG A 835    21561  16642  16268   -279   1099    479       C  
ATOM   2039  CD  ARG A 835       2.341 211.255-196.135  1.00146.56           C  
ANISOU 2039  CD  ARG A 835    22300  16750  16635    133   1293    866       C  
ATOM   2040  NE  ARG A 835       1.372 210.537-196.957  1.00145.34           N  
ANISOU 2040  NE  ARG A 835    21890  17033  16301    684   1075   1060       N  
ATOM   2041  CZ  ARG A 835       1.699 209.683-197.921  1.00143.84           C  
ANISOU 2041  CZ  ARG A 835    21445  17248  15958    694    930   1226       C  
ATOM   2042  NH1 ARG A 835       2.975 209.439-198.180  1.00142.72           N1+
ANISOU 2042  NH1 ARG A 835    21244  17133  15852    211   1026   1246       N1+
ATOM   2043  NH2 ARG A 835       0.754 209.071-198.622  1.00143.13           N  
ANISOU 2043  NH2 ARG A 835    21134  17549  15699   1181    692   1331       N  
ATOM   2044  N   ASP A 836       3.674 209.824-191.855  1.00141.85           N  
ANISOU 2044  N   ASP A 836    21137  16713  16045  -1233    778   -318       N  
ATOM   2045  CA  ASP A 836       4.160 210.772-190.857  1.00146.07           C  
ANISOU 2045  CA  ASP A 836    22031  16852  16618  -1620    880   -651       C  
ATOM   2046  C   ASP A 836       5.125 210.127-189.862  1.00141.94           C  
ANISOU 2046  C   ASP A 836    21277  16646  16009  -2138    549   -915       C  
ATOM   2047  O   ASP A 836       6.024 210.786-189.340  1.00146.41           O  
ANISOU 2047  O   ASP A 836    22002  16962  16665  -2615    530  -1177       O  
ATOM   2048  CB  ASP A 836       2.983 211.420-190.119  1.00151.28           C  
ANISOU 2048  CB  ASP A 836    23041  17263  17177  -1288   1085   -848       C  
ATOM   2049  CG  ASP A 836       2.000 212.095-191.063  1.00153.82           C  
ANISOU 2049  CG  ASP A 836    23563  17265  17615   -695   1353   -581       C  
ATOM   2050  OD1 ASP A 836       2.428 212.558-192.142  1.00154.82           O  
ANISOU 2050  OD1 ASP A 836    23815  17126  17881   -666   1466   -290       O  
ATOM   2051  OD2 ASP A 836       0.798 212.163-190.724  1.00155.12           O1-
ANISOU 2051  OD2 ASP A 836    23755  17457  17726   -243   1456   -652       O1-
ATOM   2052  N   ILE A 837       4.934 208.837-189.609  1.00133.69           N  
ANISOU 2052  N   ILE A 837    19857  16135  14803  -2039    267   -845       N  
ATOM   2053  CA  ILE A 837       5.756 208.095-188.661  1.00130.02           C  
ANISOU 2053  CA  ILE A 837    19181  16006  14212  -2417   -108  -1021       C  
ATOM   2054  C   ILE A 837       7.087 207.651-189.262  1.00125.79           C  
ANISOU 2054  C   ILE A 837    18240  15630  13923  -2725   -317   -925       C  
ATOM   2055  O   ILE A 837       7.129 207.160-190.389  1.00124.14           O  
ANISOU 2055  O   ILE A 837    17764  15539  13865  -2530   -247   -649       O  
ATOM   2056  CB  ILE A 837       5.012 206.839-188.169  1.00129.54           C  
ANISOU 2056  CB  ILE A 837    18920  16391  13907  -2170   -286   -927       C  
ATOM   2057  CG1 ILE A 837       3.849 207.228-187.262  1.00133.53           C  
ANISOU 2057  CG1 ILE A 837    19782  16803  14150  -1974    -68  -1107       C  
ATOM   2058  CG2 ILE A 837       5.953 205.893-187.439  1.00130.44           C  
ANISOU 2058  CG2 ILE A 837    18787  16863  13912  -2474   -724   -972       C  
ATOM   2059  CD1 ILE A 837       3.302 206.069-186.467  1.00133.65           C  
ANISOU 2059  CD1 ILE A 837    19675  17222  13885  -1893   -205  -1063       C  
ATOM   2060  N   GLU A 838       8.171 207.825-188.511  1.00124.55           N  
ANISOU 2060  N   GLU A 838    18017  15502  13804  -3200   -574  -1185       N  
ATOM   2061  CA  GLU A 838       9.443 207.211-188.882  1.00125.40           C  
ANISOU 2061  CA  GLU A 838    17611  15865  14171  -3468   -834  -1135       C  
ATOM   2062  C   GLU A 838       9.938 206.287-187.777  1.00123.54           C  
ANISOU 2062  C   GLU A 838    17145  16049  13744  -3600  -1369  -1259       C  
ATOM   2063  O   GLU A 838       9.584 206.460-186.613  1.00125.02           O  
ANISOU 2063  O   GLU A 838    17661  16260  13581  -3664  -1527  -1470       O  
ATOM   2064  CB  GLU A 838      10.495 208.259-189.243  1.00134.76           C  
ANISOU 2064  CB  GLU A 838    18778  16714  15711  -3937   -669  -1299       C  
ATOM   2065  CG  GLU A 838      10.243 208.958-190.578  1.00140.12           C  
ANISOU 2065  CG  GLU A 838    19631  17011  16598  -3794   -141  -1042       C  
ATOM   2066  CD  GLU A 838      10.274 208.012-191.774  1.00140.82           C  
ANISOU 2066  CD  GLU A 838    19346  17397  16762  -3491    -73   -688       C  
ATOM   2067  OE1 GLU A 838      10.794 206.879-191.646  1.00140.99           O  
ANISOU 2067  OE1 GLU A 838    18885  17859  16824  -3492   -404   -680       O  
ATOM   2068  OE2 GLU A 838       9.776 208.410-192.850  1.00140.97           O1-
ANISOU 2068  OE2 GLU A 838    19586  17193  16782  -3229    305   -423       O1-
ATOM   2069  N   ILE A 839      10.753 205.304-188.145  1.00120.92           N  
ANISOU 2069  N   ILE A 839    16280  16042  13620  -3607  -1637  -1120       N  
ATOM   2070  CA  ILE A 839      11.123 204.237-187.221  1.00119.61           C  
ANISOU 2070  CA  ILE A 839    15899  16274  13274  -3592  -2167  -1120       C  
ATOM   2071  C   ILE A 839      12.622 204.174-186.951  1.00122.75           C  
ANISOU 2071  C   ILE A 839    15829  16860  13951  -3958  -2588  -1304       C  
ATOM   2072  O   ILE A 839      13.421 204.053-187.881  1.00121.55           O  
ANISOU 2072  O   ILE A 839    15202  16734  14248  -4034  -2488  -1245       O  
ATOM   2073  CB  ILE A 839      10.631 202.873-187.742  1.00117.24           C  
ANISOU 2073  CB  ILE A 839    15362  16206  12977  -3167  -2188   -780       C  
ATOM   2074  CG1 ILE A 839       9.106 202.806-187.674  1.00116.64           C  
ANISOU 2074  CG1 ILE A 839    15688  16036  12594  -2842  -1894   -660       C  
ATOM   2075  CG2 ILE A 839      11.241 201.741-186.950  1.00118.48           C  
ANISOU 2075  CG2 ILE A 839    15259  16703  13055  -3140  -2730   -717       C  
ATOM   2076  CD1 ILE A 839       8.545 203.081-186.292  1.00119.85           C  
ANISOU 2076  CD1 ILE A 839    16549  16447  12541  -2913  -1992   -820       C  
ATOM   2077  N   GLU A 840      12.991 204.253-185.672  1.00126.74           N  
ANISOU 2077  N   GLU A 840    16457  17525  14174  -4177  -3058  -1544       N  
ATOM   2078  CA  GLU A 840      14.394 204.233-185.264  1.00131.36           C  
ANISOU 2078  CA  GLU A 840    16561  18344  15006  -4527  -3572  -1774       C  
ATOM   2079  C   GLU A 840      14.812 202.899-184.651  1.00130.44           C  
ANISOU 2079  C   GLU A 840    16138  18670  14754  -4279  -4186  -1591       C  
ATOM   2080  O   GLU A 840      13.991 202.181-184.082  1.00126.38           O  
ANISOU 2080  O   GLU A 840    15982  18254  13784  -3962  -4277  -1368       O  
ATOM   2081  CB  GLU A 840      14.693 205.370-184.282  1.00139.48           C  
ANISOU 2081  CB  GLU A 840    17913  19249  15835  -4999  -3763  -2246       C  
ATOM   2082  CG  GLU A 840      14.769 206.743-184.925  1.00144.89           C  
ANISOU 2082  CG  GLU A 840    18745  19443  16862  -5364  -3234  -2478       C  
ATOM   2083  CD  GLU A 840      15.376 207.790-184.007  1.00157.12           C  
ANISOU 2083  CD  GLU A 840    20466  20870  18364  -5932  -3497  -3029       C  
ATOM   2084  OE1 GLU A 840      15.190 207.688-182.774  1.00161.26           O  
ANISOU 2084  OE1 GLU A 840    21325  21603  18343  -5950  -3938  -3243       O  
ATOM   2085  OE2 GLU A 840      16.043 208.717-184.518  1.00162.39           O1-
ANISOU 2085  OE2 GLU A 840    20957  21222  19521  -6384  -3245  -3262       O1-
ATOM   2086  N   TYR A 841      16.100 202.585-184.768  1.00135.52           N  
ANISOU 2086  N   TYR A 841    16108  19557  15825  -4424  -4584  -1678       N  
ATOM   2087  CA  TYR A 841      16.639 201.308-184.307  1.00137.56           C  
ANISOU 2087  CA  TYR A 841    15998  20200  16068  -4127  -5191  -1474       C  
ATOM   2088  C   TYR A 841      17.852 201.484-183.388  1.00143.19           C  
ANISOU 2088  C   TYR A 841    16339  21238  16831  -4423  -5946  -1786       C  
ATOM   2089  O   TYR A 841      18.654 202.397-183.578  1.00147.72           O  
ANISOU 2089  O   TYR A 841    16564  21770  17794  -4890  -5934  -2162       O  
ATOM   2090  CB  TYR A 841      17.003 200.438-185.512  1.00138.44           C  
ANISOU 2090  CB  TYR A 841    15515  20343  16744  -3832  -4965  -1217       C  
ATOM   2091  CG  TYR A 841      17.894 199.266-185.184  1.00147.29           C  
ANISOU 2091  CG  TYR A 841    16083  21806  18076  -3558  -5587  -1079       C  
ATOM   2092  CD1 TYR A 841      17.392 198.149-184.533  1.00149.47           C  
ANISOU 2092  CD1 TYR A 841    16650  22180  17964  -3135  -5915   -742       C  
ATOM   2093  CD2 TYR A 841      19.238 199.270-185.536  1.00154.78           C  
ANISOU 2093  CD2 TYR A 841    16205  22955  19651  -3709  -5819  -1272       C  
ATOM   2094  CE1 TYR A 841      18.204 197.072-184.233  1.00156.09           C  
ANISOU 2094  CE1 TYR A 841    17026  23268  19011  -2822  -6496   -571       C  
ATOM   2095  CE2 TYR A 841      20.058 198.197-185.242  1.00160.87           C  
ANISOU 2095  CE2 TYR A 841    16427  24029  20668  -3382  -6410  -1144       C  
ATOM   2096  CZ  TYR A 841      19.537 197.101-184.589  1.00161.60           C  
ANISOU 2096  CZ  TYR A 841    16878  24176  20347  -2914  -6766   -778       C  
ATOM   2097  OH  TYR A 841      20.350 196.029-184.293  1.00167.20           O  
ANISOU 2097  OH  TYR A 841    17140  25092  21298  -2454  -7211   -648       O  
ATOM   2098  N   GLU A 842      17.981 200.604-182.396  1.00143.98           N  
ANISOU 2098  N   GLU A 842    16516  21645  16542  -4140  -6590  -1626       N  
ATOM   2099  CA  GLU A 842      19.102 200.652-181.454  1.00150.31           C  
ANISOU 2099  CA  GLU A 842    16993  22727  17392  -4126  -7201  -1920       C  
ATOM   2100  C   GLU A 842      20.140 199.561-181.714  1.00152.03           C  
ANISOU 2100  C   GLU A 842    16418  23228  18118  -3735  -7571  -1757       C  
ATOM   2101  O   GLU A 842      19.826 198.371-181.676  1.00149.06           O  
ANISOU 2101  O   GLU A 842    16127  22911  17600  -3239  -7675  -1319       O  
ATOM   2102  CB  GLU A 842      18.604 200.553-180.007  1.00152.20           C  
ANISOU 2102  CB  GLU A 842    17945  23093  16791  -3950  -7536  -1916       C  
ATOM   2103  CG  GLU A 842      19.712 200.329-178.983  1.00161.03           C  
ANISOU 2103  CG  GLU A 842    18735  24615  17832  -3809  -8253  -2137       C  
ATOM   2104  CD  GLU A 842      19.196 200.281-177.555  1.00165.10           C  
ANISOU 2104  CD  GLU A 842    20011  25286  17435  -3659  -8534  -2125       C  
ATOM   2105  OE1 GLU A 842      18.139 200.888-177.281  1.00162.73           O  
ANISOU 2105  OE1 GLU A 842    20449  24741  16640  -3840  -8141  -2176       O  
ATOM   2106  OE2 GLU A 842      19.845 199.633-176.706  1.00171.02           O1-
ANISOU 2106  OE2 GLU A 842    20616  26427  17938  -3351  -9118  -2061       O1-
ATOM   2107  N   LYS A 843      21.378 199.972-181.969  1.00157.82           N  
ANISOU 2107  N   LYS A 843    16376  24118  19469  -3965  -7735  -2130       N  
ATOM   2108  CA  LYS A 843      22.456 199.023-182.225  1.00163.20           C  
ANISOU 2108  CA  LYS A 843    16216  25137  20655  -3613  -8030  -2050       C  
ATOM   2109  C   LYS A 843      23.598 199.181-181.223  1.00174.76           C  
ANISOU 2109  C   LYS A 843    17249  27087  22065  -3662  -8658  -2415       C  
ATOM   2110  O   LYS A 843      24.138 198.194-180.722  1.00179.43           O  
ANISOU 2110  O   LYS A 843    17572  28070  22535  -3228  -9116  -2172       O  
ATOM   2111  CB  LYS A 843      22.988 199.179-183.653  1.00161.59           C  
ANISOU 2111  CB  LYS A 843    15275  24823  21300  -3821  -7533  -2121       C  
ATOM   2112  CG  LYS A 843      24.015 198.125-184.038  1.00166.05           C  
ANISOU 2112  CG  LYS A 843    14986  25758  22348  -3447  -7689  -1969       C  
ATOM   2113  CD  LYS A 843      24.517 198.306-185.461  1.00165.08           C  
ANISOU 2113  CD  LYS A 843    14179  25552  22991  -3692  -7090  -2003       C  
ATOM   2114  CE  LYS A 843      25.539 197.231-185.804  1.00170.93           C  
ANISOU 2114  CE  LYS A 843    14143  26577  24225  -3281  -7232  -1776       C  
ATOM   2115  NZ  LYS A 843      26.063 197.348-187.193  1.00171.52           N1+
ANISOU 2115  NZ  LYS A 843    13586  26508  25076  -3441  -6593  -1801       N1+
ATOM   2116  N   GLU A 844      23.966 200.424-180.935  1.00180.26           N  
ANISOU 2116  N   GLU A 844    17889  27746  22856  -4207  -8688  -2975       N  
ATOM   2117  CA  GLU A 844      25.053 200.693-180.000  1.00193.77           C  
ANISOU 2117  CA  GLU A 844    19165  29982  24475  -4366  -9248  -3364       C  
ATOM   2118  C   GLU A 844      24.577 201.532-178.820  1.00199.00           C  
ANISOU 2118  C   GLU A 844    20572  30543  24497  -4552  -9561  -3741       C  
ATOM   2119  O   GLU A 844      25.342 202.309-178.248  1.00208.15           O  
ANISOU 2119  O   GLU A 844    21486  31864  25739  -4905  -9830  -4247       O  
ATOM   2120  CB  GLU A 844      26.207 201.380-180.715  1.00199.56           C  
ANISOU 2120  CB  GLU A 844    19052  30847  25924  -4965  -8950  -3625       C  
ATOM   2121  N   GLY A 845      23.309 201.364-178.457  1.00192.67           N  
ANISOU 2121  N   GLY A 845    20739  29445  23021  -4340  -9406  -3400       N  
ATOM   2122  CA  GLY A 845      22.713 202.147-177.391  1.00194.29           C  
ANISOU 2122  CA  GLY A 845    21758  29550  22515  -4533  -9533  -3671       C  
ATOM   2123  C   GLY A 845      22.154 203.449-177.927  1.00189.00           C  
ANISOU 2123  C   GLY A 845    21457  28295  22060  -5098  -8960  -3955       C  
ATOM   2124  O   GLY A 845      21.443 204.170-177.228  1.00189.71           O  
ANISOU 2124  O   GLY A 845    22311  28203  21565  -5282  -8859  -4149       O  
ATOM   2125  N   LYS A 846      22.483 203.748-179.180  1.00183.95           N  
ANISOU 2125  N   LYS A 846    20284  27373  22237  -5374  -8532  -3956       N  
ATOM   2126  CA  LYS A 846      22.002 204.955-179.837  1.00179.70           C  
ANISOU 2126  CA  LYS A 846    20067  26290  21922  -5932  -7892  -4128       C  
ATOM   2127  C   LYS A 846      20.944 204.607-180.877  1.00168.99           C  
ANISOU 2127  C   LYS A 846    19017  24694  20495  -5810  -7207  -3623       C  
ATOM   2128  O   LYS A 846      20.971 203.526-181.467  1.00164.02           O  
ANISOU 2128  O   LYS A 846    18031  24245  20046  -5417  -7197  -3203       O  
ATOM   2129  CB  LYS A 846      23.157 205.707-180.481  1.00184.21           C  
ANISOU 2129  CB  LYS A 846    19877  26670  23442  -6432  -7842  -4480       C  
ATOM   2130  N   PHE A 847      20.010 205.525-181.096  1.00165.78           N  
ANISOU 2130  N   PHE A 847    19275  23876  19836  -6127  -6642  -3699       N  
ATOM   2131  CA  PHE A 847      18.935 205.297-182.051  1.00156.88           C  
ANISOU 2131  CA  PHE A 847    18478  22532  18599  -6025  -6021  -3290       C  
ATOM   2132  C   PHE A 847      19.209 205.934-183.408  1.00157.22           C  
ANISOU 2132  C   PHE A 847    18159  22248  19328  -6387  -5373  -3315       C  
ATOM   2133  O   PHE A 847      19.341 207.154-183.526  1.00162.08           O  
ANISOU 2133  O   PHE A 847    18946  22487  20149  -6897  -5044  -3673       O  
ATOM   2134  CB  PHE A 847      17.597 205.789-181.494  1.00152.32           C  
ANISOU 2134  CB  PHE A 847    18892  21702  17282  -6012  -5736  -3316       C  
ATOM   2135  CG  PHE A 847      16.872 204.763-180.670  1.00148.41           C  
ANISOU 2135  CG  PHE A 847    18813  21479  16097  -5481  -6018  -2982       C  
ATOM   2136  CD1 PHE A 847      16.164 203.741-181.281  1.00141.13           C  
ANISOU 2136  CD1 PHE A 847    17896  20584  15143  -5019  -5765  -2450       C  
ATOM   2137  CD2 PHE A 847      16.892 204.822-179.288  1.00152.28           C  
ANISOU 2137  CD2 PHE A 847    19692  22153  16015  -5378  -6432  -3190       C  
ATOM   2138  CE1 PHE A 847      15.495 202.797-180.529  1.00138.83           C  
ANISOU 2138  CE1 PHE A 847    18006  20501  14241  -4625  -5989  -2132       C  
ATOM   2139  CE2 PHE A 847      16.223 203.880-178.531  1.00149.82           C  
ANISOU 2139  CE2 PHE A 847    19801  22065  15060  -4918  -6594  -2842       C  
ATOM   2140  CZ  PHE A 847      15.525 202.867-179.151  1.00143.63           C  
ANISOU 2140  CZ  PHE A 847    19029  21285  14259  -4567  -6362  -2303       C  
ATOM   2141  N   VAL A 848      19.299 205.093-184.431  1.00153.40           N  
ANISOU 2141  N   VAL A 848    17225  21843  19219  -6023  -5105  -2913       N  
ATOM   2142  CA  VAL A 848      19.436 205.564-185.801  1.00154.01           C  
ANISOU 2142  CA  VAL A 848    17066  21588  19862  -6163  -4349  -2821       C  
ATOM   2143  C   VAL A 848      18.174 205.240-186.594  1.00143.47           C  
ANISOU 2143  C   VAL A 848    16242  20005  18265  -5666  -3747  -2376       C  
ATOM   2144  O   VAL A 848      17.743 204.087-186.655  1.00138.76           O  
ANISOU 2144  O   VAL A 848    15614  19638  17471  -5152  -3892  -2041       O  
ATOM   2145  CB  VAL A 848      20.676 204.957-186.498  1.00160.32           C  
ANISOU 2145  CB  VAL A 848    16862  22688  21364  -6197  -4444  -2798       C  
ATOM   2146  CG1 VAL A 848      20.576 205.107-188.013  1.00158.28           C  
ANISOU 2146  CG1 VAL A 848    16492  22144  21505  -6150  -3584  -2555       C  
ATOM   2147  CG2 VAL A 848      21.952 205.603-185.970  1.00169.65           C  
ANISOU 2147  CG2 VAL A 848    17442  24030  22986  -6825  -4871  -3314       C  
ATOM   2148  N   MET A 849      17.579 206.273-187.182  1.00140.96           N  
ANISOU 2148  N   MET A 849    16401  19200  17959  -5824  -3098  -2386       N  
ATOM   2149  CA  MET A 849      16.397 206.114-188.015  1.00134.30           C  
ANISOU 2149  CA  MET A 849    16002  18124  16902  -5372  -2547  -2001       C  
ATOM   2150  C   MET A 849      16.699 205.231-189.218  1.00133.40           C  
ANISOU 2150  C   MET A 849    15383  18185  17120  -5081  -2310  -1685       C  
ATOM   2151  O   MET A 849      17.675 205.454-189.930  1.00137.36           O  
ANISOU 2151  O   MET A 849    15381  18680  18127  -5364  -2090  -1754       O  
ATOM   2152  CB  MET A 849      15.890 207.483-188.481  1.00133.90           C  
ANISOU 2152  CB  MET A 849    16500  17493  16882  -5595  -1929  -2067       C  
ATOM   2153  CG  MET A 849      14.716 207.423-189.450  1.00127.60           C  
ANISOU 2153  CG  MET A 849    16112  16471  15900  -5112  -1394  -1671       C  
ATOM   2154  SD  MET A 849      14.126 209.053-189.953  1.00229.56           S  
ANISOU 2154  SD  MET A 849    29716  28655  28853  -5282   -724  -1692       S  
ATOM   2155  CE  MET A 849      15.609 209.749-190.680  1.00176.60           C  
ANISOU 2155  CE  MET A 849    22555  21745  22799  -5930   -421  -1824       C  
ATOM   2156  N   LEU A 850      15.865 204.218-189.430  1.00129.72           N  
ANISOU 2156  N   LEU A 850    15044  17869  16375  -4541  -2327  -1371       N  
ATOM   2157  CA  LEU A 850      15.995 203.370-190.607  1.00128.55           C  
ANISOU 2157  CA  LEU A 850    14524  17847  16472  -4231  -2067  -1112       C  
ATOM   2158  C   LEU A 850      15.042 203.817-191.717  1.00127.63           C  
ANISOU 2158  C   LEU A 850    14851  17429  16212  -4028  -1435   -887       C  
ATOM   2159  O   LEU A 850      13.862 204.091-191.473  1.00125.98           O  
ANISOU 2159  O   LEU A 850    15205  17047  15614  -3820  -1348   -800       O  
ATOM   2160  CB  LEU A 850      15.797 201.889-190.250  1.00123.99           C  
ANISOU 2160  CB  LEU A 850    13747  17601  15761  -3787  -2493   -936       C  
ATOM   2161  CG  LEU A 850      14.765 201.461-189.204  1.00119.06           C  
ANISOU 2161  CG  LEU A 850    13615  17017  14605  -3543  -2806   -841       C  
ATOM   2162  CD1 LEU A 850      13.371 201.488-189.778  1.00114.65           C  
ANISOU 2162  CD1 LEU A 850    13540  16258  13763  -3241  -2369   -640       C  
ATOM   2163  CD2 LEU A 850      15.088 200.071-188.676  1.00117.22           C  
ANISOU 2163  CD2 LEU A 850    13071  17091  14376  -3253  -3320   -700       C  
ATOM   2164  N   GLN A 851      15.574 203.909-192.932  1.00127.00           N  
ANISOU 2164  N   GLN A 851    14508  17306  16440  -4080   -995   -798       N  
ATOM   2165  CA  GLN A 851      14.790 204.344-194.078  1.00121.29           C  
ANISOU 2165  CA  GLN A 851    14210  16332  15543  -3874   -431   -557       C  
ATOM   2166  C   GLN A 851      14.491 203.188-195.018  1.00113.07           C  
ANISOU 2166  C   GLN A 851    12984  15541  14435  -3421   -342   -355       C  
ATOM   2167  O   GLN A 851      15.190 202.176-195.032  1.00107.32           O  
ANISOU 2167  O   GLN A 851    11718  15111  13948  -3342   -558   -410       O  
ATOM   2168  CB  GLN A 851      15.490 205.473-194.840  1.00125.21           C  
ANISOU 2168  CB  GLN A 851    14736  16519  16320  -4287    110   -572       C  
ATOM   2169  CG  GLN A 851      16.901 205.151-195.290  1.00128.33           C  
ANISOU 2169  CG  GLN A 851    14409  17130  17220  -4581    222   -690       C  
ATOM   2170  CD  GLN A 851      17.917 205.366-194.190  1.00131.80           C  
ANISOU 2170  CD  GLN A 851    14382  17676  18022  -5051   -211  -1045       C  
ATOM   2171  OE1 GLN A 851      17.557 205.660-193.051  1.00132.31           O  
ANISOU 2171  OE1 GLN A 851    14711  17682  17880  -5136   -637  -1207       O  
ATOM   2172  NE2 GLN A 851      19.193 205.225-194.524  1.00135.56           N  
ANISOU 2172  NE2 GLN A 851    14143  18334  19030  -5356   -108  -1196       N  
ATOM   2173  N   GLU A 852      13.443 203.363-195.812  1.00112.71           N  
ANISOU 2173  N   GLU A 852    13392  15360  14072  -3107    -38   -142       N  
ATOM   2174  CA  GLU A 852      12.918 202.293-196.641  1.00111.01           C  
ANISOU 2174  CA  GLU A 852    13101  15371  13706  -2668     -8     -5       C  
ATOM   2175  C   GLU A 852      13.917 201.799-197.675  1.00113.02           C  
ANISOU 2175  C   GLU A 852    12922  15798  14223  -2701    275    -16       C  
ATOM   2176  O   GLU A 852      13.892 200.631-198.048  1.00114.86           O  
ANISOU 2176  O   GLU A 852    12893  16272  14476  -2410    168    -31       O  
ATOM   2177  CB  GLU A 852      11.615 202.738-197.295  1.00110.13           C  
ANISOU 2177  CB  GLU A 852    13546  15101  13198  -2348    216    192       C  
ATOM   2178  CG  GLU A 852      10.571 203.121-196.265  1.00110.62           C  
ANISOU 2178  CG  GLU A 852    13965  15022  13043  -2260    -20    169       C  
ATOM   2179  CD  GLU A 852       9.255 203.527-196.879  1.00112.06           C  
ANISOU 2179  CD  GLU A 852    14594  15082  12902  -1885    151    345       C  
ATOM   2180  OE1 GLU A 852       9.184 203.616-198.122  1.00111.37           O  
ANISOU 2180  OE1 GLU A 852    14609  15005  12700  -1709    425    507       O  
ATOM   2181  OE2 GLU A 852       8.294 203.756-196.110  1.00112.63           O1-
ANISOU 2181  OE2 GLU A 852    14905  15070  12820  -1749      7    313       O1-
ATOM   2182  N   VAL A 853      14.795 202.689-198.127  1.00115.08           N  
ANISOU 2182  N   VAL A 853    13113  15907  14706  -3071    680    -31       N  
ATOM   2183  CA  VAL A 853      15.853 202.342-199.073  1.00117.92           C  
ANISOU 2183  CA  VAL A 853    13024  16429  15352  -3168   1057    -70       C  
ATOM   2184  C   VAL A 853      17.047 203.270-198.867  1.00124.51           C  
ANISOU 2184  C   VAL A 853    13561  17117  16630  -3751   1304   -202       C  
ATOM   2185  O   VAL A 853      16.887 204.489-198.863  1.00129.00           O  
ANISOU 2185  O   VAL A 853    14562  17323  17128  -4040   1577   -122       O  
ATOM   2186  CB  VAL A 853      15.381 202.479-200.540  1.00117.89           C  
ANISOU 2186  CB  VAL A 853    13422  16386  14986  -2929   1596    153       C  
ATOM   2187  CG1 VAL A 853      16.574 202.527-201.475  1.00122.78           C  
ANISOU 2187  CG1 VAL A 853    13680  17090  15883  -3168   2163    114       C  
ATOM   2188  CG2 VAL A 853      14.442 201.344-200.934  1.00113.07           C  
ANISOU 2188  CG2 VAL A 853    12912  16007  14041  -2395   1362    183       C  
ATOM   2189  N   ASP A 854      18.241 202.704-198.698  1.00127.09           N  
ANISOU 2189  N   ASP A 854    13129  17701  17457  -3926   1211   -419       N  
ATOM   2190  CA  ASP A 854      19.441 203.521-198.502  1.00134.07           C  
ANISOU 2190  CA  ASP A 854    13588  18498  18856  -4528   1425   -605       C  
ATOM   2191  C   ASP A 854      20.536 203.280-199.545  1.00137.19           C  
ANISOU 2191  C   ASP A 854    13415  19063  19649  -4669   2011   -661       C  
ATOM   2192  O   ASP A 854      20.317 202.606-200.553  1.00133.49           O  
ANISOU 2192  O   ASP A 854    13018  18737  18963  -4297   2338   -536       O  
ATOM   2193  CB  ASP A 854      20.006 203.337-197.087  1.00137.33           C  
ANISOU 2193  CB  ASP A 854    13509  19072  19598  -4733    711   -892       C  
ATOM   2194  CG  ASP A 854      20.257 201.878-196.734  1.00136.04           C  
ANISOU 2194  CG  ASP A 854    12801  19315  19573  -4307    189   -964       C  
ATOM   2195  OD1 ASP A 854      20.418 201.048-197.653  1.00135.10           O  
ANISOU 2195  OD1 ASP A 854    12443  19363  19526  -3988    477   -902       O  
ATOM   2196  OD2 ASP A 854      20.298 201.562-195.527  1.00136.24           O1-
ANISOU 2196  OD2 ASP A 854    12679  19470  19616  -4280   -505  -1081       O1-
ATOM   2197  N   ASP A 855      21.717 203.836-199.288  1.00145.08           N  
ANISOU 2197  N   ASP A 855    13830  20057  21235  -5229   2154   -889       N  
ATOM   2198  CA  ASP A 855      22.861 203.667-200.181  1.00152.46           C  
ANISOU 2198  CA  ASP A 855    14111  21169  22649  -5434   2766   -990       C  
ATOM   2199  C   ASP A 855      23.392 202.237-200.139  1.00153.60           C  
ANISOU 2199  C   ASP A 855    13490  21776  23097  -5006   2434  -1168       C  
ATOM   2200  O   ASP A 855      24.116 201.807-201.038  1.00157.03           O  
ANISOU 2200  O   ASP A 855    13449  22401  23816  -4962   2974  -1239       O  
ATOM   2201  CB  ASP A 855      23.965 204.659-199.829  1.00158.66           C  
ANISOU 2201  CB  ASP A 855    14393  21823  24068  -6199   2978  -1231       C  
ATOM   2202  N   THR A 856      23.028 201.507-199.088  1.00150.67           N  
ANISOU 2202  N   THR A 856    13035  21555  22660  -4679   1581  -1233       N  
ATOM   2203  CA  THR A 856      23.419 200.110-198.949  1.00150.83           C  
ANISOU 2203  CA  THR A 856    12436  21923  22948  -4200   1193  -1351       C  
ATOM   2204  C   THR A 856      22.261 199.199-199.339  1.00144.55           C  
ANISOU 2204  C   THR A 856    12233  21104  21585  -3584   1106  -1142       C  
ATOM   2205  O   THR A 856      21.777 198.411-198.526  1.00140.39           O  
ANISOU 2205  O   THR A 856    11770  20639  20934  -3234    440  -1111       O  
ATOM   2206  CB  THR A 856      23.842 199.781-197.506  1.00151.53           C  
ANISOU 2206  CB  THR A 856    12039  22195  23342  -4210    270  -1527       C  
ATOM   2207  OG1 THR A 856      24.537 200.898-196.942  1.00157.20           O  
ANISOU 2207  OG1 THR A 856    12477  22855  24395  -4867    218  -1732       O  
ATOM   2208  CG2 THR A 856      24.745 198.550-197.479  1.00154.28           C  
ANISOU 2208  CG2 THR A 856    11489  22888  24243  -3831      3  -1688       C  
ATOM   2209  N   SER A 857      21.810 199.323-200.582  1.00143.62           N  
ANISOU 2209  N   SER A 857    12569  20895  21107  -3476   1780   -999       N  
ATOM   2210  CA  SER A 857      20.731 198.486-201.091  1.00138.70           C  
ANISOU 2210  CA  SER A 857    12465  20273  19963  -2938   1728   -865       C  
ATOM   2211  C   SER A 857      21.097 197.930-202.458  1.00141.96           C  
ANISOU 2211  C   SER A 857    12737  20828  20372  -2730   2388   -939       C  
ATOM   2212  O   SER A 857      21.334 198.687-203.400  1.00143.77           O  
ANISOU 2212  O   SER A 857    13166  21001  20457  -2982   3100   -864       O  
ATOM   2213  CB  SER A 857      19.421 199.273-201.173  1.00134.11           C  
ANISOU 2213  CB  SER A 857    12808  19432  18713  -2942   1753   -604       C  
ATOM   2214  OG  SER A 857      18.962 199.644-199.885  1.00131.20           O  
ANISOU 2214  OG  SER A 857    12617  18939  18292  -3057   1154   -574       O  
ATOM   2215  N   GLU A 858      21.144 196.605-202.556  1.00145.35           N  
ANISOU 2215  N   GLU A 858    12867  21415  20944  -2270   2176  -1086       N  
ATOM   2216  CA  GLU A 858      21.516 195.935-203.797  1.00153.84           C  
ANISOU 2216  CA  GLU A 858    13788  22636  22029  -2025   2776  -1243       C  
ATOM   2217  C   GLU A 858      20.602 196.334-204.952  1.00151.57           C  
ANISOU 2217  C   GLU A 858    14333  22282  20974  -1959   3268  -1078       C  
ATOM   2218  O   GLU A 858      19.454 196.723-204.741  1.00146.97           O  
ANISOU 2218  O   GLU A 858    14419  21550  19871  -1910   2974   -861       O  
ATOM   2219  CB  GLU A 858      21.490 194.417-203.612  1.00158.19           C  
ANISOU 2219  CB  GLU A 858    14028  23261  22815  -1496   2383  -1429       C  
ATOM   2220  CG  GLU A 858      20.115 193.863-203.287  1.00156.53           C  
ANISOU 2220  CG  GLU A 858    14456  22906  22114  -1185   1868  -1299       C  
ATOM   2221  CD  GLU A 858      20.084 192.350-203.275  1.00161.58           C  
ANISOU 2221  CD  GLU A 858    14867  23533  22995   -694   1609  -1488       C  
ATOM   2222  OE1 GLU A 858      21.159 191.733-203.123  1.00167.42           O  
ANISOU 2222  OE1 GLU A 858    14890  24354  24367   -551   1609  -1677       O  
ATOM   2223  OE2 GLU A 858      18.983 191.777-203.422  1.00160.29           O1-
ANISOU 2223  OE2 GLU A 858    15220  23256  22427   -449   1410  -1460       O1-
ATOM   2224  N   ILE A 859      21.122 196.242-206.171  1.00154.27           N  
ANISOU 2224  N   ILE A 859    14625  22759  21234  -1937   4019  -1187       N  
ATOM   2225  CA  ILE A 859      20.359 196.603-207.361  1.00151.20           C  
ANISOU 2225  CA  ILE A 859    15039  22361  20048  -1847   4494  -1028       C  
ATOM   2226  C   ILE A 859      20.473 195.533-208.438  1.00152.69           C  
ANISOU 2226  C   ILE A 859    15201  22759  20056  -1462   4868  -1308       C  
ATOM   2227  O   ILE A 859      21.571 195.199-208.879  1.00159.66           O  
ANISOU 2227  O   ILE A 859    15512  23792  21360  -1497   5398  -1549       O  
ATOM   2228  CB  ILE A 859      20.828 197.945-207.945  1.00154.47           C  
ANISOU 2228  CB  ILE A 859    15692  22685  20316  -2316   5224   -797       C  
ATOM   2229  CG1 ILE A 859      20.609 199.074-206.936  1.00152.50           C  
ANISOU 2229  CG1 ILE A 859    15593  22155  20195  -2704   4878   -555       C  
ATOM   2230  CG2 ILE A 859      20.098 198.242-209.244  1.00155.04           C  
ANISOU 2230  CG2 ILE A 859    16632  22780  19497  -2148   5707   -598       C  
ATOM   2231  CD1 ILE A 859      21.046 200.431-207.438  1.00158.05           C  
ANISOU 2231  CD1 ILE A 859    16577  22655  20821  -3206   5595   -311       C  
ATOM   2232  N   ARG A 860      19.330 195.001-208.858  1.00147.82           N  
ANISOU 2232  N   ARG A 860    15180  22154  18830  -1101   4599  -1317       N  
ATOM   2233  CA  ARG A 860      19.295 193.966-209.884  1.00150.01           C  
ANISOU 2233  CA  ARG A 860    15537  22608  18853   -736   4891  -1643       C  
ATOM   2234  C   ARG A 860      18.956 194.554-211.251  1.00152.69           C  
ANISOU 2234  C   ARG A 860    16605  23083  18329   -745   5515  -1525       C  
ATOM   2235  O   ARG A 860      17.791 194.624-211.639  1.00146.92           O  
ANISOU 2235  O   ARG A 860    16564  22368  16889   -554   5233  -1411       O  
ATOM   2236  CB  ARG A 860      18.299 192.881-209.508  1.00144.29           C  
ANISOU 2236  CB  ARG A 860    14960  21816  18048   -356   4187  -1808       C  
ATOM   2237  N   GLY A 861      19.985 194.971-211.978  1.00162.69           N  
ANISOU 2237  N   GLY A 861    17702  24461  19651   -965   6365  -1546       N  
ATOM   2238  CA  GLY A 861      19.798 195.577-213.282  1.00169.56           C  
ANISOU 2238  CA  GLY A 861    19305  25459  19661   -996   7046  -1378       C  
ATOM   2239  C   GLY A 861      19.585 197.075-213.188  1.00170.82           C  
ANISOU 2239  C   GLY A 861    19954  25417  19535  -1365   7207   -839       C  
ATOM   2240  O   GLY A 861      20.524 197.857-213.340  1.00177.64           O  
ANISOU 2240  O   GLY A 861    20620  26213  20662  -1779   7892   -689       O  
ATOM   2241  N   HIS A 862      18.344 197.476-212.935  1.00163.50           N  
ANISOU 2241  N   HIS A 862    19646  24363  18113  -1218   6597   -561       N  
ATOM   2242  CA  HIS A 862      18.009 198.889-212.825  1.00161.90           C  
ANISOU 2242  CA  HIS A 862    19985  23896  17634  -1486   6692    -44       C  
ATOM   2243  C   HIS A 862      16.960 199.120-211.746  1.00152.89           C  
ANISOU 2243  C   HIS A 862    18969  22544  16579  -1388   5802    106       C  
ATOM   2244  O   HIS A 862      16.346 200.184-211.680  1.00152.20           O  
ANISOU 2244  O   HIS A 862    19452  22222  16156  -1456   5736    509       O  
ATOM   2245  CB  HIS A 862      17.522 199.422-214.164  1.00166.96           C  
ANISOU 2245  CB  HIS A 862    21561  24630  17246  -1330   7164    253       C  
ATOM   2246  N   VAL A 863      16.761 198.114-210.899  1.00146.15           N  
ANISOU 2246  N   VAL A 863    17598  21751  16183  -1214   5158   -213       N  
ATOM   2247  CA  VAL A 863      15.753 198.176-209.844  1.00135.37           C  
ANISOU 2247  CA  VAL A 863    16314  20224  14897  -1111   4354   -119       C  
ATOM   2248  C   VAL A 863      16.386 197.959-208.471  1.00131.23           C  
ANISOU 2248  C   VAL A 863    15067  19574  15220  -1345   3999   -256       C  
ATOM   2249  O   VAL A 863      17.172 197.034-208.284  1.00133.10           O  
ANISOU 2249  O   VAL A 863    14672  19938  15962  -1309   4005   -566       O  
ATOM   2250  CB  VAL A 863      14.657 197.119-210.068  1.00128.42           C  
ANISOU 2250  CB  VAL A 863    15613  19525  13657   -659   3824   -339       C  
ATOM   2251  CG1 VAL A 863      13.480 197.376-209.149  1.00123.07           C  
ANISOU 2251  CG1 VAL A 863    15126  18693  12944   -566   3128   -180       C  
ATOM   2252  CG2 VAL A 863      14.209 197.116-211.524  1.00131.30           C  
ANISOU 2252  CG2 VAL A 863    16599  20117  13172   -404   4149   -320       C  
ATOM   2253  N   THR A 864      16.041 198.812-207.513  1.00128.30           N  
ANISOU 2253  N   THR A 864    14811  18954  14983  -1551   3673    -34       N  
ATOM   2254  CA  THR A 864      16.628 198.738-206.177  1.00129.28           C  
ANISOU 2254  CA  THR A 864    14336  18982  15804  -1796   3297   -150       C  
ATOM   2255  C   THR A 864      15.772 197.882-205.239  1.00119.65           C  
ANISOU 2255  C   THR A 864    13043  17775  14641  -1515   2532   -252       C  
ATOM   2256  O   THR A 864      14.551 197.848-205.373  1.00117.50           O  
ANISOU 2256  O   THR A 864    13257  17484  13902  -1260   2269   -151       O  
ATOM   2257  CB  THR A 864      16.817 200.149-205.569  1.00136.66           C  
ANISOU 2257  CB  THR A 864    15436  19616  16872  -2233   3390     82       C  
ATOM   2258  OG1 THR A 864      17.366 201.031-206.557  1.00145.02           O  
ANISOU 2258  OG1 THR A 864    16755  20584  17764  -2490   4160    263       O  
ATOM   2259  CG2 THR A 864      17.751 200.102-204.370  1.00138.97           C  
ANISOU 2259  CG2 THR A 864    15027  19887  17889  -2560   3101   -110       C  
ATOM   2260  N   MET A 865      16.414 197.194-204.295  1.00115.12           N  
ANISOU 2260  N   MET A 865    11855  17239  14646  -1559   2184   -439       N  
ATOM   2261  CA  MET A 865      15.709 196.319-203.357  1.00107.29           C  
ANISOU 2261  CA  MET A 865    10805  16230  13732  -1321   1519   -498       C  
ATOM   2262  C   MET A 865      15.344 197.016-202.048  1.00102.80           C  
ANISOU 2262  C   MET A 865    10349  15492  13217  -1531   1083   -350       C  
ATOM   2263  O   MET A 865      16.177 197.698-201.449  1.00106.67           O  
ANISOU 2263  O   MET A 865    10572  15925  14034  -1877   1099   -351       O  
ATOM   2264  CB  MET A 865      16.554 195.085-203.038  1.00108.56           C  
ANISOU 2264  CB  MET A 865    10315  16494  14439  -1167   1341   -740       C  
ATOM   2265  CG  MET A 865      15.803 194.027-202.249  1.00104.77           C  
ANISOU 2265  CG  MET A 865     9860  15947  14000   -888    747   -767       C  
ATOM   2266  SD  MET A 865      16.902 192.973-201.299  1.00147.58           S  
ANISOU 2266  SD  MET A 865    14549  21381  20145   -772    361   -900       S  
ATOM   2267  CE  MET A 865      17.834 194.210-200.397  1.00 89.70           C  
ANISOU 2267  CE  MET A 865     6902  14088  13092  -1231    264   -809       C  
ATOM   2268  N   LEU A 866      14.106 196.820-201.599  1.00 95.14           N  
ANISOU 2268  N   LEU A 866     9752  14455  11941  -1338    706   -266       N  
ATOM   2269  CA  LEU A 866      13.630 197.433-200.361  1.00 91.43           C  
ANISOU 2269  CA  LEU A 866     9458  13836  11447  -1496    337   -155       C  
ATOM   2270  C   LEU A 866      14.359 196.898-199.134  1.00 91.87           C  
ANISOU 2270  C   LEU A 866     9056  13924  11928  -1599    -94   -246       C  
ATOM   2271  O   LEU A 866      14.686 195.715-199.050  1.00 89.73           O  
ANISOU 2271  O   LEU A 866     8438  13750  11907  -1387   -288   -345       O  
ATOM   2272  CB  LEU A 866      12.122 197.228-200.192  1.00 89.55           C  
ANISOU 2272  CB  LEU A 866     9648  13555  10823  -1242     88    -72       C  
ATOM   2273  CG  LEU A 866      11.163 197.826-201.225  1.00 89.61           C  
ANISOU 2273  CG  LEU A 866    10145  13549  10355  -1072    344     44       C  
ATOM   2274  CD1 LEU A 866       9.719 197.498-200.869  1.00 84.42           C  
ANISOU 2274  CD1 LEU A 866     9726  12893   9456   -832     20     65       C  
ATOM   2275  CD2 LEU A 866      11.352 199.328-201.348  1.00 93.06           C  
ANISOU 2275  CD2 LEU A 866    10899  13790  10669  -1302    651    223       C  
ATOM   2276  N   ASN A 867      14.606 197.786-198.179  1.00 97.69           N  
ANISOU 2276  N   ASN A 867     9827  14563  12728  -1909   -263   -216       N  
ATOM   2277  CA  ASN A 867      15.273 197.417-196.940  1.00104.49           C  
ANISOU 2277  CA  ASN A 867    10318  15493  13893  -2015   -750   -293       C  
ATOM   2278  C   ASN A 867      14.303 196.784-195.962  1.00105.17           C  
ANISOU 2278  C   ASN A 867    10676  15546  13736  -1810  -1204   -201       C  
ATOM   2279  O   ASN A 867      13.264 197.364-195.640  1.00106.85           O  
ANISOU 2279  O   ASN A 867    11375  15636  13585  -1831  -1201   -116       O  
ATOM   2280  CB  ASN A 867      15.928 198.638-196.289  1.00108.27           C  
ANISOU 2280  CB  ASN A 867    10746  15893  14497  -2472   -775   -363       C  
ATOM   2281  CG  ASN A 867      17.092 199.172-197.093  1.00114.35           C  
ANISOU 2281  CG  ASN A 867    11115  16696  15638  -2759   -327   -470       C  
ATOM   2282  OD1 ASN A 867      17.599 198.503-197.996  1.00115.81           O  
ANISOU 2282  OD1 ASN A 867    10956  17019  16028  -2590    -48   -515       O  
ATOM   2283  ND2 ASN A 867      17.532 200.381-196.762  1.00118.40           N  
ANISOU 2283  ND2 ASN A 867    11671  17061  16256  -3219   -213   -539       N  
ATOM   2284  N   THR A 868      14.649 195.593-195.490  1.00103.50           N  
ANISOU 2284  N   THR A 868    10153  15423  13749  -1600  -1557   -207       N  
ATOM   2285  CA  THR A 868      13.828 194.883-194.526  1.00101.08           C  
ANISOU 2285  CA  THR A 868    10106  15061  13237  -1429  -1946    -80       C  
ATOM   2286  C   THR A 868      14.410 195.036-193.137  1.00102.06           C  
ANISOU 2286  C   THR A 868    10138  15249  13393  -1589  -2438    -57       C  
ATOM   2287  O   THR A 868      15.174 195.962-192.869  1.00105.97           O  
ANISOU 2287  O   THR A 868    10467  15805  13990  -1897  -2477   -176       O  
ATOM   2288  CB  THR A 868      13.785 193.394-194.841  1.00105.98           C  
ANISOU 2288  CB  THR A 868    10539  15664  14063  -1074  -2033    -58       C  
ATOM   2289  OG1 THR A 868      15.121 192.876-194.837  1.00112.44           O  
ANISOU 2289  OG1 THR A 868    10785  16580  15355   -998  -2184   -139       O  
ATOM   2290  CG2 THR A 868      13.166 193.162-196.203  1.00106.73           C  
ANISOU 2290  CG2 THR A 868    10754  15730  14068   -918  -1604   -142       C  
ATOM   2291  N   LEU A 869      14.050 194.113-192.255  1.00101.14           N  
ANISOU 2291  N   LEU A 869    10147  15109  13172  -1393  -2817     93       N  
ATOM   2292  CA  LEU A 869      14.597 194.101-190.909  1.00106.39           C  
ANISOU 2292  CA  LEU A 869    10777  15872  13776  -1477  -3358    149       C  
ATOM   2293  C   LEU A 869      15.852 193.233-190.836  1.00115.44           C  
ANISOU 2293  C   LEU A 869    11325  17139  15397  -1276  -3709    145       C  
ATOM   2294  O   LEU A 869      16.781 193.538-190.085  1.00118.66           O  
ANISOU 2294  O   LEU A 869    11448  17725  15914  -1408  -4136     79       O  
ATOM   2295  CB  LEU A 869      13.545 193.629-189.904  1.00103.10           C  
ANISOU 2295  CB  LEU A 869    10891  15362  12922  -1377  -3558    364       C  
ATOM   2296  CG  LEU A 869      12.424 194.630-189.624  1.00 98.67           C  
ANISOU 2296  CG  LEU A 869    10866  14726  11900  -1587  -3300    331       C  
ATOM   2297  CD1 LEU A 869      11.497 194.119-188.523  1.00 99.24           C  
ANISOU 2297  CD1 LEU A 869    11407  14740  11558  -1512  -3460    533       C  
ATOM   2298  CD2 LEU A 869      13.009 195.988-189.264  1.00 99.79           C  
ANISOU 2298  CD2 LEU A 869    11011  14937  11967  -1943  -3352    124       C  
ATOM   2299  N   LYS A 870      15.881 192.160-191.624  1.00118.65           N  
ANISOU 2299  N   LYS A 870    11522  17453  16106   -944  -3546    183       N  
ATOM   2300  CA  LYS A 870      17.066 191.310-191.704  1.00126.59           C  
ANISOU 2300  CA  LYS A 870    11915  18536  17648   -675  -3802    155       C  
ATOM   2301  C   LYS A 870      18.169 192.060-192.437  1.00132.76           C  
ANISOU 2301  C   LYS A 870    12100  19511  18831   -886  -3559   -121       C  
ATOM   2302  O   LYS A 870      19.356 191.775-192.277  1.00140.34           O  
ANISOU 2302  O   LYS A 870    12423  20634  20264   -785  -3835   -209       O  
ATOM   2303  CB  LYS A 870      16.750 189.994-192.414  1.00123.96           C  
ANISOU 2303  CB  LYS A 870    11567  17985  17546   -271  -3611    210       C  
ATOM   2304  CG  LYS A 870      17.860 188.952-192.315  1.00127.61           C  
ANISOU 2304  CG  LYS A 870    11470  18446  18572    117  -3927    226       C  
ATOM   2305  CD  LYS A 870      17.301 187.539-192.427  1.00124.03           C  
ANISOU 2305  CD  LYS A 870    11253  17648  18224    518  -3923    385       C  
ATOM   2306  CE  LYS A 870      16.484 187.359-193.695  1.00115.18           C  
ANISOU 2306  CE  LYS A 870    10337  16375  17051    503  -3311    191       C  
ATOM   2307  NZ  LYS A 870      15.816 186.034-193.721  1.00112.62           N1+
ANISOU 2307  NZ  LYS A 870    10300  15670  16820    799  -3313    305       N1+
ATOM   2308  N   HIS A 871      17.751 193.027-193.245  1.00129.01           N  
ANISOU 2308  N   HIS A 871    11832  19010  18176  -1172  -3024   -240       N  
ATOM   2309  CA  HIS A 871      18.665 193.916-193.940  1.00126.57           C  
ANISOU 2309  CA  HIS A 871    11086  18831  18174  -1472  -2673   -463       C  
ATOM   2310  C   HIS A 871      19.415 194.753-192.917  1.00123.32           C  
ANISOU 2310  C   HIS A 871    10439  18573  17843  -1832  -3096   -561       C  
ATOM   2311  O   HIS A 871      20.593 195.047-193.089  1.00128.98           O  
ANISOU 2311  O   HIS A 871    10497  19464  19045  -2010  -3085   -760       O  
ATOM   2312  CB  HIS A 871      17.883 194.824-194.887  1.00124.90           C  
ANISOU 2312  CB  HIS A 871    11333  18494  17629  -1684  -2053   -479       C  
ATOM   2313  CG  HIS A 871      18.748 195.665-195.769  1.00129.98           C  
ANISOU 2313  CG  HIS A 871    11623  19206  18558  -1988  -1551   -650       C  
ATOM   2314  ND1 HIS A 871      19.078 195.297-197.054  1.00133.30           N  
ANISOU 2314  ND1 HIS A 871    11811  19664  19171  -1841  -1014   -734       N  
ATOM   2315  CD2 HIS A 871      19.348 196.860-195.552  1.00133.08           C  
ANISOU 2315  CD2 HIS A 871    11882  19613  19069  -2461  -1457   -761       C  
ATOM   2316  CE1 HIS A 871      19.848 196.228-197.592  1.00137.37           C  
ANISOU 2316  CE1 HIS A 871    12067  20226  19902  -2211   -574   -849       C  
ATOM   2317  NE2 HIS A 871      20.027 197.186-196.701  1.00137.40           N  
ANISOU 2317  NE2 HIS A 871    12112  20194  19900  -2607   -835   -869       N  
ATOM   2318  N   TYR A 872      18.722 195.125-191.845  1.00119.50           N  
ANISOU 2318  N   TYR A 872    10480  18038  16885  -1952  -3457   -456       N  
ATOM   2319  CA  TYR A 872      19.314 195.931-190.785  1.00125.74           C  
ANISOU 2319  CA  TYR A 872    11162  18973  17641  -2310  -3912   -597       C  
ATOM   2320  C   TYR A 872      19.840 195.069-189.639  1.00130.10           C  
ANISOU 2320  C   TYR A 872    11481  19721  18231  -2052  -4708   -501       C  
ATOM   2321  O   TYR A 872      20.275 195.595-188.610  1.00130.67           O  
ANISOU 2321  O   TYR A 872    11515  19962  18171  -2297  -5227   -617       O  
ATOM   2322  CB  TYR A 872      18.299 196.944-190.250  1.00122.81           C  
ANISOU 2322  CB  TYR A 872    11539  18435  16688  -2599  -3820   -590       C  
ATOM   2323  CG  TYR A 872      18.188 198.201-191.082  1.00121.72           C  
ANISOU 2323  CG  TYR A 872    11539  18121  16588  -2978  -3202   -737       C  
ATOM   2324  CD1 TYR A 872      17.436 198.220-192.253  1.00119.05           C  
ANISOU 2324  CD1 TYR A 872    11479  17601  16153  -2829  -2587   -615       C  
ATOM   2325  CD2 TYR A 872      18.833 199.370-190.694  1.00125.36           C  
ANISOU 2325  CD2 TYR A 872    11883  18576  17172  -3488  -3251   -995       C  
ATOM   2326  CE1 TYR A 872      17.334 199.367-193.016  1.00120.66           C  
ANISOU 2326  CE1 TYR A 872    11881  17614  16349  -3128  -2034   -678       C  
ATOM   2327  CE2 TYR A 872      18.739 200.522-191.449  1.00127.32           C  
ANISOU 2327  CE2 TYR A 872    12321  18578  17477  -3837  -2649  -1083       C  
ATOM   2328  CZ  TYR A 872      17.986 200.515-192.610  1.00125.48           C  
ANISOU 2328  CZ  TYR A 872    12408  18157  17112  -3630  -2038   -889       C  
ATOM   2329  OH  TYR A 872      17.881 201.657-193.372  1.00127.41           O  
ANISOU 2329  OH  TYR A 872    12914  18128  17369  -3927  -1447   -906       O  
ATOM   2330  N   GLN A 873      19.796 193.751-189.828  1.00132.29           N  
ANISOU 2330  N   GLN A 873    11638  19954  18670  -1548  -4813   -295       N  
ATOM   2331  CA  GLN A 873      20.202 192.788-188.803  1.00138.11           C  
ANISOU 2331  CA  GLN A 873    12253  20804  19421  -1192  -5550   -101       C  
ATOM   2332  C   GLN A 873      19.447 192.991-187.490  1.00138.29           C  
ANISOU 2332  C   GLN A 873    12994  20820  18730  -1283  -5977     81       C  
ATOM   2333  O   GLN A 873      20.050 193.047-186.416  1.00143.73           O  
ANISOU 2333  O   GLN A 873    13580  21741  19289  -1304  -6664     82       O  
ATOM   2334  CB  GLN A 873      21.713 192.842-188.571  1.00146.10           C  
ANISOU 2334  CB  GLN A 873    12374  22135  21000  -1208  -6019   -310       C  
ATOM   2335  N   VAL A 874      18.127 193.106-187.584  1.00132.60           N  
ANISOU 2335  N   VAL A 874    12988  19862  17534  -1331  -5566    215       N  
ATOM   2336  CA  VAL A 874      17.295 193.290-186.404  1.00132.62           C  
ANISOU 2336  CA  VAL A 874    13707  19842  16840  -1417  -5819    376       C  
ATOM   2337  C   VAL A 874      17.035 191.952-185.728  1.00133.61           C  
ANISOU 2337  C   VAL A 874    14089  19879  16798   -981  -6183    776       C  
ATOM   2338  O   VAL A 874      16.596 191.000-186.372  1.00131.96           O  
ANISOU 2338  O   VAL A 874    13902  19429  16810   -682  -5889    954       O  
ATOM   2339  CB  VAL A 874      15.951 193.950-186.758  1.00127.61           C  
ANISOU 2339  CB  VAL A 874    13673  18993  15821  -1618  -5202    350       C  
ATOM   2340  CG1 VAL A 874      15.030 193.960-185.548  1.00128.06           C  
ANISOU 2340  CG1 VAL A 874    14450  19019  15186  -1649  -5374    527       C  
ATOM   2341  CG2 VAL A 874      16.173 195.364-187.277  1.00126.72           C  
ANISOU 2341  CG2 VAL A 874    13445  18897  15806  -2044  -4868     12       C  
ATOM   2342  N   GLY A 875      17.314 191.883-184.431  1.00137.74           N  
ANISOU 2342  N   GLY A 875    14844  20580  16913   -956  -6825    913       N  
ATOM   2343  CA  GLY A 875      17.113 190.661-183.677  1.00141.02           C  
ANISOU 2343  CA  GLY A 875    15595  20886  17099   -546  -7196   1362       C  
ATOM   2344  C   GLY A 875      15.890 190.732-182.786  1.00139.07           C  
ANISOU 2344  C   GLY A 875    16246  20528  16065   -667  -7056   1587       C  
ATOM   2345  O   GLY A 875      15.248 191.778-182.686  1.00134.79           O  
ANISOU 2345  O   GLY A 875    16029  20026  15159  -1044  -6729   1354       O  
ATOM   2346  N   ASP A 876      15.567 189.614-182.141  1.00141.70           N  
ANISOU 2346  N   ASP A 876    16990  20693  16157   -339  -7259   2048       N  
ATOM   2347  CA  ASP A 876      14.428 189.552-181.230  1.00141.55           C  
ANISOU 2347  CA  ASP A 876    17828  20568  15387   -446  -7077   2309       C  
ATOM   2348  C   ASP A 876      14.629 190.467-180.026  1.00145.69           C  
ANISOU 2348  C   ASP A 876    18716  21425  15215   -680  -7418   2148       C  
ATOM   2349  O   ASP A 876      15.757 190.686-179.580  1.00150.74           O  
ANISOU 2349  O   ASP A 876    19006  22338  15931   -580  -7880   1959       O  
ATOM   2350  CB  ASP A 876      14.194 188.115-180.761  1.00146.82           C  
ANISOU 2350  CB  ASP A 876    18860  20946  15977    -49  -7219   2875       C  
ATOM   2351  CG  ASP A 876      13.017 187.996-179.812  1.00149.79           C  
ANISOU 2351  CG  ASP A 876    20125  21204  15584   -191  -6941   3176       C  
ATOM   2352  OD1 ASP A 876      13.222 188.113-178.584  1.00155.61           O1+
ANISOU 2352  OD1 ASP A 876    21318  22148  15659   -171  -7328   3334       O1+
ATOM   2353  OD2 ASP A 876      11.885 187.792-180.296  1.00146.59           O1-
ANISOU 2353  OD2 ASP A 876    19927  20512  15257   -315  -6249   3197       O1-
ATOM   2354  N   GLY A 877      13.528 191.006-179.510  1.00143.93           N  
ANISOU 2354  N   GLY A 877    19159  21173  14354   -963  -7060   2141       N  
ATOM   2355  CA  GLY A 877      13.568 191.866-178.341  1.00149.45           C  
ANISOU 2355  CA  GLY A 877    20281  22122  14380  -1150  -7184   1909       C  
ATOM   2356  C   GLY A 877      14.232 193.200-178.618  1.00149.10           C  
ANISOU 2356  C   GLY A 877    19819  22289  14543  -1475  -7265   1322       C  
ATOM   2357  O   GLY A 877      14.621 193.915-177.692  1.00154.48           O  
ANISOU 2357  O   GLY A 877    20681  23206  14810  -1608  -7518   1044       O  
ATOM   2358  N   ALA A 878      14.365 193.532-179.898  1.00142.33           N  
ANISOU 2358  N   ALA A 878    18417  21336  14326  -1619  -7036   1131       N  
ATOM   2359  CA  ALA A 878      14.976 194.791-180.293  1.00141.06           C  
ANISOU 2359  CA  ALA A 878    17863  21297  14438  -1979  -7028    613       C  
ATOM   2360  C   ALA A 878      14.093 195.964-179.888  1.00137.28           C  
ANISOU 2360  C   ALA A 878    17972  20767  13423  -2361  -6667    335       C  
ATOM   2361  O   ALA A 878      12.866 195.892-179.980  1.00134.89           O  
ANISOU 2361  O   ALA A 878    18133  20266  12853  -2346  -6137    483       O  
ATOM   2362  CB  ALA A 878      15.234 194.811-181.789  1.00136.48           C  
ANISOU 2362  CB  ALA A 878    16631  20585  14642  -2004  -6706    524       C  
ATOM   2363  N   CYS A 879      14.722 197.034-179.419  1.00137.53           N  
ANISOU 2363  N   CYS A 879    17947  20935  13374  -2647  -6861   -117       N  
ATOM   2364  CA  CYS A 879      14.002 198.252-179.087  1.00132.69           C  
ANISOU 2364  CA  CYS A 879    17857  20217  12341  -3013  -6513   -460       C  
ATOM   2365  C   CYS A 879      13.878 199.083-180.354  1.00126.63           C  
ANISOU 2365  C   CYS A 879    16776  19216  12122  -3280  -6028   -690       C  
ATOM   2366  O   CYS A 879      14.815 199.149-181.146  1.00126.12           O  
ANISOU 2366  O   CYS A 879    16041  19179  12699  -3352  -6139   -792       O  
ATOM   2367  CB  CYS A 879      14.744 199.032-178.002  1.00138.30           C  
ANISOU 2367  CB  CYS A 879    18668  21126  12754  -3195  -6919   -881       C  
ATOM   2368  SG  CYS A 879      13.794 200.394-177.301  1.00203.44           S  
ANISOU 2368  SG  CYS A 879    27710  29213  20374  -3555  -6498  -1307       S  
ATOM   2369  N   ILE A 880      12.721 199.704-180.555  1.00124.70           N  
ANISOU 2369  N   ILE A 880    16984  18702  11695  -3330  -5370   -764       N  
ATOM   2370  CA  ILE A 880      12.467 200.458-181.783  1.00122.15           C  
ANISOU 2370  CA  ILE A 880    16434  18080  11897  -3424  -4778   -907       C  
ATOM   2371  C   ILE A 880      11.637 201.708-181.517  1.00126.50           C  
ANISOU 2371  C   ILE A 880    17535  18377  12151  -3631  -4325  -1218       C  
ATOM   2372  O   ILE A 880      10.579 201.637-180.906  1.00128.46           O  
ANISOU 2372  O   ILE A 880    18316  18588  11905  -3501  -4076  -1150       O  
ATOM   2373  CB  ILE A 880      11.772 199.578-182.844  1.00112.06           C  
ANISOU 2373  CB  ILE A 880    14961  16673  10942  -3059  -4353   -537       C  
ATOM   2374  CG1 ILE A 880      12.811 198.770-183.623  1.00112.55           C  
ANISOU 2374  CG1 ILE A 880    14329  16854  11582  -2926  -4618   -391       C  
ATOM   2375  CG2 ILE A 880      10.935 200.418-183.793  1.00104.57           C  
ANISOU 2375  CG2 ILE A 880    14122  15418  10191  -3075  -3681   -636       C  
ATOM   2376  CD1 ILE A 880      12.203 197.746-184.545  1.00108.87           C  
ANISOU 2376  CD1 ILE A 880    13708  16282  11377  -2568  -4292    -70       C  
ATOM   2377  N   LYS A 881      12.119 202.855-181.981  1.00128.80           N  
ANISOU 2377  N   LYS A 881    17695  18463  12780  -3953  -4174  -1560       N  
ATOM   2378  CA  LYS A 881      11.467 204.122-181.671  1.00132.13           C  
ANISOU 2378  CA  LYS A 881    18656  18576  12970  -4153  -3783  -1900       C  
ATOM   2379  C   LYS A 881      10.484 204.599-182.739  1.00128.23           C  
ANISOU 2379  C   LYS A 881    18262  17704  12754  -3952  -3065  -1782       C  
ATOM   2380  O   LYS A 881      10.655 204.336-183.931  1.00125.33           O  
ANISOU 2380  O   LYS A 881    17480  17271  12870  -3824  -2873  -1559       O  
ATOM   2381  CB  LYS A 881      12.506 205.196-181.384  1.00138.64           C  
ANISOU 2381  CB  LYS A 881    19402  19319  13957  -4665  -4040  -2386       C  
ATOM   2382  N   VAL A 882       9.456 205.310-182.288  1.00129.44           N  
ANISOU 2382  N   VAL A 882    18978  17627  12574  -3899  -2680  -1947       N  
ATOM   2383  CA  VAL A 882       8.455 205.895-183.168  1.00127.20           C  
ANISOU 2383  CA  VAL A 882    18835  16982  12515  -3661  -2052  -1866       C  
ATOM   2384  C   VAL A 882       8.492 207.415-183.069  1.00133.48           C  
ANISOU 2384  C   VAL A 882    20002  17328  13387  -3926  -1779  -2270       C  
ATOM   2385  O   VAL A 882       8.365 207.984-181.984  1.00139.68           O  
ANISOU 2385  O   VAL A 882    21242  18055  13774  -4108  -1829  -2637       O  
ATOM   2386  CB  VAL A 882       7.042 205.416-182.805  1.00124.24           C  
ANISOU 2386  CB  VAL A 882    18751  16671  11784  -3284  -1742  -1703       C  
ATOM   2387  CG1 VAL A 882       6.027 205.965-183.797  1.00120.09           C  
ANISOU 2387  CG1 VAL A 882    18257  15825  11546  -2975  -1182  -1607       C  
ATOM   2388  CG2 VAL A 882       6.996 203.905-182.770  1.00121.88           C  
ANISOU 2388  CG2 VAL A 882    18164  16743  11402  -3082  -1994  -1325       C  
ATOM   2389  N   ILE A 883       8.676 208.070-184.209  1.00133.03           N  
ANISOU 2389  N   ILE A 883    19797  16926  13824  -3948  -1469  -2202       N  
ATOM   2390  CA  ILE A 883       8.713 209.523-184.255  1.00137.09           C  
ANISOU 2390  CA  ILE A 883    20689  16897  14501  -4186  -1147  -2526       C  
ATOM   2391  C   ILE A 883       7.617 210.026-185.181  1.00136.56           C  
ANISOU 2391  C   ILE A 883    20829  16448  14611  -3755   -575  -2295       C  
ATOM   2392  O   ILE A 883       7.286 209.371-186.169  1.00134.81           O  
ANISOU 2392  O   ILE A 883    20298  16370  14553  -3419   -478  -1892       O  
ATOM   2393  CB  ILE A 883      10.064 210.024-184.781  1.00139.18           C  
ANISOU 2393  CB  ILE A 883    20636  17007  15239  -4672  -1268  -2650       C  
ATOM   2394  CG1 ILE A 883      11.206 209.175-184.221  1.00137.88           C  
ANISOU 2394  CG1 ILE A 883    19992  17363  15035  -4958  -1918  -2732       C  
ATOM   2395  CG2 ILE A 883      10.257 211.496-184.444  1.00147.33           C  
ANISOU 2395  CG2 ILE A 883    22124  17467  16388  -5065  -1035  -3100       C  
ATOM   2396  CD1 ILE A 883      12.558 209.569-184.753  1.00140.84           C  
ANISOU 2396  CD1 ILE A 883    19903  17657  15952  -5443  -2026  -2870       C  
ATOM   2397  N   THR A 884       7.049 211.183-184.861  1.00137.32           N  
ANISOU 2397  N   THR A 884    21452  16056  14669  -3739   -220  -2569       N  
ATOM   2398  CA  THR A 884       6.036 211.781-185.718  1.00134.63           C  
ANISOU 2398  CA  THR A 884    21321  15308  14524  -3282    283  -2352       C  
ATOM   2399  C   THR A 884       6.637 212.992-186.435  1.00140.13           C  
ANISOU 2399  C   THR A 884    22223  15376  15644  -3536    556  -2399       C  
ATOM   2400  O   THR A 884       7.848 213.043-186.658  1.00140.54           O  
ANISOU 2400  O   THR A 884    22032  15434  15935  -4023    377  -2453       O  
ATOM   2401  CB  THR A 884       4.769 212.161-184.920  1.00134.11           C  
ANISOU 2401  CB  THR A 884    21693  15105  14160  -2938    570  -2567       C  
ATOM   2402  OG1 THR A 884       4.616 211.264-183.812  1.00131.04           O  
ANISOU 2402  OG1 THR A 884    21259  15233  13298  -2992    299  -2694       O  
ATOM   2403  CG2 THR A 884       3.528 212.070-185.798  1.00132.43           C  
ANISOU 2403  CG2 THR A 884    21402  14829  14086  -2289    903  -2210       C  
ATOM   2404  N   PRO A 885       5.801 213.961-186.795  1.00145.44           N  
ANISOU 2404  N   PRO A 885    23327  15490  16443  -3202   1009  -2366       N  
ATOM   2405  CA  PRO A 885       6.262 215.134-187.534  1.00150.12           C  
ANISOU 2405  CA  PRO A 885    24212  15386  17441  -3391   1343  -2326       C  
ATOM   2406  C   PRO A 885       6.446 216.359-186.641  1.00153.82           C  
ANISOU 2406  C   PRO A 885    25238  15240  17966  -3756   1520  -2875       C  
ATOM   2407  O   PRO A 885       6.951 217.388-187.084  1.00156.86           O  
ANISOU 2407  O   PRO A 885    25913  14964  18721  -4042   1805  -2918       O  
ATOM   2408  CB  PRO A 885       5.307 215.449-188.679  1.00149.89           C  
ANISOU 2408  CB  PRO A 885    24335  15062  17553  -2747   1707  -1858       C  
ATOM   2409  N   LYS A 886       6.037 216.240-185.383  1.00154.01           N  
ANISOU 2409  N   LYS A 886    25445  15463  17607  -3763   1382  -3305       N  
ATOM   2410  CA  LYS A 886       6.100 217.357-184.451  1.00161.01           C  
ANISOU 2410  CA  LYS A 886    26912  15797  18469  -4071   1552  -3911       C  
ATOM   2411  C   LYS A 886       7.140 217.125-183.363  1.00164.81           C  
ANISOU 2411  C   LYS A 886    27298  16624  18697  -4759   1064  -4426       C  
ATOM   2412  O   LYS A 886       7.290 217.942-182.456  1.00171.08           O  
ANISOU 2412  O   LYS A 886    28558  17063  19381  -5097   1105  -5028       O  
ATOM   2413  CB  LYS A 886       4.733 217.606-183.834  1.00161.17           C  
ANISOU 2413  CB  LYS A 886    27329  15695  18213  -3505   1866  -4083       C  
ATOM   2414  N   ILE A 887       7.858 216.012-183.457  1.00162.57           N  
ANISOU 2414  N   ILE A 887    26418  17031  18322  -4941    579  -4206       N  
ATOM   2415  CA  ILE A 887       8.866 215.668-182.460  1.00167.72           C  
ANISOU 2415  CA  ILE A 887    26897  18109  18720  -5516      2  -4630       C  
ATOM   2416  C   ILE A 887      10.254 216.148-182.871  1.00174.76           C  
ANISOU 2416  C   ILE A 887    27493  18783  20125  -6196   -154  -4792       C  
ATOM   2417  O   ILE A 887      10.843 217.009-182.216  1.00182.79           O  
ANISOU 2417  O   ILE A 887    28777  19465  21210  -6755   -236  -5380       O  
ATOM   2418  CB  ILE A 887       8.915 214.150-182.205  1.00160.19           C  
ANISOU 2418  CB  ILE A 887    25452  18021  17390  -5313   -485  -4320       C  
ATOM   2419  CG1 ILE A 887       7.538 213.640-181.771  1.00156.70           C  
ANISOU 2419  CG1 ILE A 887    25267  17796  16475  -4714   -275  -4168       C  
ATOM   2420  CG2 ILE A 887       9.972 213.818-181.161  1.00163.31           C  
ANISOU 2420  CG2 ILE A 887    25689  18864  17496  -5843  -1153  -4725       C  
ATOM   2421  CD1 ILE A 887       7.467 212.137-181.604  1.00151.10           C  
ANISOU 2421  CD1 ILE A 887    24138  17827  15447  -4492   -656  -3797       C  
ATOM   2422  N   HIS A 888      10.775 215.585-183.955  1.00171.21           N  
ANISOU 2422  N   HIS A 888    26477  18530  20046  -6169   -173  -4305       N  
ATOM   2423  CA  HIS A 888      12.097 215.956-184.443  1.00175.00           C  
ANISOU 2423  CA  HIS A 888    26570  18851  21070  -6808   -239  -4412       C  
ATOM   2424  C   HIS A 888      12.212 215.714-185.942  1.00170.15           C  
ANISOU 2424  C   HIS A 888    25620  18156  20873  -6595    123  -3793       C  
ATOM   2425  O   HIS A 888      13.312 215.555-186.471  1.00171.55           O  
ANISOU 2425  O   HIS A 888    25263  18461  21458  -7013     41  -3740       O  
ATOM   2426  CB  HIS A 888      13.176 215.190-183.693  1.00176.53           C  
ANISOU 2426  CB  HIS A 888    26194  19732  21148  -7228   -978  -4690       C  
ATOM   2427  N   ALA A 889      11.071 215.701-186.623  1.00165.67           N  
ANISOU 2427  N   ALA A 889    25357  17396  20194  -5940    529  -3350       N  
ATOM   2428  CA  ALA A 889      11.040 215.444-188.059  1.00161.83           C  
ANISOU 2428  CA  ALA A 889    24647  16876  19966  -5656    854  -2753       C  
ATOM   2429  C   ALA A 889      11.459 216.667-188.870  1.00166.58           C  
ANISOU 2429  C   ALA A 889    25565  16682  21048  -5980   1407  -2680       C  
ATOM   2430  O   ALA A 889      11.303 216.702-190.090  1.00163.27           O  
ANISOU 2430  O   ALA A 889    25167  16095  20772  -5709   1782  -2164       O  
ATOM   2431  CB  ALA A 889       9.663 214.965-188.489  1.00156.45           C  
ANISOU 2431  CB  ALA A 889    24142  16329  18971  -4838   1004  -2332       C  
ATOM   2432  N   PRO A 890      11.998 217.668-188.184  1.00175.45           N  
ANISOU 2432  N   PRO A 890    26968  17301  22394  -6580   1461  -3202       N  
ATOM   2433  CA  PRO A 890      12.544 218.836-188.851  1.00183.91           C  
ANISOU 2433  CA  PRO A 890    28332  17557  23989  -7029   1998  -3179       C  
ATOM   2434  C   PRO A 890      13.783 218.429-189.639  1.00187.58           C  
ANISOU 2434  C   PRO A 890    28123  18302  24848  -7505   2019  -2990       C  
ATOM   2435  O   PRO A 890      14.206 219.130-190.558  1.00194.09           O  
ANISOU 2435  O   PRO A 890    29098  18567  26080  -7776   2569  -2741       O  
ATOM   2436  CB  PRO A 890      12.886 219.912-187.838  1.00191.83           C  
ANISOU 2436  CB  PRO A 890    29737  17984  25165  -7637   1999  -3883       C  
ATOM   2437  N   LEU A 891      14.356 217.285-189.275  1.00183.54           N  
ANISOU 2437  N   LEU A 891    26879  18642  24216  -7585   1452  -3094       N  
ATOM   2438  CA  LEU A 891      15.538 216.768-189.950  1.00183.84           C  
ANISOU 2438  CA  LEU A 891    26164  19042  24645  -7973   1439  -2965       C  
ATOM   2439  C   LEU A 891      15.442 215.264-190.204  1.00174.81           C  
ANISOU 2439  C   LEU A 891    24436  18766  23219  -7466   1052  -2645       C  
ATOM   2440  O   LEU A 891      16.091 214.743-191.110  1.00175.26           O  
ANISOU 2440  O   LEU A 891    23977  19088  23528  -7515   1209  -2363       O  
ATOM   2441  CB  LEU A 891      16.793 217.098-189.154  1.00191.69           C  
ANISOU 2441  CB  LEU A 891    26710  20087  26035  -8844   1108  -3602       C  
ATOM   2442  N   LYS A 892      14.633 214.572-189.406  1.00167.83           N  
ANISOU 2442  N   LYS A 892    23654  18290  21823  -6992    597  -2700       N  
ATOM   2443  CA  LYS A 892      14.455 213.127-189.562  1.00159.50           C  
ANISOU 2443  CA  LYS A 892    22118  17978  20505  -6508    234  -2409       C  
ATOM   2444  C   LYS A 892      13.224 212.792-190.404  1.00153.54           C  
ANISOU 2444  C   LYS A 892    21694  17189  19455  -5769    548  -1890       C  
ATOM   2445  O   LYS A 892      12.360 212.027-189.973  1.00146.33           O  
ANISOU 2445  O   LYS A 892    20834  16629  18137  -5284    273  -1808       O  
ATOM   2446  CB  LYS A 892      14.344 212.438-188.198  1.00157.81           C  
ANISOU 2446  CB  LYS A 892    21793  18267  19901  -6450   -453  -2730       C  
ATOM   2447  CG  LYS A 892      15.553 212.616-187.293  1.00164.48           C  
ANISOU 2447  CG  LYS A 892    22250  19291  20953  -7118   -939  -3263       C  
ATOM   2448  CD  LYS A 892      15.328 211.951-185.940  1.00163.68           C  
ANISOU 2448  CD  LYS A 892    22188  19684  20318  -6981  -1622  -3515       C  
ATOM   2449  CE  LYS A 892      16.437 212.307-184.961  1.00171.20           C  
ANISOU 2449  CE  LYS A 892    22867  20786  21396  -7642  -2166  -4111       C  
ATOM   2450  NZ  LYS A 892      16.195 211.756-183.598  1.00171.67           N1+
ANISOU 2450  NZ  LYS A 892    23104  21308  20815  -7504  -2834  -4348       N1+
ATOM   2451  N   THR A 893      13.146 213.367-191.601  1.00158.01           N  
ANISOU 2451  N   THR A 893    22484  17336  20215  -5698   1120  -1540       N  
ATOM   2452  CA  THR A 893      12.032 213.099-192.506  1.00155.87           C  
ANISOU 2452  CA  THR A 893    22503  17059  19663  -4997   1368  -1053       C  
ATOM   2453  C   THR A 893      12.501 212.303-193.711  1.00152.22           C  
ANISOU 2453  C   THR A 893    21599  16956  19280  -4875   1505   -687       C  
ATOM   2454  O   THR A 893      13.472 212.671-194.371  1.00156.27           O  
ANISOU 2454  O   THR A 893    21939  17300  20135  -5297   1841   -631       O  
ATOM   2455  CB  THR A 893      11.374 214.393-193.019  1.00163.38           C  
ANISOU 2455  CB  THR A 893    24196  17232  20648  -4848   1907   -862       C  
ATOM   2456  OG1 THR A 893      11.075 215.258-191.917  1.00169.83           O  
ANISOU 2456  OG1 THR A 893    25445  17617  21466  -5030   1862  -1280       O  
ATOM   2457  CG2 THR A 893      10.091 214.071-193.777  1.00159.27           C  
ANISOU 2457  CG2 THR A 893    23936  16797  19782  -4044   2007   -414       C  
ATOM   2458  N   GLN A 894      11.803 211.211-193.997  1.00146.15           N  
ANISOU 2458  N   GLN A 894    20654  16673  18204  -4319   1283   -466       N  
ATOM   2459  CA  GLN A 894      12.126 210.384-195.149  1.00144.10           C  
ANISOU 2459  CA  GLN A 894    20032  16766  17954  -4136   1407   -165       C  
ATOM   2460  C   GLN A 894      11.026 210.466-196.199  1.00142.01           C  
ANISOU 2460  C   GLN A 894    20198  16392  17367  -3536   1674    253       C  
ATOM   2461  O   GLN A 894       9.873 210.760-195.883  1.00140.99           O  
ANISOU 2461  O   GLN A 894    20465  16104  17001  -3139   1601    295       O  
ATOM   2462  CB  GLN A 894      12.352 208.934-194.717  1.00140.84           C  
ANISOU 2462  CB  GLN A 894    19009  17013  17492  -4012    902   -281       C  
ATOM   2463  CG  GLN A 894      13.660 208.713-193.979  1.00144.65           C  
ANISOU 2463  CG  GLN A 894    18934  17701  18326  -4552    613   -619       C  
ATOM   2464  CD  GLN A 894      14.869 208.966-194.861  1.00150.11           C  
ANISOU 2464  CD  GLN A 894    19262  18334  19439  -4958   1002   -585       C  
ATOM   2465  OE1 GLN A 894      14.783 208.891-196.087  1.00150.19           O  
ANISOU 2465  OE1 GLN A 894    19352  18315  19398  -4755   1436   -271       O  
ATOM   2466  NE2 GLN A 894      16.002 209.274-194.240  1.00155.25           N  
ANISOU 2466  NE2 GLN A 894    19502  18990  20495  -5545    857   -927       N  
ATOM   2467  N   ASN A 895      11.390 210.215-197.452  1.00142.29           N  
ANISOU 2467  N   ASN A 895    20142  16536  17386  -3459   1980    544       N  
ATOM   2468  CA  ASN A 895      10.420 210.199-198.538  1.00142.59           C  
ANISOU 2468  CA  ASN A 895    20562  16565  17051  -2876   2156    938       C  
ATOM   2469  C   ASN A 895       9.784 208.819-198.687  1.00138.43           C  
ANISOU 2469  C   ASN A 895    19682  16648  16269  -2417   1761    935       C  
ATOM   2470  O   ASN A 895      10.479 207.831-198.925  1.00137.61           O  
ANISOU 2470  O   ASN A 895    19074  16956  16256  -2526   1665    850       O  
ATOM   2471  CB  ASN A 895      11.085 210.625-199.847  1.00148.89           C  
ANISOU 2471  CB  ASN A 895    21537  17183  17851  -3014   2710   1258       C  
ATOM   2472  CG  ASN A 895      10.092 210.787-200.981  1.00151.36           C  
ANISOU 2472  CG  ASN A 895    22364  17446  17699  -2401   2865   1694       C  
ATOM   2473  OD1 ASN A 895       8.880 210.826-200.762  1.00149.62           O  
ANISOU 2473  OD1 ASN A 895    22387  17219  17244  -1895   2589   1749       O  
ATOM   2474  ND2 ASN A 895      10.602 210.890-202.203  1.00155.69           N  
ANISOU 2474  ND2 ASN A 895    23071  17985  18101  -2438   3309   1999       N  
ATOM   2475  N   SER A 896       8.464 208.757-198.536  1.00136.20           N  
ANISOU 2475  N   SER A 896    19640  16394  15717  -1911   1553   1004       N  
ATOM   2476  CA  SER A 896       7.728 207.503-198.675  1.00130.80           C  
ANISOU 2476  CA  SER A 896    18645  16227  14824  -1505   1202    982       C  
ATOM   2477  C   SER A 896       7.910 206.894-200.066  1.00132.91           C  
ANISOU 2477  C   SER A 896    18825  16780  14897  -1303   1336   1187       C  
ATOM   2478  O   SER A 896       7.472 207.464-201.067  1.00135.68           O  
ANISOU 2478  O   SER A 896    19591  16982  14979  -1011   1563   1483       O  
ATOM   2479  CB  SER A 896       6.242 207.727-198.390  1.00128.37           C  
ANISOU 2479  CB  SER A 896    18600  15861  14313  -1015   1039   1023       C  
ATOM   2480  OG  SER A 896       5.496 206.544-198.612  1.00124.70           O  
ANISOU 2480  OG  SER A 896    17819  15872  13690   -669    734    991       O  
ATOM   2481  N   VAL A 897       8.559 205.733-200.114  1.00131.53           N  
ANISOU 2481  N   VAL A 897    18139  17004  14832  -1432   1190   1026       N  
ATOM   2482  CA  VAL A 897       8.865 205.058-201.373  1.00132.63           C  
ANISOU 2482  CA  VAL A 897    18162  17433  14798  -1284   1347   1127       C  
ATOM   2483  C   VAL A 897       7.601 204.677-202.141  1.00128.00           C  
ANISOU 2483  C   VAL A 897    17780  17061  13793   -725   1172   1250       C  
ATOM   2484  O   VAL A 897       7.518 204.850-203.362  1.00127.98           O  
ANISOU 2484  O   VAL A 897    18059  17113  13455   -510   1392   1463       O  
ATOM   2485  CB  VAL A 897       9.721 203.793-201.133  1.00132.90           C  
ANISOU 2485  CB  VAL A 897    17574  17825  15096  -1468   1181    873       C  
ATOM   2486  CG1 VAL A 897       9.847 202.971-202.397  1.00133.16           C  
ANISOU 2486  CG1 VAL A 897    17508  18170  14916  -1242   1324    900       C  
ATOM   2487  CG2 VAL A 897      11.095 204.174-200.601  1.00137.30           C  
ANISOU 2487  CG2 VAL A 897    17846  18243  16079  -2004   1350    750       C  
ATOM   2488  N   LYS A 898       6.613 204.177-201.408  1.00123.51           N  
ANISOU 2488  N   LYS A 898    17069  16626  13232   -505    777   1109       N  
ATOM   2489  CA  LYS A 898       5.370 203.703-201.998  1.00121.61           C  
ANISOU 2489  CA  LYS A 898    16875  16640  12690    -17    534   1139       C  
ATOM   2490  C   LYS A 898       4.585 204.814-202.692  1.00125.13           C  
ANISOU 2490  C   LYS A 898    17845  16875  12823    354    646   1437       C  
ATOM   2491  O   LYS A 898       3.693 204.541-203.493  1.00128.14           O  
ANISOU 2491  O   LYS A 898    18295  17503  12889    785    452   1502       O  
ATOM   2492  CB  LYS A 898       4.505 203.043-200.925  1.00118.35           C  
ANISOU 2492  CB  LYS A 898    16173  16358  12436     59    170    922       C  
ATOM   2493  CG  LYS A 898       3.680 201.881-201.428  1.00117.93           C  
ANISOU 2493  CG  LYS A 898    15855  16695  12260    345   -117    788       C  
ATOM   2494  CD  LYS A 898       2.909 201.237-200.296  1.00116.50           C  
ANISOU 2494  CD  LYS A 898    15388  16591  12286    331   -377    597       C  
ATOM   2495  CE  LYS A 898       2.258 199.944-200.751  1.00117.63           C  
ANISOU 2495  CE  LYS A 898    15208  17075  12411    491   -630    413       C  
ATOM   2496  NZ  LYS A 898       3.274 198.945-201.187  1.00118.32           N1+
ANISOU 2496  NZ  LYS A 898    15089  17286  12580    306   -605    298       N1+
ATOM   2497  N   ASP A 899       4.918 206.064-202.384  1.00125.32           N  
ANISOU 2497  N   ASP A 899    18242  16426  12946    196    933   1609       N  
ATOM   2498  CA  ASP A 899       4.243 207.206-202.992  1.00124.89           C  
ANISOU 2498  CA  ASP A 899    18752  16061  12639    574   1068   1945       C  
ATOM   2499  C   ASP A 899       4.616 207.400-204.449  1.00120.48           C  
ANISOU 2499  C   ASP A 899    18549  15551  11678    711   1325   2265       C  
ATOM   2500  O   ASP A 899       3.847 207.980-205.210  1.00124.25           O  
ANISOU 2500  O   ASP A 899    19459  15954  11797   1190   1287   2570       O  
ATOM   2501  CB  ASP A 899       4.546 208.486-202.223  1.00132.00           C  
ANISOU 2501  CB  ASP A 899    19999  16350  13805    330   1348   2013       C  
ATOM   2502  CG  ASP A 899       3.719 208.613-200.973  1.00134.72           C  
ANISOU 2502  CG  ASP A 899    20222  16600  14364    428   1113   1776       C  
ATOM   2503  OD1 ASP A 899       2.716 207.878-200.848  1.00133.19           O  
ANISOU 2503  OD1 ASP A 899    19738  16777  14090    775    769   1652       O  
ATOM   2504  OD2 ASP A 899       4.065 209.452-200.117  1.00138.64           O1-
ANISOU 2504  OD2 ASP A 899    20918  16649  15110    135   1298   1686       O1-
ATOM   2505  N   ASP A 900       5.800 206.929-204.823  1.00114.29           N  
ANISOU 2505  N   ASP A 900    17588  14896  10940    313   1595   2201       N  
ATOM   2506  CA  ASP A 900       6.288 207.064-206.189  1.00114.62           C  
ANISOU 2506  CA  ASP A 900    17977  15007  10569    374   1946   2480       C  
ATOM   2507  C   ASP A 900       5.287 206.464-207.172  1.00108.51           C  
ANISOU 2507  C   ASP A 900    17304  14680   9247    952   1598   2534       C  
ATOM   2508  O   ASP A 900       4.680 205.434-206.890  1.00103.07           O  
ANISOU 2508  O   ASP A 900    16163  14385   8612   1102   1152   2211       O  
ATOM   2509  CB  ASP A 900       7.644 206.373-206.326  1.00117.65           C  
ANISOU 2509  CB  ASP A 900    17965  15576  11162   -115   2251   2278       C  
ATOM   2510  CG  ASP A 900       8.378 206.769-207.593  1.00126.31           C  
ANISOU 2510  CG  ASP A 900    19466  16625  11901   -194   2821   2580       C  
ATOM   2511  OD1 ASP A 900       7.729 207.275-208.533  1.00130.10           O  
ANISOU 2511  OD1 ASP A 900    20542  17069  11822    221   2868   2941       O  
ATOM   2512  OD2 ASP A 900       9.609 206.568-207.649  1.00129.66           O1-
ANISOU 2512  OD2 ASP A 900    19606  17062  12597   -661   3229   2463       O1-
ATOM   2513  N   LYS A 901       5.104 207.120-208.314  1.00111.47           N  
ANISOU 2513  N   LYS A 901    18291  14981   9084   1263   1791   2942       N  
ATOM   2514  CA  LYS A 901       4.171 206.634-209.325  1.00114.40           C  
ANISOU 2514  CA  LYS A 901    18806  15809   8850   1827   1407   2991       C  
ATOM   2515  C   LYS A 901       4.558 205.234-209.789  1.00112.21           C  
ANISOU 2515  C   LYS A 901    18099  16086   8449   1699   1314   2601       C  
ATOM   2516  O   LYS A 901       3.780 204.294-209.652  1.00110.30           O  
ANISOU 2516  O   LYS A 901    17454  16233   8223   1906    803   2264       O  
ATOM   2517  CB  LYS A 901       4.101 207.590-210.522  1.00123.53           C  
ANISOU 2517  CB  LYS A 901    20783  16789   9363   2159   1673   3549       C  
ATOM   2518  CG  LYS A 901       3.176 207.118-211.642  1.00126.21           C  
ANISOU 2518  CG  LYS A 901    21317  17660   8976   2762   1213   3598       C  
ATOM   2519  CD  LYS A 901       3.261 208.018-212.866  1.00136.01           C  
ANISOU 2519  CD  LYS A 901    23451  18746   9479   3072   1513   4201       C  
ATOM   2520  CE  LYS A 901       2.409 207.480-214.014  1.00141.56           C  
ANISOU 2520  CE  LYS A 901    24304  20052   9432   3629    981   4173       C  
ATOM   2521  NZ  LYS A 901       2.468 208.343-215.234  1.00150.38           N1+
ANISOU 2521  NZ  LYS A 901    26079  20987  10072   3796   1178   4632       N1+
ATOM   2522  N   ASN A 902       5.765 205.096-210.327  1.00115.91           N  
ANISOU 2522  N   ASN A 902    18638  16560   8841   1344   1847   2624       N  
ATOM   2523  CA  ASN A 902       6.251 203.792-210.762  1.00119.49           C  
ANISOU 2523  CA  ASN A 902    18696  17475   9231   1226   1845   2225       C  
ATOM   2524  C   ASN A 902       7.100 203.105-209.695  1.00118.33           C  
ANISOU 2524  C   ASN A 902    17860  17273   9827    745   1914   1853       C  
ATOM   2525  O   ASN A 902       8.268 202.778-209.915  1.00119.76           O  
ANISOU 2525  O   ASN A 902    17845  17488  10168    408   2355   1740       O  
ATOM   2526  CB  ASN A 902       7.011 203.909-212.084  1.00126.45           C  
ANISOU 2526  CB  ASN A 902    20032  18481   9533   1200   2396   2421       C  
ATOM   2527  CG  ASN A 902       6.094 204.209-213.255  1.00132.96           C  
ANISOU 2527  CG  ASN A 902    21507  19537   9474   1761   2172   2705       C  
ATOM   2528  OD1 ASN A 902       4.941 204.602-213.071  1.00133.15           O  
ANISOU 2528  OD1 ASN A 902    21671  19536   9384   2174   1652   2846       O  
ATOM   2529  ND2 ASN A 902       6.602 204.024-214.469  1.00138.36           N  
ANISOU 2529  ND2 ASN A 902    22584  20474   9513   1800   2558   2781       N  
ATOM   2530  N   PHE A 903       6.492 202.890-208.533  1.00115.60           N  
ANISOU 2530  N   PHE A 903    17146  16855   9921    742   1474   1672       N  
ATOM   2531  CA  PHE A 903       7.148 202.237-207.409  1.00113.56           C  
ANISOU 2531  CA  PHE A 903    16287  16551  10309    358   1420   1360       C  
ATOM   2532  C   PHE A 903       7.271 200.742-207.654  1.00116.95           C  
ANISOU 2532  C   PHE A 903    16278  17367  10793    395   1232    964       C  
ATOM   2533  O   PHE A 903       8.175 200.089-207.132  1.00118.60           O  
ANISOU 2533  O   PHE A 903    16035  17576  11451    103   1325    741       O  
ATOM   2534  CB  PHE A 903       6.359 202.505-206.127  1.00108.38           C  
ANISOU 2534  CB  PHE A 903    15489  15703   9985    378   1041   1324       C  
ATOM   2535  CG  PHE A 903       6.431 201.397-205.115  1.00101.29           C  
ANISOU 2535  CG  PHE A 903    14012  14938   9534    208    735    971       C  
ATOM   2536  CD1 PHE A 903       7.525 201.270-204.282  1.00 99.84           C  
ANISOU 2536  CD1 PHE A 903    13504  14620   9813   -206    867    863       C  
ATOM   2537  CD2 PHE A 903       5.387 200.499-204.979  1.00 97.62           C  
ANISOU 2537  CD2 PHE A 903    13334  14722   9035    461    301    762       C  
ATOM   2538  CE1 PHE A 903       7.580 200.261-203.337  1.00 95.40           C  
ANISOU 2538  CE1 PHE A 903    12482  14158   9609   -310    557    606       C  
ATOM   2539  CE2 PHE A 903       5.439 199.486-204.038  1.00 92.53           C  
ANISOU 2539  CE2 PHE A 903    12234  14135   8787    299     66    500       C  
ATOM   2540  CZ  PHE A 903       6.534 199.369-203.217  1.00 90.56           C  
ANISOU 2540  CZ  PHE A 903    11736  13737   8935    -59    186    450       C  
ATOM   2541  N   SER A 904       6.358 200.208-208.458  1.00118.58           N  
ANISOU 2541  N   SER A 904    16617  17887  10553    769    945    860       N  
ATOM   2542  CA  SER A 904       6.359 198.788-208.784  1.00116.52           C  
ANISOU 2542  CA  SER A 904    16009  17944  10320    818    763    440       C  
ATOM   2543  C   SER A 904       7.354 198.466-209.898  1.00118.44           C  
ANISOU 2543  C   SER A 904    16368  18354  10278    763   1233    355       C  
ATOM   2544  O   SER A 904       7.498 197.311-210.299  1.00119.94           O  
ANISOU 2544  O   SER A 904    16324  18773  10473    809   1176    -27       O  
ATOM   2545  CB  SER A 904       4.951 198.330-209.175  1.00118.09           C  
ANISOU 2545  CB  SER A 904    16258  18421  10189   1191    236    282       C  
ATOM   2546  OG  SER A 904       4.413 199.148-210.202  1.00123.55           O  
ANISOU 2546  OG  SER A 904    17496  19236  10210   1523    232    557       O  
ATOM   2547  N   ILE A 905       8.041 199.487-210.396  1.00118.19           N  
ANISOU 2547  N   ILE A 905    16716  18176  10014    652   1747    698       N  
ATOM   2548  CA  ILE A 905       9.020 199.293-211.458  1.00120.62           C  
ANISOU 2548  CA  ILE A 905    17161  18639  10030    571   2317    649       C  
ATOM   2549  C   ILE A 905      10.401 199.720-210.980  1.00121.93           C  
ANISOU 2549  C   ILE A 905    17047  18545  10736    117   2872    737       C  
ATOM   2550  O   ILE A 905      11.421 199.259-211.494  1.00122.49           O  
ANISOU 2550  O   ILE A 905    16915  18741  10886    -34   3349    557       O  
ATOM   2551  CB  ILE A 905       8.649 200.095-212.717  1.00125.52           C  
ANISOU 2551  CB  ILE A 905    18548  19365   9779    836   2538   1002       C  
ATOM   2552  CG1 ILE A 905       7.169 199.904-213.054  1.00125.93           C  
ANISOU 2552  CG1 ILE A 905    18839  19668   9340   1306   1863    960       C  
ATOM   2553  CG2 ILE A 905       9.524 199.690-213.893  1.00130.42           C  
ANISOU 2553  CG2 ILE A 905    19341  20233   9980    794   3125    876       C  
ATOM   2554  CD1 ILE A 905       6.722 200.661-214.283  1.00133.81           C  
ANISOU 2554  CD1 ILE A 905    20618  20809   9413   1655   1951   1332       C  
ATOM   2555  N   LYS A 906      10.427 200.596-209.982  1.00123.27           N  
ANISOU 2555  N   LYS A 906    17172  18363  11302   -103   2807    969       N  
ATOM   2556  CA  LYS A 906      11.682 201.138-209.477  1.00127.35           C  
ANISOU 2556  CA  LYS A 906    17413  18623  12352   -580   3271   1035       C  
ATOM   2557  C   LYS A 906      12.172 200.409-208.227  1.00123.69           C  
ANISOU 2557  C   LYS A 906    16214  18142  12641   -798   2952    714       C  
ATOM   2558  O   LYS A 906      13.333 200.537-207.843  1.00127.61           O  
ANISOU 2558  O   LYS A 906    16298  18545  13642  -1171   3255    642       O  
ATOM   2559  CB  LYS A 906      11.545 202.634-209.209  1.00129.16           C  
ANISOU 2559  CB  LYS A 906    18103  18429  12542   -742   3454   1461       C  
ATOM   2560  N   TYR A 907      11.290 199.637-207.598  1.00116.96           N  
ANISOU 2560  N   TYR A 907    15190  17386  11863   -565   2339    529       N  
ATOM   2561  CA  TYR A 907      11.641 198.925-206.372  1.00112.97           C  
ANISOU 2561  CA  TYR A 907    14094  16847  11983   -718   1990    293       C  
ATOM   2562  C   TYR A 907      11.170 197.474-206.388  1.00106.28           C  
ANISOU 2562  C   TYR A 907    12984  16220  11178   -447   1616    -23       C  
ATOM   2563  O   TYR A 907      10.288 197.106-207.165  1.00105.64           O  
ANISOU 2563  O   TYR A 907    13185  16309  10643   -150   1494    -87       O  
ATOM   2564  CB  TYR A 907      11.061 199.641-205.149  1.00114.71           C  
ANISOU 2564  CB  TYR A 907    14400  16814  12370   -825   1637    439       C  
ATOM   2565  CG  TYR A 907      11.547 201.063-204.979  1.00124.00           C  
ANISOU 2565  CG  TYR A 907    15828  17680  13607  -1141   1981    693       C  
ATOM   2566  CD1 TYR A 907      10.922 202.116-205.638  1.00129.70           C  
ANISOU 2566  CD1 TYR A 907    17180  18228  13874  -1008   2194   1009       C  
ATOM   2567  CD2 TYR A 907      12.628 201.354-204.157  1.00127.55           C  
ANISOU 2567  CD2 TYR A 907    15888  17988  14588  -1568   2070    609       C  
ATOM   2568  CE1 TYR A 907      11.364 203.420-205.487  1.00134.94           C  
ANISOU 2568  CE1 TYR A 907    18124  18511  14635  -1314   2550   1246       C  
ATOM   2569  CE2 TYR A 907      13.077 202.655-203.997  1.00132.66           C  
ANISOU 2569  CE2 TYR A 907    16761  18305  15341  -1922   2398    787       C  
ATOM   2570  CZ  TYR A 907      12.441 203.684-204.664  1.00135.40           C  
ANISOU 2570  CZ  TYR A 907    17781  18409  15256  -1804   2668   1110       C  
ATOM   2571  OH  TYR A 907      12.881 204.981-204.510  1.00138.05           O  
ANISOU 2571  OH  TYR A 907    18392  18324  15736  -2171   3033   1293       O  
ATOM   2572  N   PHE A 908      11.774 196.652-205.532  1.00102.98           N  
ANISOU 2572  N   PHE A 908    12034  15780  11314   -552   1420   -222       N  
ATOM   2573  CA  PHE A 908      11.304 195.285-205.312  1.00102.33           C  
ANISOU 2573  CA  PHE A 908    11725  15780  11375   -332   1044   -485       C  
ATOM   2574  C   PHE A 908      11.587 194.802-203.889  1.00 99.40           C  
ANISOU 2574  C   PHE A 908    10955  15267  11547   -451    667   -510       C  
ATOM   2575  O   PHE A 908      12.402 195.387-203.175  1.00 97.41           O  
ANISOU 2575  O   PHE A 908    10493  14922  11596   -704    704   -408       O  
ATOM   2576  CB  PHE A 908      11.865 194.313-206.356  1.00107.76           C  
ANISOU 2576  CB  PHE A 908    12255  16639  12050   -174   1326   -783       C  
ATOM   2577  CG  PHE A 908      13.338 194.061-206.235  1.00115.02           C  
ANISOU 2577  CG  PHE A 908    12669  17549  13483   -322   1637   -894       C  
ATOM   2578  CD1 PHE A 908      14.253 194.954-206.765  1.00122.22           C  
ANISOU 2578  CD1 PHE A 908    13575  18500  14364   -540   2186   -778       C  
ATOM   2579  CD2 PHE A 908      13.809 192.914-205.617  1.00117.58           C  
ANISOU 2579  CD2 PHE A 908    12508  17814  14352   -229   1399  -1109       C  
ATOM   2580  CE1 PHE A 908      15.613 194.717-206.666  1.00127.24           C  
ANISOU 2580  CE1 PHE A 908    13637  19164  15543   -684   2486   -920       C  
ATOM   2581  CE2 PHE A 908      15.169 192.671-205.513  1.00122.48           C  
ANISOU 2581  CE2 PHE A 908    12585  18454  15498   -304   1645  -1225       C  
ATOM   2582  CZ  PHE A 908      16.072 193.572-206.041  1.00127.01           C  
ANISOU 2582  CZ  PHE A 908    13067  19118  16074   -539   2189  -1155       C  
ATOM   2583  N   HIS A 909      10.895 193.740-203.481  1.00 98.04           N  
ANISOU 2583  N   HIS A 909    10705  15072  11474   -282    297   -645       N  
ATOM   2584  CA  HIS A 909      10.975 193.239-202.109  1.00 96.31           C  
ANISOU 2584  CA  HIS A 909    10235  14706  11652   -353    -87   -603       C  
ATOM   2585  C   HIS A 909      11.385 191.764-202.055  1.00102.30           C  
ANISOU 2585  C   HIS A 909    10661  15412  12797   -185   -209   -818       C  
ATOM   2586  O   HIS A 909      12.518 191.444-201.697  1.00105.92           O  
ANISOU 2586  O   HIS A 909    10731  15840  13675   -207   -200   -848       O  
ATOM   2587  CB  HIS A 909       9.633 193.443-201.397  1.00 90.35           C  
ANISOU 2587  CB  HIS A 909     9764  13880  10686   -342   -399   -481       C  
ATOM   2588  CG  HIS A 909       9.640 193.054-199.950  1.00 86.94           C  
ANISOU 2588  CG  HIS A 909     9195  13305  10532   -436   -742   -387       C  
ATOM   2589  ND1 HIS A 909       8.482 192.798-199.245  1.00 82.91           N  
ANISOU 2589  ND1 HIS A 909     8857  12722   9923   -412   -981   -329       N  
ATOM   2590  CD2 HIS A 909      10.658 192.887-199.072  1.00 85.22           C  
ANISOU 2590  CD2 HIS A 909     8699  13028  10655   -547   -890   -334       C  
ATOM   2591  CE1 HIS A 909       8.787 192.489-197.997  1.00 79.80           C  
ANISOU 2591  CE1 HIS A 909     8370  12215   9737   -509  -1224   -216       C  
ATOM   2592  NE2 HIS A 909      10.100 192.536-197.865  1.00 81.11           N  
ANISOU 2592  NE2 HIS A 909     8265  12396  10156   -574  -1222   -216       N  
ATOM   2593  N   LEU A 910      10.463 190.871-202.408  1.00104.60           N  
ANISOU 2593  N   LEU A 910    11086  15673  12985    -12   -333   -981       N  
ATOM   2594  CA  LEU A 910      10.729 189.433-202.357  1.00108.07           C  
ANISOU 2594  CA  LEU A 910    11288  15960  13812    153   -435  -1192       C  
ATOM   2595  C   LEU A 910      10.576 188.754-203.719  1.00119.01           C  
ANISOU 2595  C   LEU A 910    12745  17427  15045    333   -194  -1554       C  
ATOM   2596  O   LEU A 910      10.594 187.525-203.812  1.00121.81           O  
ANISOU 2596  O   LEU A 910    12983  17604  15695    479   -257  -1796       O  
ATOM   2597  CB  LEU A 910       9.802 188.752-201.345  1.00 99.85           C  
ANISOU 2597  CB  LEU A 910    10334  14705  12898    140   -811  -1101       C  
ATOM   2598  CG  LEU A 910       9.775 189.328-199.929  1.00 92.06           C  
ANISOU 2598  CG  LEU A 910     9374  13650  11955    -27  -1067   -769       C  
ATOM   2599  CD1 LEU A 910       8.844 188.528-199.034  1.00 89.39           C  
ANISOU 2599  CD1 LEU A 910     9161  13096  11706    -39  -1333   -682       C  
ATOM   2600  CD2 LEU A 910      11.166 189.369-199.340  1.00 91.84           C  
ANISOU 2600  CD2 LEU A 910     9018  13602  12276    -40  -1129   -670       C  
ATOM   2601  N   VAL A 911      10.416 189.557-204.768  1.00124.96           N  
ANISOU 2601  N   VAL A 911    13740  18427  15310    328     80  -1593       N  
ATOM   2602  CA  VAL A 911      10.185 189.047-206.118  1.00129.57           C  
ANISOU 2602  CA  VAL A 911    14491  19159  15581    493    290  -1948       C  
ATOM   2603  C   VAL A 911      10.898 189.922-207.151  1.00134.01           C  
ANISOU 2603  C   VAL A 911    15188  19966  15765    484    776  -1917       C  
ATOM   2604  O   VAL A 911      10.858 191.148-207.056  1.00136.38           O  
ANISOU 2604  O   VAL A 911    15672  20343  15804    350    862  -1594       O  
ATOM   2605  CB  VAL A 911       8.668 189.034-206.456  1.00109.62           C  
ANISOU 2605  CB  VAL A 911    12290  16732  12628    531      4  -2035       C  
ATOM   2606  CG1 VAL A 911       8.437 188.606-207.896  1.00115.39           C  
ANISOU 2606  CG1 VAL A 911    13237  17680  12927    691    164  -2431       C  
ATOM   2607  CG2 VAL A 911       7.893 188.136-205.500  1.00106.58           C  
ANISOU 2607  CG2 VAL A 911    11778  16093  12625    484   -384  -2081       C  
ATOM   2608  N   ASP A 912      11.555 189.298-208.128  1.00135.89           N  
ANISOU 2608  N   ASP A 912    15363  20291  15978    621   1140  -2252       N  
ATOM   2609  CA  ASP A 912      12.108 190.033-209.271  1.00138.33           C  
ANISOU 2609  CA  ASP A 912    15891  20855  15814    616   1681  -2247       C  
ATOM   2610  C   ASP A 912      12.227 189.153-210.515  1.00139.12           C  
ANISOU 2610  C   ASP A 912    16120  21100  15639    825   1975  -2729       C  
ATOM   2611  O   ASP A 912      12.827 188.080-210.476  1.00139.27           O  
ANISOU 2611  O   ASP A 912    15805  20974  16139    945   2072  -3068       O  
ATOM   2612  CB  ASP A 912      13.462 190.668-208.933  1.00142.11           C  
ANISOU 2612  CB  ASP A 912    16008  21305  16681    436   2081  -2045       C  
ATOM   2613  CG  ASP A 912      14.536 189.642-208.657  1.00147.31           C  
ANISOU 2613  CG  ASP A 912    16088  21843  18038    539   2205  -2320       C  
ATOM   2614  OD1 ASP A 912      14.322 188.778-207.783  1.00146.88           O  
ANISOU 2614  OD1 ASP A 912    15802  21561  18445    635   1758  -2381       O  
ATOM   2615  OD2 ASP A 912      15.590 189.687-209.325  1.00153.08           O1-
ANISOU 2615  OD2 ASP A 912    16601  22697  18866    543   2774  -2465       O1-
ATOM   2616  N   PRO A 913      11.648 189.617-211.618  1.00140.90           N  
ANISOU 2616  N   PRO A 913    16863  21605  15068    895   2104  -2766       N  
ATOM   2617  CA  PRO A 913      11.679 188.872-212.872  1.00146.28           C  
ANISOU 2617  CA  PRO A 913    17776  22481  15324   1084   2370  -3257       C  
ATOM   2618  C   PRO A 913      12.631 189.512-213.879  1.00151.26           C  
ANISOU 2618  C   PRO A 913    18603  23348  15520   1070   3118  -3202       C  
ATOM   2619  O   PRO A 913      13.844 189.296-213.826  1.00153.29           O  
ANISOU 2619  O   PRO A 913    18456  23533  16254   1030   3616  -3297       O  
ATOM   2620  CB  PRO A 913      10.277 188.760-213.459  1.00146.38           C  
ANISOU 2620  CB  PRO A 913    18248  22690  14678   1200   1910  -3422       C  
ATOM   2621  N   PRO A 923      21.852 176.532-209.552  1.00178.58           N  
ANISOU 2621  N   PRO A 923    16170  22706  28976   4719   3704  -6351       N  
ATOM   2622  CA  PRO A 923      20.801 175.889-210.331  1.00178.61           C  
ANISOU 2622  CA  PRO A 923    16925  22454  28484   4638   3804  -6818       C  
ATOM   2623  C   PRO A 923      19.719 175.308-209.429  1.00173.82           C  
ANISOU 2623  C   PRO A 923    16757  21317  27968   4534   3079  -6523       C  
ATOM   2624  O   PRO A 923      18.589 175.090-209.864  1.00172.23           O  
ANISOU 2624  O   PRO A 923    17184  21015  27241   4269   2987  -6763       O  
ATOM   2625  CB  PRO A 923      21.389 174.805-211.223  1.00187.55           C  
ANISOU 2625  CB  PRO A 923    17967  23267  30025   5116   4401  -7564       C  
ATOM   2626  N   GLU A 924      20.073 175.060-208.172  1.00172.33           N  
ANISOU 2626  N   GLU A 924    16227  20811  28439   4734   2568  -6004       N  
ATOM   2627  CA  GLU A 924      19.148 174.472-207.210  1.00167.98           C  
ANISOU 2627  CA  GLU A 924    16081  19717  28027   4651   1941  -5651       C  
ATOM   2628  C   GLU A 924      17.916 175.346-207.035  1.00161.11           C  
ANISOU 2628  C   GLU A 924    15699  19180  26337   4047   1638  -5359       C  
ATOM   2629  O   GLU A 924      16.786 174.859-207.062  1.00156.56           O  
ANISOU 2629  O   GLU A 924    15649  18288  25548   3831   1449  -5474       O  
ATOM   2630  CB  GLU A 924      19.840 174.261-205.873  1.00167.56           C  
ANISOU 2630  CB  GLU A 924    15587  19401  28676   4970   1443  -5058       C  
ATOM   2631  N   LYS A 925      18.151 176.644-206.870  1.00163.06           N  
ANISOU 2631  N   LYS A 925    15735  20050  26171   3775   1616  -5008       N  
ATOM   2632  CA  LYS A 925      17.082 177.610-206.639  1.00161.06           C  
ANISOU 2632  CA  LYS A 925    15881  20131  25184   3261   1337  -4684       C  
ATOM   2633  C   LYS A 925      16.217 177.828-207.879  1.00166.43           C  
ANISOU 2633  C   LYS A 925    17048  21073  25113   3009   1641  -5147       C  
ATOM   2634  O   LYS A 925      15.061 178.242-207.769  1.00160.51           O  
ANISOU 2634  O   LYS A 925    16704  20439  23841   2658   1355  -5001       O  
ATOM   2635  CB  LYS A 925      17.661 178.932-206.156  1.00157.17           C  
ANISOU 2635  CB  LYS A 925    15039  20162  24518   3065   1272  -4227       C  
ATOM   2636  N   LYS A 926      16.780 177.549-209.053  1.00144.40           N  
ANISOU 2636  N   LYS A 926    17186  15195  22484   3266    930  -3370       N  
ATOM   2637  CA  LYS A 926      16.045 177.682-210.306  1.00148.29           C  
ANISOU 2637  CA  LYS A 926    18019  15859  22464   3325   1229  -3394       C  
ATOM   2638  C   LYS A 926      14.873 176.708-210.339  1.00152.65           C  
ANISOU 2638  C   LYS A 926    18994  16311  22694   3304    827  -3471       C  
ATOM   2639  O   LYS A 926      13.848 176.975-210.967  1.00153.67           O  
ANISOU 2639  O   LYS A 926    19439  16589  22359   3238    879  -3420       O  
ATOM   2640  CB  LYS A 926      16.968 177.454-211.497  1.00150.69           C  
ANISOU 2640  CB  LYS A 926    18218  16244  22794   3639   1716  -3603       C  
ATOM   2641  N   ALA A 927      15.032 175.579-209.651  1.00154.79           N  
ANISOU 2641  N   ALA A 927    19245  16316  23253   3364    418  -3581       N  
ATOM   2642  CA  ALA A 927      13.968 174.588-209.535  1.00153.97           C  
ANISOU 2642  CA  ALA A 927    19477  16037  22987   3318      6  -3627       C  
ATOM   2643  C   ALA A 927      13.254 174.701-208.186  1.00151.94           C  
ANISOU 2643  C   ALA A 927    19238  15705  22787   3043   -413  -3326       C  
ATOM   2644  O   ALA A 927      12.392 173.886-207.856  1.00150.93           O  
ANISOU 2644  O   ALA A 927    19327  15398  22622   2969   -773  -3284       O  
ATOM   2645  CB  ALA A 927      14.523 173.183-209.739  1.00155.65           C  
ANISOU 2645  CB  ALA A 927    19680  15960  23500   3583   -157  -3925       C  
ATOM   2646  N   LEU A 928      13.617 175.717-207.409  1.00150.98           N  
ANISOU 2646  N   LEU A 928    18871  15721  22771   2902   -356  -3123       N  
ATOM   2647  CA  LEU A 928      12.967 175.966-206.126  1.00148.79           C  
ANISOU 2647  CA  LEU A 928    18606  15452  22477   2673   -710  -2850       C  
ATOM   2648  C   LEU A 928      11.815 176.965-206.266  1.00146.49           C  
ANISOU 2648  C   LEU A 928    18511  15377  21772   2438   -617  -2669       C  
ATOM   2649  O   LEU A 928      11.204 177.361-205.272  1.00142.08           O  
ANISOU 2649  O   LEU A 928    17962  14880  21140   2249   -844  -2448       O  
ATOM   2650  CB  LEU A 928      13.978 176.457-205.098  1.00148.43           C  
ANISOU 2650  CB  LEU A 928    18180  15435  22780   2677   -781  -2789       C  
ATOM   2651  N   LYS A 929      11.523 177.370-207.499  1.00147.81           N  
ANISOU 2651  N   LYS A 929    18833  15677  21652   2477   -280  -2758       N  
ATOM   2652  CA  LYS A 929      10.429 178.300-207.755  1.00145.58           C  
ANISOU 2652  CA  LYS A 929    18738  15594  20980   2289   -184  -2586       C  
ATOM   2653  C   LYS A 929       9.148 177.566-208.154  1.00142.04           C  
ANISOU 2653  C   LYS A 929    18644  15095  20228   2242   -418  -2607       C  
ATOM   2654  O   LYS A 929       8.163 178.190-208.555  1.00142.77           O  
ANISOU 2654  O   LYS A 929    18920  15352  19975   2123   -354  -2501       O  
ATOM   2655  CB  LYS A 929      10.817 179.315-208.837  1.00148.64           C  
ANISOU 2655  CB  LYS A 929    19075  16187  21217   2363    327  -2602       C  
ATOM   2656  CG  LYS A 929      10.927 178.739-210.245  1.00150.02           C  
ANISOU 2656  CG  LYS A 929    19434  16408  21157   2611    565  -2828       C  
ATOM   2657  CD  LYS A 929      10.978 179.856-211.278  1.00148.54           C  
ANISOU 2657  CD  LYS A 929    19264  16483  20690   2665   1067  -2726       C  
ATOM   2658  CE  LYS A 929      10.877 179.323-212.696  1.00150.11           C  
ANISOU 2658  CE  LYS A 929    19713  16814  20508   2937   1276  -2943       C  
ATOM   2659  NZ  LYS A 929      10.812 180.432-213.691  1.00150.19           N1+
ANISOU 2659  NZ  LYS A 929    19775  17118  20172   3007   1764  -2764       N1+
ATOM   2660  N   ILE A 930       9.176 176.240-208.038  1.00135.45           N  
ANISOU 2660  N   ILE A 930    17880  14010  19575   2338   -700  -2749       N  
ATOM   2661  CA  ILE A 930       8.039 175.395-208.388  1.00126.84           C  
ANISOU 2661  CA  ILE A 930    17073  12793  18326   2292   -964  -2815       C  
ATOM   2662  C   ILE A 930       6.786 175.785-207.618  1.00115.58           C  
ANISOU 2662  C   ILE A 930    15742  11428  16745   2013  -1186  -2514       C  
ATOM   2663  O   ILE A 930       6.753 175.719-206.391  1.00111.06           O  
ANISOU 2663  O   ILE A 930    15055  10789  16355   1894  -1396  -2282       O  
ATOM   2664  CB  ILE A 930       8.343 173.922-208.108  1.00129.51           C  
ANISOU 2664  CB  ILE A 930    17404  12771  19032   2410  -1266  -2962       C  
ATOM   2665  CG1 ILE A 930       9.441 173.425-209.045  1.00132.66           C  
ANISOU 2665  CG1 ILE A 930    17742  13106  19556   2721  -1047  -3326       C  
ATOM   2666  CG2 ILE A 930       7.085 173.083-208.258  1.00130.78           C  
ANISOU 2666  CG2 ILE A 930    17805  12743  19143   2303  -1587  -2987       C  
ATOM   2667  CD1 ILE A 930       9.808 171.978-208.825  1.00136.36           C  
ANISOU 2667  CD1 ILE A 930    18188  13181  20440   2869  -1335  -3502       C  
ATOM   2668  N   LYS A 931       5.753 176.182-208.351  1.00111.53           N  
ANISOU 2668  N   LYS A 931    15435  11066  15875   1936  -1137  -2519       N  
ATOM   2669  CA  LYS A 931       4.561 176.762-207.744  1.00106.98           C  
ANISOU 2669  CA  LYS A 931    14922  10600  15125   1684  -1272  -2238       C  
ATOM   2670  C   LYS A 931       3.798 175.782-206.862  1.00107.49           C  
ANISOU 2670  C   LYS A 931    15022  10424  15396   1541  -1666  -2091       C  
ATOM   2671  O   LYS A 931       3.360 176.132-205.767  1.00103.43           O  
ANISOU 2671  O   LYS A 931    14433   9966  14900   1372  -1775  -1792       O  
ATOM   2672  CB  LYS A 931       3.648 177.340-208.817  1.00105.35           C  
ANISOU 2672  CB  LYS A 931    14916  10602  14511   1668  -1149  -2292       C  
ATOM   2673  N   GLU A 932       3.645 174.554-207.346  1.00114.93           N  
ANISOU 2673  N   GLU A 932    16067  11093  16507   1624  -1866  -2302       N  
ATOM   2674  CA  GLU A 932       2.863 173.536-206.646  1.00119.37           C  
ANISOU 2674  CA  GLU A 932    16653  11364  17337   1484  -2222  -2148       C  
ATOM   2675  C   GLU A 932       3.404 173.218-205.253  1.00117.97           C  
ANISOU 2675  C   GLU A 932    16304  11065  17455   1458  -2347  -1851       C  
ATOM   2676  O   GLU A 932       2.646 172.854-204.351  1.00118.56           O  
ANISOU 2676  O   GLU A 932    16368  11039  17642   1295  -2555  -1538       O  
ATOM   2677  CB  GLU A 932       2.763 172.258-207.485  1.00127.33           C  
ANISOU 2677  CB  GLU A 932    17772  12042  18565   1603  -2413  -2492       C  
ATOM   2678  CG  GLU A 932       1.849 172.372-208.699  1.00133.11           C  
ANISOU 2678  CG  GLU A 932    18696  12880  18998   1600  -2432  -2761       C  
ATOM   2679  CD  GLU A 932       2.399 173.296-209.768  1.00136.69           C  
ANISOU 2679  CD  GLU A 932    19222  13690  19023   1792  -2080  -2980       C  
ATOM   2680  OE1 GLU A 932       3.628 173.527-209.778  1.00138.17           O  
ANISOU 2680  OE1 GLU A 932    19302  13940  19258   1964  -1832  -3037       O  
ATOM   2681  OE2 GLU A 932       1.603 173.797-210.591  1.00137.30           O1-
ANISOU 2681  OE2 GLU A 932    19448  13990  18730   1780  -2045  -3071       O1-
ATOM   2682  N   MET A 933       4.712 173.387-205.074  1.00114.58           N  
ANISOU 2682  N   MET A 933    15726  10671  17138   1632  -2211  -1934       N  
ATOM   2683  CA  MET A 933       5.384 173.073-203.813  1.00110.38           C  
ANISOU 2683  CA  MET A 933    15021  10052  16867   1669  -2355  -1697       C  
ATOM   2684  C   MET A 933       4.923 173.977-202.668  1.00107.84           C  
ANISOU 2684  C   MET A 933    14630  10004  16338   1503  -2372  -1343       C  
ATOM   2685  O   MET A 933       5.348 173.824-201.521  1.00111.70           O  
ANISOU 2685  O   MET A 933    14992  10502  16948   1540  -2513  -1119       O  
ATOM   2686  CB  MET A 933       6.897 173.195-203.996  1.00108.15           C  
ANISOU 2686  CB  MET A 933    14559   9785  16747   1900  -2194  -1917       C  
ATOM   2687  CG  MET A 933       7.726 172.516-202.922  1.00108.28           C  
ANISOU 2687  CG  MET A 933    14400   9632  17109   2019  -2407  -1764       C  
ATOM   2688  SD  MET A 933       9.480 172.558-203.321  1.00192.17           S  
ANISOU 2688  SD  MET A 933    24779  20240  27996   2305  -2222  -2081       S  
ATOM   2689  CE  MET A 933       9.460 171.757-204.922  1.00103.95           C  
ANISOU 2689  CE  MET A 933    13776   8842  16877   2456  -2090  -2503       C  
ATOM   2690  N   TYR A 934       4.046 174.918-202.986  1.00 98.62           N  
ANISOU 2690  N   TYR A 934    13552   9077  14843   1346  -2237  -1306       N  
ATOM   2691  CA  TYR A 934       3.580 175.879-202.010  1.00 90.14           C  
ANISOU 2691  CA  TYR A 934    12415   8280  13553   1209  -2222  -1035       C  
ATOM   2692  C   TYR A 934       2.078 175.769-201.850  1.00 85.28           C  
ANISOU 2692  C   TYR A 934    11929   7678  12796   1006  -2329   -809       C  
ATOM   2693  O   TYR A 934       1.494 176.423-200.989  1.00 82.84           O  
ANISOU 2693  O   TYR A 934    11583   7589  12304    893  -2333   -561       O  
ATOM   2694  CB  TYR A 934       3.958 177.287-202.452  1.00 89.73           C  
ANISOU 2694  CB  TYR A 934    12297   8504  13292   1212  -1931  -1180       C  
ATOM   2695  CG  TYR A 934       5.445 177.512-202.537  1.00 94.41           C  
ANISOU 2695  CG  TYR A 934    12699   9093  14080   1389  -1798  -1377       C  
ATOM   2696  CD1 TYR A 934       6.167 177.082-203.639  1.00 97.88           C  
ANISOU 2696  CD1 TYR A 934    13150   9396  14644   1547  -1648  -1652       C  
ATOM   2697  CD2 TYR A 934       6.127 178.157-201.514  1.00 96.75           C  
ANISOU 2697  CD2 TYR A 934    12782   9535  14442   1411  -1827  -1312       C  
ATOM   2698  CE1 TYR A 934       7.526 177.283-203.723  1.00102.48           C  
ANISOU 2698  CE1 TYR A 934    13519   9975  15446   1709  -1498  -1819       C  
ATOM   2699  CE2 TYR A 934       7.488 178.369-201.587  1.00100.55           C  
ANISOU 2699  CE2 TYR A 934    13039   9998  15166   1562  -1722  -1505       C  
ATOM   2700  CZ  TYR A 934       8.183 177.931-202.694  1.00104.61           C  
ANISOU 2700  CZ  TYR A 934    13549  10363  15834   1703  -1541  -1739       C  
ATOM   2701  OH  TYR A 934       9.541 178.139-202.773  1.00108.76           O  
ANISOU 2701  OH  TYR A 934    13813  10870  16641   1853  -1408  -1918       O  
ATOM   2702  N   LEU A 935       1.456 174.938-202.684  1.00 85.77           N  
ANISOU 2702  N   LEU A 935    12123   7505  12960    971  -2422   -922       N  
ATOM   2703  CA  LEU A 935       0.006 174.772-202.654  1.00 86.20           C  
ANISOU 2703  CA  LEU A 935    12263   7537  12954    770  -2537   -741       C  
ATOM   2704  C   LEU A 935      -0.497 174.345-201.277  1.00 90.82           C  
ANISOU 2704  C   LEU A 935    12769   8084  13653    666  -2693   -305       C  
ATOM   2705  O   LEU A 935      -1.605 174.692-200.885  1.00 94.21           O  
ANISOU 2705  O   LEU A 935    13203   8650  13944    497  -2697    -66       O  
ATOM   2706  CB  LEU A 935      -0.456 173.781-203.721  1.00 88.53           C  
ANISOU 2706  CB  LEU A 935    12675   7528  13436    770  -2678   -989       C  
ATOM   2707  CG  LEU A 935      -0.250 174.211-205.173  1.00 91.55           C  
ANISOU 2707  CG  LEU A 935    13175   8019  13593    887  -2525  -1400       C  
ATOM   2708  CD1 LEU A 935      -0.967 173.270-206.140  1.00 97.38           C  
ANISOU 2708  CD1 LEU A 935    14034   8501  14464    877  -2732  -1665       C  
ATOM   2709  CD2 LEU A 935      -0.699 175.647-205.380  1.00 90.35           C  
ANISOU 2709  CD2 LEU A 935    13046   8255  13030    817  -2306  -1333       C  
ATOM   2710  N   ILE A 936       0.328 173.604-200.544  1.00 89.75           N  
ANISOU 2710  N   ILE A 936    12556   7784  13760    788  -2808   -182       N  
ATOM   2711  CA  ILE A 936      -0.005 173.183-199.185  1.00 84.80           C  
ANISOU 2711  CA  ILE A 936    11860   7161  13199    746  -2935    281       C  
ATOM   2712  C   ILE A 936      -0.335 174.372-198.270  1.00 86.63           C  
ANISOU 2712  C   ILE A 936    12040   7841  13036    695  -2820    489       C  
ATOM   2713  O   ILE A 936      -1.144 174.256-197.350  1.00 88.54           O  
ANISOU 2713  O   ILE A 936    12259   8179  13201    606  -2862    879       O  
ATOM   2714  CB  ILE A 936       1.135 172.339-198.573  1.00 80.91           C  
ANISOU 2714  CB  ILE A 936    11289   6472  12981    948  -3072    362       C  
ATOM   2715  CG1 ILE A 936       0.648 171.613-197.313  1.00 81.14           C  
ANISOU 2715  CG1 ILE A 936    11278   6432  13120    920  -3218    904       C  
ATOM   2716  CG2 ILE A 936       2.379 173.197-198.311  1.00 76.52           C  
ANISOU 2716  CG2 ILE A 936    10631   6193  12252   1125  -2980    173       C  
ATOM   2717  CD1 ILE A 936       1.549 170.480-196.867  1.00 83.78           C  
ANISOU 2717  CD1 ILE A 936    11555   6453  13824   1112  -3397   1038       C  
ATOM   2718  N   LYS A 937       0.281 175.519-198.543  1.00 86.40           N  
ANISOU 2718  N   LYS A 937    11977   8075  12776    759  -2661    224       N  
ATOM   2719  CA  LYS A 937      -0.003 176.748-197.809  1.00 81.46           C  
ANISOU 2719  CA  LYS A 937    11295   7845  11812    721  -2555    320       C  
ATOM   2720  C   LYS A 937      -1.456 177.171-197.989  1.00 78.12           C  
ANISOU 2720  C   LYS A 937    10938   7534  11211    524  -2481    457       C  
ATOM   2721  O   LYS A 937      -2.116 177.581-197.031  1.00 76.08           O  
ANISOU 2721  O   LYS A 937    10640   7519  10749    473  -2468    723       O  
ATOM   2722  CB  LYS A 937       0.961 177.861-198.224  1.00 77.70           C  
ANISOU 2722  CB  LYS A 937    10743   7535  11245    811  -2393    -19       C  
ATOM   2723  CG  LYS A 937       2.251 177.845-197.435  1.00 82.79           C  
ANISOU 2723  CG  LYS A 937    11238   8235  11982    997  -2485    -70       C  
ATOM   2724  CD  LYS A 937       1.941 177.722-195.944  1.00 91.29           C  
ANISOU 2724  CD  LYS A 937    12274   9519  12891   1036  -2648    268       C  
ATOM   2725  CE  LYS A 937       3.195 177.527-195.103  1.00 97.33           C  
ANISOU 2725  CE  LYS A 937    12895  10344  13741   1256  -2815    236       C  
ATOM   2726  NZ  LYS A 937       2.871 177.470-193.645  1.00101.21           N1+
ANISOU 2726  NZ  LYS A 937    13369  11113  13972   1337  -2971    569       N1+
ATOM   2727  N   LEU A 938      -1.954 177.041-199.217  1.00 77.96           N  
ANISOU 2727  N   LEU A 938    11011   7351  11259    436  -2442    266       N  
ATOM   2728  CA  LEU A 938      -3.364 177.291-199.497  1.00 82.28           C  
ANISOU 2728  CA  LEU A 938    11601   7962  11701    254  -2419    379       C  
ATOM   2729  C   LEU A 938      -4.215 176.406-198.606  1.00 92.10           C  
ANISOU 2729  C   LEU A 938    12800   9101  13095    148  -2551    786       C  
ATOM   2730  O   LEU A 938      -5.273 176.814-198.132  1.00 93.40           O  
ANISOU 2730  O   LEU A 938    12922   9448  13117     26  -2498   1022       O  
ATOM   2731  CB  LEU A 938      -3.703 177.006-200.960  1.00 80.46           C  
ANISOU 2731  CB  LEU A 938    11478   7539  11553    216  -2438     94       C  
ATOM   2732  CG  LEU A 938      -2.917 177.771-202.022  1.00 81.57           C  
ANISOU 2732  CG  LEU A 938    11679   7773  11539    340  -2267   -267       C  
ATOM   2733  CD1 LEU A 938      -3.215 177.215-203.398  1.00 83.17           C  
ANISOU 2733  CD1 LEU A 938    12009   7793  11797    356  -2331   -543       C  
ATOM   2734  CD2 LEU A 938      -3.246 179.249-201.965  1.00 81.15           C  
ANISOU 2734  CD2 LEU A 938    11599   8049  11184    303  -2069   -242       C  
ATOM   2735  N   LEU A 939      -3.745 175.185-198.379  1.00 99.18           N  
ANISOU 2735  N   LEU A 939    13688   9688  14306    204  -2704    889       N  
ATOM   2736  CA  LEU A 939      -4.472 174.263-197.525  1.00101.81           C  
ANISOU 2736  CA  LEU A 939    13963   9873  14847    113  -2805   1340       C  
ATOM   2737  C   LEU A 939      -4.401 174.787-196.101  1.00103.72           C  
ANISOU 2737  C   LEU A 939    14137  10484  14788    191  -2729   1686       C  
ATOM   2738  O   LEU A 939      -5.417 174.866-195.406  1.00105.76           O  
ANISOU 2738  O   LEU A 939    14340  10896  14946     87  -2668   2046       O  
ATOM   2739  CB  LEU A 939      -3.870 172.863-197.615  1.00100.98           C  
ANISOU 2739  CB  LEU A 939    13860   9317  15191    184  -2984   1374       C  
ATOM   2740  CG  LEU A 939      -4.720 171.739-197.039  1.00104.79           C  
ANISOU 2740  CG  LEU A 939    14272   9504  16039     54  -3088   1832       C  
ATOM   2741  CD1 LEU A 939      -6.146 171.872-197.546  1.00105.85           C  
ANISOU 2741  CD1 LEU A 939    14373   9607  16239   -192  -3068   1854       C  
ATOM   2742  CD2 LEU A 939      -4.123 170.401-197.438  1.00107.16           C  
ANISOU 2742  CD2 LEU A 939    14581   9273  16863    122  -3278   1748       C  
ATOM   2743  N   SER A 940      -3.198 175.182-195.695  1.00102.72           N  
ANISOU 2743  N   SER A 940    14000  10521  14509    390  -2733   1547       N  
ATOM   2744  CA  SER A 940      -2.950 175.580-194.321  1.00102.55           C  
ANISOU 2744  CA  SER A 940    13919  10856  14191    523  -2724   1811       C  
ATOM   2745  C   SER A 940      -3.858 176.739-193.944  1.00 97.30           C  
ANISOU 2745  C   SER A 940    13230  10588  13151    442  -2563   1857       C  
ATOM   2746  O   SER A 940      -4.574 176.679-192.943  1.00 95.70           O  
ANISOU 2746  O   SER A 940    12990  10601  12771    438  -2523   2248       O  
ATOM   2747  CB  SER A 940      -1.482 175.959-194.132  1.00104.44           C  
ANISOU 2747  CB  SER A 940    14119  11201  14363    743  -2784   1532       C  
ATOM   2748  OG  SER A 940      -1.236 176.325-192.789  1.00109.12           O  
ANISOU 2748  OG  SER A 940    14653  12163  14646    900  -2828   1740       O  
ATOM   2749  N   THR A 941      -3.844 177.774-194.778  1.00 94.83           N  
ANISOU 2749  N   THR A 941    12934  10363  12733    389  -2454   1474       N  
ATOM   2750  CA  THR A 941      -4.696 178.944-194.594  1.00 90.58           C  
ANISOU 2750  CA  THR A 941    12369  10150  11898    316  -2301   1459       C  
ATOM   2751  C   THR A 941      -6.169 178.542-194.641  1.00 88.45           C  
ANISOU 2751  C   THR A 941    12089   9827  11690    128  -2257   1768       C  
ATOM   2752  O   THR A 941      -6.985 179.045-193.862  1.00 87.17           O  
ANISOU 2752  O   THR A 941    11868   9961  11291    109  -2153   1991       O  
ATOM   2753  CB  THR A 941      -4.411 180.009-195.673  1.00 84.21           C  
ANISOU 2753  CB  THR A 941    11585   9355  11056    290  -2189   1031       C  
ATOM   2754  OG1 THR A 941      -3.000 180.089-195.902  1.00 83.10           O  
ANISOU 2754  OG1 THR A 941    11428   9136  11012    432  -2226    750       O  
ATOM   2755  CG2 THR A 941      -4.920 181.366-195.239  1.00 81.32           C  
ANISOU 2755  CG2 THR A 941    11164   9337  10398    286  -2049    978       C  
ATOM   2756  N   LYS A 942      -6.495 177.612-195.537  1.00 87.92           N  
ANISOU 2756  N   LYS A 942    12059   9380  11968      1  -2344   1762       N  
ATOM   2757  CA  LYS A 942      -7.863 177.136-195.676  1.00 90.00           C  
ANISOU 2757  CA  LYS A 942    12270   9526  12401   -198  -2340   2019       C  
ATOM   2758  C   LYS A 942      -8.272 176.472-194.376  1.00 94.88           C  
ANISOU 2758  C   LYS A 942    12802  10215  13034   -188  -2320   2555       C  
ATOM   2759  O   LYS A 942      -9.435 176.517-193.975  1.00 96.80           O  
ANISOU 2759  O   LYS A 942    12948  10573  13261   -310  -2219   2861       O  
ATOM   2760  CB  LYS A 942      -7.974 176.147-196.839  1.00 91.01           C  
ANISOU 2760  CB  LYS A 942    12440   9193  12945   -307  -2496   1851       C  
ATOM   2761  CG  LYS A 942      -9.393 175.750-197.195  1.00 95.36           C  
ANISOU 2761  CG  LYS A 942    12904   9593  13735   -530  -2532   2008       C  
ATOM   2762  CD  LYS A 942      -9.783 174.413-196.587  1.00102.54           C  
ANISOU 2762  CD  LYS A 942    13712  10184  15063   -624  -2622   2434       C  
ATOM   2763  CE  LYS A 942     -11.270 174.157-196.752  1.00107.31           C  
ANISOU 2763  CE  LYS A 942    14162  10682  15928   -862  -2626   2638       C  
ATOM   2764  NZ  LYS A 942     -11.651 172.775-196.359  1.00113.80           N1+
ANISOU 2764  NZ  LYS A 942    14857  11085  17295   -985  -2720   3029       N1+
ATOM   2765  N   VAL A 943      -7.295 175.865-193.714  1.00 98.17           N  
ANISOU 2765  N   VAL A 943    13243  10580  13478    -23  -2406   2689       N  
ATOM   2766  CA  VAL A 943      -7.536 175.197-192.447  1.00101.63           C  
ANISOU 2766  CA  VAL A 943    13620  11108  13888     40  -2382   3248       C  
ATOM   2767  C   VAL A 943      -7.675 176.238-191.351  1.00101.02           C  
ANISOU 2767  C   VAL A 943    13517  11603  13265    183  -2236   3358       C  
ATOM   2768  O   VAL A 943      -8.480 176.085-190.431  1.00103.85           O  
ANISOU 2768  O   VAL A 943    13803  12175  13482    183  -2108   3819       O  
ATOM   2769  CB  VAL A 943      -6.391 174.220-192.113  1.00102.66           C  
ANISOU 2769  CB  VAL A 943    13789  11005  14212    211  -2549   3355       C  
ATOM   2770  CG1 VAL A 943      -6.471 173.758-190.665  1.00107.55           C  
ANISOU 2770  CG1 VAL A 943    14366  11843  14654    358  -2510   3949       C  
ATOM   2771  CG2 VAL A 943      -6.419 173.038-193.069  1.00102.14           C  
ANISOU 2771  CG2 VAL A 943    13729  10339  14740     75  -2691   3299       C  
ATOM   2772  N   ALA A 944      -6.908 177.316-191.476  1.00 97.81           N  
ANISOU 2772  N   ALA A 944    13153  11437  12573    309  -2242   2917       N  
ATOM   2773  CA  ALA A 944      -6.831 178.321-190.422  1.00 97.00           C  
ANISOU 2773  CA  ALA A 944    13025  11858  11973    486  -2158   2910       C  
ATOM   2774  C   ALA A 944      -8.152 179.051-190.222  1.00 93.72           C  
ANISOU 2774  C   ALA A 944    12544  11712  11355    380  -1953   3026       C  
ATOM   2775  O   ALA A 944      -8.593 179.265-189.090  1.00 95.84           O  
ANISOU 2775  O   ALA A 944    12768  12370  11278    503  -1845   3314       O  
ATOM   2776  CB  ALA A 944      -5.713 179.320-190.715  1.00 94.57           C  
ANISOU 2776  CB  ALA A 944    12737  11661  11534    611  -2224   2367       C  
ATOM   2777  N   VAL A 945      -8.784 179.426-191.326  1.00 87.91           N  
ANISOU 2777  N   VAL A 945    11797  10789  10816    178  -1900   2801       N  
ATOM   2778  CA  VAL A 945      -9.955 180.284-191.265  1.00 86.69           C  
ANISOU 2778  CA  VAL A 945    11564  10883  10492     94  -1721   2826       C  
ATOM   2779  C   VAL A 945     -11.231 179.540-191.620  1.00 91.43           C  
ANISOU 2779  C   VAL A 945    12072  11266  11403   -135  -1665   3162       C  
ATOM   2780  O   VAL A 945     -12.230 180.150-191.978  1.00 88.31           O  
ANISOU 2780  O   VAL A 945    11596  10956  11003   -251  -1556   3116       O  
ATOM   2781  CB  VAL A 945      -9.786 181.492-192.192  1.00 81.92           C  
ANISOU 2781  CB  VAL A 945    10990  10291   9847     66  -1698   2321       C  
ATOM   2782  CG1 VAL A 945      -8.648 182.370-191.698  1.00 79.76           C  
ANISOU 2782  CG1 VAL A 945    10744  10249   9311    279  -1729   1998       C  
ATOM   2783  CG2 VAL A 945      -9.527 181.031-193.615  1.00 81.03           C  
ANISOU 2783  CG2 VAL A 945    10947   9750  10091    -73  -1810   2097       C  
ATOM   2784  N   HIS A 946     -11.205 178.220-191.502  1.00103.16           N  
ANISOU 2784  N   HIS A 946    13542  12450  13203   -198  -1748   3505       N  
ATOM   2785  CA  HIS A 946     -12.366 177.432-191.887  1.00111.53           C  
ANISOU 2785  CA  HIS A 946    14475  13225  14676   -440  -1726   3798       C  
ATOM   2786  C   HIS A 946     -13.520 177.534-190.892  1.00109.72           C  
ANISOU 2786  C   HIS A 946    14080  13304  14306   -463  -1487   4283       C  
ATOM   2787  O   HIS A 946     -14.685 177.445-191.280  1.00110.75           O  
ANISOU 2787  O   HIS A 946    14054  13327  14699   -668  -1420   4405       O  
ATOM   2788  CB  HIS A 946     -11.994 175.969-192.128  1.00120.09           C  
ANISOU 2788  CB  HIS A 946    15571  13814  16245   -513  -1894   3995       C  
ATOM   2789  CG  HIS A 946     -13.006 175.226-192.941  1.00127.51           C  
ANISOU 2789  CG  HIS A 946    16383  14337  17729   -788  -1963   4069       C  
ATOM   2790  ND1 HIS A 946     -13.787 174.218-192.419  1.00134.57           N  
ANISOU 2790  ND1 HIS A 946    17104  15018  19007   -925  -1905   4615       N  
ATOM   2791  CD2 HIS A 946     -13.384 175.365-194.235  1.00128.51           C  
ANISOU 2791  CD2 HIS A 946    16511  14230  18087   -942  -2097   3661       C  
ATOM   2792  CE1 HIS A 946     -14.593 173.757-193.359  1.00137.33           C  
ANISOU 2792  CE1 HIS A 946    17334  14988  19856  -1171  -2024   4499       C  
ATOM   2793  NE2 HIS A 946     -14.369 174.437-194.470  1.00133.72           N  
ANISOU 2793  NE2 HIS A 946    16992  14535  19280  -1171  -2157   3910       N  
ATOM   2794  N   SER A 947     -13.202 177.728-189.617  1.00108.43           N  
ANISOU 2794  N   SER A 947    13935  13544  13717   -236  -1362   4547       N  
ATOM   2795  CA  SER A 947     -14.241 177.875-188.603  1.00112.72           C  
ANISOU 2795  CA  SER A 947    14328  14457  14043   -204  -1089   5013       C  
ATOM   2796  C   SER A 947     -15.111 179.107-188.859  1.00110.63           C  
ANISOU 2796  C   SER A 947    13975  14472  13587   -248   -944   4745       C  
ATOM   2797  O   SER A 947     -16.337 179.058-188.711  1.00115.48           O  
ANISOU 2797  O   SER A 947    14394  15151  14331   -376   -754   5048       O  
ATOM   2798  CB  SER A 947     -13.629 177.923-187.201  1.00117.19           C  
ANISOU 2798  CB  SER A 947    14967  15475  14085    114  -1005   5283       C  
ATOM   2799  OG  SER A 947     -12.584 178.874-187.134  1.00116.89           O  
ANISOU 2799  OG  SER A 947    15075  15687  13650    328  -1133   4759       O  
ATOM   2800  N   PHE A 948     -14.475 180.203-189.259  1.00104.81           N  
ANISOU 2800  N   PHE A 948    13358  13874  12593   -142  -1028   4189       N  
ATOM   2801  CA  PHE A 948     -15.188 181.444-189.555  1.00102.76           C  
ANISOU 2801  CA  PHE A 948    13027  13840  12179   -158   -910   3902       C  
ATOM   2802  C   PHE A 948     -15.997 181.340-190.840  1.00100.56           C  
ANISOU 2802  C   PHE A 948    12661  13202  12344   -428   -980   3783       C  
ATOM   2803  O   PHE A 948     -17.093 181.890-190.932  1.00102.18           O  
ANISOU 2803  O   PHE A 948    12712  13546  12567   -500   -844   3821       O  
ATOM   2804  CB  PHE A 948     -14.212 182.611-189.660  1.00 99.89           C  
ANISOU 2804  CB  PHE A 948    12798  13650  11504     23   -988   3359       C  
ATOM   2805  CG  PHE A 948     -13.390 182.818-188.426  1.00100.05           C  
ANISOU 2805  CG  PHE A 948    12889  14048  11078    309   -979   3373       C  
ATOM   2806  CD1 PHE A 948     -13.844 183.636-187.408  1.00101.76           C  
ANISOU 2806  CD1 PHE A 948    13041  14767  10858    505   -798   3391       C  
ATOM   2807  CD2 PHE A 948     -12.166 182.194-188.283  1.00 99.44           C  
ANISOU 2807  CD2 PHE A 948    12933  13840  11011    408  -1169   3342       C  
ATOM   2808  CE1 PHE A 948     -13.093 183.832-186.273  1.00104.35           C  
ANISOU 2808  CE1 PHE A 948    13437  15479  10733    801   -829   3356       C  
ATOM   2809  CE2 PHE A 948     -11.408 182.385-187.149  1.00102.90           C  
ANISOU 2809  CE2 PHE A 948    13423  14648  11025    694  -1206   3334       C  
ATOM   2810  CZ  PHE A 948     -11.873 183.206-186.141  1.00105.36           C  
ANISOU 2810  CZ  PHE A 948    13683  15481  10869    895  -1048   3331       C  
ATOM   2811  N   VAL A 949     -15.442 180.643-191.829  1.00 97.65           N  
ANISOU 2811  N   VAL A 949    12390  12394  12320   -550  -1207   3614       N  
ATOM   2812  CA  VAL A 949     -16.132 180.400-193.090  1.00 95.13           C  
ANISOU 2812  CA  VAL A 949    12007  11732  12407   -777  -1334   3469       C  
ATOM   2813  C   VAL A 949     -17.400 179.595-192.848  1.00 99.75           C  
ANISOU 2813  C   VAL A 949    12349  12199  13352   -973  -1257   3922       C  
ATOM   2814  O   VAL A 949     -18.472 179.917-193.370  1.00100.89           O  
ANISOU 2814  O   VAL A 949    12332  12334  13669  -1110  -1240   3885       O  
ATOM   2815  CB  VAL A 949     -15.237 179.633-194.078  1.00 93.56           C  
ANISOU 2815  CB  VAL A 949    11961  11098  12488   -831  -1590   3214       C  
ATOM   2816  CG1 VAL A 949     -16.067 179.055-195.212  1.00 93.38           C  
ANISOU 2816  CG1 VAL A 949    11848  10715  12917  -1058  -1754   3135       C  
ATOM   2817  CG2 VAL A 949     -14.146 180.542-194.616  1.00 91.58           C  
ANISOU 2817  CG2 VAL A 949    11902  10929  11967   -678  -1642   2733       C  
ATOM   2818  N   GLU A 950     -17.280 178.548-192.043  1.00103.16           N  
ANISOU 2818  N   GLU A 950    12733  12536  13927   -980  -1209   4374       N  
ATOM   2819  CA  GLU A 950     -18.436 177.716-191.765  1.00109.36           C  
ANISOU 2819  CA  GLU A 950    13253  13165  15133  -1179  -1106   4865       C  
ATOM   2820  C   GLU A 950     -19.453 178.498-190.947  1.00112.15           C  
ANISOU 2820  C   GLU A 950    13415  13985  15212  -1124   -791   5121       C  
ATOM   2821  O   GLU A 950     -20.660 178.376-191.158  1.00114.38           O  
ANISOU 2821  O   GLU A 950    13433  14194  15832  -1312   -714   5302       O  
ATOM   2822  CB  GLU A 950     -18.035 176.434-191.044  1.00113.26           C  
ANISOU 2822  CB  GLU A 950    13737  13437  15858  -1177  -1092   5357       C  
ATOM   2823  CG  GLU A 950     -18.946 175.274-191.359  1.00120.75           C  
ANISOU 2823  CG  GLU A 950    14433  13913  17532  -1466  -1136   5700       C  
ATOM   2824  CD  GLU A 950     -18.180 174.006-191.645  1.00130.40           C  
ANISOU 2824  CD  GLU A 950    15742  14603  19201  -1521  -1364   5759       C  
ATOM   2825  OE1 GLU A 950     -17.086 173.834-191.066  1.00132.09           O  
ANISOU 2825  OE1 GLU A 950    16155  14908  19126  -1306  -1370   5835       O  
ATOM   2826  OE2 GLU A 950     -18.666 173.186-192.454  1.00136.21           O1-
ANISOU 2826  OE2 GLU A 950    16336  14822  20596  -1767  -1558   5701       O1-
ATOM   2827  N   ASN A 951     -18.957 179.307-190.019  1.00113.11           N  
ANISOU 2827  N   ASN A 951    13653  14591  14734   -854   -622   5102       N  
ATOM   2828  CA  ASN A 951     -19.829 180.112-189.174  1.00119.07           C  
ANISOU 2828  CA  ASN A 951    14247  15838  15156   -743   -310   5288       C  
ATOM   2829  C   ASN A 951     -20.673 181.071-190.013  1.00112.96           C  
ANISOU 2829  C   ASN A 951    13355  15089  14476   -841   -323   4936       C  
ATOM   2830  O   ASN A 951     -21.900 181.118-189.883  1.00114.54           O  
ANISOU 2830  O   ASN A 951    13280  15374  14866   -948   -145   5188       O  
ATOM   2831  CB  ASN A 951     -18.995 180.866-188.135  1.00126.06           C  
ANISOU 2831  CB  ASN A 951    15311  17222  15363   -401   -203   5184       C  
ATOM   2832  CG  ASN A 951     -19.845 181.652-187.151  1.00133.13           C  
ANISOU 2832  CG  ASN A 951    16054  18668  15862   -233    132   5361       C  
ATOM   2833  OD1 ASN A 951     -21.056 181.450-187.050  1.00137.09           O  
ANISOU 2833  OD1 ASN A 951    16293  19195  16601   -366    343   5707       O  
ATOM   2834  ND2 ASN A 951     -19.207 182.554-186.413  1.00133.82           N  
ANISOU 2834  ND2 ASN A 951    16286  19198  15361     73    179   5097       N  
ATOM   2835  N   LEU A 952     -20.001 181.819-190.883  1.00107.66           N  
ANISOU 2835  N   LEU A 952    12877  14336  13694   -796   -528   4380       N  
ATOM   2836  CA  LEU A 952     -20.664 182.738-191.801  1.00107.27           C  
ANISOU 2836  CA  LEU A 952    12754  14277  13726   -861   -579   4038       C  
ATOM   2837  C   LEU A 952     -21.668 182.012-192.690  1.00110.53           C  
ANISOU 2837  C   LEU A 952    12957  14330  14709  -1142   -713   4151       C  
ATOM   2838  O   LEU A 952     -22.818 182.439-192.815  1.00112.52           O  
ANISOU 2838  O   LEU A 952    12969  14690  15092  -1211   -619   4213       O  
ATOM   2839  CB  LEU A 952     -19.628 183.459-192.668  1.00104.25           C  
ANISOU 2839  CB  LEU A 952    12629  13794  13186   -773   -778   3495       C  
ATOM   2840  CG  LEU A 952     -20.124 184.462-193.714  1.00103.94           C  
ANISOU 2840  CG  LEU A 952    12568  13731  13195   -798   -848   3143       C  
ATOM   2841  CD1 LEU A 952     -20.814 185.648-193.055  1.00104.87           C  
ANISOU 2841  CD1 LEU A 952    12549  14247  13051   -653   -606   3134       C  
ATOM   2842  CD2 LEU A 952     -18.971 184.934-194.586  1.00 99.48           C  
ANISOU 2842  CD2 LEU A 952    12261  13014  12522   -722  -1018   2705       C  
ATOM   2843  N   PHE A 953     -21.230 180.911-193.301  1.00110.68           N  
ANISOU 2843  N   PHE A 953    13048  13917  15089  -1291   -952   4150       N  
ATOM   2844  CA  PHE A 953     -22.086 180.146-194.209  1.00109.76           C  
ANISOU 2844  CA  PHE A 953    12735  13410  15557  -1555  -1151   4171       C  
ATOM   2845  C   PHE A 953     -23.362 179.670-193.524  1.00114.95           C  
ANISOU 2845  C   PHE A 953    13019  14107  16552  -1706   -942   4684       C  
ATOM   2846  O   PHE A 953     -24.462 179.848-194.048  1.00115.25           O  
ANISOU 2846  O   PHE A 953    12801  14096  16892  -1848   -990   4649       O  
ATOM   2847  CB  PHE A 953     -21.340 178.943-194.790  1.00107.32           C  
ANISOU 2847  CB  PHE A 953    12559  12621  15595  -1662  -1425   4095       C  
ATOM   2848  CG  PHE A 953     -20.356 179.296-195.867  1.00101.45           C  
ANISOU 2848  CG  PHE A 953    12113  11759  14676  -1569  -1670   3545       C  
ATOM   2849  CD1 PHE A 953     -20.034 180.615-196.128  1.00 95.26           C  
ANISOU 2849  CD1 PHE A 953    11477  11280  13439  -1395  -1610   3220       C  
ATOM   2850  CD2 PHE A 953     -19.765 178.306-196.631  1.00101.35           C  
ANISOU 2850  CD2 PHE A 953    12215  11315  14981  -1647  -1944   3362       C  
ATOM   2851  CE1 PHE A 953     -19.132 180.938-197.117  1.00 90.38           C  
ANISOU 2851  CE1 PHE A 953    11110  10555  12675  -1306  -1785   2776       C  
ATOM   2852  CE2 PHE A 953     -18.862 178.626-197.625  1.00 96.58           C  
ANISOU 2852  CE2 PHE A 953    11873  10635  14187  -1538  -2126   2876       C  
ATOM   2853  CZ  PHE A 953     -18.548 179.942-197.867  1.00 91.32           C  
ANISOU 2853  CZ  PHE A 953    11346  10293  13060  -1371  -2031   2609       C  
ATOM   2854  N   LYS A 954     -23.205 179.066-192.350  1.00119.57           N  
ANISOU 2854  N   LYS A 954    13557  14789  17086  -1662   -705   5179       N  
ATOM   2855  CA  LYS A 954     -24.336 178.542-191.595  1.00124.43           C  
ANISOU 2855  CA  LYS A 954    13806  15450  18022  -1791   -436   5759       C  
ATOM   2856  C   LYS A 954     -25.256 179.665-191.140  1.00126.78           C  
ANISOU 2856  C   LYS A 954    13913  16231  18026  -1683   -151   5794       C  
ATOM   2857  O   LYS A 954     -26.473 179.496-191.087  1.00129.57           O  
ANISOU 2857  O   LYS A 954    13896  16566  18770  -1844    -17   6069       O  
ATOM   2858  CB  LYS A 954     -23.849 177.738-190.403  1.00126.32           C  
ANISOU 2858  CB  LYS A 954    14083  15750  18162  -1703   -213   6314       C  
ATOM   2859  N   SER A 955     -24.670 180.813-190.815  1.00126.42           N  
ANISOU 2859  N   SER A 955    14098  16598  17336  -1408    -62   5497       N  
ATOM   2860  CA  SER A 955     -25.454 181.958-190.359  1.00130.12           C  
ANISOU 2860  CA  SER A 955    14410  17526  17504  -1262    204   5467       C  
ATOM   2861  C   SER A 955     -26.132 182.693-191.516  1.00124.26           C  
ANISOU 2861  C   SER A 955    13560  16669  16982  -1356      8   5060       C  
ATOM   2862  O   SER A 955     -26.992 183.549-191.299  1.00126.30           O  
ANISOU 2862  O   SER A 955    13617  17224  17148  -1276    198   5050       O  
ATOM   2863  CB  SER A 955     -24.589 182.923-189.547  1.00132.20           C  
ANISOU 2863  CB  SER A 955    14937  18246  17047   -922    349   5264       C  
ATOM   2864  OG  SER A 955     -23.519 183.423-190.327  1.00130.62           O  
ANISOU 2864  OG  SER A 955    15050  17894  16684   -858     60   4727       O  
ATOM   2865  N   ILE A 956     -25.740 182.363-192.743  1.00117.12           N  
ANISOU 2865  N   ILE A 956    12795  15356  16351  -1498   -373   4724       N  
ATOM   2866  CA  ILE A 956     -26.412 182.911-193.918  1.00109.80           C  
ANISOU 2866  CA  ILE A 956    11766  14309  15645  -1581   -601   4381       C  
ATOM   2867  C   ILE A 956     -27.666 182.107-194.252  1.00117.20           C  
ANISOU 2867  C   ILE A 956    12296  14995  17238  -1854   -678   4631       C  
ATOM   2868  O   ILE A 956     -28.751 182.668-194.396  1.00120.10           O  
ANISOU 2868  O   ILE A 956    12376  15506  17751  -1875   -616   4640       O  
ATOM   2869  CB  ILE A 956     -25.492 182.947-195.152  1.00 97.29           C  
ANISOU 2869  CB  ILE A 956    10503  12445  14017  -1577   -972   3898       C  
ATOM   2870  CG1 ILE A 956     -24.427 184.027-194.988  1.00 86.06           C  
ANISOU 2870  CG1 ILE A 956     9406  11271  12021  -1314   -894   3597       C  
ATOM   2871  CG2 ILE A 956     -26.295 183.213-196.415  1.00 94.68           C  
ANISOU 2871  CG2 ILE A 956    10042  11961  13971  -1677  -1250   3623       C  
ATOM   2872  CD1 ILE A 956     -23.330 183.918-195.995  1.00 81.28           C  
ANISOU 2872  CD1 ILE A 956     9119  10409  11354  -1295  -1174   3218       C  
ATOM   2873  N   TRP A 957     -27.516 180.792-194.368  1.00120.89           N  
ANISOU 2873  N   TRP A 957    12716  15066  18151  -2062   -822   4824       N  
ATOM   2874  CA  TRP A 957     -28.648 179.927-194.697  1.00127.48           C  
ANISOU 2874  CA  TRP A 957    13134  15584  19720  -2351   -931   5041       C  
ATOM   2875  C   TRP A 957     -29.220 179.204-193.476  1.00132.70           C  
ANISOU 2875  C   TRP A 957    13477  16290  20655  -2451   -548   5719       C  
ATOM   2876  O   TRP A 957     -29.614 178.040-193.554  1.00135.63           O  
ANISOU 2876  O   TRP A 957    13598  16247  21688  -2709   -632   5995       O  
ATOM   2877  CB  TRP A 957     -28.270 178.932-195.799  1.00126.28           C  
ANISOU 2877  CB  TRP A 957    13075  14888  20019  -2538  -1391   4755       C  
ATOM   2878  CG  TRP A 957     -27.048 178.108-195.505  1.00122.83           C  
ANISOU 2878  CG  TRP A 957    12937  14228  19506  -2510  -1420   4830       C  
ATOM   2879  CD1 TRP A 957     -26.702 177.542-194.312  1.00123.45           C  
ANISOU 2879  CD1 TRP A 957    13010  14356  19540  -2483  -1113   5345       C  
ATOM   2880  CD2 TRP A 957     -26.008 177.767-196.425  1.00117.15           C  
ANISOU 2880  CD2 TRP A 957    12560  13219  18734  -2477  -1772   4384       C  
ATOM   2881  NE1 TRP A 957     -25.514 176.866-194.435  1.00120.43           N  
ANISOU 2881  NE1 TRP A 957    12935  13709  19113  -2441  -1278   5244       N  
ATOM   2882  CE2 TRP A 957     -25.067 176.989-195.724  1.00116.88           C  
ANISOU 2882  CE2 TRP A 957    12695  13044  18670  -2442  -1671   4645       C  
ATOM   2883  CE3 TRP A 957     -25.781 178.043-197.775  1.00113.74           C  
ANISOU 2883  CE3 TRP A 957    12305  12657  18254  -2449  -2151   3803       C  
ATOM   2884  CZ2 TRP A 957     -23.921 176.485-196.326  1.00115.07           C  
ANISOU 2884  CZ2 TRP A 957    12782  12529  18408  -2390  -1932   4321       C  
ATOM   2885  CZ3 TRP A 957     -24.640 177.543-198.371  1.00111.94           C  
ANISOU 2885  CZ3 TRP A 957    12403  12173  17955  -2391  -2384   3490       C  
ATOM   2886  CH2 TRP A 957     -23.725 176.774-197.649  1.00112.78           C  
ANISOU 2886  CH2 TRP A 957    12651  12123  18076  -2368  -2274   3737       C  
ATOM   2887  N   GLY A 958     -29.250 179.904-192.348  1.00135.97           N  
ANISOU 2887  N   GLY A 958    13897  17205  20560  -2230   -120   5986       N  
ATOM   2888  CA  GLY A 958     -29.836 179.373-191.132  1.00144.51           C  
ANISOU 2888  CA  GLY A 958    14683  18445  21779  -2262    316   6665       C  
ATOM   2889  C   GLY A 958     -31.073 180.164-190.760  1.00149.39           C  
ANISOU 2889  C   GLY A 958    14925  19438  22397  -2214    622   6807       C  
ATOM   2890  O   GLY A 958     -31.268 181.283-191.239  1.00148.04           O  
ANISOU 2890  O   GLY A 958    14807  19485  21958  -2081    531   6373       O  
ATOM   2891  N   LEU A 959     -31.911 179.586-189.907  1.00153.34           N  
ANISOU 2891  N   LEU A 959    15031  20007  23223  -2312   1003   7438       N  
ATOM   2892  CA  LEU A 959     -33.152 180.236-189.507  1.00155.27           C  
ANISOU 2892  CA  LEU A 959    14855  20603  23536  -2271   1338   7625       C  
ATOM   2893  C   LEU A 959     -33.261 180.348-187.989  1.00161.20           C  
ANISOU 2893  C   LEU A 959    15541  21884  23823  -2035   1944   8191       C  
ATOM   2894  O   LEU A 959     -33.536 179.359-187.311  1.00168.26           O  
ANISOU 2894  O   LEU A 959    16207  22678  25045  -2158   2225   8842       O  
ATOM   2895  CB  LEU A 959     -34.359 179.472-190.062  1.00157.88           C  
ANISOU 2895  CB  LEU A 959    14632  20515  24841  -2640   1235   7840       C  
ATOM   2896  CG  LEU A 959     -34.400 179.227-191.571  1.00153.57           C  
ANISOU 2896  CG  LEU A 959    14091  19450  24808  -2874    607   7293       C  
ATOM   2897  CD1 LEU A 959     -35.715 178.576-191.981  1.00158.00           C  
ANISOU 2897  CD1 LEU A 959    14030  19665  26338  -3212    522   7494       C  
ATOM   2898  CD2 LEU A 959     -34.175 180.519-192.334  1.00147.39           C  
ANISOU 2898  CD2 LEU A 959    13579  18904  23517  -2658    353   6634       C  
ATOM   2899  N   PRO A 960     -33.029 181.556-187.450  1.00159.48           N  
ANISOU 2899  N   PRO A 960    15527  22232  22838  -1677   2147   7942       N  
ATOM   2900  CA  PRO A 960     -33.240 181.830-186.024  1.00163.83           C  
ANISOU 2900  CA  PRO A 960    16004  23385  22859  -1389   2724   8390       C  
ATOM   2901  C   PRO A 960     -34.723 181.762-185.670  1.00170.08           C  
ANISOU 2901  C   PRO A 960    16197  24321  24107  -1490   3127   8844       C  
ATOM   2902  O   PRO A 960     -35.551 182.272-186.428  1.00170.13           O  
ANISOU 2902  O   PRO A 960    15922  24216  24503  -1607   2976   8548       O  
ATOM   2903  CB  PRO A 960     -32.729 183.268-185.864  1.00159.13           C  
ANISOU 2903  CB  PRO A 960    15731  23252  21477  -1017   2710   7807       C  
ATOM   2904  CG  PRO A 960     -31.811 183.482-187.018  1.00152.24           C  
ANISOU 2904  CG  PRO A 960    15226  21988  20629  -1101   2151   7186       C  
ATOM   2905  CD  PRO A 960     -32.407 182.696-188.143  1.00153.22           C  
ANISOU 2905  CD  PRO A 960    15087  21525  21605  -1500   1830   7208       C  
ATOM   2906  N   ASN A 961     -35.041 181.140-184.537  1.00174.27           N  
ANISOU 2906  N   ASN A 961    16630  25041  24544  -1364   3529   9373       N  
ATOM   2907  CA  ASN A 961     -36.423 180.951-184.098  1.00178.74           C  
ANISOU 2907  CA  ASN A 961    16734  25667  25512  -1383   3849   9677       C  
ATOM   2908  C   ASN A 961     -37.278 180.192-185.112  1.00178.18           C  
ANISOU 2908  C   ASN A 961    16257  24950  26492  -1815   3556   9700       C  
ATOM   2909  O   ASN A 961     -38.492 180.388-185.184  1.00183.35           O  
ANISOU 2909  O   ASN A 961    16484  25624  27559  -1877   3693   9746       O  
ATOM   2910  CB  ASN A 961     -37.077 182.289-183.729  1.00178.02           C  
ANISOU 2910  CB  ASN A 961    16496  26160  24983  -1098   4153   9457       C  
ATOM   2911  CG  ASN A 961     -36.448 182.926-182.505  1.00177.50           C  
ANISOU 2911  CG  ASN A 961    16774  26760  23908   -624   4489   9450       C  
ATOM   2912  OD1 ASN A 961     -35.965 182.233-181.608  1.00180.24           O  
ANISOU 2912  OD1 ASN A 961    17330  27210  23944   -479   4642   9790       O  
ATOM   2913  ND2 ASN A 961     -36.453 184.252-182.461  1.00174.26           N  
ANISOU 2913  ND2 ASN A 961    16414  26802  22993   -359   4580   9030       N  
ATOM   2914  N   ASN A 962     -36.626 179.333-185.893  1.00171.59           N  
ANISOU 2914  N   ASN A 962    15567  23546  26083  -2093   3128   9623       N  
ATOM   2915  CA  ASN A 962     -37.293 178.451-186.853  1.00170.25           C  
ANISOU 2915  CA  ASN A 962    15065  22712  26910  -2486   2775   9582       C  
ATOM   2916  C   ASN A 962     -38.050 179.161-187.978  1.00163.56           C  
ANISOU 2916  C   ASN A 962    13920  21754  26472  -2658   2470   9133       C  
ATOM   2917  O   ASN A 962     -38.750 178.523-188.767  1.00165.77           O  
ANISOU 2917  O   ASN A 962    13887  21535  27562  -2948   2157   9036       O  
ATOM   2918  CB  ASN A 962     -38.208 177.459-186.127  1.00178.48           C  
ANISOU 2918  CB  ASN A 962    15763  23600  28452  -2540   3079  10114       C  
ATOM   2919  CG  ASN A 962     -37.444 176.552-185.184  1.00181.58           C  
ANISOU 2919  CG  ASN A 962    16419  23985  28587  -2411   3280  10559       C  
ATOM   2920  OD1 ASN A 962     -36.287 176.213-185.437  1.00177.63           O  
ANISOU 2920  OD1 ASN A 962    16298  23292  27900  -2426   3014  10432       O  
ATOM   2921  ND2 ASN A 962     -38.086 176.157-184.089  1.00188.61           N  
ANISOU 2921  ND2 ASN A 962    17105  25091  29467  -2268   3749  11089       N  
ATOM   2922  N   LYS A 963     -37.902 180.479-188.055  1.00154.07           N  
ANISOU 2922  N   LYS A 963    12809  21019  24711  -2455   2539   8834       N  
ATOM   2923  CA  LYS A 963     -38.537 181.252-189.112  1.00147.18           C  
ANISOU 2923  CA  LYS A 963    11670  20093  24159  -2564   2233   8397       C  
ATOM   2924  C   LYS A 963     -37.486 181.919-189.994  1.00140.82           C  
ANISOU 2924  C   LYS A 963    11419  19226  22861  -2437   1745   7703       C  
ATOM   2925  O   LYS A 963     -36.343 182.118-189.577  1.00134.80           O  
ANISOU 2925  O   LYS A 963    11164  18638  21418  -2222   1791   7604       O  
ATOM   2926  CB  LYS A 963     -39.482 182.285-188.520  1.00145.49           C  
ANISOU 2926  CB  LYS A 963    11177  20410  23694  -2306   2643   8428       C  
ATOM   2927  N   ALA A 964     -37.879 182.257-191.218  1.00141.70           N  
ANISOU 2927  N   ALA A 964    11438  19090  23310  -2547   1268   7213       N  
ATOM   2928  CA  ALA A 964     -36.974 182.877-192.178  1.00135.07           C  
ANISOU 2928  CA  ALA A 964    11108  18165  22049  -2420    800   6562       C  
ATOM   2929  C   ALA A 964     -37.256 184.372-192.292  1.00129.93           C  
ANISOU 2929  C   ALA A 964    10503  17919  20947  -2120    859   6205       C  
ATOM   2930  O   ALA A 964     -38.362 184.818-191.972  1.00132.53           O  
ANISOU 2930  O   ALA A 964    10385  18481  21489  -2078   1115   6370       O  
ATOM   2931  CB  ALA A 964     -37.113 182.202-193.539  1.00135.75           C  
ANISOU 2931  CB  ALA A 964    11121  17702  22756  -2706    190   6242       C  
ATOM   2932  N   PRO A 965     -36.253 185.155-192.733  1.00122.24           N  
ANISOU 2932  N   PRO A 965    10049  17010  19386  -1906    640   5729       N  
ATOM   2933  CA  PRO A 965     -36.474 186.583-192.978  1.00118.24           C  
ANISOU 2933  CA  PRO A 965     9597  16795  18534  -1631    643   5366       C  
ATOM   2934  C   PRO A 965     -37.695 186.792-193.862  1.00122.32           C  
ANISOU 2934  C   PRO A 965     9675  17187  19615  -1743    388   5250       C  
ATOM   2935  O   PRO A 965     -37.956 185.969-194.744  1.00121.07           O  
ANISOU 2935  O   PRO A 965     9375  16638  19987  -2011    -13   5195       O  
ATOM   2936  CB  PRO A 965     -35.201 187.006-193.709  1.00108.19           C  
ANISOU 2936  CB  PRO A 965     8902  15392  16812  -1515    303   4894       C  
ATOM   2937  CG  PRO A 965     -34.160 186.105-193.161  1.00108.19           C  
ANISOU 2937  CG  PRO A 965     9198  15287  16623  -1583    375   5081       C  
ATOM   2938  CD  PRO A 965     -34.843 184.778-192.950  1.00115.61           C  
ANISOU 2938  CD  PRO A 965     9749  15980  18197  -1893    425   5539       C  
ATOM   2939  N   LEU A 966     -38.439 187.864-193.606  1.00126.42           N  
ANISOU 2939  N   LEU A 966     9964  18033  20036  -1524    605   5198       N  
ATOM   2940  CA  LEU A 966     -39.686 188.120-194.315  1.00131.86           C  
ANISOU 2940  CA  LEU A 966    10176  18657  21266  -1593    400   5128       C  
ATOM   2941  C   LEU A 966     -39.486 188.145-195.829  1.00133.07           C  
ANISOU 2941  C   LEU A 966    10516  18482  21562  -1666   -246   4697       C  
ATOM   2942  O   LEU A 966     -40.207 187.474-196.571  1.00140.18           O  
ANISOU 2942  O   LEU A 966    11079  19113  23069  -1903   -596   4689       O  
ATOM   2943  CB  LEU A 966     -40.308 189.438-193.854  1.00129.94           C  
ANISOU 2943  CB  LEU A 966     9755  18820  20797  -1275    711   5059       C  
ATOM   2944  CG  LEU A 966     -41.702 189.693-194.430  1.00130.79           C  
ANISOU 2944  CG  LEU A 966     9289  18903  21503  -1324    557   5051       C  
ATOM   2945  CD1 LEU A 966     -42.705 188.714-193.847  1.00135.42           C  
ANISOU 2945  CD1 LEU A 966     9264  19461  22727  -1585    820   5536       C  
ATOM   2946  CD2 LEU A 966     -42.153 191.124-194.195  1.00130.19           C  
ANISOU 2946  CD2 LEU A 966     9125  19168  21172   -963    769   4876       C  
ATOM   2947  N   ALA A 967     -38.492 188.908-196.272  1.00125.69           N  
ANISOU 2947  N   ALA A 967    10112  17579  20067  -1452   -401   4340       N  
ATOM   2948  CA  ALA A 967     -38.227 189.100-197.695  1.00121.77           C  
ANISOU 2948  CA  ALA A 967     9848  16852  19567  -1441   -957   3944       C  
ATOM   2949  C   ALA A 967     -37.858 187.803-198.418  1.00123.15           C  
ANISOU 2949  C   ALA A 967    10118  16636  20039  -1728  -1362   3882       C  
ATOM   2950  O   ALA A 967     -38.264 187.589-199.560  1.00122.02           O  
ANISOU 2950  O   ALA A 967     9879  16297  20188  -1806  -1849   3645       O  
ATOM   2951  CB  ALA A 967     -37.141 190.143-197.886  1.00115.72           C  
ANISOU 2951  CB  ALA A 967     9624  16193  18152  -1158   -944   3651       C  
ATOM   2952  N   VAL A 968     -37.093 186.945-197.747  1.00127.00           N  
ANISOU 2952  N   VAL A 968    10789  17017  20449  -1861  -1174   4079       N  
ATOM   2953  CA  VAL A 968     -36.669 185.667-198.316  1.00129.75           C  
ANISOU 2953  CA  VAL A 968    11232  16961  21106  -2122  -1520   4025       C  
ATOM   2954  C   VAL A 968     -37.841 184.720-198.534  1.00134.74           C  
ANISOU 2954  C   VAL A 968    11289  17343  22564  -2425  -1705   4190       C  
ATOM   2955  O   VAL A 968     -38.071 184.236-199.651  1.00138.23           O  
ANISOU 2955  O   VAL A 968    11668  17500  23352  -2553  -2233   3894       O  
ATOM   2956  CB  VAL A 968     -35.649 184.960-197.411  1.00129.72           C  
ANISOU 2956  CB  VAL A 968    11504  16900  20882  -2179  -1236   4267       C  
ATOM   2957  CG1 VAL A 968     -35.366 183.556-197.930  1.00129.47           C  
ANISOU 2957  CG1 VAL A 968    11484  16405  21305  -2464  -1573   4249       C  
ATOM   2958  CG2 VAL A 968     -34.371 185.779-197.319  1.00126.10           C  
ANISOU 2958  CG2 VAL A 968    11613  16622  19676  -1909  -1143   4034       C  
ATOM   2959  N   LYS A 969     -38.570 184.450-197.456  1.00134.42           N  
ANISOU 2959  N   LYS A 969    10816  17415  22841  -2527  -1267   4659       N  
ATOM   2960  CA  LYS A 969     -39.776 183.637-197.529  1.00139.15           C  
ANISOU 2960  CA  LYS A 969    10777  17788  24307  -2821  -1360   4879       C  
ATOM   2961  C   LYS A 969     -40.724 184.169-198.591  1.00139.59           C  
ANISOU 2961  C   LYS A 969    10537  17843  24659  -2788  -1798   4537       C  
ATOM   2962  O   LYS A 969     -41.074 183.452-199.537  1.00143.40           O  
ANISOU 2962  O   LYS A 969    10837  17980  25670  -2993  -2322   4301       O  
ATOM   2963  CB  LYS A 969     -40.492 183.615-196.177  1.00141.76           C  
ANISOU 2963  CB  LYS A 969    10673  18367  24822  -2847   -722   5457       C  
ATOM   2964  CG  LYS A 969     -41.834 182.896-196.206  1.00144.65           C  
ANISOU 2964  CG  LYS A 969    10294  18518  26149  -3147   -754   5726       C  
ATOM   2965  CD  LYS A 969     -41.683 181.447-196.618  1.00145.94           C  
ANISOU 2965  CD  LYS A 969    10356  18118  26977  -3513  -1085   5769       C  
ATOM   2966  CE  LYS A 969     -43.005 180.719-196.506  1.00156.26           C  
ANISOU 2966  CE  LYS A 969    11154  19172  29045  -3686  -1042   5940       C  
ATOM   2967  NZ  LYS A 969     -42.870 179.254-196.730  1.00161.30           N1+
ANISOU 2967  NZ  LYS A 969    11824  19232  30233  -3945  -1276   5956       N1+
ATOM   2968  N   TYR A 970     -41.128 185.428-198.426  1.00136.97           N  
ANISOU 2968  N   TYR A 970    10156  17898  23989  -2510  -1601   4494       N  
ATOM   2969  CA  TYR A 970     -42.073 186.068-199.337  1.00140.63           C  
ANISOU 2969  CA  TYR A 970    10321  18417  24694  -2422  -1975   4222       C  
ATOM   2970  C   TYR A 970     -41.644 185.925-200.793  1.00140.54           C  
ANISOU 2970  C   TYR A 970    10629  18176  24592  -2407  -2664   3720       C  
ATOM   2971  O   TYR A 970     -42.438 185.492-201.640  1.00144.00           O  
ANISOU 2971  O   TYR A 970    10710  18423  25581  -2546  -3150   3529       O  
ATOM   2972  CB  TYR A 970     -42.255 187.547-198.978  1.00139.18           C  
ANISOU 2972  CB  TYR A 970    10196  18661  24024  -2060  -1663   4203       C  
ATOM   2973  CG  TYR A 970     -42.907 188.381-200.062  1.00140.80           C  
ANISOU 2973  CG  TYR A 970    10280  18931  24288  -1879  -2100   3873       C  
ATOM   2974  CD1 TYR A 970     -44.267 188.279-200.324  1.00147.50           C  
ANISOU 2974  CD1 TYR A 970    10469  19762  25812  -1977  -2277   3925       C  
ATOM   2975  CD2 TYR A 970     -42.160 189.276-200.819  1.00136.79           C  
ANISOU 2975  CD2 TYR A 970    10298  18500  23176  -1598  -2329   3537       C  
ATOM   2976  CE1 TYR A 970     -44.864 189.039-201.315  1.00149.47           C  
ANISOU 2976  CE1 TYR A 970    10605  20089  26098  -1782  -2706   3636       C  
ATOM   2977  CE2 TYR A 970     -42.748 190.039-201.810  1.00139.02           C  
ANISOU 2977  CE2 TYR A 970    10483  18852  23486  -1402  -2722   3291       C  
ATOM   2978  CZ  TYR A 970     -44.099 189.917-202.053  1.00145.21           C  
ANISOU 2978  CZ  TYR A 970    10626  19638  24909  -1485  -2924   3336       C  
ATOM   2979  OH  TYR A 970     -44.693 190.675-203.034  1.00147.26           O  
ANISOU 2979  OH  TYR A 970    10783  19986  25183  -1261  -3341   3104       O  
ATOM   2980  N   PHE A 971     -40.383 186.258-201.069  1.00135.80           N  
ANISOU 2980  N   PHE A 971    10686  17606  23307  -2230  -2703   3503       N  
ATOM   2981  CA  PHE A 971     -39.861 186.245-202.433  1.00135.31           C  
ANISOU 2981  CA  PHE A 971    10993  17401  23017  -2147  -3283   3041       C  
ATOM   2982  C   PHE A 971     -39.763 184.842-203.027  1.00138.49           C  
ANISOU 2982  C   PHE A 971    11336  17390  23893  -2440  -3718   2877       C  
ATOM   2983  O   PHE A 971     -39.928 184.657-204.235  1.00141.39           O  
ANISOU 2983  O   PHE A 971    11736  17638  24349  -2417  -4300   2482       O  
ATOM   2984  CB  PHE A 971     -38.494 186.922-202.486  1.00131.38           C  
ANISOU 2984  CB  PHE A 971    11175  17029  21714  -1898  -3137   2901       C  
ATOM   2985  CG  PHE A 971     -38.025 187.220-203.874  1.00132.89           C  
ANISOU 2985  CG  PHE A 971    11743  17183  21567  -1723  -3636   2478       C  
ATOM   2986  CD1 PHE A 971     -38.616 188.239-204.610  1.00136.00           C  
ANISOU 2986  CD1 PHE A 971    12070  17777  21825  -1475  -3849   2331       C  
ATOM   2987  CD2 PHE A 971     -36.995 186.488-204.447  1.00131.57           C  
ANISOU 2987  CD2 PHE A 971    11993  16796  21202  -1779  -3876   2246       C  
ATOM   2988  CE1 PHE A 971     -38.193 188.525-205.894  1.00135.93           C  
ANISOU 2988  CE1 PHE A 971    12418  17776  21452  -1278  -4284   1993       C  
ATOM   2989  CE2 PHE A 971     -36.562 186.766-205.731  1.00132.03           C  
ANISOU 2989  CE2 PHE A 971    12402  16868  20896  -1584  -4297   1874       C  
ATOM   2990  CZ  PHE A 971     -37.162 187.787-206.459  1.00134.24           C  
ANISOU 2990  CZ  PHE A 971    12625  17374  21004  -1329  -4497   1763       C  
ATOM   2991  N   PHE A 972     -39.488 183.854-202.184  1.00137.14           N  
ANISOU 2991  N   PHE A 972    11084  17001  24021  -2692  -3446   3172       N  
ATOM   2992  CA  PHE A 972     -39.452 182.481-202.665  1.00135.51           C  
ANISOU 2992  CA  PHE A 972    10767  16340  24383  -2987  -3839   3034       C  
ATOM   2993  C   PHE A 972     -40.855 181.948-202.961  1.00139.95           C  
ANISOU 2993  C   PHE A 972    10620  16710  25844  -3228  -4140   3036       C  
ATOM   2994  O   PHE A 972     -41.047 181.185-203.910  1.00128.31           O  
ANISOU 2994  O   PHE A 972     9041  14917  24794  -3370  -4722   2666       O  
ATOM   2995  CB  PHE A 972     -38.675 181.576-201.707  1.00134.92           C  
ANISOU 2995  CB  PHE A 972    10835  16051  24376  -3166  -3471   3374       C  
ATOM   2996  CG  PHE A 972     -37.182 181.725-201.825  1.00128.73           C  
ANISOU 2996  CG  PHE A 972    10748  15301  22862  -2982  -3431   3194       C  
ATOM   2997  CD1 PHE A 972     -36.624 182.334-202.939  1.00124.04           C  
ANISOU 2997  CD1 PHE A 972    10578  14807  21745  -2744  -3795   2714       C  
ATOM   2998  CD2 PHE A 972     -36.337 181.259-200.830  1.00126.14           C  
ANISOU 2998  CD2 PHE A 972    10636  14918  22375  -3033  -3025   3523       C  
ATOM   2999  CE1 PHE A 972     -35.256 182.473-203.058  1.00118.69           C  
ANISOU 2999  CE1 PHE A 972    10495  14154  20448  -2582  -3733   2562       C  
ATOM   3000  CE2 PHE A 972     -34.964 181.399-200.943  1.00119.91           C  
ANISOU 3000  CE2 PHE A 972    10445  14156  20961  -2863  -3004   3342       C  
ATOM   3001  CZ  PHE A 972     -34.425 182.006-202.059  1.00116.09           C  
ANISOU 3001  CZ  PHE A 972    10349  13752  20008  -2649  -3348   2858       C  
ATOM   3002  N   ASP A 973     -41.836 182.366-202.165  1.00137.83           N  
ANISOU 3002  N   ASP A 973     9850  16643  25877  -3259  -3755   3420       N  
ATOM   3003  CA  ASP A 973     -43.220 182.031-202.473  1.00144.46           C  
ANISOU 3003  CA  ASP A 973    10091  17341  27454  -3404  -3981   3375       C  
ATOM   3004  C   ASP A 973     -43.620 182.709-203.779  1.00147.16           C  
ANISOU 3004  C   ASP A 973    10483  17819  27610  -3183  -4578   2852       C  
ATOM   3005  O   ASP A 973     -44.407 182.161-204.565  1.00150.77           O  
ANISOU 3005  O   ASP A 973    10757  18055  28476  -3247  -5005   2526       O  
ATOM   3006  CB  ASP A 973     -44.170 182.446-201.344  1.00145.56           C  
ANISOU 3006  CB  ASP A 973     9772  17719  27814  -3401  -3370   3871       C  
ATOM   3007  CG  ASP A 973     -44.132 181.494-200.161  1.00147.15           C  
ANISOU 3007  CG  ASP A 973     9851  17725  28336  -3623  -2832   4387       C  
ATOM   3008  OD1 ASP A 973     -43.020 181.118-199.731  1.00141.17           O  
ANISOU 3008  OD1 ASP A 973     9439  16896  27301  -3675  -2661   4551       O  
ATOM   3009  OD2 ASP A 973     -45.217 181.123-199.663  1.00154.15           O1-
ANISOU 3009  OD2 ASP A 973    10297  18533  29740  -3728  -2581   4645       O1-
ATOM   3010  N   PHE A 974     -43.065 183.899-204.005  1.00145.00           N  
ANISOU 3010  N   PHE A 974    10554  17913  26626  -2870  -4560   2762       N  
ATOM   3011  CA  PHE A 974     -43.298 184.630-205.248  1.00147.07           C  
ANISOU 3011  CA  PHE A 974    10943  18343  26594  -2601  -5103   2324       C  
ATOM   3012  C   PHE A 974     -42.750 183.869-206.450  1.00149.17           C  
ANISOU 3012  C   PHE A 974    11521  18353  26803  -2632  -5757   1821       C  
ATOM   3013  O   PHE A 974     -43.450 183.695-207.444  1.00153.85           O  
ANISOU 3013  O   PHE A 974    12034  18894  27527  -2559  -6234   1435       O  
ATOM   3014  CB  PHE A 974     -42.698 186.037-205.188  1.00140.18           C  
ANISOU 3014  CB  PHE A 974    10553  17860  24851  -2204  -4812   2350       C  
ATOM   3015  CG  PHE A 974     -42.857 186.815-206.464  1.00138.92           C  
ANISOU 3015  CG  PHE A 974    10570  17877  24337  -1894  -5329   1975       C  
ATOM   3016  CD1 PHE A 974     -44.111 187.196-206.906  1.00142.38           C  
ANISOU 3016  CD1 PHE A 974    10491  18430  25178  -1825  -5641   1910       C  
ATOM   3017  CD2 PHE A 974     -41.756 187.169-207.222  1.00135.05           C  
ANISOU 3017  CD2 PHE A 974    10748  17451  23115  -1655  -5493   1717       C  
ATOM   3018  CE1 PHE A 974     -44.266 187.914-208.081  1.00141.81           C  
ANISOU 3018  CE1 PHE A 974    10589  18545  24747  -1505  -6129   1604       C  
ATOM   3019  CE2 PHE A 974     -41.908 187.888-208.398  1.00135.11           C  
ANISOU 3019  CE2 PHE A 974    10924  17647  22763  -1341  -5940   1436       C  
ATOM   3020  CZ  PHE A 974     -43.166 188.258-208.826  1.00137.77           C  
ANISOU 3020  CZ  PHE A 974    10764  18108  23472  -1258  -6269   1385       C  
ATOM   3021  N   LEU A 975     -41.506 183.408-206.348  1.00146.01           N  
ANISOU 3021  N   LEU A 975    11657  17809  26013  -2655  -5632   1777       N  
ATOM   3022  CA  LEU A 975     -40.905 182.576-207.390  1.00147.22           C  
ANISOU 3022  CA  LEU A 975    12112  17700  26124  -2686  -6193   1298       C  
ATOM   3023  C   LEU A 975     -41.698 181.291-207.650  1.00155.96           C  
ANISOU 3023  C   LEU A 975    12882  18392  27984  -2948  -6458   1107       C  
ATOM   3024  O   LEU A 975     -41.951 180.930-208.805  1.00158.80           O  
ANISOU 3024  O   LEU A 975    13345  18667  28325  -2848  -6989    597       O  
ATOM   3025  CB  LEU A 975     -39.454 182.237-207.042  1.00140.09           C  
ANISOU 3025  CB  LEU A 975    11803  16688  24737  -2676  -5897   1346       C  
ATOM   3026  CG  LEU A 975     -38.425 183.249-207.543  1.00131.88           C  
ANISOU 3026  CG  LEU A 975    11425  15962  22722  -2296  -5824   1186       C  
ATOM   3027  CD1 LEU A 975     -37.009 182.815-207.192  1.00125.71           C  
ANISOU 3027  CD1 LEU A 975    11160  15040  21562  -2312  -5559   1215       C  
ATOM   3028  CD2 LEU A 975     -38.581 183.446-209.045  1.00133.21           C  
ANISOU 3028  CD2 LEU A 975    11745  16230  22637  -2067  -6476    674       C  
ATOM   3029  N   ASP A 976     -42.087 180.605-206.578  1.00158.54           N  
ANISOU 3029  N   ASP A 976    12850  18475  28912  -3241  -6038   1525       N  
ATOM   3030  CA  ASP A 976     -42.885 179.388-206.699  1.00165.40           C  
ANISOU 3030  CA  ASP A 976    13395  18914  30535  -3476  -6196   1417       C  
ATOM   3031  C   ASP A 976     -44.169 179.662-207.478  1.00172.34           C  
ANISOU 3031  C   ASP A 976    13933  19894  31656  -3382  -6570   1123       C  
ATOM   3032  O   ASP A 976     -44.486 178.963-208.449  1.00178.86           O  
ANISOU 3032  O   ASP A 976    14763  20491  32704  -3386  -7080    642       O  
ATOM   3033  CB  ASP A 976     -43.202 178.817-205.322  1.00167.15           C  
ANISOU 3033  CB  ASP A 976    13262  18938  31308  -3749  -5597   2029       C  
ATOM   3034  N   GLU A 977     -44.896 180.692-207.054  1.00171.47           N  
ANISOU 3034  N   GLU A 977    13526  20135  31488  -3277  -6316   1398       N  
ATOM   3035  CA  GLU A 977     -46.142 181.073-207.713  1.00176.11           C  
ANISOU 3035  CA  GLU A 977    13765  20858  32291  -3168  -6636   1168       C  
ATOM   3036  C   GLU A 977     -45.921 181.498-209.170  1.00173.73           C  
ANISOU 3036  C   GLU A 977    13825  20752  31434  -2862  -7274    586       C  
ATOM   3037  O   GLU A 977     -46.799 181.312-210.019  1.00178.96           O  
ANISOU 3037  O   GLU A 977    14285  21391  32322  -2807  -7721    230       O  
ATOM   3038  CB  GLU A 977     -46.848 182.172-206.912  1.00176.00           C  
ANISOU 3038  CB  GLU A 977    13400  21204  32267  -3073  -6188   1595       C  
ATOM   3039  CG  GLU A 977     -47.381 181.700-205.562  1.00178.84           C  
ANISOU 3039  CG  GLU A 977    13324  21411  33216  -3342  -5569   2151       C  
ATOM   3040  CD  GLU A 977     -47.546 182.832-204.564  1.00175.68           C  
ANISOU 3040  CD  GLU A 977    12765  21420  32565  -3202  -4980   2613       C  
ATOM   3041  OE1 GLU A 977     -47.283 183.995-204.932  1.00171.95           O  
ANISOU 3041  OE1 GLU A 977    12491  21312  31530  -2904  -5075   2498       O  
ATOM   3042  OE2 GLU A 977     -47.934 182.558-203.409  1.00177.20           O1-
ANISOU 3042  OE2 GLU A 977    12646  21576  33107  -3362  -4408   3095       O1-
ATOM   3043  N   GLN A 978     -44.744 182.053-209.455  1.00165.09           N  
ANISOU 3043  N   GLN A 978    13267  19860  29599  -2651  -7303    504       N  
ATOM   3044  CA  GLN A 978     -44.377 182.418-210.823  1.00162.63           C  
ANISOU 3044  CA  GLN A 978    13380  19755  28658  -2327  -7844      0       C  
ATOM   3045  C   GLN A 978     -44.200 181.174-211.687  1.00162.89           C  
ANISOU 3045  C   GLN A 978    13576  19453  28863  -2411  -8299   -507       C  
ATOM   3046  O   GLN A 978     -44.697 181.117-212.814  1.00167.09           O  
ANISOU 3046  O   GLN A 978    14132  20074  29281  -2233  -8804   -954       O  
ATOM   3047  CB  GLN A 978     -43.091 183.248-210.842  1.00158.43           C  
ANISOU 3047  CB  GLN A 978    13392  19485  27320  -2089  -7706     82       C  
ATOM   3048  CG  GLN A 978     -43.250 184.692-210.367  1.00156.93           C  
ANISOU 3048  CG  GLN A 978    13124  19689  26813  -1870  -7399    451       C  
ATOM   3049  CD  GLN A 978     -44.105 185.539-211.294  1.00161.58           C  
ANISOU 3049  CD  GLN A 978    13628  20589  27176  -1548  -7749    254       C  
ATOM   3050  OE1 GLN A 978     -44.719 186.515-210.865  1.00162.22           O  
ANISOU 3050  OE1 GLN A 978    13437  20905  27294  -1423  -7522    540       O  
ATOM   3051  NE2 GLN A 978     -44.136 185.178-212.571  1.00165.56           N  
ANISOU 3051  NE2 GLN A 978    14369  21111  27424  -1388  -8289   -233       N  
ATOM   3052  N   ALA A 979     -43.489 180.184-211.153  1.00158.82           N  
ANISOU 3052  N   ALA A 979    13169  18557  28618  -2662  -8113   -430       N  
ATOM   3053  CA  ALA A 979     -43.334 178.900-211.828  1.00160.33           C  
ANISOU 3053  CA  ALA A 979    13465  18358  29095  -2760  -8487   -882       C  
ATOM   3054  C   ALA A 979     -44.696 178.252-212.048  1.00166.31           C  
ANISOU 3054  C   ALA A 979    13686  18880  30623  -2917  -8737  -1032       C  
ATOM   3055  O   ALA A 979     -44.905 177.545-213.035  1.00170.51           O  
ANISOU 3055  O   ALA A 979    14267  19247  31273  -2862  -9234  -1557       O  
ATOM   3056  CB  ALA A 979     -42.430 177.981-211.026  1.00157.18           C  
ANISOU 3056  CB  ALA A 979    13200  17563  28956  -3012  -8169   -666       C  
ATOM   3057  N   GLU A 980     -45.621 178.500-211.124  1.00167.67           N  
ANISOU 3057  N   GLU A 980    13341  19048  31317  -3098  -8381   -575       N  
ATOM   3058  CA  GLU A 980     -46.994 178.024-211.277  1.00175.98           C  
ANISOU 3058  CA  GLU A 980    13837  19910  33115  -3238  -8584   -670       C  
ATOM   3059  C   GLU A 980     -47.721 178.788-212.381  1.00177.69           C  
ANISOU 3059  C   GLU A 980    14014  20501  33000  -2942  -9073  -1058       C  
ATOM   3060  O   GLU A 980     -48.617 178.250-213.036  1.00182.89           O  
ANISOU 3060  O   GLU A 980    14380  21003  34105  -2975  -9495  -1406       O  
ATOM   3061  CB  GLU A 980     -47.752 178.142-209.961  1.00177.40           C  
ANISOU 3061  CB  GLU A 980    13491  20029  33882  -3479  -8011    -42       C  
ATOM   3062  N   ARG A 981     -47.328 180.042-212.581  1.00173.74           N  
ANISOU 3062  N   ARG A 981    13803  20487  31722  -2640  -9017   -982       N  
ATOM   3063  CA  ARG A 981     -47.959 180.897-213.579  1.00177.09           C  
ANISOU 3063  CA  ARG A 981    14222  21314  31749  -2312  -9430  -1259       C  
ATOM   3064  C   ARG A 981     -47.454 180.632-214.994  1.00178.99           C  
ANISOU 3064  C   ARG A 981    14930  21648  31431  -2046 -10011  -1866       C  
ATOM   3065  O   ARG A 981     -48.001 181.161-215.960  1.00183.74           O  
ANISOU 3065  O   ARG A 981    15542  22564  31707  -1763 -10420  -2141       O  
ATOM   3066  CB  ARG A 981     -47.767 182.360-213.217  1.00165.24           C  
ANISOU 3066  CB  ARG A 981    12834  20274  29677  -2065  -9117   -895       C  
ATOM   3067  N   LYS A 982     -46.418 179.809-215.120  1.00175.48           N  
ANISOU 3067  N   LYS A 982    14868  20945  30860  -2116 -10034  -2064       N  
ATOM   3068  CA  LYS A 982     -45.823 179.547-216.427  1.00175.60           C  
ANISOU 3068  CA  LYS A 982    15367  21073  30282  -1836 -10516  -2632       C  
ATOM   3069  C   LYS A 982     -45.832 178.072-216.805  1.00181.65           C  
ANISOU 3069  C   LYS A 982    16077  21356  31587  -2019 -10823  -3068       C  
ATOM   3070  O   LYS A 982     -45.261 177.691-217.829  1.00184.01           O  
ANISOU 3070  O   LYS A 982    16777  21700  31441  -1800 -11187  -3564       O  
ATOM   3071  CB  LYS A 982     -44.393 180.074-216.474  1.00165.70           C  
ANISOU 3071  CB  LYS A 982    14738  20041  28178  -1628 -10301  -2551       C  
ATOM   3072  CG  LYS A 982     -44.290 181.568-216.285  1.00159.74           C  
ANISOU 3072  CG  LYS A 982    14105  19765  26824  -1375 -10061  -2181       C  
ATOM   3073  CD  LYS A 982     -42.847 182.013-216.356  1.00152.83           C  
ANISOU 3073  CD  LYS A 982    13846  19061  25161  -1176  -9861  -2117       C  
ATOM   3074  CE  LYS A 982     -42.203 181.542-217.645  1.00156.60           C  
ANISOU 3074  CE  LYS A 982    14809  19616  25077   -918 -10261  -2661       C  
ATOM   3075  NZ  LYS A 982     -42.981 181.980-218.835  1.00160.81           N1+
ANISOU 3075  NZ  LYS A 982    15328  20500  25270   -594 -10715  -2956       N1+
ATOM   3076  N   LYS A 983     -46.480 177.255-215.978  1.00184.16           N  
ANISOU 3076  N   LYS A 983    15895  21213  32864  -2399 -10653  -2868       N  
ATOM   3077  CA  LYS A 983     -46.547 175.813-216.197  1.00189.75           C  
ANISOU 3077  CA  LYS A 983    16482  21382  34231  -2598 -10902  -3217       C  
ATOM   3078  C   LYS A 983     -45.157 175.194-216.329  1.00186.07           C  
ANISOU 3078  C   LYS A 983    16548  20736  33416  -2557 -10850  -3396       C  
ATOM   3079  O   LYS A 983     -44.744 174.794-217.419  1.00189.51           O  
ANISOU 3079  O   LYS A 983    17315  21202  33486  -2328 -11275  -3964       O  
ATOM   3080  CB  LYS A 983     -47.408 175.488-217.416  1.00198.66           C  
ANISOU 3080  CB  LYS A 983    17454  22542  35484  -2436 -11561  -3821       C  
ATOM   3081  N   ILE A 984     -44.438 175.131-215.213  1.00179.56           N  
ANISOU 3081  N   ILE A 984    15795  19742  32686  -2761 -10316  -2906       N  
ATOM   3082  CA  ILE A 984     -43.113 174.531-215.188  1.00174.81           C  
ANISOU 3082  CA  ILE A 984    15656  18938  31825  -2750 -10215  -3011       C  
ATOM   3083  C   ILE A 984     -43.107 173.319-214.278  1.00177.23           C  
ANISOU 3083  C   ILE A 984    15681  18626  33033  -3118  -9966  -2761       C  
ATOM   3084  O   ILE A 984     -43.439 173.418-213.097  1.00175.69           O  
ANISOU 3084  O   ILE A 984    15157  18315  33281  -3376  -9501  -2162       O  
ATOM   3085  CB  ILE A 984     -42.060 175.520-214.691  1.00173.14           C  
ANISOU 3085  CB  ILE A 984    15853  19076  30854  -2631  -9808  -2648       C  
ATOM   3086  CG1 ILE A 984     -42.059 176.765-215.575  1.00172.72           C  
ANISOU 3086  CG1 ILE A 984    16081  19632  29914  -2240 -10021  -2829       C  
ATOM   3087  CG2 ILE A 984     -40.685 174.862-214.662  1.00162.16           C  
ANISOU 3087  CG2 ILE A 984    14923  17462  29229  -2621  -9710  -2767       C  
ATOM   3088  CD1 ILE A 984     -41.024 177.784-215.177  1.00165.53           C  
ANISOU 3088  CD1 ILE A 984    15575  19061  28257  -2088  -9658  -2502       C  
ATOM   3089  N   THR A 985     -42.726 172.175-214.834  1.00186.61           N  
ANISOU 3089  N   THR A 985    16999  19428  34477  -3115 -10263  -3206       N  
ATOM   3090  CA  THR A 985     -42.762 170.919-214.099  1.00189.51           C  
ANISOU 3090  CA  THR A 985    17087  19163  35754  -3430 -10090  -3007       C  
ATOM   3091  C   THR A 985     -41.360 170.414-213.757  1.00184.70           C  
ANISOU 3091  C   THR A 985    16908  18353  34916  -3432  -9852  -2931       C  
ATOM   3092  O   THR A 985     -41.151 169.215-213.570  1.00187.88           O  
ANISOU 3092  O   THR A 985    17222  18227  35938  -3578  -9872  -2986       O  
ATOM   3093  CB  THR A 985     -43.527 169.875-214.891  1.00194.94           C  
ANISOU 3093  CB  THR A 985    17485  19469  37114  -3453 -10611  -3545       C  
ATOM   3094  N   ASP A 986     -40.407 171.336-213.668  1.00176.78           N  
ANISOU 3094  N   ASP A 986    16355  17763  33051  -3260  -9630  -2795       N  
ATOM   3095  CA  ASP A 986     -39.027 170.987-213.354  1.00173.64           C  
ANISOU 3095  CA  ASP A 986    16384  17227  32363  -3237  -9402  -2723       C  
ATOM   3096  C   ASP A 986     -38.529 171.781-212.146  1.00168.07           C  
ANISOU 3096  C   ASP A 986    15741  16719  31399  -3354  -8823  -2034       C  
ATOM   3097  O   ASP A 986     -38.233 172.968-212.261  1.00161.94           O  
ANISOU 3097  O   ASP A 986    15204  16438  29887  -3172  -8741  -1967       O  
ATOM   3098  CB  ASP A 986     -38.129 171.255-214.566  1.00173.22           C  
ANISOU 3098  CB  ASP A 986    16896  17480  31438  -2861  -9730  -3322       C  
ATOM   3099  CG  ASP A 986     -36.762 170.601-214.444  1.00171.91           C  
ANISOU 3099  CG  ASP A 986    17133  17076  31110  -2823  -9593  -3395       C  
ATOM   3100  OD1 ASP A 986     -36.331 170.306-213.309  1.00168.99           O  
ANISOU 3100  OD1 ASP A 986    16695  16440  31073  -3058  -9172  -2879       O  
ATOM   3101  OD2 ASP A 986     -36.115 170.379-215.490  1.00174.22           O1-
ANISOU 3101  OD2 ASP A 986    17808  17464  30925  -2539  -9895  -3962       O1-
ATOM   3102  N   PRO A 987     -38.429 171.120-210.982  1.00170.56           N  
ANISOU 3102  N   PRO A 987    15838  16651  32315  -3637  -8417  -1508       N  
ATOM   3103  CA  PRO A 987     -37.950 171.728-209.732  1.00165.28           C  
ANISOU 3103  CA  PRO A 987    15203  16139  31458  -3756  -7840   -823       C  
ATOM   3104  C   PRO A 987     -36.565 172.366-209.858  1.00158.47           C  
ANISOU 3104  C   PRO A 987    14914  15563  29735  -3555  -7754   -899       C  
ATOM   3105  O   PRO A 987     -36.226 173.267-209.080  1.00154.99           O  
ANISOU 3105  O   PRO A 987    14539  15422  28927  -3571  -7372   -446       O  
ATOM   3106  CB  PRO A 987     -37.890 170.540-208.770  1.00168.85           C  
ANISOU 3106  CB  PRO A 987    15424  16052  32681  -4023  -7540   -403       C  
ATOM   3107  CG  PRO A 987     -38.926 169.594-209.289  1.00177.30           C  
ANISOU 3107  CG  PRO A 987    16098  16736  34533  -4118  -7890   -703       C  
ATOM   3108  CD  PRO A 987     -38.883 169.731-210.783  1.00178.28           C  
ANISOU 3108  CD  PRO A 987    16478  17026  34235  -3850  -8489  -1511       C  
ATOM   3109  N   ASP A 988     -35.780 171.902-210.827  1.00159.36           N  
ANISOU 3109  N   ASP A 988    15423  15589  29539  -3356  -8095  -1471       N  
ATOM   3110  CA  ASP A 988     -34.455 172.461-211.080  1.00154.66           C  
ANISOU 3110  CA  ASP A 988    15383  15257  28125  -3135  -8041  -1606       C  
ATOM   3111  C   ASP A 988     -34.531 173.936-211.462  1.00146.05           C  
ANISOU 3111  C   ASP A 988    14455  14772  26265  -2911  -8070  -1627       C  
ATOM   3112  O   ASP A 988     -33.643 174.713-211.124  1.00134.24           O  
ANISOU 3112  O   ASP A 988    13268  13537  24200  -2820  -7832  -1425       O  
ATOM   3113  CB  ASP A 988     -33.739 171.681-212.183  1.00161.57           C  
ANISOU 3113  CB  ASP A 988    16615  15966  28806  -2917  -8413  -2266       C  
ATOM   3114  CG  ASP A 988     -33.537 170.229-211.828  1.00169.33           C  
ANISOU 3114  CG  ASP A 988    17464  16340  30532  -3097  -8392  -2256       C  
ATOM   3115  OD1 ASP A 988     -33.232 169.947-210.650  1.00167.96           O  
ANISOU 3115  OD1 ASP A 988    17183  15934  30702  -3320  -7984  -1690       O  
ATOM   3116  OD2 ASP A 988     -33.687 169.371-212.726  1.00177.63           O1-
ANISOU 3116  OD2 ASP A 988    18514  17157  31820  -2996  -8782  -2801       O1-
ATOM   3117  N   VAL A 989     -35.592 174.308-212.175  1.00149.10           N  
ANISOU 3117  N   VAL A 989    14627  15369  26656  -2810  -8373  -1869       N  
ATOM   3118  CA  VAL A 989     -35.822 175.695-212.565  1.00143.82           C  
ANISOU 3118  CA  VAL A 989    14061  15265  25321  -2573  -8416  -1857       C  
ATOM   3119  C   VAL A 989     -36.065 176.564-211.344  1.00140.42           C  
ANISOU 3119  C   VAL A 989    13381  15011  24962  -2735  -7958  -1194       C  
ATOM   3120  O   VAL A 989     -35.507 177.652-211.228  1.00137.71           O  
ANISOU 3120  O   VAL A 989    13287  15048  23988  -2566  -7800  -1029       O  
ATOM   3121  CB  VAL A 989     -37.040 175.829-213.489  1.00149.37           C  
ANISOU 3121  CB  VAL A 989    14513  16121  26120  -2450  -8829  -2201       C  
ATOM   3122  CG1 VAL A 989     -37.302 177.292-213.808  1.00139.09           C  
ANISOU 3122  CG1 VAL A 989    13296  15393  24158  -2191  -8836  -2105       C  
ATOM   3123  CG2 VAL A 989     -36.832 175.032-214.757  1.00154.96           C  
ANISOU 3123  CG2 VAL A 989    15463  16718  26697  -2250  -9296  -2882       C  
ATOM   3124  N   LEU A 990     -36.912 176.082-210.440  1.00141.78           N  
ANISOU 3124  N   LEU A 990    13053  14916  25903  -3041  -7729   -805       N  
ATOM   3125  CA  LEU A 990     -37.186 176.798-209.202  1.00137.53           C  
ANISOU 3125  CA  LEU A 990    12239  14547  25468  -3193  -7232   -150       C  
ATOM   3126  C   LEU A 990     -35.906 176.971-208.400  1.00131.85           C  
ANISOU 3126  C   LEU A 990    11839  13847  24413  -3230  -6859    177       C  
ATOM   3127  O   LEU A 990     -35.618 178.069-207.913  1.00126.14           O  
ANISOU 3127  O   LEU A 990    11275  13520  23133  -3080  -6486    485       O  
ATOM   3128  CB  LEU A 990     -38.245 176.078-208.367  1.00142.08           C  
ANISOU 3128  CB  LEU A 990    12250  14808  26928  -3499  -6998    227       C  
ATOM   3129  CG  LEU A 990     -39.617 176.756-208.312  1.00144.77           C  
ANISOU 3129  CG  LEU A 990    12122  15392  27491  -3497  -6985    366       C  
ATOM   3130  CD1 LEU A 990     -40.587 175.956-207.462  1.00149.74           C  
ANISOU 3130  CD1 LEU A 990    12212  15685  28998  -3794  -6713    756       C  
ATOM   3131  CD2 LEU A 990     -39.487 178.177-207.784  1.00139.87           C  
ANISOU 3131  CD2 LEU A 990    11532  15275  26337  -3360  -6664    720       C  
ATOM   3132  N   HIS A 991     -35.133 175.892-208.279  1.00132.03           N  
ANISOU 3132  N   HIS A 991    12052  13464  24648  -3338  -6847    103       N  
ATOM   3133  CA  HIS A 991     -33.865 175.953-207.554  1.00125.99           C  
ANISOU 3133  CA  HIS A 991    11649  12701  23518  -3331  -6468    387       C  
ATOM   3134  C   HIS A 991     -32.935 176.989-208.166  1.00122.20           C  
ANISOU 3134  C   HIS A 991    11766  12668  21998  -2936  -6413    148       C  
ATOM   3135  O   HIS A 991     -32.399 177.839-207.463  1.00116.45           O  
ANISOU 3135  O   HIS A 991    11272  12248  20725  -2800  -5910    503       O  
ATOM   3136  CB  HIS A 991     -33.172 174.595-207.541  1.00126.09           C  
ANISOU 3136  CB  HIS A 991    11780  12185  23943  -3469  -6569    252       C  
ATOM   3137  CG  HIS A 991     -31.850 174.604-206.835  1.00121.90           C  
ANISOU 3137  CG  HIS A 991    11668  11668  22980  -3398  -6151    525       C  
ATOM   3138  ND1 HIS A 991     -31.711 174.248-205.512  1.00121.64           N  
ANISOU 3138  ND1 HIS A 991    11493  11491  23233  -3581  -5655   1153       N  
ATOM   3139  CD2 HIS A 991     -30.613 174.944-207.267  1.00118.65           C  
ANISOU 3139  CD2 HIS A 991    11828  11437  21815  -3116  -6111    268       C  
ATOM   3140  CE1 HIS A 991     -30.440 174.356-205.160  1.00116.10           C  
ANISOU 3140  CE1 HIS A 991    11258  10877  21978  -3413  -5373   1240       C  
ATOM   3141  NE2 HIS A 991     -29.754 174.773-206.206  1.00115.06           N  
ANISOU 3141  NE2 HIS A 991    11548  10925  21244  -3144  -5634    708       N  
ATOM   3142  N   ILE A 992     -32.756 176.901-209.480  1.00127.62           N  
ANISOU 3142  N   ILE A 992    12678  13382  22430  -2745  -6935   -462       N  
ATOM   3143  CA  ILE A 992     -31.928 177.836-210.239  1.00126.84           C  
ANISOU 3143  CA  ILE A 992    13121  13695  21376  -2355  -6920   -702       C  
ATOM   3144  C   ILE A 992     -32.341 179.289-210.023  1.00123.95           C  
ANISOU 3144  C   ILE A 992    12751  13818  20528  -2171  -6629   -402       C  
ATOM   3145  O   ILE A 992     -31.494 180.145-209.783  1.00118.95           O  
ANISOU 3145  O   ILE A 992    12497  13455  19244  -1963  -6237   -227       O  
ATOM   3146  CB  ILE A 992     -31.959 177.520-211.752  1.00133.47           C  
ANISOU 3146  CB  ILE A 992    14119  14547  22046  -2157  -7574  -1398       C  
ATOM   3147  CG1 ILE A 992     -31.120 176.280-212.056  1.00136.62           C  
ANISOU 3147  CG1 ILE A 992    14715  14527  22666  -2217  -7786  -1766       C  
ATOM   3148  CG2 ILE A 992     -31.443 178.700-212.560  1.00131.13           C  
ANISOU 3148  CG2 ILE A 992    14280  14763  20780  -1735  -7536  -1536       C  
ATOM   3149  CD1 ILE A 992     -29.677 176.415-211.655  1.00132.33           C  
ANISOU 3149  CD1 ILE A 992    14656  14027  21596  -2085  -7330  -1599       C  
ATOM   3150  N   TRP A 993     -33.638 179.567-210.110  1.00126.64           N  
ANISOU 3150  N   TRP A 993    12637  14245  21234  -2245  -6828   -358       N  
ATOM   3151  CA  TRP A 993     -34.129 180.919-209.874  1.00124.42           C  
ANISOU 3151  CA  TRP A 993    12297  14389  20589  -2071  -6563    -72       C  
ATOM   3152  C   TRP A 993     -33.792 181.369-208.457  1.00123.47           C  
ANISOU 3152  C   TRP A 993    12174  14341  20398  -2154  -5874    492       C  
ATOM   3153  O   TRP A 993     -33.287 182.474-208.253  1.00120.77           O  
ANISOU 3153  O   TRP A 993    12120  14317  19448  -1922  -5531    650       O  
ATOM   3154  CB  TRP A 993     -35.635 181.013-210.132  1.00127.26           C  
ANISOU 3154  CB  TRP A 993    12095  14789  21470  -2159  -6903   -113       C  
ATOM   3155  CG  TRP A 993     -35.984 181.035-211.587  1.00130.20           C  
ANISOU 3155  CG  TRP A 993    12531  15280  21660  -1942  -7572   -664       C  
ATOM   3156  CD1 TRP A 993     -35.121 181.185-212.632  1.00129.81           C  
ANISOU 3156  CD1 TRP A 993    13010  15388  20922  -1634  -7803  -1050       C  
ATOM   3157  CD2 TRP A 993     -37.290 180.899-212.162  1.00137.00           C  
ANISOU 3157  CD2 TRP A 993    12962  16149  22940  -1963  -7995   -880       C  
ATOM   3158  NE1 TRP A 993     -35.806 181.153-213.821  1.00135.58           N  
ANISOU 3158  NE1 TRP A 993    13685  16256  21575  -1445  -8348  -1486       N  
ATOM   3159  CE2 TRP A 993     -37.139 180.978-213.561  1.00139.42           C  
ANISOU 3159  CE2 TRP A 993    13623  16650  22699  -1630  -8420  -1393       C  
ATOM   3160  CE3 TRP A 993     -38.569 180.717-211.631  1.00142.78           C  
ANISOU 3160  CE3 TRP A 993    13109  16769  24374  -2187  -7924   -667       C  
ATOM   3161  CZ2 TRP A 993     -38.220 180.882-214.435  1.00145.81           C  
ANISOU 3161  CZ2 TRP A 993    14215  17547  23639  -1522  -8809  -1707       C  
ATOM   3162  CZ3 TRP A 993     -39.642 180.621-212.501  1.00148.99           C  
ANISOU 3162  CZ3 TRP A 993    13673  17612  25325  -2090  -8319   -995       C  
ATOM   3163  CH2 TRP A 993     -39.460 180.703-213.887  1.00150.30           C  
ANISOU 3163  CH2 TRP A 993    14198  17975  24933  -1763  -8774  -1515       C  
ATOM   3164  N   LYS A 994     -34.055 180.499-207.486  1.00126.96           N  
ANISOU 3164  N   LYS A 994    12288  14482  21468  -2473  -5680    790       N  
ATOM   3165  CA  LYS A 994     -33.758 180.803-206.089  1.00125.65           C  
ANISOU 3165  CA  LYS A 994    12110  14408  21225  -2537  -5043   1325       C  
ATOM   3166  C   LYS A 994     -32.278 181.134-205.871  1.00123.61           C  
ANISOU 3166  C   LYS A 994    12425  14253  20290  -2348  -4745   1331       C  
ATOM   3167  O   LYS A 994     -31.949 182.054-205.122  1.00121.42           O  
ANISOU 3167  O   LYS A 994    12279  14258  19597  -2213  -4298   1606       O  
ATOM   3168  CB  LYS A 994     -34.198 179.653-205.178  1.00128.47           C  
ANISOU 3168  CB  LYS A 994    12050  14398  22364  -2895  -4907   1661       C  
ATOM   3169  CG  LYS A 994     -35.709 179.511-205.072  1.00134.75           C  
ANISOU 3169  CG  LYS A 994    12191  15137  23870  -3098  -5031   1800       C  
ATOM   3170  CD  LYS A 994     -36.116 178.199-204.418  1.00140.76           C  
ANISOU 3170  CD  LYS A 994    12527  15437  25517  -3474  -4981   2083       C  
ATOM   3171  CE  LYS A 994     -37.615 177.952-204.567  1.00146.54           C  
ANISOU 3171  CE  LYS A 994    12569  16045  27064  -3693  -5216   2116       C  
ATOM   3172  NZ  LYS A 994     -38.005 176.568-204.167  1.00150.95           N1+
ANISOU 3172  NZ  LYS A 994    12834  16092  28429  -3976  -5168   2291       N1+
ATOM   3173  N   THR A 995     -31.392 180.406-206.544  1.00124.54           N  
ANISOU 3173  N   THR A 995    12864  14141  20314  -2324  -5007    994       N  
ATOM   3174  CA  THR A 995     -29.957 180.593-206.343  1.00121.98           C  
ANISOU 3174  CA  THR A 995    13037  13872  19437  -2164  -4739    992       C  
ATOM   3175  C   THR A 995     -29.357 181.694-207.215  1.00121.57           C  
ANISOU 3175  C   THR A 995    13392  14146  18653  -1826  -4771    735       C  
ATOM   3176  O   THR A 995     -28.231 182.128-206.982  1.00120.10           O  
ANISOU 3176  O   THR A 995    13573  14065  17997  -1676  -4483    778       O  
ATOM   3177  CB  THR A 995     -29.172 179.297-206.590  1.00124.90           C  
ANISOU 3177  CB  THR A 995    13568  13836  20051  -2273  -4944    776       C  
ATOM   3178  OG1 THR A 995     -29.176 178.993-207.989  1.00128.79           O  
ANISOU 3178  OG1 THR A 995    14195  14256  20484  -2162  -5468    223       O  
ATOM   3179  CG2 THR A 995     -29.788 178.145-205.816  1.00129.50           C  
ANISOU 3179  CG2 THR A 995    13729  14030  21445  -2615  -4936   1053       C  
ATOM   3180  N   ASN A 996     -30.105 182.131-208.224  1.00122.96           N  
ANISOU 3180  N   ASN A 996    13487  14475  18758  -1700  -5125    483       N  
ATOM   3181  CA  ASN A 996     -29.669 183.215-209.103  1.00116.90           C  
ANISOU 3181  CA  ASN A 996    13071  14026  17318  -1361  -5150    308       C  
ATOM   3182  C   ASN A 996     -30.174 184.559-208.604  1.00115.77           C  
ANISOU 3182  C   ASN A 996    12812  14195  16979  -1242  -4833    619       C  
ATOM   3183  O   ASN A 996     -29.608 185.600-208.926  1.00113.24           O  
ANISOU 3183  O   ASN A 996    12793  14107  16128   -982  -4663    625       O  
ATOM   3184  CB  ASN A 996     -30.172 182.996-210.535  1.00116.88           C  
ANISOU 3184  CB  ASN A 996    13080  14064  17265  -1225  -5731   -133       C  
ATOM   3185  CG  ASN A 996     -29.330 182.002-211.311  1.00115.79           C  
ANISOU 3185  CG  ASN A 996    13234  13719  17042  -1188  -6019   -552       C  
ATOM   3186  OD1 ASN A 996     -28.410 181.392-210.770  1.00112.53           O  
ANISOU 3186  OD1 ASN A 996    12980  13085  16690  -1292  -5800   -498       O  
ATOM   3187  ND2 ASN A 996     -29.648 181.832-212.591  1.00119.23           N  
ANISOU 3187  ND2 ASN A 996    13736  14240  17324  -1013  -6527   -987       N  
ATOM   3188  N   SER A 997     -31.252 184.530-207.827  1.00120.11           N  
ANISOU 3188  N   SER A 997    12905  14734  17998  -1428  -4745    879       N  
ATOM   3189  CA  SER A 997     -31.877 185.756-207.347  1.00121.69           C  
ANISOU 3189  CA  SER A 997    12935  15217  18084  -1308  -4469   1140       C  
ATOM   3190  C   SER A 997     -31.294 186.226-206.019  1.00119.65           C  
ANISOU 3190  C   SER A 997    12749  15039  17674  -1323  -3895   1473       C  
ATOM   3191  O   SER A 997     -30.930 187.394-205.871  1.00118.19           O  
ANISOU 3191  O   SER A 997    12748  15073  17086  -1105  -3630   1543       O  
ATOM   3192  CB  SER A 997     -33.385 185.565-207.201  1.00126.51           C  
ANISOU 3192  CB  SER A 997    12982  15818  19269  -1465  -4647   1238       C  
ATOM   3193  OG  SER A 997     -33.663 184.587-206.216  1.00129.23           O  
ANISOU 3193  OG  SER A 997    13014  15931  20156  -1779  -4485   1472       O  
ATOM   3194  N   LEU A 998     -31.214 185.322-205.048  1.00118.27           N  
ANISOU 3194  N   LEU A 998    12419  14683  17833  -1564  -3712   1679       N  
ATOM   3195  CA  LEU A 998     -30.776 185.724-203.717  1.00114.74           C  
ANISOU 3195  CA  LEU A 998    12004  14363  17228  -1556  -3194   1997       C  
ATOM   3196  C   LEU A 998     -29.266 185.587-203.466  1.00110.46           C  
ANISOU 3196  C   LEU A 998    11905  13762  16303  -1487  -3019   1942       C  
ATOM   3197  O   LEU A 998     -28.601 186.599-203.274  1.00107.53           O  
ANISOU 3197  O   LEU A 998    11777  13582  15498  -1284  -2778   1929       O  
ATOM   3198  CB  LEU A 998     -31.618 185.067-202.614  1.00120.13           C  
ANISOU 3198  CB  LEU A 998    12243  14990  18413  -1796  -2988   2359       C  
ATOM   3199  CG  LEU A 998     -31.197 185.435-201.188  1.00120.16           C  
ANISOU 3199  CG  LEU A 998    12282  15184  18189  -1748  -2456   2689       C  
ATOM   3200  CD1 LEU A 998     -31.311 186.931-200.956  1.00119.14           C  
ANISOU 3200  CD1 LEU A 998    12201  15395  17670  -1489  -2211   2676       C  
ATOM   3201  CD2 LEU A 998     -32.007 184.668-200.154  1.00123.91           C  
ANISOU 3201  CD2 LEU A 998    12327  15613  19141  -1971  -2233   3096       C  
ATOM   3202  N   PRO A 999     -28.709 184.355-203.476  1.00110.49           N  
ANISOU 3202  N   PRO A 999    11995  13479  16509  -1650  -3149   1897       N  
ATOM   3203  CA  PRO A 999     -27.277 184.334-203.142  1.00101.90           C  
ANISOU 3203  CA  PRO A 999    11294  12368  15055  -1557  -2953   1866       C  
ATOM   3204  C   PRO A 999     -26.382 185.019-204.189  1.00 92.42           C  
ANISOU 3204  C   PRO A 999    10490  11241  13386  -1321  -3063   1539       C  
ATOM   3205  O   PRO A 999     -25.565 185.843-203.796  1.00 87.91           O  
ANISOU 3205  O   PRO A 999    10135  10822  12446  -1166  -2781   1572       O  
ATOM   3206  CB  PRO A 999     -26.957 182.836-203.012  1.00103.96           C  
ANISOU 3206  CB  PRO A 999    11533  12275  15694  -1769  -3101   1887       C  
ATOM   3207  CG  PRO A 999     -27.995 182.148-203.802  1.00108.89           C  
ANISOU 3207  CG  PRO A 999    11876  12698  16800  -1926  -3502   1742       C  
ATOM   3208  CD  PRO A 999     -29.233 183.001-203.749  1.00113.12           C  
ANISOU 3208  CD  PRO A 999    12088  13479  17412  -1902  -3462   1860       C  
ATOM   3209  N   LEU A1000     -26.544 184.705-205.474  1.00 92.10           N  
ANISOU 3209  N   LEU A1000    10525  11105  13362  -1283  -3454   1235       N  
ATOM   3210  CA  LEU A1000     -25.728 185.320-206.520  1.00 93.57           C  
ANISOU 3210  CA  LEU A1000    11083  11390  13080  -1036  -3528    971       C  
ATOM   3211  C   LEU A1000     -25.831 186.841-206.499  1.00 98.54           C  
ANISOU 3211  C   LEU A1000    11760  12303  13380   -826  -3293   1078       C  
ATOM   3212  O   LEU A1000     -24.822 187.546-206.414  1.00 99.22           O  
ANISOU 3212  O   LEU A1000    12110  12462  13127   -674  -3042   1077       O  
ATOM   3213  CB  LEU A1000     -26.125 184.813-207.914  1.00 96.36           C  
ANISOU 3213  CB  LEU A1000    11473  11677  13464   -985  -4009    631       C  
ATOM   3214  CG  LEU A1000     -25.500 185.573-209.099  1.00 93.28           C  
ANISOU 3214  CG  LEU A1000    11437  11470  12533   -680  -4073    413       C  
ATOM   3215  CD1 LEU A1000     -24.027 185.224-209.267  1.00 91.56           C  
ANISOU 3215  CD1 LEU A1000    11582  11153  12055   -601  -3941    271       C  
ATOM   3216  CD2 LEU A1000     -26.257 185.354-210.408  1.00 95.41           C  
ANISOU 3216  CD2 LEU A1000    11676  11803  12772   -572  -4558    121       C  
ATOM   3217  N   ARG A1001     -27.059 187.341-206.571  1.00100.48           N  
ANISOU 3217  N   ARG A1001    11719  12679  13780   -819  -3380   1169       N  
ATOM   3218  CA  ARG A1001     -27.292 188.770-206.740  1.00 94.80           C  
ANISOU 3218  CA  ARG A1001    11023  12190  12805   -596  -3225   1247       C  
ATOM   3219  C   ARG A1001     -27.290 189.557-205.439  1.00 88.72           C  
ANISOU 3219  C   ARG A1001    10132  11533  12044   -594  -2796   1491       C  
ATOM   3220  O   ARG A1001     -27.292 190.786-205.462  1.00 89.72           O  
ANISOU 3220  O   ARG A1001    10303  11803  11984   -403  -2622   1538       O  
ATOM   3221  CB  ARG A1001     -28.593 189.015-207.498  1.00 98.26           C  
ANISOU 3221  CB  ARG A1001    11215  12732  13389   -540  -3544   1208       C  
ATOM   3222  CG  ARG A1001     -28.522 188.597-208.945  1.00101.81           C  
ANISOU 3222  CG  ARG A1001    11851  13165  13668   -425  -3978    916       C  
ATOM   3223  CD  ARG A1001     -29.322 189.538-209.812  1.00107.40           C  
ANISOU 3223  CD  ARG A1001    12498  14088  14222   -189  -4170    912       C  
ATOM   3224  NE  ARG A1001     -28.984 189.384-211.221  1.00111.59           N  
ANISOU 3224  NE  ARG A1001    13317  14687  14394     20  -4507    652       N  
ATOM   3225  CZ  ARG A1001     -27.976 190.009-211.820  1.00109.68           C  
ANISOU 3225  CZ  ARG A1001    13467  14538  13667    263  -4343    646       C  
ATOM   3226  NH1 ARG A1001     -27.746 189.806-213.110  1.00112.52           N1+
ANISOU 3226  NH1 ARG A1001    14076  15006  13671    477  -4646    419       N1+
ATOM   3227  NH2 ARG A1001     -27.200 190.836-211.131  1.00103.55           N  
ANISOU 3227  NH2 ARG A1001    12820  13753  12771    302  -3876    857       N  
ATOM   3228  N   PHE A1002     -27.293 188.861-204.309  1.00 83.71           N  
ANISOU 3228  N   PHE A1002     9344  10836  11627   -786  -2628   1645       N  
ATOM   3229  CA  PHE A1002     -27.174 189.551-203.033  1.00 81.87           C  
ANISOU 3229  CA  PHE A1002     9035  10753  11321   -746  -2224   1834       C  
ATOM   3230  C   PHE A1002     -26.017 189.066-202.168  1.00 87.39           C  
ANISOU 3230  C   PHE A1002     9923  11388  11893   -799  -2014   1871       C  
ATOM   3231  O   PHE A1002     -25.069 189.805-201.935  1.00 90.01           O  
ANISOU 3231  O   PHE A1002    10477  11778  11944   -654  -1819   1796       O  
ATOM   3232  CB  PHE A1002     -28.477 189.498-202.238  1.00 80.95           C  
ANISOU 3232  CB  PHE A1002     8487  10750  11522   -849  -2123   2065       C  
ATOM   3233  CG  PHE A1002     -28.354 190.061-200.859  1.00 80.06           C  
ANISOU 3233  CG  PHE A1002     8299  10826  11293   -788  -1706   2238       C  
ATOM   3234  CD1 PHE A1002     -28.431 191.429-200.655  1.00 78.61           C  
ANISOU 3234  CD1 PHE A1002     8121  10823  10923   -570  -1508   2192       C  
ATOM   3235  CD2 PHE A1002     -28.142 189.228-199.767  1.00 81.13           C  
ANISOU 3235  CD2 PHE A1002     8364  10961  11498   -924  -1520   2438       C  
ATOM   3236  CE1 PHE A1002     -28.319 191.959-199.389  1.00 78.62           C  
ANISOU 3236  CE1 PHE A1002     8057  11018  10799   -483  -1151   2281       C  
ATOM   3237  CE2 PHE A1002     -28.017 189.751-198.496  1.00 80.62           C  
ANISOU 3237  CE2 PHE A1002     8250  11130  11251   -823  -1152   2572       C  
ATOM   3238  CZ  PHE A1002     -28.108 191.116-198.306  1.00 78.74           C  
ANISOU 3238  CZ  PHE A1002     8017  11086  10815   -600   -977   2461       C  
ATOM   3239  N   TRP A1003     -26.098 187.834-201.678  1.00 91.41           N  
ANISOU 3239  N   TRP A1003    10322  11764  12647  -1002  -2060   1997       N  
ATOM   3240  CA  TRP A1003     -25.129 187.358-200.691  1.00 92.64           C  
ANISOU 3240  CA  TRP A1003    10610  11892  12696  -1035  -1853   2099       C  
ATOM   3241  C   TRP A1003     -23.684 187.402-201.167  1.00 87.74           C  
ANISOU 3241  C   TRP A1003    10368  11167  11804   -932  -1889   1869       C  
ATOM   3242  O   TRP A1003     -22.782 187.682-200.387  1.00 88.33           O  
ANISOU 3242  O   TRP A1003    10575  11315  11670   -853  -1673   1885       O  
ATOM   3243  CB  TRP A1003     -25.477 185.960-200.193  1.00 99.19           C  
ANISOU 3243  CB  TRP A1003    11255  12547  13887  -1266  -1913   2319       C  
ATOM   3244  CG  TRP A1003     -26.593 185.974-199.214  1.00105.05           C  
ANISOU 3244  CG  TRP A1003    11625  13451  14837  -1345  -1698   2648       C  
ATOM   3245  CD1 TRP A1003     -27.839 185.460-199.393  1.00111.79           C  
ANISOU 3245  CD1 TRP A1003    12118  14225  16133  -1517  -1820   2791       C  
ATOM   3246  CD2 TRP A1003     -26.578 186.553-197.900  1.00105.02           C  
ANISOU 3246  CD2 TRP A1003    11553  13740  14608  -1235  -1313   2863       C  
ATOM   3247  NE1 TRP A1003     -28.601 185.669-198.269  1.00115.90           N  
ANISOU 3247  NE1 TRP A1003    12339  14968  16728  -1528  -1494   3123       N  
ATOM   3248  CE2 TRP A1003     -27.850 186.338-197.338  1.00110.00           C  
ANISOU 3248  CE2 TRP A1003    11782  14473  15541  -1341  -1179   3165       C  
ATOM   3249  CE3 TRP A1003     -25.610 187.222-197.143  1.00101.88           C  
ANISOU 3249  CE3 TRP A1003    11381  13537  13793  -1047  -1080   2807       C  
ATOM   3250  CZ2 TRP A1003     -28.183 186.773-196.052  1.00107.69           C  
ANISOU 3250  CZ2 TRP A1003    11331  14503  15085  -1240   -791   3421       C  
ATOM   3251  CZ3 TRP A1003     -25.944 187.653-195.868  1.00101.46           C  
ANISOU 3251  CZ3 TRP A1003    11176  13797  13578   -946   -744   3018       C  
ATOM   3252  CH2 TRP A1003     -27.219 187.426-195.337  1.00103.50           C  
ANISOU 3252  CH2 TRP A1003    11056  14183  14084  -1031   -588   3328       C  
ATOM   3253  N   VAL A1004     -23.468 187.126-202.444  1.00 85.99           N  
ANISOU 3253  N   VAL A1004    10304  10791  11578   -918  -2165   1643       N  
ATOM   3254  CA  VAL A1004     -22.130 187.209-203.006  1.00 83.95           C  
ANISOU 3254  CA  VAL A1004    10383  10450  11065   -800  -2170   1429       C  
ATOM   3255  C   VAL A1004     -21.647 188.655-202.974  1.00 80.55           C  
ANISOU 3255  C   VAL A1004    10069  10189  10347   -599  -1938   1380       C  
ATOM   3256  O   VAL A1004     -20.484 188.924-202.691  1.00 77.91           O  
ANISOU 3256  O   VAL A1004     9917   9838   9847   -520  -1780   1307       O  
ATOM   3257  CB  VAL A1004     -22.090 186.656-204.441  1.00 88.41           C  
ANISOU 3257  CB  VAL A1004    11088  10868  11638   -784  -2501   1185       C  
ATOM   3258  CG1 VAL A1004     -20.724 186.852-205.059  1.00 87.80           C  
ANISOU 3258  CG1 VAL A1004    11343  10747  11272   -630  -2447    985       C  
ATOM   3259  CG2 VAL A1004     -22.445 185.189-204.427  1.00 91.59           C  
ANISOU 3259  CG2 VAL A1004    11367  11033  12398   -990  -2745   1183       C  
ATOM   3260  N   ASN A1005     -22.562 189.582-203.235  1.00 83.35           N  
ANISOU 3260  N   ASN A1005    10288  10683  10698   -518  -1923   1423       N  
ATOM   3261  CA  ASN A1005     -22.253 191.012-203.252  1.00 81.88           C  
ANISOU 3261  CA  ASN A1005    10175  10609  10327   -326  -1713   1392       C  
ATOM   3262  C   ASN A1005     -21.809 191.561-201.895  1.00 77.40           C  
ANISOU 3262  C   ASN A1005     9553  10141   9713   -294  -1416   1443       C  
ATOM   3263  O   ASN A1005     -21.018 192.506-201.827  1.00 72.83           O  
ANISOU 3263  O   ASN A1005     9095   9565   9013   -159  -1249   1343       O  
ATOM   3264  CB  ASN A1005     -23.463 191.804-203.748  1.00 84.15           C  
ANISOU 3264  CB  ASN A1005    10288  11009  10677   -242  -1782   1455       C  
ATOM   3265  CG  ASN A1005     -23.072 192.995-204.578  1.00 86.91           C  
ANISOU 3265  CG  ASN A1005    10804  11369  10850    -26  -1715   1396       C  
ATOM   3266  OD1 ASN A1005     -21.955 193.502-204.470  1.00 86.05           O  
ANISOU 3266  OD1 ASN A1005    10877  11202  10619     54  -1524   1331       O  
ATOM   3267  ND2 ASN A1005     -23.987 193.448-205.426  1.00 91.16           N  
ANISOU 3267  ND2 ASN A1005    11264  11973  11401     73  -1875   1438       N  
ATOM   3268  N   ILE A1006     -22.331 190.978-200.820  1.00 77.85           N  
ANISOU 3268  N   ILE A1006     9417  10284   9877   -407  -1351   1597       N  
ATOM   3269  CA  ILE A1006     -21.924 191.381-199.480  1.00 84.26           C  
ANISOU 3269  CA  ILE A1006    10189  11246  10579   -345  -1096   1628       C  
ATOM   3270  C   ILE A1006     -20.650 190.626-199.140  1.00 89.11           C  
ANISOU 3270  C   ILE A1006    10996  11760  11101   -383  -1104   1572       C  
ATOM   3271  O   ILE A1006     -19.755 191.135-198.461  1.00 88.64           O  
ANISOU 3271  O   ILE A1006    11022  11766  10892   -278   -959   1465       O  
ATOM   3272  CB  ILE A1006     -23.011 191.085-198.430  1.00 89.73           C  
ANISOU 3272  CB  ILE A1006    10595  12129  11370   -409   -980   1861       C  
ATOM   3273  CG1 ILE A1006     -24.077 192.173-198.448  1.00 97.82           C  
ANISOU 3273  CG1 ILE A1006    11411  13306  12450   -301   -885   1872       C  
ATOM   3274  CG2 ILE A1006     -22.425 191.041-197.043  1.00 89.32           C  
ANISOU 3274  CG2 ILE A1006    10554  12248  11136   -349   -767   1908       C  
ATOM   3275  CD1 ILE A1006     -25.006 192.073-199.615  1.00106.60           C  
ANISOU 3275  CD1 ILE A1006    12421  14321  13761   -359  -1115   1899       C  
ATOM   3276  N   LEU A1007     -20.572 189.404-199.646  1.00 93.59           N  
ANISOU 3276  N   LEU A1007    11619  12151  11790   -524  -1300   1618       N  
ATOM   3277  CA  LEU A1007     -19.402 188.571-199.442  1.00 97.36           C  
ANISOU 3277  CA  LEU A1007    12269  12495  12228   -556  -1339   1572       C  
ATOM   3278  C   LEU A1007     -18.183 189.188-200.122  1.00 95.71           C  
ANISOU 3278  C   LEU A1007    12293  12199  11875   -430  -1321   1321       C  
ATOM   3279  O   LEU A1007     -17.076 189.134-199.595  1.00 96.57           O  
ANISOU 3279  O   LEU A1007    12503  12292  11899   -378  -1247   1244       O  
ATOM   3280  CB  LEU A1007     -19.663 187.166-199.989  1.00103.49           C  
ANISOU 3280  CB  LEU A1007    13039  13050  13234   -725  -1576   1637       C  
ATOM   3281  CG  LEU A1007     -18.737 186.026-199.570  1.00107.55           C  
ANISOU 3281  CG  LEU A1007    13658  13400  13806   -783  -1625   1678       C  
ATOM   3282  CD1 LEU A1007     -18.438 186.094-198.082  1.00110.51           C  
ANISOU 3282  CD1 LEU A1007    13972  13964  14054   -734  -1416   1869       C  
ATOM   3283  CD2 LEU A1007     -19.403 184.709-199.908  1.00110.97           C  
ANISOU 3283  CD2 LEU A1007    13984  13605  14576   -972  -1841   1792       C  
ATOM   3284  N   LYS A1008     -18.389 189.786-201.288  1.00 93.36           N  
ANISOU 3284  N   LYS A1008    12062  11854  11556   -368  -1381   1214       N  
ATOM   3285  CA  LYS A1008     -17.272 190.294-202.071  1.00 88.09           C  
ANISOU 3285  CA  LYS A1008    11602  11091  10778   -251  -1334   1031       C  
ATOM   3286  C   LYS A1008     -16.995 191.765-201.798  1.00 86.97           C  
ANISOU 3286  C   LYS A1008    11435  11029  10582   -113  -1114    977       C  
ATOM   3287  O   LYS A1008     -15.984 192.305-202.249  1.00 85.77           O  
ANISOU 3287  O   LYS A1008    11409  10786  10395    -22  -1016    857       O  
ATOM   3288  CB  LYS A1008     -17.512 190.061-203.560  1.00 87.76           C  
ANISOU 3288  CB  LYS A1008    11680  10964  10702   -224  -1512    962       C  
ATOM   3289  CG  LYS A1008     -17.456 188.598-203.951  1.00 89.05           C  
ANISOU 3289  CG  LYS A1008    11903  10982  10949   -336  -1748    909       C  
ATOM   3290  CD  LYS A1008     -16.576 188.389-205.166  1.00 90.06           C  
ANISOU 3290  CD  LYS A1008    12268  11011  10941   -229  -1811    716       C  
ATOM   3291  CE  LYS A1008     -15.131 188.751-204.873  1.00 88.58           C  
ANISOU 3291  CE  LYS A1008    12197  10778  10682   -146  -1590    641       C  
ATOM   3292  NZ  LYS A1008     -14.387 189.024-206.139  1.00 90.29           N1+
ANISOU 3292  NZ  LYS A1008    12613  10965  10729     10  -1543    508       N1+
ATOM   3293  N   ASN A1009     -17.898 192.408-201.065  1.00 88.96           N  
ANISOU 3293  N   ASN A1009    11501  11433  10866    -94  -1027   1061       N  
ATOM   3294  CA  ASN A1009     -17.746 193.820-200.720  1.00 87.30           C  
ANISOU 3294  CA  ASN A1009    11235  11271  10665     43   -834    978       C  
ATOM   3295  C   ASN A1009     -18.074 194.112-199.258  1.00 86.51           C  
ANISOU 3295  C   ASN A1009    10965  11361  10545     69   -714    975       C  
ATOM   3296  O   ASN A1009     -19.012 194.854-198.973  1.00 90.97           O  
ANISOU 3296  O   ASN A1009    11371  12044  11151    134   -636   1014       O  
ATOM   3297  CB  ASN A1009     -18.641 194.684-201.611  1.00 86.28           C  
ANISOU 3297  CB  ASN A1009    11057  11139  10587    125   -839   1045       C  
ATOM   3298  CG  ASN A1009     -18.427 194.422-203.085  1.00 85.64           C  
ANISOU 3298  CG  ASN A1009    11153  10940  10445    147   -965   1061       C  
ATOM   3299  OD1 ASN A1009     -17.470 194.917-203.678  1.00 87.18           O  
ANISOU 3299  OD1 ASN A1009    11493  11020  10610    235   -862    997       O  
ATOM   3300  ND2 ASN A1009     -19.326 193.651-203.689  1.00 84.06           N  
ANISOU 3300  ND2 ASN A1009    10928  10779  10232     80  -1185   1139       N  
ATOM   3301  N   PRO A1010     -17.294 193.543-198.324  1.00 82.05           N  
ANISOU 3301  N   PRO A1010    10432  10848   9895     49   -699    925       N  
ATOM   3302  CA  PRO A1010     -17.585 193.689-196.893  1.00 83.18           C  
ANISOU 3302  CA  PRO A1010    10437  11238   9932    110   -594    932       C  
ATOM   3303  C   PRO A1010     -17.504 195.138-196.430  1.00 84.60           C  
ANISOU 3303  C   PRO A1010    10533  11482  10127    276   -448    711       C  
ATOM   3304  O   PRO A1010     -17.960 195.460-195.332  1.00 85.42           O  
ANISOU 3304  O   PRO A1010    10505  11827  10122    371   -350    679       O  
ATOM   3305  CB  PRO A1010     -16.482 192.863-196.225  1.00 81.92           C  
ANISOU 3305  CB  PRO A1010    10378  11086   9663     95   -645    895       C  
ATOM   3306  CG  PRO A1010     -15.377 192.837-197.216  1.00 79.59           C  
ANISOU 3306  CG  PRO A1010    10247  10530   9463     74   -714    752       C  
ATOM   3307  CD  PRO A1010     -16.052 192.788-198.553  1.00 79.60           C  
ANISOU 3307  CD  PRO A1010    10289  10391   9564      7   -777    849       C  
ATOM   3308  N   ASP A1011     -16.927 195.999-197.262  1.00 86.37           N  
ANISOU 3308  N   ASP A1011    10828  11489  10500    324   -425    563       N  
ATOM   3309  CA  ASP A1011     -16.835 197.415-196.947  1.00 91.90           C  
ANISOU 3309  CA  ASP A1011    11434  12162  11324    471   -297    346       C  
ATOM   3310  C   ASP A1011     -18.198 198.088-197.074  1.00 84.14           C  
ANISOU 3310  C   ASP A1011    10299  11259  10411    534   -231    447       C  
ATOM   3311  O   ASP A1011     -18.416 199.168-196.537  1.00 88.18           O  
ANISOU 3311  O   ASP A1011    10687  11802  11015    674   -123    272       O  
ATOM   3312  CB  ASP A1011     -15.784 198.102-197.829  1.00105.27           C  
ANISOU 3312  CB  ASP A1011    13220  13553  13222    490   -261    220       C  
ATOM   3313  CG  ASP A1011     -15.866 197.669-199.282  1.00117.00           C  
ANISOU 3313  CG  ASP A1011    14845  14884  14726    415   -316    431       C  
ATOM   3314  OD1 ASP A1011     -16.995 197.454-199.770  1.00123.61           O  
ANISOU 3314  OD1 ASP A1011    15654  15797  15517    393   -375    622       O  
ATOM   3315  OD2 ASP A1011     -14.803 197.536-199.931  1.00119.06           O1-
ANISOU 3315  OD2 ASP A1011    15231  14967  15041    393   -305    391       O1-
ATOM   3316  N   PHE A1012     -19.120 197.443-197.780  1.00 73.18           N  
ANISOU 3316  N   PHE A1012     8902   9894   9008    440   -316    702       N  
ATOM   3317  CA  PHE A1012     -20.480 197.958-197.877  1.00 65.46           C  
ANISOU 3317  CA  PHE A1012     7745   9014   8113    498   -279    816       C  
ATOM   3318  C   PHE A1012     -21.129 197.895-196.515  1.00 69.17           C  
ANISOU 3318  C   PHE A1012     8031   9779   8472    553   -168    803       C  
ATOM   3319  O   PHE A1012     -21.981 198.710-196.182  1.00 74.66           O  
ANISOU 3319  O   PHE A1012     8547  10578   9242    678    -60    768       O  
ATOM   3320  CB  PHE A1012     -21.332 197.149-198.854  1.00 64.67           C  
ANISOU 3320  CB  PHE A1012     7640   8896   8035    378   -441   1063       C  
ATOM   3321  CG  PHE A1012     -20.938 197.316-200.282  1.00 58.61           C  
ANISOU 3321  CG  PHE A1012     7044   7910   7315    384   -545   1091       C  
ATOM   3322  CD1 PHE A1012     -19.877 198.134-200.625  1.00 66.91           C  
ANISOU 3322  CD1 PHE A1012     8226   8777   8421    473   -445    959       C  
ATOM   3323  CD2 PHE A1012     -21.632 196.663-201.282  1.00 59.16           C  
ANISOU 3323  CD2 PHE A1012     7130   7969   7379    314   -739   1246       C  
ATOM   3324  CE1 PHE A1012     -19.500 198.291-201.940  1.00 66.91           C  
ANISOU 3324  CE1 PHE A1012     8385   8610   8426    505   -492   1033       C  
ATOM   3325  CE2 PHE A1012     -21.267 196.817-202.601  1.00 60.85           C  
ANISOU 3325  CE2 PHE A1012     7521   8041   7557    366   -830   1268       C  
ATOM   3326  CZ  PHE A1012     -20.199 197.633-202.933  1.00 63.81           C  
ANISOU 3326  CZ  PHE A1012     8042   8259   7943    469   -683   1188       C  
ATOM   3327  N   VAL A1013     -20.732 196.917-195.719  1.00 67.65           N  
ANISOU 3327  N   VAL A1013     7881   9734   8090    483   -180    847       N  
ATOM   3328  CA  VAL A1013     -21.401 196.712-194.449  1.00 75.40           C  
ANISOU 3328  CA  VAL A1013     8696  11047   8907    549    -49    913       C  
ATOM   3329  C   VAL A1013     -20.626 197.333-193.295  1.00 77.45           C  
ANISOU 3329  C   VAL A1013     8977  11467   8986    733     47    612       C  
ATOM   3330  O   VAL A1013     -21.201 197.645-192.250  1.00 79.40           O  
ANISOU 3330  O   VAL A1013     9078  12017   9075    882    194    565       O  
ATOM   3331  CB  VAL A1013     -21.676 195.213-194.187  1.00 78.08           C  
ANISOU 3331  CB  VAL A1013     9026  11488   9154    382   -100   1229       C  
ATOM   3332  CG1 VAL A1013     -22.698 195.040-193.070  1.00 78.33           C  
ANISOU 3332  CG1 VAL A1013     8832  11869   9062    448     88   1411       C  
ATOM   3333  CG2 VAL A1013     -22.188 194.551-195.456  1.00 77.93           C  
ANISOU 3333  CG2 VAL A1013     9014  11244   9351    194   -273   1423       C  
ATOM   3334  N   PHE A1014     -19.327 197.536-193.476  1.00 81.84           N  
ANISOU 3334  N   PHE A1014     9694  11833   9567    739    -39    384       N  
ATOM   3335  CA  PHE A1014     -18.526 198.048-192.369  1.00 92.90           C  
ANISOU 3335  CA  PHE A1014    11099  13386  10814    911     -8     53       C  
ATOM   3336  C   PHE A1014     -17.836 199.371-192.677  1.00 96.39           C  
ANISOU 3336  C   PHE A1014    11536  13570  11519   1010    -10   -320       C  
ATOM   3337  O   PHE A1014     -17.686 199.768-193.832  1.00 94.03           O  
ANISOU 3337  O   PHE A1014    11282  12943  11501    929    -28   -275       O  
ATOM   3338  CB  PHE A1014     -17.501 197.007-191.921  1.00100.13           C  
ANISOU 3338  CB  PHE A1014    12156  14364  11526    857   -121     88       C  
ATOM   3339  CG  PHE A1014     -18.096 195.656-191.652  1.00107.46           C  
ANISOU 3339  CG  PHE A1014    13085  15472  12273    747   -116    494       C  
ATOM   3340  CD1 PHE A1014     -19.152 195.507-190.768  1.00111.93           C  
ANISOU 3340  CD1 PHE A1014    13501  16387  12642    831     38    675       C  
ATOM   3341  CD2 PHE A1014     -17.610 194.534-192.302  1.00110.58           C  
ANISOU 3341  CD2 PHE A1014    13612  15669  12735    563   -250    701       C  
ATOM   3342  CE1 PHE A1014     -19.702 194.257-190.532  1.00114.73           C  
ANISOU 3342  CE1 PHE A1014    13823  16863  12908    711     68   1097       C  
ATOM   3343  CE2 PHE A1014     -18.156 193.285-192.068  1.00112.87           C  
ANISOU 3343  CE2 PHE A1014    13880  16058  12949    448   -252   1077       C  
ATOM   3344  CZ  PHE A1014     -19.204 193.148-191.181  1.00114.56           C  
ANISOU 3344  CZ  PHE A1014    13929  16594  13006    512    -88   1296       C  
ATOM   3345  N   SER A1015     -17.426 200.057-191.620  1.00 99.61           N  
ANISOU 3345  N   SER A1015    11879  14130  11839   1199     11   -688       N  
ATOM   3346  CA  SER A1015     -16.716 201.315-191.761  1.00103.42           C  
ANISOU 3346  CA  SER A1015    12315  14336  12642   1291     -3  -1087       C  
ATOM   3347  C   SER A1015     -15.226 201.117-191.522  1.00107.79           C  
ANISOU 3347  C   SER A1015    12955  14788  13215   1270   -144  -1331       C  
ATOM   3348  O   SER A1015     -14.814 200.130-190.911  1.00107.11           O  
ANISOU 3348  O   SER A1015    12950  14940  12808   1260   -232  -1260       O  
ATOM   3349  CB  SER A1015     -17.282 202.360-190.799  1.00105.96           C  
ANISOU 3349  CB  SER A1015    12468  14847  12945   1535     85  -1429       C  
ATOM   3350  OG  SER A1015     -17.458 201.822-189.500  1.00107.57           O  
ANISOU 3350  OG  SER A1015    12659  15530  12682   1680     92  -1494       O  
ATOM   3351  N   ASP A1016     -14.429 202.062-192.015  1.00114.24           N  
ANISOU 3351  N   ASP A1016    13730  15233  14445   1266   -159  -1593       N  
ATOM   3352  CA  ASP A1016     -12.971 202.015-191.904  1.00117.10           C  
ANISOU 3352  CA  ASP A1016    14115  15433  14943   1236   -287  -1848       C  
ATOM   3353  C   ASP A1016     -12.405 200.670-192.334  1.00110.75           C  
ANISOU 3353  C   ASP A1016    13475  14649  13954   1076   -365  -1545       C  
ATOM   3354  O   ASP A1016     -11.458 200.158-191.746  1.00112.11           O  
ANISOU 3354  O   ASP A1016    13675  14919  14002   1099   -504  -1699       O  
ATOM   3355  CB  ASP A1016     -12.525 202.379-190.491  1.00126.33           C  
ANISOU 3355  CB  ASP A1016    15189  16861  15951   1442   -408  -2329       C  
ATOM   3356  CG  ASP A1016     -12.827 203.822-190.148  1.00135.19           C  
ANISOU 3356  CG  ASP A1016    16131  17858  17376   1605   -360  -2743       C  
ATOM   3357  OD1 ASP A1016     -12.841 204.660-191.080  1.00135.39           O  
ANISOU 3357  OD1 ASP A1016    16092  17454  17896   1529   -260  -2713       O  
ATOM   3358  OD2 ASP A1016     -13.055 204.119-188.954  1.00140.76           O1-
ANISOU 3358  OD2 ASP A1016    16761  18897  17823   1828   -417  -3093       O1-
ATOM   3359  N   MET A1017     -13.013 200.107-193.369  1.00104.64           N  
ANISOU 3359  N   MET A1017    12802  13783  13174    933   -295  -1136       N  
ATOM   3360  CA  MET A1017     -12.585 198.845-193.937  1.00 99.12           C  
ANISOU 3360  CA  MET A1017    12257  13053  12350    783   -366   -860       C  
ATOM   3361  C   MET A1017     -11.849 199.119-195.236  1.00 97.89           C  
ANISOU 3361  C   MET A1017    12157  12511  12526    682   -317   -814       C  
ATOM   3362  O   MET A1017     -12.471 199.422-196.252  1.00 98.15           O  
ANISOU 3362  O   MET A1017    12221  12395  12675    638   -223   -604       O  
ATOM   3363  CB  MET A1017     -13.805 197.972-194.223  1.00 96.80           C  
ANISOU 3363  CB  MET A1017    12021  12925  11833    701   -345   -468       C  
ATOM   3364  CG  MET A1017     -13.479 196.624-194.817  1.00 92.49           C  
ANISOU 3364  CG  MET A1017    11625  12320  11198    551   -438   -208       C  
ATOM   3365  SD  MET A1017     -12.841 195.531-193.544  1.00184.14           S  
ANISOU 3365  SD  MET A1017    23267  24191  22506    593   -563   -219       S  
ATOM   3366  CE  MET A1017     -14.208 195.598-192.393  1.00119.33           C  
ANISOU 3366  CE  MET A1017    14939  16393  14007    704   -471    -99       C  
ATOM   3367  N   GLU A1018     -10.524 199.033-195.203  1.00 99.18           N  
ANISOU 3367  N   GLU A1018    12320  12531  12834    666   -374  -1000       N  
ATOM   3368  CA  GLU A1018      -9.732 199.156-196.420  1.00100.82           C  
ANISOU 3368  CA  GLU A1018    12575  12405  13328    579   -288   -919       C  
ATOM   3369  C   GLU A1018      -9.533 197.777-197.028  1.00101.35           C  
ANISOU 3369  C   GLU A1018    12817  12508  13184    478   -353   -664       C  
ATOM   3370  O   GLU A1018      -8.859 196.921-196.450  1.00 99.51           O  
ANISOU 3370  O   GLU A1018    12611  12376  12821    472   -482   -731       O  
ATOM   3371  CB  GLU A1018      -8.395 199.806-196.129  1.00102.84           C  
ANISOU 3371  CB  GLU A1018    12690  12455  13928    608   -296  -1254       C  
ATOM   3372  N   LYS A1019     -10.135 197.556-198.192  1.00101.14           N  
ANISOU 3372  N   LYS A1019    12905  12400  13123    419   -283   -388       N  
ATOM   3373  CA  LYS A1019     -10.037 196.260-198.843  1.00 99.66           C  
ANISOU 3373  CA  LYS A1019    12881  12227  12758    336   -363   -194       C  
ATOM   3374  C   LYS A1019      -8.881 196.232-199.842  1.00 98.45           C  
ANISOU 3374  C   LYS A1019    12789  11837  12780    324   -271   -210       C  
ATOM   3375  O   LYS A1019      -8.731 197.140-200.663  1.00 99.39           O  
ANISOU 3375  O   LYS A1019    12889  11779  13096    356    -98   -168       O  
ATOM   3376  CB  LYS A1019     -11.356 195.902-199.526  1.00100.17           C  
ANISOU 3376  CB  LYS A1019    13028  12372  12660    295   -390     69       C  
ATOM   3377  CG  LYS A1019     -11.480 194.432-199.907  1.00 97.15           C  
ANISOU 3377  CG  LYS A1019    12782  12031  12101    206   -536    218       C  
ATOM   3378  CD  LYS A1019     -12.656 194.230-200.839  1.00 94.20           C  
ANISOU 3378  CD  LYS A1019    12468  11681  11644    173   -582    419       C  
ATOM   3379  CE  LYS A1019     -12.671 192.836-201.413  1.00 93.48           C  
ANISOU 3379  CE  LYS A1019    12506  11560  11452     91   -744    501       C  
ATOM   3380  NZ  LYS A1019     -13.643 192.713-202.536  1.00 94.86           N1+
ANISOU 3380  NZ  LYS A1019    12743  11738  11563     84   -824    627       N1+
ATOM   3381  N   SER A1020      -8.066 195.185-199.752  1.00 95.76           N  
ANISOU 3381  N   SER A1020    12512  11496  12376    292   -368   -248       N  
ATOM   3382  CA  SER A1020      -6.930 194.999-200.649  1.00 95.34           C  
ANISOU 3382  CA  SER A1020    12505  11252  12470    296   -270   -271       C  
ATOM   3383  C   SER A1020      -7.342 194.064-201.778  1.00 93.28           C  
ANISOU 3383  C   SER A1020    12442  10995  12004    273   -298    -78       C  
ATOM   3384  O   SER A1020      -8.315 193.322-201.639  1.00 92.01           O  
ANISOU 3384  O   SER A1020    12357  10965  11638    226   -454     34       O  
ATOM   3385  CB  SER A1020      -5.740 194.406-199.888  1.00 96.11           C  
ANISOU 3385  CB  SER A1020    12532  11339  12648    303   -376   -464       C  
ATOM   3386  OG  SER A1020      -5.897 193.010-199.699  1.00 94.06           O  
ANISOU 3386  OG  SER A1020    12393  11181  12164    272   -556   -373       O  
ATOM   3387  N   PRO A1021      -6.611 194.096-202.906  1.00 93.33           N  
ANISOU 3387  N   PRO A1021    12520  10864  12078    316   -145    -48       N  
ATOM   3388  CA  PRO A1021      -6.925 193.161-203.992  1.00 93.95           C  
ANISOU 3388  CA  PRO A1021    12797  10971  11928    331   -199     64       C  
ATOM   3389  C   PRO A1021      -6.675 191.708-203.583  1.00 95.92           C  
ANISOU 3389  C   PRO A1021    13109  11244  12093    283   -417    -11       C  
ATOM   3390  O   PRO A1021      -7.315 190.797-204.116  1.00 98.72           O  
ANISOU 3390  O   PRO A1021    13599  11634  12277    263   -563     50       O  
ATOM   3391  CB  PRO A1021      -5.962 193.582-205.109  1.00 92.76           C  
ANISOU 3391  CB  PRO A1021    12682  10696  11868    425     58     86       C  
ATOM   3392  CG  PRO A1021      -4.855 194.300-204.415  1.00 93.14           C  
ANISOU 3392  CG  PRO A1021    12519  10607  12263    415    194    -53       C  
ATOM   3393  CD  PRO A1021      -5.501 194.998-203.259  1.00 93.77           C  
ANISOU 3393  CD  PRO A1021    12461  10737  12430    363     97   -114       C  
ATOM   3394  N   HIS A1022      -5.754 191.499-202.646  1.00 93.03           N  
ANISOU 3394  N   HIS A1022    12631  10842  11875    274   -457   -148       N  
ATOM   3395  CA  HIS A1022      -5.439 190.158-202.173  1.00 86.65           C  
ANISOU 3395  CA  HIS A1022    11866  10030  11026    249   -657   -185       C  
ATOM   3396  C   HIS A1022      -6.622 189.575-201.408  1.00 83.26           C  
ANISOU 3396  C   HIS A1022    11452   9731  10452    168   -854    -50       C  
ATOM   3397  O   HIS A1022      -7.164 188.529-201.768  1.00 86.37           O  
ANISOU 3397  O   HIS A1022    11951  10097  10771    119   -996     35       O  
ATOM   3398  CB  HIS A1022      -4.201 190.183-201.280  1.00 85.85           C  
ANISOU 3398  CB  HIS A1022    11619   9889  11111    286   -673   -348       C  
ATOM   3399  CG  HIS A1022      -3.816 188.835-200.769  1.00 88.51           C  
ANISOU 3399  CG  HIS A1022    11994  10210  11427    289   -878   -353       C  
ATOM   3400  ND1 HIS A1022      -3.392 188.616-199.477  1.00 91.41           N  
ANISOU 3400  ND1 HIS A1022    12253  10660  11821    316  -1023   -401       N  
ATOM   3401  CD2 HIS A1022      -3.812 187.625-201.377  1.00 89.63           C  
ANISOU 3401  CD2 HIS A1022    12270  10255  11532    286   -975   -313       C  
ATOM   3402  CE1 HIS A1022      -3.137 187.330-199.313  1.00 92.38           C  
ANISOU 3402  CE1 HIS A1022    12440  10724  11935    327  -1185   -341       C  
ATOM   3403  NE2 HIS A1022      -3.386 186.706-200.450  1.00 91.31           N  
ANISOU 3403  NE2 HIS A1022    12445  10456  11791    300  -1160   -303       N  
ATOM   3404  N   LEU A1023      -7.017 190.275-200.350  1.00 77.79           N  
ANISOU 3404  N   LEU A1023    10637   9175   9746    161   -851    -42       N  
ATOM   3405  CA  LEU A1023      -8.222 189.954-199.599  1.00 77.09           C  
ANISOU 3405  CA  LEU A1023    10527   9249   9517    102   -961    120       C  
ATOM   3406  C   LEU A1023      -9.426 189.844-200.539  1.00 78.65           C  
ANISOU 3406  C   LEU A1023    10799   9439   9644     39   -977    265       C  
ATOM   3407  O   LEU A1023     -10.360 189.084-200.280  1.00 83.61           O  
ANISOU 3407  O   LEU A1023    11425  10124  10221    -42  -1102    421       O  
ATOM   3408  CB  LEU A1023      -8.471 191.039-198.554  1.00 78.80           C  
ANISOU 3408  CB  LEU A1023    10599   9633   9709    151   -894     55       C  
ATOM   3409  CG  LEU A1023      -9.361 190.721-197.355  1.00 78.34           C  
ANISOU 3409  CG  LEU A1023    10477   9808   9479    143   -973    193       C  
ATOM   3410  CD1 LEU A1023      -8.781 189.558-196.585  1.00 77.97           C  
ANISOU 3410  CD1 LEU A1023    10455   9798   9373    156  -1117    260       C  
ATOM   3411  CD2 LEU A1023      -9.476 191.944-196.463  1.00 77.77           C  
ANISOU 3411  CD2 LEU A1023    10271   9903   9374    239   -891     37       C  
ATOM   3412  N   ASP A1024      -9.403 190.603-201.630  1.00 77.42           N  
ANISOU 3412  N   ASP A1024    10695   9217   9504     85   -851    227       N  
ATOM   3413  CA  ASP A1024     -10.431 190.482-202.646  1.00 80.93           C  
ANISOU 3413  CA  ASP A1024    11223   9673   9855     64   -904    334       C  
ATOM   3414  C   ASP A1024     -10.347 189.099-203.263  1.00 79.67           C  
ANISOU 3414  C   ASP A1024    11188   9417   9668     25  -1081    315       C  
ATOM   3415  O   ASP A1024     -11.369 188.483-203.545  1.00 83.88           O  
ANISOU 3415  O   ASP A1024    11735   9965  10169    -46  -1246    394       O  
ATOM   3416  CB  ASP A1024     -10.273 191.561-203.722  1.00 90.67           C  
ANISOU 3416  CB  ASP A1024    12506  10868  11076    166   -723    329       C  
ATOM   3417  CG  ASP A1024     -11.522 191.725-204.588  1.00102.38           C  
ANISOU 3417  CG  ASP A1024    14041  12428  12430    181   -796    455       C  
ATOM   3418  OD1 ASP A1024     -12.310 190.765-204.718  1.00104.68           O  
ANISOU 3418  OD1 ASP A1024    14360  12753  12660    107  -1012    488       O  
ATOM   3419  OD2 ASP A1024     -11.720 192.826-205.149  1.00108.92           O1-
ANISOU 3419  OD2 ASP A1024    14866  13268  13251    272   -648    525       O1-
ATOM   3420  N   GLY A1025      -9.130 188.604-203.465  1.00 75.76           N  
ANISOU 3420  N   GLY A1025    10758   8802   9225     74  -1055    186       N  
ATOM   3421  CA  GLY A1025      -8.942 187.290-204.058  1.00 77.11           C  
ANISOU 3421  CA  GLY A1025    11045   8849   9404     63  -1221    117       C  
ATOM   3422  C   GLY A1025      -9.382 186.167-203.132  1.00 79.23           C  
ANISOU 3422  C   GLY A1025    11254   9070   9779    -55  -1425    216       C  
ATOM   3423  O   GLY A1025     -10.025 185.198-203.558  1.00 83.44           O  
ANISOU 3423  O   GLY A1025    11831   9509  10363   -123  -1616    228       O  
ATOM   3424  N   CYS A1026      -9.038 186.299-201.856  1.00 73.89           N  
ANISOU 3424  N   CYS A1026    10468   8458   9148    -69  -1388    289       N  
ATOM   3425  CA  CYS A1026      -9.440 185.312-200.870  1.00 75.64           C  
ANISOU 3425  CA  CYS A1026    10627   8667   9447   -156  -1534    462       C  
ATOM   3426  C   CYS A1026     -10.963 185.259-200.758  1.00 79.03           C  
ANISOU 3426  C   CYS A1026    10981   9178   9870   -274  -1596    654       C  
ATOM   3427  O   CYS A1026     -11.571 184.177-200.805  1.00 86.75           O  
ANISOU 3427  O   CYS A1026    11941  10028  10992   -381  -1758    770       O  
ATOM   3428  CB  CYS A1026      -8.789 185.614-199.520  1.00 75.88           C  
ANISOU 3428  CB  CYS A1026    10563   8827   9441    -97  -1477    503       C  
ATOM   3429  SG  CYS A1026      -6.958 185.591-199.595  1.00101.84           S  
ANISOU 3429  SG  CYS A1026    13878  12000  12817     36  -1442    265       S  
ATOM   3430  N   LEU A1027     -11.580 186.429-200.641  1.00 74.90           N  
ANISOU 3430  N   LEU A1027    10387   8840   9232   -254  -1469    682       N  
ATOM   3431  CA  LEU A1027     -13.036 186.519-200.611  1.00 72.97           C  
ANISOU 3431  CA  LEU A1027    10039   8689   8997   -347  -1508    848       C  
ATOM   3432  C   LEU A1027     -13.671 185.988-201.895  1.00 79.83           C  
ANISOU 3432  C   LEU A1027    10971   9422   9939   -404  -1677    789       C  
ATOM   3433  O   LEU A1027     -14.768 185.438-201.864  1.00 82.63           O  
ANISOU 3433  O   LEU A1027    11219   9757  10420   -523  -1806    922       O  
ATOM   3434  CB  LEU A1027     -13.482 187.956-200.353  1.00 64.87           C  
ANISOU 3434  CB  LEU A1027     8929   7864   7855   -279  -1337    845       C  
ATOM   3435  CG  LEU A1027     -13.301 188.445-198.919  1.00 62.87           C  
ANISOU 3435  CG  LEU A1027     8566   7802   7521   -225  -1215    896       C  
ATOM   3436  CD1 LEU A1027     -13.532 189.929-198.871  1.00 60.60           C  
ANISOU 3436  CD1 LEU A1027     8212   7641   7173   -132  -1057    797       C  
ATOM   3437  CD2 LEU A1027     -14.249 187.728-197.985  1.00 55.72           C  
ANISOU 3437  CD2 LEU A1027     7532   7014   6623   -310  -1248   1162       C  
ATOM   3438  N   SER A1028     -12.983 186.170-203.019  1.00 79.79           N  
ANISOU 3438  N   SER A1028    11123   9338   9854   -305  -1675    582       N  
ATOM   3439  CA  SER A1028     -13.414 185.607-204.293  1.00 80.09           C  
ANISOU 3439  CA  SER A1028    11257   9279   9896   -305  -1864    460       C  
ATOM   3440  C   SER A1028     -13.496 184.097-204.164  1.00 80.26           C  
ANISOU 3440  C   SER A1028    11263   9084  10148   -420  -2090    450       C  
ATOM   3441  O   SER A1028     -14.504 183.490-204.530  1.00 82.70           O  
ANISOU 3441  O   SER A1028    11502   9318  10601   -523  -2301    461       O  
ATOM   3442  CB  SER A1028     -12.424 185.966-205.405  1.00 81.90           C  
ANISOU 3442  CB  SER A1028    11674   9490   9954   -136  -1774    253       C  
ATOM   3443  OG  SER A1028     -13.045 186.697-206.449  1.00 85.42           O  
ANISOU 3443  OG  SER A1028    12179  10058  10220    -44  -1776    229       O  
ATOM   3444  N   VAL A1029     -12.429 183.502-203.632  1.00 79.81           N  
ANISOU 3444  N   VAL A1029    11249   8903  10171   -400  -2055    429       N  
ATOM   3445  CA  VAL A1029     -12.366 182.051-203.427  1.00 78.61           C  
ANISOU 3445  CA  VAL A1029    11081   8494  10293   -493  -2252    446       C  
ATOM   3446  C   VAL A1029     -13.505 181.532-202.552  1.00 81.17           C  
ANISOU 3446  C   VAL A1029    11208   8790  10842   -676  -2331    742       C  
ATOM   3447  O   VAL A1029     -14.244 180.610-202.942  1.00 83.97           O  
ANISOU 3447  O   VAL A1029    11496   8941  11466   -798  -2550    735       O  
ATOM   3448  CB  VAL A1029     -11.028 181.627-202.805  1.00 71.69           C  
ANISOU 3448  CB  VAL A1029    10255   7521   9464   -418  -2181    433       C  
ATOM   3449  CG1 VAL A1029     -11.138 180.249-202.207  1.00 73.52           C  
ANISOU 3449  CG1 VAL A1029    10419   7501  10015   -525  -2348    586       C  
ATOM   3450  CG2 VAL A1029      -9.939 181.658-203.853  1.00 72.05           C  
ANISOU 3450  CG2 VAL A1029    10467   7496   9413   -260  -2149    123       C  
ATOM   3451  N   ILE A1030     -13.654 182.133-201.376  1.00 78.17           N  
ANISOU 3451  N   ILE A1030    10719   8616  10366   -684  -2148    990       N  
ATOM   3452  CA  ILE A1030     -14.731 181.751-200.468  1.00 81.97           C  
ANISOU 3452  CA  ILE A1030    10996   9130  11017   -831  -2147   1323       C  
ATOM   3453  C   ILE A1030     -16.120 181.969-201.086  1.00 83.97           C  
ANISOU 3453  C   ILE A1030    11119   9416  11369   -938  -2241   1333       C  
ATOM   3454  O   ILE A1030     -17.063 181.224-200.810  1.00 87.59           O  
ANISOU 3454  O   ILE A1030    11392   9759  12130  -1102  -2335   1539       O  
ATOM   3455  CB  ILE A1030     -14.618 182.510-199.140  1.00 81.29           C  
ANISOU 3455  CB  ILE A1030    10835   9339  10712   -761  -1912   1538       C  
ATOM   3456  CG1 ILE A1030     -13.223 182.313-198.551  1.00 81.49           C  
ANISOU 3456  CG1 ILE A1030    10972   9349  10641   -636  -1869   1494       C  
ATOM   3457  CG2 ILE A1030     -15.696 182.067-198.157  1.00 81.04           C  
ANISOU 3457  CG2 ILE A1030    10591   9380  10822   -883  -1857   1927       C  
ATOM   3458  CD1 ILE A1030     -12.988 183.079-197.274  1.00 81.93           C  
ANISOU 3458  CD1 ILE A1030    10970   9719  10440   -526  -1686   1620       C  
ATOM   3459  N   ALA A1031     -16.238 182.986-201.933  1.00 79.54           N  
ANISOU 3459  N   ALA A1031    10633   9002  10585   -840  -2218   1128       N  
ATOM   3460  CA  ALA A1031     -17.504 183.283-202.591  1.00 77.64           C  
ANISOU 3460  CA  ALA A1031    10272   8819  10408   -901  -2335   1114       C  
ATOM   3461  C   ALA A1031     -17.846 182.179-203.560  1.00 77.23           C  
ANISOU 3461  C   ALA A1031    10226   8500  10616   -990  -2657    936       C  
ATOM   3462  O   ALA A1031     -18.970 181.699-203.588  1.00 79.28           O  
ANISOU 3462  O   ALA A1031    10277   8678  11167  -1142  -2817   1028       O  
ATOM   3463  CB  ALA A1031     -17.441 184.620-203.315  1.00 76.10           C  
ANISOU 3463  CB  ALA A1031    10181   8829   9904   -738  -2240    960       C  
ATOM   3464  N   GLN A1032     -16.865 181.783-204.359  1.00 77.94           N  
ANISOU 3464  N   GLN A1032    10538   8451  10623   -885  -2753    655       N  
ATOM   3465  CA  GLN A1032     -17.075 180.718-205.323  1.00 82.12           C  
ANISOU 3465  CA  GLN A1032    11099   8725  11380   -929  -3081    399       C  
ATOM   3466  C   GLN A1032     -17.458 179.431-204.594  1.00 83.58           C  
ANISOU 3466  C   GLN A1032    11093   8601  12064  -1142  -3207    583       C  
ATOM   3467  O   GLN A1032     -18.391 178.722-205.006  1.00 83.57           O  
ANISOU 3467  O   GLN A1032    10930   8407  12415  -1284  -3478    515       O  
ATOM   3468  CB  GLN A1032     -15.828 180.506-206.180  1.00 85.79           C  
ANISOU 3468  CB  GLN A1032    11836   9116  11645   -745  -3105     70       C  
ATOM   3469  CG  GLN A1032     -16.028 179.515-207.305  1.00 92.88           C  
ANISOU 3469  CG  GLN A1032    12794   9794  12703   -732  -3457   -287       C  
ATOM   3470  CD  GLN A1032     -16.960 180.043-208.372  1.00 98.19           C  
ANISOU 3470  CD  GLN A1032    13468  10653  13186   -662  -3647   -469       C  
ATOM   3471  OE1 GLN A1032     -16.510 180.527-209.406  1.00101.60           O  
ANISOU 3471  OE1 GLN A1032    14117  11258  13230   -438  -3642   -711       O  
ATOM   3472  NE2 GLN A1032     -18.267 179.959-208.128  1.00100.20           N  
ANISOU 3472  NE2 GLN A1032    13467  10891  13711   -837  -3809   -333       N  
ATOM   3473  N   ALA A1033     -16.751 179.149-203.497  1.00 81.45           N  
ANISOU 3473  N   ALA A1033    10823   8280  11844  -1159  -3016    830       N  
ATOM   3474  CA  ALA A1033     -17.072 177.999-202.652  1.00 79.60           C  
ANISOU 3474  CA  ALA A1033    10404   7769  12071  -1342  -3070   1120       C  
ATOM   3475  C   ALA A1033     -18.515 178.056-202.177  1.00 82.58           C  
ANISOU 3475  C   ALA A1033    10478   8203  12696  -1529  -3059   1419       C  
ATOM   3476  O   ALA A1033     -19.212 177.050-202.152  1.00 78.37           O  
ANISOU 3476  O   ALA A1033     9741   7365  12671  -1720  -3234   1522       O  
ATOM   3477  CB  ALA A1033     -16.138 177.933-201.463  1.00 77.57           C  
ANISOU 3477  CB  ALA A1033    10200   7564  11710  -1277  -2836   1395       C  
ATOM   3478  N   PHE A1034     -18.948 179.252-201.800  1.00 81.26           N  
ANISOU 3478  N   PHE A1034    10258   8409  12208  -1471  -2843   1550       N  
ATOM   3479  CA  PHE A1034     -20.325 179.510-201.397  1.00 84.71           C  
ANISOU 3479  CA  PHE A1034    10395   8966  12826  -1610  -2792   1809       C  
ATOM   3480  C   PHE A1034     -21.319 179.245-202.533  1.00 86.20           C  
ANISOU 3480  C   PHE A1034    10448   9008  13295  -1711  -3123   1562       C  
ATOM   3481  O   PHE A1034     -22.435 178.774-202.295  1.00 88.52           O  
ANISOU 3481  O   PHE A1034    10426   9187  14020  -1905  -3198   1759       O  
ATOM   3482  CB  PHE A1034     -20.438 180.957-200.901  1.00 83.14           C  
ANISOU 3482  CB  PHE A1034    10206   9196  12185  -1470  -2507   1901       C  
ATOM   3483  CG  PHE A1034     -21.841 181.401-200.593  1.00 91.09           C  
ANISOU 3483  CG  PHE A1034    10908  10373  13329  -1564  -2436   2116       C  
ATOM   3484  CD1 PHE A1034     -22.463 181.023-199.409  1.00 94.60           C  
ANISOU 3484  CD1 PHE A1034    11096  10862  13986  -1683  -2236   2550       C  
ATOM   3485  CD2 PHE A1034     -22.528 182.230-201.471  1.00 94.20           C  
ANISOU 3485  CD2 PHE A1034    11263  10906  13622  -1509  -2548   1909       C  
ATOM   3486  CE1 PHE A1034     -23.753 181.444-199.117  1.00 96.19           C  
ANISOU 3486  CE1 PHE A1034    10986  11235  14328  -1757  -2136   2751       C  
ATOM   3487  CE2 PHE A1034     -23.816 182.656-201.184  1.00 96.01           C  
ANISOU 3487  CE2 PHE A1034    11184  11292  14003  -1580  -2484   2099       C  
ATOM   3488  CZ  PHE A1034     -24.428 182.261-200.005  1.00 96.55           C  
ANISOU 3488  CZ  PHE A1034    10977  11396  14310  -1709  -2270   2509       C  
ATOM   3489  N   MET A1035     -20.903 179.539-203.763  1.00 83.66           N  
ANISOU 3489  N   MET A1035    10353   8704  12730  -1566  -3320   1135       N  
ATOM   3490  CA  MET A1035     -21.763 179.400-204.937  1.00 86.58           C  
ANISOU 3490  CA  MET A1035    10638   9009  13251  -1594  -3675    834       C  
ATOM   3491  C   MET A1035     -21.913 177.946-205.404  1.00 93.40           C  
ANISOU 3491  C   MET A1035    11413   9430  14646  -1747  -4032    634       C  
ATOM   3492  O   MET A1035     -22.958 177.564-205.937  1.00 95.48           O  
ANISOU 3492  O   MET A1035    11444   9567  15269  -1872  -4337    502       O  
ATOM   3493  CB  MET A1035     -21.239 180.288-206.071  1.00 85.02           C  
ANISOU 3493  CB  MET A1035    10735   9042  12525  -1336  -3728    485       C  
ATOM   3494  CG  MET A1035     -22.107 180.338-207.319  1.00 89.94           C  
ANISOU 3494  CG  MET A1035    11307   9705  13160  -1291  -4098    172       C  
ATOM   3495  SD  MET A1035     -23.821 180.823-207.020  1.00128.74           S  
ANISOU 3495  SD  MET A1035    15805  14761  18349  -1438  -4161    407       S  
ATOM   3496  CE  MET A1035     -23.604 182.245-205.962  1.00 76.63           C  
ANISOU 3496  CE  MET A1035     9230   8515  11370  -1337  -3645    791       C  
ATOM   3497  N   ASP A1036     -20.873 177.139-205.194  1.00 96.00           N  
ANISOU 3497  N   ASP A1036    11904   9505  15066  -1733  -4012    594       N  
ATOM   3498  CA  ASP A1036     -20.917 175.715-205.550  1.00 99.36           C  
ANISOU 3498  CA  ASP A1036    12244   9448  16058  -1869  -4336    402       C  
ATOM   3499  C   ASP A1036     -21.874 174.908-204.670  1.00 97.95           C  
ANISOU 3499  C   ASP A1036    11672   8981  16565  -2167  -4338    804       C  
ATOM   3500  O   ASP A1036     -22.278 173.806-205.030  1.00 99.81           O  
ANISOU 3500  O   ASP A1036    11733   8784  17406  -2330  -4652    649       O  
ATOM   3501  CB  ASP A1036     -19.522 175.096-205.479  1.00102.98           C  
ANISOU 3501  CB  ASP A1036    12965   9705  16459  -1754  -4283    290       C  
ATOM   3502  CG  ASP A1036     -18.542 175.753-206.429  1.00104.52           C  
ANISOU 3502  CG  ASP A1036    13517  10139  16056  -1465  -4271   -112       C  
ATOM   3503  OD1 ASP A1036     -18.969 176.155-207.535  1.00108.20           O  
ANISOU 3503  OD1 ASP A1036    14047  10761  16302  -1362  -4483   -461       O  
ATOM   3504  OD2 ASP A1036     -17.347 175.864-206.067  1.00101.65           O1-
ANISOU 3504  OD2 ASP A1036    13356   9816  15449  -1332  -4047    -63       O1-
ATOM   3505  N   SER A1037     -22.225 175.457-203.513  1.00 95.19           N  
ANISOU 3505  N   SER A1037    11169   8865  16132  -2229  -3977   1318       N  
ATOM   3506  CA  SER A1037     -23.166 174.808-202.611  1.00 96.89           C  
ANISOU 3506  CA  SER A1037    10993   8876  16945  -2491  -3890   1786       C  
ATOM   3507  C   SER A1037     -24.588 174.958-203.129  1.00102.28           C  
ANISOU 3507  C   SER A1037    11334   9565  17961  -2642  -4107   1698       C  
ATOM   3508  O   SER A1037     -25.516 174.357-202.598  1.00103.32           O  
ANISOU 3508  O   SER A1037    11075   9477  18704  -2887  -4090   2027       O  
ATOM   3509  CB  SER A1037     -23.073 175.426-201.222  1.00 92.87           C  
ANISOU 3509  CB  SER A1037    10449   8700  16139  -2451  -3412   2340       C  
ATOM   3510  OG  SER A1037     -21.728 175.686-200.884  1.00 90.21           O  
ANISOU 3510  OG  SER A1037    10457   8498  15320  -2243  -3239   2317       O  
ATOM   3511  N   PHE A1038     -24.759 175.779-204.157  1.00104.80           N  
ANISOU 3511  N   PHE A1038    11785  10145  17890  -2486  -4302   1279       N  
ATOM   3512  CA  PHE A1038     -26.074 175.990-204.743  1.00109.54           C  
ANISOU 3512  CA  PHE A1038    12072  10788  18759  -2587  -4560   1146       C  
ATOM   3513  C   PHE A1038     -26.155 175.308-206.099  1.00114.40           C  
ANISOU 3513  C   PHE A1038    12732  11130  19605  -2576  -5111    542       C  
ATOM   3514  O   PHE A1038     -27.150 175.424-206.821  1.00117.29           O  
ANISOU 3514  O   PHE A1038    12875  11527  20163  -2617  -5441    298       O  
ATOM   3515  CB  PHE A1038     -26.376 177.483-204.844  1.00105.10           C  
ANISOU 3515  CB  PHE A1038    11579  10752  17600  -2396  -4383   1170       C  
ATOM   3516  CG  PHE A1038     -26.555 178.139-203.511  1.00103.65           C  
ANISOU 3516  CG  PHE A1038    11271  10837  17273  -2414  -3888   1709       C  
ATOM   3517  CD1 PHE A1038     -27.781 178.105-202.869  1.00105.89           C  
ANISOU 3517  CD1 PHE A1038    11106  11140  17986  -2602  -3775   2064       C  
ATOM   3518  CD2 PHE A1038     -25.492 178.762-202.884  1.00101.67           C  
ANISOU 3518  CD2 PHE A1038    11331  10823  16475  -2233  -3539   1843       C  
ATOM   3519  CE1 PHE A1038     -27.949 178.695-201.633  1.00105.12           C  
ANISOU 3519  CE1 PHE A1038    10900  11329  17711  -2581  -3304   2539       C  
ATOM   3520  CE2 PHE A1038     -25.652 179.357-201.649  1.00101.10           C  
ANISOU 3520  CE2 PHE A1038    11152  11024  16238  -2217  -3114   2281       C  
ATOM   3521  CZ  PHE A1038     -26.886 179.321-201.021  1.00103.34           C  
ANISOU 3521  CZ  PHE A1038    11014  11358  16894  -2379  -2986   2629       C  
ATOM   3522  N   SER A1039     -25.094 174.581-206.427  1.00114.33           N  
ANISOU 3522  N   SER A1039    13004  10863  19573  -2500  -5221    281       N  
ATOM   3523  CA  SER A1039     -25.027 173.846-207.674  1.00118.51           C  
ANISOU 3523  CA  SER A1039    13612  11126  20289  -2451  -5734   -343       C  
ATOM   3524  C   SER A1039     -26.038 172.707-207.616  1.00126.31           C  
ANISOU 3524  C   SER A1039    14143  11611  22238  -2769  -6055   -354       C  
ATOM   3525  O   SER A1039     -26.507 172.345-206.538  1.00128.22           O  
ANISOU 3525  O   SER A1039    14064  11660  22992  -3019  -5809    184       O  
ATOM   3526  CB  SER A1039     -23.609 173.308-207.890  1.00116.18           C  
ANISOU 3526  CB  SER A1039    13699  10658  19787  -2289  -5711   -576       C  
ATOM   3527  OG  SER A1039     -23.400 172.909-209.232  1.00119.05           O  
ANISOU 3527  OG  SER A1039    14237  10929  20066  -2127  -6157  -1254       O  
ATOM   3528  N   LEU A1040     -26.391 172.158-208.772  1.00131.42           N  
ANISOU 3528  N   LEU A1040    14742  12055  23138  -2751  -6603   -963       N  
ATOM   3529  CA  LEU A1040     -27.300 171.021-208.815  1.00139.37           C  
ANISOU 3529  CA  LEU A1040    15330  12581  25043  -2988  -6873  -1035       C  
ATOM   3530  C   LEU A1040     -26.588 169.781-209.331  1.00148.01           C  
ANISOU 3530  C   LEU A1040    16599  13271  26369  -2874  -7047  -1436       C  
ATOM   3531  O   LEU A1040     -27.095 168.664-209.212  1.00153.37           O  
ANISOU 3531  O   LEU A1040    16989  13526  27761  -3004  -7127  -1414       O  
ATOM   3532  CB  LEU A1040     -28.520 171.326-209.685  1.00138.21           C  
ANISOU 3532  CB  LEU A1040    14952  12636  24925  -2934  -7206  -1364       C  
ATOM   3533  CG  LEU A1040     -29.600 172.192-209.037  1.00133.07           C  
ANISOU 3533  CG  LEU A1040    13929  12249  24383  -3107  -7030   -899       C  
ATOM   3534  CD1 LEU A1040     -30.841 172.281-209.918  1.00137.06           C  
ANISOU 3534  CD1 LEU A1040    14172  12870  25035  -3049  -7392  -1250       C  
ATOM   3535  CD2 LEU A1040     -29.950 171.656-207.658  1.00132.33           C  
ANISOU 3535  CD2 LEU A1040    13474  11858  24949  -3418  -6629   -209       C  
ATOM   3536  N   THR A1041     -25.407 169.989-209.903  1.00149.38           N  
ANISOU 3536  N   THR A1041    17230  13580  25946  -2616  -7092  -1796       N  
ATOM   3537  CA  THR A1041     -24.639 168.902-210.489  1.00156.98           C  
ANISOU 3537  CA  THR A1041    18381  14223  27040  -2453  -7248  -2230       C  
ATOM   3538  C   THR A1041     -23.433 168.533-209.640  1.00153.43           C  
ANISOU 3538  C   THR A1041    18124  13541  26632  -2475  -6937  -1912       C  
ATOM   3539  O   THR A1041     -22.640 169.395-209.261  1.00147.14           O  
ANISOU 3539  O   THR A1041    17600  12999  25306  -2414  -6709  -1723       O  
ATOM   3540  CB  THR A1041     -24.163 169.250-211.912  1.00161.33           C  
ANISOU 3540  CB  THR A1041    19305  15104  26888  -2082  -7526  -2934       C  
ATOM   3541  OG1 THR A1041     -23.140 168.330-212.311  1.00165.32           O  
ANISOU 3541  OG1 THR A1041    20039  15350  27423  -1902  -7569  -3282       O  
ATOM   3542  CG2 THR A1041     -23.608 170.665-211.956  1.00154.95           C  
ANISOU 3542  CG2 THR A1041    18822  14814  25236  -1930  -7363  -2853       C  
ATOM   3543  N   ASP A1042     -23.303 167.246-209.342  1.00157.72           N  
ANISOU 3543  N   ASP A1042    18513  13595  27820  -2551  -6940  -1849       N  
ATOM   3544  CA  ASP A1042     -22.155 166.758-208.596  1.00155.23           C  
ANISOU 3544  CA  ASP A1042    18365  13037  27578  -2532  -6679  -1567       C  
ATOM   3545  C   ASP A1042     -20.918 166.786-209.487  1.00152.34           C  
ANISOU 3545  C   ASP A1042    18438  12784  26660  -2200  -6781  -2134       C  
ATOM   3546  O   ASP A1042     -20.666 165.857-210.256  1.00155.83           O  
ANISOU 3546  O   ASP A1042    18912  13001  27296  -2045  -7009  -2614       O  
ATOM   3547  CB  ASP A1042     -22.425 165.350-208.065  1.00161.82           C  
ANISOU 3547  CB  ASP A1042    18882  13327  29274  -2685  -6668  -1327       C  
ATOM   3548  CG  ASP A1042     -23.574 165.316-207.076  1.00164.40           C  
ANISOU 3548  CG  ASP A1042    18773  13563  30130  -2993  -6477   -681       C  
ATOM   3549  OD1 ASP A1042     -23.693 166.267-206.273  1.00159.17           O  
ANISOU 3549  OD1 ASP A1042    18108  13198  29172  -3100  -6179   -181       O  
ATOM   3550  OD2 ASP A1042     -24.358 164.346-207.105  1.00170.92           O1-
ANISOU 3550  OD2 ASP A1042    19248  14029  31667  -3118  -6613   -675       O1-
ATOM   3551  N   THR A1043     -20.158 167.870-209.384  1.00145.66           N  
ANISOU 3551  N   THR A1043    17915  12298  25129  -2082  -6597  -2074       N  
ATOM   3552  CA  THR A1043     -19.001 168.084-210.242  1.00143.89           C  
ANISOU 3552  CA  THR A1043    18109  12264  24298  -1744  -6636  -2581       C  
ATOM   3553  C   THR A1043     -17.843 167.158-209.893  1.00142.81           C  
ANISOU 3553  C   THR A1043    18087  11776  24399  -1649  -6503  -2557       C  
ATOM   3554  O   THR A1043     -17.399 167.104-208.747  1.00138.40           O  
ANISOU 3554  O   THR A1043    17499  11054  24034  -1779  -6230  -2012       O  
ATOM   3555  CB  THR A1043     -18.515 169.546-210.179  1.00139.69           C  
ANISOU 3555  CB  THR A1043    17857  12335  22885  -1576  -6321  -2413       C  
ATOM   3556  OG1 THR A1043     -19.574 170.422-210.587  1.00140.89           O  
ANISOU 3556  OG1 THR A1043    17904  12869  22759  -1601  -6419  -2433       O  
ATOM   3557  CG2 THR A1043     -17.316 169.752-211.093  1.00138.02           C  
ANISOU 3557  CG2 THR A1043    18048  12346  22047  -1203  -6292  -2892       C  
ATOM   3558  N   HIS A1044     -17.362 166.430-210.896  1.00146.21           N  
ANISOU 3558  N   HIS A1044    18640  12116  24795  -1401  -6699  -3141       N  
ATOM   3559  CA  HIS A1044     -16.197 165.573-210.733  1.00147.24           C  
ANISOU 3559  CA  HIS A1044    18887  11954  25103  -1259  -6596  -3204       C  
ATOM   3560  C   HIS A1044     -14.908 166.378-210.876  1.00142.57           C  
ANISOU 3560  C   HIS A1044    18689  11670  23812  -1001  -6371  -3314       C  
ATOM   3561  O   HIS A1044     -14.465 166.666-211.990  1.00141.90           O  
ANISOU 3561  O   HIS A1044    18850  11876  23189   -706  -6449  -3854       O  
ATOM   3562  CB  HIS A1044     -16.230 164.438-211.743  1.00152.86           C  
ANISOU 3562  CB  HIS A1044    19539  12440  26101  -1097  -6894  -3793       C  
ATOM   3563  N   LEU A1045     -14.313 166.740-209.741  1.00139.47           N  
ANISOU 3563  N   LEU A1045    18344  11226  23424  -1097  -6079  -2782       N  
ATOM   3564  CA  LEU A1045     -13.048 167.473-209.727  1.00134.92           C  
ANISOU 3564  CA  LEU A1045    18076  10980  22208   -839  -5774  -2784       C  
ATOM   3565  C   LEU A1045     -11.855 166.535-209.884  1.00139.06           C  
ANISOU 3565  C   LEU A1045    18714  11164  22959   -638  -5792  -3055       C  
ATOM   3566  O   LEU A1045     -11.639 165.641-209.065  1.00140.50           O  
ANISOU 3566  O   LEU A1045    18727  10961  23694   -743  -5743  -2717       O  
ATOM   3567  CB  LEU A1045     -12.898 168.282-208.437  1.00126.66           C  
ANISOU 3567  CB  LEU A1045    16978  10218  20927   -944  -5348  -2050       C  
ATOM   3568  CG  LEU A1045     -13.960 169.334-208.115  1.00122.65           C  
ANISOU 3568  CG  LEU A1045    16350  10117  20135  -1105  -5226  -1707       C  
ATOM   3569  CD1 LEU A1045     -13.600 170.062-206.831  1.00117.87           C  
ANISOU 3569  CD1 LEU A1045    15725   9783  19276  -1145  -4807  -1070       C  
ATOM   3570  CD2 LEU A1045     -14.131 170.316-209.263  1.00120.10           C  
ANISOU 3570  CD2 LEU A1045    16211  10271  19149   -912  -5266  -2115       C  
ATOM   3571  N   ASP A1046     -11.083 166.755-210.944  1.00140.85           N  
ANISOU 3571  N   ASP A1046    19197  11642  22679   -311  -5785  -3598       N  
ATOM   3572  CA  ASP A1046      -9.909 165.943-211.230  1.00143.68           C  
ANISOU 3572  CA  ASP A1046    19637  11827  23128    -60  -5722  -3868       C  
ATOM   3573  C   ASP A1046      -8.647 166.797-211.227  1.00138.10           C  
ANISOU 3573  C   ASP A1046    19202  11409  21860    189  -5416  -3891       C  
ATOM   3574  O   ASP A1046      -8.559 167.781-210.494  1.00132.23           O  
ANISOU 3574  O   ASP A1046    18451  11028  20763    116  -5091  -3382       O  
ATOM   3575  CB  ASP A1046     -10.075 165.202-212.565  1.00151.89           C  
ANISOU 3575  CB  ASP A1046    20686  12877  24149    141  -5972  -4526       C  
ATOM   3576  CG  ASP A1046     -10.457 166.127-213.713  1.00153.40           C  
ANISOU 3576  CG  ASP A1046    21074  13583  23629    321  -6039  -4930       C  
ATOM   3577  OD1 ASP A1046     -10.655 167.335-213.468  1.00150.77           O  
ANISOU 3577  OD1 ASP A1046    20856  13573  22858    268  -5903  -4694       O  
ATOM   3578  OD2 ASP A1046     -10.573 165.641-214.859  1.00157.74           O1-
ANISOU 3578  OD2 ASP A1046    21662  14224  24048    530  -6235  -5472       O1-
ATOM   3579  N   LYS A1047      -7.671 166.418-212.045  1.00141.73           N  
ANISOU 3579  N   LYS A1047    19801  11926  22126    509  -5362  -4347       N  
ATOM   3580  CA  LYS A1047      -6.418 167.162-212.143  1.00140.13           C  
ANISOU 3580  CA  LYS A1047    19802  12031  21411    775  -5020  -4377       C  
ATOM   3581  C   LYS A1047      -6.609 168.410-212.992  1.00140.00           C  
ANISOU 3581  C   LYS A1047    19959  12651  20585    921  -4843  -4501       C  
ATOM   3582  O   LYS A1047      -5.748 169.289-213.033  1.00137.13           O  
ANISOU 3582  O   LYS A1047    19702  12673  19727   1093  -4461  -4369       O  
ATOM   3583  CB  LYS A1047      -5.325 166.282-212.730  1.00143.10           C  
ANISOU 3583  CB  LYS A1047    20223  12257  21890   1068  -4989  -4792       C  
ATOM   3584  N   HIS A1048      -7.754 168.478-213.662  1.00142.77           N  
ANISOU 3584  N   HIS A1048    20316  13090  20842    855  -5132  -4738       N  
ATOM   3585  CA  HIS A1048      -8.044 169.569-214.579  1.00140.96           C  
ANISOU 3585  CA  HIS A1048    20258  13445  19856   1025  -5024  -4874       C  
ATOM   3586  C   HIS A1048      -8.843 170.698-213.926  1.00138.29           C  
ANISOU 3586  C   HIS A1048    19824  13413  19307    788  -4863  -4310       C  
ATOM   3587  O   HIS A1048      -9.031 171.751-214.528  1.00140.39           O  
ANISOU 3587  O   HIS A1048    20216  14164  18960    919  -4713  -4296       O  
ATOM   3588  CB  HIS A1048      -8.796 169.036-215.806  1.00143.21           C  
ANISOU 3588  CB  HIS A1048    20615  13721  20077   1159  -5460  -5516       C  
ATOM   3589  CG  HIS A1048      -8.038 168.004-216.585  1.00144.71           C  
ANISOU 3589  CG  HIS A1048    20830  13809  20342   1429  -5480  -5975       C  
ATOM   3590  ND1 HIS A1048      -6.675 168.070-216.779  1.00142.44           N  
ANISOU 3590  ND1 HIS A1048    20697  13624  19799   1712  -5158  -6090       N  
ATOM   3591  CD2 HIS A1048      -8.455 166.884-217.220  1.00148.78           C  
ANISOU 3591  CD2 HIS A1048    21221  14128  21180   1464  -5785  -6358       C  
ATOM   3592  CE1 HIS A1048      -6.286 167.034-217.500  1.00147.20           C  
ANISOU 3592  CE1 HIS A1048    21275  14110  20545   1908  -5260  -6519       C  
ATOM   3593  NE2 HIS A1048      -7.346 166.298-217.780  1.00150.83           N  
ANISOU 3593  NE2 HIS A1048    21576  14381  21351   1765  -5650  -6699       N  
ATOM   3594  N   SER A1049      -9.309 170.486-212.698  1.00134.07           N  
ANISOU 3594  N   SER A1049    19065  12604  19273    462  -4879  -3831       N  
ATOM   3595  CA  SER A1049     -10.156 171.479-212.029  1.00128.11           C  
ANISOU 3595  CA  SER A1049    18193  12118  18365    240  -4744  -3326       C  
ATOM   3596  C   SER A1049      -9.344 172.543-211.287  1.00120.58           C  
ANISOU 3596  C   SER A1049    17279  11479  17057    278  -4277  -2883       C  
ATOM   3597  O   SER A1049      -8.273 172.245-210.758  1.00120.83           O  
ANISOU 3597  O   SER A1049    17319  11367  17223    344  -4102  -2792       O  
ATOM   3598  CB  SER A1049     -11.137 170.787-211.089  1.00129.10           C  
ANISOU 3598  CB  SER A1049    18043  11847  19162   -111  -4961  -3015       C  
ATOM   3599  OG  SER A1049     -12.160 170.131-211.819  1.00133.16           O  
ANISOU 3599  OG  SER A1049    18471  12152  19974   -186  -5401  -3399       O  
ATOM   3600  N   PRO A1050      -9.853 173.790-211.248  1.00115.51           N  
ANISOU 3600  N   PRO A1050    16643  11249  15996    243  -4096  -2628       N  
ATOM   3601  CA  PRO A1050      -9.142 174.903-210.604  1.00110.22           C  
ANISOU 3601  CA  PRO A1050    15994  10873  15013    281  -3676  -2262       C  
ATOM   3602  C   PRO A1050      -9.026 174.738-209.092  1.00104.87           C  
ANISOU 3602  C   PRO A1050    15136  10019  14692     70  -3573  -1802       C  
ATOM   3603  O   PRO A1050      -9.959 174.250-208.454  1.00105.04           O  
ANISOU 3603  O   PRO A1050    14987   9841  15081   -163  -3753  -1586       O  
ATOM   3604  CB  PRO A1050     -10.020 176.117-210.930  1.00109.52           C  
ANISOU 3604  CB  PRO A1050    15917  11175  14520    263  -3601  -2121       C  
ATOM   3605  CG  PRO A1050     -11.376 175.553-211.160  1.00112.01           C  
ANISOU 3605  CG  PRO A1050    16116  11345  15098     98  -3987  -2223       C  
ATOM   3606  CD  PRO A1050     -11.133 174.228-211.827  1.00116.06           C  
ANISOU 3606  CD  PRO A1050    16683  11515  15901    181  -4300  -2695       C  
ATOM   3607  N   THR A1051      -7.894 175.159-208.536  1.00101.39           N  
ANISOU 3607  N   THR A1051    14718   9672  14134    166  -3285  -1649       N  
ATOM   3608  CA  THR A1051      -7.587 174.964-207.122  1.00101.35           C  
ANISOU 3608  CA  THR A1051    14570   9542  14397     38  -3201  -1254       C  
ATOM   3609  C   THR A1051      -8.638 175.552-206.184  1.00103.48           C  
ANISOU 3609  C   THR A1051    14691   9964  14662   -180  -3161   -832       C  
ATOM   3610  O   THR A1051      -8.892 175.012-205.109  1.00103.45           O  
ANISOU 3610  O   THR A1051    14548   9792  14966   -326  -3206   -504       O  
ATOM   3611  CB  THR A1051      -6.223 175.582-206.761  1.00 98.72           C  
ANISOU 3611  CB  THR A1051    14271   9373  13867    200  -2906  -1205       C  
ATOM   3612  OG1 THR A1051      -5.256 175.244-207.762  1.00101.08           O  
ANISOU 3612  OG1 THR A1051    14698   9611  14098    432  -2873  -1602       O  
ATOM   3613  CG2 THR A1051      -5.749 175.082-205.410  1.00 99.13           C  
ANISOU 3613  CG2 THR A1051    14195   9258  14214    133  -2905   -887       C  
ATOM   3614  N   ASN A1052      -9.243 176.662-206.595  1.00107.16           N  
ANISOU 3614  N   ASN A1052    15185  10757  14774   -179  -3058   -824       N  
ATOM   3615  CA  ASN A1052     -10.245 177.350-205.779  1.00108.54           C  
ANISOU 3615  CA  ASN A1052    15215  11116  14910   -350  -2991   -463       C  
ATOM   3616  C   ASN A1052     -11.478 176.495-205.492  1.00111.18           C  
ANISOU 3616  C   ASN A1052    15383  11219  15641   -572  -3239   -320       C  
ATOM   3617  O   ASN A1052     -12.216 176.758-204.539  1.00109.86           O  
ANISOU 3617  O   ASN A1052    15052  11140  15550   -725  -3165     50       O  
ATOM   3618  CB  ASN A1052     -10.668 178.659-206.449  1.00109.19           C  
ANISOU 3618  CB  ASN A1052    15359  11549  14579   -279  -2860   -523       C  
ATOM   3619  CG  ASN A1052     -11.085 178.462-207.892  1.00112.32           C  
ANISOU 3619  CG  ASN A1052    15876  11948  14852   -183  -3059   -883       C  
ATOM   3620  OD1 ASN A1052     -10.280 178.636-208.808  1.00114.62           O  
ANISOU 3620  OD1 ASN A1052    16343  12321  14888     30  -2978  -1153       O  
ATOM   3621  ND2 ASN A1052     -12.344 178.087-208.104  1.00112.10           N  
ANISOU 3621  ND2 ASN A1052    15741  11846  15004   -324  -3322   -894       N  
ATOM   3622  N   LYS A1053     -11.704 175.487-206.331  1.00113.08           N  
ANISOU 3622  N   LYS A1053    15649  11166  16152   -581  -3527   -628       N  
ATOM   3623  CA  LYS A1053     -12.777 174.526-206.103  1.00109.12           C  
ANISOU 3623  CA  LYS A1053    14951  10348  16161   -806  -3789   -525       C  
ATOM   3624  C   LYS A1053     -12.244 173.335-205.326  1.00108.53           C  
ANISOU 3624  C   LYS A1053    14805   9867  16564   -869  -3838   -351       C  
ATOM   3625  O   LYS A1053     -12.954 172.750-204.511  1.00111.58           O  
ANISOU 3625  O   LYS A1053    14984  10042  17368  -1076  -3888      7       O  
ATOM   3626  CB  LYS A1053     -13.383 174.067-207.430  1.00107.80           C  
ANISOU 3626  CB  LYS A1053    14819  10052  16087   -783  -4128   -996       C  
ATOM   3627  CG  LYS A1053     -14.070 175.178-208.192  1.00105.66           C  
ANISOU 3627  CG  LYS A1053    14598  10178  15368   -714  -4122  -1116       C  
ATOM   3628  CD  LYS A1053     -14.674 174.681-209.486  1.00108.88           C  
ANISOU 3628  CD  LYS A1053    15041  10495  15834   -659  -4507  -1604       C  
ATOM   3629  CE  LYS A1053     -15.390 175.805-210.202  1.00108.41           C  
ANISOU 3629  CE  LYS A1053    15026  10854  15311   -566  -4511  -1665       C  
ATOM   3630  NZ  LYS A1053     -16.402 176.446-209.316  1.00107.20           N1+
ANISOU 3630  NZ  LYS A1053    14635  10832  15266   -776  -4400  -1217       N1+
ATOM   3631  N   LEU A1054     -10.984 172.993-205.586  1.00106.11           N  
ANISOU 3631  N   LEU A1054    14658   9456  16204   -677  -3806   -579       N  
ATOM   3632  CA  LEU A1054     -10.312 171.883-204.917  1.00107.09           C  
ANISOU 3632  CA  LEU A1054    14735   9190  16765   -682  -3857   -434       C  
ATOM   3633  C   LEU A1054     -10.258 172.093-203.405  1.00107.24           C  
ANISOU 3633  C   LEU A1054    14634   9318  16794   -765  -3644    159       C  
ATOM   3634  O   LEU A1054     -10.550 171.179-202.630  1.00109.14           O  
ANISOU 3634  O   LEU A1054    14729   9245  17495   -895  -3715    501       O  
ATOM   3635  CB  LEU A1054      -8.889 171.708-205.464  1.00104.26           C  
ANISOU 3635  CB  LEU A1054    14561   8788  16266   -419  -3812   -790       C  
ATOM   3636  CG  LEU A1054      -8.621 170.711-206.598  1.00104.53           C  
ANISOU 3636  CG  LEU A1054    14682   8471  16563   -306  -4077  -1329       C  
ATOM   3637  CD1 LEU A1054      -9.608 170.894-207.734  1.00105.85           C  
ANISOU 3637  CD1 LEU A1054    14883   8728  16606   -336  -4284  -1698       C  
ATOM   3638  CD2 LEU A1054      -7.189 170.851-207.107  1.00102.22           C  
ANISOU 3638  CD2 LEU A1054    14562   8276  16001    -13  -3927  -1642       C  
ATOM   3639  N   LEU A1055      -9.887 173.306-203.003  1.00106.49           N  
ANISOU 3639  N   LEU A1055    14598   9670  16192   -673  -3383    275       N  
ATOM   3640  CA  LEU A1055      -9.705 173.658-201.596  1.00107.55           C  
ANISOU 3640  CA  LEU A1055    14650  10002  16212   -685  -3182    753       C  
ATOM   3641  C   LEU A1055     -10.940 173.381-200.757  1.00109.57           C  
ANISOU 3641  C   LEU A1055    14705  10222  16705   -902  -3180   1216       C  
ATOM   3642  O   LEU A1055     -10.841 172.900-199.628  1.00112.42           O  
ANISOU 3642  O   LEU A1055    14976  10521  17217   -923  -3113   1652       O  
ATOM   3643  CB  LEU A1055      -9.335 175.136-201.462  1.00103.87           C  
ANISOU 3643  CB  LEU A1055    14254  10018  15193   -571  -2940    709       C  
ATOM   3644  CG  LEU A1055      -7.902 175.557-201.781  1.00101.52           C  
ANISOU 3644  CG  LEU A1055    14091   9817  14665   -349  -2836    429       C  
ATOM   3645  CD1 LEU A1055      -7.898 176.959-202.365  1.00100.40           C  
ANISOU 3645  CD1 LEU A1055    14018  10032  14098   -283  -2657    236       C  
ATOM   3646  CD2 LEU A1055      -7.041 175.493-200.526  1.00 99.62           C  
ANISOU 3646  CD2 LEU A1055    13801   9644  14405   -258  -2751    701       C  
ATOM   3647  N   TYR A1056     -12.104 173.694-201.311  1.00107.58           N  
ANISOU 3647  N   TYR A1056    14371  10027  16479  -1047  -3244   1138       N  
ATOM   3648  CA  TYR A1056     -13.354 173.527-200.584  1.00108.57           C  
ANISOU 3648  CA  TYR A1056    14264  10145  16844  -1259  -3210   1569       C  
ATOM   3649  C   TYR A1056     -14.189 172.383-201.150  1.00114.90           C  
ANISOU 3649  C   TYR A1056    14910  10469  18276  -1456  -3487   1499       C  
ATOM   3650  O   TYR A1056     -15.394 172.320-200.928  1.00116.27           O  
ANISOU 3650  O   TYR A1056    14858  10619  18700  -1656  -3499   1737       O  
ATOM   3651  CB  TYR A1056     -14.136 174.848-200.568  1.00101.90           C  
ANISOU 3651  CB  TYR A1056    13373   9752  15591  -1279  -3048   1601       C  
ATOM   3652  CG  TYR A1056     -13.601 175.824-199.545  1.00 94.90           C  
ANISOU 3652  CG  TYR A1056    12537   9285  14237  -1142  -2762   1828       C  
ATOM   3653  CD1 TYR A1056     -12.601 176.728-199.872  1.00 86.35           C  
ANISOU 3653  CD1 TYR A1056    11640   8436  12734   -948  -2669   1531       C  
ATOM   3654  CD2 TYR A1056     -14.078 175.816-198.239  1.00 98.55           C  
ANISOU 3654  CD2 TYR A1056    12845   9905  14695  -1195  -2584   2333       C  
ATOM   3655  CE1 TYR A1056     -12.101 177.607-198.929  1.00 84.99           C  
ANISOU 3655  CE1 TYR A1056    11485   8612  12195   -826  -2450   1681       C  
ATOM   3656  CE2 TYR A1056     -13.587 176.692-197.290  1.00 96.25           C  
ANISOU 3656  CE2 TYR A1056    12600  10014  13955  -1041  -2360   2478       C  
ATOM   3657  CZ  TYR A1056     -12.598 177.584-197.637  1.00 91.91           C  
ANISOU 3657  CZ  TYR A1056    12224   9660  13039   -863  -2316   2126       C  
ATOM   3658  OH  TYR A1056     -12.116 178.448-196.677  1.00 93.57           O  
ANISOU 3658  OH  TYR A1056    12452  10239  12860   -714  -2134   2219       O  
ATOM   3659  N   GLY A1057     -13.535 171.468-201.859  1.00117.76           N  
ANISOU 3659  N   GLY A1057    15370  10438  18935  -1396  -3713   1156       N  
ATOM   3660  CA  GLY A1057     -14.226 170.371-202.515  1.00123.20           C  
ANISOU 3660  CA  GLY A1057    15918  10630  20261  -1561  -4030    965       C  
ATOM   3661  C   GLY A1057     -14.838 169.358-201.564  1.00127.85           C  
ANISOU 3661  C   GLY A1057    16241  10829  21507  -1780  -4032   1502       C  
ATOM   3662  O   GLY A1057     -15.824 168.696-201.896  1.00129.22           O  
ANISOU 3662  O   GLY A1057    16190  10653  22255  -1997  -4244   1473       O  
ATOM   3663  N   LYS A1058     -14.253 169.237-200.378  1.00127.76           N  
ANISOU 3663  N   LYS A1058    16239  10880  21426  -1715  -3798   2005       N  
ATOM   3664  CA  LYS A1058     -14.732 168.279-199.391  1.00131.87           C  
ANISOU 3664  CA  LYS A1058    16522  11057  22526  -1884  -3742   2616       C  
ATOM   3665  C   LYS A1058     -15.929 168.791-198.600  1.00130.07           C  
ANISOU 3665  C   LYS A1058    16056  11117  22248  -2058  -3510   3129       C  
ATOM   3666  O   LYS A1058     -16.788 168.015-198.191  1.00134.92           O  
ANISOU 3666  O   LYS A1058    16390  11397  23479  -2280  -3511   3535       O  
ATOM   3667  CB  LYS A1058     -13.607 167.883-198.437  1.00136.39           C  
ANISOU 3667  CB  LYS A1058    17206  11598  23017  -1701  -3602   2976       C  
ATOM   3668  CG  LYS A1058     -12.766 166.716-198.926  1.00143.02           C  
ANISOU 3668  CG  LYS A1058    18118  11862  24359  -1625  -3851   2716       C  
ATOM   3669  CD  LYS A1058     -11.663 166.379-197.938  1.00145.11           C  
ANISOU 3669  CD  LYS A1058    18478  12132  24525  -1420  -3722   3105       C  
ATOM   3670  CE  LYS A1058     -10.961 165.093-198.323  1.00150.74           C  
ANISOU 3670  CE  LYS A1058    19209  12196  25868  -1358  -3965   2930       C  
ATOM   3671  NZ  LYS A1058      -9.776 164.835-197.460  1.00153.26           N1+
ANISOU 3671  NZ  LYS A1058    19633  12553  26045  -1112  -3872   3246       N1+
ATOM   3672  N   ASP A1059     -15.987 170.098-198.387  1.00126.10           N  
ANISOU 3672  N   ASP A1059    15644  11217  21050  -1953  -3298   3113       N  
ATOM   3673  CA  ASP A1059     -17.035 170.673-197.557  1.00128.50           C  
ANISOU 3673  CA  ASP A1059    15735  11858  21233  -2065  -3037   3588       C  
ATOM   3674  C   ASP A1059     -18.278 171.016-198.368  1.00124.48           C  
ANISOU 3674  C   ASP A1059    15033  11352  20913  -2255  -3170   3342       C  
ATOM   3675  O   ASP A1059     -19.323 171.344-197.807  1.00124.61           O  
ANISOU 3675  O   ASP A1059    14803  11561  20983  -2386  -2984   3713       O  
ATOM   3676  CB  ASP A1059     -16.516 171.916-196.838  1.00130.84           C  
ANISOU 3676  CB  ASP A1059    16199  12787  20728  -1843  -2752   3682       C  
ATOM   3677  CG  ASP A1059     -15.137 171.708-196.249  1.00133.68           C  
ANISOU 3677  CG  ASP A1059    16773  13182  20839  -1614  -2701   3761       C  
ATOM   3678  OD1 ASP A1059     -15.034 171.032-195.201  1.00137.57           O  
ANISOU 3678  OD1 ASP A1059    17186  13590  21494  -1599  -2579   4311       O  
ATOM   3679  OD2 ASP A1059     -14.160 172.221-196.837  1.00130.56           O1-
ANISOU 3679  OD2 ASP A1059    16611  12904  20094  -1439  -2779   3294       O1-
ATOM   3680  N   ILE A1060     -18.157 170.933-199.690  1.00121.75           N  
ANISOU 3680  N   ILE A1060    14793  10814  20652  -2247  -3493   2711       N  
ATOM   3681  CA  ILE A1060     -19.260 171.276-200.594  1.00119.50           C  
ANISOU 3681  CA  ILE A1060    14351  10556  20498  -2382  -3689   2397       C  
ATOM   3682  C   ILE A1060     -20.555 170.470-200.391  1.00119.82           C  
ANISOU 3682  C   ILE A1060    13973  10230  21323  -2691  -3781   2696       C  
ATOM   3683  O   ILE A1060     -21.619 171.068-200.272  1.00119.34           O  
ANISOU 3683  O   ILE A1060    13686  10414  21244  -2800  -3692   2844       O  
ATOM   3684  CB  ILE A1060     -18.831 171.256-202.097  1.00115.69           C  
ANISOU 3684  CB  ILE A1060    14084   9956  19916  -2267  -4047   1642       C  
ATOM   3685  CG1 ILE A1060     -17.956 172.464-202.438  1.00102.04           C  
ANISOU 3685  CG1 ILE A1060    12686   8720  17365  -1992  -3899   1370       C  
ATOM   3686  CG2 ILE A1060     -20.050 171.213-203.011  1.00120.75           C  
ANISOU 3686  CG2 ILE A1060    14507  10493  20879  -2427  -4353   1337       C  
ATOM   3687  CD1 ILE A1060     -18.545 173.783-202.037  1.00 96.27           C  
ANISOU 3687  CD1 ILE A1060    11903   8512  16161  -1968  -3645   1576       C  
ATOM   3688  N   PRO A1061     -20.477 169.123-200.354  1.00122.21           N  
ANISOU 3688  N   PRO A1061    14147   9924  22365  -2832  -3955   2788       N  
ATOM   3689  CA  PRO A1061     -21.737 168.370-200.268  1.00130.76           C  
ANISOU 3689  CA  PRO A1061    14787  10605  24291  -3149  -4062   3033       C  
ATOM   3690  C   PRO A1061     -22.563 168.629-199.002  1.00137.55           C  
ANISOU 3690  C   PRO A1061    15352  11700  25211  -3279  -3643   3812       C  
ATOM   3691  O   PRO A1061     -23.799 168.635-199.078  1.00142.52           O  
ANISOU 3691  O   PRO A1061    15611  12273  26269  -3503  -3673   3927       O  
ATOM   3692  CB  PRO A1061     -21.274 166.913-200.315  1.00131.05           C  
ANISOU 3692  CB  PRO A1061    14778   9978  25036  -3208  -4250   3027       C  
ATOM   3693  CG  PRO A1061     -19.978 166.964-201.028  1.00126.26           C  
ANISOU 3693  CG  PRO A1061    14587   9344  24044  -2966  -4442   2479       C  
ATOM   3694  CD  PRO A1061     -19.329 168.218-200.547  1.00120.50           C  
ANISOU 3694  CD  PRO A1061    14139   9303  22343  -2720  -4107   2602       C  
ATOM   3695  N   GLN A1062     -21.905 168.839-197.865  1.00138.23           N  
ANISOU 3695  N   GLN A1062    15584  12066  24871  -3125  -3267   4325       N  
ATOM   3696  CA  GLN A1062     -22.624 169.130-196.628  1.00143.19           C  
ANISOU 3696  CA  GLN A1062    15969  13001  25437  -3186  -2835   5058       C  
ATOM   3697  C   GLN A1062     -23.404 170.427-196.795  1.00138.51           C  
ANISOU 3697  C   GLN A1062    15307  12964  24356  -3157  -2721   4900       C  
ATOM   3698  O   GLN A1062     -24.585 170.528-196.430  1.00140.95           O  
ANISOU 3698  O   GLN A1062    15244  13345  24965  -3332  -2556   5245       O  
ATOM   3699  CB  GLN A1062     -21.650 169.249-195.456  1.00146.33           C  
ANISOU 3699  CB  GLN A1062    16603  13698  25298  -2947  -2501   5523       C  
ATOM   3700  CG  GLN A1062     -22.332 169.298-194.099  1.00155.09           C  
ANISOU 3700  CG  GLN A1062    17464  15081  26383  -2981  -2045   6345       C  
ATOM   3701  CD  GLN A1062     -21.349 169.270-192.947  1.00159.57           C  
ANISOU 3701  CD  GLN A1062    18267  15924  26439  -2716  -1774   6799       C  
ATOM   3702  OE1 GLN A1062     -20.157 169.523-193.127  1.00158.77           O  
ANISOU 3702  OE1 GLN A1062    18521  15935  25871  -2488  -1902   6446       O  
ATOM   3703  NE2 GLN A1062     -21.843 168.956-191.753  1.00164.02           N  
ANISOU 3703  NE2 GLN A1062    18624  16690  27006  -2685  -1390   7486       N  
ATOM   3704  N   TYR A1063     -22.725 171.410-197.376  1.00130.74           N  
ANISOU 3704  N   TYR A1063    14668  12348  22661  -2929  -2806   4381       N  
ATOM   3705  CA  TYR A1063     -23.314 172.706-197.667  1.00123.71           C  
ANISOU 3705  CA  TYR A1063    13764  11955  21284  -2859  -2736   4163       C  
ATOM   3706  C   TYR A1063     -24.494 172.559-198.621  1.00124.13           C  
ANISOU 3706  C   TYR A1063    13514  11785  21866  -3077  -3038   3878       C  
ATOM   3707  O   TYR A1063     -25.511 173.223-198.455  1.00127.18           O  
ANISOU 3707  O   TYR A1063    13647  12451  22222  -3138  -2904   4018       O  
ATOM   3708  CB  TYR A1063     -22.263 173.633-198.277  1.00117.47           C  
ANISOU 3708  CB  TYR A1063    13398  11473  19761  -2588  -2813   3640       C  
ATOM   3709  CG  TYR A1063     -21.075 173.925-197.382  1.00115.67           C  
ANISOU 3709  CG  TYR A1063    13450  11506  18992  -2356  -2554   3837       C  
ATOM   3710  CD1 TYR A1063     -21.136 173.699-196.012  1.00118.98           C  
ANISOU 3710  CD1 TYR A1063    13757  12065  19384  -2343  -2223   4469       C  
ATOM   3711  CD2 TYR A1063     -19.894 174.438-197.909  1.00109.92           C  
ANISOU 3711  CD2 TYR A1063    13082  10905  17776  -2136  -2642   3394       C  
ATOM   3712  CE1 TYR A1063     -20.054 173.967-195.193  1.00115.83           C  
ANISOU 3712  CE1 TYR A1063    13606  11933  18471  -2106  -2038   4613       C  
ATOM   3713  CE2 TYR A1063     -18.808 174.708-197.099  1.00106.85           C  
ANISOU 3713  CE2 TYR A1063    12909  10744  16944  -1928  -2444   3539       C  
ATOM   3714  CZ  TYR A1063     -18.892 174.472-195.742  1.00109.26           C  
ANISOU 3714  CZ  TYR A1063    13105  11194  17213  -1909  -2168   4127       C  
ATOM   3715  OH  TYR A1063     -17.816 174.739-194.929  1.00105.33           O  
ANISOU 3715  OH  TYR A1063    12814  10951  16255  -1678  -2019   4238       O  
ATOM   3716  N   LYS A1064     -24.344 171.686-199.614  1.00121.53           N  
ANISOU 3716  N   LYS A1064    13199  10958  22021  -3174  -3461   3450       N  
ATOM   3717  CA  LYS A1064     -25.388 171.410-200.596  1.00120.45           C  
ANISOU 3717  CA  LYS A1064    12773  10561  22431  -3368  -3842   3094       C  
ATOM   3718  C   LYS A1064     -26.641 170.886-199.907  1.00123.57           C  
ANISOU 3718  C   LYS A1064    12633  10747  23570  -3666  -3700   3633       C  
ATOM   3719  O   LYS A1064     -27.761 171.345-200.172  1.00121.68           O  
ANISOU 3719  O   LYS A1064    12085  10654  23494  -3775  -3759   3587       O  
ATOM   3720  CB  LYS A1064     -24.890 170.373-201.603  1.00121.98           C  
ANISOU 3720  CB  LYS A1064    13075  10207  23064  -3403  -4309   2565       C  
ATOM   3721  CG  LYS A1064     -24.588 170.906-202.992  1.00121.48           C  
ANISOU 3721  CG  LYS A1064    13294  10309  22556  -3212  -4678   1793       C  
ATOM   3722  CD  LYS A1064     -24.017 169.800-203.868  1.00127.54           C  
ANISOU 3722  CD  LYS A1064    14178  10545  23737  -3211  -5101   1278       C  
ATOM   3723  CE  LYS A1064     -24.263 170.049-205.348  1.00131.39           C  
ANISOU 3723  CE  LYS A1064    14764  11105  24053  -3099  -5569    513       C  
ATOM   3724  NZ  LYS A1064     -24.018 168.815-206.153  1.00137.26           N1+
ANISOU 3724  NZ  LYS A1064    15512  11305  25335  -3113  -5996      1       N1+
ATOM   3725  N   GLN A1065     -26.436 169.919-199.018  1.00130.11           N  
ANISOU 3725  N   GLN A1065    13338  11229  24866  -3786  -3501   4171       N  
ATOM   3726  CA  GLN A1065     -27.531 169.347-198.245  1.00140.17           C  
ANISOU 3726  CA  GLN A1065    14135  12379  26746  -3975  -3250   4738       C  
ATOM   3727  C   GLN A1065     -28.219 170.427-197.424  1.00140.49           C  
ANISOU 3727  C   GLN A1065    13993  12961  26425  -3987  -2828   5216       C  
ATOM   3728  O   GLN A1065     -29.449 170.522-197.409  1.00142.01           O  
ANISOU 3728  O   GLN A1065    13779  13222  26955  -4103  -2770   5317       O  
ATOM   3729  CB  GLN A1065     -27.020 168.232-197.338  1.00144.73           C  
ANISOU 3729  CB  GLN A1065    14724  12699  27568  -3921  -3008   5219       C  
ATOM   3730  N   GLU A1066     -27.420 171.246-196.746  1.00138.84           N  
ANISOU 3730  N   GLU A1066    14138  13269  25347  -3712  -2505   5374       N  
ATOM   3731  CA  GLU A1066     -27.969 172.314-195.920  1.00141.19           C  
ANISOU 3731  CA  GLU A1066    14335  14184  25125  -3597  -2072   5721       C  
ATOM   3732  C   GLU A1066     -28.770 173.304-196.765  1.00138.81           C  
ANISOU 3732  C   GLU A1066    13922  14149  24670  -3589  -2258   5257       C  
ATOM   3733  O   GLU A1066     -29.746 173.889-196.298  1.00141.54           O  
ANISOU 3733  O   GLU A1066    13957  14807  25014  -3619  -1993   5535       O  
ATOM   3734  CB  GLU A1066     -26.856 173.028-195.151  1.00141.15           C  
ANISOU 3734  CB  GLU A1066    14764  14668  24200  -3269  -1778   5825       C  
ATOM   3735  CG  GLU A1066     -27.343 174.164-194.266  1.00144.18           C  
ANISOU 3735  CG  GLU A1066    15073  15704  24003  -3106  -1342   6114       C  
ATOM   3736  CD  GLU A1066     -28.405 173.730-193.273  1.00152.32           C  
ANISOU 3736  CD  GLU A1066    15642  16761  25472  -3263   -951   6844       C  
ATOM   3737  OE1 GLU A1066     -28.220 172.680-192.622  1.00156.58           O  
ANISOU 3737  OE1 GLU A1066    16092  17004  26396  -3355   -809   7369       O  
ATOM   3738  OE2 GLU A1066     -29.425 174.442-193.146  1.00154.10           O1-
ANISOU 3738  OE2 GLU A1066    15581  17299  25670  -3282   -770   6914       O1-
ATOM   3739  N   VAL A1067     -28.356 173.470-198.017  1.00133.08           N  
ANISOU 3739  N   VAL A1067    13443  13304  23816  -3526  -2709   4563       N  
ATOM   3740  CA  VAL A1067     -29.034 174.364-198.949  1.00127.13           C  
ANISOU 3740  CA  VAL A1067    12624  12782  22898  -3484  -2947   4100       C  
ATOM   3741  C   VAL A1067     -30.398 173.815-199.346  1.00134.88           C  
ANISOU 3741  C   VAL A1067    13059  13450  24739  -3778  -3175   4116       C  
ATOM   3742  O   VAL A1067     -31.406 174.521-199.266  1.00135.10           O  
ANISOU 3742  O   VAL A1067    12787  13766  24778  -3798  -3069   4208       O  
ATOM   3743  CB  VAL A1067     -28.185 174.603-200.214  1.00118.81           C  
ANISOU 3743  CB  VAL A1067    11993  11691  21459  -3311  -3363   3386       C  
ATOM   3744  CG1 VAL A1067     -29.051 175.099-201.357  1.00120.47           C  
ANISOU 3744  CG1 VAL A1067    12053  11973  21747  -3323  -3737   2919       C  
ATOM   3745  CG2 VAL A1067     -27.072 175.586-199.920  1.00109.08           C  
ANISOU 3745  CG2 VAL A1067    11224  10897  19325  -3003  -3114   3324       C  
ATOM   3746  N   LYS A1068     -30.430 172.555-199.771  1.00142.70           N  
ANISOU 3746  N   LYS A1068    13895  13830  26494  -4003  -3500   4009       N  
ATOM   3747  CA  LYS A1068     -31.691 171.934-200.173  1.00152.02           C  
ANISOU 3747  CA  LYS A1068    14548  14666  28546  -4264  -3750   3960       C  
ATOM   3748  C   LYS A1068     -32.673 171.866-199.000  1.00154.85           C  
ANISOU 3748  C   LYS A1068    14481  15167  29189  -4347  -3235   4661       C  
ATOM   3749  O   LYS A1068     -33.871 172.151-199.150  1.00156.41           O  
ANISOU 3749  O   LYS A1068    14288  15472  29669  -4413  -3251   4652       O  
ATOM   3750  CB  LYS A1068     -31.437 170.553-200.781  1.00159.45           C  
ANISOU 3750  CB  LYS A1068    15540  15023  30022  -4294  -4102   3617       C  
ATOM   3751  CG  LYS A1068     -30.618 170.612-202.066  1.00158.78           C  
ANISOU 3751  CG  LYS A1068    15850  14839  29638  -4165  -4624   2842       C  
ATOM   3752  CD  LYS A1068     -30.138 169.241-202.509  1.00164.54           C  
ANISOU 3752  CD  LYS A1068    16680  15025  30813  -4147  -4887   2547       C  
ATOM   3753  CE  LYS A1068     -29.202 169.351-203.705  1.00162.64           C  
ANISOU 3753  CE  LYS A1068    16879  14763  30152  -3960  -5324   1800       C  
ATOM   3754  NZ  LYS A1068     -28.527 168.059-204.012  1.00166.53           N1+
ANISOU 3754  NZ  LYS A1068    17507  14767  30999  -3903  -5506   1548       N1+
ATOM   3755  N   SER A1069     -32.151 171.512-197.829  1.00154.94           N  
ANISOU 3755  N   SER A1069    14581  15214  29075  -4305  -2775   5260       N  
ATOM   3756  CA  SER A1069     -32.941 171.515-196.605  1.00157.61           C  
ANISOU 3756  CA  SER A1069    14586  15784  29514  -4313  -2222   5959       C  
ATOM   3757  C   SER A1069     -33.439 172.924-196.287  1.00152.00           C  
ANISOU 3757  C   SER A1069    13768  15681  28302  -4239  -1947   6090       C  
ATOM   3758  O   SER A1069     -34.537 173.097-195.762  1.00155.69           O  
ANISOU 3758  O   SER A1069    13841  16337  28977  -4264  -1653   6413       O  
ATOM   3759  CB  SER A1069     -32.121 170.967-195.433  1.00158.81           C  
ANISOU 3759  CB  SER A1069    14942  15956  29444  -4203  -1807   6534       C  
ATOM   3760  OG  SER A1069     -31.784 169.604-195.635  1.00163.69           O  
ANISOU 3760  OG  SER A1069    15577  16005  30613  -4266  -2020   6475       O  
ATOM   3761  N   TYR A1070     -32.627 173.925-196.617  1.00142.79           N  
ANISOU 3761  N   TYR A1070    13011  14860  26385  -4054  -2030   5758       N  
ATOM   3762  CA  TYR A1070     -32.975 175.322-196.372  1.00136.75           C  
ANISOU 3762  CA  TYR A1070    12283  14731  24946  -3823  -1779   5717       C  
ATOM   3763  C   TYR A1070     -34.143 175.768-197.242  1.00135.79           C  
ANISOU 3763  C   TYR A1070    11791  14621  25183  -3923  -2076   5382       C  
ATOM   3764  O   TYR A1070     -35.086 176.393-196.757  1.00134.49           O  
ANISOU 3764  O   TYR A1070    11277  14780  25041  -3908  -1781   5647       O  
ATOM   3765  CB  TYR A1070     -31.760 176.222-196.618  1.00129.42           C  
ANISOU 3765  CB  TYR A1070    11973  14142  23060  -3492  -1826   5306       C  
ATOM   3766  CG  TYR A1070     -32.049 177.707-196.577  1.00125.82           C  
ANISOU 3766  CG  TYR A1070    11584  14257  21964  -3247  -1659   5143       C  
ATOM   3767  CD1 TYR A1070     -32.047 178.402-195.376  1.00124.71           C  
ANISOU 3767  CD1 TYR A1070    11455  14598  21333  -3062  -1132   5537       C  
ATOM   3768  CD2 TYR A1070     -32.307 178.417-197.743  1.00122.87           C  
ANISOU 3768  CD2 TYR A1070    11272  13944  21470  -3175  -2036   4586       C  
ATOM   3769  CE1 TYR A1070     -32.304 179.757-195.335  1.00120.95           C  
ANISOU 3769  CE1 TYR A1070    11029  14597  20328  -2830   -990   5354       C  
ATOM   3770  CE2 TYR A1070     -32.567 179.770-197.711  1.00119.22           C  
ANISOU 3770  CE2 TYR A1070    10863  13954  20483  -2945  -1883   4463       C  
ATOM   3771  CZ  TYR A1070     -32.564 180.435-196.506  1.00117.86           C  
ANISOU 3771  CZ  TYR A1070    10683  14206  19894  -2782  -1363   4832       C  
ATOM   3772  OH  TYR A1070     -32.823 181.784-196.469  1.00113.85           O  
ANISOU 3772  OH  TYR A1070    10215  14126  18918  -2545  -1220   4677       O  
ATOM   3773  N   TYR A1071     -34.068 175.451-198.531  1.00136.40           N  
ANISOU 3773  N   TYR A1071    11943  14366  25516  -3995  -2668   4783       N  
ATOM   3774  CA  TYR A1071     -35.135 175.792-199.465  1.00138.61           C  
ANISOU 3774  CA  TYR A1071    11884  14640  26142  -4070  -3048   4411       C  
ATOM   3775  C   TYR A1071     -36.415 175.059-199.106  1.00142.11           C  
ANISOU 3775  C   TYR A1071    11702  14819  27473  -4325  -2955   4754       C  
ATOM   3776  O   TYR A1071     -37.512 175.614-199.225  1.00143.11           O  
ANISOU 3776  O   TYR A1071    11469  15153  27752  -4317  -2943   4735       O  
ATOM   3777  CB  TYR A1071     -34.724 175.484-200.908  1.00142.77           C  
ANISOU 3777  CB  TYR A1071    12661  14881  26704  -4050  -3717   3681       C  
ATOM   3778  CG  TYR A1071     -33.784 176.512-201.495  1.00141.93           C  
ANISOU 3778  CG  TYR A1071    13149  15158  25621  -3698  -3802   3253       C  
ATOM   3779  CD1 TYR A1071     -33.474 177.671-200.796  1.00139.31           C  
ANISOU 3779  CD1 TYR A1071    13036  15346  24549  -3452  -3350   3479       C  
ATOM   3780  CD2 TYR A1071     -33.217 176.333-202.751  1.00143.17           C  
ANISOU 3780  CD2 TYR A1071    13628  15155  25614  -3601  -4322   2623       C  
ATOM   3781  CE1 TYR A1071     -32.621 178.617-201.320  1.00134.53           C  
ANISOU 3781  CE1 TYR A1071    12932  15041  23142  -3151  -3408   3120       C  
ATOM   3782  CE2 TYR A1071     -32.361 177.279-203.287  1.00138.95           C  
ANISOU 3782  CE2 TYR A1071    13610  14967  24216  -3280  -4349   2294       C  
ATOM   3783  CZ  TYR A1071     -32.067 178.418-202.566  1.00134.65           C  
ANISOU 3783  CZ  TYR A1071    13250  14888  23023  -3072  -3888   2560       C  
ATOM   3784  OH  TYR A1071     -31.218 179.364-203.088  1.00130.89           O  
ANISOU 3784  OH  TYR A1071    13248  14707  21777  -2773  -3898   2262       O  
ATOM   3785  N   LYS A1072     -36.271 173.812-198.662  1.00144.32           N  
ANISOU 3785  N   LYS A1072    11961  14678  28196  -4429  -2847   5009       N  
ATOM   3786  CA  LYS A1072     -37.416 173.068-198.150  1.00148.08           C  
ANISOU 3786  CA  LYS A1072    11967  14946  29352  -4550  -2635   5367       C  
ATOM   3787  C   LYS A1072     -38.053 173.814-196.978  1.00147.42           C  
ANISOU 3787  C   LYS A1072    11629  15352  29033  -4477  -2005   5969       C  
ATOM   3788  O   LYS A1072     -39.214 174.211-197.053  1.00147.16           O  
ANISOU 3788  O   LYS A1072    11199  15459  29255  -4500  -1967   5972       O  
ATOM   3789  CB  LYS A1072     -37.005 171.654-197.730  1.00151.45           C  
ANISOU 3789  CB  LYS A1072    12436  14880  30228  -4635  -2565   5623       C  
ATOM   3790  CG  LYS A1072     -36.856 170.667-198.883  1.00153.97           C  
ANISOU 3790  CG  LYS A1072    12816  14632  31055  -4722  -3177   5026       C  
ATOM   3791  CD  LYS A1072     -38.199 170.339-199.521  1.00160.44           C  
ANISOU 3791  CD  LYS A1072    13172  15223  32566  -4843  -3469   4765       C  
ATOM   3792  CE  LYS A1072     -39.152 169.700-198.521  1.00166.66           C  
ANISOU 3792  CE  LYS A1072    13488  15871  33965  -4963  -3031   5405       C  
ATOM   3793  NZ  LYS A1072     -40.518 169.532-199.090  1.00167.94           N1+
ANISOU 3793  NZ  LYS A1072    13166  15857  34787  -5082  -3285   5174       N1+
ATOM   3794  N   LEU A1073     -37.276 174.016-195.914  1.00147.80           N  
ANISOU 3794  N   LEU A1073    11919  15680  28557  -4357  -1522   6445       N  
ATOM   3795  CA  LEU A1073     -37.736 174.718-194.711  1.00151.91           C  
ANISOU 3795  CA  LEU A1073    12273  16729  28716  -4218   -885   7001       C  
ATOM   3796  C   LEU A1073     -38.425 176.041-195.023  1.00149.50           C  
ANISOU 3796  C   LEU A1073    11777  16872  28154  -4130   -884   6784       C  
ATOM   3797  O   LEU A1073     -39.441 176.384-194.416  1.00151.27           O  
ANISOU 3797  O   LEU A1073    11639  17357  28478  -4080   -518   7084       O  
ATOM   3798  CB  LEU A1073     -36.570 174.964-193.751  1.00150.89           C  
ANISOU 3798  CB  LEU A1073    12556  16918  27857  -4034   -489   7359       C  
ATOM   3799  CG  LEU A1073     -36.032 173.742-193.006  1.00157.22           C  
ANISOU 3799  CG  LEU A1073    13485  17427  28826  -4039   -298   7782       C  
ATOM   3800  CD1 LEU A1073     -34.728 174.074-192.302  1.00154.73           C  
ANISOU 3800  CD1 LEU A1073    13649  17423  27716  -3829    -53   7980       C  
ATOM   3801  CD2 LEU A1073     -37.060 173.234-192.012  1.00164.34           C  
ANISOU 3801  CD2 LEU A1073    13983  18379  30079  -4034    164   8364       C  
ATOM   3802  N   VAL A1074     -37.863 176.782-195.971  1.00144.24           N  
ANISOU 3802  N   VAL A1074    11352  16295  27158  -4091  -1293   6263       N  
ATOM   3803  CA  VAL A1074     -38.454 178.040-196.402  1.00140.70           C  
ANISOU 3803  CA  VAL A1074    10753  16248  26459  -3965  -1370   5994       C  
ATOM   3804  C   VAL A1074     -39.795 177.794-197.081  1.00145.87           C  
ANISOU 3804  C   VAL A1074    10941  16682  27799  -4089  -1673   5774       C  
ATOM   3805  O   VAL A1074     -40.755 178.524-196.854  1.00149.16           O  
ANISOU 3805  O   VAL A1074    11024  17413  28235  -4004  -1469   5870       O  
ATOM   3806  CB  VAL A1074     -37.513 178.808-197.350  1.00132.26           C  
ANISOU 3806  CB  VAL A1074    10294  15313  24645  -3705  -1764   5334       C  
ATOM   3807  CG1 VAL A1074     -38.223 180.005-197.962  1.00130.83           C  
ANISOU 3807  CG1 VAL A1074     9998  15467  24246  -3525  -1920   4996       C  
ATOM   3808  CG2 VAL A1074     -36.272 179.252-196.601  1.00126.58           C  
ANISOU 3808  CG2 VAL A1074    10138  14895  23061  -3441  -1412   5445       C  
ATOM   3809  N   LYS A1075     -39.859 176.749-197.900  1.00146.29           N  
ANISOU 3809  N   LYS A1075    10991  16197  28396  -4257  -2154   5451       N  
ATOM   3810  CA  LYS A1075     -41.084 176.425-198.623  1.00149.36           C  
ANISOU 3810  CA  LYS A1075    10977  16345  29426  -4360  -2500   5172       C  
ATOM   3811  C   LYS A1075     -42.213 175.993-197.684  1.00155.99           C  
ANISOU 3811  C   LYS A1075    11335  17151  30781  -4445  -2035   5703       C  
ATOM   3812  O   LYS A1075     -43.384 176.277-197.938  1.00157.68           O  
ANISOU 3812  O   LYS A1075    11145  17423  31344  -4463  -2106   5614       O  
ATOM   3813  CB  LYS A1075     -40.817 175.337-199.668  1.00150.22           C  
ANISOU 3813  CB  LYS A1075    11220  15891  29967  -4489  -3104   4681       C  
ATOM   3814  CG  LYS A1075     -41.979 175.083-200.611  1.00155.86           C  
ANISOU 3814  CG  LYS A1075    11576  16387  31255  -4560  -3567   4262       C  
ATOM   3815  CD  LYS A1075     -41.677 173.968-201.603  1.00161.03           C  
ANISOU 3815  CD  LYS A1075    12378  16506  32299  -4650  -4140   3750       C  
ATOM   3816  CE  LYS A1075     -42.915 173.621-202.426  1.00170.98           C  
ANISOU 3816  CE  LYS A1075    13238  17546  34181  -4721  -4566   3373       C  
ATOM   3817  NZ  LYS A1075     -42.714 172.435-203.308  1.00176.96           N1+
ANISOU 3817  NZ  LYS A1075    14087  17766  35382  -4797  -5087   2887       N1+
ATOM   3818  N   ASP A1076     -41.856 175.320-196.594  1.00160.49           N  
ANISOU 3818  N   ASP A1076    11955  17646  31378  -4477  -1558   6263       N  
ATOM   3819  CA  ASP A1076     -42.851 174.742-195.689  1.00167.70           C  
ANISOU 3819  CA  ASP A1076    12435  18483  32799  -4551  -1117   6801       C  
ATOM   3820  C   ASP A1076     -43.251 175.683-194.553  1.00169.70           C  
ANISOU 3820  C   ASP A1076    12555  19337  32586  -4363   -456   7283       C  
ATOM   3821  O   ASP A1076     -44.174 175.388-193.794  1.00175.35           O  
ANISOU 3821  O   ASP A1076    12893  20080  33652  -4386    -56   7722       O  
ATOM   3822  CB  ASP A1076     -42.358 173.408-195.136  1.00168.56           C  
ANISOU 3822  CB  ASP A1076    12633  18171  33241  -4656   -975   7166       C  
ATOM   3823  N   GLN A1077     -42.554 176.810-194.438  1.00165.90           N  
ANISOU 3823  N   GLN A1077    12381  19337  31317  -4160   -340   7188       N  
ATOM   3824  CA  GLN A1077     -42.891 177.824-193.442  1.00167.97           C  
ANISOU 3824  CA  GLN A1077    12546  20210  31064  -3929    251   7534       C  
ATOM   3825  C   GLN A1077     -44.250 178.439-193.770  1.00176.50           C  
ANISOU 3825  C   GLN A1077    13151  21426  32484  -3918    209   7382       C  
ATOM   3826  O   GLN A1077     -44.626 178.529-194.938  1.00176.28           O  
ANISOU 3826  O   GLN A1077    13006  21175  32798  -4016   -356   6879       O  
ATOM   3827  CB  GLN A1077     -41.811 178.909-193.394  1.00158.03           C  
ANISOU 3827  CB  GLN A1077    11713  19395  28938  -3712    307   7372       C  
ATOM   3828  CG  GLN A1077     -42.025 179.965-192.315  1.00156.41           C  
ANISOU 3828  CG  GLN A1077    11465  19844  28121  -3420    926   7676       C  
ATOM   3829  CD  GLN A1077     -40.948 181.035-192.314  1.00147.41           C  
ANISOU 3829  CD  GLN A1077    10724  19115  26169  -3201    956   7473       C  
ATOM   3830  OE1 GLN A1077     -40.005 180.983-193.102  1.00140.75           O  
ANISOU 3830  OE1 GLN A1077    10251  18063  25165  -3250    520   7105       O  
ATOM   3831  NE2 GLN A1077     -41.085 182.014-191.425  1.00146.61           N  
ANISOU 3831  NE2 GLN A1077    10612  19596  25499  -2906   1461   7644       N  
ATOM   3832  N   THR A1078     -44.984 178.847-192.737  1.00184.36           N  
ANISOU 3832  N   THR A1078    13886  22801  33362  -3774    797   7803       N  
ATOM   3833  CA  THR A1078     -46.314 179.435-192.910  1.00189.65           C  
ANISOU 3833  CA  THR A1078    14080  23622  34358  -3743    830   7711       C  
ATOM   3834  C   THR A1078     -46.297 180.648-193.842  1.00182.71           C  
ANISOU 3834  C   THR A1078    13256  22982  33185  -3606    448   7164       C  
ATOM   3835  O   THR A1078     -45.381 181.470-193.793  1.00174.35           O  
ANISOU 3835  O   THR A1078    12558  22250  31438  -3414    494   7041       O  
ATOM   3836  CB  THR A1078     -46.950 179.818-191.551  1.00195.18           C  
ANISOU 3836  CB  THR A1078    14562  24778  34819  -3544   1583   8238       C  
ATOM   3837  OG1 THR A1078     -48.163 180.548-191.774  1.00198.26           O  
ANISOU 3837  OG1 THR A1078    14515  25350  35462  -3482   1599   8089       O  
ATOM   3838  CG2 THR A1078     -45.993 180.671-190.728  1.00190.78           C  
ANISOU 3838  CG2 THR A1078    14417  24774  33295  -3236   1995   8367       C  
ATOM   3839  N   SER A1079     -47.311 180.742-194.700  1.00185.53           N  
ANISOU 3839  N   SER A1079    13248  23170  34076  -3693     56   6841       N  
ATOM   3840  CA  SER A1079     -47.400 181.828-195.672  1.00180.10           C  
ANISOU 3840  CA  SER A1079    12586  22678  33167  -3544   -369   6325       C  
ATOM   3841  C   SER A1079     -47.701 183.169-195.016  1.00178.66           C  
ANISOU 3841  C   SER A1079    12315  23084  32485  -3229     89   6439       C  
ATOM   3842  O   SER A1079     -48.089 183.235-193.850  1.00183.87           O  
ANISOU 3842  O   SER A1079    12817  24003  33043  -3135    721   6880       O  
ATOM   3843  CB  SER A1079     -48.437 181.518-196.755  1.00183.19           C  
ANISOU 3843  CB  SER A1079    12616  22744  34244  -3691   -934   5945       C  
ATOM   3844  OG  SER A1079     -47.879 180.702-197.769  1.00181.32           O  
ANISOU 3844  OG  SER A1079    12613  22057  34226  -3870  -1554   5565       O  
ATOM   3845  N   ILE A1080     -47.524 184.236-195.783  1.00171.69           N  
ANISOU 3845  N   ILE A1080    11544  22410  31281  -3036   -243   6025       N  
ATOM   3846  CA  ILE A1080     -47.573 185.581-195.241  1.00168.06           C  
ANISOU 3846  CA  ILE A1080    11084  22486  30286  -2694    143   6061       C  
ATOM   3847  C   ILE A1080     -48.576 186.447-195.982  1.00169.10           C  
ANISOU 3847  C   ILE A1080    10896  22721  30634  -2547   -154   5735       C  
ATOM   3848  O   ILE A1080     -48.360 186.805-197.141  1.00167.09           O  
ANISOU 3848  O   ILE A1080    10775  22366  30344  -2503   -752   5308       O  
ATOM   3849  CB  ILE A1080     -46.198 186.249-195.359  1.00161.52           C  
ANISOU 3849  CB  ILE A1080    10755  21865  28750  -2518     83   5903       C  
ATOM   3850  CG1 ILE A1080     -45.113 185.319-194.815  1.00160.54           C  
ANISOU 3850  CG1 ILE A1080    10981  21587  28430  -2680    256   6167       C  
ATOM   3851  CG2 ILE A1080     -46.191 187.593-194.648  1.00159.71           C  
ANISOU 3851  CG2 ILE A1080    10539  22180  27965  -2138    548   5949       C  
ATOM   3852  CD1 ILE A1080     -43.719 185.720-195.204  1.00154.49           C  
ANISOU 3852  CD1 ILE A1080    10903  20847  26949  -2526     28   5839       C  
ATOM   3853  N   SER A1081     -49.669 186.791-195.311  1.00172.71           N  
ANISOU 3853  N   SER A1081    10944  23393  31286  -2447    263   5940       N  
ATOM   3854  CA  SER A1081     -50.631 187.724-195.881  1.00174.11           C  
ANISOU 3854  CA  SER A1081    10810  23717  31627  -2259     50   5663       C  
ATOM   3855  C   SER A1081     -49.974 189.092-196.020  1.00170.06           C  
ANISOU 3855  C   SER A1081    10587  23560  30469  -1893     51   5441       C  
ATOM   3856  O   SER A1081     -48.953 189.363-195.388  1.00165.80           O  
ANISOU 3856  O   SER A1081    10402  23227  29366  -1771    377   5565       O  
ATOM   3857  CB  SER A1081     -51.877 187.808-195.015  1.00178.86           C  
ANISOU 3857  CB  SER A1081    10920  24493  32545  -2216    563   5953       C  
ATOM   3858  N   SER A1082     -50.557 189.956-196.842  1.00171.86           N  
ANISOU 3858  N   SER A1082    10663  23852  30782  -1702   -318   5116       N  
ATOM   3859  CA  SER A1082     -49.958 191.259-197.110  1.00168.36           C  
ANISOU 3859  CA  SER A1082    10494  23676  29800  -1339   -384   4895       C  
ATOM   3860  C   SER A1082     -50.174 192.260-195.978  1.00170.44           C  
ANISOU 3860  C   SER A1082    10666  24364  29729  -1012    291   5055       C  
ATOM   3861  O   SER A1082     -49.847 193.436-196.117  1.00168.15           O  
ANISOU 3861  O   SER A1082    10538  24284  29065   -671    288   4864       O  
ATOM   3862  CB  SER A1082     -50.471 191.824-198.435  1.00169.32           C  
ANISOU 3862  CB  SER A1082    10534  23701  30100  -1211  -1045   4509       C  
ATOM   3863  OG  SER A1082     -49.969 191.071-199.525  1.00168.43           O  
ANISOU 3863  OG  SER A1082    10660  23263  30072  -1421  -1690   4275       O  
ATOM   3864  N   GLN A1083     -50.728 191.789-194.863  1.00175.27           N  
ANISOU 3864  N   GLN A1083    11031  25092  30472  -1094    864   5393       N  
ATOM   3865  CA  GLN A1083     -50.866 192.606-193.663  1.00176.92           C  
ANISOU 3865  CA  GLN A1083    11203  25733  30285   -777   1546   5533       C  
ATOM   3866  C   GLN A1083     -49.504 192.783-193.003  1.00170.48           C  
ANISOU 3866  C   GLN A1083    10881  25122  28770   -646   1847   5599       C  
ATOM   3867  O   GLN A1083     -49.120 193.892-192.615  1.00167.99           O  
ANISOU 3867  O   GLN A1083    10741  25120  27967   -280   2088   5442       O  
ATOM   3868  CB  GLN A1083     -51.852 191.957-192.687  1.00185.99           C  
ANISOU 3868  CB  GLN A1083    11966  26953  31749   -900   2054   5897       C  
ATOM   3869  CG  GLN A1083     -51.764 192.478-191.258  1.00189.07           C  
ANISOU 3869  CG  GLN A1083    12429  27803  31605   -607   2811   6096       C  
ATOM   3870  CD  GLN A1083     -52.098 193.952-191.141  1.00190.24           C  
ANISOU 3870  CD  GLN A1083    12511  28275  31496   -172   2956   5800       C  
ATOM   3871  OE1 GLN A1083     -51.451 194.687-190.395  1.00188.51           O  
ANISOU 3871  OE1 GLN A1083    12583  28390  30654    143   3326   5726       O  
ATOM   3872  NE2 GLN A1083     -53.119 194.390-191.870  1.00193.06           N  
ANISOU 3872  NE2 GLN A1083    12487  28526  32339   -136   2650   5605       N  
ATOM   3873  N   GLU A1084     -48.777 191.676-192.880  1.00170.06           N  
ANISOU 3873  N   GLU A1084    11051  24875  28690   -938   1817   5811       N  
ATOM   3874  CA  GLU A1084     -47.416 191.700-192.350  1.00166.17           C  
ANISOU 3874  CA  GLU A1084    11035  24544  27558   -853   2028   5872       C  
ATOM   3875  C   GLU A1084     -46.512 192.495-193.284  1.00159.30           C  
ANISOU 3875  C   GLU A1084    10758  23534  26235   -680   1533   5356       C  
ATOM   3876  O   GLU A1084     -45.639 193.241-192.834  1.00154.72           O  
ANISOU 3876  O   GLU A1084    10672  23144  24971   -404   1722   5163       O  
ATOM   3877  CB  GLU A1084     -46.884 190.284-192.172  1.00167.01           C  
ANISOU 3877  CB  GLU A1084    11294  24376  27786  -1215   2007   6171       C  
ATOM   3878  N   LEU A1085     -46.728 192.322-194.585  1.00157.56           N  
ANISOU 3878  N   LEU A1085    10490  22977  26399   -835    894   5126       N  
ATOM   3879  CA  LEU A1085     -46.021 193.102-195.587  1.00149.58           C  
ANISOU 3879  CA  LEU A1085     9993  21836  25005   -652    423   4678       C  
ATOM   3880  C   LEU A1085     -46.312 194.573-195.363  1.00152.51           C  
ANISOU 3880  C   LEU A1085    10345  22483  25119   -234    630   4491       C  
ATOM   3881  O   LEU A1085     -45.415 195.406-195.420  1.00148.81           O  
ANISOU 3881  O   LEU A1085    10400  22046  24093      9    621   4226       O  
ATOM   3882  CB  LEU A1085     -46.462 192.708-196.995  1.00144.50           C  
ANISOU 3882  CB  LEU A1085     9191  20870  24843   -835   -276   4491       C  
ATOM   3883  CG  LEU A1085     -45.896 191.420-197.589  1.00137.12           C  
ANISOU 3883  CG  LEU A1085     8455  19575  24071  -1193   -671   4479       C  
ATOM   3884  CD1 LEU A1085     -46.435 191.234-198.992  1.00137.52           C  
ANISOU 3884  CD1 LEU A1085     8326  19384  24542  -1282  -1382   4210       C  
ATOM   3885  CD2 LEU A1085     -44.378 191.442-197.596  1.00126.32           C  
ANISOU 3885  CD2 LEU A1085     7851  18143  22003  -1130   -682   4318       C  
ATOM   3886  N   LYS A1086     -47.578 194.879-195.103  1.00159.14           N  
ANISOU 3886  N   LYS A1086    10548  23496  26421   -153    822   4628       N  
ATOM   3887  CA  LYS A1086     -48.002 196.250-194.871  1.00163.23           C  
ANISOU 3887  CA  LYS A1086    10961  24257  26801    255   1029   4455       C  
ATOM   3888  C   LYS A1086     -47.235 196.856-193.706  1.00164.41           C  
ANISOU 3888  C   LYS A1086    11478  24695  26295    521   1576   4407       C  
ATOM   3889  O   LYS A1086     -46.487 197.815-193.890  1.00159.06           O  
ANISOU 3889  O   LYS A1086    11263  23997  25175    781   1490   4085       O  
ATOM   3890  CB  LYS A1086     -49.501 196.314-194.621  1.00170.44           C  
ANISOU 3890  CB  LYS A1086    11069  25334  28355    279   1223   4658       C  
ATOM   3891  N   THR A1087     -47.405 196.285-192.516  1.00170.90           N  
ANISOU 3891  N   THR A1087    12090  25782  27061    461   2128   4732       N  
ATOM   3892  CA  THR A1087     -46.756 196.823-191.320  1.00173.42           C  
ANISOU 3892  CA  THR A1087    12718  26447  26728    748   2652   4675       C  
ATOM   3893  C   THR A1087     -45.233 196.893-191.469  1.00169.44           C  
ANISOU 3893  C   THR A1087    12973  25792  25615    759   2445   4419       C  
ATOM   3894  O   THR A1087     -44.610 197.879-191.070  1.00169.00           O  
ANISOU 3894  O   THR A1087    13260  25877  25075   1079   2586   4109       O  
ATOM   3895  CB  THR A1087     -47.129 196.023-190.050  1.00179.17           C  
ANISOU 3895  CB  THR A1087    13128  27506  27441    672   3268   5137       C  
ATOM   3896  OG1 THR A1087     -48.551 196.040-189.870  1.00185.15           O  
ANISOU 3896  OG1 THR A1087    13266  28360  28721    676   3475   5309       O  
ATOM   3897  CG2 THR A1087     -46.467 196.628-188.818  1.00178.86           C  
ANISOU 3897  CG2 THR A1087    13421  27885  26652   1028   3773   5026       C  
ATOM   3898  N   PHE A1088     -44.643 195.861-192.066  1.00167.94           N  
ANISOU 3898  N   PHE A1088    13019  25294  25498    414   2097   4521       N  
ATOM   3899  CA  PHE A1088     -43.191 195.818-192.248  1.00164.56           C  
ANISOU 3899  CA  PHE A1088    13272  24707  24544    401   1897   4304       C  
ATOM   3900  C   PHE A1088     -42.678 196.895-193.197  1.00161.43           C  
ANISOU 3900  C   PHE A1088    13233  24112  23989    595   1511   3869       C  
ATOM   3901  O   PHE A1088     -41.879 197.747-192.810  1.00159.52           O  
ANISOU 3901  O   PHE A1088    13367  23960  23283    852   1644   3602       O  
ATOM   3902  CB  PHE A1088     -42.738 194.445-192.748  1.00162.50           C  
ANISOU 3902  CB  PHE A1088    13144  24137  24460     -2   1596   4499       C  
ATOM   3903  CG  PHE A1088     -41.292 194.398-193.163  1.00154.71           C  
ANISOU 3903  CG  PHE A1088    12822  22942  23017    -23   1319   4249       C  
ATOM   3904  CD1 PHE A1088     -40.288 194.346-192.211  1.00152.39           C  
ANISOU 3904  CD1 PHE A1088    12904  22826  22173     77   1617   4255       C  
ATOM   3905  CD2 PHE A1088     -40.938 194.404-194.502  1.00151.06           C  
ANISOU 3905  CD2 PHE A1088    12597  22134  22666   -123    763   4007       C  
ATOM   3906  CE1 PHE A1088     -38.959 194.302-192.586  1.00147.67           C  
ANISOU 3906  CE1 PHE A1088    12872  22031  21204     57   1367   4024       C  
ATOM   3907  CE2 PHE A1088     -39.611 194.360-194.884  1.00146.08           C  
ANISOU 3907  CE2 PHE A1088    12547  21324  21632   -134    551   3794       C  
ATOM   3908  CZ  PHE A1088     -38.619 194.309-193.925  1.00144.44           C  
ANISOU 3908  CZ  PHE A1088    12677  21265  20940    -55    854   3802       C  
ATOM   3909  N   LEU A1089     -43.132 196.837-194.445  1.00160.96           N  
ANISOU 3909  N   LEU A1089    13048  23778  24331    476   1026   3808       N  
ATOM   3910  CA  LEU A1089     -42.703 197.780-195.470  1.00157.95           C  
ANISOU 3910  CA  LEU A1089    12989  23196  23829    655    645   3480       C  
ATOM   3911  C   LEU A1089     -43.016 199.223-195.077  1.00164.32           C  
ANISOU 3911  C   LEU A1089    13712  24176  24546   1056    892   3283       C  
ATOM   3912  O   LEU A1089     -42.254 200.135-195.398  1.00164.18           O  
ANISOU 3912  O   LEU A1089    14089  24040  24253   1260    790   3012       O  
ATOM   3913  CB  LEU A1089     -43.324 197.427-196.825  1.00154.00           C  
ANISOU 3913  CB  LEU A1089    12295  22449  23769    498     90   3484       C  
ATOM   3914  CG  LEU A1089     -42.879 196.087-197.423  1.00147.83           C  
ANISOU 3914  CG  LEU A1089    11671  21425  23074    130   -256   3563       C  
ATOM   3915  CD1 LEU A1089     -43.619 195.780-198.714  1.00147.68           C  
ANISOU 3915  CD1 LEU A1089    11404  21213  23495     18   -824   3510       C  
ATOM   3916  CD2 LEU A1089     -41.378 196.080-197.658  1.00141.71           C  
ANISOU 3916  CD2 LEU A1089    11570  20502  21770    133   -358   3382       C  
ATOM   3917  N   GLN A1090     -44.124 199.426-194.368  1.00169.87           N  
ANISOU 3917  N   GLN A1090    13885  25144  25515   1172   1235   3418       N  
ATOM   3918  CA  GLN A1090     -44.451 200.752-193.849  1.00172.04           C  
ANISOU 3918  CA  GLN A1090    14050  25601  25718   1576   1521   3209       C  
ATOM   3919  C   GLN A1090     -43.478 201.157-192.744  1.00171.74           C  
ANISOU 3919  C   GLN A1090    14389  25755  25110   1764   1910   3024       C  
ATOM   3920  O   GLN A1090     -43.127 202.331-192.620  1.00171.63           O  
ANISOU 3920  O   GLN A1090    14564  25724  24924   2077   1970   2700       O  
ATOM   3921  CB  GLN A1090     -45.885 200.801-193.343  1.00177.01           C  
ANISOU 3921  CB  GLN A1090    13990  26490  26775   1662   1817   3399       C  
ATOM   3922  N   GLU A1091     -43.044 200.183-191.946  1.00171.55           N  
ANISOU 3922  N   GLU A1091    14463  25902  24818   1582   2153   3224       N  
ATOM   3923  CA  GLU A1091     -42.085 200.451-190.877  1.00171.16           C  
ANISOU 3923  CA  GLU A1091    14775  26072  24184   1762   2476   3049       C  
ATOM   3924  C   GLU A1091     -40.724 200.852-191.444  1.00167.14           C  
ANISOU 3924  C   GLU A1091    14866  25264  23377   1769   2154   2733       C  
ATOM   3925  O   GLU A1091     -40.099 201.800-190.967  1.00166.83           O  
ANISOU 3925  O   GLU A1091    15072  25282  23036   2047   2280   2386       O  
ATOM   3926  CB  GLU A1091     -41.948 199.243-189.959  1.00172.54           C  
ANISOU 3926  CB  GLU A1091    14913  26496  24147   1571   2781   3403       C  
ATOM   3927  N   GLU A1092     -40.274 200.127-192.464  1.00164.50           N  
ANISOU 3927  N   GLU A1092    14742  24605  23156   1468   1740   2837       N  
ATOM   3928  CA  GLU A1092     -39.006 200.425-193.114  1.00161.08           C  
ANISOU 3928  CA  GLU A1092    14845  23878  22481   1453   1442   2586       C  
ATOM   3929  C   GLU A1092     -39.073 201.771-193.827  1.00163.21           C  
ANISOU 3929  C   GLU A1092    15165  23947  22900   1708   1272   2311       C  
ATOM   3930  O   GLU A1092     -38.160 202.595-193.712  1.00161.93           O  
ANISOU 3930  O   GLU A1092    15338  23679  22508   1884   1291   2014       O  
ATOM   3931  CB  GLU A1092     -38.640 199.320-194.092  1.00157.89           C  
ANISOU 3931  CB  GLU A1092    14608  23200  22185   1101   1051   2762       C  
ATOM   3932  N   SER A1093     -40.164 201.986-194.558  1.00166.90           N  
ANISOU 3932  N   SER A1093    15277  24347  23791   1731   1100   2421       N  
ATOM   3933  CA  SER A1093     -40.383 203.241-195.269  1.00168.44           C  
ANISOU 3933  CA  SER A1093    15467  24351  24183   1994    937   2236       C  
ATOM   3934  C   SER A1093     -40.368 204.438-194.323  1.00170.08           C  
ANISOU 3934  C   SER A1093    15629  24692  24301   2354   1296   1951       C  
ATOM   3935  O   SER A1093     -39.704 205.439-194.591  1.00169.76           O  
ANISOU 3935  O   SER A1093    15860  24424  24218   2544   1227   1695       O  
ATOM   3936  CB  SER A1093     -41.706 203.198-196.037  1.00172.61           C  
ANISOU 3936  CB  SER A1093    15538  24861  25186   1986    714   2425       C  
ATOM   3937  OG  SER A1093     -41.655 202.252-197.090  1.00171.56           O  
ANISOU 3937  OG  SER A1093    15485  24555  25146   1697    290   2592       O  
ATOM   3938  N   LYS A1094     -41.098 204.329-193.216  1.00170.99           N  
ANISOU 3938  N   LYS A1094    15392  25171  24407   2457   1690   1992       N  
ATOM   3939  CA  LYS A1094     -41.132 205.394-192.219  1.00169.88           C  
ANISOU 3939  CA  LYS A1094    15189  25214  24146   2827   2048   1673       C  
ATOM   3940  C   LYS A1094     -39.780 205.539-191.523  1.00163.76           C  
ANISOU 3940  C   LYS A1094    14876  24456  22890   2877   2157   1384       C  
ATOM   3941  O   LYS A1094     -39.436 206.615-191.034  1.00163.70           O  
ANISOU 3941  O   LYS A1094    14961  24429  22808   3179   2290    997       O  
ATOM   3942  CB  LYS A1094     -42.239 205.142-191.200  1.00174.74           C  
ANISOU 3942  CB  LYS A1094    15311  26271  24810   2936   2472   1812       C  
ATOM   3943  N   LYS A1095     -39.015 204.451-191.484  1.00158.40           N  
ANISOU 3943  N   LYS A1095    14467  23794  21923   2585   2077   1551       N  
ATOM   3944  CA  LYS A1095     -37.681 204.482-190.894  1.00154.42           C  
ANISOU 3944  CA  LYS A1095    14395  23299  20978   2609   2124   1296       C  
ATOM   3945  C   LYS A1095     -36.673 205.179-191.796  1.00151.64           C  
ANISOU 3945  C   LYS A1095    14418  22496  20701   2608   1807   1058       C  
ATOM   3946  O   LYS A1095     -35.667 205.703-191.317  1.00150.85           O  
ANISOU 3946  O   LYS A1095    14598  22344  20373   2732   1851    719       O  
ATOM   3947  CB  LYS A1095     -37.181 203.069-190.603  1.00150.20           C  
ANISOU 3947  CB  LYS A1095    14017  22902  20149   2306   2128   1583       C  
ATOM   3948  CG  LYS A1095     -37.524 202.549-189.226  1.00152.58           C  
ANISOU 3948  CG  LYS A1095    14138  23706  20131   2397   2552   1709       C  
ATOM   3949  CD  LYS A1095     -36.786 201.251-188.956  1.00150.02           C  
ANISOU 3949  CD  LYS A1095    14048  23446  19508   2125   2525   1975       C  
ATOM   3950  CE  LYS A1095     -37.058 200.223-190.043  1.00147.47           C  
ANISOU 3950  CE  LYS A1095    13662  22829  19541   1736   2223   2346       C  
ATOM   3951  NZ  LYS A1095     -36.218 199.004-189.880  1.00145.18           N1+
ANISOU 3951  NZ  LYS A1095    13636  22512  19013   1477   2154   2564       N1+
ATOM   3952  N   HIS A1096     -36.932 205.175-193.100  1.00150.36           N  
ANISOU 3952  N   HIS A1096    14250  22019  20861   2478   1487   1241       N  
ATOM   3953  CA  HIS A1096     -35.946 205.677-194.052  1.00147.28           C  
ANISOU 3953  CA  HIS A1096    14227  21215  20518   2449   1208   1119       C  
ATOM   3954  C   HIS A1096     -36.499 206.677-195.072  1.00149.62           C  
ANISOU 3954  C   HIS A1096    14408  21220  21220   2617   1026   1134       C  
ATOM   3955  O   HIS A1096     -35.877 206.909-196.110  1.00148.67           O  
ANISOU 3955  O   HIS A1096    14552  20770  21166   2562    772   1178       O  
ATOM   3956  CB  HIS A1096     -35.270 204.504-194.780  1.00142.24           C  
ANISOU 3956  CB  HIS A1096    13863  20457  19726   2106    947   1349       C  
ATOM   3957  CG  HIS A1096     -34.686 203.472-193.862  1.00138.69           C  
ANISOU 3957  CG  HIS A1096    13538  20247  18910   1941   1094   1385       C  
ATOM   3958  ND1 HIS A1096     -34.851 202.118-194.066  1.00136.31           N  
ANISOU 3958  ND1 HIS A1096    13208  20015  18567   1646    992   1699       N  
ATOM   3959  CD2 HIS A1096     -33.936 203.594-192.741  1.00136.71           C  
ANISOU 3959  CD2 HIS A1096    13438  20175  18329   2047   1317   1149       C  
ATOM   3960  CE1 HIS A1096     -34.232 201.452-193.107  1.00134.72           C  
ANISOU 3960  CE1 HIS A1096    13139  20017  18032   1579   1168   1702       C  
ATOM   3961  NE2 HIS A1096     -33.668 202.323-192.291  1.00134.85           N  
ANISOU 3961  NE2 HIS A1096    13271  20129  17836   1827   1358   1369       N  
ATOM   3962  N   GLN A1097     -37.653 207.275-194.783  1.00152.71           N  
ANISOU 3962  N   GLN A1097    14402  21743  21877   2842   1169   1120       N  
ATOM   3963  CA  GLN A1097     -38.233 208.263-195.694  1.00152.62           C  
ANISOU 3963  CA  GLN A1097    14254  21462  22270   3042    999   1154       C  
ATOM   3964  C   GLN A1097     -37.435 209.563-195.692  1.00151.73           C  
ANISOU 3964  C   GLN A1097    14364  21019  22268   3279   1042    843       C  
ATOM   3965  O   GLN A1097     -37.258 210.195-196.735  1.00152.53           O  
ANISOU 3965  O   GLN A1097    14586  20765  22602   3346    827    938       O  
ATOM   3966  CB  GLN A1097     -39.696 208.562-195.342  1.00155.17           C  
ANISOU 3966  CB  GLN A1097    14055  22011  22892   3238   1149   1210       C  
ATOM   3967  CG  GLN A1097     -40.332 209.624-196.237  1.00155.52           C  
ANISOU 3967  CG  GLN A1097    13936  21780  23375   3486    965   1253       C  
ATOM   3968  CD  GLN A1097     -41.685 210.090-195.736  1.00159.62           C  
ANISOU 3968  CD  GLN A1097    13925  22510  24214   3739   1160   1230       C  
ATOM   3969  OE1 GLN A1097     -42.284 209.466-194.860  1.00162.34           O  
ANISOU 3969  OE1 GLN A1097    13983  23233  24465   3687   1416   1260       O  
ATOM   3970  NE2 GLN A1097     -42.172 211.195-196.287  1.00160.68           N  
ANISOU 3970  NE2 GLN A1097    13912  22396  24742   4027   1058   1203       N  
ATOM   3971  N   ASN A1098     -36.954 209.952-194.515  1.00149.45           N  
ANISOU 3971  N   ASN A1098    14120  20847  21819   3415   1317    474       N  
ATOM   3972  CA  ASN A1098     -36.264 211.227-194.349  1.00146.94           C  
ANISOU 3972  CA  ASN A1098    13941  20202  21689   3652   1372    103       C  
ATOM   3973  C   ASN A1098     -34.741 211.130-194.487  1.00143.42           C  
ANISOU 3973  C   ASN A1098    13927  19513  21051   3487   1276    -31       C  
ATOM   3974  O   ASN A1098     -34.050 212.150-194.502  1.00142.80           O  
ANISOU 3974  O   ASN A1098    13971  19083  21204   3634   1283   -308       O  
ATOM   3975  CB  ASN A1098     -36.634 211.863-193.003  1.00147.04           C  
ANISOU 3975  CB  ASN A1098    13725  20460  21685   3954   1693   -317       C  
ATOM   3976  CG  ASN A1098     -38.126 212.128-192.869  1.00147.58           C  
ANISOU 3976  CG  ASN A1098    13328  20733  22011   4165   1825   -216       C  
ATOM   3977  OD1 ASN A1098     -38.823 212.350-193.859  1.00147.04           O  
ANISOU 3977  OD1 ASN A1098    13103  20471  22294   4183   1639     69       O  
ATOM   3978  ND2 ASN A1098     -38.621 212.108-191.636  1.00149.18           N  
ANISOU 3978  ND2 ASN A1098    13300  21356  22026   4349   2148   -447       N  
ATOM   3979  N   GLU A1099     -34.224 209.908-194.597  1.00140.59           N  
ANISOU 3979  N   GLU A1099    13774  19316  20328   3182   1185    167       N  
ATOM   3980  CA  GLU A1099     -32.777 209.688-194.656  1.00136.32           C  
ANISOU 3980  CA  GLU A1099    13615  18594  19587   3020   1107     43       C  
ATOM   3981  C   GLU A1099     -32.149 210.100-195.986  1.00131.00           C  
ANISOU 3981  C   GLU A1099    13168  17455  19149   2953    889    217       C  
ATOM   3982  O   GLU A1099     -31.120 210.776-196.011  1.00130.33           O  
ANISOU 3982  O   GLU A1099    13274  17055  19189   2992    900     -3       O  
ATOM   3983  CB  GLU A1099     -32.428 208.232-194.335  1.00136.90           C  
ANISOU 3983  CB  GLU A1099    13824  18975  19217   2738   1086    207       C  
ATOM   3984  CG  GLU A1099     -32.632 207.846-192.874  1.00143.90           C  
ANISOU 3984  CG  GLU A1099    14581  20315  19779   2817   1343     20       C  
ATOM   3985  CD  GLU A1099     -31.767 208.655-191.914  1.00148.29           C  
ANISOU 3985  CD  GLU A1099    15252  20852  20240   3024   1467   -495       C  
ATOM   3986  OE1 GLU A1099     -30.693 209.144-192.333  1.00146.75           O  
ANISOU 3986  OE1 GLU A1099    15296  20286  20175   2989   1333   -671       O  
ATOM   3987  OE2 GLU A1099     -32.165 208.801-190.736  1.00152.33           O1-
ANISOU 3987  OE2 GLU A1099    15598  21729  20552   3233   1700   -733       O1-
ATOM   3988  N   PHE A1100     -32.760 209.681-197.087  1.00127.06           N  
ANISOU 3988  N   PHE A1100    12638  16928  18711   2860    694    614       N  
ATOM   3989  CA  PHE A1100     -32.305 210.094-198.407  1.00123.03           C  
ANISOU 3989  CA  PHE A1100    12331  16040  18375   2852    505    834       C  
ATOM   3990  C   PHE A1100     -33.184 211.225-198.904  1.00129.12           C  
ANISOU 3990  C   PHE A1100    12878  16610  19573   3134    487    926       C  
ATOM   3991  O   PHE A1100     -34.191 211.552-198.274  1.00132.82           O  
ANISOU 3991  O   PHE A1100    13020  17251  20195   3306    599    820       O  
ATOM   3992  CB  PHE A1100     -32.366 208.926-199.390  1.00116.73           C  
ANISOU 3992  CB  PHE A1100    11672  15351  17329   2613    256   1187       C  
ATOM   3993  CG  PHE A1100     -31.667 207.693-198.904  1.00111.92           C  
ANISOU 3993  CG  PHE A1100    11239  14946  16338   2340    261   1134       C  
ATOM   3994  CD1 PHE A1100     -30.293 207.568-199.024  1.00107.32           C  
ANISOU 3994  CD1 PHE A1100    10987  14181  15610   2223    261   1038       C  
ATOM   3995  CD2 PHE A1100     -32.384 206.658-198.320  1.00111.21           C  
ANISOU 3995  CD2 PHE A1100    10964  15214  16078   2205    276   1204       C  
ATOM   3996  CE1 PHE A1100     -29.645 206.436-198.572  1.00104.06           C  
ANISOU 3996  CE1 PHE A1100    10727  13944  14866   1994    254    998       C  
ATOM   3997  CE2 PHE A1100     -31.743 205.521-197.869  1.00106.71           C  
ANISOU 3997  CE2 PHE A1100    10553  14801  15190   1967    283   1196       C  
ATOM   3998  CZ  PHE A1100     -30.372 205.409-197.993  1.00103.93           C  
ANISOU 3998  CZ  PHE A1100    10544  14271  14675   1871    261   1085       C  
ATOM   3999  N   ASN A1101     -32.806 211.827-200.029  1.00131.55           N  
ANISOU 3999  N   ASN A1101    13351  16560  20074   3200    364   1146       N  
ATOM   4000  CA  ASN A1101     -33.651 212.837-200.659  1.00137.44           C  
ANISOU 4000  CA  ASN A1101    13901  17100  21219   3478    308   1326       C  
ATOM   4001  C   ASN A1101     -34.126 212.408-202.046  1.00138.51           C  
ANISOU 4001  C   ASN A1101    14100  17277  21251   3457     15   1782       C  
ATOM   4002  O   ASN A1101     -33.325 212.115-202.933  1.00135.54           O  
ANISOU 4002  O   ASN A1101    14036  16778  20684   3347    -99   1987       O  
ATOM   4003  CB  ASN A1101     -32.954 214.204-200.704  1.00139.11           C  
ANISOU 4003  CB  ASN A1101    14186  16815  21855   3672    446   1199       C  
ATOM   4004  CG  ASN A1101     -31.813 214.252-201.698  1.00136.67           C  
ANISOU 4004  CG  ASN A1101    14226  16199  21504   3565    383   1442       C  
ATOM   4005  OD1 ASN A1101     -31.976 214.719-202.826  1.00138.68           O  
ANISOU 4005  OD1 ASN A1101    14540  16241  21910   3696    276   1825       O  
ATOM   4006  ND2 ASN A1101     -30.650 213.770-201.285  1.00132.77           N  
ANISOU 4006  ND2 ASN A1101    13956  15697  20793   3345    460   1238       N  
ATOM   4007  N   GLU A1102     -35.441 212.360-202.219  1.00143.98           N  
ANISOU 4007  N   GLU A1102    14479  18167  22061   3581   -111   1920       N  
ATOM   4008  CA  GLU A1102     -36.029 211.931-203.479  1.00149.94           C  
ANISOU 4008  CA  GLU A1102    15244  19014  22711   3593   -445   2299       C  
ATOM   4009  C   GLU A1102     -35.841 213.002-204.554  1.00155.16           C  
ANISOU 4009  C   GLU A1102    16040  19321  23592   3855   -525   2586       C  
ATOM   4010  O   GLU A1102     -36.021 212.741-205.746  1.00155.89           O  
ANISOU 4010  O   GLU A1102    16253  19464  23513   3900   -804   2919       O  
ATOM   4011  CB  GLU A1102     -37.514 211.602-203.286  1.00155.93           C  
ANISOU 4011  CB  GLU A1102    15569  20079  23599   3655   -566   2338       C  
ATOM   4012  CG  GLU A1102     -37.776 210.537-202.221  1.00157.58           C  
ANISOU 4012  CG  GLU A1102    15607  20639  23627   3404   -444   2133       C  
ATOM   4013  CD  GLU A1102     -39.244 210.417-201.848  1.00164.37           C  
ANISOU 4013  CD  GLU A1102    15962  21762  24727   3494   -461   2156       C  
ATOM   4014  OE1 GLU A1102     -40.085 211.066-202.508  1.00168.33           O  
ANISOU 4014  OE1 GLU A1102    16248  22191  25517   3740   -632   2323       O  
ATOM   4015  OE2 GLU A1102     -39.556 209.676-200.889  1.00165.03           O1-
ANISOU 4015  OE2 GLU A1102    15851  22130  24724   3331   -291   2029       O1-
ATOM   4016  N   SER A1103     -35.463 214.202-204.119  1.00159.84           N  
ANISOU 4016  N   SER A1103    16610  19554  24566   4040   -280   2452       N  
ATOM   4017  CA  SER A1103     -35.260 215.337-205.016  1.00164.30           C  
ANISOU 4017  CA  SER A1103    17271  19713  25441   4303   -292   2752       C  
ATOM   4018  C   SER A1103     -34.146 215.085-206.031  1.00161.94           C  
ANISOU 4018  C   SER A1103    17393  19280  24859   4193   -347   3038       C  
ATOM   4019  O   SER A1103     -34.376 215.143-207.241  1.00165.12           O  
ANISOU 4019  O   SER A1103    17907  19691  25140   4337   -556   3459       O  
ATOM   4020  CB  SER A1103     -34.977 216.602-204.214  1.00166.74           C  
ANISOU 4020  CB  SER A1103    17457  19614  26284   4481     -2   2482       C  
ATOM   4021  N   ALA A1104     -32.942 214.805-205.539  1.00154.67           N  
ANISOU 4021  N   ALA A1104    16696  18258  23813   3962   -161   2810       N  
ATOM   4022  CA  ALA A1104     -31.814 214.530-206.422  1.00148.64           C  
ANISOU 4022  CA  ALA A1104    16309  17377  22789   3849   -164   3053       C  
ATOM   4023  C   ALA A1104     -32.068 213.289-207.270  1.00142.21           C  
ANISOU 4023  C   ALA A1104    15650  16966  21417   3726   -463   3258       C  
ATOM   4024  O   ALA A1104     -31.644 213.221-208.423  1.00144.14           O  
ANISOU 4024  O   ALA A1104    16154  17182  21431   3788   -558   3605       O  
ATOM   4025  CB  ALA A1104     -30.531 214.379-205.625  1.00145.62           C  
ANISOU 4025  CB  ALA A1104    16081  16846  22403   3615     69   2716       C  
ATOM   4026  N   ALA A1105     -32.770 212.315-206.697  1.00133.98           N  
ANISOU 4026  N   ALA A1105    14437  16295  20175   3564   -603   3041       N  
ATOM   4027  CA  ALA A1105     -33.106 211.087-207.410  1.00128.74           C  
ANISOU 4027  CA  ALA A1105    13863  15987  19066   3431   -920   3162       C  
ATOM   4028  C   ALA A1105     -33.957 211.372-208.641  1.00130.25           C  
ANISOU 4028  C   ALA A1105    14012  16255  19221   3700  -1221   3534       C  
ATOM   4029  O   ALA A1105     -33.587 211.016-209.763  1.00130.22           O  
ANISOU 4029  O   ALA A1105    14285  16327  18864   3738  -1404   3777       O  
ATOM   4030  CB  ALA A1105     -33.828 210.126-206.487  1.00127.03           C  
ANISOU 4030  CB  ALA A1105    13388  16090  18788   3224   -984   2892       C  
ATOM   4031  N   LEU A1106     -35.099 212.017-208.418  1.00131.79           N  
ANISOU 4031  N   LEU A1106    13855  16453  19765   3913  -1275   3565       N  
ATOM   4032  CA  LEU A1106     -36.024 212.358-209.495  1.00134.12           C  
ANISOU 4032  CA  LEU A1106    14053  16835  20070   4208  -1590   3907       C  
ATOM   4033  C   LEU A1106     -35.389 213.302-210.513  1.00136.68           C  
ANISOU 4033  C   LEU A1106    14660  16877  20394   4474  -1527   4309       C  
ATOM   4034  O   LEU A1106     -35.588 213.150-211.723  1.00138.34           O  
ANISOU 4034  O   LEU A1106    15024  17246  20294   4650  -1812   4637       O  
ATOM   4035  CB  LEU A1106     -37.299 212.981-208.924  1.00135.72           C  
ANISOU 4035  CB  LEU A1106    13788  17048  20730   4400  -1603   3842       C  
ATOM   4036  CG  LEU A1106     -38.153 212.070-208.039  1.00133.41           C  
ANISOU 4036  CG  LEU A1106    13147  17078  20465   4184  -1669   3540       C  
ATOM   4037  CD1 LEU A1106     -39.326 212.831-207.450  1.00135.90           C  
ANISOU 4037  CD1 LEU A1106    12991  17379  21267   4413  -1607   3482       C  
ATOM   4038  CD2 LEU A1106     -38.641 210.868-208.828  1.00134.05           C  
ANISOU 4038  CD2 LEU A1106    13228  17507  20198   4055  -2098   3617       C  
ATOM   4039  N   ARG A1107     -34.624 214.273-210.021  1.00137.94           N  
ANISOU 4039  N   ARG A1107    14879  16623  20910   4515  -1155   4286       N  
ATOM   4040  CA  ARG A1107     -33.931 215.202-210.907  1.00142.06           C  
ANISOU 4040  CA  ARG A1107    15645  16813  21519   4741  -1023   4705       C  
ATOM   4041  C   ARG A1107     -32.903 214.484-211.782  1.00138.73           C  
ANISOU 4041  C   ARG A1107    15644  16516  20553   4618  -1049   4885       C  
ATOM   4042  O   ARG A1107     -32.680 214.873-212.930  1.00140.06           O  
ANISOU 4042  O   ARG A1107    16027  16642  20549   4858  -1091   5346       O  
ATOM   4043  CB  ARG A1107     -33.279 216.345-210.118  1.00143.93           C  
ANISOU 4043  CB  ARG A1107    15816  16528  22344   4768   -619   4583       C  
ATOM   4044  CG  ARG A1107     -34.272 217.338-209.517  1.00146.73           C  
ANISOU 4044  CG  ARG A1107    15783  16684  23285   5010   -580   4493       C  
ATOM   4045  CD  ARG A1107     -33.600 218.656-209.150  1.00148.38           C  
ANISOU 4045  CD  ARG A1107    15969  16288  24122   5128   -235   4493       C  
ATOM   4046  NE  ARG A1107     -32.451 218.475-208.263  1.00144.70           N  
ANISOU 4046  NE  ARG A1107    15612  15658  23708   4831     30   4081       N  
ATOM   4047  CZ  ARG A1107     -32.481 218.656-206.946  1.00142.56           C  
ANISOU 4047  CZ  ARG A1107    15125  15312  23729   4740    182   3540       C  
ATOM   4048  NH1 ARG A1107     -33.606 219.029-206.351  1.00143.83           N1+
ANISOU 4048  NH1 ARG A1107    14944  15542  24165   4920    136   3347       N1+
ATOM   4049  NH2 ARG A1107     -31.385 218.468-206.224  1.00139.56           N  
ANISOU 4049  NH2 ARG A1107    14864  14810  23351   4492    378   3182       N  
ATOM   4050  N   GLU A1108     -32.291 213.432-211.242  1.00133.84           N  
ANISOU 4050  N   GLU A1108    15136  16065  19652   4271  -1016   4535       N  
ATOM   4051  CA  GLU A1108     -31.324 212.634-211.998  1.00131.66           C  
ANISOU 4051  CA  GLU A1108    15237  15930  18859   4144  -1044   4636       C  
ATOM   4052  C   GLU A1108     -31.973 211.503-212.798  1.00129.43           C  
ANISOU 4052  C   GLU A1108    15020  16119  18038   4145  -1483   4661       C  
ATOM   4053  O   GLU A1108     -31.293 210.791-213.538  1.00126.79           O  
ANISOU 4053  O   GLU A1108    14996  15948  17229   4088  -1557   4728       O  
ATOM   4054  CB  GLU A1108     -30.230 212.077-211.081  1.00130.21           C  
ANISOU 4054  CB  GLU A1108    15156  15657  18662   3791   -798   4260       C  
ATOM   4055  CG  GLU A1108     -29.242 213.125-210.591  1.00134.77           C  
ANISOU 4055  CG  GLU A1108    15758  15753  19696   3791   -390   4254       C  
ATOM   4056  CD  GLU A1108     -28.453 213.767-211.722  1.00140.42           C  
ANISOU 4056  CD  GLU A1108    16732  16242  20381   3978   -228   4737       C  
ATOM   4057  OE1 GLU A1108     -28.053 214.943-211.578  1.00142.87           O  
ANISOU 4057  OE1 GLU A1108    16974  16098  21213   4093     54   4882       O  
ATOM   4058  OE2 GLU A1108     -28.232 213.091-212.750  1.00141.88           O1-
ANISOU 4058  OE2 GLU A1108    17179  16699  20031   4018   -374   4969       O1-
ATOM   4059  N   LEU A1109     -33.286 211.342-212.645  1.00131.50           N  
ANISOU 4059  N   LEU A1109    14968  16591  18404   4216  -1777   4581       N  
ATOM   4060  CA  LEU A1109     -34.050 210.405-213.470  1.00132.67           C  
ANISOU 4060  CA  LEU A1109    15113  17153  18143   4259  -2256   4600       C  
ATOM   4061  C   LEU A1109     -34.696 211.128-214.657  1.00140.93           C  
ANISOU 4061  C   LEU A1109    16177  18275  19095   4693  -2501   5038       C  
ATOM   4062  O   LEU A1109     -34.935 210.521-215.711  1.00145.32           O  
ANISOU 4062  O   LEU A1109    16887  19157  19173   4820  -2877   5144       O  
ATOM   4063  CB  LEU A1109     -35.117 209.678-212.640  1.00129.74           C  
ANISOU 4063  CB  LEU A1109    14348  16986  17961   4060  -2462   4257       C  
ATOM   4064  CG  LEU A1109     -34.972 208.161-212.465  1.00124.37           C  
ANISOU 4064  CG  LEU A1109    13719  16557  16979   3715  -2652   3943       C  
ATOM   4065  CD1 LEU A1109     -36.094 207.591-211.608  1.00122.78           C  
ANISOU 4065  CD1 LEU A1109    13069  16510  17071   3538  -2793   3690       C  
ATOM   4066  CD2 LEU A1109     -34.928 207.463-213.814  1.00125.59           C  
ANISOU 4066  CD2 LEU A1109    14129  16976  16613   3823  -3055   4049       C  
ATOM   4067  N   TYR A1110     -34.977 212.421-214.485  1.00143.44           N  
ANISOU 4067  N   TYR A1110    16338  18294  19869   4941  -2304   5280       N  
ATOM   4068  CA  TYR A1110     -35.541 213.222-215.572  1.00149.94           C  
ANISOU 4068  CA  TYR A1110    17180  19147  20643   5388  -2501   5762       C  
ATOM   4069  C   TYR A1110     -34.612 213.221-216.778  1.00153.36           C  
ANISOU 4069  C   TYR A1110    18074  19646  20550   5557  -2462   6147       C  
ATOM   4070  O   TYR A1110     -35.068 213.195-217.921  1.00157.87           O  
ANISOU 4070  O   TYR A1110    18793  20477  20714   5789  -2781   6343       O  
ATOM   4071  CB  TYR A1110     -35.825 214.662-215.132  1.00153.63           C  
ANISOU 4071  CB  TYR A1110    17422  19189  21761   5617  -2230   5970       C  
ATOM   4072  CG  TYR A1110     -36.297 215.562-216.263  1.00158.50           C  
ANISOU 4072  CG  TYR A1110    18141  19774  22308   5993  -2372   6401       C  
ATOM   4073  CD1 TYR A1110     -37.616 215.526-216.705  1.00161.49           C  
ANISOU 4073  CD1 TYR A1110    18300  20421  22637   6184  -2811   6394       C  
ATOM   4074  CD2 TYR A1110     -35.423 216.444-216.891  1.00159.56           C  
ANISOU 4074  CD2 TYR A1110    18601  19604  22421   6088  -2057   6739       C  
ATOM   4075  CE1 TYR A1110     -38.049 216.340-217.739  1.00167.34           C  
ANISOU 4075  CE1 TYR A1110    19171  21136  23275   6486  -2951   6717       C  
ATOM   4076  CE2 TYR A1110     -35.848 217.261-217.924  1.00165.77           C  
ANISOU 4076  CE2 TYR A1110    19505  20369  23112   6372  -2165   7091       C  
ATOM   4077  CZ  TYR A1110     -37.160 217.205-218.346  1.00169.61           C  
ANISOU 4077  CZ  TYR A1110    19797  21132  23514   6582  -2622   7080       C  
ATOM   4078  OH  TYR A1110     -37.583 218.021-219.373  1.00175.91           O  
ANISOU 4078  OH  TYR A1110    20715  21911  24211   6886  -2748   7443       O  
ATOM   4079  N   LYS A1111     -33.309 213.239-216.512  1.00152.49           N  
ANISOU 4079  N   LYS A1111    18218  19294  20428   5355  -2052   6119       N  
ATOM   4080  CA  LYS A1111     -32.305 213.172-217.566  1.00156.15           C  
ANISOU 4080  CA  LYS A1111    19109  19821  20398   5473  -1931   6455       C  
ATOM   4081  C   LYS A1111     -32.518 211.947-218.448  1.00160.05           C  
ANISOU 4081  C   LYS A1111    19805  20848  20160   5479  -2371   6318       C  
ATOM   4082  O   LYS A1111     -32.210 211.965-219.640  1.00166.06           O  
ANISOU 4082  O   LYS A1111    20895  21778  20423   5623  -2424   6512       O  
ATOM   4083  CB  LYS A1111     -30.900 213.144-216.965  1.00150.03           C  
ANISOU 4083  CB  LYS A1111    18501  18735  19768   5176  -1456   6320       C  
ATOM   4084  CG  LYS A1111     -30.510 214.428-216.262  1.00148.44           C  
ANISOU 4084  CG  LYS A1111    18146  17964  20288   5188  -1019   6447       C  
ATOM   4085  CD  LYS A1111     -29.030 214.445-215.943  1.00143.59           C  
ANISOU 4085  CD  LYS A1111    17723  17059  19774   4946   -583   6381       C  
ATOM   4086  CE  LYS A1111     -28.609 215.790-215.386  1.00144.52           C  
ANISOU 4086  CE  LYS A1111    17684  16572  20655   4987   -177   6523       C  
ATOM   4087  NZ  LYS A1111     -27.144 215.835-215.139  1.00142.87           N1+
ANISOU 4087  NZ  LYS A1111    17628  16067  20590   4758    226   6468       N1+
ATOM   4088  N   TYR A1112     -33.054 210.888-217.851  1.00156.26           N  
ANISOU 4088  N   TYR A1112    19130  20589  19654   5215  -2663   5842       N  
ATOM   4089  CA  TYR A1112     -33.353 209.660-218.573  1.00154.12           C  
ANISOU 4089  CA  TYR A1112    18979  20781  18798   5200  -3135   5632       C  
ATOM   4090  C   TYR A1112     -34.743 209.683-219.198  1.00157.01           C  
ANISOU 4090  C   TYR A1112    19124  21448  19085   5484  -3675   5699       C  
ATOM   4091  O   TYR A1112     -34.975 209.035-220.219  1.00160.97           O  
ANISOU 4091  O   TYR A1112    19813  22284  19064   5562  -4069   5593       O  
ATOM   4092  CB  TYR A1112     -33.223 208.453-217.647  1.00146.85           C  
ANISOU 4092  CB  TYR A1112    17947  19899  17949   4731  -3182   5071       C  
ATOM   4093  CG  TYR A1112     -31.803 207.984-217.458  1.00141.03           C  
ANISOU 4093  CG  TYR A1112    17526  19040  17017   4487  -2835   4950       C  
ATOM   4094  CD1 TYR A1112     -30.931 207.902-218.535  1.00141.81           C  
ANISOU 4094  CD1 TYR A1112    18032  19268  16582   4678  -2769   5185       C  
ATOM   4095  CD2 TYR A1112     -31.332 207.630-216.204  1.00134.81           C  
ANISOU 4095  CD2 TYR A1112    16621  18032  16566   4093  -2568   4611       C  
ATOM   4096  CE1 TYR A1112     -29.631 207.471-218.368  1.00136.86           C  
ANISOU 4096  CE1 TYR A1112    17661  18529  15810   4464  -2443   5071       C  
ATOM   4097  CE2 TYR A1112     -30.033 207.202-216.026  1.00129.87           C  
ANISOU 4097  CE2 TYR A1112    16261  17298  15787   3885  -2277   4496       C  
ATOM   4098  CZ  TYR A1112     -29.187 207.123-217.110  1.00129.81           C  
ANISOU 4098  CZ  TYR A1112    16629  17395  15297   4063  -2214   4721       C  
ATOM   4099  OH  TYR A1112     -27.893 206.698-216.931  1.00125.29           O  
ANISOU 4099  OH  TYR A1112    16288  16712  14606   3863  -1915   4603       O  
ATOM   4100  N   MET A1113     -35.669 210.419-218.588  1.00153.75           N  
ANISOU 4100  N   MET A1113    18318  20872  19229   5562  -3684   5758       N  
ATOM   4101  CA  MET A1113     -37.030 210.463-219.118  1.00153.93           C  
ANISOU 4101  CA  MET A1113    18105  21117  19265   5746  -4182   5716       C  
ATOM   4102  C   MET A1113     -37.111 211.192-220.457  1.00161.72           C  
ANISOU 4102  C   MET A1113    19394  22143  19908   6062  -4288   6041       C  
ATOM   4103  O   MET A1113     -37.820 210.759-221.364  1.00166.37           O  
ANISOU 4103  O   MET A1113    20007  23054  20153   6188  -4789   5960       O  
ATOM   4104  CB  MET A1113     -37.999 211.101-218.120  1.00149.96           C  
ANISOU 4104  CB  MET A1113    17086  20425  19467   5763  -4130   5691       C  
ATOM   4105  CG  MET A1113     -39.462 210.849-218.459  1.00152.60           C  
ANISOU 4105  CG  MET A1113    17077  21026  19877   5881  -4684   5544       C  
ATOM   4106  SD  MET A1113     -40.589 212.067-217.760  1.00200.38           S  
ANISOU 4106  SD  MET A1113    22638  26817  26680   6063  -4576   5643       S  
ATOM   4107  CE  MET A1113     -40.116 213.524-218.687  1.00140.30           C  
ANISOU 4107  CE  MET A1113    15430  18912  18967   6413  -4331   6124       C  
ATOM   4108  N   GLN A1114     -36.379 212.295-220.579  1.00164.82           N  
ANISOU 4108  N   GLN A1114    19995  22203  20426   6177  -3818   6411       N  
ATOM   4109  CA  GLN A1114     -36.450 213.130-221.775  1.00173.18           C  
ANISOU 4109  CA  GLN A1114    21298  23270  21232   6480  -3846   6799       C  
ATOM   4110  C   GLN A1114     -35.495 212.666-222.872  1.00173.02           C  
ANISOU 4110  C   GLN A1114    21753  23482  20504   6502  -3794   6909       C  
ATOM   4111  O   GLN A1114     -35.622 213.075-224.028  1.00180.54           O  
ANISOU 4111  O   GLN A1114    22917  24588  21091   6758  -3908   7192       O  
ATOM   4112  CB  GLN A1114     -36.154 214.591-221.425  1.00176.58           C  
ANISOU 4112  CB  GLN A1114    21687  23208  22197   6591  -3358   7163       C  
ATOM   4113  CG  GLN A1114     -34.722 214.842-220.982  1.00174.41           C  
ANISOU 4113  CG  GLN A1114    21615  22605  22047   6401  -2764   7267       C  
ATOM   4114  CD  GLN A1114     -34.399 216.318-220.864  1.00178.65           C  
ANISOU 4114  CD  GLN A1114    22130  22643  23105   6516  -2319   7635       C  
ATOM   4115  OE1 GLN A1114     -35.262 217.172-221.064  1.00183.96           O  
ANISOU 4115  OE1 GLN A1114    22639  23207  24051   6747  -2442   7816       O  
ATOM   4116  NE2 GLN A1114     -33.148 216.625-220.541  1.00176.75           N  
ANISOU 4116  NE2 GLN A1114    22037  22079  23042   6350  -1810   7731       N  
ATOM   4117  N   ARG A1115     -34.542 211.814-222.503  1.00162.52           N  
ANISOU 4117  N   ARG A1115    20577  22193  18981   6249  -3610   6685       N  
ATOM   4118  CA  ARG A1115     -33.521 211.344-223.433  1.00159.22           C  
ANISOU 4118  CA  ARG A1115    20589  21979  17928   6255  -3485   6749       C  
ATOM   4119  C   ARG A1115     -34.058 210.236-224.330  1.00159.98           C  
ANISOU 4119  C   ARG A1115    20782  22582  17421   6306  -4061   6453       C  
ATOM   4120  O   ARG A1115     -33.523 209.980-225.409  1.00161.48           O  
ANISOU 4120  O   ARG A1115    21312  23028  17016   6427  -4056   6533       O  
ATOM   4121  CB  ARG A1115     -32.303 210.848-222.659  1.00152.63           C  
ANISOU 4121  CB  ARG A1115    19861  20973  17160   5969  -3080   6594       C  
ATOM   4122  CG  ARG A1115     -30.996 210.875-223.427  1.00154.91           C  
ANISOU 4122  CG  ARG A1115    20551  21284  17024   5994  -2694   6803       C  
ATOM   4123  CD  ARG A1115     -29.865 210.433-222.516  1.00152.51           C  
ANISOU 4123  CD  ARG A1115    20290  20761  16897   5703  -2312   6634       C  
ATOM   4124  NE  ARG A1115     -28.546 210.657-223.099  1.00157.05           N  
ANISOU 4124  NE  ARG A1115    21177  21265  17230   5716  -1845   6876       N  
ATOM   4125  CZ  ARG A1115     -27.405 210.480-222.440  1.00155.76           C  
ANISOU 4125  CZ  ARG A1115    21068  20859  17252   5492  -1437   6813       C  
ATOM   4126  NH1 ARG A1115     -27.422 210.080-221.172  1.00149.26           N1+
ANISOU 4126  NH1 ARG A1115    20035  19853  16824   5250  -1446   6525       N1+
ATOM   4127  NH2 ARG A1115     -26.247 210.707-223.045  1.00158.88           N  
ANISOU 4127  NH2 ARG A1115    21708  21206  17452   5519  -1014   7047       N  
ATOM   4128  N   TYR A1116     -35.118 209.579-223.871  1.00160.61           N  
ANISOU 4128  N   TYR A1116    20531  22803  17689   6212  -4544   6095       N  
ATOM   4129  CA  TYR A1116     -35.768 208.525-224.640  1.00166.24           C  
ANISOU 4129  CA  TYR A1116    21247  23951  17964   6225  -5145   5757       C  
ATOM   4130  C   TYR A1116     -37.282 208.715-224.612  1.00170.77           C  
ANISOU 4130  C   TYR A1116    21417  24603  18865   6331  -5645   5694       C  
ATOM   4131  O   TYR A1116     -38.032 207.754-224.453  1.00170.65           O  
ANISOU 4131  O   TYR A1116    21137  24793  18907   6181  -6117   5290       O  
ATOM   4132  CB  TYR A1116     -35.405 207.148-224.073  1.00161.74           C  
ANISOU 4132  CB  TYR A1116    20648  23490  17315   5904  -5268   5260       C  
ATOM   4133  CG  TYR A1116     -33.923 206.833-224.089  1.00159.90           C  
ANISOU 4133  CG  TYR A1116    20794  23196  16765   5792  -4816   5270       C  
ATOM   4134  CD1 TYR A1116     -33.102 207.207-223.033  1.00156.18           C  
ANISOU 4134  CD1 TYR A1116    20303  22370  16669   5630  -4296   5389       C  
ATOM   4135  CD2 TYR A1116     -33.347 206.154-225.157  1.00163.40           C  
ANISOU 4135  CD2 TYR A1116    21590  23942  16551   5858  -4907   5141       C  
ATOM   4136  CE1 TYR A1116     -31.748 206.918-223.041  1.00155.12           C  
ANISOU 4136  CE1 TYR A1116    20484  22168  16287   5522  -3893   5397       C  
ATOM   4137  CE2 TYR A1116     -31.993 205.861-225.175  1.00161.54           C  
ANISOU 4137  CE2 TYR A1116    21673  23652  16053   5768  -4483   5142       C  
ATOM   4138  CZ  TYR A1116     -31.199 206.246-224.114  1.00157.66           C  
ANISOU 4138  CZ  TYR A1116    21147  22791  15967   5593  -3984   5279       C  
ATOM   4139  OH  TYR A1116     -29.853 205.957-224.125  1.00155.55           O  
ANISOU 4139  OH  TYR A1116    21165  22459  15479   5499  -3569   5282       O  
ATOM   4140  N   PHE A1117     -37.722 209.959-224.776  1.00174.87           N  
ANISOU 4140  N   PHE A1117    21866  24940  19636   6585  -5535   6093       N  
ATOM   4141  CA  PHE A1117     -39.128 210.312-224.606  1.00179.06           C  
ANISOU 4141  CA  PHE A1117    21975  25471  20587   6703  -5937   6069       C  
ATOM   4142  C   PHE A1117     -40.053 209.637-225.618  1.00185.24           C  
ANISOU 4142  C   PHE A1117    22690  26680  21014   6802  -6608   5876       C  
ATOM   4143  O   PHE A1117     -41.091 209.088-225.245  1.00186.70           O  
ANISOU 4143  O   PHE A1117    22449  26967  21521   6686  -7042   5573       O  
ATOM   4144  CB  PHE A1117     -39.307 211.831-224.666  1.00184.20           C  
ANISOU 4144  CB  PHE A1117    22614  25817  21555   6983  -5654   6550       C  
ATOM   4145  CG  PHE A1117     -40.682 212.297-224.274  1.00188.70           C  
ANISOU 4145  CG  PHE A1117    22718  26312  22668   7105  -5975   6512       C  
ATOM   4146  CD1 PHE A1117     -41.416 211.610-223.320  1.00186.43           C  
ANISOU 4146  CD1 PHE A1117    21980  26055  22802   6891  -6207   6107       C  
ATOM   4147  CD2 PHE A1117     -41.243 213.416-224.866  1.00194.36           C  
ANISOU 4147  CD2 PHE A1117    23429  26933  23487   7443  -6034   6888       C  
ATOM   4148  CE1 PHE A1117     -42.682 212.036-222.960  1.00189.52           C  
ANISOU 4148  CE1 PHE A1117    21910  26387  23711   7015  -6472   6056       C  
ATOM   4149  CE2 PHE A1117     -42.511 213.846-224.512  1.00197.18           C  
ANISOU 4149  CE2 PHE A1117    23346  27217  24357   7575  -6330   6832       C  
ATOM   4150  CZ  PHE A1117     -43.230 213.156-223.558  1.00194.57           C  
ANISOU 4150  CZ  PHE A1117    22557  26924  24446   7363  -6541   6405       C  
ATOM   4151  N   THR A1118     -39.674 209.681-226.892  1.00189.39           N  
ANISOU 4151  N   THR A1118    23603  27464  20894   7014  -6669   6055       N  
ATOM   4152  CA  THR A1118     -40.514 209.159-227.971  1.00195.05           C  
ANISOU 4152  CA  THR A1118    24281  28611  21219   7162  -7283   5902       C  
ATOM   4153  C   THR A1118     -40.802 207.664-227.837  1.00192.58           C  
ANISOU 4153  C   THR A1118    23786  28565  20821   6872  -7699   5306       C  
ATOM   4154  O   THR A1118     -41.904 207.202-228.146  1.00195.38           O  
ANISOU 4154  O   THR A1118    23821  29159  21255   6878  -8254   5071       O  
ATOM   4155  CB  THR A1118     -39.878 209.456-229.320  1.00200.02           C  
ANISOU 4155  CB  THR A1118    25398  29492  21108   7461  -7181   6192       C  
ATOM   4156  N   GLU A1119     -39.806 206.914-227.376  1.00186.29           N  
ANISOU 4156  N   GLU A1119    23176  27711  19895   6615  -7420   5062       N  
ATOM   4157  CA  GLU A1119     -39.937 205.469-227.229  1.00183.87           C  
ANISOU 4157  CA  GLU A1119    22734  27604  19523   6328  -7760   4484       C  
ATOM   4158  C   GLU A1119     -40.887 205.109-226.091  1.00179.46           C  
ANISOU 4158  C   GLU A1119    21590  26905  19690   6059  -7971   4235       C  
ATOM   4159  O   GLU A1119     -41.684 204.177-226.205  1.00181.56           O  
ANISOU 4159  O   GLU A1119    21552  27384  20049   5912  -8445   3829       O  
ATOM   4160  CB  GLU A1119     -38.567 204.822-227.003  1.00179.68           C  
ANISOU 4160  CB  GLU A1119    22564  27011  18693   6141  -7378   4317       C  
ATOM   4161  CG  GLU A1119     -37.651 204.836-228.222  1.00184.40           C  
ANISOU 4161  CG  GLU A1119    23696  27844  18522   6377  -7219   4437       C  
ATOM   4162  CD  GLU A1119     -37.073 206.208-228.516  1.00185.88           C  
ANISOU 4162  CD  GLU A1119    24148  27869  18609   6650  -6721   5061       C  
ATOM   4163  OE1 GLU A1119     -37.118 207.079-227.621  1.00182.15           O  
ANISOU 4163  OE1 GLU A1119    23500  27029  18681   6607  -6411   5351       O  
ATOM   4164  OE2 GLU A1119     -36.575 206.415-229.644  1.00190.84           O1-
ANISOU 4164  OE2 GLU A1119    25145  28733  18632   6916  -6625   5254       O1-
ATOM   4165  N   ILE A1120     -40.799 205.854-224.994  1.00174.10           N  
ANISOU 4165  N   ILE A1120    20739  25870  19542   6006  -7591   4466       N  
ATOM   4166  CA  ILE A1120     -41.669 205.627-223.849  1.00171.91           C  
ANISOU 4166  CA  ILE A1120    19887  25466  19968   5789  -7706   4276       C  
ATOM   4167  C   ILE A1120     -43.096 206.021-224.194  1.00177.50           C  
ANISOU 4167  C   ILE A1120    20167  26304  20973   5951  -8136   4353       C  
ATOM   4168  O   ILE A1120     -44.051 205.318-223.853  1.00179.03           O  
ANISOU 4168  O   ILE A1120    19863  26642  21518   5765  -8465   4052       O  
ATOM   4169  CB  ILE A1120     -41.207 206.436-222.629  1.00167.18           C  
ANISOU 4169  CB  ILE A1120    19225  24471  19825   5762  -7161   4494       C  
ATOM   4170  CG1 ILE A1120     -39.735 206.151-222.337  1.00162.10           C  
ANISOU 4170  CG1 ILE A1120    19007  23711  18871   5626  -6696   4481       C  
ATOM   4171  CG2 ILE A1120     -42.064 206.106-221.417  1.00165.18           C  
ANISOU 4171  CG2 ILE A1120    18367  24136  20259   5544  -7247   4263       C  
ATOM   4172  CD1 ILE A1120     -39.112 207.109-221.350  1.00157.57           C  
ANISOU 4172  CD1 ILE A1120    18446  22778  18647   5647  -6080   4766       C  
ATOM   4173  N   PHE A1121     -43.228 207.152-224.880  1.00180.49           N  
ANISOU 4173  N   PHE A1121    20727  26633  21216   6302  -8103   4766       N  
ATOM   4174  CA  PHE A1121     -44.525 207.636-225.322  1.00185.25           C  
ANISOU 4174  CA  PHE A1121    20973  27356  22060   6508  -8516   4894       C  
ATOM   4175  C   PHE A1121     -45.174 206.614-226.247  1.00190.88           C  
ANISOU 4175  C   PHE A1121    21572  28527  22426   6470  -9092   4563       C  
ATOM   4176  O   PHE A1121     -46.371 206.350-226.152  1.00195.28           O  
ANISOU 4176  O   PHE A1121    21604  29242  23351   6425  -9468   4408       O  
ATOM   4177  CB  PHE A1121     -44.370 208.972-226.044  1.00189.10           C  
ANISOU 4177  CB  PHE A1121    21783  27717  22348   6914  -8369   5394       C  
ATOM   4178  CG  PHE A1121     -45.615 209.810-226.039  1.00194.09           C  
ANISOU 4178  CG  PHE A1121    22007  28270  23470   7136  -8634   5592       C  
ATOM   4179  CD1 PHE A1121     -46.638 209.562-226.940  1.00201.58           C  
ANISOU 4179  CD1 PHE A1121    22735  29579  24277   7267  -9209   5559       C  
ATOM   4180  CD2 PHE A1121     -45.761 210.846-225.132  1.00191.45           C  
ANISOU 4180  CD2 PHE A1121    21506  27509  23728   7240  -8300   5769       C  
ATOM   4181  CE1 PHE A1121     -47.783 210.329-226.935  1.00207.17           C  
ANISOU 4181  CE1 PHE A1121    23043  30215  25458   7474  -9457   5756       C  
ATOM   4182  CE2 PHE A1121     -46.902 211.618-225.121  1.00196.56           C  
ANISOU 4182  CE2 PHE A1121    21785  28057  24842   7472  -8546   5899       C  
ATOM   4183  CZ  PHE A1121     -47.915 211.361-226.025  1.00204.91           C  
ANISOU 4183  CZ  PHE A1121    22603  29459  25793   7575  -9136   5926       C  
ATOM   4184  N   GLN A1122     -44.372 206.038-227.137  1.00192.01           N  
ANISOU 4184  N   GLN A1122    22201  28888  21866   6503  -9135   4424       N  
ATOM   4185  CA  GLN A1122     -44.858 205.026-228.069  1.00199.27           C  
ANISOU 4185  CA  GLN A1122    23091  30218  22403   6495  -9677   4018       C  
ATOM   4186  C   GLN A1122     -45.300 203.762-227.340  1.00198.80           C  
ANISOU 4186  C   GLN A1122    22610  30184  22741   6096  -9886   3458       C  
ATOM   4187  O   GLN A1122     -46.394 203.242-227.578  1.00203.15           O  
ANISOU 4187  O   GLN A1122    22754  30939  23497   6052 -10363   3167       O  
ATOM   4188  CB  GLN A1122     -43.775 204.675-229.087  1.00200.37           C  
ANISOU 4188  CB  GLN A1122    23860  30557  21715   6628  -9597   3956       C  
ATOM   4189  CG  GLN A1122     -44.166 203.552-230.030  1.00206.63           C  
ANISOU 4189  CG  GLN A1122    24665  31744  22100   6630 -10145   3443       C  
ATOM   4190  CD  GLN A1122     -43.026 203.123-230.926  1.00207.80           C  
ANISOU 4190  CD  GLN A1122    25416  32084  21455   6756 -10010   3327       C  
ATOM   4191  OE1 GLN A1122     -41.913 203.639-230.822  1.00203.79           O  
ANISOU 4191  OE1 GLN A1122    25302  31421  20709   6817  -9478   3647       O  
ATOM   4192  NE2 GLN A1122     -43.295 202.171-231.812  1.00213.37           N  
ANISOU 4192  NE2 GLN A1122    26180  33125  21767   6806 -10479   2847       N  
ATOM   4193  N   LYS A1123     -44.439 203.273-226.453  1.00194.68           N  
ANISOU 4193  N   LYS A1123    22187  29437  22346   5808  -9520   3304       N  
ATOM   4194  CA  LYS A1123     -44.722 202.063-225.689  1.00194.52           C  
ANISOU 4194  CA  LYS A1123    21811  29373  22725   5410  -9654   2788       C  
ATOM   4195  C   LYS A1123     -45.967 202.225-224.822  1.00197.01           C  
ANISOU 4195  C   LYS A1123    21434  29618  23802   5295  -9750   2774       C  
ATOM   4196  O   LYS A1123     -46.676 201.256-224.550  1.00199.62           O  
ANISOU 4196  O   LYS A1123    21366  29989  24490   5030 -10039   2333       O  
ATOM   4197  CB  LYS A1123     -43.519 201.682-224.833  1.00185.79           C  
ANISOU 4197  CB  LYS A1123    20955  28010  21628   5160  -9201   2714       C  
ATOM   4198  N   LEU A1124     -46.231 203.454-224.391  1.00195.98           N  
ANISOU 4198  N   LEU A1124    21156  29354  23953   5497  -9486   3246       N  
ATOM   4199  CA  LEU A1124     -47.399 203.730-223.565  1.00195.93           C  
ANISOU 4199  CA  LEU A1124    20491  29311  24645   5452  -9501   3255       C  
ATOM   4200  C   LEU A1124     -48.649 203.893-224.427  1.00202.98           C  
ANISOU 4200  C   LEU A1124    21075  30486  25563   5662 -10006   3255       C  
ATOM   4201  O   LEU A1124     -49.751 203.541-224.008  1.00205.40           O  
ANISOU 4201  O   LEU A1124    20808  30857  26377   5540 -10202   3013       O  
ATOM   4202  CB  LEU A1124     -47.167 204.975-222.701  1.00192.47           C  
ANISOU 4202  CB  LEU A1124    20000  28597  24534   5607  -8992   3713       C  
ATOM   4203  CG  LEU A1124     -48.179 205.276-221.592  1.00191.87           C  
ANISOU 4203  CG  LEU A1124    19276  28467  25160   5586  -8833   3656       C  
ATOM   4204  CD1 LEU A1124     -48.364 204.081-220.667  1.00188.88           C  
ANISOU 4204  CD1 LEU A1124    18586  27996  25185   5139  -8836   3139       C  
ATOM   4205  CD2 LEU A1124     -47.759 206.506-220.800  1.00187.36           C  
ANISOU 4205  CD2 LEU A1124    18758  27636  24796   5816  -8285   4026       C  
ATOM   4206  N   GLU A1125     -48.467 204.417-225.635  1.00207.67           N  
ANISOU 4206  N   GLU A1125    22059  31233  25613   5979 -10212   3512       N  
ATOM   4207  CA  GLU A1125     -49.578 204.612-226.561  1.00216.56           C  
ANISOU 4207  CA  GLU A1125    22953  32647  26685   6221 -10726   3535       C  
ATOM   4208  C   GLU A1125     -50.052 203.284-227.141  1.00220.93           C  
ANISOU 4208  C   GLU A1125    23381  33460  27101   6042 -11255   2929       C  
ATOM   4209  O   GLU A1125     -51.218 203.136-227.509  1.00227.57           O  
ANISOU 4209  O   GLU A1125    23806  34503  28158   6107 -11702   2771       O  
ATOM   4210  CB  GLU A1125     -49.182 205.570-227.678  1.00220.27           C  
ANISOU 4210  CB  GLU A1125    23921  33181  26591   6628 -10776   3987       C  
ATOM   4211  N   GLN A1126     -49.141 202.319-227.218  1.00217.00           N  
ANISOU 4211  N   GLN A1126    23239  32929  26281   5819 -11210   2574       N  
ATOM   4212  CA  GLN A1126     -49.478 200.995-227.731  1.00219.95           C  
ANISOU 4212  CA  GLN A1126    23529  33463  26579   5627 -11692   1950       C  
ATOM   4213  C   GLN A1126     -50.234 200.176-226.691  1.00217.26           C  
ANISOU 4213  C   GLN A1126    22575  32939  27033   5217 -11741   1564       C  
ATOM   4214  O   GLN A1126     -50.796 199.126-227.003  1.00221.88           O  
ANISOU 4214  O   GLN A1126    22939  33583  27781   5029 -12175   1050       O  
ATOM   4215  CB  GLN A1126     -48.220 200.265-228.173  1.00217.66           C  
ANISOU 4215  CB  GLN A1126    23830  33172  25698   5552 -11600   1703       C  
ATOM   4216  N   THR A1127     -50.244 200.663-225.454  1.00210.33           N  
ANISOU 4216  N   THR A1127    21426  31815  26674   5085 -11281   1807       N  
ATOM   4217  CA  THR A1127     -50.883 199.952-224.352  1.00207.48           C  
ANISOU 4217  CA  THR A1127    20502  31241  27089   4687 -11224   1497       C  
ATOM   4218  C   THR A1127     -52.100 200.703-223.826  1.00209.21           C  
ANISOU 4218  C   THR A1127    20121  31477  27893   4792 -11194   1704       C  
ATOM   4219  O   THR A1127     -52.417 200.627-222.639  1.00204.74           O  
ANISOU 4219  O   THR A1127    19151  30683  27959   4546 -10885   1670       O  
ATOM   4220  CB  THR A1127     -49.879 199.713-223.229  1.00198.94           C  
ANISOU 4220  CB  THR A1127    19578  29846  26165   4403 -10697   1514       C  
ATOM   4221  N   ASP A1128     -52.774 201.423-224.721  1.00216.09           N  
ANISOU 4221  N   ASP A1128    20940  32616  28550   5166 -11508   1919       N  
ATOM   4222  CA  ASP A1128     -53.964 202.213-224.379  1.00219.49           C  
ANISOU 4222  CA  ASP A1128    20815  33100  29482   5338 -11517   2129       C  
ATOM   4223  C   ASP A1128     -53.735 203.157-223.200  1.00213.10           C  
ANISOU 4223  C   ASP A1128    19894  32062  29011   5396 -10891   2484       C  
ATOM   4224  O   ASP A1128     -54.079 202.842-222.061  1.00209.63           O  
ANISOU 4224  O   ASP A1128    19050  31409  29191   5107 -10632   2306       O  
ATOM   4225  CB  ASP A1128     -55.160 201.298-224.122  1.00224.08           C  
ANISOU 4225  CB  ASP A1128    20764  33672  30705   5041 -11858   1671       C  
ATOM   4226  N   ALA A1129     -53.161 204.320-223.482  1.00212.39           N  
ANISOU 4226  N   ALA A1129    20167  31986  28546   5767 -10645   2988       N  
ATOM   4227  CA  ALA A1129     -52.889 205.299-222.435  1.00208.68           C  
ANISOU 4227  CA  ALA A1129    19641  31281  28368   5886 -10057   3294       C  
ATOM   4228  C   ALA A1129     -53.951 206.396-222.366  1.00216.71           C  
ANISOU 4228  C   ALA A1129    20248  32374  29717   6250 -10044   3562       C  
ATOM   4229  O   ALA A1129     -54.388 206.917-223.399  1.00224.32           O  
ANISOU 4229  O   ALA A1129    21247  33563  30422   6567 -10380   3838       O  
ATOM   4230  CB  ALA A1129     -51.517 205.902-222.631  1.00203.28           C  
ANISOU 4230  CB  ALA A1129    19595  30461  27181   6034  -9717   3672       C  
ATOM   4231  N   PRO A1130     -54.377 206.743-221.143  1.00215.40           N  
ANISOU 4231  N   PRO A1130    19699  31988  30154   6194  -9665   3471       N  
ATOM   4232  CA  PRO A1130     -55.322 207.845-220.939  1.00220.33           C  
ANISOU 4232  CA  PRO A1130    19963  32623  31130   6560  -9582   3667       C  
ATOM   4233  C   PRO A1130     -54.707 209.189-221.336  1.00218.68           C  
ANISOU 4233  C   PRO A1130    20188  32367  30533   7078  -9337   4148       C  
ATOM   4234  O   PRO A1130     -53.494 209.277-221.527  1.00216.08           O  
ANISOU 4234  O   PRO A1130    20402  31941  29757   7094  -9125   4334       O  
ATOM   4235  CB  PRO A1130     -55.577 207.812-219.427  1.00216.78           C  
ANISOU 4235  CB  PRO A1130    19134  31841  31393   6275  -9139   3443       C  
ATOM   4236  CG  PRO A1130     -55.217 206.420-219.006  1.00212.13           C  
ANISOU 4236  CG  PRO A1130    18508  31181  30910   5716  -9166   3097       C  
ATOM   4237  CD  PRO A1130     -54.065 206.048-219.885  1.00208.99           C  
ANISOU 4237  CD  PRO A1130    18742  30881  29782   5738  -9322   3165       C  
ATOM   4238  N   SER A1131     -55.533 210.221-221.463  1.00219.70           N  
ANISOU 4238  N   SER A1131    20082  32540  30855   7505  -9359   4341       N  
ATOM   4239  CA  SER A1131     -55.029 211.545-221.793  1.00217.42           C  
ANISOU 4239  CA  SER A1131    20275  32050  30285   7990  -9104   4668       C  
ATOM   4240  C   SER A1131     -54.284 212.129-220.603  1.00208.02           C  
ANISOU 4240  C   SER A1131    19296  30277  29464   7962  -8628   4521       C  
ATOM   4241  O   SER A1131     -53.361 212.933-220.762  1.00205.18           O  
ANISOU 4241  O   SER A1131    19530  29485  28944   8145  -8462   4671       O  
ATOM   4242  CB  SER A1131     -56.169 212.460-222.205  1.00224.85           C  
ANISOU 4242  CB  SER A1131    20913  33107  31413   8432  -9299   4835       C  
ATOM   4243  N   ASN A1132     -54.688 211.708-219.408  1.00204.36           N  
ANISOU 4243  N   ASN A1132    18348  29667  29633   7544  -8380   4286       N  
ATOM   4244  CA  ASN A1132     -54.133 212.231-218.163  1.00200.04           C  
ANISOU 4244  CA  ASN A1132    17830  28633  29543   7346  -7793   4294       C  
ATOM   4245  C   ASN A1132     -52.627 212.005-218.052  1.00194.68           C  
ANISOU 4245  C   ASN A1132    17731  27726  28511   7148  -7530   4365       C  
ATOM   4246  O   ASN A1132     -51.877 212.932-217.750  1.00192.03           O  
ANISOU 4246  O   ASN A1132    17712  27011  28239   7250  -7141   4593       O  
ATOM   4247  CB  ASN A1132     -54.851 211.618-216.970  1.00198.97           C  
ANISOU 4247  CB  ASN A1132    17067  28491  30042   6923  -7578   4027       C  
ATOM   4248  N   LEU A1133     -52.199 210.769-218.295  1.00193.00           N  
ANISOU 4248  N   LEU A1133    17628  27743  27959   6843  -7726   4182       N  
ATOM   4249  CA  LEU A1133     -50.791 210.397-218.187  1.00186.06           C  
ANISOU 4249  CA  LEU A1133    17265  26689  26738   6625  -7503   4218       C  
ATOM   4250  C   LEU A1133     -49.898 211.209-219.115  1.00185.94           C  
ANISOU 4250  C   LEU A1133    17923  26502  26224   6989  -7535   4514       C  
ATOM   4251  O   LEU A1133     -48.874 211.744-218.694  1.00183.02           O  
ANISOU 4251  O   LEU A1133    17882  25776  25881   6903  -7083   4728       O  
ATOM   4252  CB  LEU A1133     -50.602 208.906-218.472  1.00184.88           C  
ANISOU 4252  CB  LEU A1133    17110  26845  26291   6270  -7792   3958       C  
ATOM   4253  CG  LEU A1133     -50.846 207.946-217.309  1.00182.33           C  
ANISOU 4253  CG  LEU A1133    16351  26431  26495   5724  -7621   3664       C  
ATOM   4254  CD1 LEU A1133     -50.421 206.537-217.693  1.00181.08           C  
ANISOU 4254  CD1 LEU A1133    16333  26447  26024   5375  -7909   3412       C  
ATOM   4255  CD2 LEU A1133     -50.102 208.417-216.070  1.00176.75           C  
ANISOU 4255  CD2 LEU A1133    15702  25345  26111   5548  -7002   3769       C  
ATOM   4256  N   LYS A1134     -50.292 211.294-220.380  1.00189.51           N  
ANISOU 4256  N   LYS A1134    18574  27174  26257   7341  -8046   4537       N  
ATOM   4257  CA  LYS A1134     -49.517 212.015-221.379  1.00190.60           C  
ANISOU 4257  CA  LYS A1134    19355  26939  26124   7487  -8203   4898       C  
ATOM   4258  C   LYS A1134     -49.511 213.517-221.103  1.00194.46           C  
ANISOU 4258  C   LYS A1134    19866  27107  26913   7791  -7797   5284       C  
ATOM   4259  O   LYS A1134     -48.482 214.185-221.264  1.00192.63           O  
ANISOU 4259  O   LYS A1134    20078  26610  26504   7810  -7409   5647       O  
ATOM   4260  CB  LYS A1134     -50.056 211.721-222.780  1.00195.79           C  
ANISOU 4260  CB  LYS A1134    20056  27698  26637   7396  -8884   5101       C  
ATOM   4261  CG  LYS A1134     -49.968 210.251-223.169  1.00192.98           C  
ANISOU 4261  CG  LYS A1134    19425  27928  25973   6880  -8993   5246       C  
ATOM   4262  CD  LYS A1134     -50.710 209.968-224.465  1.00200.28           C  
ANISOU 4262  CD  LYS A1134    20227  29381  26489   7069  -9545   5382       C  
ATOM   4263  CE  LYS A1134     -50.473 208.543-224.933  1.00199.21           C  
ANISOU 4263  CE  LYS A1134    20160  29700  25830   6853  -9835   5007       C  
ATOM   4264  NZ  LYS A1134     -51.134 208.268-226.238  1.00207.55           N1+
ANISOU 4264  NZ  LYS A1134    21240  31137  26482   7034 -10433   4942       N1+
ATOM   4265  N   GLU A1135     -50.657 214.046-220.682  1.00201.02           N  
ANISOU 4265  N   GLU A1135    20197  27986  28195   8004  -7811   5203       N  
ATOM   4266  CA  GLU A1135     -50.738 215.451-220.297  1.00205.42           C  
ANISOU 4266  CA  GLU A1135    20712  28185  29154   8228  -7400   5514       C  
ATOM   4267  C   GLU A1135     -49.799 215.729-219.123  1.00199.74           C  
ANISOU 4267  C   GLU A1135    20037  27141  28715   7936  -6679   5570       C  
ATOM   4268  O   GLU A1135     -49.188 216.796-219.039  1.00198.69           O  
ANISOU 4268  O   GLU A1135    20155  26639  28700   8061  -6281   5878       O  
ATOM   4269  CB  GLU A1135     -52.171 215.832-219.947  1.00210.69           C  
ANISOU 4269  CB  GLU A1135    20772  28978  30304   8443  -7533   5373       C  
ATOM   4270  N   ASN A1136     -49.680 214.755-218.224  1.00197.68           N  
ANISOU 4270  N   ASN A1136    19523  27007  28579   7542  -6525   5263       N  
ATOM   4271  CA  ASN A1136     -48.750 214.852-217.102  1.00194.96           C  
ANISOU 4271  CA  ASN A1136    19229  26380  28468   7243  -5911   5261       C  
ATOM   4272  C   ASN A1136     -47.297 214.766-217.552  1.00192.34           C  
ANISOU 4272  C   ASN A1136    19514  25918  27649   7156  -5727   5471       C  
ATOM   4273  O   ASN A1136     -46.417 215.384-216.956  1.00190.04           O  
ANISOU 4273  O   ASN A1136    19395  25290  27521   7087  -5205   5607       O  
ATOM   4274  CB  ASN A1136     -49.033 213.766-216.059  1.00192.83           C  
ANISOU 4274  CB  ASN A1136    18527  26283  28456   6828  -5831   4901       C  
ATOM   4275  CG  ASN A1136     -50.328 213.999-215.311  1.00197.03           C  
ANISOU 4275  CG  ASN A1136    18419  26862  29580   6856  -5795   4719       C  
ATOM   4276  OD1 ASN A1136     -51.062 213.058-215.014  1.00197.88           O  
ANISOU 4276  OD1 ASN A1136    18115  27236  29834   6625  -5993   4455       O  
ATOM   4277  ND2 ASN A1136     -50.618 215.259-215.008  1.00199.79           N  
ANISOU 4277  ND2 ASN A1136    18676  26940  30296   7129  -5526   4857       N  
ATOM   4278  N   MET A1137     -47.053 213.989-218.603  1.00192.30           N  
ANISOU 4278  N   MET A1137    19825  26182  27056   7161  -6157   5464       N  
ATOM   4279  CA  MET A1137     -45.723 213.865-219.187  1.00187.90           C  
ANISOU 4279  CA  MET A1137    19864  25557  25973   7096  -6005   5671       C  
ATOM   4280  C   MET A1137     -45.266 215.211-219.737  1.00188.94           C  
ANISOU 4280  C   MET A1137    20338  25374  26075   7395  -5741   6118       C  
ATOM   4281  O   MET A1137     -44.201 215.730-219.369  1.00185.92           O  
ANISOU 4281  O   MET A1137    20211  24686  25742   7313  -5215   6303       O  
ATOM   4282  CB  MET A1137     -45.747 212.832-220.314  1.00190.47           C  
ANISOU 4282  CB  MET A1137    20427  26241  25703   7076  -6585   5555       C  
ATOM   4283  CG  MET A1137     -44.901 211.597-220.064  1.00184.94           C  
ANISOU 4283  CG  MET A1137    19886  25689  24692   6707  -6540   5319       C  
ATOM   4284  SD  MET A1137     -45.222 210.313-221.291  1.00179.46           S  
ANISOU 4284  SD  MET A1137    19311  25395  23480   6621  -7304   5098       S  
ATOM   4285  CE  MET A1137     -43.789 209.268-221.066  1.00153.54           C  
ANISOU 4285  CE  MET A1137    16407  22177  19755   6265  -7023   4956       C  
ATOM   4286  N   HIS A1138     -46.084 215.775-220.620  1.00193.56           N  
ANISOU 4286  N   HIS A1138    20907  26021  26616   7737  -6117   6289       N  
ATOM   4287  CA  HIS A1138     -45.774 217.071-221.204  1.00196.57           C  
ANISOU 4287  CA  HIS A1138    21574  26111  27003   8034  -5899   6749       C  
ATOM   4288  C   HIS A1138     -45.751 218.158-220.131  1.00194.44           C  
ANISOU 4288  C   HIS A1138    21068  25401  27410   8059  -5361   6809       C  
ATOM   4289  O   HIS A1138     -45.050 219.162-220.268  1.00195.12           O  
ANISOU 4289  O   HIS A1138    21417  25128  27590   8164  -4974   7149       O  
ATOM   4290  CB  HIS A1138     -46.760 217.421-222.323  1.00205.32           C  
ANISOU 4290  CB  HIS A1138    22662  27389  27960   8398  -6455   6918       C  
ATOM   4291  CG  HIS A1138     -46.621 216.563-223.544  1.00207.38           C  
ANISOU 4291  CG  HIS A1138    23234  28025  27538   8388  -6948   6942       C  
ATOM   4292  ND1 HIS A1138     -45.666 216.792-224.513  1.00208.35           N  
ANISOU 4292  ND1 HIS A1138    23892  28168  27105   8463  -6804   7321       N  
ATOM   4293  CD2 HIS A1138     -47.319 215.477-223.958  1.00208.99           C  
ANISOU 4293  CD2 HIS A1138    23256  28600  27550   8293  -7565   6634       C  
ATOM   4294  CE1 HIS A1138     -45.780 215.886-225.467  1.00210.71           C  
ANISOU 4294  CE1 HIS A1138    24338  28873  26848   8429  -7291   7237       C  
ATOM   4295  NE2 HIS A1138     -46.775 215.076-225.154  1.00211.17           N  
ANISOU 4295  NE2 HIS A1138    23960  29131  27145   8303  -7776   6829       N  
ATOM   4296  N   ARG A1139     -46.509 217.955-219.056  1.00192.96           N  
ANISOU 4296  N   ARG A1139    20368  25233  27716   7946  -5323   6468       N  
ATOM   4297  CA  ARG A1139     -46.460 218.892-217.939  1.00193.61           C  
ANISOU 4297  CA  ARG A1139    20212  24907  28446   7930  -4809   6443       C  
ATOM   4298  C   ARG A1139     -45.107 218.840-217.246  1.00184.70           C  
ANISOU 4298  C   ARG A1139    19324  23513  27341   7639  -4277   6430       C  
ATOM   4299  O   ARG A1139     -44.550 219.872-216.895  1.00183.45           O  
ANISOU 4299  O   ARG A1139    19264  22916  27523   7694  -3849   6583       O  
ATOM   4300  CB  ARG A1139     -47.562 218.627-216.918  1.00197.75           C  
ANISOU 4300  CB  ARG A1139    20121  25551  29463   7853  -4850   6065       C  
ATOM   4301  CG  ARG A1139     -47.495 219.592-215.748  1.00200.53           C  
ANISOU 4301  CG  ARG A1139    20245  25487  30460   7847  -4321   5983       C  
ATOM   4302  CD  ARG A1139     -48.527 219.300-214.691  1.00203.20           C  
ANISOU 4302  CD  ARG A1139    19985  25970  31252   7752  -4295   5605       C  
ATOM   4303  NE  ARG A1139     -48.415 220.245-213.580  1.00204.77           N  
ANISOU 4303  NE  ARG A1139    20005  25777  32021   7771  -3788   5474       N  
ATOM   4304  CZ  ARG A1139     -49.203 220.249-212.512  1.00207.13           C  
ANISOU 4304  CZ  ARG A1139    19809  26127  32765   7722  -3626   5144       C  
ATOM   4305  NH1 ARG A1139     -50.171 219.355-212.402  1.00208.99           N1+
ANISOU 4305  NH1 ARG A1139    19649  26773  32984   7622  -3908   4951       N1+
ATOM   4306  NH2 ARG A1139     -49.024 221.150-211.556  1.00207.59           N  
ANISOU 4306  NH2 ARG A1139    19762  25826  33287   7771  -3176   4988       N  
ATOM   4307  N   VAL A1140     -44.592 217.631-217.046  1.00179.49           N  
ANISOU 4307  N   VAL A1140    18742  23108  26350   7331  -4326   6226       N  
ATOM   4308  CA  VAL A1140     -43.271 217.441-216.461  1.00173.16           C  
ANISOU 4308  CA  VAL A1140    18185  22101  25506   7058  -3876   6202       C  
ATOM   4309  C   VAL A1140     -42.207 218.110-217.324  1.00175.83           C  
ANISOU 4309  C   VAL A1140    19048  22201  25559   7172  -3667   6599       C  
ATOM   4310  O   VAL A1140     -41.333 218.822-216.815  1.00174.05           O  
ANISOU 4310  O   VAL A1140    18941  21560  25631   7103  -3186   6682       O  
ATOM   4311  CB  VAL A1140     -42.938 215.945-216.302  1.00166.99           C  
ANISOU 4311  CB  VAL A1140    17430  21681  24339   6736  -4044   5950       C  
ATOM   4312  CG1 VAL A1140     -41.468 215.753-215.991  1.00162.22           C  
ANISOU 4312  CG1 VAL A1140    17177  20891  23569   6510  -3635   5991       C  
ATOM   4313  CG2 VAL A1140     -43.797 215.324-215.214  1.00164.74           C  
ANISOU 4313  CG2 VAL A1140    16594  21555  24444   6541  -4100   5576       C  
ATOM   4314  N   LYS A1141     -42.291 217.888-218.633  1.00181.07           N  
ANISOU 4314  N   LYS A1141    20007  23125  25666   7342  -4029   6829       N  
ATOM   4315  CA  LYS A1141     -41.378 218.551-219.560  1.00185.33           C  
ANISOU 4315  CA  LYS A1141    21019  23483  25914   7470  -3824   7256       C  
ATOM   4316  C   LYS A1141     -41.452 220.075-219.439  1.00188.92           C  
ANISOU 4316  C   LYS A1141    21413  23456  26912   7687  -3510   7540       C  
ATOM   4317  O   LYS A1141     -40.423 220.752-219.378  1.00187.36           O  
ANISOU 4317  O   LYS A1141    21443  22885  26861   7628  -3055   7759       O  
ATOM   4318  CB  LYS A1141     -41.662 218.131-221.001  1.00192.64           C  
ANISOU 4318  CB  LYS A1141    22220  24805  26170   7664  -4304   7443       C  
ATOM   4319  CG  LYS A1141     -41.152 216.749-221.363  1.00191.73           C  
ANISOU 4319  CG  LYS A1141    22331  25087  25432   7444  -4516   7232       C  
ATOM   4320  CD  LYS A1141     -41.123 216.573-222.870  1.00200.36           C  
ANISOU 4320  CD  LYS A1141    23790  26492  25848   7648  -4857   7476       C  
ATOM   4321  CE  LYS A1141     -40.292 217.666-223.528  1.00206.32           C  
ANISOU 4321  CE  LYS A1141    24901  26979  26513   7823  -4443   7996       C  
ATOM   4322  NZ  LYS A1141     -40.297 217.577-225.015  1.00213.36           N1+
ANISOU 4322  NZ  LYS A1141    26131  28207  26729   8057  -4734   8278       N1+
ATOM   4323  N   GLU A1142     -42.671 220.606-219.392  1.00194.17           N  
ANISOU 4323  N   GLU A1142    21749  24115  27912   7930  -3758   7517       N  
ATOM   4324  CA  GLU A1142     -42.876 222.052-219.325  1.00199.90           C  
ANISOU 4324  CA  GLU A1142    22394  24391  29169   8167  -3519   7770       C  
ATOM   4325  C   GLU A1142     -42.391 222.650-218.005  1.00196.34           C  
ANISOU 4325  C   GLU A1142    21748  23465  29389   7983  -2998   7554       C  
ATOM   4326  O   GLU A1142     -41.923 223.790-217.963  1.00201.45           O  
ANISOU 4326  O   GLU A1142    22478  23638  30424   8063  -2652   7779       O  
ATOM   4327  CB  GLU A1142     -44.344 222.393-219.555  1.00204.90           C  
ANISOU 4327  CB  GLU A1142    22696  25161  29995   8478  -3936   7749       C  
ATOM   4328  N   LEU A1143     -42.510 221.876-216.931  1.00187.40           N  
ANISOU 4328  N   LEU A1143    20343  22459  28403   7735  -2955   7104       N  
ATOM   4329  CA  LEU A1143     -42.097 222.324-215.606  1.00181.63           C  
ANISOU 4329  CA  LEU A1143    19409  21335  28267   7562  -2504   6811       C  
ATOM   4330  C   LEU A1143     -40.581 222.333-215.489  1.00177.31           C  
ANISOU 4330  C   LEU A1143    19208  20517  27645   7326  -2105   6886       C  
ATOM   4331  O   LEU A1143     -39.998 223.269-214.941  1.00175.75           O  
ANISOU 4331  O   LEU A1143    19007  19821  27949   7293  -1713   6860       O  
ATOM   4332  CB  LEU A1143     -42.706 221.432-214.519  1.00176.40           C  
ANISOU 4332  CB  LEU A1143    18343  20946  27735   7377  -2579   6326       C  
ATOM   4333  CG  LEU A1143     -44.216 221.547-214.295  1.00180.03           C  
ANISOU 4333  CG  LEU A1143    18340  21598  28465   7571  -2857   6160       C  
ATOM   4334  CD1 LEU A1143     -44.725 220.434-213.391  1.00175.22           C  
ANISOU 4334  CD1 LEU A1143    17360  21345  27870   7334  -2938   5743       C  
ATOM   4335  CD2 LEU A1143     -44.566 222.911-213.723  1.00184.93           C  
ANISOU 4335  CD2 LEU A1143    18753  21768  29745   7772  -2586   6111       C  
ATOM   4336  N   PHE A1144     -39.946 221.285-216.002  1.00176.06           N  
ANISOU 4336  N   PHE A1144    19334  20683  26878   7160  -2216   6947       N  
ATOM   4337  CA  PHE A1144     -38.491 221.217-216.002  1.00174.49           C  
ANISOU 4337  CA  PHE A1144    19471  20270  26556   6944  -1853   7037       C  
ATOM   4338  C   PHE A1144     -37.892 222.263-216.936  1.00183.12           C  
ANISOU 4338  C   PHE A1144    20865  21047  27664   7100  -1652   7518       C  
ATOM   4339  O   PHE A1144     -36.796 222.769-216.695  1.00184.25           O  
ANISOU 4339  O   PHE A1144    21151  20795  28060   6955  -1236   7584       O  
ATOM   4340  CB  PHE A1144     -38.015 219.822-216.399  1.00169.77           C  
ANISOU 4340  CB  PHE A1144    19107  20127  25272   6757  -2042   6983       C  
ATOM   4341  CG  PHE A1144     -37.966 218.850-215.256  1.00164.98           C  
ANISOU 4341  CG  PHE A1144    18272  19666  24746   6485  -2019   6536       C  
ATOM   4342  CD1 PHE A1144     -39.106 218.178-214.847  1.00164.25           C  
ANISOU 4342  CD1 PHE A1144    17814  19918  24674   6482  -2351   6269       C  
ATOM   4343  CD2 PHE A1144     -36.776 218.606-214.589  1.00159.75           C  
ANISOU 4343  CD2 PHE A1144    17738  18797  24161   6228  -1660   6392       C  
ATOM   4344  CE1 PHE A1144     -39.059 217.282-213.796  1.00158.25           C  
ANISOU 4344  CE1 PHE A1144    16824  19306  23999   6222  -2303   5899       C  
ATOM   4345  CE2 PHE A1144     -36.724 217.713-213.537  1.00153.02           C  
ANISOU 4345  CE2 PHE A1144    16678  18091  23373   5995  -1639   6006       C  
ATOM   4346  CZ  PHE A1144     -37.866 217.051-213.140  1.00152.67           C  
ANISOU 4346  CZ  PHE A1144    16272  18402  23334   5987  -1950   5774       C  
ATOM   4347  N   ASP A1145     -38.619 222.583-218.002  1.00189.43           N  
ANISOU 4347  N   ASP A1145    21738  22026  28212   7394  -1951   7854       N  
ATOM   4348  CA  ASP A1145     -38.165 223.582-218.962  1.00196.01           C  
ANISOU 4348  CA  ASP A1145    22832  22605  29040   7574  -1775   8370       C  
ATOM   4349  C   ASP A1145     -38.392 224.994-218.435  1.00200.83           C  
ANISOU 4349  C   ASP A1145    23213  22645  30450   7692  -1514   8425       C  
ATOM   4350  O   ASP A1145     -37.446 225.763-218.257  1.00202.19           O  
ANISOU 4350  O   ASP A1145    23473  22350  31002   7584  -1087   8557       O  
ATOM   4351  CB  ASP A1145     -38.872 223.395-220.295  1.00202.08           C  
ANISOU 4351  CB  ASP A1145    23766  23792  29222   7867  -2214   8698       C  
ATOM   4352  N   ASN A1146     -39.654 225.328-218.189  1.00202.96           N  
ANISOU 4352  N   ASN A1146    23167  22950  30999   7912  -1779   8300       N  
ATOM   4353  CA  ASN A1146     -40.017 226.641-217.675  1.00205.24           C  
ANISOU 4353  CA  ASN A1146    23212  22725  32046   8056  -1580   8299       C  
ATOM   4354  C   ASN A1146     -40.040 226.630-216.151  1.00200.01           C  
ANISOU 4354  C   ASN A1146    22220  21837  31937   7854  -1370   7717       C  
ATOM   4355  O   ASN A1146     -39.150 226.064-215.514  1.00193.70           O  
ANISOU 4355  O   ASN A1146    21490  21006  31103   7553  -1147   7455       O  
ATOM   4356  CB  ASN A1146     -41.366 227.070-218.227  1.00210.31           C  
ANISOU 4356  CB  ASN A1146    23681  23517  32709   8430  -1963   8468       C  
TER   
ATOM  17071  N   MET E   1       9.661 177.699-220.935  1.00173.18           N  
ANISOU17071  N   MET E   1    20432  29525  15845   6957   1618  -2295       N  
ATOM  17072  CA  MET E   1       8.245 177.901-221.215  1.00168.13           C  
ANISOU17072  CA  MET E   1    20438  28172  15272   6633   1327  -2575       C  
ATOM  17073  C   MET E   1       7.729 179.147-220.508  1.00164.02           C  
ANISOU17073  C   MET E   1    19810  27625  14884   5847   1075  -2393       C  
ATOM  17074  O   MET E   1       7.653 179.183-219.281  1.00162.69           O  
ANISOU17074  O   MET E   1    19424  27393  14999   5634    872  -2232       O  
ATOM  17075  CB  MET E   1       7.443 176.681-220.795  1.00166.12           C  
ANISOU17075  CB  MET E   1    20615  27196  15306   6983   1104  -2815       C  
ATOM  17076  N   ARG E   2       7.373 180.165-221.286  1.00162.88           N  
ANISOU17076  N   ARG E   2    19844  27521  14521   5436   1102  -2414       N  
ATOM  17077  CA  ARG E   2       6.893 181.424-220.727  1.00158.95           C  
ANISOU17077  CA  ARG E   2    19302  26971  14121   4710    913  -2246       C  
ATOM  17078  C   ARG E   2       5.439 181.326-220.275  1.00154.58           C  
ANISOU17078  C   ARG E   2    19238  25661  13836   4506    554  -2411       C  
ATOM  17079  O   ARG E   2       4.664 180.531-220.807  1.00155.60           O  
ANISOU17079  O   ARG E   2    19826  25311  13984   4811    453  -2683       O  
ATOM  17080  CB  ARG E   2       7.063 182.553-221.734  1.00159.65           C  
ANISOU17080  CB  ARG E   2    19404  27368  13886   4373   1099  -2167       C  
ATOM  17081  N   GLU E   3       5.074 182.142-219.292  1.00150.05           N  
ANISOU17081  N   GLU E   3    18566  24989  13457   3979    366  -2243       N  
ATOM  17082  CA  GLU E   3       3.712 182.145-218.771  1.00144.24           C  
ANISOU17082  CA  GLU E   3    18232  23590  12983   3769     51  -2341       C  
ATOM  17083  C   GLU E   3       2.864 183.231-219.421  1.00138.41           C  
ANISOU17083  C   GLU E   3    17820  22639  12129   3344      3  -2351       C  
ATOM  17084  O   GLU E   3       3.241 184.404-219.440  1.00136.65           O  
ANISOU17084  O   GLU E   3    17426  22716  11780   2917    116  -2164       O  
ATOM  17085  CB  GLU E   3       3.721 182.314-217.257  1.00143.27           C  
ANISOU17085  CB  GLU E   3    17861  23438  13136   3508   -117  -2160       C  
ATOM  17086  N   TYR E   4       1.713 182.829-219.949  1.00135.01           N  
ANISOU17086  N   TYR E   4    17861  21689  11746   3455   -171  -2553       N  
ATOM  17087  CA  TYR E   4       0.772 183.769-220.543  1.00131.78           C  
ANISOU17087  CA  TYR E   4    17773  21046  11251   3103   -249  -2538       C  
ATOM  17088  C   TYR E   4      -0.489 183.876-219.687  1.00126.82           C  
ANISOU17088  C   TYR E   4    17366  19867  10951   2871   -543  -2510       C  
ATOM  17089  O   TYR E   4      -0.958 182.881-219.140  1.00124.97           O  
ANISOU17089  O   TYR E   4    17224  19296  10961   3101   -728  -2617       O  
ATOM  17090  CB  TYR E   4       0.412 183.331-221.965  1.00133.55           C  
ANISOU17090  CB  TYR E   4    18350  21185  11209   3382   -221  -2760       C  
ATOM  17091  CG  TYR E   4       1.585 183.324-222.917  1.00138.28           C  
ANISOU17091  CG  TYR E   4    18765  22340  11435   3618    109  -2774       C  
ATOM  17092  CD1 TYR E   4       1.951 184.475-223.602  1.00140.63           C  
ANISOU17092  CD1 TYR E   4    18978  22998  11456   3327    310  -2603       C  
ATOM  17093  CD2 TYR E   4       2.324 182.168-223.135  1.00142.27           C  
ANISOU17093  CD2 TYR E   4    19186  23004  11867   4152    244  -2938       C  
ATOM  17094  CE1 TYR E   4       3.023 184.476-224.477  1.00146.21           C  
ANISOU17094  CE1 TYR E   4    19492  24247  11814   3544    634  -2584       C  
ATOM  17095  CE2 TYR E   4       3.397 182.160-224.008  1.00147.46           C  
ANISOU17095  CE2 TYR E   4    19660  24198  12172   4409    582  -2931       C  
ATOM  17096  CZ  TYR E   4       3.742 183.317-224.677  1.00148.39           C  
ANISOU17096  CZ  TYR E   4    19667  24705  12011   4095    775  -2748       C  
ATOM  17097  OH  TYR E   4       4.807 183.319-225.547  1.00150.82           O  
ANISOU17097  OH  TYR E   4    19766  25577  11960   4350   1131  -2710       O  
ATOM  17098  N   LYS E   5      -1.030 185.084-219.564  1.00126.23           N  
ANISOU17098  N   LYS E   5    17380  19696  10886   2431   -566  -2348       N  
ATOM  17099  CA  LYS E   5      -2.235 185.301-218.764  1.00125.00           C  
ANISOU17099  CA  LYS E   5    17422  19051  11023   2223   -801  -2286       C  
ATOM  17100  C   LYS E   5      -3.421 185.713-219.634  1.00127.09           C  
ANISOU17100  C   LYS E   5    18059  19003  11226   2130   -912  -2300       C  
ATOM  17101  O   LYS E   5      -3.585 186.892-219.949  1.00127.42           O  
ANISOU17101  O   LYS E   5    18168  19097  11148   1826   -813  -2142       O  
ATOM  17102  CB  LYS E   5      -1.988 186.360-217.683  1.00121.99           C  
ANISOU17102  CB  LYS E   5    16858  18753  10740   1803   -743  -2070       C  
ATOM  17103  CG  LYS E   5      -0.893 186.004-216.685  1.00122.69           C  
ANISOU17103  CG  LYS E   5    16552  19173  10890   1838   -686  -2021       C  
ATOM  17104  CD  LYS E   5      -0.865 186.974-215.508  1.00120.82           C  
ANISOU17104  CD  LYS E   5    16221  18928  10757   1394   -696  -1847       C  
ATOM  17105  CE  LYS E   5       0.170 186.557-214.472  1.00122.17           C  
ANISOU17105  CE  LYS E   5    15988  19456  10974   1420   -690  -1788       C  
ATOM  17106  NZ  LYS E   5       0.134 187.414-213.252  1.00119.89           N1+
ANISOU17106  NZ  LYS E   5    15658  19133  10762    983   -736  -1657       N1+
ATOM  17107  N   LEU E   6      -4.250 184.743-220.012  1.00128.24           N  
ANISOU17107  N   LEU E   6    18447  18821  11456   2381  -1125  -2472       N  
ATOM  17108  CA  LEU E   6      -5.406 185.023-220.862  1.00129.56           C  
ANISOU17108  CA  LEU E   6    18939  18734  11554   2302  -1276  -2476       C  
ATOM  17109  C   LEU E   6      -6.682 185.163-220.040  1.00127.27           C  
ANISOU17109  C   LEU E   6    18757  17999  11603   2134  -1507  -2343       C  
ATOM  17110  O   LEU E   6      -7.041 184.261-219.290  1.00126.52           O  
ANISOU17110  O   LEU E   6    18647  17643  11782   2262  -1678  -2406       O  
ATOM  17111  CB  LEU E   6      -5.579 183.931-221.913  1.00132.87           C  
ANISOU17111  CB  LEU E   6    19586  19091  11809   2628  -1390  -2752       C  
ATOM  17112  CG  LEU E   6      -4.346 183.656-222.773  1.00138.90           C  
ANISOU17112  CG  LEU E   6    20269  20290  12217   2881  -1135  -2902       C  
ATOM  17113  CD1 LEU E   6      -4.654 182.629-223.852  1.00142.94           C  
ANISOU17113  CD1 LEU E   6    21103  20679  12528   3191  -1253  -3206       C  
ATOM  17114  CD2 LEU E   6      -3.836 184.946-223.385  1.00141.28           C  
ANISOU17114  CD2 LEU E   6    20478  20978  12225   2646   -887  -2714       C  
ATOM  17115  N   VAL E   7      -7.367 186.292-220.194  1.00125.93           N  
ANISOU17115  N   VAL E   7    18693  17745  11411   1867  -1491  -2136       N  
ATOM  17116  CA  VAL E   7      -8.559 186.583-219.404  1.00122.58           C  
ANISOU17116  CA  VAL E   7    18345  16940  11290   1721  -1652  -1960       C  
ATOM  17117  C   VAL E   7      -9.830 186.482-220.237  1.00123.32           C  
ANISOU17117  C   VAL E   7    18673  16810  11373   1742  -1878  -1928       C  
ATOM  17118  O   VAL E   7      -9.916 187.067-221.317  1.00127.58           O  
ANISOU17118  O   VAL E   7    19336  17500  11638   1696  -1825  -1885       O  
ATOM  17119  CB  VAL E   7      -8.487 187.989-218.782  1.00120.93           C  
ANISOU17119  CB  VAL E   7    18094  16749  11106   1415  -1455  -1712       C  
ATOM  17120  CG1 VAL E   7      -9.753 188.284-218.005  1.00119.86           C  
ANISOU17120  CG1 VAL E   7    18055  16222  11263   1325  -1583  -1524       C  
ATOM  17121  CG2 VAL E   7      -7.266 188.114-217.883  1.00120.69           C  
ANISOU17121  CG2 VAL E   7    17818  16960  11079   1327  -1277  -1734       C  
ATOM  17122  N   VAL E   8     -10.819 185.750-219.730  1.00119.39           N  
ANISOU17122  N   VAL E   8    18218  15977  11168   1797  -2135  -1922       N  
ATOM  17123  CA  VAL E   8     -12.069 185.562-220.461  1.00118.48           C  
ANISOU17123  CA  VAL E   8    18280  15674  11065   1788  -2397  -1874       C  
ATOM  17124  C   VAL E   8     -13.208 186.425-219.916  1.00116.60           C  
ANISOU17124  C   VAL E   8    18034  15223  11046   1620  -2434  -1537       C  
ATOM  17125  O   VAL E   8     -13.785 186.124-218.873  1.00114.66           O  
ANISOU17125  O   VAL E   8    17706  14729  11130   1610  -2524  -1434       O  
ATOM  17126  CB  VAL E   8     -12.495 184.089-220.462  1.00119.04           C  
ANISOU17126  CB  VAL E   8    18419  15513  11297   1944  -2690  -2087       C  
ATOM  17127  CG1 VAL E   8     -13.683 183.890-221.385  1.00120.96           C  
ANISOU17127  CG1 VAL E   8    18841  15634  11483   1887  -2988  -2062       C  
ATOM  17128  CG2 VAL E   8     -11.339 183.217-220.900  1.00121.44           C  
ANISOU17128  CG2 VAL E   8    18751  15988  11402   2171  -2607  -2417       C  
ATOM  17129  N   LEU E   9     -13.532 187.488-220.646  1.00117.53           N  
ANISOU17129  N   LEU E   9    18241  15443  10970   1516  -2347  -1346       N  
ATOM  17130  CA  LEU E   9     -14.546 188.448-220.225  1.00117.89           C  
ANISOU17130  CA  LEU E   9    18296  15308  11188   1404  -2318   -996       C  
ATOM  17131  C   LEU E   9     -15.862 188.216-220.943  1.00121.28           C  
ANISOU17131  C   LEU E   9    18789  15645  11645   1425  -2614   -855       C  
ATOM  17132  O   LEU E   9     -15.892 187.645-222.033  1.00124.84           O  
ANISOU17132  O   LEU E   9    19334  16231  11866   1472  -2803  -1023       O  
ATOM  17133  CB  LEU E   9     -14.075 189.857-220.555  1.00121.30           C  
ANISOU17133  CB  LEU E   9    18797  15890  11402   1280  -2011   -824       C  
ATOM  17134  CG  LEU E   9     -12.652 190.187-220.125  1.00122.60           C  
ANISOU17134  CG  LEU E   9    18890  16238  11452   1196  -1728   -960       C  
ATOM  17135  CD1 LEU E   9     -12.175 191.437-220.836  1.00124.10           C  
ANISOU17135  CD1 LEU E   9    19178  16609  11367   1055  -1467   -813       C  
ATOM  17136  CD2 LEU E   9     -12.613 190.371-218.625  1.00120.29           C  
ANISOU17136  CD2 LEU E   9    18511  15748  11445   1116  -1633   -895       C  
ATOM  17137  N   GLY E  10     -16.951 188.681-220.340  1.00120.78           N  
ANISOU17137  N   GLY E  10    18673  15374  11843   1389  -2650   -538       N  
ATOM  17138  CA  GLY E  10     -18.247 188.612-220.989  1.00123.28           C  
ANISOU17138  CA  GLY E  10    18991  15656  12192   1390  -2922   -322       C  
ATOM  17139  C   GLY E  10     -19.417 188.846-220.055  1.00121.94           C  
ANISOU17139  C   GLY E  10    18692  15249  12390   1395  -2960     21       C  
ATOM  17140  O   GLY E  10     -19.245 189.319-218.931  1.00120.68           O  
ANISOU17140  O   GLY E  10    18492  14940  12420   1402  -2718    118       O  
ATOM  17141  N   SER E  11     -20.613 188.510-220.529  1.00121.42           N  
ANISOU17141  N   SER E  11    18555  15172  12408   1387  -3268    211       N  
ATOM  17142  CA  SER E  11     -21.828 188.673-219.740  1.00117.05           C  
ANISOU17142  CA  SER E  11    17830  14442  12203   1412  -3318    585       C  
ATOM  17143  C   SER E  11     -22.200 187.376-219.031  1.00114.85           C  
ANISOU17143  C   SER E  11    17417  13988  12233   1382  -3575    474       C  
ATOM  17144  O   SER E  11     -21.399 186.446-218.954  1.00115.20           O  
ANISOU17144  O   SER E  11    17525  13998  12248   1368  -3649    103       O  
ATOM  17145  CB  SER E  11     -22.982 189.133-220.630  1.00117.33           C  
ANISOU17145  CB  SER E  11    17802  14609  12169   1414  -3501    943       C  
ATOM  17146  OG  SER E  11     -22.591 190.233-221.430  1.00117.46           O  
ANISOU17146  OG  SER E  11    17967  14793  11869   1446  -3286   1038       O  
ATOM  17147  N   GLY E  12     -23.421 187.319-218.514  1.00114.40           N  
ANISOU17147  N   GLY E  12    17166  13821  12478   1386  -3695    825       N  
ATOM  17148  CA  GLY E  12     -23.875 186.157-217.774  1.00115.08           C  
ANISOU17148  CA  GLY E  12    17106  13726  12892   1339  -3921    794       C  
ATOM  17149  C   GLY E  12     -24.331 185.021-218.670  1.00120.08           C  
ANISOU17149  C   GLY E  12    17738  14392  13496   1192  -4388    640       C  
ATOM  17150  O   GLY E  12     -25.316 185.149-219.397  1.00124.57           O  
ANISOU17150  O   GLY E  12    18209  15090  14032   1110  -4636    885       O  
ATOM  17151  N   GLY E  13     -23.606 183.907-218.622  1.00119.22           N  
ANISOU17151  N   GLY E  13    17748  14165  13385   1158  -4510    235       N  
ATOM  17152  CA  GLY E  13     -24.008 182.700-219.319  1.00120.34           C  
ANISOU17152  CA  GLY E  13    17949  14245  13530   1004  -4948     38       C  
ATOM  17153  C   GLY E  13     -23.796 182.727-220.820  1.00122.55           C  
ANISOU17153  C   GLY E  13    18437  14744  13381    942  -5130   -188       C  
ATOM  17154  O   GLY E  13     -24.641 182.251-221.579  1.00126.84           O  
ANISOU17154  O   GLY E  13    18975  15335  13881    766  -5523   -149       O  
ATOM  17155  N   VAL E  14     -22.667 183.277-221.256  1.00118.93           N  
ANISOU17155  N   VAL E  14    18158  14443  12588   1069  -4853   -417       N  
ATOM  17156  CA  VAL E  14     -22.359 183.318-222.683  1.00117.85           C  
ANISOU17156  CA  VAL E  14    18238  14543  11998   1041  -4978   -642       C  
ATOM  17157  C   VAL E  14     -21.496 182.124-223.082  1.00117.61           C  
ANISOU17157  C   VAL E  14    18461  14414  11811   1072  -5087  -1171       C  
ATOM  17158  O   VAL E  14     -21.355 181.812-224.262  1.00120.68           O  
ANISOU17158  O   VAL E  14    19074  14945  11835   1035  -5267  -1424       O  
ATOM  17159  CB  VAL E  14     -21.665 184.638-223.091  1.00112.85           C  
ANISOU17159  CB  VAL E  14    17658  14168  11051   1156  -4610   -552       C  
ATOM  17160  CG1 VAL E  14     -22.461 185.828-222.589  1.00110.43           C  
ANISOU17160  CG1 VAL E  14    17149  13885  10925   1171  -4445    -36       C  
ATOM  17161  CG2 VAL E  14     -20.253 184.688-222.552  1.00110.24           C  
ANISOU17161  CG2 VAL E  14    17402  13814  10669   1292  -4246   -822       C  
ATOM  17162  N   GLY E  15     -20.928 181.458-222.083  1.00114.44           N  
ANISOU17162  N   GLY E  15    18037  13769  11675   1162  -4965  -1328       N  
ATOM  17163  CA  GLY E  15     -20.131 180.269-222.314  1.00115.81           C  
ANISOU17163  CA  GLY E  15    18444  13796  11762   1246  -5034  -1794       C  
ATOM  17164  C   GLY E  15     -18.651 180.465-222.047  1.00111.63           C  
ANISOU17164  C   GLY E  15    17960  13375  11080   1481  -4635  -2016       C  
ATOM  17165  O   GLY E  15     -17.815 179.784-222.638  1.00113.23           O  
ANISOU17165  O   GLY E  15    18384  13595  11045   1614  -4614  -2402       O  
ATOM  17166  N   LYS E  16     -18.321 181.397-221.159  1.00106.44           N  
ANISOU17166  N   LYS E  16    17095  12800  10548   1532  -4315  -1769       N  
ATOM  17167  CA  LYS E  16     -16.924 181.641-220.815  1.00105.11           C  
ANISOU17167  CA  LYS E  16    16912  12775  10252   1705  -3953  -1933       C  
ATOM  17168  C   LYS E  16     -16.357 180.405-220.123  1.00108.17           C  
ANISOU17168  C   LYS E  16    17317  12935  10847   1849  -3975  -2173       C  
ATOM  17169  O   LYS E  16     -15.288 179.889-220.489  1.00110.91           O  
ANISOU17169  O   LYS E  16    17780  13369  10991   2034  -3854  -2487       O  
ATOM  17170  CB  LYS E  16     -16.793 182.862-219.901  1.00100.98           C  
ANISOU17170  CB  LYS E  16    16185  12340   9842   1671  -3648  -1618       C  
ATOM  17171  CG  LYS E  16     -17.358 184.158-220.477  1.00 98.35           C  
ANISOU17171  CG  LYS E  16    15847  12178   9342   1561  -3578  -1332       C  
ATOM  17172  CD  LYS E  16     -17.063 185.340-219.557  1.00 96.08           C  
ANISOU17172  CD  LYS E  16    15438  11925   9144   1537  -3234  -1084       C  
ATOM  17173  CE  LYS E  16     -17.809 185.245-218.235  1.00 88.58           C  
ANISOU17173  CE  LYS E  16    14333  10718   8604   1515  -3256   -847       C  
ATOM  17174  NZ  LYS E  16     -19.267 185.476-218.395  1.00 89.28           N1+
ANISOU17174  NZ  LYS E  16    14363  10706   8853   1447  -3454   -521       N1+
ATOM  17175  N   SER E  17     -17.097 179.930-219.128  1.00106.41           N  
ANISOU17175  N   SER E  17    16972  12427  11032   1783  -4115  -1995       N  
ATOM  17176  CA  SER E  17     -16.719 178.741-218.383  1.00103.65           C  
ANISOU17176  CA  SER E  17    16633  11817  10930   1912  -4155  -2151       C  
ATOM  17177  C   SER E  17     -16.787 177.518-219.286  1.00103.81           C  
ANISOU17177  C   SER E  17    16945  11640  10860   1946  -4423  -2497       C  
ATOM  17178  O   SER E  17     -15.929 176.649-219.223  1.00102.32           O  
ANISOU17178  O   SER E  17    16877  11347  10652   2161  -4348  -2773       O  
ATOM  17179  CB  SER E  17     -17.642 178.558-217.178  1.00106.17           C  
ANISOU17179  CB  SER E  17    16761  11884  11696   1807  -4256  -1832       C  
ATOM  17180  OG  SER E  17     -17.805 179.774-216.462  1.00105.87           O  
ANISOU17180  OG  SER E  17    16514  12004  11708   1754  -4030  -1509       O  
ATOM  17181  N   ALA E  18     -17.816 177.460-220.125  1.00107.31           N  
ANISOU17181  N   ALA E  18    17507  12031  11235   1737  -4736  -2476       N  
ATOM  17182  CA  ALA E  18     -17.979 176.367-221.073  1.00106.65           C  
ANISOU17182  CA  ALA E  18    17755  11751  11014   1707  -5028  -2828       C  
ATOM  17183  C   ALA E  18     -16.750 176.237-221.969  1.00115.25           C  
ANISOU17183  C   ALA E  18    19088  13033  11667   1958  -4824  -3224       C  
ATOM  17184  O   ALA E  18     -16.170 175.154-222.095  1.00111.29           O  
ANISOU17184  O   ALA E  18    18825  12311  11149   2144  -4829  -3560       O  
ATOM  17185  CB  ALA E  18     -19.213 176.590-221.911  1.00108.76           C  
ANISOU17185  CB  ALA E  18    18072  12061  11190   1410  -5386  -2707       C  
ATOM  17186  N   LEU E  19     -16.356 177.352-222.579  1.00113.40           N  
ANISOU17186  N   LEU E  19    18795  13206  11085   1979  -4622  -3160       N  
ATOM  17187  CA  LEU E  19     -15.187 177.393-223.454  1.00115.69           C  
ANISOU17187  CA  LEU E  19    19264  13762  10932   2214  -4385  -3473       C  
ATOM  17188  C   LEU E  19     -13.901 177.043-222.711  1.00117.97           C  
ANISOU17188  C   LEU E  19    19450  14069  11305   2519  -4051  -3587       C  
ATOM  17189  O   LEU E  19     -13.044 176.328-223.240  1.00120.54           O  
ANISOU17189  O   LEU E  19    19987  14404  11410   2782  -3941  -3929       O  
ATOM  17190  CB  LEU E  19     -15.054 178.769-224.114  1.00110.96           C  
ANISOU17190  CB  LEU E  19    18568  13600   9991   2145  -4209  -3292       C  
ATOM  17191  CG  LEU E  19     -15.991 179.103-225.279  1.00112.48           C  
ANISOU17191  CG  LEU E  19    18922  13911   9902   1939  -4490  -3255       C  
ATOM  17192  CD1 LEU E  19     -15.846 180.564-225.675  1.00109.77           C  
ANISOU17192  CD1 LEU E  19    18435  13966   9307   1890  -4262  -2978       C  
ATOM  17193  CD2 LEU E  19     -15.721 178.194-226.470  1.00116.25           C  
ANISOU17193  CD2 LEU E  19    19801  14376   9993   2035  -4639  -3707       C  
ATOM  17194  N   THR E  20     -13.766 177.546-221.486  1.00117.70           N  
ANISOU17194  N   THR E  20    19093  14055  11572   2498  -3885  -3293       N  
ATOM  17195  CA  THR E  20     -12.565 177.273-220.697  1.00120.94           C  
ANISOU17195  CA  THR E  20    19349  14540  12064   2760  -3594  -3347       C  
ATOM  17196  C   THR E  20     -12.437 175.796-220.310  1.00124.32           C  
ANISOU17196  C   THR E  20    19929  14579  12728   2962  -3707  -3557       C  
ATOM  17197  O   THR E  20     -11.359 175.214-220.424  1.00126.18           O  
ANISOU17197  O   THR E  20    20222  14880  12839   3282  -3509  -3780       O  
ATOM  17198  CB  THR E  20     -12.499 178.147-219.433  1.00120.34           C  
ANISOU17198  CB  THR E  20    18921  14574  12231   2654  -3422  -2991       C  
ATOM  17199  OG1 THR E  20     -12.686 179.523-219.792  1.00121.20           O  
ANISOU17199  OG1 THR E  20    18941  14966  12142   2460  -3313  -2791       O  
ATOM  17200  CG2 THR E  20     -11.152 177.984-218.746  1.00119.35           C  
ANISOU17200  CG2 THR E  20    18607  14638  12104   2899  -3129  -3038       C  
ATOM  17201  N   VAL E  21     -13.536 175.195-219.856  1.00124.82           N  
ANISOU17201  N   VAL E  21    20051  14240  13137   2785  -4012  -3460       N  
ATOM  17202  CA  VAL E  21     -13.553 173.776-219.499  1.00124.99           C  
ANISOU17202  CA  VAL E  21    20256  13817  13416   2933  -4146  -3633       C  
ATOM  17203  C   VAL E  21     -13.328 172.899-220.728  1.00128.45           C  
ANISOU17203  C   VAL E  21    21138  14102  13566   3075  -4245  -4077       C  
ATOM  17204  O   VAL E  21     -12.537 171.959-220.686  1.00130.38           O  
ANISOU17204  O   VAL E  21    21550  14174  13814   3403  -4119  -4318       O  
ATOM  17205  CB  VAL E  21     -14.875 173.368-218.805  1.00122.70           C  
ANISOU17205  CB  VAL E  21    19926  13134  13561   2651  -4467  -3398       C  
ATOM  17206  CG1 VAL E  21     -14.941 171.855-218.625  1.00124.98           C  
ANISOU17206  CG1 VAL E  21    20482  12912  14094   2764  -4631  -3600       C  
ATOM  17207  CG2 VAL E  21     -15.019 174.077-217.466  1.00118.15           C  
ANISOU17207  CG2 VAL E  21    18951  12670  13270   2581  -4328  -2983       C  
ATOM  17208  N   GLN E  22     -14.024 173.216-221.819  1.00129.61           N  
ANISOU17208  N   GLN E  22    21484  14317  13445   2845  -4463  -4177       N  
ATOM  17209  CA  GLN E  22     -13.847 172.502-223.080  1.00134.97           C  
ANISOU17209  CA  GLN E  22    22624  14896  13764   2949  -4563  -4621       C  
ATOM  17210  C   GLN E  22     -12.394 172.566-223.542  1.00136.21           C  
ANISOU17210  C   GLN E  22    22829  15369  13556   3370  -4159  -4855       C  
ATOM  17211  O   GLN E  22     -11.863 171.603-224.096  1.00141.09           O  
ANISOU17211  O   GLN E  22    23809  15793  14004   3650  -4109  -5234       O  
ATOM  17212  CB  GLN E  22     -14.764 173.082-224.160  1.00136.88           C  
ANISOU17212  CB  GLN E  22    22998  15301  13710   2620  -4840  -4626       C  
ATOM  17213  CG  GLN E  22     -14.600 172.444-225.538  1.00141.61           C  
ANISOU17213  CG  GLN E  22    24103  15851  13851   2700  -4953  -5100       C  
ATOM  17214  CD  GLN E  22     -14.939 170.964-225.548  1.00146.05           C  
ANISOU17214  CD  GLN E  22    25079  15816  14597   2694  -5216  -5420       C  
ATOM  17215  OE1 GLN E  22     -14.108 170.127-225.904  1.00149.84           O  
ANISOU17215  OE1 GLN E  22    25903  16122  14906   3038  -5049  -5804       O  
ATOM  17216  NE2 GLN E  22     -16.167 170.636-225.163  1.00146.43           N  
ANISOU17216  NE2 GLN E  22    25102  15537  14996   2304  -5617  -5249       N  
ATOM  17217  N   PHE E  23     -11.753 173.705-223.306  1.00132.36           N  
ANISOU17217  N   PHE E  23    21980  15363  12948   3414  -3860  -4618       N  
ATOM  17218  CA  PHE E  23     -10.354 173.871-223.672  1.00134.43           C  
ANISOU17218  CA  PHE E  23    22193  16002  12884   3781  -3460  -4763       C  
ATOM  17219  C   PHE E  23      -9.431 173.100-222.728  1.00136.72           C  
ANISOU17219  C   PHE E  23    22347  16170  13429   4142  -3239  -4775       C  
ATOM  17220  O   PHE E  23      -8.372 172.615-223.132  1.00137.54           O  
ANISOU17220  O   PHE E  23    22550  16399  13307   4543  -2975  -5004       O  
ATOM  17221  CB  PHE E  23      -9.982 175.356-223.687  1.00129.80           C  
ANISOU17221  CB  PHE E  23    21253  15954  12110   3651  -3229  -4477       C  
ATOM  17222  CG  PHE E  23      -8.549 175.619-224.044  1.00130.62           C  
ANISOU17222  CG  PHE E  23    21237  16504  11887   3974  -2816  -4566       C  
ATOM  17223  CD1 PHE E  23      -8.080 175.348-225.320  1.00134.73           C  
ANISOU17223  CD1 PHE E  23    22059  17188  11943   4191  -2711  -4883       C  
ATOM  17224  CD2 PHE E  23      -7.671 176.143-223.108  1.00127.22           C  
ANISOU17224  CD2 PHE E  23    20384  16359  11595   4050  -2535  -4323       C  
ATOM  17225  CE1 PHE E  23      -6.761 175.588-225.655  1.00135.90           C  
ANISOU17225  CE1 PHE E  23    22060  17786  11792   4502  -2307  -4929       C  
ATOM  17226  CE2 PHE E  23      -6.350 176.386-223.438  1.00128.77           C  
ANISOU17226  CE2 PHE E  23    20416  17011  11500   4320  -2165  -4366       C  
ATOM  17227  CZ  PHE E  23      -5.895 176.107-224.714  1.00133.16           C  
ANISOU17227  CZ  PHE E  23    21245  17736  11614   4559  -2038  -4656       C  
ATOM  17228  N   VAL E  24      -9.848 172.980-221.472  1.00137.11           N  
ANISOU17228  N   VAL E  24    22163  15993  13939   4021  -3338  -4505       N  
ATOM  17229  CA  VAL E  24      -9.016 172.366-220.442  1.00139.05           C  
ANISOU17229  CA  VAL E  24    22216  16175  14441   4338  -3141  -4430       C  
ATOM  17230  C   VAL E  24      -9.224 170.858-220.314  1.00146.46           C  
ANISOU17230  C   VAL E  24    23500  16530  15617   4545  -3289  -4649       C  
ATOM  17231  O   VAL E  24      -8.261 170.093-220.347  1.00151.26           O  
ANISOU17231  O   VAL E  24    24198  17103  16171   4987  -3066  -4822       O  
ATOM  17232  CB  VAL E  24      -9.237 173.034-219.070  1.00132.99           C  
ANISOU17232  CB  VAL E  24    21015  15503  14013   4130  -3133  -4010       C  
ATOM  17233  CG1 VAL E  24      -8.673 172.169-217.955  1.00134.08           C  
ANISOU17233  CG1 VAL E  24    21011  15467  14467   4418  -3037  -3920       C  
ATOM  17234  CG2 VAL E  24      -8.608 174.419-219.051  1.00129.08           C  
ANISOU17234  CG2 VAL E  24    20179  15587  13280   4027  -2883  -3820       C  
ATOM  17235  N   GLN E  25     -10.476 170.433-220.171  1.00148.16           N  
ANISOU17235  N   GLN E  25    23906  16286  16104   4230  -3656  -4622       N  
ATOM  17236  CA  GLN E  25     -10.778 169.020-219.950  1.00150.75           C  
ANISOU17236  CA  GLN E  25    24571  15995  16714   4350  -3823  -4790       C  
ATOM  17237  C   GLN E  25     -11.300 168.322-221.204  1.00152.14           C  
ANISOU17237  C   GLN E  25    25319  15828  16661   4271  -4062  -5213       C  
ATOM  17238  O   GLN E  25     -11.290 167.094-221.287  1.00156.85           O  
ANISOU17238  O   GLN E  25    26309  15907  17382   4446  -4135  -5464       O  
ATOM  17239  CB  GLN E  25     -11.785 168.860-218.810  1.00150.10           C  
ANISOU17239  CB  GLN E  25    24306  15589  17135   4045  -4070  -4449       C  
ATOM  17240  CG  GLN E  25     -11.599 169.855-217.681  1.00146.41           C  
ANISOU17240  CG  GLN E  25    23297  15509  16822   3972  -3907  -4020       C  
ATOM  17241  CD  GLN E  25     -12.490 169.563-216.491  1.00146.23           C  
ANISOU17241  CD  GLN E  25    23114  15163  17284   3755  -4097  -3686       C  
ATOM  17242  OE1 GLN E  25     -13.140 168.520-216.430  1.00149.87           O  
ANISOU17242  OE1 GLN E  25    23840  15095  18010   3686  -4332  -3754       O  
ATOM  17243  NE2 GLN E  25     -12.524 170.487-215.535  1.00142.29           N  
ANISOU17243  NE2 GLN E  25    22195  14974  16894   3637  -3989  -3323       N  
ATOM  17244  N   GLY E  26     -11.761 169.105-222.174  1.00148.53           N  
ANISOU17244  N   GLY E  26    24929  15649  15858   4000  -4188  -5288       N  
ATOM  17245  CA  GLY E  26     -12.300 168.555-223.405  1.00151.40           C  
ANISOU17245  CA  GLY E  26    25827  15761  15937   3869  -4450  -5683       C  
ATOM  17246  C   GLY E  26     -13.728 168.064-223.254  1.00151.06           C  
ANISOU17246  C   GLY E  26    25942  15245  16208   3397  -4935  -5622       C  
ATOM  17247  O   GLY E  26     -14.274 167.428-224.156  1.00154.28           O  
ANISOU17247  O   GLY E  26    26826  15355  16440   3227  -5222  -5957       O  
ATOM  17248  N   ILE E  27     -14.336 168.368-222.111  1.00147.88           N  
ANISOU17248  N   ILE E  27    25136  14795  16256   3172  -5027  -5186       N  
ATOM  17249  CA  ILE E  27     -15.683 167.898-221.809  1.00148.63           C  
ANISOU17249  CA  ILE E  27    25290  14470  16711   2728  -5460  -5044       C  
ATOM  17250  C   ILE E  27     -16.698 169.044-221.772  1.00143.75           C  
ANISOU17250  C   ILE E  27    24306  14196  16118   2306  -5655  -4667       C  
ATOM  17251  O   ILE E  27     -16.413 170.129-221.259  1.00139.32           O  
ANISOU17251  O   ILE E  27    23322  14061  15551   2366  -5413  -4356       O  
ATOM  17252  CB  ILE E  27     -15.714 167.105-220.474  1.00146.88           C  
ANISOU17252  CB  ILE E  27    24941  13826  17041   2815  -5431  -4821       C  
ATOM  17253  CG1 ILE E  27     -17.117 166.569-220.181  1.00149.49           C  
ANISOU17253  CG1 ILE E  27    25322  13721  17756   2333  -5875  -4651       C  
ATOM  17254  CG2 ILE E  27     -15.221 167.959-219.319  1.00139.64           C  
ANISOU17254  CG2 ILE E  27    23467  13291  16297   2971  -5123  -4403       C  
ATOM  17255  CD1 ILE E  27     -17.225 165.855-218.850  1.00149.01           C  
ANISOU17255  CD1 ILE E  27    25111  13270  18237   2390  -5844  -4372       C  
ATOM  17256  N   PHE E  28     -17.876 168.802-222.339  1.00142.93           N  
ANISOU17256  N   PHE E  28    24375  13906  16028   1879  -6092  -4693       N  
ATOM  17257  CA  PHE E  28     -18.970 169.760-222.255  1.00136.37           C  
ANISOU17257  CA  PHE E  28    23182  13355  15276   1492  -6304  -4286       C  
ATOM  17258  C   PHE E  28     -20.156 169.148-221.518  1.00137.32           C  
ANISOU17258  C   PHE E  28    23189  13081  15906   1129  -6647  -4010       C  
ATOM  17259  O   PHE E  28     -20.713 168.139-221.950  1.00141.48           O  
ANISOU17259  O   PHE E  28    24066  13191  16499    887  -6997  -4236       O  
ATOM  17260  CB  PHE E  28     -19.395 170.235-223.649  1.00135.60           C  
ANISOU17260  CB  PHE E  28    23279  13545  14699   1277  -6532  -4460       C  
ATOM  17261  CG  PHE E  28     -20.580 171.166-223.637  1.00130.87           C  
ANISOU17261  CG  PHE E  28    22314  13231  14181    901  -6769  -4018       C  
ATOM  17262  CD1 PHE E  28     -20.410 172.523-223.422  1.00124.69           C  
ANISOU17262  CD1 PHE E  28    21149  12924  13302    997  -6498  -3684       C  
ATOM  17263  CD2 PHE E  28     -21.862 170.681-223.839  1.00131.13           C  
ANISOU17263  CD2 PHE E  28    22385  13050  14390    453  -7258  -3919       C  
ATOM  17264  CE1 PHE E  28     -21.496 173.375-223.405  1.00121.91           C  
ANISOU17264  CE1 PHE E  28    20476  12812  13032    710  -6681  -3258       C  
ATOM  17265  CE2 PHE E  28     -22.951 171.529-223.822  1.00129.70           C  
ANISOU17265  CE2 PHE E  28    21826  13165  14290    149  -7459  -3469       C  
ATOM  17266  CZ  PHE E  28     -22.767 172.876-223.608  1.00125.09           C  
ANISOU17266  CZ  PHE E  28    20880  13039  13610    307  -7157  -3138       C  
ATOM  17267  N   VAL E  29     -20.534 169.763-220.403  1.00134.41           N  
ANISOU17267  N   VAL E  29    22342  12843  15886   1082  -6537  -3521       N  
ATOM  17268  CA  VAL E  29     -21.698 169.325-219.645  1.00136.74           C  
ANISOU17268  CA  VAL E  29    22444  12847  16664    745  -6821  -3173       C  
ATOM  17269  C   VAL E  29     -22.700 170.460-219.484  1.00133.06           C  
ANISOU17269  C   VAL E  29    21533  12764  16258    490  -6909  -2694       C  
ATOM  17270  O   VAL E  29     -22.425 171.450-218.803  1.00125.48           O  
ANISOU17270  O   VAL E  29    20232  12118  15329    671  -6590  -2401       O  
ATOM  17271  CB  VAL E  29     -21.312 168.804-218.246  1.00137.19           C  
ANISOU17271  CB  VAL E  29    22342  12628  17155    958  -6595  -2977       C  
ATOM  17272  CG1 VAL E  29     -22.562 168.428-217.456  1.00138.68           C  
ANISOU17272  CG1 VAL E  29    22292  12563  17835    601  -6865  -2562       C  
ATOM  17273  CG2 VAL E  29     -20.369 167.618-218.357  1.00140.66           C  
ANISOU17273  CG2 VAL E  29    23214  12651  17578   1248  -6501  -3401       C  
ATOM  17274  N   GLU E  30     -23.860 170.308-220.117  1.00139.29           N  
ANISOU17274  N   GLU E  30    22339  13527  17058     71  -7344  -2612       N  
ATOM  17275  CA  GLU E  30     -24.934 171.285-219.997  1.00142.17           C  
ANISOU17275  CA  GLU E  30    22268  14242  17510   -165  -7457  -2114       C  
ATOM  17276  C   GLU E  30     -25.409 171.384-218.551  1.00145.89           C  
ANISOU17276  C   GLU E  30    22322  14624  18487   -158  -7317  -1619       C  
ATOM  17277  O   GLU E  30     -26.289 170.636-218.123  1.00148.90           O  
ANISOU17277  O   GLU E  30    22612  14719  19244   -446  -7592  -1415       O  
ATOM  17278  CB  GLU E  30     -26.090 170.924-220.919  1.00145.62           C  
ANISOU17278  CB  GLU E  30    22783  14660  17884   -636  -7995  -2110       C  
ATOM  17279  N   LYS E  31     -24.809 172.308-217.806  1.00147.38           N  
ANISOU17279  N   LYS E  31    22272  15062  18665    157  -6885  -1429       N  
ATOM  17280  CA  LYS E  31     -25.169 172.551-216.412  1.00149.54           C  
ANISOU17280  CA  LYS E  31    22169  15308  19340    213  -6692   -970       C  
ATOM  17281  C   LYS E  31     -25.388 174.044-216.167  1.00148.26           C  
ANISOU17281  C   LYS E  31    21678  15584  19071    316  -6432   -612       C  
ATOM  17282  O   LYS E  31     -25.340 174.846-217.099  1.00149.89           O  
ANISOU17282  O   LYS E  31    21932  16094  18926    315  -6433   -685       O  
ATOM  17283  CB  LYS E  31     -24.087 172.010-215.475  1.00148.03           C  
ANISOU17283  CB  LYS E  31    22071  14893  19281    527  -6389  -1119       C  
ATOM  17284  CG  LYS E  31     -22.723 172.647-215.677  1.00145.19           C  
ANISOU17284  CG  LYS E  31    21826  14788  18551    882  -6022  -1400       C  
ATOM  17285  CD  LYS E  31     -21.648 171.926-214.887  1.00144.68           C  
ANISOU17285  CD  LYS E  31    21862  14509  18602   1181  -5789  -1566       C  
ATOM  17286  CE  LYS E  31     -20.314 172.645-214.997  1.00142.84           C  
ANISOU17286  CE  LYS E  31    21652  14603  18018   1506  -5418  -1772       C  
ATOM  17287  NZ  LYS E  31     -19.241 171.946-214.236  1.00143.12           N1+
ANISOU17287  NZ  LYS E  31    21737  14489  18151   1817  -5199  -1898       N1+
ATOM  17288  N   TYR E  32     -25.630 174.418-214.915  1.00145.66           N  
ANISOU17288  N   TYR E  32    21042  15271  19031    413  -6197   -223       N  
ATOM  17289  CA  TYR E  32     -25.904 175.812-214.587  1.00143.53           C  
ANISOU17289  CA  TYR E  32    20500  15347  18687    520  -5929    128       C  
ATOM  17290  C   TYR E  32     -25.239 176.222-213.281  1.00143.85           C  
ANISOU17290  C   TYR E  32    20428  15398  18831    788  -5508    247       C  
ATOM  17291  O   TYR E  32     -25.844 176.149-212.211  1.00145.53           O  
ANISOU17291  O   TYR E  32    20400  15530  19365    782  -5438    611       O  
ATOM  17292  CB  TYR E  32     -27.413 176.060-214.522  1.00142.74           C  
ANISOU17292  CB  TYR E  32    20072  15336  18826    285  -6143    624       C  
ATOM  17293  CG  TYR E  32     -28.126 175.731-215.811  1.00144.02           C  
ANISOU17293  CG  TYR E  32    20310  15554  18858    -22  -6596    543       C  
ATOM  17294  CD1 TYR E  32     -28.018 176.564-216.914  1.00144.05           C  
ANISOU17294  CD1 TYR E  32    20403  15868  18462     -4  -6615    441       C  
ATOM  17295  CD2 TYR E  32     -28.898 174.584-215.929  1.00145.92           C  
ANISOU17295  CD2 TYR E  32    20543  15540  19360   -353  -7014    574       C  
ATOM  17296  CE1 TYR E  32     -28.658 176.268-218.096  1.00147.65           C  
ANISOU17296  CE1 TYR E  32    20933  16413  18753   -291  -7046    367       C  
ATOM  17297  CE2 TYR E  32     -29.543 174.279-217.109  1.00150.29           C  
ANISOU17297  CE2 TYR E  32    21180  16161  19761   -678  -7460    482       C  
ATOM  17298  CZ  TYR E  32     -29.419 175.126-218.190  1.00152.03           C  
ANISOU17298  CZ  TYR E  32    21483  16727  19554   -638  -7479    376       C  
ATOM  17299  OH  TYR E  32     -30.059 174.833-219.372  1.00158.96           O  
ANISOU17299  OH  TYR E  32    22448  17713  20236   -967  -7942    288       O  
ATOM  17300  N   ASP E  33     -23.984 176.644-213.377  1.00142.44           N  
ANISOU17300  N   ASP E  33    20418  15343  18360   1012  -5235    -56       N  
ATOM  17301  CA  ASP E  33     -23.232 177.083-212.210  1.00136.83           C  
ANISOU17301  CA  ASP E  33    19620  14689  17679   1236  -4857     15       C  
ATOM  17302  C   ASP E  33     -22.608 178.442-212.480  1.00124.35           C  
ANISOU17302  C   ASP E  33    18066  13426  15756   1351  -4557    -33       C  
ATOM  17303  O   ASP E  33     -21.657 178.549-213.256  1.00124.30           O  
ANISOU17303  O   ASP E  33    18250  13539  15439   1422  -4503   -375       O  
ATOM  17304  CB  ASP E  33     -22.133 176.078-211.870  1.00144.10           C  
ANISOU17304  CB  ASP E  33    20704  15428  18620   1392  -4813   -304       C  
ATOM  17305  CG  ASP E  33     -22.624 174.643-211.889  1.00153.12           C  
ANISOU17305  CG  ASP E  33    21930  16193  20057   1267  -5132   -346       C  
ATOM  17306  OD1 ASP E  33     -23.779 174.394-211.482  1.00155.47           O  
ANISOU17306  OD1 ASP E  33    22046  16360  20665   1079  -5303     -3       O  
ATOM  17307  OD2 ASP E  33     -21.850 173.761-212.312  1.00157.56           O1-
ANISOU17307  OD2 ASP E  33    22744  16579  20541   1361  -5200   -712       O1-
ATOM  17308  N   PRO E  34     -23.152 179.492-211.854  1.00113.45           N  
ANISOU17308  N   PRO E  34    16506  12171  14428   1373  -4347    322       N  
ATOM  17309  CA  PRO E  34     -22.554 180.820-211.987  1.00104.45           C  
ANISOU17309  CA  PRO E  34    15424  11273  12991   1464  -4035    296       C  
ATOM  17310  C   PRO E  34     -21.102 180.840-211.512  1.00 99.34           C  
ANISOU17310  C   PRO E  34    14878  10694  12173   1600  -3790      8       C  
ATOM  17311  O   PRO E  34     -20.807 180.535-210.356  1.00 93.90           O  
ANISOU17311  O   PRO E  34    14109   9930  11638   1680  -3667     69       O  
ATOM  17312  CB  PRO E  34     -23.433 181.687-211.082  1.00101.71           C  
ANISOU17312  CB  PRO E  34    14891  10943  12811   1496  -3836    736       C  
ATOM  17313  CG  PRO E  34     -24.745 180.996-211.071  1.00106.90           C  
ANISOU17313  CG  PRO E  34    15361  11472  13785   1378  -4124   1028       C  
ATOM  17314  CD  PRO E  34     -24.415 179.530-211.099  1.00112.29           C  
ANISOU17314  CD  PRO E  34    16112  11945  14610   1309  -4387    778       C  
ATOM  17315  N   THR E  35     -20.204 181.177-212.429  1.00100.22           N  
ANISOU17315  N   THR E  35    15144  10979  11955   1622  -3729   -284       N  
ATOM  17316  CA  THR E  35     -18.805 181.401-212.106  1.00 98.00           C  
ANISOU17316  CA  THR E  35    14914  10850  11471   1729  -3481   -516       C  
ATOM  17317  C   THR E  35     -18.666 182.695-211.326  1.00100.18           C  
ANISOU17317  C   THR E  35    15141  11251  11674   1716  -3162   -324       C  
ATOM  17318  O   THR E  35     -19.240 183.720-211.699  1.00102.97           O  
ANISOU17318  O   THR E  35    15523  11657  11942   1653  -3076   -145       O  
ATOM  17319  CB  THR E  35     -17.959 181.558-213.373  1.00 94.32           C  
ANISOU17319  CB  THR E  35    14605  10580  10652   1744  -3472   -827       C  
ATOM  17320  OG1 THR E  35     -18.111 180.403-214.204  1.00100.41           O  
ANISOU17320  OG1 THR E  35    15493  11218  11441   1757  -3762  -1046       O  
ATOM  17321  CG2 THR E  35     -16.497 181.746-213.014  1.00 88.21           C  
ANISOU17321  CG2 THR E  35    13822  10006   9686   1844  -3219  -1029       C  
ATOM  17322  N   ILE E  36     -17.904 182.645-210.241  1.00 97.99           N  
ANISOU17322  N   ILE E  36    14804  11011  11415   1777  -2988   -358       N  
ATOM  17323  CA  ILE E  36     -17.572 183.837-209.479  1.00 93.64           C  
ANISOU17323  CA  ILE E  36    14262  10576  10740   1736  -2685   -252       C  
ATOM  17324  C   ILE E  36     -16.110 184.189-209.705  1.00104.99           C  
ANISOU17324  C   ILE E  36    15743  12269  11878   1714  -2528   -520       C  
ATOM  17325  O   ILE E  36     -15.775 185.329-210.024  1.00108.24           O  
ANISOU17325  O   ILE E  36    16246  12813  12067   1610  -2337   -527       O  
ATOM  17326  CB  ILE E  36     -17.807 183.621-207.986  1.00 83.66           C  
ANISOU17326  CB  ILE E  36    12896   9214   9678   1784  -2604    -68       C  
ATOM  17327  CG1 ILE E  36     -19.298 183.449-207.709  1.00 84.10           C  
ANISOU17327  CG1 ILE E  36    12873   9056  10025   1798  -2706    261       C  
ATOM  17328  CG2 ILE E  36     -17.248 184.783-207.189  1.00 77.68           C  
ANISOU17328  CG2 ILE E  36    12201   8583   8730   1720  -2299    -45       C  
ATOM  17329  CD1 ILE E  36     -19.632 183.480-206.248  1.00 77.21           C  
ANISOU17329  CD1 ILE E  36    11919   8112   9307   1855  -2561    490       C  
ATOM  17330  N   GLU E  37     -15.241 183.199-209.536  1.00114.26           N  
ANISOU17330  N   GLU E  37    16843  13512  13058   1818  -2601   -716       N  
ATOM  17331  CA  GLU E  37     -13.822 183.353-209.831  1.00122.37           C  
ANISOU17331  CA  GLU E  37    17849  14830  13815   1826  -2474   -952       C  
ATOM  17332  C   GLU E  37     -13.177 181.984-209.974  1.00122.49           C  
ANISOU17332  C   GLU E  37    17798  14853  13890   2024  -2612  -1145       C  
ATOM  17333  O   GLU E  37     -13.054 181.239-209.001  1.00122.64           O  
ANISOU17333  O   GLU E  37    17710  14799  14089   2129  -2651  -1086       O  
ATOM  17334  CB  GLU E  37     -13.116 184.159-208.738  1.00130.40           C  
ANISOU17334  CB  GLU E  37    18800  16024  14721   1721  -2248   -895       C  
ATOM  17335  CG  GLU E  37     -11.608 184.292-208.936  1.00139.12           C  
ANISOU17335  CG  GLU E  37    19813  17484  15561   1699  -2130  -1096       C  
ATOM  17336  CD  GLU E  37     -10.805 183.477-207.931  1.00144.76           C  
ANISOU17336  CD  GLU E  37    20334  18334  16334   1819  -2150  -1122       C  
ATOM  17337  OE1 GLU E  37     -11.411 182.660-207.203  1.00146.47           O  
ANISOU17337  OE1 GLU E  37    20513  18335  16802   1945  -2271  -1009       O  
ATOM  17338  OE2 GLU E  37      -9.568 183.659-207.863  1.00146.17           O1-
ANISOU17338  OE2 GLU E  37    20378  18855  16305   1785  -2045  -1226       O1-
ATOM  17339  N   ASP E  38     -12.776 181.652-211.195  1.00123.22           N  
ANISOU17339  N   ASP E  38    17973  15024  13819   2095  -2671  -1366       N  
ATOM  17340  CA  ASP E  38     -12.138 180.370-211.461  1.00124.22           C  
ANISOU17340  CA  ASP E  38    18093  15129  13975   2325  -2767  -1576       C  
ATOM  17341  C   ASP E  38     -10.846 180.550-212.245  1.00119.71           C  
ANISOU17341  C   ASP E  38    17499  14907  13080   2413  -2609  -1798       C  
ATOM  17342  O   ASP E  38     -10.830 181.173-213.308  1.00114.50           O  
ANISOU17342  O   ASP E  38    16946  14372  12185   2331  -2564  -1881       O  
ATOM  17343  CB  ASP E  38     -13.093 179.432-212.197  1.00131.32           C  
ANISOU17343  CB  ASP E  38    19165  15696  15034   2372  -3037  -1647       C  
ATOM  17344  CG  ASP E  38     -14.209 178.918-211.303  1.00135.21           C  
ANISOU17344  CG  ASP E  38    19619  15857  15897   2324  -3201  -1414       C  
ATOM  17345  OD1 ASP E  38     -13.981 178.783-210.080  1.00135.37           O  
ANISOU17345  OD1 ASP E  38    19492  15879  16064   2374  -3117  -1267       O  
ATOM  17346  OD2 ASP E  38     -15.312 178.647-211.825  1.00137.49           O1-
ANISOU17346  OD2 ASP E  38    20011  15911  16317   2225  -3419  -1360       O1-
ATOM  17347  N   SER E  39      -9.763 180.001-211.704  1.00121.62           N  
ANISOU17347  N   SER E  39    17576  15329  13304   2593  -2517  -1862       N  
ATOM  17348  CA  SER E  39      -8.444 180.154-212.299  1.00125.49           C  
ANISOU17348  CA  SER E  39    17968  16213  13500   2698  -2337  -2023       C  
ATOM  17349  C   SER E  39      -7.922 178.833-212.857  1.00130.35           C  
ANISOU17349  C   SER E  39    18639  16769  14117   3054  -2383  -2240       C  
ATOM  17350  O   SER E  39      -7.573 177.919-212.107  1.00132.89           O  
ANISOU17350  O   SER E  39    18857  17019  14617   3273  -2407  -2213       O  
ATOM  17351  CB  SER E  39      -7.460 180.719-211.272  1.00124.40           C  
ANISOU17351  CB  SER E  39    17551  16429  13286   2616  -2163  -1900       C  
ATOM  17352  OG  SER E  39      -7.922 181.953-210.753  1.00121.12           O  
ANISOU17352  OG  SER E  39    17151  16021  12847   2288  -2101  -1733       O  
ATOM  17353  N   TYR E  40      -7.880 178.749-214.182  1.00130.32           N  
ANISOU17353  N   TYR E  40    18825  16790  13901   3125  -2382  -2450       N  
ATOM  17354  CA  TYR E  40      -7.378 177.579-214.890  1.00131.86           C  
ANISOU17354  CA  TYR E  40    19150  16916  14034   3477  -2390  -2703       C  
ATOM  17355  C   TYR E  40      -5.981 177.844-215.431  1.00135.50           C  
ANISOU17355  C   TYR E  40    19446  17870  14167   3650  -2117  -2802       C  
ATOM  17356  O   TYR E  40      -5.568 178.992-215.567  1.00135.58           O  
ANISOU17356  O   TYR E  40    19304  18241  13968   3430  -1962  -2705       O  
ATOM  17357  CB  TYR E  40      -8.309 177.217-216.049  1.00130.07           C  
ANISOU17357  CB  TYR E  40    19286  16382  13752   3447  -2587  -2896       C  
ATOM  17358  CG  TYR E  40      -9.681 176.768-215.613  1.00127.29           C  
ANISOU17358  CG  TYR E  40    19076  15552  13738   3290  -2878  -2795       C  
ATOM  17359  CD1 TYR E  40     -10.658 177.691-215.282  1.00124.69           C  
ANISOU17359  CD1 TYR E  40    18696  15174  13508   2966  -2963  -2556       C  
ATOM  17360  CD2 TYR E  40     -10.002 175.419-215.533  1.00128.80           C  
ANISOU17360  CD2 TYR E  40    19451  15332  14155   3471  -3054  -2920       C  
ATOM  17361  CE1 TYR E  40     -11.913 177.290-214.882  1.00124.53           C  
ANISOU17361  CE1 TYR E  40    18752  14766  13799   2829  -3214  -2423       C  
ATOM  17362  CE2 TYR E  40     -11.258 175.008-215.135  1.00128.42           C  
ANISOU17362  CE2 TYR E  40    19500  14866  14426   3289  -3324  -2796       C  
ATOM  17363  CZ  TYR E  40     -12.208 175.948-214.808  1.00126.26           C  
ANISOU17363  CZ  TYR E  40    19121  14609  14242   2970  -3403  -2537       C  
ATOM  17364  OH  TYR E  40     -13.461 175.548-214.408  1.00126.65           O  
ANISOU17364  OH  TYR E  40    19218  14292  14613   2796  -3656  -2373       O  
ATOM  17365  N   ARG E  41      -5.259 176.770-215.732  1.00139.43           N  
ANISOU17365  N   ARG E  41    19977  18372  14628   4051  -2046  -2979       N  
ATOM  17366  CA  ARG E  41      -3.944 176.868-216.353  1.00143.14           C  
ANISOU17366  CA  ARG E  41    20285  19318  14783   4287  -1769  -3071       C  
ATOM  17367  C   ARG E  41      -3.547 175.547-217.007  1.00145.40           C  
ANISOU17367  C   ARG E  41    20787  19436  15024   4772  -1724  -3335       C  
ATOM  17368  O   ARG E  41      -3.857 174.471-216.494  1.00144.78           O  
ANISOU17368  O   ARG E  41    20834  18954  15222   4980  -1852  -3371       O  
ATOM  17369  CB  ARG E  41      -2.883 177.309-215.339  1.00145.07           C  
ANISOU17369  CB  ARG E  41    20065  20020  15035   4272  -1593  -2836       C  
ATOM  17370  CG  ARG E  41      -2.636 176.329-214.207  1.00147.19           C  
ANISOU17370  CG  ARG E  41    20180  20156  15591   4532  -1645  -2729       C  
ATOM  17371  CD  ARG E  41      -1.442 176.766-213.374  1.00150.02           C  
ANISOU17371  CD  ARG E  41    20052  21075  15874   4528  -1472  -2507       C  
ATOM  17372  NE  ARG E  41      -1.641 178.086-212.781  1.00150.10           N  
ANISOU17372  NE  ARG E  41    19909  21281  15842   4024  -1495  -2324       N  
ATOM  17373  CZ  ARG E  41      -0.701 178.760-212.124  1.00153.27           C  
ANISOU17373  CZ  ARG E  41    19919  22190  16127   3860  -1377  -2141       C  
ATOM  17374  NH1 ARG E  41      -0.972 179.956-211.614  1.00151.27           N1+
ANISOU17374  NH1 ARG E  41    19619  22025  15832   3382  -1402  -2014       N1+
ATOM  17375  NH2 ARG E  41       0.511 178.240-211.979  1.00157.29           N  
ANISOU17375  NH2 ARG E  41    20088  23119  16555   4174  -1232  -2080       N  
ATOM  17376  N   LYS E  42      -2.864 175.635-218.142  1.00148.40           N  
ANISOU17376  N   LYS E  42    21232  20108  15046   4960  -1523  -3516       N  
ATOM  17377  CA  LYS E  42      -2.521 174.438-218.901  1.00154.07           C  
ANISOU17377  CA  LYS E  42    22233  20643  15662   5438  -1449  -3810       C  
ATOM  17378  C   LYS E  42      -1.321 174.654-219.813  1.00158.44           C  
ANISOU17378  C   LYS E  42    22662  21730  15807   5721  -1104  -3901       C  
ATOM  17379  O   LYS E  42      -1.160 175.721-220.407  1.00158.07           O  
ANISOU17379  O   LYS E  42    22514  22062  15482   5468  -1000  -3844       O  
ATOM  17380  CB  LYS E  42      -3.724 173.964-219.712  1.00154.42           C  
ANISOU17380  CB  LYS E  42    22813  20155  15705   5337  -1718  -4076       C  
ATOM  17381  N   GLN E  43      -0.479 173.630-219.918  1.00161.52           N  
ANISOU17381  N   GLN E  43    23058  22146  16168   6264   -909  -4020       N  
ATOM  17382  CA  GLN E  43       0.669 173.671-220.812  1.00163.68           C  
ANISOU17382  CA  GLN E  43    23222  22916  16054   6621   -549  -4108       C  
ATOM  17383  C   GLN E  43       0.239 173.241-222.208  1.00165.52           C  
ANISOU17383  C   GLN E  43    24018  22892  15982   6777   -557  -4499       C  
ATOM  17384  O   GLN E  43      -0.335 172.166-222.387  1.00167.24           O  
ANISOU17384  O   GLN E  43    24693  22534  16318   6983   -712  -4765       O  
ATOM  17385  CB  GLN E  43       1.785 172.777-220.293  1.00166.68           C  
ANISOU17385  CB  GLN E  43    23336  23467  16526   7188   -304  -4030       C  
ATOM  17386  N   VAL E  44       0.512 174.088-223.193  1.00165.43           N  
ANISOU17386  N   VAL E  44    23987  23303  15566   6655   -396  -4529       N  
ATOM  17387  CA  VAL E  44       0.101 173.809-224.560  1.00168.50           C  
ANISOU17387  CA  VAL E  44    24905  23522  15594   6760   -411  -4887       C  
ATOM  17388  C   VAL E  44       1.162 174.262-225.560  1.00172.80           C  
ANISOU17388  C   VAL E  44    25309  24698  15649   7002    -10  -4906       C  
ATOM  17389  O   VAL E  44       1.764 175.325-225.403  1.00171.53           O  
ANISOU17389  O   VAL E  44    24681  25096  15396   6778    164  -4604       O  
ATOM  17390  CB  VAL E  44      -1.263 174.467-224.882  1.00164.12           C  
ANISOU17390  CB  VAL E  44    24628  22688  15043   6201   -777  -4913       C  
ATOM  17391  CG1 VAL E  44      -1.200 175.975-224.677  1.00159.08           C  
ANISOU17391  CG1 VAL E  44    23588  22506  14350   5741   -729  -4568       C  
ATOM  17392  CG2 VAL E  44      -1.712 174.120-226.297  1.00167.14           C  
ANISOU17392  CG2 VAL E  44    25571  22913  15022   6294   -836  -5290       C  
ATOM  17393  N   GLU E  45       1.395 173.436-226.578  1.00176.73           N  
ANISOU17393  N   GLU E  45    26229  25093  15830   7456    146  -5260       N  
ATOM  17394  CA  GLU E  45       2.357 173.745-227.630  1.00179.92           C  
ANISOU17394  CA  GLU E  45    26559  26076  15726   7750    552  -5306       C  
ATOM  17395  C   GLU E  45       1.756 174.707-228.651  1.00178.00           C  
ANISOU17395  C   GLU E  45    26523  25997  15110   7342    456  -5347       C  
ATOM  17396  O   GLU E  45       0.872 174.336-229.423  1.00179.80           O  
ANISOU17396  O   GLU E  45    27321  25836  15160   7283    225  -5670       O  
ATOM  17397  CB  GLU E  45       2.825 172.460-228.324  1.00185.45           C  
ANISOU17397  CB  GLU E  45    27684  26578  16201   8440    783  -5688       C  
ATOM  17398  CG  GLU E  45       3.888 172.659-229.404  1.00189.65           C  
ANISOU17398  CG  GLU E  45    28143  27727  16189   8844   1262  -5737       C  
ATOM  17399  CD  GLU E  45       4.246 171.361-230.115  1.00195.50           C  
ANISOU17399  CD  GLU E  45    29376  28177  16728   9503   1483  -6123       C  
ATOM  17400  OE1 GLU E  45       3.684 170.310-229.743  1.00195.59           O  
ANISOU17400  OE1 GLU E  45    29782  27484  17048   9613   1254  -6342       O  
ATOM  17401  OE2 GLU E  45       5.084 171.386-231.044  1.00200.08           O1-
ANISOU17401  OE2 GLU E  45    29893  29164  16965   9772   1860  -6099       O1-
ATOM  17402  N   VAL E  46       2.236 175.946-228.641  1.00176.40           N  
ANISOU17402  N   VAL E  46    25858  26374  14792   7043    622  -5003       N  
ATOM  17403  CA  VAL E  46       1.800 176.957-229.597  1.00177.03           C  
ANISOU17403  CA  VAL E  46    26076  26678  14510   6683    588  -4966       C  
ATOM  17404  C   VAL E  46       2.912 177.275-230.594  1.00184.50           C  
ANISOU17404  C   VAL E  46    26875  28282  14944   6983   1054  -4934       C  
ATOM  17405  O   VAL E  46       4.027 177.629-230.202  1.00185.56           O  
ANISOU17405  O   VAL E  46    26462  28939  15103   7090   1378  -4650       O  
ATOM  17406  CB  VAL E  46       1.359 178.260-228.896  1.00170.13           C  
ANISOU17406  CB  VAL E  46    24856  25903  13884   6047    416  -4578       C  
ATOM  17407  CG1 VAL E  46       0.961 179.304-229.928  1.00169.30           C  
ANISOU17407  CG1 VAL E  46    24897  26033  13396   5726    418  -4504       C  
ATOM  17408  CG2 VAL E  46       0.210 177.989-227.936  1.00165.11           C  
ANISOU17408  CG2 VAL E  46    24358  24646  13729   5762    -21  -4586       C  
ATOM  17409  N   ASP E  47       2.590 177.145-231.879  1.00189.95           N  
ANISOU17409  N   ASP E  47    28047  28967  15158   7103   1077  -5212       N  
ATOM  17410  CA  ASP E  47       3.545 177.368-232.961  1.00196.29           C  
ANISOU17410  CA  ASP E  47    28796  30373  15410   7425   1526  -5216       C  
ATOM  17411  C   ASP E  47       4.821 176.565-232.749  1.00200.58           C  
ANISOU17411  C   ASP E  47    29075  31191  15945   8063   1948  -5237       C  
ATOM  17412  O   ASP E  47       5.919 177.123-232.726  1.00202.75           O  
ANISOU17412  O   ASP E  47    28806  32120  16108   8151   2330  -4920       O  
ATOM  17413  CB  ASP E  47       3.871 178.856-233.105  1.00194.76           C  
ANISOU17413  CB  ASP E  47    28160  30751  15089   6982   1676  -4780       C  
ATOM  17414  CG  ASP E  47       2.699 179.662-233.631  1.00192.83           C  
ANISOU17414  CG  ASP E  47    28231  30316  14720   6470   1349  -4755       C  
ATOM  17415  OD1 ASP E  47       1.874 179.101-234.383  1.00193.78           O1+
ANISOU17415  OD1 ASP E  47    28917  30071  14642   6529   1117  -5089       O1+
ATOM  17416  OD2 ASP E  47       2.608 180.860-233.294  1.00190.37           O1-
ANISOU17416  OD2 ASP E  47    27593  30202  14538   5984   1321  -4376       O1-
ATOM  17417  N   ALA E  48       4.656 175.256-232.576  1.00202.78           N  
ANISOU17417  N   ALA E  48    29700  30922  16427   8437   1856  -5545       N  
ATOM  17418  CA  ALA E  48       5.770 174.344-232.340  1.00207.13           C  
ANISOU17418  CA  ALA E  48    30042  31599  17059   9066   2223  -5544       C  
ATOM  17419  C   ALA E  48       6.610 174.761-231.135  1.00204.66           C  
ANISOU17419  C   ALA E  48    28986  31758  17019   9105   2391  -5152       C  
ATOM  17420  O   ALA E  48       7.794 174.434-231.055  1.00211.24           O  
ANISOU17420  O   ALA E  48    29433  33044  17784   9606   2806  -5010       O  
ATOM  17421  CB  ALA E  48       6.642 174.219-233.588  1.00212.77           C  
ANISOU17421  CB  ALA E  48    30782  32691  17370   9388   2644  -5547       C  
ATOM  17422  N   GLN E  49       5.996 175.487-230.204  1.00194.94           N  
ANISOU17422  N   GLN E  49    27505  30379  16184   8483   2039  -4900       N  
ATOM  17423  CA  GLN E  49       6.695 175.952-229.012  1.00191.32           C  
ANISOU17423  CA  GLN E  49    26328  30280  16086   8314   2097  -4467       C  
ATOM  17424  C   GLN E  49       5.825 175.780-227.767  1.00186.56           C  
ANISOU17424  C   GLN E  49    25751  29105  16028   7973   1655  -4426       C  
ATOM  17425  O   GLN E  49       4.831 176.483-227.598  1.00181.51           O  
ANISOU17425  O   GLN E  49    25256  28197  15512   7400   1319  -4388       O  
ATOM  17426  CB  GLN E  49       7.100 177.422-229.163  1.00188.41           C  
ANISOU17426  CB  GLN E  49    25491  30542  15556   7806   2223  -4088       C  
ATOM  17427  CG  GLN E  49       8.009 177.714-230.349  1.00193.12           C  
ANISOU17427  CG  GLN E  49    25978  31784  15616   8092   2686  -4046       C  
ATOM  17428  CD  GLN E  49       9.393 177.122-230.183  1.00199.01           C  
ANISOU17428  CD  GLN E  49    26247  33052  16317   8697   3124  -3899       C  
ATOM  17429  OE1 GLN E  49       9.866 176.933-229.064  1.00198.27           O  
ANISOU17429  OE1 GLN E  49    25685  33051  16596   8722   3092  -3667       O  
ATOM  17430  NE2 GLN E  49      10.049 176.822-231.299  1.00205.09           N  
ANISOU17430  NE2 GLN E  49    27124  34190  16609   9207   3543  -4016       N  
ATOM  17431  N   GLN E  50       6.213 174.853-226.894  1.00187.99           N  
ANISOU17431  N   GLN E  50    25778  29122  16527   8351   1676  -4403       N  
ATOM  17432  CA  GLN E  50       5.440 174.547-225.692  1.00183.97           C  
ANISOU17432  CA  GLN E  50    25302  28073  16526   8104   1288  -4358       C  
ATOM  17433  C   GLN E  50       5.450 175.690-224.677  1.00180.66           C  
ANISOU17433  C   GLN E  50    24350  27941  16352   7497   1142  -3953       C  
ATOM  17434  O   GLN E  50       6.460 175.937-224.014  1.00181.54           O  
ANISOU17434  O   GLN E  50    23865  28574  16540   7550   1331  -3638       O  
ATOM  17435  CB  GLN E  50       5.944 173.257-225.049  1.00186.50           C  
ANISOU17435  CB  GLN E  50    25583  28183  17096   8709   1389  -4400       C  
ATOM  17436  N   CYS E  51       4.318 176.378-224.559  1.00177.49           N  
ANISOU17436  N   CYS E  51    24177  27199  16063   6922    804  -3961       N  
ATOM  17437  CA  CYS E  51       4.179 177.490-223.619  1.00172.96           C  
ANISOU17437  CA  CYS E  51    23215  26793  15709   6329    656  -3624       C  
ATOM  17438  C   CYS E  51       3.169 177.182-222.518  1.00167.91           C  
ANISOU17438  C   CYS E  51    22719  25562  15518   6102    272  -3618       C  
ATOM  17439  O   CYS E  51       2.313 176.308-222.673  1.00169.14           O  
ANISOU17439  O   CYS E  51    23341  25129  15796   6262     63  -3881       O  
ATOM  17440  CB  CYS E  51       3.764 178.766-224.351  1.00171.70           C  
ANISOU17440  CB  CYS E  51    23143  26799  15298   5832    641  -3555       C  
ATOM  17441  SG  CYS E  51       4.944 179.333-225.592  1.00244.37           S  
ANISOU17441  SG  CYS E  51    32122  36761  23968   6000   1105  -3476       S  
ATOM  17442  N   MET E  52       3.268 177.909-221.409  1.00162.95           N  
ANISOU17442  N   MET E  52    21698  25097  15121   5709    183  -3316       N  
ATOM  17443  CA  MET E  52       2.371 177.702-220.277  1.00157.30           C  
ANISOU17443  CA  MET E  52    21066  23889  14812   5490   -145  -3263       C  
ATOM  17444  C   MET E  52       1.282 178.763-220.194  1.00152.74           C  
ANISOU17444  C   MET E  52    20663  23075  14295   4898   -374  -3195       C  
ATOM  17445  O   MET E  52       1.544 179.915-219.838  1.00150.12           O  
ANISOU17445  O   MET E  52    20051  23064  13923   4485   -319  -2961       O  
ATOM  17446  CB  MET E  52       3.150 177.675-218.965  1.00155.63           C  
ANISOU17446  CB  MET E  52    20336  23974  14821   5495   -109  -2982       C  
ATOM  17447  CG  MET E  52       2.262 177.538-217.744  1.00150.14           C  
ANISOU17447  CG  MET E  52    19708  22825  14513   5257   -421  -2895       C  
ATOM  17448  SD  MET E  52       3.204 177.566-216.210  1.00211.28           S  
ANISOU17448  SD  MET E  52    26845  30986  22445   5237   -395  -2555       S  
ATOM  17449  CE  MET E  52       1.902 177.329-215.001  1.00183.08           C  
ANISOU17449  CE  MET E  52    23504  26775  19282   4994   -758  -2510       C  
ATOM  17450  N   LEU E  53       0.056 178.363-220.511  1.00152.58           N  
ANISOU17450  N   LEU E  53    21110  22485  14377   4858   -630  -3389       N  
ATOM  17451  CA  LEU E  53      -1.077 179.283-220.495  1.00149.78           C  
ANISOU17451  CA  LEU E  53    20936  21885  14088   4365   -846  -3310       C  
ATOM  17452  C   LEU E  53      -1.786 179.302-219.145  1.00147.19           C  
ANISOU17452  C   LEU E  53    20536  21221  14168   4129  -1081  -3146       C  
ATOM  17453  O   LEU E  53      -1.731 178.331-218.385  1.00147.32           O  
ANISOU17453  O   LEU E  53    20509  21028  14439   4375  -1161  -3164       O  
ATOM  17454  CB  LEU E  53      -2.070 178.936-221.605  1.00150.44           C  
ANISOU17454  CB  LEU E  53    21523  21602  14036   4402  -1017  -3565       C  
ATOM  17455  CG  LEU E  53      -1.896 179.666-222.937  1.00153.70           C  
ANISOU17455  CG  LEU E  53    22056  22332  14009   4331   -860  -3620       C  
ATOM  17456  CD1 LEU E  53      -0.532 179.382-223.546  1.00159.05           C  
ANISOU17456  CD1 LEU E  53    22557  23502  14374   4715   -502  -3695       C  
ATOM  17457  CD2 LEU E  53      -3.007 179.279-223.896  1.00155.25           C  
ANISOU17457  CD2 LEU E  53    22752  22147  14087   4327  -1102  -3860       C  
ATOM  17458  N   GLU E  54      -2.456 180.416-218.862  1.00145.46           N  
ANISOU17458  N   GLU E  54    20321  20949  14001   3674  -1172  -2973       N  
ATOM  17459  CA  GLU E  54      -3.237 180.572-217.638  1.00142.38           C  
ANISOU17459  CA  GLU E  54    19897  20244  13957   3434  -1371  -2809       C  
ATOM  17460  C   GLU E  54      -4.540 181.330-217.911  1.00134.70           C  
ANISOU17460  C   GLU E  54    19189  18963  13027   3097  -1541  -2748       C  
ATOM  17461  O   GLU E  54      -4.544 182.553-218.085  1.00134.16           O  
ANISOU17461  O   GLU E  54    19080  19077  12819   2786  -1439  -2604       O  
ATOM  17462  CB  GLU E  54      -2.414 181.275-216.559  1.00144.88           C  
ANISOU17462  CB  GLU E  54    19816  20919  14314   3231  -1240  -2577       C  
ATOM  17463  CG  GLU E  54      -2.993 181.134-215.168  1.00147.49           C  
ANISOU17463  CG  GLU E  54    20091  20969  14979   3107  -1414  -2433       C  
ATOM  17464  CD  GLU E  54      -2.000 181.509-214.097  1.00154.20           C  
ANISOU17464  CD  GLU E  54    20544  22216  15831   2992  -1304  -2252       C  
ATOM  17465  OE1 GLU E  54      -0.862 181.879-214.460  1.00158.53           O  
ANISOU17465  OE1 GLU E  54    20834  23263  16139   2991  -1099  -2225       O  
ATOM  17466  OE2 GLU E  54      -2.351 181.432-212.898  1.00154.80           O1-
ANISOU17466  OE2 GLU E  54    20555  22131  16132   2893  -1425  -2125       O1-
ATOM  17467  N   ILE E  55      -5.642 180.589-217.951  1.00127.78           N  
ANISOU17467  N   ILE E  55    18579  17618  12353   3161  -1798  -2838       N  
ATOM  17468  CA  ILE E  55      -6.932 181.136-218.338  1.00121.49           C  
ANISOU17468  CA  ILE E  55    18017  16549  11593   2904  -1982  -2773       C  
ATOM  17469  C   ILE E  55      -7.716 181.549-217.106  1.00115.40           C  
ANISOU17469  C   ILE E  55    17161  15539  11148   2669  -2091  -2531       C  
ATOM  17470  O   ILE E  55      -7.973 180.732-216.235  1.00114.08           O  
ANISOU17470  O   ILE E  55    16953  15126  11266   2774  -2216  -2513       O  
ATOM  17471  CB  ILE E  55      -7.751 180.095-219.126  1.00124.93           C  
ANISOU17471  CB  ILE E  55    18782  16633  12052   3062  -2229  -2995       C  
ATOM  17472  CG1 ILE E  55      -6.882 179.428-220.197  1.00129.45           C  
ANISOU17472  CG1 ILE E  55    19478  17399  12309   3384  -2102  -3285       C  
ATOM  17473  CG2 ILE E  55      -8.984 180.727-219.743  1.00125.35           C  
ANISOU17473  CG2 ILE E  55    19035  16525  12068   2800  -2415  -2908       C  
ATOM  17474  CD1 ILE E  55      -6.164 180.403-221.108  1.00130.70           C  
ANISOU17474  CD1 ILE E  55    19574  18025  12061   3326  -1851  -3267       C  
ATOM  17475  N   LEU E  56      -8.083 182.823-217.030  1.00113.26           N  
ANISOU17475  N   LEU E  56    16877  15332  10823   2368  -2021  -2335       N  
ATOM  17476  CA  LEU E  56      -8.897 183.319-215.928  1.00110.34           C  
ANISOU17476  CA  LEU E  56    16471  14728  10724   2163  -2088  -2105       C  
ATOM  17477  C   LEU E  56     -10.357 183.413-216.346  1.00117.46           C  
ANISOU17477  C   LEU E  56    17583  15304  11744   2072  -2299  -2016       C  
ATOM  17478  O   LEU E  56     -10.709 184.130-217.291  1.00118.58           O  
ANISOU17478  O   LEU E  56    17854  15513  11689   1966  -2281  -1978       O  
ATOM  17479  CB  LEU E  56      -8.393 184.676-215.437  1.00102.40           C  
ANISOU17479  CB  LEU E  56    15347  13954   9608   1895  -1860  -1935       C  
ATOM  17480  CG  LEU E  56      -9.172 185.328-214.290  1.00 93.87           C  
ANISOU17480  CG  LEU E  56    14274  12639   8753   1694  -1873  -1711       C  
ATOM  17481  CD1 LEU E  56      -9.450 184.341-213.172  1.00 93.20           C  
ANISOU17481  CD1 LEU E  56    14096  12353   8963   1832  -2016  -1690       C  
ATOM  17482  CD2 LEU E  56      -8.406 186.514-213.750  1.00 89.54           C  
ANISOU17482  CD2 LEU E  56    13634  12324   8061   1433  -1639  -1614       C  
ATOM  17483  N   ASP E  57     -11.201 182.672-215.636  1.00122.12           N  
ANISOU17483  N   ASP E  57    18182  15565  12653   2116  -2500  -1954       N  
ATOM  17484  CA  ASP E  57     -12.621 182.620-215.946  1.00125.25           C  
ANISOU17484  CA  ASP E  57    18716  15674  13201   2028  -2730  -1837       C  
ATOM  17485  C   ASP E  57     -13.401 183.554-215.037  1.00122.55           C  
ANISOU17485  C   ASP E  57    18306  15216  13041   1852  -2668  -1523       C  
ATOM  17486  O   ASP E  57     -13.689 183.220-213.887  1.00122.89           O  
ANISOU17486  O   ASP E  57    18248  15094  13351   1866  -2695  -1405       O  
ATOM  17487  CB  ASP E  57     -13.151 181.192-215.810  1.00128.63           C  
ANISOU17487  CB  ASP E  57    19204  15793  13877   2161  -2998  -1941       C  
ATOM  17488  CG  ASP E  57     -14.624 181.089-216.138  1.00130.39           C  
ANISOU17488  CG  ASP E  57    19524  15757  14262   2028  -3268  -1799       C  
ATOM  17489  OD1 ASP E  57     -15.109 181.908-216.950  1.00130.46           O  
ANISOU17489  OD1 ASP E  57    19604  15871  14092   1907  -3281  -1712       O  
ATOM  17490  OD2 ASP E  57     -15.296 180.194-215.584  1.00131.63           O1-
ANISOU17490  OD2 ASP E  57    19667  15621  14726   2041  -3469  -1746       O1-
ATOM  17491  N   THR E  58     -13.743 184.723-215.564  1.00118.83           N  
ANISOU17491  N   THR E  58    17907  14828  12413   1709  -2566  -1380       N  
ATOM  17492  CA  THR E  58     -14.441 185.740-214.790  1.00116.07           C  
ANISOU17492  CA  THR E  58    17542  14362  12199   1576  -2450  -1086       C  
ATOM  17493  C   THR E  58     -15.943 185.491-214.751  1.00115.04           C  
ANISOU17493  C   THR E  58    17423  13969  12319   1578  -2669   -868       C  
ATOM  17494  O   THR E  58     -16.441 184.532-215.341  1.00118.69           O  
ANISOU17494  O   THR E  58    17909  14339  12849   1631  -2940   -955       O  
ATOM  17495  CB  THR E  58     -14.189 187.143-215.365  1.00118.28           C  
ANISOU17495  CB  THR E  58    17918  14803  12221   1439  -2222   -990       C  
ATOM  17496  OG1 THR E  58     -14.737 187.226-216.688  1.00123.76           O  
ANISOU17496  OG1 THR E  58    18724  15538  12760   1452  -2350   -973       O  
ATOM  17497  CG2 THR E  58     -12.699 187.431-215.419  1.00117.32           C  
ANISOU17497  CG2 THR E  58    17748  14976  11855   1390  -2007  -1170       C  
ATOM  17498  N   ALA E  59     -16.661 186.365-214.055  1.00110.74           N  
ANISOU17498  N   ALA E  59    16863  13307  11905   1515  -2543   -580       N  
ATOM  17499  CA  ALA E  59     -18.107 186.249-213.942  1.00109.99           C  
ANISOU17499  CA  ALA E  59    16722  13011  12056   1528  -2710   -303       C  
ATOM  17500  C   ALA E  59     -18.790 187.138-214.970  1.00112.19           C  
ANISOU17500  C   ALA E  59    17084  13352  12190   1486  -2711   -117       C  
ATOM  17501  O   ALA E  59     -18.127 187.783-215.784  1.00113.37           O  
ANISOU17501  O   ALA E  59    17347  13680  12047   1446  -2587   -218       O  
ATOM  17502  CB  ALA E  59     -18.556 186.623-212.542  1.00107.98           C  
ANISOU17502  CB  ALA E  59    16395  12600  12031   1543  -2548    -66       C  
ATOM  17503  N   GLY E  60     -20.117 187.176-214.925  1.00114.37           N  
ANISOU17503  N   GLY E  60    17279  13505  12673   1502  -2845    190       N  
ATOM  17504  CA  GLY E  60     -20.883 188.040-215.803  1.00116.89           C  
ANISOU17504  CA  GLY E  60    17638  13895  12882   1495  -2848    444       C  
ATOM  17505  C   GLY E  60     -20.553 189.491-215.527  1.00117.34           C  
ANISOU17505  C   GLY E  60    17823  13952  12810   1503  -2461    588       C  
ATOM  17506  O   GLY E  60     -19.947 189.801-214.502  1.00115.58           O  
ANISOU17506  O   GLY E  60    17640  13647  12627   1491  -2220    522       O  
ATOM  17507  N   THR E  61     -20.948 190.379-216.433  1.00119.91           N  
ANISOU17507  N   THR E  61    18229  14360  12971   1512  -2407    788       N  
ATOM  17508  CA  THR E  61     -20.621 191.794-216.294  1.00121.87           C  
ANISOU17508  CA  THR E  61    18653  14563  13087   1507  -2030    927       C  
ATOM  17509  C   THR E  61     -21.114 192.383-214.971  1.00124.86           C  
ANISOU17509  C   THR E  61    19047  14694  13698   1583  -1777   1153       C  
ATOM  17510  O   THR E  61     -20.308 192.849-214.166  1.00128.13           O  
ANISOU17510  O   THR E  61    19592  15026  14064   1513  -1517   1013       O  
ATOM  17511  CB  THR E  61     -21.155 192.623-217.468  1.00124.96           C  
ANISOU17511  CB  THR E  61    19121  15058  13301   1545  -2021   1185       C  
ATOM  17512  OG1 THR E  61     -20.493 192.219-218.672  1.00126.97           O  
ANISOU17512  OG1 THR E  61    19417  15563  13261   1467  -2189    939       O  
ATOM  17513  CG2 THR E  61     -20.896 194.101-217.230  1.00125.09           C  
ANISOU17513  CG2 THR E  61    19355  14946  13227   1548  -1607   1362       C  
ATOM  17514  N   GLU E  62     -22.423 192.353-214.737  1.00123.17           N  
ANISOU17514  N   GLU E  62    18696  14383  13718   1722  -1852   1502       N  
ATOM  17515  CA  GLU E  62     -22.961 192.875-213.482  1.00120.65           C  
ANISOU17515  CA  GLU E  62    18398  13838  13607   1841  -1587   1731       C  
ATOM  17516  C   GLU E  62     -23.850 191.868-212.763  1.00111.84           C  
ANISOU17516  C   GLU E  62    17015  12674  12805   1920  -1792   1871       C  
ATOM  17517  O   GLU E  62     -25.077 191.961-212.794  1.00112.19           O  
ANISOU17517  O   GLU E  62    16895  12700  13032   2057  -1843   2257       O  
ATOM  17518  CB  GLU E  62     -23.709 194.194-213.700  1.00130.29           C  
ANISOU17518  CB  GLU E  62    19747  14948  14809   1994  -1316   2122       C  
ATOM  17519  CG  GLU E  62     -24.207 194.861-212.412  1.00137.28           C  
ANISOU17519  CG  GLU E  62    20728  15572  15862   2155   -970   2338       C  
ATOM  17520  CD  GLU E  62     -23.117 195.601-211.653  1.00141.28           C  
ANISOU17520  CD  GLU E  62    21560  15913  16208   2032   -633   2074       C  
ATOM  17521  OE1 GLU E  62     -22.092 195.956-212.275  1.00143.23           O  
ANISOU17521  OE1 GLU E  62    21970  16238  16212   1844   -598   1834       O  
ATOM  17522  OE2 GLU E  62     -23.291 195.830-210.436  1.00141.54           O1-
ANISOU17522  OE2 GLU E  62    21683  15755  16343   2111   -407   2114       O1-
ATOM  17523  N   GLN E  63     -23.218 190.896-212.118  1.00103.72           N  
ANISOU17523  N   GLN E  63    15924  11641  11842   1836  -1906   1586       N  
ATOM  17524  CA  GLN E  63     -23.935 189.958-211.273  1.00 96.27           C  
ANISOU17524  CA  GLN E  63    14755  10622  11202   1893  -2055   1718       C  
ATOM  17525  C   GLN E  63     -23.685 190.341-209.825  1.00 99.23           C  
ANISOU17525  C   GLN E  63    15220  10849  11635   1959  -1737   1730       C  
ATOM  17526  O   GLN E  63     -24.492 190.059-208.940  1.00100.88           O  
ANISOU17526  O   GLN E  63    15285  10967  12080   2073  -1703   1976       O  
ATOM  17527  CB  GLN E  63     -23.479 188.532-211.562  1.00 88.31           C  
ANISOU17527  CB  GLN E  63    13632   9683  10238   1776  -2412   1421       C  
ATOM  17528  CG  GLN E  63     -23.761 188.111-212.987  1.00 84.19           C  
ANISOU17528  CG  GLN E  63    13066   9298   9623   1698  -2741   1377       C  
ATOM  17529  CD  GLN E  63     -23.294 186.712-213.286  1.00 84.31           C  
ANISOU17529  CD  GLN E  63    13041   9326   9666   1599  -3066   1051       C  
ATOM  17530  OE1 GLN E  63     -22.606 186.090-212.479  1.00 82.94           O  
ANISOU17530  OE1 GLN E  63    12870   9076   9565   1605  -3025    850       O  
ATOM  17531  NE2 GLN E  63     -23.667 186.202-214.454  1.00 86.33           N  
ANISOU17531  NE2 GLN E  63    13279   9675   9850   1515  -3391   1001       N  
ATOM  17532  N   PHE E  64     -22.555 191.001-209.602  1.00102.26           N  
ANISOU17532  N   PHE E  64    15845  11229  11781   1871  -1505   1469       N  
ATOM  17533  CA  PHE E  64     -22.247 191.610-208.314  1.00105.87           C  
ANISOU17533  CA  PHE E  64    16464  11553  12207   1895  -1181   1456       C  
ATOM  17534  C   PHE E  64     -21.193 192.692-208.506  1.00108.07           C  
ANISOU17534  C   PHE E  64    17044  11829  12188   1748   -932   1242       C  
ATOM  17535  O   PHE E  64     -20.499 192.715-209.526  1.00113.36           O  
ANISOU17535  O   PHE E  64    17742  12644  12685   1621  -1035   1059       O  
ATOM  17536  CB  PHE E  64     -21.753 190.559-207.316  1.00106.04           C  
ANISOU17536  CB  PHE E  64    16361  11611  12320   1857  -1293   1278       C  
ATOM  17537  CG  PHE E  64     -20.778 189.581-207.902  1.00105.00           C  
ANISOU17537  CG  PHE E  64    16133  11649  12114   1729  -1565    947       C  
ATOM  17538  CD1 PHE E  64     -19.453 189.930-208.085  1.00102.90           C  
ANISOU17538  CD1 PHE E  64    16002  11513  11582   1580  -1476    639       C  
ATOM  17539  CD2 PHE E  64     -21.189 188.315-208.275  1.00104.84           C  
ANISOU17539  CD2 PHE E  64    15893  11654  12289   1759  -1900    955       C  
ATOM  17540  CE1 PHE E  64     -18.560 189.038-208.628  1.00101.97           C  
ANISOU17540  CE1 PHE E  64    15784  11568  11391   1517  -1689    360       C  
ATOM  17541  CE2 PHE E  64     -20.297 187.422-208.818  1.00104.39           C  
ANISOU17541  CE2 PHE E  64    15793  11715  12154   1687  -2115    643       C  
ATOM  17542  CZ  PHE E  64     -18.982 187.785-208.995  1.00103.68           C  
ANISOU17542  CZ  PHE E  64    15823  11777  11795   1593  -1996    353       C  
ATOM  17543  N   THR E  65     -21.084 193.588-207.531  1.00104.86           N  
ANISOU17543  N   THR E  65    16875  11255  11711   1754   -601   1267       N  
ATOM  17544  CA  THR E  65     -20.067 194.631-207.561  1.00103.16           C  
ANISOU17544  CA  THR E  65    16970  11003  11224   1555   -362   1061       C  
ATOM  17545  C   THR E  65     -18.684 193.994-207.556  1.00104.30           C  
ANISOU17545  C   THR E  65    17026  11388  11215   1321   -524    688       C  
ATOM  17546  O   THR E  65     -18.272 193.421-206.553  1.00106.06           O  
ANISOU17546  O   THR E  65    17173  11668  11458   1285   -563    558       O  
ATOM  17547  CB  THR E  65     -20.193 195.548-206.348  1.00 99.15           C  
ANISOU17547  CB  THR E  65    16760  10249  10662   1579     -7   1109       C  
ATOM  17548  OG1 THR E  65     -21.461 196.218-206.385  1.00 98.78           O  
ANISOU17548  OG1 THR E  65    16806   9976  10749   1849    196   1480       O  
ATOM  17549  CG2 THR E  65     -19.078 196.570-206.355  1.00 99.12           C  
ANISOU17549  CG2 THR E  65    17089  10195  10376   1297    203    868       C  
ATOM  17550  N   ALA E  66     -17.964 194.087-208.671  1.00104.43           N  
ANISOU17550  N   ALA E  66    17038  11571  11069   1184   -606    542       N  
ATOM  17551  CA  ALA E  66     -16.764 193.269-208.831  1.00103.72           C  
ANISOU17551  CA  ALA E  66    16781  11760  10868   1039   -790    235       C  
ATOM  17552  C   ALA E  66     -15.463 193.984-209.208  1.00107.80           C  
ANISOU17552  C   ALA E  66    17423  12434  11101    769   -655     24       C  
ATOM  17553  O   ALA E  66     -15.445 195.163-209.562  1.00103.27           O  
ANISOU17553  O   ALA E  66    17099  11737  10401    657   -432    104       O  
ATOM  17554  CB  ALA E  66     -17.040 192.129-209.792  1.00103.25           C  
ANISOU17554  CB  ALA E  66    16479  11843  10909   1164  -1109    214       C  
ATOM  17555  N   MET E  67     -14.380 193.215-209.136  1.00117.98           N  
ANISOU17555  N   MET E  67    18520  14003  12306    674   -793   -220       N  
ATOM  17556  CA  MET E  67     -13.013 193.695-209.312  1.00126.24           C  
ANISOU17556  CA  MET E  67    19587  15282  13096    401   -693   -416       C  
ATOM  17557  C   MET E  67     -12.546 193.636-210.766  1.00129.32           C  
ANISOU17557  C   MET E  67    19907  15887  13343    385   -750   -474       C  
ATOM  17558  O   MET E  67     -11.546 192.987-211.073  1.00132.25           O  
ANISOU17558  O   MET E  67    20072  16570  13606    351   -847   -660       O  
ATOM  17559  CB  MET E  67     -12.078 192.843-208.448  1.00128.14           C  
ANISOU17559  CB  MET E  67    19600  15770  13316    350   -807   -605       C  
ATOM  17560  CG  MET E  67     -12.584 191.411-208.216  1.00126.55           C  
ANISOU17560  CG  MET E  67    19166  15573  13345    634  -1056   -596       C  
ATOM  17561  SD  MET E  67     -12.817 190.442-209.727  1.00188.36           S  
ANISOU17561  SD  MET E  67    26849  23493  21227    842  -1288   -641       S  
ATOM  17562  CE  MET E  67     -14.260 189.461-209.309  1.00114.07           C  
ANISOU17562  CE  MET E  67    17368  13810  12164   1101  -1495   -466       C  
ATOM  17563  N   ARG E  68     -13.258 194.321-211.654  1.00127.02           N  
ANISOU17563  N   ARG E  68    19782  15446  13034    433   -675   -297       N  
ATOM  17564  CA  ARG E  68     -12.993 194.216-213.085  1.00125.89           C  
ANISOU17564  CA  ARG E  68    19587  15507  12738    458   -744   -322       C  
ATOM  17565  C   ARG E  68     -11.568 194.640-213.458  1.00127.31           C  
ANISOU17565  C   ARG E  68    19739  15979  12655    202   -612   -480       C  
ATOM  17566  O   ARG E  68     -10.906 193.982-214.259  1.00126.75           O  
ANISOU17566  O   ARG E  68    19492  16212  12457    253   -716   -619       O  
ATOM  17567  CB  ARG E  68     -14.018 195.032-213.887  1.00128.43           C  
ANISOU17567  CB  ARG E  68    20104  15627  13065    541   -665    -52       C  
ATOM  17568  CG  ARG E  68     -15.482 194.778-213.508  1.00129.85           C  
ANISOU17568  CG  ARG E  68    20283  15546  13509    780   -764    174       C  
ATOM  17569  CD  ARG E  68     -15.887 193.322-213.726  1.00130.01           C  
ANISOU17569  CD  ARG E  68    20050  15677  13670    961  -1104     92       C  
ATOM  17570  NE  ARG E  68     -17.166 192.988-213.094  1.00126.67           N  
ANISOU17570  NE  ARG E  68    19568  15031  13529   1137  -1198    308       N  
ATOM  17571  CZ  ARG E  68     -17.672 191.760-213.031  1.00120.86           C  
ANISOU17571  CZ  ARG E  68    18631  14313  12978   1262  -1484    281       C  
ATOM  17572  NH1 ARG E  68     -18.838 191.553-212.430  1.00117.62           N1+
ANISOU17572  NH1 ARG E  68    18146  13717  12827   1394  -1541    524       N1+
ATOM  17573  NH2 ARG E  68     -17.008 190.739-213.558  1.00119.53           N  
ANISOU17573  NH2 ARG E  68    18343  14337  12735   1257  -1696     20       N  
ATOM  17574  N   ASP E  69     -11.092 195.720-212.847  1.00131.33           N  
ANISOU17574  N   ASP E  69    20423  16396  13079    -77   -379   -458       N  
ATOM  17575  CA  ASP E  69      -9.874 196.397-213.297  1.00136.15           C  
ANISOU17575  CA  ASP E  69    21038  17247  13443   -384   -222   -530       C  
ATOM  17576  C   ASP E  69      -8.565 195.663-213.012  1.00134.43           C  
ANISOU17576  C   ASP E  69    20505  17450  13123   -490   -307   -749       C  
ATOM  17577  O   ASP E  69      -7.542 195.941-213.640  1.00136.52           O  
ANISOU17577  O   ASP E  69    20666  18023  13184   -678   -219   -794       O  
ATOM  17578  CB  ASP E  69      -9.815 197.806-212.703  1.00142.29           C  
ANISOU17578  CB  ASP E  69    22146  17746  14172   -694     44   -439       C  
ATOM  17579  CG  ASP E  69     -10.999 198.660-213.116  1.00146.37           C  
ANISOU17579  CG  ASP E  69    22983  17863  14767   -562    185   -182       C  
ATOM  17580  OD1 ASP E  69     -10.941 199.270-214.205  1.00148.58           O  
ANISOU17580  OD1 ASP E  69    23362  18170  14920   -606    290    -51       O  
ATOM  17581  OD2 ASP E  69     -11.988 198.720-212.352  1.00146.95           O1-
ANISOU17581  OD2 ASP E  69    23196  17615  15023   -393    204    -85       O1-
ATOM  17582  N   LEU E  70      -8.598 194.729-212.071  1.00130.98           N  
ANISOU17582  N   LEU E  70    19896  17044  12828   -356   -467   -853       N  
ATOM  17583  CA  LEU E  70      -7.386 194.044-211.625  1.00128.75           C  
ANISOU17583  CA  LEU E  70    19300  17155  12465   -428   -542  -1020       C  
ATOM  17584  C   LEU E  70      -6.841 193.096-212.690  1.00126.27           C  
ANISOU17584  C   LEU E  70    18728  17180  12067   -204   -643  -1116       C  
ATOM  17585  O   LEU E  70      -5.678 193.200-213.106  1.00130.17           O  
ANISOU17585  O   LEU E  70    19035  18058  12365   -345   -560  -1175       O  
ATOM  17586  CB  LEU E  70      -7.656 193.281-210.326  1.00127.39           C  
ANISOU17586  CB  LEU E  70    19032  16902  12470   -304   -682  -1065       C  
ATOM  17587  CG  LEU E  70      -7.608 194.039-208.994  1.00127.94           C  
ANISOU17587  CG  LEU E  70    19263  16825  12523   -578   -582  -1052       C  
ATOM  17588  CD1 LEU E  70      -8.411 195.333-209.025  1.00128.82           C  
ANISOU17588  CD1 LEU E  70    19790  16523  12633   -722   -378   -923       C  
ATOM  17589  CD2 LEU E  70      -8.110 193.141-207.876  1.00126.18           C  
ANISOU17589  CD2 LEU E  70    18950  16510  12483   -361   -731  -1055       C  
ATOM  17590  N   TYR E  71      -7.683 192.172-213.136  1.00120.95           N  
ANISOU17590  N   TYR E  71    18053  16367  11534    141   -816  -1131       N  
ATOM  17591  CA  TYR E  71      -7.263 191.229-214.162  1.00122.39           C  
ANISOU17591  CA  TYR E  71    18070  16809  11623    381   -910  -1256       C  
ATOM  17592  C   TYR E  71      -7.122 191.888-215.530  1.00125.12           C  
ANISOU17592  C   TYR E  71    18524  17280  11736    319   -785  -1208       C  
ATOM  17593  O   TYR E  71      -6.487 191.337-216.427  1.00126.19           O  
ANISOU17593  O   TYR E  71    18531  17715  11702    463   -788  -1319       O  
ATOM  17594  CB  TYR E  71      -8.193 190.015-214.228  1.00120.21           C  
ANISOU17594  CB  TYR E  71    17798  16320  11555    721  -1154  -1308       C  
ATOM  17595  CG  TYR E  71      -9.667 190.332-214.284  1.00116.69           C  
ANISOU17595  CG  TYR E  71    17580  15479  11277    763  -1230  -1145       C  
ATOM  17596  CD1 TYR E  71     -10.226 190.942-215.399  1.00117.90           C  
ANISOU17596  CD1 TYR E  71    17907  15576  11313    752  -1197  -1042       C  
ATOM  17597  CD2 TYR E  71     -10.505 189.993-213.233  1.00114.59           C  
ANISOU17597  CD2 TYR E  71    17328  14932  11280    833  -1334  -1064       C  
ATOM  17598  CE1 TYR E  71     -11.572 191.224-215.460  1.00117.74           C  
ANISOU17598  CE1 TYR E  71    18046  15243  11447    811  -1271   -851       C  
ATOM  17599  CE2 TYR E  71     -11.857 190.268-213.284  1.00115.79           C  
ANISOU17599  CE2 TYR E  71    17637  14767  11592    891  -1391   -876       C  
ATOM  17600  CZ  TYR E  71     -12.384 190.884-214.401  1.00117.52           C  
ANISOU17600  CZ  TYR E  71    18004  14951  11699    883  -1364   -765       C  
ATOM  17601  OH  TYR E  71     -13.729 191.163-214.466  1.00117.41           O  
ANISOU17601  OH  TYR E  71    18100  14667  11843    960  -1424   -536       O  
ATOM  17602  N   MET E  72      -7.724 193.062-215.692  1.00126.19           N  
ANISOU17602  N   MET E  72    18911  17182  11853    133   -659  -1030       N  
ATOM  17603  CA  MET E  72      -7.499 193.852-216.893  1.00129.88           C  
ANISOU17603  CA  MET E  72    19487  17778  12085     29   -505   -936       C  
ATOM  17604  C   MET E  72      -6.095 194.436-216.845  1.00135.26           C  
ANISOU17604  C   MET E  72    20019  18807  12567   -275   -302   -959       C  
ATOM  17605  O   MET E  72      -5.375 194.438-217.847  1.00139.48           O  
ANISOU17605  O   MET E  72    20448  19677  12870   -270   -211   -974       O  
ATOM  17606  CB  MET E  72      -8.518 194.982-217.005  1.00127.59           C  
ANISOU17606  CB  MET E  72    19513  17117  11849    -71   -404   -699       C  
ATOM  17607  CG  MET E  72      -9.918 194.531-217.346  1.00124.86           C  
ANISOU17607  CG  MET E  72    19275  16512  11655    214   -595   -608       C  
ATOM  17608  SD  MET E  72     -10.969 195.946-217.718  1.00154.62           S  
ANISOU17608  SD  MET E  72    23374  19938  15435    145   -427   -268       S  
ATOM  17609  CE  MET E  72     -12.514 195.126-218.096  1.00169.50           C  
ANISOU17609  CE  MET E  72    25249  21653  17499    490   -722   -165       C  
ATOM  17610  N   LYS E  73      -5.715 194.931-215.670  1.00133.82           N  
ANISOU17610  N   LYS E  73    19825  18561  12460   -552   -236   -955       N  
ATOM  17611  CA  LYS E  73      -4.390 195.502-215.465  1.00133.95           C  
ANISOU17611  CA  LYS E  73    19673  18915  12306   -913    -79   -963       C  
ATOM  17612  C   LYS E  73      -3.309 194.464-215.698  1.00132.93           C  
ANISOU17612  C   LYS E  73    19136  19298  12074   -751   -139  -1099       C  
ATOM  17613  O   LYS E  73      -2.328 194.727-216.393  1.00136.99           O  
ANISOU17613  O   LYS E  73    19474  20203  12375   -882      4  -1067       O  
ATOM  17614  CB  LYS E  73      -4.252 196.056-214.048  1.00135.24           C  
ANISOU17614  CB  LYS E  73    19909  18914  12561  -1233    -58   -972       C  
ATOM  17615  CG  LYS E  73      -2.850 196.545-213.713  1.00140.10           C  
ANISOU17615  CG  LYS E  73    20306  19921  13005  -1657     46   -989       C  
ATOM  17616  CD  LYS E  73      -2.459 197.735-214.579  1.00145.34           C  
ANISOU17616  CD  LYS E  73    21119  20613  13491  -1993    276   -846       C  
ATOM  17617  CE  LYS E  73      -1.027 198.173-214.312  1.00149.85           C  
ANISOU17617  CE  LYS E  73    21418  21624  13893  -2454    362   -840       C  
ATOM  17618  NZ  LYS E  73      -0.805 198.513-212.878  1.00150.48           N1+
ANISOU17618  NZ  LYS E  73    21549  21603  14024  -2801    297   -915       N1+
ATOM  17619  N   ASN E  74      -3.486 193.281-215.118  1.00128.26           N  
ANISOU17619  N   ASN E  74    18391  18706  11638   -447   -332  -1227       N  
ATOM  17620  CA  ASN E  74      -2.445 192.264-215.219  1.00123.60           C  
ANISOU17620  CA  ASN E  74    17419  18575  10970   -245   -369  -1341       C  
ATOM  17621  C   ASN E  74      -2.551 191.356-216.447  1.00119.17           C  
ANISOU17621  C   ASN E  74    16835  18124  10320    170   -405  -1440       C  
ATOM  17622  O   ASN E  74      -1.565 190.748-216.858  1.00119.25           O  
ANISOU17622  O   ASN E  74    16564  18555  10189    336   -343  -1510       O  
ATOM  17623  CB  ASN E  74      -2.355 191.438-213.936  1.00119.44           C  
ANISOU17623  CB  ASN E  74    16712  18040  10628   -134   -532  -1413       C  
ATOM  17624  CG  ASN E  74      -0.933 191.304-213.441  1.00122.25           C  
ANISOU17624  CG  ASN E  74    16659  18923  10866   -276   -481  -1411       C  
ATOM  17625  OD1 ASN E  74       0.019 191.487-214.202  1.00123.84           O  
ANISOU17625  OD1 ASN E  74    16648  19542  10864   -338   -335  -1380       O  
ATOM  17626  ND2 ASN E  74      -0.777 190.985-212.163  1.00123.78           N  
ANISOU17626  ND2 ASN E  74    16719  19137  11176   -326   -599  -1418       N  
ATOM  17627  N   GLY E  75      -3.741 191.285-217.035  1.00116.50           N  
ANISOU17627  N   GLY E  75    16796  17424  10047    335   -500  -1439       N  
ATOM  17628  CA  GLY E  75      -3.982 190.419-218.177  1.00118.88           C  
ANISOU17628  CA  GLY E  75    17146  17777  10244    698   -575  -1561       C  
ATOM  17629  C   GLY E  75      -3.237 190.801-219.444  1.00124.00           C  
ANISOU17629  C   GLY E  75    17752  18803  10561    684   -376  -1540       C  
ATOM  17630  O   GLY E  75      -3.174 191.974-219.815  1.00124.65           O  
ANISOU17630  O   GLY E  75    17935  18914  10513    388   -212  -1370       O  
ATOM  17631  N   GLN E  76      -2.687 189.795-220.117  1.00128.00           N  
ANISOU17631  N   GLN E  76    18130  19581  10923   1024   -374  -1708       N  
ATOM  17632  CA  GLN E  76      -1.883 190.004-221.318  1.00134.18           C  
ANISOU17632  CA  GLN E  76    18839  20783  11358   1076   -159  -1699       C  
ATOM  17633  C   GLN E  76      -2.677 189.728-222.598  1.00137.22           C  
ANISOU17633  C   GLN E  76    19530  21046  11561   1306   -236  -1783       C  
ATOM  17634  O   GLN E  76      -2.353 190.243-223.668  1.00139.45           O  
ANISOU17634  O   GLN E  76    19860  21589  11535   1274    -63  -1711       O  
ATOM  17635  CB  GLN E  76      -0.636 189.117-221.273  1.00137.55           C  
ANISOU17635  CB  GLN E  76    18915  21654  11692   1335    -53  -1817       C  
ATOM  17636  CG  GLN E  76       0.229 189.315-220.036  1.00137.73           C  
ANISOU17636  CG  GLN E  76    18582  21889  11859   1113     -5  -1719       C  
ATOM  17637  CD  GLN E  76       1.448 188.406-220.015  1.00142.24           C  
ANISOU17637  CD  GLN E  76    18764  22939  12344   1421    104  -1788       C  
ATOM  17638  OE1 GLN E  76       1.585 187.506-220.843  1.00143.71           O  
ANISOU17638  OE1 GLN E  76    18989  23222  12391   1855    145  -1947       O  
ATOM  17639  NE2 GLN E  76       2.342 188.643-219.062  1.00145.16           N  
ANISOU17639  NE2 GLN E  76    18760  23615  12779   1204    154  -1663       N  
ATOM  17640  N   GLY E  77      -3.710 188.902-222.480  1.00136.97           N  
ANISOU17640  N   GLY E  77    19698  20637  11707   1519   -507  -1924       N  
ATOM  17641  CA  GLY E  77      -4.583 188.592-223.598  1.00137.69           C  
ANISOU17641  CA  GLY E  77    20088  20590  11638   1692   -649  -2011       C  
ATOM  17642  C   GLY E  77      -6.026 188.576-223.135  1.00135.45           C  
ANISOU17642  C   GLY E  77    20011  19814  11640   1625   -929  -1950       C  
ATOM  17643  O   GLY E  77      -6.306 188.300-221.969  1.00134.96           O  
ANISOU17643  O   GLY E  77    19868  19506  11906   1588  -1039  -1940       O  
ATOM  17644  N   PHE E  78      -6.949 188.881-224.038  1.00133.62           N  
ANISOU17644  N   PHE E  78    20026  19471  11274   1613  -1041  -1881       N  
ATOM  17645  CA  PHE E  78      -8.354 188.956-223.667  1.00128.28           C  
ANISOU17645  CA  PHE E  78    19501  18382  10858   1545  -1294  -1762       C  
ATOM  17646  C   PHE E  78      -9.241 188.308-224.719  1.00129.73           C  
ANISOU17646  C   PHE E  78    19909  18491  10891   1705  -1557  -1874       C  
ATOM  17647  O   PHE E  78      -9.076 188.541-225.914  1.00134.01           O  
ANISOU17647  O   PHE E  78    20571  19282  11064   1748  -1497  -1888       O  
ATOM  17648  CB  PHE E  78      -8.777 190.409-223.447  1.00125.86           C  
ANISOU17648  CB  PHE E  78    19247  17971  10603   1265  -1156  -1424       C  
ATOM  17649  CG  PHE E  78      -8.068 191.086-222.302  1.00125.02           C  
ANISOU17649  CG  PHE E  78    18979  17862  10661   1044   -941  -1326       C  
ATOM  17650  CD1 PHE E  78      -8.572 191.012-221.015  1.00122.42           C  
ANISOU17650  CD1 PHE E  78    18612  17220  10681    983  -1032  -1281       C  
ATOM  17651  CD2 PHE E  78      -6.902 191.807-222.516  1.00127.16           C  
ANISOU17651  CD2 PHE E  78    19138  18458  10718    875   -654  -1271       C  
ATOM  17652  CE1 PHE E  78      -7.923 191.642-219.962  1.00121.68           C  
ANISOU17652  CE1 PHE E  78    18405  17135  10694    757   -854  -1213       C  
ATOM  17653  CE2 PHE E  78      -6.249 192.436-221.467  1.00125.96           C  
ANISOU17653  CE2 PHE E  78    18849  18315  10697    615   -491  -1192       C  
ATOM  17654  CZ  PHE E  78      -6.761 192.354-220.191  1.00122.98           C  
ANISOU17654  CZ  PHE E  78    18468  17619  10639    555   -598  -1177       C  
ATOM  17655  N   ALA E  79     -10.178 187.486-224.265  1.00127.22           N  
ANISOU17655  N   ALA E  79    19646  17846  10847   1772  -1858  -1947       N  
ATOM  17656  CA  ALA E  79     -11.129 186.846-225.158  1.00127.21           C  
ANISOU17656  CA  ALA E  79    19854  17744  10735   1856  -2168  -2047       C  
ATOM  17657  C   ALA E  79     -12.541 187.239-224.756  1.00126.50           C  
ANISOU17657  C   ALA E  79    19785  17360  10922   1710  -2387  -1770       C  
ATOM  17658  O   ALA E  79     -13.164 186.576-223.929  1.00125.17           O  
ANISOU17658  O   ALA E  79    19563  16897  11098   1717  -2586  -1786       O  
ATOM  17659  CB  ALA E  79     -10.965 185.338-225.112  1.00126.12           C  
ANISOU17659  CB  ALA E  79    19778  17483  10657   2070  -2353  -2405       C  
ATOM  17660  N   LEU E  80     -13.040 188.327-225.332  1.00126.98           N  
ANISOU17660  N   LEU E  80    19906  17507  10833   1593  -2331  -1484       N  
ATOM  17661  CA  LEU E  80     -14.390 188.787-225.025  1.00123.95           C  
ANISOU17661  CA  LEU E  80    19517  16887  10691   1497  -2504  -1167       C  
ATOM  17662  C   LEU E  80     -15.394 187.828-225.645  1.00126.57           C  
ANISOU17662  C   LEU E  80    19941  17144  11006   1538  -2923  -1267       C  
ATOM  17663  O   LEU E  80     -15.248 187.447-226.800  1.00132.01           O  
ANISOU17663  O   LEU E  80    20786  18042  11331   1593  -3038  -1452       O  
ATOM  17664  CB  LEU E  80     -14.611 190.210-225.543  1.00121.24           C  
ANISOU17664  CB  LEU E  80    19228  16661  10175   1401  -2311   -812       C  
ATOM  17665  CG  LEU E  80     -14.086 191.361-224.679  1.00117.48           C  
ANISOU17665  CG  LEU E  80    18691  16106   9839   1279  -1946   -605       C  
ATOM  17666  CD1 LEU E  80     -12.564 191.392-224.628  1.00116.70           C  
ANISOU17666  CD1 LEU E  80    18535  16239   9564   1246  -1670   -820       C  
ATOM  17667  CD2 LEU E  80     -14.634 192.692-225.172  1.00119.53           C  
ANISOU17667  CD2 LEU E  80    19052  16367   9995   1207  -1805   -209       C  
ATOM  17668  N   VAL E  81     -16.403 187.420-224.881  1.00123.05           N  
ANISOU17668  N   VAL E  81    19405  16411  10937   1497  -3154  -1148       N  
ATOM  17669  CA  VAL E  81     -17.349 186.423-225.378  1.00124.21           C  
ANISOU17669  CA  VAL E  81    19621  16469  11105   1477  -3584  -1249       C  
ATOM  17670  C   VAL E  81     -18.801 186.908-225.352  1.00121.61           C  
ANISOU17670  C   VAL E  81    19190  16061  10955   1373  -3797   -838       C  
ATOM  17671  O   VAL E  81     -19.209 187.635-224.443  1.00117.24           O  
ANISOU17671  O   VAL E  81    18486  15366  10695   1358  -3638   -516       O  
ATOM  17672  CB  VAL E  81     -17.239 185.088-224.601  1.00124.12           C  
ANISOU17672  CB  VAL E  81    19587  16189  11385   1523  -3744  -1531       C  
ATOM  17673  CG1 VAL E  81     -17.888 183.959-225.387  1.00126.77           C  
ANISOU17673  CG1 VAL E  81    20086  16454  11625   1481  -4168  -1756       C  
ATOM  17674  CG2 VAL E  81     -15.785 184.752-224.315  1.00123.59           C  
ANISOU17674  CG2 VAL E  81    19537  16194  11228   1668  -3464  -1838       C  
ATOM  17675  N   TYR E  82     -19.573 186.505-226.360  1.00123.65           N  
ANISOU17675  N   TYR E  82    19533  16431  11015   1308  -4154   -846       N  
ATOM  17676  CA  TYR E  82     -21.001 186.805-226.411  1.00122.40           C  
ANISOU17676  CA  TYR E  82    19232  16254  11021   1209  -4417   -443       C  
ATOM  17677  C   TYR E  82     -21.802 185.655-227.012  1.00123.36           C  
ANISOU17677  C   TYR E  82    19408  16359  11102   1074  -4929   -606       C  
ATOM  17678  O   TYR E  82     -21.380 185.032-227.983  1.00125.12           O  
ANISOU17678  O   TYR E  82    19868  16714  10957   1061  -5086   -966       O  
ATOM  17679  CB  TYR E  82     -21.268 188.096-227.193  1.00122.11           C  
ANISOU17679  CB  TYR E  82    19201  16484  10711   1231  -4285    -78       C  
ATOM  17680  CG  TYR E  82     -21.072 187.993-228.693  1.00125.62           C  
ANISOU17680  CG  TYR E  82    19849  17262  10619   1215  -4446   -238       C  
ATOM  17681  CD1 TYR E  82     -19.830 188.221-229.269  1.00125.60           C  
ANISOU17681  CD1 TYR E  82    20031  17448  10243   1300  -4164   -491       C  
ATOM  17682  CD2 TYR E  82     -22.137 187.688-229.535  1.00130.08           C  
ANISOU17682  CD2 TYR E  82    20408  17986  11029   1105  -4882   -114       C  
ATOM  17683  CE1 TYR E  82     -19.650 188.139-230.641  1.00129.31           C  
ANISOU17683  CE1 TYR E  82    20701  18244  10188   1306  -4286   -629       C  
ATOM  17684  CE2 TYR E  82     -21.966 187.601-230.908  1.00133.40           C  
ANISOU17684  CE2 TYR E  82    21040  18734  10911   1085  -5039   -266       C  
ATOM  17685  CZ  TYR E  82     -20.722 187.828-231.455  1.00132.34           C  
ANISOU17685  CZ  TYR E  82    21114  18770  10401   1201  -4727   -528       C  
ATOM  17686  OH  TYR E  82     -20.550 187.744-232.817  1.00135.84           O  
ANISOU17686  OH  TYR E  82    21779  19557  10276   1202  -4858   -675       O  
ATOM  17687  N   SER E  83     -22.961 185.382-226.424  1.00123.41           N  
ANISOU17687  N   SER E  83    19203  16204  11482    964  -5184   -336       N  
ATOM  17688  CA  SER E  83     -23.868 184.374-226.950  1.00127.41           C  
ANISOU17688  CA  SER E  83    19726  16695  11988    765  -5706   -420       C  
ATOM  17689  C   SER E  83     -24.644 184.953-228.123  1.00128.83           C  
ANISOU17689  C   SER E  83    19890  17231  11830    677  -5946   -151       C  
ATOM  17690  O   SER E  83     -25.199 186.047-228.027  1.00128.79           O  
ANISOU17690  O   SER E  83    19679  17365  11889    743  -5806    339       O  
ATOM  17691  CB  SER E  83     -24.835 183.906-225.862  1.00129.86           C  
ANISOU17691  CB  SER E  83    19765  16740  12838    659  -5878   -171       C  
ATOM  17692  OG  SER E  83     -25.919 183.182-226.420  1.00136.53           O  
ANISOU17692  OG  SER E  83    20556  17627  13690    408  -6403   -114       O  
ATOM  17693  N   ILE E  84     -24.686 184.220-229.230  1.00130.16           N  
ANISOU17693  N   ILE E  84    20290  17543  11623    541  -6304   -465       N  
ATOM  17694  CA  ILE E  84     -25.340 184.719-230.430  1.00134.31           C  
ANISOU17694  CA  ILE E  84    20822  18459  11749    452  -6559   -238       C  
ATOM  17695  C   ILE E  84     -26.860 184.569-230.346  1.00138.65           C  
ANISOU17695  C   ILE E  84    21065  19065  12550    229  -7002    178       C  
ATOM  17696  O   ILE E  84     -27.581 184.888-231.294  1.00141.24           O  
ANISOU17696  O   ILE E  84    21338  19745  12581    121  -7297    421       O  
ATOM  17697  CB  ILE E  84     -24.792 184.035-231.699  1.00137.22           C  
ANISOU17697  CB  ILE E  84    21587  19001  11548    389  -6770   -743       C  
ATOM  17698  CG1 ILE E  84     -25.269 182.587-231.789  1.00141.28           C  
ANISOU17698  CG1 ILE E  84    22246  19294  12139    130  -7265  -1104       C  
ATOM  17699  CG2 ILE E  84     -23.273 184.091-231.715  1.00133.93           C  
ANISOU17699  CG2 ILE E  84    21425  18543  10919    630  -6314  -1137       C  
ATOM  17700  CD1 ILE E  84     -24.954 181.930-233.116  1.00144.73           C  
ANISOU17700  CD1 ILE E  84    23108  19906  11976     41  -7534  -1579       C  
ATOM  17701  N   THR E  85     -27.340 184.090-229.201  1.00138.18           N  
ANISOU17701  N   THR E  85    20780  18692  13029    163  -7045    291       N  
ATOM  17702  CA  THR E  85     -28.772 183.942-228.972  1.00140.29           C  
ANISOU17702  CA  THR E  85    20688  19015  13599    -43  -7424    736       C  
ATOM  17703  C   THR E  85     -29.335 185.194-228.293  1.00140.50           C  
ANISOU17703  C   THR E  85    20349  19128  13908    167  -7104   1383       C  
ATOM  17704  O   THR E  85     -30.550 185.400-228.254  1.00143.48           O  
ANISOU17704  O   THR E  85    20375  19673  14469     76  -7346   1882       O  
ATOM  17705  CB  THR E  85     -29.080 182.692-228.118  1.00135.78           C  
ANISOU17705  CB  THR E  85    20060  18063  13468   -244  -7657    550       C  
ATOM  17706  OG1 THR E  85     -28.208 181.622-228.500  1.00134.22           O  
ANISOU17706  OG1 THR E  85    20287  17657  13055   -318  -7761   -113       O  
ATOM  17707  CG2 THR E  85     -30.526 182.253-228.302  1.00138.18           C  
ANISOU17707  CG2 THR E  85    20062  18499  13943   -575  -8201    894       C  
ATOM  17708  N   ALA E  86     -28.444 186.030-227.765  1.00135.18           N  
ANISOU17708  N   ALA E  86    19764  18341  13258    447  -6554   1377       N  
ATOM  17709  CA  ALA E  86     -28.849 187.272-227.109  1.00132.42           C  
ANISOU17709  CA  ALA E  86    19165  18004  13142    674  -6185   1932       C  
ATOM  17710  C   ALA E  86     -28.062 188.486-227.611  1.00133.70           C  
ANISOU17710  C   ALA E  86    19523  18311  12966    893  -5770   1990       C  
ATOM  17711  O   ALA E  86     -26.854 188.589-227.386  1.00128.56           O  
ANISOU17711  O   ALA E  86    19116  17515  12216    982  -5432   1634       O  
ATOM  17712  CB  ALA E  86     -28.722 187.139-225.599  1.00125.45           C  
ANISOU17712  CB  ALA E  86    18161  16748  12756    768  -5896   1955       C  
ATOM  17713  N   GLN E  87     -28.757 189.399-228.287  1.00139.74           N  
ANISOU17713  N   GLN E  87    20161  19372  13561    973  -5800   2470       N  
ATOM  17714  CA  GLN E  87     -28.148 190.611-228.824  1.00142.01           C  
ANISOU17714  CA  GLN E  87    20625  19796  13538   1168  -5421   2612       C  
ATOM  17715  C   GLN E  87     -27.602 191.482-227.702  1.00137.44           C  
ANISOU17715  C   GLN E  87    20082  18894  13245   1376  -4846   2718       C  
ATOM  17716  O   GLN E  87     -26.579 192.137-227.876  1.00135.43           O  
ANISOU17716  O   GLN E  87    20072  18612  12773   1459  -4482   2569       O  
ATOM  17717  CB  GLN E  87     -29.175 191.405-229.642  1.00149.92           C  
ANISOU17717  CB  GLN E  87    21439  21154  14371   1241  -5575   3201       C  
ATOM  17718  CG  GLN E  87     -28.732 192.816-230.042  1.00153.93           C  
ANISOU17718  CG  GLN E  87    22095  21742  14649   1479  -5132   3492       C  
ATOM  17719  CD  GLN E  87     -27.925 192.849-231.331  1.00159.43           C  
ANISOU17719  CD  GLN E  87    23089  22729  14758   1418  -5185   3213       C  
ATOM  17720  OE1 GLN E  87     -27.869 191.864-232.070  1.00163.16           O  
ANISOU17720  OE1 GLN E  87    23650  23400  14945   1217  -5599   2849       O  
ATOM  17721  NE2 GLN E  87     -27.302 193.990-231.610  1.00159.72           N  
ANISOU17721  NE2 GLN E  87    23301  22783  14602   1589  -4753   3386       N  
ATOM  17722  N   SER E  88     -28.284 191.492-226.555  1.00137.39           N  
ANISOU17722  N   SER E  88    19836  18657  13710   1443  -4766   2980       N  
ATOM  17723  CA  SER E  88     -27.860 192.312-225.407  1.00135.84           C  
ANISOU17723  CA  SER E  88    19696  18138  13779   1629  -4234   3080       C  
ATOM  17724  C   SER E  88     -26.395 192.058-225.047  1.00132.16           C  
ANISOU17724  C   SER E  88    19509  17487  13219   1570  -3985   2525       C  
ATOM  17725  O   SER E  88     -25.597 192.993-224.960  1.00130.84           O  
ANISOU17725  O   SER E  88    19540  17242  12931   1659  -3572   2515       O  
ATOM  17726  CB  SER E  88     -28.731 192.051-224.174  1.00135.99           C  
ANISOU17726  CB  SER E  88    19435  17941  14295   1687  -4227   3333       C  
ATOM  17727  OG  SER E  88     -28.410 190.798-223.592  1.00135.19           O  
ANISOU17727  OG  SER E  88    19319  17679  14367   1512  -4425   2912       O  
ATOM  17728  N   THR E  89     -26.050 190.787-224.852  1.00130.71           N  
ANISOU17728  N   THR E  89    19334  17236  13093   1415  -4240   2085       N  
ATOM  17729  CA  THR E  89     -24.678 190.393-224.545  1.00127.02           C  
ANISOU17729  CA  THR E  89    19084  16643  12537   1378  -4046   1570       C  
ATOM  17730  C   THR E  89     -23.677 190.878-225.600  1.00127.57           C  
ANISOU17730  C   THR E  89    19403  16935  12135   1384  -3894   1374       C  
ATOM  17731  O   THR E  89     -22.533 191.212-225.280  1.00125.25           O  
ANISOU17731  O   THR E  89    19254  16567  11766   1408  -3552   1151       O  
ATOM  17732  CB  THR E  89     -24.553 188.865-224.427  1.00125.66           C  
ANISOU17732  CB  THR E  89    18903  16390  12451   1237  -4395   1151       C  
ATOM  17733  OG1 THR E  89     -24.688 188.265-225.722  1.00127.10           O  
ANISOU17733  OG1 THR E  89    19188  16819  12285   1121  -4774    968       O  
ATOM  17734  CG2 THR E  89     -25.633 188.310-223.512  1.00126.53           C  
ANISOU17734  CG2 THR E  89    18745  16316  13013   1195  -4593   1384       C  
ATOM  17735  N   PHE E  90     -24.116 190.916-226.856  1.00128.86           N  
ANISOU17735  N   PHE E  90    19597  17398  11968   1349  -4154   1479       N  
ATOM  17736  CA  PHE E  90     -23.280 191.416-227.940  1.00126.09           C  
ANISOU17736  CA  PHE E  90    19470  17302  11138   1368  -4012   1358       C  
ATOM  17737  C   PHE E  90     -23.121 192.934-227.858  1.00125.49           C  
ANISOU17737  C   PHE E  90    19441  17204  11036   1489  -3573   1752       C  
ATOM  17738  O   PHE E  90     -22.085 193.475-228.226  1.00124.71           O  
ANISOU17738  O   PHE E  90    19527  17183  10673   1495  -3278   1624       O  
ATOM  17739  CB  PHE E  90     -23.839 191.012-229.303  1.00127.66           C  
ANISOU17739  CB  PHE E  90    19704  17847  10954   1293  -4433   1367       C  
ATOM  17740  CG  PHE E  90     -23.084 191.601-230.454  1.00128.79           C  
ANISOU17740  CG  PHE E  90    20067  18290  10577   1334  -4273   1314       C  
ATOM  17741  CD1 PHE E  90     -21.829 191.121-230.794  1.00127.91           C  
ANISOU17741  CD1 PHE E  90    20172  18244  10185   1323  -4146    821       C  
ATOM  17742  CD2 PHE E  90     -23.619 192.643-231.189  1.00132.18           C  
ANISOU17742  CD2 PHE E  90    20477  18950  10797   1409  -4227   1790       C  
ATOM  17743  CE1 PHE E  90     -21.125 191.665-231.849  1.00129.22           C  
ANISOU17743  CE1 PHE E  90    20522  18713   9864   1366  -3973    799       C  
ATOM  17744  CE2 PHE E  90     -22.920 193.190-232.247  1.00135.00           C  
ANISOU17744  CE2 PHE E  90    21036  19591  10666   1445  -4066   1772       C  
ATOM  17745  CZ  PHE E  90     -21.669 192.699-232.577  1.00133.02           C  
ANISOU17745  CZ  PHE E  90    20994  19416  10133   1415  -3936   1272       C  
ATOM  17746  N   ASN E  91     -24.150 193.615-227.365  1.00127.02           N  
ANISOU17746  N   ASN E  91    19472  17279  11511   1590  -3517   2243       N  
ATOM  17747  CA  ASN E  91     -24.082 195.053-227.158  1.00128.23           C  
ANISOU17747  CA  ASN E  91    19712  17316  11694   1727  -3077   2627       C  
ATOM  17748  C   ASN E  91     -23.182 195.411-225.965  1.00128.02           C  
ANISOU17748  C   ASN E  91    19801  16949  11894   1713  -2657   2433       C  
ATOM  17749  O   ASN E  91     -22.533 196.462-225.959  1.00129.41           O  
ANISOU17749  O   ASN E  91    20165  17038  11967   1729  -2265   2527       O  
ATOM  17750  CB  ASN E  91     -25.490 195.631-226.971  1.00130.15           C  
ANISOU17750  CB  ASN E  91    19750  17528  12175   1890  -3126   3223       C  
ATOM  17751  CG  ASN E  91     -26.373 195.428-228.199  1.00137.65           C  
ANISOU17751  CG  ASN E  91    20563  18873  12863   1888  -3543   3482       C  
ATOM  17752  OD1 ASN E  91     -25.875 195.347-229.323  1.00141.27           O  
ANISOU17752  OD1 ASN E  91    21170  19620  12887   1813  -3660   3320       O  
ATOM  17753  ND2 ASN E  91     -27.686 195.346-227.988  1.00140.26           N  
ANISOU17753  ND2 ASN E  91    20597  19253  13441   1968  -3770   3898       N  
ATOM  17754  N   ASP E  92     -23.129 194.521-224.972  1.00126.25           N  
ANISOU17754  N   ASP E  92    19469  16541  11960   1660  -2753   2166       N  
ATOM  17755  CA  ASP E  92     -22.468 194.815-223.700  1.00121.88           C  
ANISOU17755  CA  ASP E  92    18985  15679  11646   1647  -2404   2030       C  
ATOM  17756  C   ASP E  92     -20.940 194.805-223.787  1.00120.48           C  
ANISOU17756  C   ASP E  92    18980  15557  11239   1519  -2198   1619       C  
ATOM  17757  O   ASP E  92     -20.255 195.151-222.826  1.00117.23           O  
ANISOU17757  O   ASP E  92    18638  14942  10961   1467  -1907   1503       O  
ATOM  17758  CB  ASP E  92     -22.918 193.837-222.606  1.00119.66           C  
ANISOU17758  CB  ASP E  92    18515  15215  11734   1643  -2580   1913       C  
ATOM  17759  CG  ASP E  92     -24.420 193.868-222.361  1.00121.76           C  
ANISOU17759  CG  ASP E  92    18558  15434  12270   1765  -2744   2359       C  
ATOM  17760  OD1 ASP E  92     -25.069 194.877-222.719  1.00124.63           O  
ANISOU17760  OD1 ASP E  92    18927  15825  12599   1903  -2606   2799       O  
ATOM  17761  OD2 ASP E  92     -24.956 192.884-221.804  1.00121.07           O1-
ANISOU17761  OD2 ASP E  92    18275  15288  12440   1731  -3001   2299       O1-
ATOM  17762  N   LEU E  93     -20.400 194.412-224.933  1.00124.77           N  
ANISOU17762  N   LEU E  93    19586  16401  11421   1466  -2346   1407       N  
ATOM  17763  CA  LEU E  93     -18.951 194.263-225.059  1.00127.50           C  
ANISOU17763  CA  LEU E  93    20038  16859  11546   1368  -2165   1025       C  
ATOM  17764  C   LEU E  93     -18.205 195.572-225.296  1.00131.08           C  
ANISOU17764  C   LEU E  93    20658  17333  11813   1307  -1756   1185       C  
ATOM  17765  O   LEU E  93     -16.998 195.653-225.044  1.00129.55           O  
ANISOU17765  O   LEU E  93    20511  17179  11532   1194  -1532    939       O  
ATOM  17766  CB  LEU E  93     -18.608 193.271-226.168  1.00129.87           C  
ANISOU17766  CB  LEU E  93    20361  17472  11514   1363  -2448    708       C  
ATOM  17767  CG  LEU E  93     -19.153 191.864-225.948  1.00128.47           C  
ANISOU17767  CG  LEU E  93    20073  17234  11505   1375  -2852    469       C  
ATOM  17768  CD1 LEU E  93     -19.220 191.115-227.268  1.00131.00           C  
ANISOU17768  CD1 LEU E  93    20483  17840  11451   1375  -3170    265       C  
ATOM  17769  CD2 LEU E  93     -18.302 191.114-224.931  1.00125.25           C  
ANISOU17769  CD2 LEU E  93    19618  16669  11303   1359  -2767    111       C  
ATOM  17770  N   GLN E  94     -18.921 196.585-225.777  1.00136.50           N  
ANISOU17770  N   GLN E  94    21422  17996  12446   1377  -1661   1619       N  
ATOM  17771  CA  GLN E  94     -18.313 197.858-226.161  1.00141.62           C  
ANISOU17771  CA  GLN E  94    22263  18643  12903   1315  -1285   1822       C  
ATOM  17772  C   GLN E  94     -17.615 198.576-225.004  1.00145.48           C  
ANISOU17772  C   GLN E  94    22859  18817  13599   1182   -908   1776       C  
ATOM  17773  O   GLN E  94     -16.427 198.907-225.093  1.00148.47           O  
ANISOU17773  O   GLN E  94    23321  19283  13807   1005   -678   1608       O  
ATOM  17774  CB  GLN E  94     -19.358 198.780-226.792  1.00140.97           C  
ANISOU17774  CB  GLN E  94    22244  18543  12776   1461  -1258   2349       C  
ATOM  17775  CG  GLN E  94     -18.795 200.111-227.239  1.00139.88           C  
ANISOU17775  CG  GLN E  94    22336  18364  12449   1402   -865   2602       C  
ATOM  17776  CD  GLN E  94     -17.584 199.950-228.132  1.00138.53           C  
ANISOU17776  CD  GLN E  94    22218  18536  11881   1255   -808   2349       C  
ATOM  17777  OE1 GLN E  94     -17.575 199.124-229.044  1.00138.64           O  
ANISOU17777  OE1 GLN E  94    22150  18911  11617   1299  -1093   2181       O  
ATOM  17778  NE2 GLN E  94     -16.547 200.735-227.869  1.00137.92           N  
ANISOU17778  NE2 GLN E  94    22285  18353  11765   1070   -433   2318       N  
ATOM  17779  N   ASP E  95     -18.352 198.818-223.924  1.00144.89           N  
ANISOU17779  N   ASP E  95    22779  18397  13875   1256   -846   1931       N  
ATOM  17780  CA  ASP E  95     -17.786 199.494-222.763  1.00144.23           C  
ANISOU17780  CA  ASP E  95    22838  17993  13969   1122   -510   1872       C  
ATOM  17781  C   ASP E  95     -16.676 198.647-222.144  1.00138.43           C  
ANISOU17781  C   ASP E  95    21991  17368  13239    949   -559   1406       C  
ATOM  17782  O   ASP E  95     -15.749 199.176-221.532  1.00139.28           O  
ANISOU17782  O   ASP E  95    22205  17375  13341    744   -300   1282       O  
ATOM  17783  CB  ASP E  95     -18.869 199.800-221.724  1.00147.41           C  
ANISOU17783  CB  ASP E  95    23261  18028  14722   1282   -443   2114       C  
ATOM  17784  CG  ASP E  95     -18.498 200.965-220.819  1.00149.68           C  
ANISOU17784  CG  ASP E  95    23830  17931  15109   1174    -22   2187       C  
ATOM  17785  OD1 ASP E  95     -18.073 202.015-221.347  1.00152.38           O  
ANISOU17785  OD1 ASP E  95    24407  18207  15283   1075    244   2346       O  
ATOM  17786  OD2 ASP E  95     -18.628 200.830-219.582  1.00147.79           O1-
ANISOU17786  OD2 ASP E  95    23600  17448  15104   1175     45   2082       O1-
ATOM  17787  N   LEU E  96     -16.772 197.333-222.316  1.00133.60           N  
ANISOU17787  N   LEU E  96    21169  16961  12632   1027   -899   1160       N  
ATOM  17788  CA  LEU E  96     -15.758 196.414-221.809  1.00130.00           C  
ANISOU17788  CA  LEU E  96    20585  16630  12178    928   -962    744       C  
ATOM  17789  C   LEU E  96     -14.425 196.611-222.522  1.00130.49           C  
ANISOU17789  C   LEU E  96    20676  16991  11912    777   -804    570       C  
ATOM  17790  O   LEU E  96     -13.398 196.840-221.878  1.00131.44           O  
ANISOU17790  O   LEU E  96    20784  17120  12036    595   -605    414       O  
ATOM  17791  CB  LEU E  96     -16.222 194.965-221.951  1.00127.63           C  
ANISOU17791  CB  LEU E  96    20103  16439  11952   1068  -1352    543       C  
ATOM  17792  CG  LEU E  96     -16.898 194.316-220.740  1.00122.53           C  
ANISOU17792  CG  LEU E  96    19335  15542  11679   1137  -1490    524       C  
ATOM  17793  CD1 LEU E  96     -18.099 195.125-220.264  1.00122.97           C  
ANISOU17793  CD1 LEU E  96    19443  15321  11959   1225  -1400    926       C  
ATOM  17794  CD2 LEU E  96     -17.306 192.895-221.083  1.00120.79           C  
ANISOU17794  CD2 LEU E  96    18970  15425  11502   1235  -1883    332       C  
ATOM  17795  N   ARG E  97     -14.449 196.516-223.851  1.00129.58           N  
ANISOU17795  N   ARG E  97    20583  17151  11500    847   -897    611       N  
ATOM  17796  CA  ARG E  97     -13.269 196.795-224.670  1.00129.70           C  
ANISOU17796  CA  ARG E  97    20623  17485  11170    731   -715    513       C  
ATOM  17797  C   ARG E  97     -12.733 198.202-224.399  1.00128.06           C  
ANISOU17797  C   ARG E  97    20567  17140  10948    504   -331    734       C  
ATOM  17798  O   ARG E  97     -11.515 198.425-224.364  1.00126.32           O  
ANISOU17798  O   ARG E  97    20306  17098  10591    306   -129    602       O  
ATOM  17799  CB  ARG E  97     -13.602 196.619-226.156  1.00133.45           C  
ANISOU17799  CB  ARG E  97    21148  18252  11306    863   -865    592       C  
ATOM  17800  CG  ARG E  97     -13.009 197.678-227.081  1.00136.46           C  
ANISOU17800  CG  ARG E  97    21658  18827  11365    756   -582    809       C  
ATOM  17801  CD  ARG E  97     -11.915 197.110-227.978  1.00138.78           C  
ANISOU17801  CD  ARG E  97    21882  19567  11281    762   -553    549       C  
ATOM  17802  NE  ARG E  97     -11.421 198.109-228.926  1.00142.59           N  
ANISOU17802  NE  ARG E  97    22476  20260  11440    665   -285    801       N  
ATOM  17803  CZ  ARG E  97     -10.480 197.882-229.838  1.00144.22           C  
ANISOU17803  CZ  ARG E  97    22640  20889  11267    672   -182    675       C  
ATOM  17804  NH1 ARG E  97      -9.918 196.685-229.939  1.00143.77           N1+
ANISOU17804  NH1 ARG E  97    22451  21074  11101    798   -314    282       N1+
ATOM  17805  NH2 ARG E  97     -10.103 198.857-230.653  1.00146.40           N  
ANISOU17805  NH2 ARG E  97    23018  21338  11271    570     77    960       N  
ATOM  17806  N   GLU E  98     -13.650 199.146-224.199  1.00129.04           N  
ANISOU17806  N   GLU E  98    20867  16940  11220    531   -227   1080       N  
ATOM  17807  CA  GLU E  98     -13.269 200.509-223.858  1.00133.43           C  
ANISOU17807  CA  GLU E  98    21641  17256  11800    316    140   1291       C  
ATOM  17808  C   GLU E  98     -12.451 200.529-222.569  1.00134.81           C  
ANISOU17808  C   GLU E  98    21790  17288  12145     79    272   1049       C  
ATOM  17809  O   GLU E  98     -11.409 201.178-222.498  1.00139.30           O  
ANISOU17809  O   GLU E  98    22418  17910  12599   -211    512   1016       O  
ATOM  17810  CB  GLU E  98     -14.501 201.396-223.733  1.00134.46           C  
ANISOU17810  CB  GLU E  98    21978  17009  12102    461    229   1693       C  
ATOM  17811  N   GLN E  99     -12.917 199.804-221.557  1.00132.28           N  
ANISOU17811  N   GLN E  99    21365  16811  12085    184    101    895       N  
ATOM  17812  CA  GLN E  99     -12.200 199.729-220.288  1.00132.18           C  
ANISOU17812  CA  GLN E  99    21313  16697  12213    -20    185    667       C  
ATOM  17813  C   GLN E  99     -10.849 199.045-220.442  1.00131.31           C  
ANISOU17813  C   GLN E  99    20963  17003  11926   -165    145    365       C  
ATOM  17814  O   GLN E  99      -9.872 199.445-219.810  1.00131.21           O  
ANISOU17814  O   GLN E  99    20938  17025  11892   -455    310    262       O  
ATOM  17815  CB  GLN E  99     -13.037 199.016-219.229  1.00133.18           C  
ANISOU17815  CB  GLN E  99    21361  16604  12636    161      3    597       C  
ATOM  17816  CG  GLN E  99     -14.185 199.853-218.698  1.00137.26           C  
ANISOU17816  CG  GLN E  99    22115  16682  13357    269    137    894       C  
ATOM  17817  CD  GLN E  99     -14.928 199.168-217.576  1.00137.70           C  
ANISOU17817  CD  GLN E  99    22073  16553  13695    431     -5    839       C  
ATOM  17818  OE1 GLN E  99     -14.569 198.065-217.160  1.00136.87           O  
ANISOU17818  OE1 GLN E  99    21735  16625  13643    444   -213    578       O  
ATOM  17819  NE2 GLN E  99     -15.973 199.818-217.076  1.00139.11           N  
ANISOU17819  NE2 GLN E  99    22428  16374  14054    578    127   1107       N  
ATOM  17820  N   ILE E 100     -10.801 198.014-221.280  1.00132.17           N  
ANISOU17820  N   ILE E 100    20884  17434  11900     40    -73    228       N  
ATOM  17821  CA  ILE E 100      -9.544 197.342-221.591  1.00133.94           C  
ANISOU17821  CA  ILE E 100    20881  18080  11929    -16    -78    -29       C  
ATOM  17822  C   ILE E 100      -8.527 198.344-222.120  1.00138.75           C  
ANISOU17822  C   ILE E 100    21535  18885  12297   -301    217     84       C  
ATOM  17823  O   ILE E 100      -7.426 198.471-221.577  1.00142.43           O  
ANISOU17823  O   ILE E 100    21865  19514  12738   -549    345    -30       O  
ATOM  17824  CB  ILE E 100      -9.724 196.239-222.653  1.00134.45           C  
ANISOU17824  CB  ILE E 100    20838  18425  11822    272   -311   -169       C  
ATOM  17825  CG1 ILE E 100     -10.747 195.204-222.192  1.00132.79           C  
ANISOU17825  CG1 ILE E 100    20586  18011  11858    511   -626   -271       C  
ATOM  17826  CG2 ILE E 100      -8.393 195.562-222.946  1.00134.11           C  
ANISOU17826  CG2 ILE E 100    20572  18811  11573    269   -263   -425       C  
ATOM  17827  CD1 ILE E 100     -10.319 194.446-220.974  1.00130.65           C  
ANISOU17827  CD1 ILE E 100    20142  17689  11810    505   -693   -495       C  
ATOM  17828  N   LEU E 101      -8.906 199.064-223.175  1.00138.48           N  
ANISOU17828  N   LEU E 101    21679  18852  12086   -279    317    337       N  
ATOM  17829  CA  LEU E 101      -8.003 200.027-223.805  1.00138.40           C  
ANISOU17829  CA  LEU E 101    21723  19026  11838   -547    606    493       C  
ATOM  17830  C   LEU E 101      -7.627 201.180-222.875  1.00135.56           C  
ANISOU17830  C   LEU E 101    21525  18361  11621   -934    853    604       C  
ATOM  17831  O   LEU E 101      -6.499 201.671-222.911  1.00137.45           O  
ANISOU17831  O   LEU E 101    21690  18804  11729  -1261   1051    606       O  
ATOM  17832  CB  LEU E 101      -8.609 200.570-225.101  1.00141.25           C  
ANISOU17832  CB  LEU E 101    22265  19420  11984   -417    655    783       C  
ATOM  17833  CG  LEU E 101      -8.929 199.538-226.184  1.00142.96           C  
ANISOU17833  CG  LEU E 101    22376  19972  11973    -85    415    673       C  
ATOM  17834  CD1 LEU E 101      -9.281 200.229-227.492  1.00146.80           C  
ANISOU17834  CD1 LEU E 101    23031  20575  12171    -25    506    986       C  
ATOM  17835  CD2 LEU E 101      -7.773 198.568-226.378  1.00143.51           C  
ANISOU17835  CD2 LEU E 101    22174  20490  11862    -54    392    348       C  
ATOM  17836  N   ARG E 102      -8.573 201.606-222.046  1.00132.33           N  
ANISOU17836  N   ARG E 102    21343  17466  11471   -903    846    697       N  
ATOM  17837  CA  ARG E 102      -8.325 202.694-221.108  1.00134.58           C  
ANISOU17837  CA  ARG E 102    21865  17388  11883  -1254   1078    768       C  
ATOM  17838  C   ARG E 102      -7.308 202.284-220.046  1.00138.55           C  
ANISOU17838  C   ARG E 102    22156  18051  12436  -1518   1042    477       C  
ATOM  17839  O   ARG E 102      -6.371 203.028-219.756  1.00143.19           O  
ANISOU17839  O   ARG E 102    22786  18668  12951  -1941   1229    481       O  
ATOM  17840  CB  ARG E 102      -9.627 203.152-220.458  1.00131.72           C  
ANISOU17840  CB  ARG E 102    21799  16480  11769  -1082   1094    924       C  
ATOM  17841  N   VAL E 103      -7.493 201.095-219.477  1.00137.63           N  
ANISOU17841  N   VAL E 103    21805  18050  12440  -1283    790    245       N  
ATOM  17842  CA  VAL E 103      -6.600 200.591-218.433  1.00138.29           C  
ANISOU17842  CA  VAL E 103    21655  18315  12573  -1474    724     -7       C  
ATOM  17843  C   VAL E 103      -5.207 200.248-218.964  1.00142.33           C  
ANISOU17843  C   VAL E 103    21827  19392  12860  -1633    760   -106       C  
ATOM  17844  O   VAL E 103      -4.197 200.579-218.337  1.00144.11           O  
ANISOU17844  O   VAL E 103    21934  19775  13045  -2007    845   -171       O  
ATOM  17845  CB  VAL E 103      -7.201 199.360-217.722  1.00134.58           C  
ANISOU17845  CB  VAL E 103    21024  17811  12300  -1143    453   -190       C  
ATOM  17846  CG1 VAL E 103      -6.188 198.742-216.771  1.00134.37           C  
ANISOU17846  CG1 VAL E 103    20709  18057  12287  -1296    375   -422       C  
ATOM  17847  CG2 VAL E 103      -8.466 199.749-216.976  1.00132.96           C  
ANISOU17847  CG2 VAL E 103    21111  17082  12327  -1027    452    -77       C  
ATOM  17848  N   LYS E 104      -5.154 199.586-220.117  1.00144.34           N  
ANISOU17848  N   LYS E 104    21921  19970  12951  -1351    696   -112       N  
ATOM  17849  CA  LYS E 104      -3.875 199.263-220.750  1.00147.86           C  
ANISOU17849  CA  LYS E 104    22046  20976  13157  -1431    775   -174       C  
ATOM  17850  C   LYS E 104      -3.192 200.511-221.313  1.00151.22           C  
ANISOU17850  C   LYS E 104    22566  21490  13402  -1831   1061     56       C  
ATOM  17851  O   LYS E 104      -1.988 200.501-221.580  1.00153.43           O  
ANISOU17851  O   LYS E 104    22559  22229  13509  -2030   1177     50       O  
ATOM  17852  CB  LYS E 104      -4.058 198.212-221.851  1.00148.28           C  
ANISOU17852  CB  LYS E 104    21967  21318  13053   -990    648   -265       C  
ATOM  17853  CG  LYS E 104      -3.965 196.780-221.352  1.00146.95           C  
ANISOU17853  CG  LYS E 104    21549  21294  12991   -683    416   -544       C  
ATOM  17854  CD  LYS E 104      -2.653 196.557-220.619  1.00148.64           C  
ANISOU17854  CD  LYS E 104    21417  21864  13196   -884    480   -650       C  
ATOM  17855  CE  LYS E 104      -2.608 195.197-219.946  1.00146.62           C  
ANISOU17855  CE  LYS E 104    20939  21682  13087   -574    262   -889       C  
ATOM  17856  NZ  LYS E 104      -1.365 195.028-219.142  1.00147.36           N1+
ANISOU17856  NZ  LYS E 104    20673  22140  13179   -766    312   -946       N1+
ATOM  17857  N   ASP E 105      -3.975 201.576-221.480  1.00149.80           N  
ANISOU17857  N   ASP E 105    22777  20867  13272  -1938   1185    283       N  
ATOM  17858  CA  ASP E 105      -3.494 202.854-222.004  1.00150.30           C  
ANISOU17858  CA  ASP E 105    23015  20895  13198  -2321   1469    542       C  
ATOM  17859  C   ASP E 105      -2.783 202.706-223.344  1.00150.08           C  
ANISOU17859  C   ASP E 105    22772  21389  12861  -2261   1582    648       C  
ATOM  17860  O   ASP E 105      -1.753 203.334-223.585  1.00154.76           O  
ANISOU17860  O   ASP E 105    23254  22233  13313  -2641   1791    771       O  
ATOM  17861  CB  ASP E 105      -2.594 203.552-220.989  1.00151.06           C  
ANISOU17861  CB  ASP E 105    23100  20937  13360  -2874   1585    502       C  
ATOM  17862  N   THR E 106      -3.336 201.869-224.213  1.00145.28           N  
ANISOU17862  N   THR E 106    22111  20953  12136  -1795   1441    601       N  
ATOM  17863  CA  THR E 106      -2.761 201.647-225.533  1.00147.36           C  
ANISOU17863  CA  THR E 106    22212  21715  12061  -1667   1546    679       C  
ATOM  17864  C   THR E 106      -3.847 201.238-226.518  1.00148.16           C  
ANISOU17864  C   THR E 106    22492  21761  12041  -1228   1404    727       C  
ATOM  17865  O   THR E 106      -5.031 201.483-226.283  1.00145.26           O  
ANISOU17865  O   THR E 106    22393  20947  11852  -1108   1288    816       O  
ATOM  17866  CB  THR E 106      -1.648 200.580-225.493  1.00146.39           C  
ANISOU17866  CB  THR E 106    21642  22156  11822  -1567   1506    430       C  
ATOM  17867  OG1 THR E 106      -1.377 200.111-226.821  1.00144.64           O  
ANISOU17867  OG1 THR E 106    21318  22377  11260  -1281   1569    449       O  
ATOM  17868  CG2 THR E 106      -2.069 199.410-224.626  1.00144.70           C  
ANISOU17868  CG2 THR E 106    21323  21827  11829  -1278   1216    117       C  
ATOM  17869  N   ASP E 107      -3.443 200.619-227.621  1.00152.91           N  
ANISOU17869  N   ASP E 107    22940  22839  12321   -990   1414    676       N  
ATOM  17870  CA  ASP E 107      -4.388 200.205-228.648  1.00156.60           C  
ANISOU17870  CA  ASP E 107    23576  23323  12603   -611   1257    705       C  
ATOM  17871  C   ASP E 107      -3.990 198.870-229.261  1.00159.98           C  
ANISOU17871  C   ASP E 107    23798  24197  12791   -259   1129    400       C  
ATOM  17872  O   ASP E 107      -4.811 198.195-229.882  1.00161.33           O  
ANISOU17872  O   ASP E 107    24096  24356  12846     68    903    299       O  
ATOM  17873  CB  ASP E 107      -4.502 201.274-229.726  1.00160.77           C  
ANISOU17873  CB  ASP E 107    24309  23904  12874   -710   1476   1088       C  
ATOM  17874  N   ASP E 108      -2.728 198.492-229.086  1.00163.61           N  
ANISOU17874  N   ASP E 108    23946  25050  13170   -327   1274    258       N  
ATOM  17875  CA  ASP E 108      -2.232 197.232-229.632  1.00165.94           C  
ANISOU17875  CA  ASP E 108    24056  25760  13235     42   1211    -34       C  
ATOM  17876  C   ASP E 108      -2.283 196.130-228.576  1.00163.16           C  
ANISOU17876  C   ASP E 108    23556  25261  13175    208    979   -364       C  
ATOM  17877  O   ASP E 108      -1.258 195.555-228.207  1.00163.49           O  
ANISOU17877  O   ASP E 108    23288  25616  13217    252   1063   -517       O  
ATOM  17878  CB  ASP E 108      -0.810 197.395-230.173  1.00168.97           C  
ANISOU17878  CB  ASP E 108    24152  26723  13328    -49   1539     45       C  
ATOM  17879  CG  ASP E 108      -0.426 196.292-231.140  1.00170.25           C  
ANISOU17879  CG  ASP E 108    24234  27324  13130    398   1549   -189       C  
ATOM  17880  OD1 ASP E 108      -1.335 195.712-231.771  1.00169.21           O  
ANISOU17880  OD1 ASP E 108    24367  27063  12864    707   1333   -334       O  
ATOM  17881  OD2 ASP E 108       0.782 196.010-231.272  1.00173.00           O1-
ANISOU17881  OD2 ASP E 108    24259  28153  13321    439   1776   -223       O1-
ATOM  17882  N   VAL E 109      -3.490 195.845-228.099  1.00159.59           N  
ANISOU17882  N   VAL E 109    23310  24350  12976    311    693   -439       N  
ATOM  17883  CA  VAL E 109      -3.699 194.839-227.069  1.00156.73           C  
ANISOU17883  CA  VAL E 109    22847  23788  12918    460    459   -710       C  
ATOM  17884  C   VAL E 109      -4.185 193.531-227.682  1.00158.21           C  
ANISOU17884  C   VAL E 109    23120  24007  12987    883    218   -994       C  
ATOM  17885  O   VAL E 109      -5.121 193.534-228.482  1.00161.58           O  
ANISOU17885  O   VAL E 109    23796  24321  13276    999     69   -952       O  
ATOM  17886  CB  VAL E 109      -4.739 195.318-226.046  1.00153.63           C  
ANISOU17886  CB  VAL E 109    22616  22853  12903    295    306   -602       C  
ATOM  17887  CG1 VAL E 109      -4.969 194.262-224.979  1.00151.32           C  
ANISOU17887  CG1 VAL E 109    22212  22368  12915    451     72   -854       C  
ATOM  17888  CG2 VAL E 109      -4.296 196.627-225.420  1.00154.53           C  
ANISOU17888  CG2 VAL E 109    22726  22866  13121   -137    544   -358       C  
ATOM  17889  N   PRO E 110      -3.539 192.409-227.317  1.00156.45           N  
ANISOU17889  N   PRO E 110    22699  23938  12807   1108    177  -1276       N  
ATOM  17890  CA  PRO E 110      -3.965 191.080-227.771  1.00155.06           C  
ANISOU17890  CA  PRO E 110    22645  23715  12555   1498    -54  -1588       C  
ATOM  17891  C   PRO E 110      -5.400 190.803-227.341  1.00148.99           C  
ANISOU17891  C   PRO E 110    22093  22444  12071   1508   -404  -1611       C  
ATOM  17892  O   PRO E 110      -5.677 190.692-226.147  1.00146.84           O  
ANISOU17892  O   PRO E 110    21734  21882  12177   1417   -510  -1606       O  
ATOM  17893  CB  PRO E 110      -3.002 190.139-227.045  1.00155.82           C  
ANISOU17893  CB  PRO E 110    22463  23966  12777   1676     -2  -1806       C  
ATOM  17894  CG  PRO E 110      -1.795 190.972-226.781  1.00157.50           C  
ANISOU17894  CG  PRO E 110    22368  24550  12927   1426    319  -1605       C  
ATOM  17895  CD  PRO E 110      -2.318 192.346-226.498  1.00155.76           C  
ANISOU17895  CD  PRO E 110    22260  24100  12822   1004    356  -1300       C  
ATOM  17896  N   MET E 111      -6.302 190.698-228.310  1.00145.63           N  
ANISOU17896  N   MET E 111    21929  21953  11450   1609   -582  -1616       N  
ATOM  17897  CA  MET E 111      -7.725 190.601-228.013  1.00138.39           C  
ANISOU17897  CA  MET E 111    21180  20617  10783   1577   -906  -1554       C  
ATOM  17898  C   MET E 111      -8.479 189.862-229.112  1.00139.26           C  
ANISOU17898  C   MET E 111    21533  20744  10634   1773  -1177  -1719       C  
ATOM  17899  O   MET E 111      -8.138 189.965-230.292  1.00143.42           O  
ANISOU17899  O   MET E 111    22171  21597  10724   1861  -1078  -1747       O  
ATOM  17900  CB  MET E 111      -8.308 192.003-227.827  1.00134.48           C  
ANISOU17900  CB  MET E 111    20739  19964  10392   1306   -814  -1156       C  
ATOM  17901  CG  MET E 111      -9.780 192.039-227.470  1.00130.89           C  
ANISOU17901  CG  MET E 111    20407  19114  10211   1287  -1102  -1016       C  
ATOM  17902  SD  MET E 111     -10.418 193.720-227.518  1.00166.60           S  
ANISOU17902  SD  MET E 111    25041  23484  14774   1061   -933   -526       S  
ATOM  17903  CE  MET E 111      -9.277 194.534-226.404  1.00105.57           C  
ANISOU17903  CE  MET E 111    17163  15723   7224    798   -573   -465       C  
ATOM  17904  N   ILE E 112      -9.507 189.118-228.719  1.00135.79           N  
ANISOU17904  N   ILE E 112    21178  19966  10452   1821  -1525  -1821       N  
ATOM  17905  CA  ILE E 112     -10.320 188.385-229.678  1.00137.94           C  
ANISOU17905  CA  ILE E 112    21688  20219  10503   1941  -1844  -1985       C  
ATOM  17906  C   ILE E 112     -11.810 188.454-229.315  1.00135.20           C  
ANISOU17906  C   ILE E 112    21386  19531  10453   1815  -2186  -1792       C  
ATOM  17907  O   ILE E 112     -12.190 188.354-228.141  1.00131.97           O  
ANISOU17907  O   ILE E 112    20845  18812  10487   1747  -2253  -1719       O  
ATOM  17908  CB  ILE E 112      -9.824 186.920-229.830  1.00115.77           C  
ANISOU17908  CB  ILE E 112    18966  17411   7612   2196  -1942  -2444       C  
ATOM  17909  CG1 ILE E 112     -10.613 186.170-230.903  1.00118.35           C  
ANISOU17909  CG1 ILE E 112    19600  17717   7650   2279  -2279  -2657       C  
ATOM  17910  CG2 ILE E 112      -9.882 186.186-228.506  1.00113.29           C  
ANISOU17910  CG2 ILE E 112    18511  16751   7783   2221  -2044  -2551       C  
ATOM  17911  CD1 ILE E 112     -10.163 184.735-231.082  1.00120.69           C  
ANISOU17911  CD1 ILE E 112    20062  17940   7856   2536  -2363  -3130       C  
ATOM  17912  N   LEU E 113     -12.639 188.664-230.334  1.00135.27           N  
ANISOU17912  N   LEU E 113    21561  19640  10196   1788  -2390  -1677       N  
ATOM  17913  CA  LEU E 113     -14.086 188.721-230.171  1.00131.19           C  
ANISOU17913  CA  LEU E 113    21054  18885   9907   1682  -2731  -1455       C  
ATOM  17914  C   LEU E 113     -14.697 187.374-230.541  1.00131.29           C  
ANISOU17914  C   LEU E 113    21215  18788   9880   1734  -3152  -1779       C  
ATOM  17915  O   LEU E 113     -14.614 186.941-231.689  1.00135.30           O  
ANISOU17915  O   LEU E 113    21939  19520   9949   1802  -3277  -1993       O  
ATOM  17916  CB  LEU E 113     -14.677 189.823-231.050  1.00131.30           C  
ANISOU17916  CB  LEU E 113    21130  19100   9658   1608  -2720  -1071       C  
ATOM  17917  CG  LEU E 113     -16.189 190.023-230.945  1.00128.30           C  
ANISOU17917  CG  LEU E 113    20707  18547   9494   1520  -3047   -753       C  
ATOM  17918  CD1 LEU E 113     -16.556 190.434-229.534  1.00122.52           C  
ANISOU17918  CD1 LEU E 113    19784  17464   9306   1458  -2944   -524       C  
ATOM  17919  CD2 LEU E 113     -16.681 191.050-231.957  1.00130.19           C  
ANISOU17919  CD2 LEU E 113    21014  19042   9409   1497  -3031   -369       C  
ATOM  17920  N   VAL E 114     -15.312 186.718-229.563  1.00127.05           N  
ANISOU17920  N   VAL E 114    20584  17899   9791   1689  -3368  -1814       N  
ATOM  17921  CA  VAL E 114     -15.834 185.371-229.751  1.00127.60           C  
ANISOU17921  CA  VAL E 114    20800  17789   9894   1699  -3760  -2133       C  
ATOM  17922  C   VAL E 114     -17.350 185.289-229.594  1.00129.82           C  
ANISOU17922  C   VAL E 114    21014  17886  10427   1519  -4165  -1881       C  
ATOM  17923  O   VAL E 114     -17.886 185.552-228.517  1.00124.73           O  
ANISOU17923  O   VAL E 114    20151  17008  10234   1451  -4157  -1616       O  
ATOM  17924  CB  VAL E 114     -15.186 184.381-228.768  1.00121.71           C  
ANISOU17924  CB  VAL E 114    20009  16775   9460   1812  -3693  -2431       C  
ATOM  17925  CG1 VAL E 114     -15.684 182.965-229.041  1.00124.04           C  
ANISOU17925  CG1 VAL E 114    20520  16837   9773   1817  -4083  -2779       C  
ATOM  17926  CG2 VAL E 114     -13.672 184.452-228.867  1.00118.77           C  
ANISOU17926  CG2 VAL E 114    19636  16630   8860   2005  -3288  -2636       C  
ATOM  17927  N   GLY E 115     -18.030 184.913-230.673  1.00136.56           N  
ANISOU17927  N   GLY E 115    22047  18872  10966   1439  -4519  -1960       N  
ATOM  17928  CA  GLY E 115     -19.464 184.695-230.641  1.00139.88           C  
ANISOU17928  CA  GLY E 115    22383  19177  11590   1244  -4958  -1736       C  
ATOM  17929  C   GLY E 115     -19.785 183.234-230.405  1.00143.66           C  
ANISOU17929  C   GLY E 115    22984  19347  12251   1162  -5313  -2095       C  
ATOM  17930  O   GLY E 115     -19.952 182.466-231.354  1.00150.67           O  
ANISOU17930  O   GLY E 115    24147  20295  12806   1095  -5619  -2407       O  
ATOM  17931  N   ASN E 116     -19.870 182.852-229.135  1.00139.13           N  
ANISOU17931  N   ASN E 116    22233  18432  12199   1160  -5269  -2052       N  
ATOM  17932  CA  ASN E 116     -20.115 181.467-228.756  1.00139.04           C  
ANISOU17932  CA  ASN E 116    22332  18067  12430   1089  -5559  -2359       C  
ATOM  17933  C   ASN E 116     -21.495 180.964-229.172  1.00141.17           C  
ANISOU17933  C   ASN E 116    22608  18278  12753    800  -6103  -2256       C  
ATOM  17934  O   ASN E 116     -22.347 181.745-229.602  1.00143.60           O  
ANISOU17934  O   ASN E 116    22759  18833  12969    675  -6250  -1875       O  
ATOM  17935  CB  ASN E 116     -19.935 181.292-227.248  1.00135.43           C  
ANISOU17935  CB  ASN E 116    21645  17293  12519   1152  -5369  -2252       C  
ATOM  17936  CG  ASN E 116     -19.520 179.886-226.873  1.00136.30           C  
ANISOU17936  CG  ASN E 116    21938  17057  12794   1212  -5468  -2666       C  
ATOM  17937  OD1 ASN E 116     -18.789 179.227-227.612  1.00138.69           O  
ANISOU17937  OD1 ASN E 116    22552  17377  12765   1336  -5455  -3098       O  
ATOM  17938  ND2 ASN E 116     -19.990 179.414-225.726  1.00134.84           N  
ANISOU17938  ND2 ASN E 116    21572  16546  13114   1145  -5549  -2524       N  
ATOM  17939  N   LYS E 117     -21.695 179.655-229.040  1.00140.27           N  
ANISOU17939  N   LYS E 117    22672  17834  12789    692  -6398  -2581       N  
ATOM  17940  CA  LYS E 117     -22.966 179.002-229.350  1.00141.15           C  
ANISOU17940  CA  LYS E 117    22795  17844  12991    356  -6951  -2523       C  
ATOM  17941  C   LYS E 117     -23.355 179.160-230.815  1.00148.03           C  
ANISOU17941  C   LYS E 117    23880  19067  13298    209  -7256  -2606       C  
ATOM  17942  O   LYS E 117     -24.517 179.412-231.136  1.00150.89           O  
ANISOU17942  O   LYS E 117    24060  19599  13672    -53  -7624  -2274       O  
ATOM  17943  CB  LYS E 117     -24.085 179.524-228.440  1.00134.76           C  
ANISOU17943  CB  LYS E 117    21529  17001  12672    205  -7043  -1943       C  
ATOM  17944  CG  LYS E 117     -23.802 179.368-226.960  1.00126.58           C  
ANISOU17944  CG  LYS E 117    20285  15637  12172    331  -6766  -1835       C  
ATOM  17945  CD  LYS E 117     -24.842 180.094-226.133  1.00123.51           C  
ANISOU17945  CD  LYS E 117    19456  15286  12188    247  -6769  -1234       C  
ATOM  17946  CE  LYS E 117     -24.541 179.992-224.646  1.00120.57           C  
ANISOU17946  CE  LYS E 117    18897  14619  12297    384  -6473  -1126       C  
ATOM  17947  NZ  LYS E 117     -25.409 180.900-223.840  1.00118.37           N1+
ANISOU17947  NZ  LYS E 117    18219  14411  12346    384  -6360   -541       N1+
ATOM  17948  N   CYS E 118     -22.377 179.001-231.702  1.00151.39           N  
ANISOU17948  N   CYS E 118    24677  19629  13214    388  -7099  -3033       N  
ATOM  17949  CA  CYS E 118     -22.627 179.095-233.136  1.00158.62           C  
ANISOU17949  CA  CYS E 118    25854  20897  13519    274  -7365  -3166       C  
ATOM  17950  C   CYS E 118     -23.145 177.770-233.691  1.00166.34           C  
ANISOU17950  C   CYS E 118    27195  21638  14370     -4  -7877  -3590       C  
ATOM  17951  O   CYS E 118     -23.164 177.558-234.904  1.00173.76           O  
ANISOU17951  O   CYS E 118    28341  22810  14869    -96  -7940  -3800       O  
ATOM  17952  CB  CYS E 118     -21.363 179.534-233.881  1.00159.08           C  
ANISOU17952  CB  CYS E 118    26155  21238  13049    593  -6946  -3418       C  
ATOM  17953  SG  CYS E 118     -20.057 178.289-233.971  1.00239.59           S  
ANISOU17953  SG  CYS E 118    36824  31129  23080    864  -6728  -4143       S  
ATOM  17954  N   ASP E 119     -23.566 176.884-232.792  1.00164.72           N  
ANISOU17954  N   ASP E 119    26940  20970  14678   -160  -8072  -3641       N  
ATOM  17955  CA  ASP E 119     -24.136 175.599-233.177  1.00171.06           C  
ANISOU17955  CA  ASP E 119    27983  21475  15536   -482  -8448  -3958       C  
ATOM  17956  C   ASP E 119     -25.660 175.665-233.168  1.00174.19           C  
ANISOU17956  C   ASP E 119    28062  21972  16151   -937  -8969  -3538       C  
ATOM  17957  O   ASP E 119     -26.338 174.742-233.629  1.00181.54           O  
ANISOU17957  O   ASP E 119    29121  22757  17099  -1293  -9321  -3712       O  
ATOM  17958  CB  ASP E 119     -23.636 174.485-232.249  1.00170.48           C  
ANISOU17958  CB  ASP E 119    28103  20801  15869   -383  -8362  -4286       C  
ATOM  17959  CG  ASP E 119     -24.075 174.678-230.804  1.00165.19           C  
ANISOU17959  CG  ASP E 119    27015  19906  15845   -415  -8358  -3865       C  
ATOM  17960  OD1 ASP E 119     -23.528 175.572-230.126  1.00159.54           O  
ANISOU17960  OD1 ASP E 119    25986  19342  15289   -123  -7900  -3580       O  
ATOM  17961  OD2 ASP E 119     -24.955 173.921-230.337  1.00166.42           O1-
ANISOU17961  OD2 ASP E 119    27104  19738  16388   -742  -8730  -3786       O1-
ATOM  17962  N   LEU E 120     -26.189 176.767-232.645  1.00168.77           N  
ANISOU17962  N   LEU E 120    26948  21545  15630   -915  -8996  -2962       N  
ATOM  17963  CA  LEU E 120     -27.630 176.984-232.582  1.00170.82           C  
ANISOU17963  CA  LEU E 120    26809  21978  16117  -1286  -9439  -2454       C  
ATOM  17964  C   LEU E 120     -28.070 177.995-233.638  1.00174.44           C  
ANISOU17964  C   LEU E 120    27105  23044  16129  -1311  -9496  -2131       C  
ATOM  17965  O   LEU E 120     -28.518 179.094-233.310  1.00171.16           O  
ANISOU17965  O   LEU E 120    26288  22905  15838  -1212  -9411  -1553       O  
ATOM  17966  CB  LEU E 120     -28.027 177.469-231.185  1.00163.99           C  
ANISOU17966  CB  LEU E 120    25415  20977  15917  -1198  -9203  -1917       C  
ATOM  17967  CG  LEU E 120     -27.594 176.575-230.020  1.00160.22           C  
ANISOU17967  CG  LEU E 120    24993  19937  15944  -1132  -9032  -2132       C  
ATOM  17968  CD1 LEU E 120     -27.974 177.191-228.682  1.00154.10           C  
ANISOU17968  CD1 LEU E 120    23699  19102  15749  -1016  -8760  -1577       C  
ATOM  17969  CD2 LEU E 120     -28.200 175.189-230.162  1.00165.86           C  
ANISOU17969  CD2 LEU E 120    25941  20294  16783  -1546  -9561  -2423       C  
ATOM  17970  N   GLU E 121     -27.941 177.615-234.906  1.00181.43           N  
ANISOU17970  N   GLU E 121    28280  24132  16521  -1418  -9572  -2485       N  
ATOM  17971  CA  GLU E 121     -28.250 178.509-236.018  1.00186.06           C  
ANISOU17971  CA  GLU E 121    28761  25318  16617  -1419  -9614  -2231       C  
ATOM  17972  C   GLU E 121     -29.747 178.794-236.111  1.00191.27           C  
ANISOU17972  C   GLU E 121    28952  26275  17446  -1755 -10058  -1671       C  
ATOM  17973  O   GLU E 121     -30.160 179.830-236.633  1.00193.12           O  
ANISOU17973  O   GLU E 121    28931  27004  17441  -1684 -10065  -1222       O  
ATOM  17974  CB  GLU E 121     -27.743 177.912-237.335  1.00192.15           C  
ANISOU17974  CB  GLU E 121    29969  26226  16813  -1460  -9599  -2782       C  
ATOM  17975  CG  GLU E 121     -27.720 178.888-238.506  1.00194.33           C  
ANISOU17975  CG  GLU E 121    30207  27128  16500  -1360  -9529  -2587       C  
ATOM  17976  CD  GLU E 121     -26.582 179.888-238.414  1.00187.92           C  
ANISOU17976  CD  GLU E 121    29469  26449  15482   -908  -8997  -2519       C  
ATOM  17977  OE1 GLU E 121     -25.620 179.630-237.658  1.00182.54           O  
ANISOU17977  OE1 GLU E 121    28959  25391  15008   -662  -8660  -2789       O  
ATOM  17978  OE2 GLU E 121     -26.648 180.933-239.098  1.00187.73           O1-
ANISOU17978  OE2 GLU E 121    29325  26915  15090   -799  -8913  -2180       O1-
ATOM  17979  N   ASP E 122     -30.555 177.871-235.600  1.00194.37           N  
ANISOU17979  N   ASP E 122    29217  26370  18263  -2110 -10409  -1670       N  
ATOM  17980  CA  ASP E 122     -32.005 178.030-235.615  1.00197.79           C  
ANISOU17980  CA  ASP E 122    29152  27083  18916  -2446 -10820  -1125       C  
ATOM  17981  C   ASP E 122     -32.446 179.030-234.549  1.00190.80           C  
ANISOU17981  C   ASP E 122    27755  26269  18473  -2257 -10689   -427       C  
ATOM  17982  O   ASP E 122     -33.578 179.515-234.572  1.00193.59           O  
ANISOU17982  O   ASP E 122    27614  26964  18977  -2397 -10903    160       O  
ATOM  17983  CB  ASP E 122     -32.698 176.683-235.393  1.00203.32           C  
ANISOU17983  CB  ASP E 122    29886  27425  19941  -2911 -11216  -1342       C  
ATOM  17984  CG  ASP E 122     -32.714 176.267-233.932  1.00200.07           C  
ANISOU17984  CG  ASP E 122    29336  26495  20188  -2909 -11162  -1227       C  
ATOM  17985  OD1 ASP E 122     -31.678 175.773-233.435  1.00197.40           O  
ANISOU17985  OD1 ASP E 122    29379  25697  19927  -2698 -10897  -1673       O  
ATOM  17986  OD2 ASP E 122     -33.767 176.431-233.279  1.00200.06           O1-
ANISOU17986  OD2 ASP E 122    28820  26567  20625  -3102 -11370   -671       O1-
ATOM  17987  N   GLU E 123     -31.542 179.333-233.620  1.00181.01           N  
ANISOU17987  N   GLU E 123    26630  24714  17431  -1917 -10313   -489       N  
ATOM  17988  CA  GLU E 123     -31.835 180.248-232.520  1.00172.15           C  
ANISOU17988  CA  GLU E 123    25061  23591  16759  -1687 -10065    119       C  
ATOM  17989  C   GLU E 123     -30.928 181.474-232.544  1.00163.13           C  
ANISOU17989  C   GLU E 123    23961  22603  15418  -1211  -9452    228       C  
ATOM  17990  O   GLU E 123     -30.910 182.257-231.596  1.00157.20           O  
ANISOU17990  O   GLU E 123    22907  21770  15051   -946  -9030    620       O  
ATOM  17991  CB  GLU E 123     -31.680 179.535-231.178  1.00169.81           C  
ANISOU17991  CB  GLU E 123    24692  22749  17080  -1682  -9894     16       C  
ATOM  17992  CG  GLU E 123     -32.459 178.242-231.068  1.00176.89           C  
ANISOU17992  CG  GLU E 123    25593  23399  18218  -2167 -10455   -126       C  
ATOM  17993  CD  GLU E 123     -32.116 177.471-229.813  1.00176.53           C  
ANISOU17993  CD  GLU E 123    25568  22783  18723  -2125 -10245   -293       C  
ATOM  17994  OE1 GLU E 123     -32.422 176.261-229.756  1.00181.19           O  
ANISOU17994  OE1 GLU E 123    26327  23046  19471  -2490 -10633   -571       O  
ATOM  17995  OE2 GLU E 123     -31.539 178.075-228.884  1.00171.32           O1-
ANISOU17995  OE2 GLU E 123    24770  21996  18327  -1739  -9697   -143       O1-
ATOM  17996  N   ARG E 124     -30.173 181.632-233.626  1.00162.02           N  
ANISOU17996  N   ARG E 124    24216  22677  14667  -1116  -9401   -124       N  
ATOM  17997  CA  ARG E 124     -29.257 182.758-233.765  1.00156.43           C  
ANISOU17997  CA  ARG E 124    23581  22128  13728   -713  -8838    -41       C  
ATOM  17998  C   ARG E 124     -30.002 184.083-233.856  1.00153.56           C  
ANISOU17998  C   ARG E 124    22808  22148  13390   -584  -8743    694       C  
ATOM  17999  O   ARG E 124     -31.039 184.184-234.508  1.00158.78           O  
ANISOU17999  O   ARG E 124    23265  23171  13892   -792  -9185   1034       O  
ATOM  18000  CB  ARG E 124     -28.370 182.584-235.001  1.00159.01           C  
ANISOU18000  CB  ARG E 124    24406  22654  13359   -662  -8838   -546       C  
ATOM  18001  CG  ARG E 124     -27.405 183.738-235.231  1.00155.35           C  
ANISOU18001  CG  ARG E 124    24012  22385  12630   -285  -8268   -442       C  
ATOM  18002  CD  ARG E 124     -26.821 183.729-236.636  1.00159.14           C  
ANISOU18002  CD  ARG E 124    24899  23213  12355   -257  -8329   -776       C  
ATOM  18003  NE  ARG E 124     -25.845 182.662-236.837  1.00159.56           N  
ANISOU18003  NE  ARG E 124    25409  23012  12203   -234  -8275  -1506       N  
ATOM  18004  CZ  ARG E 124     -24.571 182.738-236.467  1.00155.00           C  
ANISOU18004  CZ  ARG E 124    25001  22256  11634     64  -7759  -1792       C  
ATOM  18005  NH1 ARG E 124     -24.120 183.828-235.863  1.00143.65           N1+
ANISOU18005  NH1 ARG E 124    23317  20849  10416    307  -7259  -1430       N1+
ATOM  18006  NH2 ARG E 124     -23.751 181.721-236.693  1.00156.80           N  
ANISOU18006  NH2 ARG E 124    25607  22273  11697    111  -7693  -2419       N  
ATOM  18007  N   VAL E 125     -29.464 185.096-233.191  1.00148.17           N  
ANISOU18007  N   VAL E 125    22016  21378  12904   -239  -8164    943       N  
ATOM  18008  CA  VAL E 125     -30.020 186.436-233.246  1.00148.71           C  
ANISOU18008  CA  VAL E 125    21773  21735  12994    -45  -7969   1619       C  
ATOM  18009  C   VAL E 125     -28.992 187.376-233.857  1.00147.74           C  
ANISOU18009  C   VAL E 125    21914  21774  12445    224  -7529   1558       C  
ATOM  18010  O   VAL E 125     -29.289 188.125-234.789  1.00150.46           O  
ANISOU18010  O   VAL E 125    22236  22525  12407    280  -7590   1882       O  
ATOM  18011  CB  VAL E 125     -30.383 186.939-231.844  1.00147.08           C  
ANISOU18011  CB  VAL E 125    21215  21244  13426    125  -7634   2035       C  
ATOM  18012  CG1 VAL E 125     -30.845 188.386-231.905  1.00149.71           C  
ANISOU18012  CG1 VAL E 125    21303  21816  13764    390  -7351   2707       C  
ATOM  18013  CG2 VAL E 125     -31.452 186.053-231.228  1.00147.52           C  
ANISOU18013  CG2 VAL E 125    20959  21175  13915   -140  -8049   2171       C  
ATOM  18014  N   VAL E 126     -27.779 187.326-233.317  1.00142.60           N  
ANISOU18014  N   VAL E 126    21494  20821  11866    383  -7087   1169       N  
ATOM  18015  CA  VAL E 126     -26.670 188.121-233.824  1.00139.96           C  
ANISOU18015  CA  VAL E 126    21408  20616  11155    602  -6646   1067       C  
ATOM  18016  C   VAL E 126     -26.080 187.481-235.067  1.00143.90           C  
ANISOU18016  C   VAL E 126    22286  21358  11032    516  -6856    573       C  
ATOM  18017  O   VAL E 126     -25.561 186.368-235.013  1.00147.15           O  
ANISOU18017  O   VAL E 126    22934  21566  11411    427  -6974      6       O  
ATOM  18018  CB  VAL E 126     -25.541 188.240-232.787  1.00131.38           C  
ANISOU18018  CB  VAL E 126    20402  19158  10357    772  -6120    821       C  
ATOM  18019  CG1 VAL E 126     -24.377 189.031-233.364  1.00129.53           C  
ANISOU18019  CG1 VAL E 126    20401  19093   9723    949  -5687    728       C  
ATOM  18020  CG2 VAL E 126     -26.051 188.881-231.510  1.00128.20           C  
ANISOU18020  CG2 VAL E 126    19685  18494  10531    870  -5875   1263       C  
ATOM  18021  N   GLY E 127     -26.153 188.189-236.187  1.00146.16           N  
ANISOU18021  N   GLY E 127    22647  22074  10813    566  -6883    797       N  
ATOM  18022  CA  GLY E 127     -25.533 187.721-237.409  1.00151.15           C  
ANISOU18022  CA  GLY E 127    23663  22979  10787    527  -7015    354       C  
ATOM  18023  C   GLY E 127     -24.027 187.658-237.261  1.00151.41           C  
ANISOU18023  C   GLY E 127    23968  22857  10705    721  -6520    -92       C  
ATOM  18024  O   GLY E 127     -23.449 188.301-236.384  1.00146.41           O  
ANISOU18024  O   GLY E 127    23210  22003  10415    883  -6048     51       O  
ATOM  18025  N   LYS E 128     -23.387 186.870-238.116  1.00159.10           N  
ANISOU18025  N   LYS E 128    25315  23955  11180    702  -6629   -634       N  
ATOM  18026  CA  LYS E 128     -21.936 186.760-238.104  1.00160.66           C  
ANISOU18026  CA  LYS E 128    25753  24081  11208    911  -6164  -1047       C  
ATOM  18027  C   LYS E 128     -21.325 188.065-238.589  1.00163.61           C  
ANISOU18027  C   LYS E 128    26104  24773  11288   1096  -5716   -702       C  
ATOM  18028  O   LYS E 128     -20.279 188.487-238.102  1.00157.79           O  
ANISOU18028  O   LYS E 128    25352  23928  10671   1257  -5216   -752       O  
ATOM  18029  CB  LYS E 128     -21.488 185.604-238.982  1.00165.85           C  
ANISOU18029  CB  LYS E 128    26837  24812  11365    882  -6385  -1686       C  
ATOM  18030  N   GLU E 129     -22.000 188.699-239.547  1.00171.94           N  
ANISOU18030  N   GLU E 129    27145  26227  11957   1052  -5914   -329       N  
ATOM  18031  CA  GLU E 129     -21.537 189.951-240.141  1.00174.90           C  
ANISOU18031  CA  GLU E 129    27521  26921  12011   1210  -5529     54       C  
ATOM  18032  C   GLU E 129     -21.572 191.102-239.144  1.00171.83           C  
ANISOU18032  C   GLU E 129    26840  26297  12152   1298  -5130    568       C  
ATOM  18033  O   GLU E 129     -20.847 192.080-239.300  1.00172.75           O  
ANISOU18033  O   GLU E 129    26983  26514  12140   1426  -4676    787       O  
ATOM  18034  CB  GLU E 129     -22.373 190.319-241.371  1.00181.63           C  
ANISOU18034  CB  GLU E 129    28412  28259  12339   1147  -5880    382       C  
ATOM  18035  CG  GLU E 129     -23.754 190.891-241.050  1.00183.66           C  
ANISOU18035  CG  GLU E 129    28317  28527  12938   1064  -6158   1009       C  
ATOM  18036  CD  GLU E 129     -24.752 189.821-240.649  1.00186.05           C  
ANISOU18036  CD  GLU E 129    28501  28660  13530    824  -6721    839       C  
ATOM  18037  OE1 GLU E 129     -24.481 188.635-240.928  1.00188.78           O  
ANISOU18037  OE1 GLU E 129    29115  28946  13668    692  -6983    234       O  
ATOM  18038  OE2 GLU E 129     -25.802 190.161-240.061  1.00185.21           O1-
ANISOU18038  OE2 GLU E 129    28042  28471  13858    770  -6889   1318       O1-
ATOM  18039  N   GLN E 130     -22.429 190.992-238.134  1.00167.53           N  
ANISOU18039  N   GLN E 130    26034  25435  12186   1221  -5297    765       N  
ATOM  18040  CA  GLN E 130     -22.492 192.000-237.087  1.00160.58           C  
ANISOU18040  CA  GLN E 130    24921  24274  11820   1314  -4917   1198       C  
ATOM  18041  C   GLN E 130     -21.179 191.990-236.335  1.00151.49           C  
ANISOU18041  C   GLN E 130    23850  22858  10850   1384  -4446    866       C  
ATOM  18042  O   GLN E 130     -20.463 192.991-236.289  1.00150.15           O  
ANISOU18042  O   GLN E 130    23707  22705  10638   1472  -3988   1067       O  
ATOM  18043  CB  GLN E 130     -23.632 191.709-236.110  1.00160.74           C  
ANISOU18043  CB  GLN E 130    24654  24012  12408   1233  -5187   1410       C  
ATOM  18044  CG  GLN E 130     -25.025 191.992-236.644  1.00167.03           C  
ANISOU18044  CG  GLN E 130    25249  25075  13140   1182  -5590   1916       C  
ATOM  18045  CD  GLN E 130     -26.070 192.010-235.541  1.00165.30           C  
ANISOU18045  CD  GLN E 130    24685  24580  13540   1164  -5700   2259       C  
ATOM  18046  OE1 GLN E 130     -25.847 192.573-234.468  1.00159.32           O  
ANISOU18046  OE1 GLN E 130    23832  23482  13221   1286  -5302   2411       O  
ATOM  18047  NE2 GLN E 130     -27.215 191.385-235.798  1.00169.59           N  
ANISOU18047  NE2 GLN E 130    25042  25286  14109    998  -6244   2383       N  
ATOM  18048  N   GLY E 131     -20.868 190.836-235.754  1.00146.11           N  
ANISOU18048  N   GLY E 131    23206  21938  10370   1329  -4572    370       N  
ATOM  18049  CA  GLY E 131     -19.656 190.665-234.979  1.00139.29           C  
ANISOU18049  CA  GLY E 131    22378  20849   9697   1396  -4181     45       C  
ATOM  18050  C   GLY E 131     -18.414 190.886-235.812  1.00137.65           C  
ANISOU18050  C   GLY E 131    22374  20937   8989   1494  -3862   -164       C  
ATOM  18051  O   GLY E 131     -17.408 191.384-235.313  1.00134.85           O  
ANISOU18051  O   GLY E 131    21982  20513   8741   1547  -3421   -178       O  
ATOM  18052  N   GLN E 132     -18.484 190.513-237.085  1.00139.97           N  
ANISOU18052  N   GLN E 132    22878  21584   8719   1505  -4087   -319       N  
ATOM  18053  CA  GLN E 132     -17.364 190.710-237.991  1.00142.07           C  
ANISOU18053  CA  GLN E 132    23341  22191   8450   1620  -3781   -490       C  
ATOM  18054  C   GLN E 132     -17.122 192.195-238.223  1.00140.75           C  
ANISOU18054  C   GLN E 132    23094  22194   8189   1648  -3397     35       C  
ATOM  18055  O   GLN E 132     -15.989 192.666-238.125  1.00137.42           O  
ANISOU18055  O   GLN E 132    22675  21832   7707   1702  -2945      8       O  
ATOM  18056  CB  GLN E 132     -17.600 189.985-239.317  1.00150.27           C  
ANISOU18056  CB  GLN E 132    24657  23573   8865   1628  -4129   -767       C  
ATOM  18057  CG  GLN E 132     -17.365 188.487-239.245  1.00154.15           C  
ANISOU18057  CG  GLN E 132    25346  23896   9329   1640  -4365  -1409       C  
ATOM  18058  CD  GLN E 132     -17.674 187.786-240.551  1.00164.80           C  
ANISOU18058  CD  GLN E 132    27029  25550  10039   1618  -4732  -1705       C  
ATOM  18059  OE1 GLN E 132     -18.325 188.347-241.433  1.00170.16           O  
ANISOU18059  OE1 GLN E 132    27706  26558  10390   1532  -4903  -1382       O  
ATOM  18060  NE2 GLN E 132     -17.204 186.552-240.684  1.00168.03           N  
ANISOU18060  NE2 GLN E 132    27615  25805  10425   1629  -4761  -2279       N  
ATOM  18061  N   ASN E 133     -18.191 192.931-238.519  1.00143.77           N  
ANISOU18061  N   ASN E 133    23398  22653   8573   1606  -3574    535       N  
ATOM  18062  CA  ASN E 133     -18.092 194.373-238.715  1.00145.69           C  
ANISOU18062  CA  ASN E 133    23594  22992   8768   1642  -3218   1086       C  
ATOM  18063  C   ASN E 133     -17.616 195.068-237.452  1.00143.39           C  
ANISOU18063  C   ASN E 133    23161  22303   9019   1616  -2806   1231       C  
ATOM  18064  O   ASN E 133     -16.923 196.081-237.517  1.00144.02           O  
ANISOU18064  O   ASN E 133    23268  22417   9035   1617  -2378   1478       O  
ATOM  18065  CB  ASN E 133     -19.432 194.970-239.147  1.00148.28           C  
ANISOU18065  CB  ASN E 133    23838  23437   9066   1643  -3502   1627       C  
ATOM  18066  CG  ASN E 133     -19.846 194.534-240.536  1.00153.98           C  
ANISOU18066  CG  ASN E 133    24714  24639   9153   1644  -3882   1571       C  
ATOM  18067  OD1 ASN E 133     -19.015 194.121-241.346  1.00156.18           O  
ANISOU18067  OD1 ASN E 133    25211  25204   8926   1680  -3808   1220       O  
ATOM  18068  ND2 ASN E 133     -21.140 194.622-240.819  1.00156.29           N  
ANISOU18068  ND2 ASN E 133    24886  25048   9450   1608  -4291   1926       N  
ATOM  18069  N   LEU E 134     -17.997 194.516-236.304  1.00142.18           N  
ANISOU18069  N   LEU E 134    22868  21772   9383   1571  -2943   1078       N  
ATOM  18070  CA  LEU E 134     -17.593 195.064-235.017  1.00139.27           C  
ANISOU18070  CA  LEU E 134    22382  21017   9517   1532  -2596   1165       C  
ATOM  18071  C   LEU E 134     -16.109 194.823-234.759  1.00139.01           C  
ANISOU18071  C   LEU E 134    22387  21012   9417   1511  -2261    783       C  
ATOM  18072  O   LEU E 134     -15.421 195.674-234.198  1.00137.73           O  
ANISOU18072  O   LEU E 134    22191  20719   9421   1446  -1861    933       O  
ATOM  18073  CB  LEU E 134     -18.421 194.455-233.889  1.00136.14           C  
ANISOU18073  CB  LEU E 134    21823  20255   9649   1504  -2849   1105       C  
ATOM  18074  CG  LEU E 134     -18.134 195.071-232.521  1.00132.99           C  
ANISOU18074  CG  LEU E 134    21325  19457   9747   1469  -2508   1221       C  
ATOM  18075  CD1 LEU E 134     -18.629 196.511-232.476  1.00133.39           C  
ANISOU18075  CD1 LEU E 134    21387  19401   9895   1500  -2258   1800       C  
ATOM  18076  CD2 LEU E 134     -18.740 194.242-231.400  1.00129.91           C  
ANISOU18076  CD2 LEU E 134    20783  18748   9829   1452  -2741   1065       C  
ATOM  18077  N   ALA E 135     -15.623 193.656-235.167  1.00140.79           N  
ANISOU18077  N   ALA E 135    22686  21409   9397   1563  -2425    294       N  
ATOM  18078  CA  ALA E 135     -14.206 193.342-235.046  1.00141.13           C  
ANISOU18078  CA  ALA E 135    22738  21557   9330   1595  -2114    -53       C  
ATOM  18079  C   ALA E 135     -13.389 194.233-235.977  1.00146.26           C  
ANISOU18079  C   ALA E 135    23466  22572   9535   1602  -1756    146       C  
ATOM  18080  O   ALA E 135     -12.325 194.721-235.595  1.00145.06           O  
ANISOU18080  O   ALA E 135    23231  22442   9443   1544  -1362    159       O  
ATOM  18081  CB  ALA E 135     -13.955 191.875-235.347  1.00142.80           C  
ANISOU18081  CB  ALA E 135    23048  21849   9360   1705  -2361   -601       C  
ATOM  18082  N   ARG E 136     -13.892 194.446-237.193  1.00151.53           N  
ANISOU18082  N   ARG E 136    24280  23548   9748   1656  -1904    322       N  
ATOM  18083  CA  ARG E 136     -13.260 195.362-238.141  1.00155.76           C  
ANISOU18083  CA  ARG E 136    24897  24442   9844   1665  -1575    592       C  
ATOM  18084  C   ARG E 136     -13.243 196.778-237.575  1.00156.93           C  
ANISOU18084  C   ARG E 136    24962  24367  10299   1531  -1240   1099       C  
ATOM  18085  O   ARG E 136     -12.290 197.530-237.774  1.00160.52           O  
ANISOU18085  O   ARG E 136    25415  24964  10610   1461   -832   1250       O  
ATOM  18086  CB  ARG E 136     -14.007 195.366-239.478  1.00158.46           C  
ANISOU18086  CB  ARG E 136    25411  25137   9662   1744  -1848    747       C  
ATOM  18087  CG  ARG E 136     -13.979 194.049-240.226  1.00160.19           C  
ANISOU18087  CG  ARG E 136    25799  25601   9464   1856  -2162    235       C  
ATOM  18088  CD  ARG E 136     -14.975 194.060-241.374  1.00163.10           C  
ANISOU18088  CD  ARG E 136    26323  26270   9377   1877  -2535    415       C  
ATOM  18089  NE  ARG E 136     -15.135 192.737-241.965  1.00167.38           N  
ANISOU18089  NE  ARG E 136    27070  26954   9571   1935  -2912   -112       N  
ATOM  18090  CZ  ARG E 136     -16.087 192.417-242.836  1.00175.94           C  
ANISOU18090  CZ  ARG E 136    28301  28262  10285   1904  -3362    -90       C  
ATOM  18091  NH1 ARG E 136     -16.972 193.326-243.222  1.00179.82           N1+
ANISOU18091  NH1 ARG E 136    28713  28898  10713   1851  -3489    472       N1+
ATOM  18092  NH2 ARG E 136     -16.156 191.185-243.323  1.00180.19           N  
ANISOU18092  NH2 ARG E 136    29016  28834  10612   1874  -3658   -613       N  
ATOM  18093  N   GLN E 137     -14.312 197.126-236.864  1.00154.00           N  
ANISOU18093  N   GLN E 137    24531  23633  10348   1494  -1407   1362       N  
ATOM  18094  CA  GLN E 137     -14.471 198.449-236.277  1.00152.50           C  
ANISOU18094  CA  GLN E 137    24323  23149  10471   1398  -1109   1837       C  
ATOM  18095  C   GLN E 137     -13.536 198.629-235.084  1.00150.44           C  
ANISOU18095  C   GLN E 137    23971  22600  10589   1246   -793   1667       C  
ATOM  18096  O   GLN E 137     -13.228 199.754-234.689  1.00149.18           O  
ANISOU18096  O   GLN E 137    23848  22241  10594   1112   -449   1974       O  
ATOM  18097  CB  GLN E 137     -15.923 198.652-235.845  1.00150.76           C  
ANISOU18097  CB  GLN E 137    24058  22642  10582   1458  -1380   2147       C  
ATOM  18098  CG  GLN E 137     -16.349 200.100-235.697  1.00151.68           C  
ANISOU18098  CG  GLN E 137    24235  22530  10865   1451  -1105   2739       C  
ATOM  18099  CD  GLN E 137     -17.788 200.232-235.232  1.00151.13           C  
ANISOU18099  CD  GLN E 137    24083  22206  11133   1565  -1353   3053       C  
ATOM  18100  OE1 GLN E 137     -18.302 199.373-234.514  1.00149.41           O  
ANISOU18100  OE1 GLN E 137    23731  21828  11210   1577  -1632   2810       O  
ATOM  18101  NE2 GLN E 137     -18.446 201.308-235.644  1.00153.03           N  
ANISOU18101  NE2 GLN E 137    24392  22418  11336   1664  -1239   3626       N  
ATOM  18102  N   TRP E 138     -13.094 197.512-234.511  1.00151.32           N  
ANISOU18102  N   TRP E 138    23977  22686  10830   1260   -920   1183       N  
ATOM  18103  CA  TRP E 138     -12.165 197.525-233.383  1.00149.59           C  
ANISOU18103  CA  TRP E 138    23638  22269  10932   1123   -670    990       C  
ATOM  18104  C   TRP E 138     -10.730 197.287-233.848  1.00152.09           C  
ANISOU18104  C   TRP E 138    23899  22964  10925   1098   -412    752       C  
ATOM  18105  O   TRP E 138     -10.015 196.464-233.276  1.00149.96           O  
ANISOU18105  O   TRP E 138    23495  22716  10765   1116   -407    379       O  
ATOM  18106  CB  TRP E 138     -12.555 196.466-232.346  1.00145.96           C  
ANISOU18106  CB  TRP E 138    23064  21539  10856   1172   -946    659       C  
ATOM  18107  CG  TRP E 138     -13.797 196.799-231.566  1.00145.37           C  
ANISOU18107  CG  TRP E 138    22982  21060  11193   1169  -1105    916       C  
ATOM  18108  CD1 TRP E 138     -14.519 197.955-231.629  1.00147.29           C  
ANISOU18108  CD1 TRP E 138    23311  21135  11517   1149   -993   1396       C  
ATOM  18109  CD2 TRP E 138     -14.460 195.964-230.606  1.00143.70           C  
ANISOU18109  CD2 TRP E 138    22665  20566  11366   1213  -1377    735       C  
ATOM  18110  NE1 TRP E 138     -15.589 197.893-230.769  1.00145.56           N  
ANISOU18110  NE1 TRP E 138    23034  20568  11702   1199  -1167   1522       N  
ATOM  18111  CE2 TRP E 138     -15.576 196.681-230.129  1.00143.27           C  
ANISOU18111  CE2 TRP E 138    22620  20213  11604   1222  -1408   1126       C  
ATOM  18112  CE3 TRP E 138     -14.219 194.681-230.102  1.00142.60           C  
ANISOU18112  CE3 TRP E 138    22431  20395  11358   1261  -1579    302       C  
ATOM  18113  CZ2 TRP E 138     -16.449 196.158-229.174  1.00140.97           C  
ANISOU18113  CZ2 TRP E 138    22219  19627  11717   1266  -1631   1103       C  
ATOM  18114  CZ3 TRP E 138     -15.087 194.163-229.153  1.00139.39           C  
ANISOU18114  CZ3 TRP E 138    21932  19668  11361   1282  -1813    282       C  
ATOM  18115  CH2 TRP E 138     -16.187 194.901-228.700  1.00138.65           C  
ANISOU18115  CH2 TRP E 138    21826  19315  11540   1278  -1837    682       C  
ATOM  18116  N   ASN E 139     -10.327 198.008-234.892  1.00156.82           N  
ANISOU18116  N   ASN E 139    24586  23876  11123   1076   -188   1002       N  
ATOM  18117  CA  ASN E 139      -8.968 197.935-235.429  1.00160.26           C  
ANISOU18117  CA  ASN E 139    24948  24725  11220   1054    111    866       C  
ATOM  18118  C   ASN E 139      -8.543 196.537-235.875  1.00162.24           C  
ANISOU18118  C   ASN E 139    25166  25280  11197   1288    -51    376       C  
ATOM  18119  O   ASN E 139      -7.638 195.942-235.285  1.00161.14           O  
ANISOU18119  O   ASN E 139    24857  25190  11179   1300     61     77       O  
ATOM  18120  CB  ASN E 139      -7.954 198.496-234.424  1.00158.56           C  
ANISOU18120  CB  ASN E 139    24563  24378  11306    797    445    895       C  
ATOM  18121  CG  ASN E 139      -8.244 199.935-234.047  1.00158.56           C  
ANISOU18121  CG  ASN E 139    24665  24052  11531    547    659   1356       C  
ATOM  18122  OD1 ASN E 139      -8.956 200.642-234.761  1.00160.68           O  
ANISOU18122  OD1 ASN E 139    25112  24295  11645    587    658   1718       O  
ATOM  18123  ND2 ASN E 139      -7.690 200.378-232.925  1.00156.64           N  
ANISOU18123  ND2 ASN E 139    24326  23552  11639    290    845   1348       N  
ATOM  18124  N   ASN E 140      -9.198 196.031-236.919  1.00165.11           N  
ANISOU18124  N   ASN E 140    25708  25846  11182   1478   -312    304       N  
ATOM  18125  CA  ASN E 140      -8.901 194.715-237.490  1.00165.87           C  
ANISOU18125  CA  ASN E 140    25872  26197  10954   1716   -475   -175       C  
ATOM  18126  C   ASN E 140      -8.785 193.625-236.425  1.00160.56           C  
ANISOU18126  C   ASN E 140    25088  25242  10678   1777   -637   -591       C  
ATOM  18127  O   ASN E 140      -7.881 192.791-236.473  1.00161.08           O  
ANISOU18127  O   ASN E 140    25103  25492  10609   1938   -527   -950       O  
ATOM  18128  CB  ASN E 140      -7.636 194.773-238.338  1.00169.24           C  
ANISOU18128  CB  ASN E 140    26276  27127  10901   1809   -103   -230       C  
ATOM  18129  N   CYS E 141      -9.704 193.646-235.465  1.00155.31           N  
ANISOU18129  N   CYS E 141    24380  24135  10497   1673   -878   -515       N  
ATOM  18130  CA  CYS E 141      -9.663 192.713-234.346  1.00151.56           C  
ANISOU18130  CA  CYS E 141    23789  23359  10440   1708  -1023   -839       C  
ATOM  18131  C   CYS E 141      -9.980 191.287-234.779  1.00152.15           C  
ANISOU18131  C   CYS E 141    24016  23446  10348   1920  -1358  -1282       C  
ATOM  18132  O   CYS E 141     -10.681 191.064-235.767  1.00154.11           O  
ANISOU18132  O   CYS E 141    24476  23824  10256   1980  -1608  -1302       O  
ATOM  18133  CB  CYS E 141     -10.628 193.152-233.244  1.00148.68           C  
ANISOU18133  CB  CYS E 141    23352  22535  10607   1550  -1175   -605       C  
ATOM  18134  SG  CYS E 141     -10.503 192.176-231.724  1.00148.32           S  
ANISOU18134  SG  CYS E 141    23135  22124  11096   1564  -1294   -922       S  
ATOM  18135  N   ALA E 142      -9.454 190.325-234.025  1.00150.05           N  
ANISOU18135  N   ALA E 142    23658  23039  10317   2024  -1365  -1631       N  
ATOM  18136  CA  ALA E 142      -9.669 188.914-234.314  1.00150.08           C  
ANISOU18136  CA  ALA E 142    23839  22970  10213   2225  -1653  -2080       C  
ATOM  18137  C   ALA E 142     -11.063 188.476-233.880  1.00146.13           C  
ANISOU18137  C   ALA E 142    23411  22076  10037   2123  -2113  -2074       C  
ATOM  18138  O   ALA E 142     -11.491 188.747-232.758  1.00143.01           O  
ANISOU18138  O   ALA E 142    22838  21363  10136   1990  -2158  -1892       O  
ATOM  18139  CB  ALA E 142      -8.611 188.067-233.633  1.00149.22           C  
ANISOU18139  CB  ALA E 142    23600  22832  10265   2399  -1474  -2405       C  
ATOM  18140  N   PHE E 143     -11.766 187.795-234.777  1.00144.77           N  
ANISOU18140  N   PHE E 143    23497  21943   9566   2175  -2455  -2268       N  
ATOM  18141  CA  PHE E 143     -13.138 187.390-234.521  1.00139.71           C  
ANISOU18141  CA  PHE E 143    22905  20996   9184   2041  -2924  -2226       C  
ATOM  18142  C   PHE E 143     -13.334 185.913-234.830  1.00142.07           C  
ANISOU18142  C   PHE E 143    23456  21152   9374   2139  -3249  -2723       C  
ATOM  18143  O   PHE E 143     -12.772 185.394-235.793  1.00147.70           O  
ANISOU18143  O   PHE E 143    24422  22100   9599   2305  -3199  -3046       O  
ATOM  18144  CB  PHE E 143     -14.095 188.239-235.357  1.00139.18           C  
ANISOU18144  CB  PHE E 143    22895  21121   8867   1912  -3100  -1849       C  
ATOM  18145  CG  PHE E 143     -15.527 187.806-235.272  1.00137.50           C  
ANISOU18145  CG  PHE E 143    22703  20691   8849   1769  -3609  -1779       C  
ATOM  18146  CD1 PHE E 143     -16.317 188.191-234.204  1.00133.72           C  
ANISOU18146  CD1 PHE E 143    21984  19904   8920   1643  -3691  -1456       C  
ATOM  18147  CD2 PHE E 143     -16.089 187.022-236.270  1.00140.48           C  
ANISOU18147  CD2 PHE E 143    23339  21194   8842   1748  -4004  -2026       C  
ATOM  18148  CE1 PHE E 143     -17.639 187.797-234.126  1.00134.37           C  
ANISOU18148  CE1 PHE E 143    22033  19832   9191   1509  -4149  -1346       C  
ATOM  18149  CE2 PHE E 143     -17.410 186.623-236.197  1.00140.49           C  
ANISOU18149  CE2 PHE E 143    23322  21031   9027   1568  -4498  -1936       C  
ATOM  18150  CZ  PHE E 143     -18.186 187.012-235.124  1.00137.64           C  
ANISOU18150  CZ  PHE E 143    22669  20389   9239   1452  -4565  -1576       C  
ATOM  18151  N   LEU E 144     -14.134 185.242-234.007  1.00139.22           N  
ANISOU18151  N   LEU E 144    23045  20391   9463   2037  -3567  -2779       N  
ATOM  18152  CA  LEU E 144     -14.443 183.831-234.214  1.00141.14           C  
ANISOU18152  CA  LEU E 144    23550  20408   9669   2074  -3911  -3229       C  
ATOM  18153  C   LEU E 144     -15.806 183.449-233.657  1.00140.17           C  
ANISOU18153  C   LEU E 144    23360  19943   9957   1837  -4373  -3100       C  
ATOM  18154  O   LEU E 144     -16.140 183.789-232.525  1.00134.48           O  
ANISOU18154  O   LEU E 144    22354  18992   9750   1753  -4333  -2821       O  
ATOM  18155  CB  LEU E 144     -13.373 182.949-233.571  1.00139.02           C  
ANISOU18155  CB  LEU E 144    23295  19956   9569   2307  -3674  -3595       C  
ATOM  18156  CG  LEU E 144     -12.225 182.510-234.475  1.00143.68           C  
ANISOU18156  CG  LEU E 144    24129  20824   9640   2598  -3406  -3969       C  
ATOM  18157  CD1 LEU E 144     -11.311 181.556-233.730  1.00144.62           C  
ANISOU18157  CD1 LEU E 144    24230  20718  10000   2853  -3209  -4286       C  
ATOM  18158  CD2 LEU E 144     -12.769 181.866-235.741  1.00147.96           C  
ANISOU18158  CD2 LEU E 144    25102  21439   9676   2586  -3736  -4277       C  
ATOM  18159  N   GLU E 145     -16.596 182.743-234.459  1.00145.55           N  
ANISOU18159  N   GLU E 145    24303  20608  10390   1717  -4812  -3300       N  
ATOM  18160  CA  GLU E 145     -17.814 182.120-233.956  1.00146.37           C  
ANISOU18160  CA  GLU E 145    24356  20377  10880   1476  -5279  -3247       C  
ATOM  18161  C   GLU E 145     -17.464 180.723-233.450  1.00144.22           C  
ANISOU18161  C   GLU E 145    24276  19693  10829   1554  -5361  -3717       C  
ATOM  18162  O   GLU E 145     -16.904 179.908-234.182  1.00145.46           O  
ANISOU18162  O   GLU E 145    24807  19852  10609   1692  -5370  -4189       O  
ATOM  18163  CB  GLU E 145     -18.903 182.066-235.032  1.00154.47           C  
ANISOU18163  CB  GLU E 145    25541  21600  11551   1245  -5759  -3191       C  
ATOM  18164  CG  GLU E 145     -19.615 183.395-235.267  1.00156.91           C  
ANISOU18164  CG  GLU E 145    25577  22225  11816   1140  -5767  -2598       C  
ATOM  18165  CD  GLU E 145     -20.869 183.255-236.120  1.00164.77           C  
ANISOU18165  CD  GLU E 145    26638  23401  12567    878  -6318  -2471       C  
ATOM  18166  OE1 GLU E 145     -20.989 182.249-236.853  1.00169.44           O  
ANISOU18166  OE1 GLU E 145    27572  23974  12835    777  -6652  -2907       O  
ATOM  18167  OE2 GLU E 145     -21.736 184.153-236.050  1.00165.76           O1-
ANISOU18167  OE2 GLU E 145    26470  23687  12823    774  -6413  -1929       O1-
ATOM  18168  N   SER E 146     -17.785 180.457-232.188  1.00142.64           N  
ANISOU18168  N   SER E 146    23836  19130  11231   1489  -5395  -3577       N  
ATOM  18169  CA  SER E 146     -17.333 179.238-231.532  1.00144.81           C  
ANISOU18169  CA  SER E 146    24247  18997  11778   1606  -5390  -3949       C  
ATOM  18170  C   SER E 146     -18.470 178.437-230.912  1.00141.42           C  
ANISOU18170  C   SER E 146    23782  18154  11798   1341  -5829  -3904       C  
ATOM  18171  O   SER E 146     -19.565 178.952-230.685  1.00138.76           O  
ANISOU18171  O   SER E 146    23194  17853  11675   1090  -6070  -3500       O  
ATOM  18172  CB  SER E 146     -16.289 179.567-230.463  1.00145.68           C  
ANISOU18172  CB  SER E 146    24097  19070  12186   1843  -4914  -3857       C  
ATOM  18173  OG  SER E 146     -15.184 180.256-231.023  1.00149.40           O  
ANISOU18173  OG  SER E 146    24577  19932  12257   2060  -4505  -3893       O  
ATOM  18174  N   SER E 147     -18.190 177.168-230.640  1.00141.65           N  
ANISOU18174  N   SER E 147    24060  17790  11972   1414  -5914  -4299       N  
ATOM  18175  CA  SER E 147     -19.159 176.278-230.024  1.00141.38           C  
ANISOU18175  CA  SER E 147    24021  17317  12380   1158  -6310  -4284       C  
ATOM  18176  C   SER E 147     -18.439 175.265-229.146  1.00138.43           C  
ANISOU18176  C   SER E 147    23743  16513  12340   1377  -6134  -4547       C  
ATOM  18177  O   SER E 147     -17.897 174.277-229.641  1.00139.95           O  
ANISOU18177  O   SER E 147    24357  16498  12321   1529  -6145  -5028       O  
ATOM  18178  CB  SER E 147     -19.978 175.555-231.091  1.00149.19           C  
ANISOU18178  CB  SER E 147    25381  18239  13064    872  -6823  -4552       C  
ATOM  18179  OG  SER E 147     -20.938 174.702-230.495  1.00151.48           O  
ANISOU18179  OG  SER E 147    25648  18105  13802    571  -7221  -4509       O  
ATOM  18180  N   ALA E 148     -18.432 175.522-227.842  1.00135.14           N  
ANISOU18180  N   ALA E 148    22951  15965  12430   1414  -5959  -4222       N  
ATOM  18181  CA  ALA E 148     -17.776 174.639-226.887  1.00134.15           C  
ANISOU18181  CA  ALA E 148    22852  15466  12653   1631  -5786  -4384       C  
ATOM  18182  C   ALA E 148     -18.488 173.294-226.823  1.00138.35           C  
ANISOU18182  C   ALA E 148    23666  15479  13421   1435  -6190  -4605       C  
ATOM  18183  O   ALA E 148     -17.898 172.289-226.428  1.00139.29           O  
ANISOU18183  O   ALA E 148    23993  15232  13699   1642  -6094  -4879       O  
ATOM  18184  CB  ALA E 148     -17.729 175.286-225.512  1.00127.36           C  
ANISOU18184  CB  ALA E 148    21525  14622  12245   1668  -5548  -3952       C  
ATOM  18185  N   LYS E 149     -19.757 173.283-227.219  1.00141.21           N  
ANISOU18185  N   LYS E 149    24029  15814  13810   1029  -6644  -4466       N  
ATOM  18186  CA  LYS E 149     -20.538 172.054-227.241  1.00147.25           C  
ANISOU18186  CA  LYS E 149    25063  16099  14786    746  -7082  -4656       C  
ATOM  18187  C   LYS E 149     -20.133 171.182-228.421  1.00152.66           C  
ANISOU18187  C   LYS E 149    26365  16637  15001    799  -7215  -5258       C  
ATOM  18188  O   LYS E 149     -19.981 169.967-228.288  1.00155.94           O  
ANISOU18188  O   LYS E 149    27146  16544  15560    828  -7311  -5601       O  
ATOM  18189  CB  LYS E 149     -22.035 172.364-227.312  1.00150.65           C  
ANISOU18189  CB  LYS E 149    25246  16614  15379    265  -7541  -4276       C  
ATOM  18190  CG  LYS E 149     -22.914 171.119-227.321  1.00158.07           C  
ANISOU18190  CG  LYS E 149    26427  17073  16560   -114  -8033  -4431       C  
ATOM  18191  CD  LYS E 149     -24.385 171.463-227.490  1.00160.60           C  
ANISOU18191  CD  LYS E 149    26451  17570  16999   -604  -8502  -4026       C  
ATOM  18192  CE  LYS E 149     -25.250 170.213-227.401  1.00165.87           C  
ANISOU18192  CE  LYS E 149    27318  17748  17955  -1035  -8995  -4145       C  
ATOM  18193  NZ  LYS E 149     -24.825 169.178-228.386  1.00172.80           N1+
ANISOU18193  NZ  LYS E 149    28861  18335  18459  -1070  -9149  -4791       N1+
ATOM  18194  N   SER E 150     -19.957 171.814-229.576  1.00153.83           N  
ANISOU18194  N   SER E 150    26653  17220  14575    825  -7203  -5382       N  
ATOM  18195  CA  SER E 150     -19.633 171.098-230.800  1.00161.05           C  
ANISOU18195  CA  SER E 150    28020  18107  15063    854  -7184  -5831       C  
ATOM  18196  C   SER E 150     -18.145 171.192-231.124  1.00160.94           C  
ANISOU18196  C   SER E 150    28156  18275  14720   1379  -6633  -6101       C  
ATOM  18197  O   SER E 150     -17.724 170.855-232.234  1.00166.05           O  
ANISOU18197  O   SER E 150    29108  19038  14945   1469  -6499  -6413       O  
ATOM  18198  CB  SER E 150     -20.466 171.632-231.968  1.00164.85           C  
ANISOU18198  CB  SER E 150    28476  19001  15158    508  -7460  -5718       C  
ATOM  18199  OG  SER E 150     -21.853 171.504-231.702  1.00154.51           O  
ANISOU18199  OG  SER E 150    26985  17568  14153     19  -7974  -5439       O  
ATOM  18200  N   LYS E 151     -17.364 171.650-230.146  1.00154.51           N  
ANISOU18200  N   LYS E 151    27107  17506  14095   1713  -6319  -5969       N  
ATOM  18201  CA  LYS E 151     -15.909 171.747-230.272  1.00153.89           C  
ANISOU18201  CA  LYS E 151    27080  17623  13766   2221  -5785  -6165       C  
ATOM  18202  C   LYS E 151     -15.476 172.536-231.505  1.00158.33           C  
ANISOU18202  C   LYS E 151    27663  18749  13745   2296  -5565  -6190       C  
ATOM  18203  O   LYS E 151     -14.628 172.084-232.272  1.00164.08           O  
ANISOU18203  O   LYS E 151    28647  19546  14149   2569  -5275  -6501       O  
ATOM  18204  CB  LYS E 151     -15.283 170.350-230.297  1.00156.10           C  
ANISOU18204  CB  LYS E 151    27737  17442  14132   2483  -5637  -6571       C  
ATOM  18205  CG  LYS E 151     -15.404 169.580-228.994  1.00152.72           C  
ANISOU18205  CG  LYS E 151    27283  16468  14276   2529  -5734  -6537       C  
ATOM  18206  CD  LYS E 151     -15.326 168.081-229.235  1.00159.63           C  
ANISOU18206  CD  LYS E 151    28612  16782  15259   2592  -5769  -6901       C  
ATOM  18207  CE  LYS E 151     -14.151 167.712-230.129  1.00164.40           C  
ANISOU18207  CE  LYS E 151    29496  17532  15436   3030  -5337  -7246       C  
ATOM  18208  NZ  LYS E 151     -14.218 166.290-230.576  1.00171.00           N1+
ANISOU18208  NZ  LYS E 151    30839  17828  16305   3033  -5399  -7615       N1+
ATOM  18209  N   ILE E 152     -16.064 173.712-231.697  1.00155.76           N  
ANISOU18209  N   ILE E 152    27073  18820  13289   2067  -5695  -5840       N  
ATOM  18210  CA  ILE E 152     -15.762 174.526-232.869  1.00156.16           C  
ANISOU18210  CA  ILE E 152    27132  19406  12795   2100  -5515  -5806       C  
ATOM  18211  C   ILE E 152     -14.951 175.761-232.493  1.00151.93           C  
ANISOU18211  C   ILE E 152    26277  19295  12156   2340  -5127  -5533       C  
ATOM  18212  O   ILE E 152     -15.410 176.599-231.717  1.00145.53           O  
ANISOU18212  O   ILE E 152    25074  18554  11668   2180  -5152  -5097       O  
ATOM  18213  CB  ILE E 152     -17.046 174.973-233.589  1.00155.16           C  
ANISOU18213  CB  ILE E 152    26973  19466  12515   1660  -5946  -5592       C  
ATOM  18214  CG1 ILE E 152     -17.999 173.790-233.755  1.00158.42           C  
ANISOU18214  CG1 ILE E 152    27635  19446  13111   1331  -6394  -5800       C  
ATOM  18215  CG2 ILE E 152     -16.710 175.605-234.932  1.00157.53           C  
ANISOU18215  CG2 ILE E 152    27359  20282  12212   1707  -5769  -5615       C  
ATOM  18216  CD1 ILE E 152     -19.316 174.155-234.400  1.00161.27           C  
ANISOU18216  CD1 ILE E 152    27910  20015  13350    874  -6857  -5566       C  
ATOM  18217  N   ASN E 153     -13.747 175.861-233.051  1.00154.82           N  
ANISOU18217  N   ASN E 153    26707  19944  12175   2677  -4679  -5703       N  
ATOM  18218  CA  ASN E 153     -12.859 176.995-232.802  1.00151.37           C  
ANISOU18218  CA  ASN E 153    25975  19942  11596   2885  -4275  -5462       C  
ATOM  18219  C   ASN E 153     -12.652 177.295-231.318  1.00145.22           C  
ANISOU18219  C   ASN E 153    24744  19014  11421   2888  -4100  -5138       C  
ATOM  18220  O   ASN E 153     -12.553 178.455-230.923  1.00141.69           O  
ANISOU18220  O   ASN E 153    23926  18836  11073   2796  -3908  -4737       O  
ATOM  18221  CB  ASN E 153     -13.355 178.246-233.535  1.00151.98           C  
ANISOU18221  CB  ASN E 153    25933  20462  11352   2664  -4332  -5131       C  
ATOM  18222  CG  ASN E 153     -13.109 178.184-235.034  1.00159.80           C  
ANISOU18222  CG  ASN E 153    27159  21758  11802   2691  -4228  -5305       C  
ATOM  18223  OD1 ASN E 153     -12.093 177.655-235.485  1.00163.55           O  
ANISOU18223  OD1 ASN E 153    27784  22301  12059   2985  -3897  -5593       O  
ATOM  18224  ND2 ASN E 153     -14.039 178.727-235.811  1.00162.13           N  
ANISOU18224  ND2 ASN E 153    27479  22258  11865   2399  -4508  -5113       N  
ATOM  18225  N   VAL E 154     -12.589 176.243-230.506  1.00145.13           N  
ANISOU18225  N   VAL E 154    24788  18556  11797   2990  -4165  -5313       N  
ATOM  18226  CA  VAL E 154     -12.403 176.385-229.064  1.00140.08           C  
ANISOU18226  CA  VAL E 154    23750  17761  11715   3002  -4023  -5030       C  
ATOM  18227  C   VAL E 154     -10.955 176.716-228.724  1.00140.66           C  
ANISOU18227  C   VAL E 154    23588  18139  11719   3340  -3514  -5005       C  
ATOM  18228  O   VAL E 154     -10.684 177.605-227.916  1.00137.14           O  
ANISOU18228  O   VAL E 154    22737  17877  11492   3268  -3315  -4654       O  
ATOM  18229  CB  VAL E 154     -12.823 175.102-228.307  1.00139.76           C  
ANISOU18229  CB  VAL E 154    23851  17142  12109   3004  -4264  -5196       C  
ATOM  18230  CG1 VAL E 154     -12.448 175.194-226.838  1.00133.51           C  
ANISOU18230  CG1 VAL E 154    22661  16242  11824   3083  -4067  -4924       C  
ATOM  18231  CG2 VAL E 154     -14.315 174.857-228.462  1.00141.48           C  
ANISOU18231  CG2 VAL E 154    24197  17080  12478   2595  -4783  -5131       C  
ATOM  18232  N   ASN E 155     -10.028 176.001-229.350  1.00147.44           N  
ANISOU18232  N   ASN E 155    24705  19060  12258   3705  -3304  -5375       N  
ATOM  18233  CA  ASN E 155      -8.605 176.184-229.080  1.00149.87           C  
ANISOU18233  CA  ASN E 155    24765  19691  12487   4057  -2823  -5351       C  
ATOM  18234  C   ASN E 155      -8.012 177.367-229.839  1.00149.15           C  
ANISOU18234  C   ASN E 155    24517  20194  11962   4047  -2533  -5188       C  
ATOM  18235  O   ASN E 155      -7.096 178.030-229.350  1.00145.32           O  
ANISOU18235  O   ASN E 155    23648  20040  11525   4127  -2188  -4959       O  
ATOM  18236  CB  ASN E 155      -7.827 174.906-229.408  1.00158.59           C  
ANISOU18236  CB  ASN E 155    26192  20621  13443   4515  -2672  -5783       C  
ATOM  18237  CG  ASN E 155      -8.312 173.703-228.615  1.00160.63           C  
ANISOU18237  CG  ASN E 155    26620  20257  14155   4548  -2919  -5926       C  
ATOM  18238  OD1 ASN E 155      -9.406 173.716-228.052  1.00159.61           O  
ANISOU18238  OD1 ASN E 155    26448  19814  14383   4188  -3274  -5761       O  
ATOM  18239  ND2 ASN E 155      -7.498 172.655-228.573  1.00163.63           N  
ANISOU18239  ND2 ASN E 155    27190  20456  14524   4996  -2714  -6211       N  
ATOM  18240  N   GLU E 156      -8.545 177.625-231.030  1.00153.15           N  
ANISOU18240  N   GLU E 156    25316  20837  12036   3923  -2688  -5290       N  
ATOM  18241  CA  GLU E 156      -8.056 178.698-231.896  1.00155.86           C  
ANISOU18241  CA  GLU E 156    25569  21732  11919   3913  -2427  -5134       C  
ATOM  18242  C   GLU E 156      -8.153 180.077-231.244  1.00150.10           C  
ANISOU18242  C   GLU E 156    24397  21214  11419   3619  -2322  -4632       C  
ATOM  18243  O   GLU E 156      -7.419 180.995-231.606  1.00150.92           O  
ANISOU18243  O   GLU E 156    24315  21764  11264   3636  -1996  -4444       O  
ATOM  18244  CB  GLU E 156      -8.808 178.693-233.231  1.00162.03           C  
ANISOU18244  CB  GLU E 156    26762  22587  12213   3795  -2688  -5305       C  
ATOM  18245  CG  GLU E 156      -8.397 177.577-234.188  1.00171.65           C  
ANISOU18245  CG  GLU E 156    28362  23725  13133   4054  -2611  -5736       C  
ATOM  18246  CD  GLU E 156      -8.743 176.187-233.676  1.00175.49           C  
ANISOU18246  CD  GLU E 156    29096  23616  13966   4129  -2846  -6050       C  
ATOM  18247  OE1 GLU E 156      -9.586 176.075-232.761  1.00172.21           O  
ANISOU18247  OE1 GLU E 156    28623  22847  13962   3910  -3185  -5952       O  
ATOM  18248  OE2 GLU E 156      -8.166 175.206-234.191  1.00181.57           O1-
ANISOU18248  OE2 GLU E 156    30129  24260  14598   4413  -2678  -6380       O1-
ATOM  18249  N   ILE E 157      -9.065 180.213-230.286  1.00144.96           N  
ANISOU18249  N   ILE E 157    23600  20228  11249   3349  -2586  -4416       N  
ATOM  18250  CA  ILE E 157      -9.206 181.440-229.513  1.00140.20           C  
ANISOU18250  CA  ILE E 157    22628  19731  10912   3090  -2483  -3968       C  
ATOM  18251  C   ILE E 157      -7.918 181.751-228.759  1.00140.64           C  
ANISOU18251  C   ILE E 157    22339  20016  11081   3227  -2078  -3867       C  
ATOM  18252  O   ILE E 157      -7.198 182.709-229.073  1.00141.85           O  
ANISOU18252  O   ILE E 157    22320  20574  11001   3190  -1772  -3682       O  
ATOM  18253  CB  ILE E 157     -10.338 181.303-228.478  1.00134.66           C  
ANISOU18253  CB  ILE E 157    21838  18594  10734   2855  -2807  -3796       C  
ATOM  18254  CG1 ILE E 157     -11.663 180.991-229.171  1.00136.60           C  
ANISOU18254  CG1 ILE E 157    22362  18642  10898   2675  -3244  -3852       C  
ATOM  18255  CG2 ILE E 157     -10.451 182.562-227.637  1.00129.88           C  
ANISOU18255  CG2 ILE E 157    20898  18066  10383   2625  -2663  -3362       C  
ATOM  18256  CD1 ILE E 157     -12.797 180.712-228.211  1.00133.60           C  
ANISOU18256  CD1 ILE E 157    21885  17849  11028   2462  -3567  -3684       C  
ATOM  18257  N   PHE E 158      -7.639 180.918-227.764  1.00140.16           N  
ANISOU18257  N   PHE E 158    22173  19703  11380   3371  -2090  -3970       N  
ATOM  18258  CA  PHE E 158      -6.468 181.065-226.913  1.00139.37           C  
ANISOU18258  CA  PHE E 158    21717  19813  11426   3497  -1766  -3868       C  
ATOM  18259  C   PHE E 158      -5.186 180.996-227.733  1.00146.66           C  
ANISOU18259  C   PHE E 158    22610  21191  11923   3798  -1405  -4010       C  
ATOM  18260  O   PHE E 158      -4.212 181.699-227.444  1.00147.36           O  
ANISOU18260  O   PHE E 158    22357  21665  11967   3776  -1091  -3809       O  
ATOM  18261  CB  PHE E 158      -6.475 179.978-225.841  1.00134.95           C  
ANISOU18261  CB  PHE E 158    21108  18886  11282   3656  -1883  -3979       C  
ATOM  18262  CG  PHE E 158      -7.783 179.864-225.110  1.00130.41           C  
ANISOU18262  CG  PHE E 158    20588  17853  11110   3397  -2242  -3859       C  
ATOM  18263  CD1 PHE E 158      -8.028 180.635-223.985  1.00125.54           C  
ANISOU18263  CD1 PHE E 158    19680  17199  10822   3150  -2229  -3531       C  
ATOM  18264  CD2 PHE E 158      -8.771 178.995-225.552  1.00131.37           C  
ANISOU18264  CD2 PHE E 158    21054  17593  11266   3388  -2587  -4069       C  
ATOM  18265  CE1 PHE E 158      -9.227 180.541-223.307  1.00122.31           C  
ANISOU18265  CE1 PHE E 158    19298  16400  10772   2944  -2523  -3393       C  
ATOM  18266  CE2 PHE E 158      -9.975 178.896-224.880  1.00128.82           C  
ANISOU18266  CE2 PHE E 158    20731  16891  11322   3138  -2909  -3915       C  
ATOM  18267  CZ  PHE E 158     -10.204 179.671-223.755  1.00125.30           C  
ANISOU18267  CZ  PHE E 158    19970  16434  11206   2938  -2861  -3566       C  
ATOM  18268  N   TYR E 159      -5.195 180.148-228.758  1.00152.21           N  
ANISOU18268  N   TYR E 159    23675  21856  12300   4066  -1449  -4354       N  
ATOM  18269  CA  TYR E 159      -4.074 180.052-229.685  1.00158.29           C  
ANISOU18269  CA  TYR E 159    24470  23068  12606   4393  -1093  -4501       C  
ATOM  18270  C   TYR E 159      -3.767 181.407-230.310  1.00157.41           C  
ANISOU18270  C   TYR E 159    24191  23441  12176   4175   -872  -4218       C  
ATOM  18271  O   TYR E 159      -2.646 181.906-230.203  1.00157.00           O  
ANISOU18271  O   TYR E 159    23802  23821  12028   4246   -508  -4053       O  
ATOM  18272  CB  TYR E 159      -4.360 179.026-230.787  1.00165.77           C  
ANISOU18272  CB  TYR E 159    25937  23849  13199   4665  -1215  -4934       C  
ATOM  18273  CG  TYR E 159      -4.242 177.583-230.346  1.00169.95           C  
ANISOU18273  CG  TYR E 159    26661  23962  13948   5003  -1290  -5258       C  
ATOM  18274  CD1 TYR E 159      -3.708 177.255-229.107  1.00168.59           C  
ANISOU18274  CD1 TYR E 159    26152  23691  14213   5124  -1186  -5133       C  
ATOM  18275  CD2 TYR E 159      -4.655 176.548-231.177  1.00175.05           C  
ANISOU18275  CD2 TYR E 159    27851  24308  14351   5197  -1465  -5688       C  
ATOM  18276  CE1 TYR E 159      -3.596 175.938-228.703  1.00171.21           C  
ANISOU18276  CE1 TYR E 159    26671  23623  14757   5455  -1238  -5393       C  
ATOM  18277  CE2 TYR E 159      -4.546 175.227-230.781  1.00177.69           C  
ANISOU18277  CE2 TYR E 159    28412  24203  14900   5506  -1517  -5982       C  
ATOM  18278  CZ  TYR E 159      -4.016 174.928-229.543  1.00175.99           C  
ANISOU18278  CZ  TYR E 159    27842  23886  15143   5649  -1394  -5817       C  
ATOM  18279  OH  TYR E 159      -3.905 173.616-229.143  1.00179.26           O  
ANISOU18279  OH  TYR E 159    28486  23844  15782   5979  -1430  -6073       O  
ATOM  18280  N   ASP E 160      -4.768 182.005-230.952  1.00157.30           N  
ANISOU18280  N   ASP E 160    24397  23361  12008   3900  -1098  -4133       N  
ATOM  18281  CA  ASP E 160      -4.569 183.274-231.643  1.00156.90           C  
ANISOU18281  CA  ASP E 160    24249  23727  11638   3704   -900  -3849       C  
ATOM  18282  C   ASP E 160      -4.226 184.379-230.661  1.00149.25           C  
ANISOU18282  C   ASP E 160    22860  22864  10984   3408   -732  -3451       C  
ATOM  18283  O   ASP E 160      -3.526 185.326-231.009  1.00149.05           O  
ANISOU18283  O   ASP E 160    22647  23247  10740   3305   -430  -3218       O  
ATOM  18284  CB  ASP E 160      -5.798 183.663-232.469  1.00159.64           C  
ANISOU18284  CB  ASP E 160    24910  23964  11784   3484  -1207  -3801       C  
ATOM  18285  CG  ASP E 160      -5.515 184.807-233.429  1.00163.42           C  
ANISOU18285  CG  ASP E 160    25363  24898  11830   3373   -974  -3546       C  
ATOM  18286  OD1 ASP E 160      -5.071 184.536-234.565  1.00168.51           O  
ANISOU18286  OD1 ASP E 160    26214  25853  11957   3604   -831  -3733       O  
ATOM  18287  OD2 ASP E 160      -5.731 185.976-233.047  1.00161.61           O1-
ANISOU18287  OD2 ASP E 160    24930  24704  11770   3064   -919  -3155       O1-
ATOM  18288  N   LEU E 161      -4.720 184.255-229.433  1.00145.02           N  
ANISOU18288  N   LEU E 161    22197  21955  10949   3257   -926  -3373       N  
ATOM  18289  CA  LEU E 161      -4.340 185.193-228.382  1.00143.64           C  
ANISOU18289  CA  LEU E 161    21659  21848  11069   2986   -773  -3051       C  
ATOM  18290  C   LEU E 161      -2.842 185.109-228.090  1.00146.84           C  
ANISOU18290  C   LEU E 161    21721  22660  11411   3149   -416  -3044       C  
ATOM  18291  O   LEU E 161      -2.160 186.134-227.993  1.00147.71           O  
ANISOU18291  O   LEU E 161    21571  23099  11452   2927   -161  -2780       O  
ATOM  18292  CB  LEU E 161      -5.152 184.954-227.108  1.00139.81           C  
ANISOU18292  CB  LEU E 161    21128  20895  11099   2841  -1044  -2997       C  
ATOM  18293  CG  LEU E 161      -6.471 185.724-227.016  1.00137.46           C  
ANISOU18293  CG  LEU E 161    20966  20309  10954   2530  -1279  -2770       C  
ATOM  18294  CD1 LEU E 161      -7.151 185.478-225.678  1.00134.67           C  
ANISOU18294  CD1 LEU E 161    20524  19542  11103   2419  -1485  -2698       C  
ATOM  18295  CD2 LEU E 161      -6.232 187.210-227.231  1.00136.25           C  
ANISOU18295  CD2 LEU E 161    20708  20401  10660   2253  -1043  -2438       C  
ATOM  18296  N   VAL E 162      -2.336 183.885-227.961  1.00149.15           N  
ANISOU18296  N   VAL E 162    22010  22930  11728   3532   -396  -3318       N  
ATOM  18297  CA  VAL E 162      -0.910 183.669-227.727  1.00151.69           C  
ANISOU18297  CA  VAL E 162    21977  23677  11982   3760    -59  -3301       C  
ATOM  18298  C   VAL E 162      -0.074 184.172-228.899  1.00155.05           C  
ANISOU18298  C   VAL E 162    22351  24647  11913   3852    283  -3246       C  
ATOM  18299  O   VAL E 162       0.967 184.803-228.710  1.00154.21           O  
ANISOU18299  O   VAL E 162    21852  24992  11748   3758    580  -3016       O  
ATOM  18300  CB  VAL E 162      -0.600 182.181-227.481  1.00155.62           C  
ANISOU18300  CB  VAL E 162    22539  24007  12581   4233    -90  -3606       C  
ATOM  18301  CG1 VAL E 162       0.900 181.958-227.374  1.00159.88           C  
ANISOU18301  CG1 VAL E 162    22686  25055  13004   4533    288  -3554       C  
ATOM  18302  CG2 VAL E 162      -1.300 181.702-226.224  1.00152.29           C  
ANISOU18302  CG2 VAL E 162    22108  23093  12664   4136   -389  -3605       C  
ATOM  18303  N   ARG E 163      -0.544 183.898-230.111  1.00159.83           N  
ANISOU18303  N   ARG E 163    23351  25228  12151   4014    230  -3446       N  
ATOM  18304  CA  ARG E 163       0.137 184.346-231.319  1.00165.81           C  
ANISOU18304  CA  ARG E 163    24115  26496  12390   4121    548  -3396       C  
ATOM  18305  C   ARG E 163       0.109 185.870-231.442  1.00166.22           C  
ANISOU18305  C   ARG E 163    24001  26773  12381   3658    657  -2994       C  
ATOM  18306  O   ARG E 163       0.975 186.464-232.083  1.00170.25           O  
ANISOU18306  O   ARG E 163    24331  27788  12567   3656    999  -2822       O  
ATOM  18307  CB  ARG E 163      -0.491 183.691-232.551  1.00168.43           C  
ANISOU18307  CB  ARG E 163    24966  26712  12320   4372    415  -3721       C  
ATOM  18308  CG  ARG E 163      -0.375 182.175-232.554  1.00171.63           C  
ANISOU18308  CG  ARG E 163    25604  26874  12734   4847    353  -4148       C  
ATOM  18309  CD  ARG E 163      -1.371 181.527-233.505  1.00176.27           C  
ANISOU18309  CD  ARG E 163    26781  27152  13041   4941     60  -4495       C  
ATOM  18310  NE  ARG E 163      -1.295 180.068-233.453  1.00181.36           N  
ANISOU18310  NE  ARG E 163    27708  27475  13726   5364     -7  -4919       N  
ATOM  18311  CZ  ARG E 163      -2.161 179.248-234.041  1.00185.30           C  
ANISOU18311  CZ  ARG E 163    28743  27585  14076   5437   -316  -5286       C  
ATOM  18312  NH1 ARG E 163      -3.183 179.740-234.729  1.00186.37           N1+
ANISOU18312  NH1 ARG E 163    29120  27638  14054   5090   -603  -5234       N1+
ATOM  18313  NH2 ARG E 163      -2.009 177.933-233.938  1.00187.76           N  
ANISOU18313  NH2 ARG E 163    29290  27540  14510   5779   -339  -5628       N  
ATOM  18314  N   GLN E 164      -0.883 186.500-230.820  1.00162.85           N  
ANISOU18314  N   GLN E 164    23643  25962  12272   3275    386  -2830       N  
ATOM  18315  CA  GLN E 164      -0.987 187.955-230.841  1.00164.54           C  
ANISOU18315  CA  GLN E 164    23752  26287  12477   2839    487  -2445       C  
ATOM  18316  C   GLN E 164      -0.092 188.610-229.797  1.00164.88           C  
ANISOU18316  C   GLN E 164    23354  26507  12785   2573    690  -2197       C  
ATOM  18317  O   GLN E 164       0.459 189.687-230.031  1.00167.56           O  
ANISOU18317  O   GLN E 164    23524  27151  12988   2295    938  -1905       O  
ATOM  18318  CB  GLN E 164      -2.433 188.410-230.641  1.00162.12           C  
ANISOU18318  CB  GLN E 164    23715  25500  12383   2574    147  -2347       C  
ATOM  18319  CG  GLN E 164      -3.275 188.366-231.900  1.00164.38           C  
ANISOU18319  CG  GLN E 164    24386  25767  12303   2662     -7  -2417       C  
ATOM  18320  CD  GLN E 164      -4.568 189.138-231.755  1.00161.26           C  
ANISOU18320  CD  GLN E 164    24156  25023  12091   2363   -265  -2181       C  
ATOM  18321  OE1 GLN E 164      -4.750 189.892-230.798  1.00156.89           O  
ANISOU18321  OE1 GLN E 164    23449  24266  11897   2080   -254  -1936       O  
ATOM  18322  NE2 GLN E 164      -5.476 188.956-232.707  1.00163.64           N  
ANISOU18322  NE2 GLN E 164    24777  25268  12131   2433   -495  -2246       N  
ATOM  18323  N   ILE E 165       0.039 187.965-228.642  1.00162.19           N  
ANISOU18323  N   ILE E 165    22837  25974  12815   2635    572  -2304       N  
ATOM  18324  CA  ILE E 165       0.913 188.472-227.587  1.00160.22           C  
ANISOU18324  CA  ILE E 165    22160  25920  12797   2383    722  -2097       C  
ATOM  18325  C   ILE E 165       2.361 188.567-228.067  1.00167.36           C  
ANISOU18325  C   ILE E 165    22702  27476  13410   2493   1104  -1999       C  
ATOM  18326  O   ILE E 165       3.064 189.532-227.769  1.00168.53           O  
ANISOU18326  O   ILE E 165    22549  27917  13569   2128   1295  -1715       O  
ATOM  18327  CB  ILE E 165       0.842 187.596-226.318  1.00153.76           C  
ANISOU18327  CB  ILE E 165    21214  24831  12377   2505    524  -2240       C  
ATOM  18328  CG1 ILE E 165      -0.533 187.725-225.661  1.00147.05           C  
ANISOU18328  CG1 ILE E 165    20639  23380  11854   2305    185  -2245       C  
ATOM  18329  CG2 ILE E 165       1.925 187.989-225.328  1.00152.92           C  
ANISOU18329  CG2 ILE E 165    20630  25048  12424   2291    686  -2046       C  
ATOM  18330  CD1 ILE E 165      -0.670 186.939-224.381  1.00142.90           C  
ANISOU18330  CD1 ILE E 165    19997  22580  11719   2393     -6  -2343       C  
ATOM  18331  N   ASN E 166       2.792 187.567-228.829  1.00172.40           N  
ANISOU18331  N   ASN E 166    23385  28338  13783   2993   1221  -2229       N  
ATOM  18332  CA  ASN E 166       4.158 187.529-229.338  1.00177.48           C  
ANISOU18332  CA  ASN E 166    23670  29633  14132   3190   1613  -2134       C  
ATOM  18333  C   ASN E 166       4.320 188.333-230.626  1.00179.24           C  
ANISOU18333  C   ASN E 166    23997  30195  13909   3096   1857  -1974       C  
ATOM  18334  O   ASN E 166       5.406 188.384-231.202  1.00183.74           O  
ANISOU18334  O   ASN E 166    24284  31343  14186   3254   2213  -1861       O  
ATOM  18335  CB  ASN E 166       4.602 186.086-229.568  1.00181.43           C  
ANISOU18335  CB  ASN E 166    24185  30220  14532   3828   1684  -2444       C  
ATOM  18336  CG  ASN E 166       4.302 185.191-228.382  1.00179.69           C  
ANISOU18336  CG  ASN E 166    23936  29594  14743   3964   1422  -2607       C  
ATOM  18337  OD1 ASN E 166       3.716 184.121-228.532  1.00180.00           O  
ANISOU18337  OD1 ASN E 166    24321  29255  14816   4327   1246  -2927       O  
ATOM  18338  ND2 ASN E 166       4.701 185.630-227.191  1.00177.85           N  
ANISOU18338  ND2 ASN E 166    23308  29435  14833   3652   1389  -2382       N  
ATOM  18339  N   SER E 167       3.236 188.958-231.071  1.00176.02           N  
ANISOU18339  N   SER E 167    23978  29452  13449   2855   1672  -1933       N  
ATOM  18340  CA  SER E 167       3.248 189.730-232.304  1.00178.86           C  
ANISOU18340  CA  SER E 167    24487  30092  13382   2768   1871  -1759       C  
ATOM  18341  C   SER E 167       3.549 191.197-232.037  1.00177.75           C  
ANISOU18341  C   SER E 167    24125  30084  13326   2203   2025  -1330       C  
ATOM  18342  O   SER E 167       3.798 191.591-230.896  1.00174.51           O  
ANISOU18342  O   SER E 167    23453  29568  13284   1875   1978  -1199       O  
ATOM  18343  CB  SER E 167       1.923 189.577-233.031  1.00178.01           C  
ANISOU18343  CB  SER E 167    24917  29593  13126   2847   1587  -1924       C  
ATOM  18344  N   GLY E 168       3.527 192.004-233.096  1.00180.58           N  
ANISOU18344  N   GLY E 168    24617  30664  13330   2081   2208  -1111       N  
ATOM  18345  CA  GLY E 168       3.813 193.429-232.987  1.00180.22           C  
ANISOU18345  CA  GLY E 168    24423  30718  13333   1542   2384   -687       C  
ATOM  18346  C   GLY E 168       2.599 194.283-233.332  1.00177.26           C  
ANISOU18346  C   GLY E 168    24471  29915  12964   1296   2210   -531       C  
ATOM  18347  O   GLY E 168       2.683 195.503-233.389  1.00177.10           O  
ANISOU18347  O   GLY E 168    24436  29896  12956    876   2359   -173       O  
TER   
HETATM22095 MG    MG E 200     -18.705 181.594-215.895  1.00 88.34          MG  
ANISOU22095 MG    MG E 200    14087   9933   9545   1613  -3823   -993      MG  
HETATM22096  PB  GDP E 201     -20.578 181.567-218.258  1.00101.76           P  
ANISOU22096  PB  GDP E 201    15940  11709  11017   1350  -4407   -897       P  
HETATM22097  O1B GDP E 201     -19.826 182.311-219.331  1.00 94.16           O  
ANISOU22097  O1B GDP E 201    15131  11036   9611   1397  -4256  -1060       O  
HETATM22098  O2B GDP E 201     -19.614 180.733-217.451  1.00 92.47           O1-
ANISOU22098  O2B GDP E 201    14787  10382   9964   1485  -4291  -1142       O1-
HETATM22099  O3B GDP E 201     -21.289 182.549-217.352  1.00 91.26           O  
ANISOU22099  O3B GDP E 201    14392  10376   9906   1336  -4231   -455       O  
HETATM22100  O3A GDP E 201     -21.645 180.608-218.987  1.00183.04           O  
ANISOU22100  O3A GDP E 201    26288  21869  21390   1173  -4879   -920       O  
HETATM22101  PA  GDP E 201     -21.735 179.023-218.709  1.00105.24           P  
ANISOU22101  PA  GDP E 201    16527  11676  11784   1123  -5155  -1149       P  
HETATM22102  O1A GDP E 201     -20.418 178.360-219.040  1.00104.81           O1-
ANISOU22102  O1A GDP E 201    16724  11588  11509   1303  -5043  -1619       O1-
HETATM22103  O2A GDP E 201     -22.133 178.725-217.281  1.00103.25           O  
ANISOU22103  O2A GDP E 201    16051  11198  11980   1130  -5095   -882       O  
HETATM22104  O5' GDP E 201     -22.876 178.573-219.748  1.00102.94           O  
ANISOU22104  O5' GDP E 201    16303  11368  11441    862  -5621  -1124       O  
HETATM22105  C5' GDP E 201     -24.234 178.475-219.322  1.00115.95           C  
ANISOU22105  C5' GDP E 201    17701  12927  13429    656  -5866   -725       C  
HETATM22106  C4' GDP E 201     -24.991 177.576-220.290  1.00121.01           C  
ANISOU22106  C4' GDP E 201    18482  13482  14013    374  -6366   -864       C  
HETATM22107  O4' GDP E 201     -24.627 177.899-221.633  1.00125.87           O  
ANISOU22107  O4' GDP E 201    19338  14348  14137    375  -6437  -1125       O  
HETATM22108  C3' GDP E 201     -24.654 176.108-220.081  1.00123.34           C  
ANISOU22108  C3' GDP E 201    19014  13376  14476    327  -6539  -1220       C  
HETATM22109  O3' GDP E 201     -25.764 175.416-219.504  1.00125.11           O  
ANISOU22109  O3' GDP E 201    19050  13361  15127     68  -6835   -945       O  
HETATM22110  C2' GDP E 201     -24.382 175.548-221.462  1.00131.50           C  
ANISOU22110  C2' GDP E 201    20439  14418  15107    234  -6801  -1677       C  
HETATM22111  O2' GDP E 201     -25.306 174.498-221.758  1.00139.18           O  
ANISOU22111  O2' GDP E 201    21507  15129  16245   -110  -7283  -1724       O  
HETATM22112  C1' GDP E 201     -24.598 176.707-222.422  1.00132.04           C  
ANISOU22112  C1' GDP E 201    20451  14934  14784    217  -6791  -1541       C  
HETATM22113  N9  GDP E 201     -23.484 176.756-223.400  1.00131.63           N  
ANISOU22113  N9  GDP E 201    20752  15026  14235    400  -6647  -1996       N  
HETATM22114  C8  GDP E 201     -22.244 177.202-223.134  1.00127.53           C  
ANISOU22114  C8  GDP E 201    20277  14604  13574    716  -6204  -2143       C  
HETATM22115  N7  GDP E 201     -21.455 177.122-224.232  1.00128.53           N  
ANISOU22115  N7  GDP E 201    20724  14886  13223    828  -6159  -2537       N  
HETATM22116  C5  GDP E 201     -22.201 176.617-225.229  1.00132.31           C  
ANISOU22116  C5  GDP E 201    21407  15358  13507    581  -6588  -2673       C  
HETATM22117  C6  GDP E 201     -21.978 176.277-226.651  1.00136.60           C  
ANISOU22117  C6  GDP E 201    22349  16032  13521    542  -6779  -3076       C  
HETATM22118  O6  GDP E 201     -20.859 176.459-227.178  1.00135.86           O  
ANISOU22118  O6  GDP E 201    22464  16106  13052    811  -6482  -3369       O  
HETATM22119  N1  GDP E 201     -23.005 175.774-227.346  1.00141.28           N  
ANISOU22119  N1  GDP E 201    23064  16583  14035    203  -7279  -3107       N  
HETATM22120  C2  GDP E 201     -24.216 175.572-226.793  1.00140.69           C  
ANISOU22120  C2  GDP E 201    22720  16366  14371   -103  -7602  -2757       C  
HETATM22121  N2  GDP E 201     -25.198 175.060-227.575  1.00145.85           N  
ANISOU22121  N2  GDP E 201    23492  17021  14904   -481  -8131  -2801       N  
HETATM22122  N3  GDP E 201     -24.494 175.860-225.493  1.00136.02           N  
ANISOU22122  N3  GDP E 201    21739  15654  14289    -58  -7422  -2355       N  
HETATM22123  C4  GDP E 201     -23.541 176.376-224.680  1.00133.10           C  
ANISOU22123  C4  GDP E 201    21252  15296  14023    277  -6927  -2311       C  
HETATM22124 AL   AF3 E 202     -21.447 183.264-215.338  1.00 89.19          AL  
ANISOU22124 AL   AF3 E 202    13899   9981  10008   1426  -3858    -79      AL  
HETATM22125  F1  AF3 E 202     -21.193 184.736-216.012  1.00128.56           F  
ANISOU22125  F1  AF3 E 202    18973  15197  14675   1438  -3611      9       F  
HETATM22126  F2  AF3 E 202     -20.175 182.289-215.016  1.00129.10           F  
ANISOU22126  F2  AF3 E 202    19044  14978  15030   1513  -3824   -476       F  
HETATM22127  F3  AF3 E 202     -22.977 182.682-215.207  1.00128.78           F  
ANISOU22127  F3  AF3 E 202    18734  14844  15354   1319  -4175    237       F  
HETATM22227  O   HOH A1201     -15.591 200.739-195.285  1.00 62.29           O  
HETATM22228  O   HOH A1202     -36.218 189.419-191.622  1.00 94.82           O  
HETATM22229  O   HOH A1203      -6.961 179.279-206.270  1.00 90.28           O  
HETATM22230  O   HOH A1204     -46.386 193.067-201.650  1.00 93.69           O  
CONECT2209622097220982209922100
CONECT2209722096
CONECT2209822096
CONECT2209922096
CONECT221002209622101
CONECT2210122100221022210322104
CONECT2210222101
CONECT2210322101
CONECT221042210122105
CONECT221052210422106
CONECT22106221052210722108
CONECT221072210622112
CONECT22108221062210922110
CONECT2210922108
CONECT22110221082211122112
CONECT2211122110
CONECT22112221072211022113
CONECT22113221122211422123
CONECT221142211322115
CONECT221152211422116
CONECT22116221152211722123
CONECT22117221162211822119
CONECT2211822117
CONECT221192211722120
CONECT22120221192212122122
CONECT2212122120
CONECT221222212022123
CONECT22123221132211622122
CONECT22124221252212622127
CONECT2212522124
CONECT2212622124
CONECT2212722124
END



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