CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 2004212157366210

Job options:

ID        	=	 2004212157366210
JOBID     	=	 
USERID    	=	 meat
PRIVAT    	=	 0

NMODES    	=	 25
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 0

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   GLN A  22       9.802 -19.377  -1.129  1.00 35.84           N  
ANISOU    1  N   GLN A  22     4704   3783   5132  -1281    466   1031       N  
ATOM      2  CA  GLN A  22      10.738 -19.280  -0.006  1.00 48.46           C  
ANISOU    2  CA  GLN A  22     6415   5398   6602  -1206    528   1101       C  
ATOM      3  C   GLN A  22      12.158 -19.836  -0.278  1.00 51.61           C  
ANISOU    3  C   GLN A  22     6929   5717   6964  -1170    450   1051       C  
ATOM      4  O   GLN A  22      12.338 -21.014  -0.614  1.00 54.65           O  
ANISOU    4  O   GLN A  22     7324   5975   7465  -1225    408   1050       O  
ATOM      5  CB  GLN A  22      10.128 -19.949   1.231  1.00 51.07           C  
ANISOU    5  CB  GLN A  22     6727   5703   6974  -1245    647   1259       C  
ATOM      6  CG  GLN A  22      10.631 -19.422   2.560  1.00 52.19           C  
ANISOU    6  CG  GLN A  22     6952   5928   6951  -1166    739   1345       C  
ATOM      7  CD  GLN A  22       9.776 -19.904   3.732  1.00 53.73           C  
ANISOU    7  CD  GLN A  22     7110   6129   7174  -1212    875   1503       C  
ATOM      8  NE2 GLN A  22       9.217 -18.958   4.488  1.00 55.37           N  
ANISOU    8  NE2 GLN A  22     7287   6464   7287  -1176    981   1534       N  
ATOM      9  OE1 GLN A  22       9.606 -21.111   3.940  1.00 46.97           O  
ANISOU    9  OE1 GLN A  22     6253   5164   6431  -1282    890   1595       O  
ATOM     10  N   ALA A  23      13.157 -18.970  -0.101  1.00 44.71           N  
ANISOU   10  N   ALA A  23     6136   4913   5937  -1076    435   1006       N  
ATOM     11  CA  ALA A  23      14.573 -19.319  -0.266  1.00 40.83           C  
ANISOU   11  CA  ALA A  23     5748   4366   5400  -1027    369    957       C  
ATOM     12  C   ALA A  23      15.251 -19.703   1.074  1.00 39.15           C  
ANISOU   12  C   ALA A  23     5620   4139   5117   -980    423   1075       C  
ATOM     13  O   ALA A  23      14.686 -19.466   2.141  1.00 35.09           O  
ANISOU   13  O   ALA A  23     5097   3687   4550   -975    517   1183       O  
ATOM     14  CB  ALA A  23      15.297 -18.150  -0.903  1.00 25.79           C  
ANISOU   14  CB  ALA A  23     3875   2544   3380   -958    316    838       C  
ATOM     15  N   PRO A  24      16.471 -20.281   1.024  1.00 33.19           N  
ANISOU   15  N   PRO A  24     4946   3308   4358   -942    363   1053       N  
ATOM     16  CA  PRO A  24      17.118 -20.579   2.305  1.00 29.58           C  
ANISOU   16  CA  PRO A  24     4567   2849   3823   -892    401   1172       C  
ATOM     17  C   PRO A  24      17.459 -19.322   3.130  1.00 27.31           C  
ANISOU   17  C   PRO A  24     4322   2710   3346   -810    442   1178       C  
ATOM     18  O   PRO A  24      17.767 -18.226   2.594  1.00 27.02           O  
ANISOU   18  O   PRO A  24     4282   2751   3233   -767    413   1063       O  
ATOM     19  CB  PRO A  24      18.407 -21.313   1.897  1.00 27.84           C  
ANISOU   19  CB  PRO A  24     4409   2521   3647   -859    312   1122       C  
ATOM     20  CG  PRO A  24      18.647 -20.917   0.498  1.00 26.79           C  
ANISOU   20  CG  PRO A  24     4248   2387   3543   -865    241    951       C  
ATOM     21  CD  PRO A  24      17.299 -20.713  -0.119  1.00 26.98           C  
ANISOU   21  CD  PRO A  24     4180   2438   3633   -942    264    927       C  
ATOM     22  N   ARG A  25      17.399 -19.513   4.436  1.00 28.24           N  
ANISOU   22  N   ARG A  25     4480   2861   3388   -794    511   1314       N  
ATOM     23  CA  ARG A  25      17.704 -18.488   5.410  1.00 27.95           C  
ANISOU   23  CA  ARG A  25     4492   2961   3168   -722    557   1329       C  
ATOM     24  C   ARG A  25      19.174 -18.140   5.354  1.00 27.03           C  
ANISOU   24  C   ARG A  25     4452   2854   2965   -641    471   1253       C  
ATOM     25  O   ARG A  25      19.997 -19.002   5.111  1.00 27.18           O  
ANISOU   25  O   ARG A  25     4507   2771   3050   -633    399   1258       O  
ATOM     26  CB  ARG A  25      17.351 -19.002   6.813  1.00 29.47           C  
ANISOU   26  CB  ARG A  25     4720   3179   3298   -732    645   1503       C  
ATOM     27  CG  ARG A  25      15.879 -19.266   7.010  1.00 56.02           C  
ANISOU   27  CG  ARG A  25     8000   6546   6737   -813    751   1587       C  
ATOM     28  CD  ARG A  25      15.080 -17.993   6.810  1.00 58.15           C  
ANISOU   28  CD  ARG A  25     8200   6933   6959   -804    809   1501       C  
ATOM     29  NE  ARG A  25      13.879 -17.936   7.648  1.00 66.59           N  
ANISOU   29  NE  ARG A  25     9217   8068   8015   -845    946   1604       N  
ATOM     30  CZ  ARG A  25      13.845 -17.480   8.900  1.00 59.82           C  
ANISOU   30  CZ  ARG A  25     8407   7324   6996   -807   1040   1673       C  
ATOM     31  NH1 ARG A  25      14.947 -17.041   9.498  1.00 54.28           N1+
ANISOU   31  NH1 ARG A  25     7809   6684   6131   -728   1001   1652       N1+
ATOM     32  NH2 ARG A  25      12.700 -17.463   9.558  1.00 59.98           N  
ANISOU   32  NH2 ARG A  25     8370   7402   7019   -851   1174   1759       N  
ATOM     33  N   ARG A  26      19.496 -16.869   5.553  1.00 26.16           N  
ANISOU   33  N   ARG A  26     4358   2859   2722   -582    478   1176       N  
ATOM     34  CA  ARG A  26      20.878 -16.464   5.753  1.00 25.51           C  
ANISOU   34  CA  ARG A  26     4346   2803   2543   -504    409   1117       C  
ATOM     35  C   ARG A  26      21.480 -17.244   6.934  1.00 26.66           C  
ANISOU   35  C   ARG A  26     4567   2936   2627   -475    402   1248       C  
ATOM     36  O   ARG A  26      20.948 -17.202   8.025  1.00 27.65           O  
ANISOU   36  O   ARG A  26     4713   3133   2658   -479    479   1354       O  
ATOM     37  CB  ARG A  26      20.956 -14.966   6.049  1.00 28.27           C  
ANISOU   37  CB  ARG A  26     4700   3284   2757   -452    438   1035       C  
ATOM     38  CG  ARG A  26      22.385 -14.478   6.233  1.00 26.12           C  
ANISOU   38  CG  ARG A  26     4490   3041   2394   -378    364    963       C  
ATOM     39  CD  ARG A  26      22.478 -13.007   6.620  1.00 29.77           C  
ANISOU   39  CD  ARG A  26     4959   3623   2729   -330    394    880       C  
ATOM     40  NE  ARG A  26      21.687 -12.104   5.780  1.00 28.18           N  
ANISOU   40  NE  ARG A  26     4688   3444   2575   -351    430    796       N  
ATOM     41  CZ  ARG A  26      22.032 -11.708   4.555  1.00 24.03           C  
ANISOU   41  CZ  ARG A  26     4132   2880   2118   -353    373    691       C  
ATOM     42  NH1 ARG A  26      23.142 -12.158   3.990  1.00 24.29           N1+
ANISOU   42  NH1 ARG A  26     4194   2849   2188   -338    288    645       N1+
ATOM     43  NH2 ARG A  26      21.248 -10.878   3.887  1.00 21.21           N  
ANISOU   43  NH2 ARG A  26     3714   2550   1796   -370    403    636       N  
ATOM     44  N   PRO A  27      22.586 -17.965   6.700  1.00 27.20           N  
ANISOU   44  N   PRO A  27     4673   2914   2747   -447    310   1242       N  
ATOM     45  CA  PRO A  27      23.215 -18.814   7.728  1.00 27.88           C  
ANISOU   45  CA  PRO A  27     4827   2970   2796   -416    283   1377       C  
ATOM     46  C   PRO A  27      24.031 -18.025   8.742  1.00 27.91           C  
ANISOU   46  C   PRO A  27     4896   3099   2611   -339    263   1377       C  
ATOM     47  O   PRO A  27      24.351 -18.557   9.785  1.00 29.13           O  
ANISOU   47  O   PRO A  27     5108   3267   2693   -316    254   1507       O  
ATOM     48  CB  PRO A  27      24.158 -19.701   6.908  1.00 27.71           C  
ANISOU   48  CB  PRO A  27     4804   2804   2919   -404    184   1333       C  
ATOM     49  CG  PRO A  27      24.526 -18.828   5.718  1.00 26.10           C  
ANISOU   49  CG  PRO A  27     4563   2620   2735   -392    148   1144       C  
ATOM     50  CD  PRO A  27      23.293 -18.030   5.406  1.00 25.61           C  
ANISOU   50  CD  PRO A  27     4448   2632   2650   -441    228   1107       C  
ATOM     51  N   GLY A  28      24.364 -16.779   8.424  1.00 26.70           N  
ANISOU   51  N   GLY A  28     4731   3032   2382   -304    252   1234       N  
ATOM     52  CA  GLY A  28      25.227 -15.960   9.266  1.00 26.72           C  
ANISOU   52  CA  GLY A  28     4788   3146   2218   -233    220   1202       C  
ATOM     53  C   GLY A  28      25.841 -14.859   8.409  1.00 25.16           C  
ANISOU   53  C   GLY A  28     4562   2974   2025   -203    178   1021       C  
ATOM     54  O   GLY A  28      25.624 -14.837   7.208  1.00 24.25           O  
ANISOU   54  O   GLY A  28     4393   2791   2029   -235    173    941       O  
ATOM     55  N   ILE A  29      26.601 -13.953   9.008  1.00 25.00           N  
ANISOU   55  N   ILE A  29     4576   3050   1874   -147    149    959       N  
ATOM     56  CA  ILE A  29      27.277 -12.924   8.233  1.00 23.71           C  
ANISOU   56  CA  ILE A  29     4385   2900   1722   -120    109    797       C  
ATOM     57  C   ILE A  29      28.767 -13.220   8.122  1.00 23.61           C  
ANISOU   57  C   ILE A  29     4391   2845   1735    -70     -3    757       C  
ATOM     58  O   ILE A  29      29.333 -13.890   8.974  1.00 24.64           O  
ANISOU   58  O   ILE A  29     4566   2976   1820    -38    -54    847       O  
ATOM     59  CB  ILE A  29      27.064 -11.507   8.831  1.00 23.77           C  
ANISOU   59  CB  ILE A  29     4402   3038   1593    -96    158    722       C  
ATOM     60  CG1 ILE A  29      27.782 -11.371  10.181  1.00 26.23           C  
ANISOU   60  CG1 ILE A  29     4780   3441   1745    -45    122    756       C  
ATOM     61  CG2 ILE A  29      25.571 -11.206   8.996  1.00 23.77           C  
ANISOU   61  CG2 ILE A  29     4373   3082   1578   -139    276    761       C  
ATOM     62  CD1 ILE A  29      27.735  -9.946  10.740  1.00 27.79           C  
ANISOU   62  CD1 ILE A  29     4987   3758   1813    -19    161    652       C  
ATOM     63  N   GLY A  30      29.398 -12.682   7.083  1.00 22.48           N  
ANISOU   63  N   GLY A  30     4210   2669   1662    -62    -40    624       N  
ATOM     64  CA  GLY A  30      30.803 -12.932   6.816  1.00 22.36           C  
ANISOU   64  CA  GLY A  30     4194   2606   1695    -18   -136    569       C  
ATOM     65  C   GLY A  30      31.747 -12.211   7.759  1.00 22.87           C  
ANISOU   65  C   GLY A  30     4290   2764   1638     39   -190    534       C  
ATOM     66  O   GLY A  30      31.420 -11.140   8.278  1.00 22.59           O  
ANISOU   66  O   GLY A  30     4266   2828   1489     44   -149    490       O  
ATOM     67  N   THR A  31      32.916 -12.810   7.976  1.00 24.82           N  
ANISOU   67  N   THR A  31     4543   2971   1917     84   -285    547       N  
ATOM     68  CA  THR A  31      33.923 -12.288   8.897  1.00 25.90           C  
ANISOU   68  CA  THR A  31     4703   3190   1947    140   -360    520       C  
ATOM     69  C   THR A  31      35.281 -12.041   8.236  1.00 26.80           C  
ANISOU   69  C   THR A  31     4769   3263   2150    174   -439    401       C  
ATOM     70  O   THR A  31      36.192 -11.508   8.867  1.00 29.64           O  
ANISOU   70  O   THR A  31     5132   3688   2441    217   -508    355       O  
ATOM     71  CB  THR A  31      34.169 -13.267  10.062  1.00 32.02           C  
ANISOU   71  CB  THR A  31     5531   3977   2659    174   -420    672       C  
ATOM     72  CG2 THR A  31      32.879 -13.525  10.870  1.00 26.12           C  
ANISOU   72  CG2 THR A  31     4835   3284   1807    139   -334    804       C  
ATOM     73  OG1 THR A  31      34.680 -14.503   9.540  1.00 25.65           O  
ANISOU   73  OG1 THR A  31     4701   3037   2007    186   -475    727       O  
ATOM     74  N   VAL A  32      35.423 -12.436   6.973  1.00 22.93           N  
ANISOU   74  N   VAL A  32     4232   2670   1812    153   -428    348       N  
ATOM     75  CA  VAL A  32      36.716 -12.343   6.309  1.00 22.19           C  
ANISOU   75  CA  VAL A  32     4087   2530   1814    183   -491    243       C  
ATOM     76  C   VAL A  32      36.953 -10.957   5.700  1.00 21.13           C  
ANISOU   76  C   VAL A  32     3919   2447   1663    168   -458     98       C  
ATOM     77  O   VAL A  32      36.022 -10.317   5.206  1.00 25.57           O  
ANISOU   77  O   VAL A  32     4482   3029   2204    124   -377     70       O  
ATOM     78  CB  VAL A  32      36.869 -13.480   5.256  1.00 24.01           C  
ANISOU   78  CB  VAL A  32     4284   2626   2214    171   -492    246       C  
ATOM     79  CG1 VAL A  32      37.984 -13.187   4.278  1.00 26.88           C  
ANISOU   79  CG1 VAL A  32     4585   2949   2678    186   -517    110       C  
ATOM     80  CG2 VAL A  32      37.104 -14.821   5.964  1.00 24.21           C  
ANISOU   80  CG2 VAL A  32     4332   2585   2283    207   -555    379       C  
ATOM     81  N   GLY A  33      38.189 -10.478   5.773  1.00 21.23           N  
ANISOU   81  N   GLY A  33     3898   2477   1691    205   -523     13       N  
ATOM     82  CA  GLY A  33      38.594  -9.283   5.063  1.00 20.35           C  
ANISOU   82  CA  GLY A  33     3745   2388   1600    188   -495   -123       C  
ATOM     83  C   GLY A  33      38.696  -8.029   5.897  1.00 27.74           C  
ANISOU   83  C   GLY A  33     4695   3426   2420    198   -503   -177       C  
ATOM     84  O   GLY A  33      38.508  -8.070   7.114  1.00 26.95           O  
ANISOU   84  O   GLY A  33     4642   3396   2203    221   -536   -116       O  
ATOM     85  N   LYS A  34      39.002  -6.900   5.264  1.00 30.21           N  
ANISOU   85  N   LYS A  34     4970   3749   2761    178   -472   -292       N  
ATOM     86  CA  LYS A  34      39.148  -5.681   6.052  1.00 33.06           C  
ANISOU   86  CA  LYS A  34     5340   4194   3029    186   -482   -359       C  
ATOM     87  C   LYS A  34      37.905  -4.809   5.971  1.00 24.25           C  
ANISOU   87  C   LYS A  34     4250   3110   1853    150   -385   -366       C  
ATOM     88  O   LYS A  34      37.433  -4.497   4.889  1.00 22.87           O  
ANISOU   88  O   LYS A  34     4052   2890   1746    114   -319   -388       O  
ATOM     89  CB  LYS A  34      40.436  -4.908   5.728  1.00 42.96           C  
ANISOU   89  CB  LYS A  34     6531   5441   4351    194   -526   -483       C  
ATOM     90  CG  LYS A  34      40.503  -4.252   4.381  1.00 59.28           C  
ANISOU   90  CG  LYS A  34     8551   7455   6518    153   -456   -560       C  
ATOM     91  CD  LYS A  34      41.768  -3.399   4.238  1.00 71.87           C  
ANISOU   91  CD  LYS A  34    10083   9051   8175    156   -494   -677       C  
ATOM     92  CE  LYS A  34      41.929  -2.897   2.790  1.00 76.95           C  
ANISOU   92  CE  LYS A  34    10679   9636   8924    113   -420   -736       C  
ATOM     93  NZ  LYS A  34      43.267  -2.286   2.513  1.00 77.59           N1+
ANISOU   93  NZ  LYS A  34    10686   9703   9092    111   -450   -839       N1+
ATOM     94  N   PRO A  35      37.356  -4.442   7.138  1.00 20.07           N  
ANISOU   94  N   PRO A  35     3768   2663   1194    163   -378   -343       N  
ATOM     95  CA  PRO A  35      36.154  -3.610   7.175  1.00 29.01           C  
ANISOU   95  CA  PRO A  35     4919   3828   2277    138   -283   -352       C  
ATOM     96  C   PRO A  35      36.366  -2.298   6.428  1.00 29.31           C  
ANISOU   96  C   PRO A  35     4913   3843   2381    118   -248   -469       C  
ATOM     97  O   PRO A  35      37.466  -1.747   6.421  1.00 28.64           O  
ANISOU   97  O   PRO A  35     4795   3756   2332    128   -299   -559       O  
ATOM     98  CB  PRO A  35      35.946  -3.361   8.683  1.00 20.84           C  
ANISOU   98  CB  PRO A  35     3935   2896   1087    164   -298   -341       C  
ATOM     99  CG  PRO A  35      36.550  -4.564   9.314  1.00 24.15           C  
ANISOU   99  CG  PRO A  35     4382   3325   1467    194   -385   -252       C  
ATOM    100  CD  PRO A  35      37.761  -4.889   8.482  1.00 21.29           C  
ANISOU  100  CD  PRO A  35     3964   2887   1237    203   -456   -296       C  
ATOM    101  N   ILE A  36      35.318  -1.815   5.781  1.00 21.35           N  
ANISOU  101  N   ILE A  36     3896   2813   1402     88   -161   -460       N  
ATOM    102  CA  ILE A  36      35.396  -0.536   5.099  1.00 22.46           C  
ANISOU  102  CA  ILE A  36     3973   2931   1631     68   -120   -543       C  
ATOM    103  C   ILE A  36      34.069   0.191   5.241  1.00 23.99           C  
ANISOU  103  C   ILE A  36     4161   3146   1808     58    -35   -527       C  
ATOM    104  O   ILE A  36      33.009  -0.403   5.037  1.00 20.67           O  
ANISOU  104  O   ILE A  36     3771   2719   1362     46      9   -447       O  
ATOM    105  CB  ILE A  36      35.761  -0.700   3.606  1.00 27.71           C  
ANISOU  105  CB  ILE A  36     4614   3516   2397     39   -114   -553       C  
ATOM    106  CG1 ILE A  36      35.858   0.668   2.922  1.00 23.65           C  
ANISOU  106  CG1 ILE A  36     4039   2979   1968     18    -72   -621       C  
ATOM    107  CG2 ILE A  36      34.759  -1.663   2.865  1.00 17.12           C  
ANISOU  107  CG2 ILE A  36     3289   2143   1071     15    -78   -458       C  
ATOM    108  CD1 ILE A  36      36.314   0.586   1.456  1.00 16.06           C  
ANISOU  108  CD1 ILE A  36     3049   1955   1097    -13    -62   -630       C  
ATOM    109  N   LYS A  37      34.122   1.472   5.578  1.00 18.09           N  
ANISOU  109  N   LYS A  37     3376   2418   1080     62    -12   -608       N  
ATOM    110  CA  LYS A  37      32.898   2.236   5.783  1.00 26.31           C  
ANISOU  110  CA  LYS A  37     4414   3474   2108     63     67   -608       C  
ATOM    111  C   LYS A  37      32.363   2.773   4.458  1.00 21.10           C  
ANISOU  111  C   LYS A  37     3736   2741   1540     39    114   -602       C  
ATOM    112  O   LYS A  37      33.100   3.373   3.677  1.00 26.46           O  
ANISOU  112  O   LYS A  37     4383   3370   2300     25     98   -650       O  
ATOM    113  CB  LYS A  37      33.110   3.355   6.811  1.00 34.05           C  
ANISOU  113  CB  LYS A  37     5371   4504   3064     80     73   -706       C  
ATOM    114  CG  LYS A  37      31.809   3.937   7.344  1.00 50.29           C  
ANISOU  114  CG  LYS A  37     7435   6591   5081     92    157   -709       C  
ATOM    115  CD  LYS A  37      32.039   5.002   8.426  1.00 58.70           C  
ANISOU  115  CD  LYS A  37     8478   7709   6115    107    164   -822       C  
ATOM    116  CE  LYS A  37      32.252   4.389   9.811  1.00 68.19           C  
ANISOU  116  CE  LYS A  37     9708   9017   7183    115    134   -813       C  
ATOM    117  NZ  LYS A  37      30.978   4.001  10.496  1.00 69.79           N1+
ANISOU  117  NZ  LYS A  37     9940   9282   7293    127    208   -750       N1+
ATOM    118  N   LEU A  38      31.080   2.529   4.206  1.00 17.28           N  
ANISOU  118  N   LEU A  38     3276   2253   1037     31    174   -535       N  
ATOM    119  CA  LEU A  38      30.463   2.810   2.924  1.00 16.64           C  
ANISOU  119  CA  LEU A  38     3178   2113   1033      5    209   -504       C  
ATOM    120  C   LEU A  38      29.178   3.605   3.098  1.00 19.68           C  
ANISOU  120  C   LEU A  38     3539   2502   1435     16    283   -495       C  
ATOM    121  O   LEU A  38      28.602   3.626   4.167  1.00 22.20           O  
ANISOU  121  O   LEU A  38     3875   2874   1686     38    322   -500       O  
ATOM    122  CB  LEU A  38      30.105   1.496   2.224  1.00 16.21           C  
ANISOU  122  CB  LEU A  38     3126   2047    988    -23    192   -408       C  
ATOM    123  CG  LEU A  38      31.220   0.465   2.049  1.00 19.47           C  
ANISOU  123  CG  LEU A  38     3557   2449   1394    -29    125   -405       C  
ATOM    124  CD1 LEU A  38      30.668  -0.850   1.534  1.00 17.95           C  
ANISOU  124  CD1 LEU A  38     3368   2240   1212    -54    118   -315       C  
ATOM    125  CD2 LEU A  38      32.234   0.993   1.085  1.00 17.70           C  
ANISOU  125  CD2 LEU A  38     3308   2178   1239    -43    100   -465       C  
ATOM    126  N   LEU A  39      28.708   4.214   2.014  1.00 22.10           N  
ANISOU  126  N   LEU A  39     3806   2756   1834      0    304   -475       N  
ATOM    127  CA  LEU A  39      27.395   4.835   1.982  1.00 27.74           C  
ANISOU  127  CA  LEU A  39     4484   3466   2590     11    368   -447       C  
ATOM    128  C   LEU A  39      26.601   4.223   0.831  1.00 28.39           C  
ANISOU  128  C   LEU A  39     4537   3528   2721    -21    361   -348       C  
ATOM    129  O   LEU A  39      27.156   3.951  -0.245  1.00 21.86           O  
ANISOU  129  O   LEU A  39     3711   2669   1925    -51    317   -329       O  
ATOM    130  CB  LEU A  39      27.530   6.342   1.780  1.00 36.25           C  
ANISOU  130  CB  LEU A  39     5533   4491   3749     28    392   -516       C  
ATOM    131  CG  LEU A  39      28.351   7.106   2.821  1.00 40.50           C  
ANISOU  131  CG  LEU A  39     6094   5039   4257     54    394   -635       C  
ATOM    132  CD1 LEU A  39      28.770   8.446   2.244  1.00 39.82           C  
ANISOU  132  CD1 LEU A  39     5977   4873   4281     54    399   -693       C  
ATOM    133  CD2 LEU A  39      27.557   7.301   4.094  1.00 18.51           C  
ANISOU  133  CD2 LEU A  39     3316   2309   1407     89    454   -672       C  
ATOM    134  N   ALA A  40      25.309   3.987   1.047  1.00 25.11           N  
ANISOU  134  N   ALA A  40     4094   3135   2311    -18    406   -290       N  
ATOM    135  CA  ALA A  40      24.497   3.349   0.012  1.00 23.71           C  
ANISOU  135  CA  ALA A  40     3884   2946   2180    -52    390   -201       C  
ATOM    136  C   ALA A  40      23.342   4.258  -0.349  1.00 23.23           C  
ANISOU  136  C   ALA A  40     3759   2865   2201    -37    430   -175       C  
ATOM    137  O   ALA A  40      22.797   4.931   0.524  1.00 18.01           O  
ANISOU  137  O   ALA A  40     3077   2217   1548      0    492   -207       O  
ATOM    138  CB  ALA A  40      23.985   1.996   0.488  1.00 24.48           C  
ANISOU  138  CB  ALA A  40     3994   3082   2225    -72    395   -140       C  
ATOM    139  N   ASN A  41      22.957   4.274  -1.625  1.00 17.25           N  
ANISOU  139  N   ASN A  41     2969   2081   1506    -64    394   -118       N  
ATOM    140  CA  ASN A  41      21.827   5.091  -2.058  1.00 17.70           C  
ANISOU  140  CA  ASN A  41     2957   2117   1652    -48    417    -77       C  
ATOM    141  C   ASN A  41      20.491   4.457  -1.638  1.00 18.25           C  
ANISOU  141  C   ASN A  41     2978   2224   1734    -51    454    -22       C  
ATOM    142  O   ASN A  41      19.556   4.327  -2.430  1.00 19.65           O  
ANISOU  142  O   ASN A  41     3097   2398   1972    -69    432     46       O  
ATOM    143  CB  ASN A  41      21.896   5.406  -3.567  1.00 20.07           C  
ANISOU  143  CB  ASN A  41     3240   2382   2002    -75    358    -29       C  
ATOM    144  CG  ASN A  41      21.861   4.148  -4.443  1.00 24.45           C  
ANISOU  144  CG  ASN A  41     3808   2963   2519   -131    300     22       C  
ATOM    145  ND2 ASN A  41      21.494   4.319  -5.712  1.00 18.22           N  
ANISOU  145  ND2 ASN A  41     2993   2165   1765   -156    252     78       N  
ATOM    146  OD1 ASN A  41      22.153   3.039  -3.979  1.00 25.98           O  
ANISOU  146  OD1 ASN A  41     4037   3182   2653   -150    296     11       O  
ATOM    147  N   TYR A  42      20.441   4.060  -0.366  1.00 22.16           N  
ANISOU  147  N   TYR A  42     3494   2758   2166    -35    509    -50       N  
ATOM    148  CA  TYR A  42      19.257   3.530   0.290  1.00 25.93           C  
ANISOU  148  CA  TYR A  42     3928   3277   2648    -36    567     -5       C  
ATOM    149  C   TYR A  42      18.863   4.523   1.377  1.00 23.40           C  
ANISOU  149  C   TYR A  42     3586   2971   2336     20    657    -66       C  
ATOM    150  O   TYR A  42      19.707   5.026   2.096  1.00 24.93           O  
ANISOU  150  O   TYR A  42     3831   3169   2471     47    673   -148       O  
ATOM    151  CB  TYR A  42      19.572   2.169   0.916  1.00 26.36           C  
ANISOU  151  CB  TYR A  42     4035   3370   2609    -67    565     19       C  
ATOM    152  CG  TYR A  42      19.361   0.995  -0.020  1.00 25.30           C  
ANISOU  152  CG  TYR A  42     3892   3223   2497   -125    503     90       C  
ATOM    153  CD1 TYR A  42      19.699   1.078  -1.362  1.00 27.32           C  
ANISOU  153  CD1 TYR A  42     4144   3443   2793   -150    427     96       C  
ATOM    154  CD2 TYR A  42      18.826  -0.204   0.446  1.00 29.96           C  
ANISOU  154  CD2 TYR A  42     4479   3837   3065   -158    524    149       C  
ATOM    155  CE1 TYR A  42      19.493   0.008  -2.219  1.00 33.42           C  
ANISOU  155  CE1 TYR A  42     4911   4208   3581   -205    371    144       C  
ATOM    156  CE2 TYR A  42      18.622  -1.279  -0.401  1.00 31.28           C  
ANISOU  156  CE2 TYR A  42     4637   3984   3265   -214    467    201       C  
ATOM    157  CZ  TYR A  42      18.956  -1.164  -1.734  1.00 33.50           C  
ANISOU  157  CZ  TYR A  42     4914   4232   3582   -236    390    191       C  
ATOM    158  OH  TYR A  42      18.753  -2.223  -2.578  1.00 36.49           O  
ANISOU  158  OH  TYR A  42     5283   4593   3987   -294    333    225       O  
ATOM    159  N   PHE A  43      17.584   4.839   1.477  1.00 21.09           N  
ANISOU  159  N   PHE A  43     3209   2683   2121     37    715    -35       N  
ATOM    160  CA  PHE A  43      17.147   5.836   2.441  1.00 24.01           C  
ANISOU  160  CA  PHE A  43     3549   3060   2512     94    810   -104       C  
ATOM    161  C   PHE A  43      16.046   5.234   3.307  1.00 22.57           C  
ANISOU  161  C   PHE A  43     3324   2941   2312     91    901    -70       C  
ATOM    162  O   PHE A  43      15.034   4.751   2.796  1.00 22.58           O  
ANISOU  162  O   PHE A  43     3250   2944   2388     66    900     12       O  
ATOM    163  CB  PHE A  43      16.687   7.108   1.719  1.00 31.57           C  
ANISOU  163  CB  PHE A  43     4433   3949   3611    132    805   -113       C  
ATOM    164  CG  PHE A  43      17.768   7.751   0.872  1.00 31.66           C  
ANISOU  164  CG  PHE A  43     4488   3898   3643    130    727   -137       C  
ATOM    165  CD1 PHE A  43      18.527   8.797   1.371  1.00 28.48           C  
ANISOU  165  CD1 PHE A  43     4118   3459   3244    167    751   -238       C  
ATOM    166  CD2 PHE A  43      18.039   7.289  -0.404  1.00 23.89           C  
ANISOU  166  CD2 PHE A  43     3511   2894   2672     85    633    -63       C  
ATOM    167  CE1 PHE A  43      19.518   9.380   0.614  1.00 23.23           C  
ANISOU  167  CE1 PHE A  43     3486   2733   2606    159    688   -254       C  
ATOM    168  CE2 PHE A  43      19.036   7.868  -1.170  1.00 28.27           C  
ANISOU  168  CE2 PHE A  43     4104   3397   3239     79    575    -81       C  
ATOM    169  CZ  PHE A  43      19.776   8.915  -0.659  1.00 25.87           C  
ANISOU  169  CZ  PHE A  43     3827   3052   2949    115    604   -171       C  
ATOM    170  N   GLU A  44      16.271   5.227   4.614  1.00 26.71           N  
ANISOU  170  N   GLU A  44     3896   3522   2731    112    978   -130       N  
ATOM    171  CA  GLU A  44      15.349   4.587   5.555  1.00 31.94           C  
ANISOU  171  CA  GLU A  44     4532   4255   3348    104   1077    -94       C  
ATOM    172  C   GLU A  44      13.925   5.132   5.483  1.00 27.94           C  
ANISOU  172  C   GLU A  44     3902   3741   2974    129   1159    -78       C  
ATOM    173  O   GLU A  44      13.704   6.345   5.456  1.00 24.66           O  
ANISOU  173  O   GLU A  44     3439   3286   2644    183   1192   -148       O  
ATOM    174  CB  GLU A  44      15.892   4.668   6.985  1.00 38.89           C  
ANISOU  174  CB  GLU A  44     5492   5207   4076    127   1146   -172       C  
ATOM    175  CG  GLU A  44      17.249   3.988   7.168  1.00 50.18           C  
ANISOU  175  CG  GLU A  44     7035   6654   5376    103   1062   -175       C  
ATOM    176  CD  GLU A  44      17.775   4.062   8.599  1.00 59.20           C  
ANISOU  176  CD  GLU A  44     8258   7879   6355    126   1116   -247       C  
ATOM    177  OE1 GLU A  44      19.008   3.938   8.782  1.00 59.33           O  
ANISOU  177  OE1 GLU A  44     8357   7902   6282    124   1040   -285       O  
ATOM    178  OE2 GLU A  44      16.961   4.233   9.536  1.00 64.60           O1-
ANISOU  178  OE2 GLU A  44     8919   8628   6997    144   1233   -265       O1-
ATOM    179  N   VAL A  45      12.965   4.216   5.418  1.00 28.29           N  
ANISOU  179  N   VAL A  45     3886   3814   3050     90   1188     16       N  
ATOM    180  CA  VAL A  45      11.551   4.566   5.428  1.00 29.48           C  
ANISOU  180  CA  VAL A  45     3905   3967   3329    109   1271     39       C  
ATOM    181  C   VAL A  45      10.922   4.122   6.753  1.00 33.75           C  
ANISOU  181  C   VAL A  45     4439   4594   3791    106   1415     40       C  
ATOM    182  O   VAL A  45      11.170   3.014   7.235  1.00 38.35           O  
ANISOU  182  O   VAL A  45     5085   5225   4260     57   1422     97       O  
ATOM    183  CB  VAL A  45      10.802   3.917   4.241  1.00 33.93           C  
ANISOU  183  CB  VAL A  45     4382   4496   4013     60   1193    147       C  
ATOM    184  CG1 VAL A  45       9.327   4.298   4.251  1.00 26.58           C  
ANISOU  184  CG1 VAL A  45     3301   3569   3231     82   1272    172       C  
ATOM    185  CG2 VAL A  45      11.461   4.311   2.886  1.00 25.15           C  
ANISOU  185  CG2 VAL A  45     3289   3313   2954     58   1051    153       C  
ATOM    186  N   ASP A  46      10.127   4.998   7.349  1.00 33.24           N  
ANISOU  186  N   ASP A  46     4297   4545   3787    159   1533    -22       N  
ATOM    187  CA  ASP A  46       9.410   4.668   8.577  1.00 36.83           C  
ANISOU  187  CA  ASP A  46     4732   5090   4174    158   1689    -25       C  
ATOM    188  C   ASP A  46       7.936   4.567   8.245  1.00 36.53           C  
ANISOU  188  C   ASP A  46     4533   5043   4302    150   1752     40       C  
ATOM    189  O   ASP A  46       7.310   5.552   7.858  1.00 37.22           O  
ANISOU  189  O   ASP A  46     4515   5082   4544    204   1771     -2       O  
ATOM    190  CB  ASP A  46       9.611   5.756   9.626  1.00 44.37           C  
ANISOU  190  CB  ASP A  46     5716   6078   5062    226   1796   -167       C  
ATOM    191  CG  ASP A  46      10.969   5.683  10.295  1.00 62.95           C  
ANISOU  191  CG  ASP A  46     8228   8473   7219    225   1758   -232       C  
ATOM    192  OD1 ASP A  46      11.900   5.072   9.724  1.00 66.98           O  
ANISOU  192  OD1 ASP A  46     8816   8955   7679    187   1628   -181       O  
ATOM    193  OD2 ASP A  46      11.103   6.248  11.403  1.00 74.04           O1-
ANISOU  193  OD2 ASP A  46     9673   9939   8519    263   1858   -340       O1-
ATOM    194  N   ILE A  47       7.372   3.378   8.365  1.00 33.27           N  
ANISOU  194  N   ILE A  47     4094   4672   3877     84   1781    146       N  
ATOM    195  CA  ILE A  47       5.956   3.249   8.085  1.00 36.94           C  
ANISOU  195  CA  ILE A  47     4394   5133   4508     71   1842    206       C  
ATOM    196  C   ILE A  47       5.177   3.057   9.381  1.00 38.13           C  
ANISOU  196  C   ILE A  47     4507   5375   4606     70   2037    200       C  
ATOM    197  O   ILE A  47       5.644   2.405  10.312  1.00 37.40           O  
ANISOU  197  O   ILE A  47     4522   5354   4334     40   2096    216       O  
ATOM    198  CB  ILE A  47       5.676   2.127   7.069  1.00 40.63           C  
ANISOU  198  CB  ILE A  47     4822   5564   5052    -10   1729    329       C  
ATOM    199  CG1 ILE A  47       5.731   0.755   7.730  1.00 39.07           C  
ANISOU  199  CG1 ILE A  47     4685   5421   4740    -87   1776    414       C  
ATOM    200  CG2 ILE A  47       6.688   2.196   5.922  1.00 42.61           C  
ANISOU  200  CG2 ILE A  47     5148   5744   5297    -17   1545    327       C  
ATOM    201  CD1 ILE A  47       5.412  -0.382   6.778  1.00 42.97           C  
ANISOU  201  CD1 ILE A  47     5134   5870   5322   -171   1673    522       C  
ATOM    202  N   PRO A  48       3.996   3.671   9.458  1.00 38.75           N  
ANISOU  202  N   PRO A  48     4431   5454   4838    108   2141    177       N  
ATOM    203  CA  PRO A  48       3.096   3.452  10.590  1.00 39.01           C  
ANISOU  203  CA  PRO A  48     4404   5576   4844    102   2340    179       C  
ATOM    204  C   PRO A  48       2.556   2.026  10.565  1.00 47.66           C  
ANISOU  204  C   PRO A  48     5466   6701   5943      4   2354    323       C  
ATOM    205  O   PRO A  48       2.374   1.459   9.485  1.00 50.67           O  
ANISOU  205  O   PRO A  48     5794   7018   6440    -45   2223    406       O  
ATOM    206  CB  PRO A  48       1.972   4.457  10.335  1.00 39.32           C  
ANISOU  206  CB  PRO A  48     4260   5580   5101    168   2410    126       C  
ATOM    207  CG  PRO A  48       1.996   4.678   8.851  1.00 43.47           C  
ANISOU  207  CG  PRO A  48     4726   6001   5791    171   2222    169       C  
ATOM    208  CD  PRO A  48       3.443   4.615   8.471  1.00 40.88           C  
ANISOU  208  CD  PRO A  48     4572   5640   5321    161   2076    152       C  
ATOM    209  N   LYS A  49       2.311   1.455  11.739  1.00 55.17           N  
ANISOU  209  N   LYS A  49     6450   7747   6765    -27   2511    351       N  
ATOM    210  CA  LYS A  49       1.777   0.101  11.846  1.00 58.32           C  
ANISOU  210  CA  LYS A  49     6818   8170   7171   -124   2545    494       C  
ATOM    211  C   LYS A  49       0.261   0.115  11.669  1.00 59.77           C  
ANISOU  211  C   LYS A  49     6789   8352   7567   -139   2647    531       C  
ATOM    212  O   LYS A  49      -0.482  -0.179  12.604  1.00 64.68           O  
ANISOU  212  O   LYS A  49     7358   9053   8164   -162   2831    560       O  
ATOM    213  CB  LYS A  49       2.140  -0.496  13.210  1.00 64.72           C  
ANISOU  213  CB  LYS A  49     7755   9087   7750   -152   2677    524       C  
ATOM    214  CG  LYS A  49       3.385  -1.372  13.221  1.00 70.44           C  
ANISOU  214  CG  LYS A  49     8658   9802   8304   -196   2552    587       C  
ATOM    215  CD  LYS A  49       4.449  -0.871  12.260  1.00 76.83           C  
ANISOU  215  CD  LYS A  49     9540  10528   9126   -157   2356    519       C  
ATOM    216  CE  LYS A  49       5.282   0.264  12.828  1.00 79.64           C  
ANISOU  216  CE  LYS A  49     9992  10918   9348    -73   2369    374       C  
ATOM    217  NZ  LYS A  49       6.418   0.577  11.907  1.00 76.10           N1+
ANISOU  217  NZ  LYS A  49     9623  10387   8903    -51   2177    330       N1+
ATOM    218  N   ILE A  50      -0.194   0.454  10.467  1.00 56.31           N  
ANISOU  218  N   ILE A  50     6227   7829   7338   -127   2526    533       N  
ATOM    219  CA  ILE A  50      -1.615   0.663  10.214  1.00 40.94           C  
ANISOU  219  CA  ILE A  50     4062   5875   5619   -125   2603    552       C  
ATOM    220  C   ILE A  50      -2.177  -0.169   9.057  1.00 53.46           C  
ANISOU  220  C   ILE A  50     5538   7396   7377   -203   2466    659       C  
ATOM    221  O   ILE A  50      -1.431  -0.772   8.267  1.00 53.05           O  
ANISOU  221  O   ILE A  50     5580   7292   7283   -250   2293    703       O  
ATOM    222  CB  ILE A  50      -1.911   2.149   9.909  1.00 41.18           C  
ANISOU  222  CB  ILE A  50     3998   5868   5782    -14   2603    437       C  
ATOM    223  CG1 ILE A  50      -1.308   2.554   8.565  1.00 48.90           C  
ANISOU  223  CG1 ILE A  50     5001   6748   6832      9   2375    432       C  
ATOM    224  CG2 ILE A  50      -1.354   3.039  10.989  1.00 45.44           C  
ANISOU  224  CG2 ILE A  50     4639   6460   6165     65   2729    309       C  
ATOM    225  CD1 ILE A  50      -1.758   3.909   8.086  1.00 51.46           C  
ANISOU  225  CD1 ILE A  50     5206   7015   7331    109   2357    354       C  
ATOM    226  N   ASP A  51      -3.506  -0.183   8.967  1.00 48.86           N  
ANISOU  226  N   ASP A  51     4751   6820   6993   -218   2546    691       N  
ATOM    227  CA  ASP A  51      -4.217  -0.742   7.824  1.00 50.19           C  
ANISOU  227  CA  ASP A  51     4778   6929   7361   -280   2413    770       C  
ATOM    228  C   ASP A  51      -4.514   0.351   6.808  1.00 50.22           C  
ANISOU  228  C   ASP A  51     4673   6874   7535   -201   2290    716       C  
ATOM    229  O   ASP A  51      -4.999   1.428   7.156  1.00 54.48           O  
ANISOU  229  O   ASP A  51     5120   7424   8158   -110   2388    642       O  
ATOM    230  CB  ASP A  51      -5.541  -1.367   8.265  1.00 56.67           C  
ANISOU  230  CB  ASP A  51     5419   7789   8324   -344   2562    839       C  
ATOM    231  CG  ASP A  51      -5.351  -2.631   9.070  1.00 65.72           C  
ANISOU  231  CG  ASP A  51     6658   8978   9334   -444   2660    928       C  
ATOM    232  OD1 ASP A  51      -4.355  -3.347   8.821  1.00 68.09           O  
ANISOU  232  OD1 ASP A  51     7124   9248   9500   -491   2542    967       O  
ATOM    233  OD2 ASP A  51      -6.197  -2.907   9.952  1.00 70.52           O1-
ANISOU  233  OD2 ASP A  51     7198   9646   9950   -472   2808    944       O1-
ATOM    234  N   VAL A  52      -4.224   0.073   5.548  1.00 49.40           N  
ANISOU  234  N   VAL A  52     4580   6708   7483   -234   2076    754       N  
ATOM    235  CA  VAL A  52      -4.582   0.991   4.488  1.00 40.47           C  
ANISOU  235  CA  VAL A  52     3337   5523   6517   -170   1942    731       C  
ATOM    236  C   VAL A  52      -5.670   0.322   3.667  1.00 45.90           C  
ANISOU  236  C   VAL A  52     3841   6196   7403   -243   1858    812       C  
ATOM    237  O   VAL A  52      -5.798  -0.898   3.676  1.00 52.39           O  
ANISOU  237  O   VAL A  52     4671   7028   8208   -351   1852    878       O  
ATOM    238  CB  VAL A  52      -3.355   1.357   3.627  1.00 38.98           C  
ANISOU  238  CB  VAL A  52     3308   5283   6220   -143   1756    705       C  
ATOM    239  CG1 VAL A  52      -2.206   1.768   4.528  1.00 38.23           C  
ANISOU  239  CG1 VAL A  52     3404   5208   5915    -95   1838    630       C  
ATOM    240  CG2 VAL A  52      -2.936   0.191   2.771  1.00 37.47           C  
ANISOU  240  CG2 VAL A  52     3186   5070   5982   -247   1596    773       C  
ATOM    241  N   TYR A  53      -6.467   1.111   2.964  1.00 49.83           N  
ANISOU  241  N   TYR A  53     4168   6665   8099   -187   1790    807       N  
ATOM    242  CA  TYR A  53      -7.613   0.559   2.256  1.00 49.02           C  
ANISOU  242  CA  TYR A  53     3865   6558   8203   -251   1715    876       C  
ATOM    243  C   TYR A  53      -7.443   0.572   0.738  1.00 47.30           C  
ANISOU  243  C   TYR A  53     3641   6295   8037   -267   1454    908       C  
ATOM    244  O   TYR A  53      -7.099   1.591   0.148  1.00 43.54           O  
ANISOU  244  O   TYR A  53     3188   5786   7570   -181   1354    880       O  
ATOM    245  CB  TYR A  53      -8.889   1.264   2.710  1.00 53.70           C  
ANISOU  245  CB  TYR A  53     4227   7168   9008   -187   1853    859       C  
ATOM    246  CG  TYR A  53      -9.114   1.101   4.196  1.00 57.59           C  
ANISOU  246  CG  TYR A  53     4725   7720   9436   -188   2121    831       C  
ATOM    247  CD1 TYR A  53      -9.911   0.073   4.688  1.00 61.86           C  
ANISOU  247  CD1 TYR A  53     5162   8302  10041   -286   2237    892       C  
ATOM    248  CD2 TYR A  53      -8.506   1.955   5.109  1.00 57.80           C  
ANISOU  248  CD2 TYR A  53     4866   7765   9331    -97   2258    743       C  
ATOM    249  CE1 TYR A  53     -10.113  -0.088   6.046  1.00 63.15           C  
ANISOU  249  CE1 TYR A  53     5342   8528  10123   -291   2482    874       C  
ATOM    250  CE2 TYR A  53      -8.702   1.801   6.468  1.00 61.62           C  
ANISOU  250  CE2 TYR A  53     5362   8318   9733   -100   2502    713       C  
ATOM    251  CZ  TYR A  53      -9.505   0.778   6.930  1.00 63.08           C  
ANISOU  251  CZ  TYR A  53     5455   8548   9964   -197   2609    782       C  
ATOM    252  OH  TYR A  53      -9.694   0.618   8.280  1.00 62.05           O  
ANISOU  252  OH  TYR A  53     5394   8494   9690   -203   2795    744       O  
ATOM    253  N   HIS A  54      -7.686  -0.585   0.127  1.00 48.53           N  
ANISOU  253  N   HIS A  54     3768   6450   8222   -383   1349    966       N  
ATOM    254  CA  HIS A  54      -7.365  -0.835  -1.274  1.00 45.85           C  
ANISOU  254  CA  HIS A  54     3462   6081   7878   -423   1103    989       C  
ATOM    255  C   HIS A  54      -8.644  -0.946  -2.103  1.00 49.81           C  
ANISOU  255  C   HIS A  54     3728   6585   8612   -455    992   1035       C  
ATOM    256  O   HIS A  54      -9.452  -1.856  -1.907  1.00 51.31           O  
ANISOU  256  O   HIS A  54     3796   6790   8910   -546   1038   1069       O  
ATOM    257  CB  HIS A  54      -6.534  -2.123  -1.366  1.00 45.74           C  
ANISOU  257  CB  HIS A  54     3615   6060   7706   -533   1055   1003       C  
ATOM    258  CG  HIS A  54      -6.137  -2.511  -2.757  1.00 49.48           C  
ANISOU  258  CG  HIS A  54     4139   6510   8151   -585    818   1013       C  
ATOM    259  CD2 HIS A  54      -6.235  -1.853  -3.938  1.00 50.13           C  
ANISOU  259  CD2 HIS A  54     4175   6585   8285   -547    635   1016       C  
ATOM    260  ND1 HIS A  54      -5.545  -3.723  -3.045  1.00 47.82           N  
ANISOU  260  ND1 HIS A  54     4045   6284   7842   -689    751   1019       N  
ATOM    261  CE1 HIS A  54      -5.300  -3.796  -4.340  1.00 48.84           C  
ANISOU  261  CE1 HIS A  54     4197   6401   7957   -715    543   1014       C  
ATOM    262  NE2 HIS A  54      -5.709  -2.674  -4.905  1.00 49.73           N  
ANISOU  262  NE2 HIS A  54     4217   6525   8152   -631    467   1017       N  
ATOM    263  N   TYR A  55      -8.830  -0.011  -3.027  1.00 49.19           N  
ANISOU  263  N   TYR A  55     3583   6492   8615   -382    844   1039       N  
ATOM    264  CA  TYR A  55     -10.018  -0.014  -3.863  1.00 44.84           C  
ANISOU  264  CA  TYR A  55     2805   5948   8282   -402    716   1085       C  
ATOM    265  C   TYR A  55      -9.651  -0.315  -5.293  1.00 50.93           C  
ANISOU  265  C   TYR A  55     3634   6716   8999   -452    456   1108       C  
ATOM    266  O   TYR A  55      -8.529  -0.060  -5.727  1.00 45.69           O  
ANISOU  266  O   TYR A  55     3165   6039   8157   -429    374   1090       O  
ATOM    267  CB  TYR A  55     -10.750   1.325  -3.788  1.00 49.11           C  
ANISOU  267  CB  TYR A  55     3182   6479   9000   -272    750   1085       C  
ATOM    268  CG  TYR A  55     -11.274   1.630  -2.413  1.00 54.15           C  
ANISOU  268  CG  TYR A  55     3733   7128   9715   -222   1013   1050       C  
ATOM    269  CD1 TYR A  55     -12.607   1.400  -2.086  1.00 60.33           C  
ANISOU  269  CD1 TYR A  55     4269   7933  10721   -245   1101   1073       C  
ATOM    270  CD2 TYR A  55     -10.430   2.124  -1.429  1.00 53.53           C  
ANISOU  270  CD2 TYR A  55     3816   7044   9479   -158   1179    990       C  
ATOM    271  CE1 TYR A  55     -13.087   1.666  -0.808  1.00 60.04           C  
ANISOU  271  CE1 TYR A  55     4154   7916  10745   -202   1359   1037       C  
ATOM    272  CE2 TYR A  55     -10.896   2.390  -0.158  1.00 60.26           C  
ANISOU  272  CE2 TYR A  55     4598   7918  10381   -117   1425    949       C  
ATOM    273  CZ  TYR A  55     -12.222   2.164   0.147  1.00 59.20           C  
ANISOU  273  CZ  TYR A  55     4221   7808  10462   -137   1520    973       C  
ATOM    274  OH  TYR A  55     -12.665   2.437   1.415  1.00 63.92           O  
ANISOU  274  OH  TYR A  55     4754   8436  11097    -96   1778    927       O  
ATOM    275  N   GLU A  56     -10.613  -0.861  -6.022  1.00 57.07           N  
ANISOU  275  N   GLU A  56     4241   7513   9932   -524    329   1144       N  
ATOM    276  CA  GLU A  56     -10.429  -1.148  -7.426  1.00 63.84           C  
ANISOU  276  CA  GLU A  56     5128   8381  10746   -576     74   1162       C  
ATOM    277  C   GLU A  56     -11.112  -0.060  -8.246  1.00 66.77           C  
ANISOU  277  C   GLU A  56     5346   8761  11261   -486    -71   1205       C  
ATOM    278  O   GLU A  56     -12.268   0.292  -7.992  1.00 64.33           O  
ANISOU  278  O   GLU A  56     4810   8459  11174   -450    -26   1231       O  
ATOM    279  CB  GLU A  56     -11.010  -2.524  -7.764  1.00 73.33           C  
ANISOU  279  CB  GLU A  56     6246   9598  12018   -724      6   1166       C  
ATOM    280  CG  GLU A  56     -10.326  -3.216  -8.934  1.00 85.56           C  
ANISOU  280  CG  GLU A  56     7931  11155  13424   -809   -205   1148       C  
ATOM    281  CD  GLU A  56     -11.254  -3.423 -10.114  1.00 97.79           C  
ANISOU  281  CD  GLU A  56     9309  12740  15108   -863   -428   1171       C  
ATOM    282  OE1 GLU A  56     -12.329  -4.032  -9.925  1.00102.95           O  
ANISOU  282  OE1 GLU A  56     9766  13399  15951   -934   -407   1181       O  
ATOM    283  OE2 GLU A  56     -10.911  -2.972 -11.228  1.00100.30           O1-
ANISOU  283  OE2 GLU A  56     9684  13083  15341   -837   -624   1180       O1-
ATOM    284  N   VAL A  57     -10.385   0.496  -9.209  1.00 68.10           N  
ANISOU  284  N   VAL A  57     5639   8930  11306   -447   -238   1219       N  
ATOM    285  CA  VAL A  57     -11.006   1.365 -10.196  1.00 72.75           C  
ANISOU  285  CA  VAL A  57     6094   9532  12014   -380   -420   1280       C  
ATOM    286  C   VAL A  57     -10.887   0.704 -11.556  1.00 75.10           C  
ANISOU  286  C   VAL A  57     6432   9876  12227   -474   -669   1296       C  
ATOM    287  O   VAL A  57      -9.856   0.117 -11.891  1.00 74.22           O  
ANISOU  287  O   VAL A  57     6525   9770  11905   -538   -712   1259       O  
ATOM    288  CB  VAL A  57     -10.388   2.787 -10.233  1.00 63.57           C  
ANISOU  288  CB  VAL A  57     5018   8330  10805   -239   -411   1299       C  
ATOM    289  CG1 VAL A  57     -10.405   3.411  -8.849  1.00 64.80           C  
ANISOU  289  CG1 VAL A  57     5156   8442  11023   -151   -157   1259       C  
ATOM    290  CG2 VAL A  57      -8.976   2.757 -10.780  1.00 60.82           C  
ANISOU  290  CG2 VAL A  57     4932   7980  10197   -257   -487   1282       C  
ATOM    291  N   ASP A  58     -11.964   0.762 -12.324  1.00 79.36           N  
ANISOU  291  N   ASP A  58     6769  10452  12933   -486   -833   1345       N  
ATOM    292  CA  ASP A  58     -11.903   0.328 -13.706  1.00 85.51           C  
ANISOU  292  CA  ASP A  58     7578  11286  13626   -561  -1092   1362       C  
ATOM    293  C   ASP A  58     -12.546   1.402 -14.567  1.00 83.33           C  
ANISOU  293  C   ASP A  58     7165  11033  13462   -469  -1270   1450       C  
ATOM    294  O   ASP A  58     -13.589   1.958 -14.225  1.00 85.93           O  
ANISOU  294  O   ASP A  58     7273  11350  14027   -401  -1236   1492       O  
ATOM    295  CB  ASP A  58     -12.569  -1.037 -13.907  1.00 92.32           C  
ANISOU  295  CB  ASP A  58     8338  12181  14560   -710  -1152   1323       C  
ATOM    296  CG  ASP A  58     -14.072  -0.967 -13.824  1.00100.93           C  
ANISOU  296  CG  ASP A  58     9126  13287  15934   -707  -1179   1361       C  
ATOM    297  OD1 ASP A  58     -14.750  -1.581 -14.677  1.00104.14           O  
ANISOU  297  OD1 ASP A  58     9440  13740  16389   -791  -1359   1354       O  
ATOM    298  OD2 ASP A  58     -14.576  -0.291 -12.904  1.00104.65           O1-
ANISOU  298  OD2 ASP A  58     9476  13723  16563   -616  -1010   1383       O1-
ATOM    299  N   ILE A  59     -11.894   1.712 -15.675  1.00 77.16           N  
ANISOU  299  N   ILE A  59     6519  10287  12512   -464  -1456   1484       N  
ATOM    300  CA  ILE A  59     -12.328   2.803 -16.519  1.00 72.12           C  
ANISOU  300  CA  ILE A  59     5787   9667  11947   -369  -1629   1586       C  
ATOM    301  C   ILE A  59     -12.617   2.256 -17.906  1.00 75.41           C  
ANISOU  301  C   ILE A  59     6182  10177  12294   -459  -1906   1610       C  
ATOM    302  O   ILE A  59     -11.894   1.395 -18.399  1.00 74.32           O  
ANISOU  302  O   ILE A  59     6211  10079  11951   -564  -1966   1549       O  
ATOM    303  CB  ILE A  59     -11.240   3.888 -16.589  1.00 63.00           C  
ANISOU  303  CB  ILE A  59     4824   8469  10646   -265  -1594   1623       C  
ATOM    304  CG1 ILE A  59     -10.793   4.276 -15.177  1.00 56.83           C  
ANISOU  304  CG1 ILE A  59     4097   7601   9893   -195  -1315   1570       C  
ATOM    305  CG2 ILE A  59     -11.741   5.103 -17.334  1.00 63.86           C  
ANISOU  305  CG2 ILE A  59     4824   8577  10861   -154  -1751   1746       C  
ATOM    306  CD1 ILE A  59      -9.520   5.104 -15.135  1.00 52.41           C  
ANISOU  306  CD1 ILE A  59     3759   6994   9162   -122  -1258   1575       C  
ATOM    307  N   LYS A  60     -13.696   2.730 -18.520  1.00 81.07           N  
ANISOU  307  N   LYS A  60     6754  10916  13132   -412  -2038   1664       N  
ATOM    308  CA  LYS A  60     -13.982   2.396 -19.906  1.00 82.25           C  
ANISOU  308  CA  LYS A  60     6943  11151  13157   -473  -2279   1669       C  
ATOM    309  C   LYS A  60     -13.822   3.648 -20.759  1.00 85.32           C  
ANISOU  309  C   LYS A  60     7392  11548  13477   -363  -2410   1779       C  
ATOM    310  O   LYS A  60     -14.348   4.707 -20.411  1.00 85.11           O  
ANISOU  310  O   LYS A  60     7260  11462  13617   -239  -2357   1848       O  
ATOM    311  CB  LYS A  60     -15.383   1.803 -20.058  1.00 84.59           C  
ANISOU  311  CB  LYS A  60     7052  11475  13612   -523  -2335   1629       C  
ATOM    312  CG  LYS A  60     -15.544   0.422 -19.432  1.00 86.06           C  
ANISOU  312  CG  LYS A  60     7201  11658  13841   -656  -2232   1520       C  
ATOM    313  CD  LYS A  60     -14.601  -0.594 -20.067  1.00 86.97           C  
ANISOU  313  CD  LYS A  60     7502  11822  13722   -783  -2322   1448       C  
ATOM    314  CE  LYS A  60     -14.779  -1.985 -19.463  1.00 86.03           C  
ANISOU  314  CE  LYS A  60     7349  11682  13658   -917  -2220   1342       C  
ATOM    315  NZ  LYS A  60     -13.853  -2.984 -20.075  1.00 82.43           N1+
ANISOU  315  NZ  LYS A  60     7077  11259  12983  -1038  -2302   1260       N1+
ATOM    316  N   PRO A  61     -13.075   3.540 -21.871  1.00 87.48           N  
ANISOU  316  N   PRO A  61     7845  11891  13504   -408  -2569   1793       N  
ATOM    317  CA  PRO A  61     -12.393   2.325 -22.341  1.00 86.35           C  
ANISOU  317  CA  PRO A  61     7842  11814  13151   -550  -2628   1697       C  
ATOM    318  C   PRO A  61     -11.162   2.019 -21.495  1.00 78.34           C  
ANISOU  318  C   PRO A  61     6956  10755  12055   -579  -2471   1656       C  
ATOM    319  O   PRO A  61     -10.708   2.911 -20.785  1.00 73.27           O  
ANISOU  319  O   PRO A  61     6332  10043  11465   -477  -2340   1710       O  
ATOM    320  CB  PRO A  61     -11.978   2.693 -23.768  1.00 89.07           C  
ANISOU  320  CB  PRO A  61     8339  12240  13264   -548  -2822   1745       C  
ATOM    321  CG  PRO A  61     -11.827   4.174 -23.740  1.00 88.68           C  
ANISOU  321  CG  PRO A  61     8297  12137  13260   -402  -2804   1877       C  
ATOM    322  CD  PRO A  61     -12.865   4.681 -22.781  1.00 88.53           C  
ANISOU  322  CD  PRO A  61     8057  12037  13543   -315  -2693   1905       C  
ATOM    323  N   ASP A  62     -10.642   0.794 -21.563  1.00 80.22           N  
ANISOU  323  N   ASP A  62     7288  11025  12166   -712  -2472   1551       N  
ATOM    324  CA  ASP A  62      -9.540   0.389 -20.686  1.00 83.37           C  
ANISOU  324  CA  ASP A  62     7867  11356  12453   -731  -2256   1468       C  
ATOM    325  C   ASP A  62      -8.249  -0.018 -21.398  1.00 88.51           C  
ANISOU  325  C   ASP A  62     8776  12045  12810   -791  -2303   1412       C  
ATOM    326  O   ASP A  62      -7.426  -0.731 -20.821  1.00 90.70           O  
ANISOU  326  O   ASP A  62     9193  12277  12990   -841  -2157   1317       O  
ATOM    327  CB  ASP A  62      -9.982  -0.723 -19.726  1.00 80.96           C  
ANISOU  327  CB  ASP A  62     7475  11007  12278   -815  -2112   1374       C  
ATOM    328  CG  ASP A  62     -10.515  -1.947 -20.447  1.00 80.93           C  
ANISOU  328  CG  ASP A  62     7406  11069  12276   -959  -2271   1305       C  
ATOM    329  OD1 ASP A  62     -11.689  -1.921 -20.877  1.00 83.03           O  
ANISOU  329  OD1 ASP A  62     7493  11373  12682   -963  -2390   1329       O  
ATOM    330  OD2 ASP A  62      -9.766  -2.941 -20.569  1.00 78.78           O1-
ANISOU  330  OD2 ASP A  62     7289  10796  11849  -1058  -2251   1205       O1-
ATOM    331  N   LYS A  63      -8.071   0.431 -22.639  1.00 91.20           N  
ANISOU  331  N   LYS A  63     9175  12468  13008   -785  -2502   1474       N  
ATOM    332  CA  LYS A  63      -6.809   0.226 -23.348  1.00 90.31           C  
ANISOU  332  CA  LYS A  63     9307  12396  12612   -827  -2535   1431       C  
ATOM    333  C   LYS A  63      -5.971   1.490 -23.223  1.00 89.33           C  
ANISOU  333  C   LYS A  63     9304  12227  12411   -708  -2454   1520       C  
ATOM    334  O   LYS A  63      -4.901   1.607 -23.825  1.00 89.91           O  
ANISOU  334  O   LYS A  63     9573  12331  12259   -721  -2473   1513       O  
ATOM    335  CB  LYS A  63      -7.042  -0.099 -24.828  1.00 95.15           C  
ANISOU  335  CB  LYS A  63     9941  13135  13077   -900  -2782   1430       C  
ATOM    336  CG  LYS A  63      -7.394   1.109 -25.706  1.00 97.91           C  
ANISOU  336  CG  LYS A  63    10288  13523  13391   -798  -2896   1557       C  
ATOM    337  CD  LYS A  63      -7.170   0.813 -27.189  1.00 98.17           C  
ANISOU  337  CD  LYS A  63    10460  13666  13172   -852  -3048   1517       C  
ATOM    338  CE  LYS A  63      -7.523   2.010 -28.059  1.00 99.22           C  
ANISOU  338  CE  LYS A  63    10591  13837  13270   -755  -3157   1654       C  
ATOM    339  NZ  LYS A  63      -8.986   2.306 -28.050  1.00100.98           N1+
ANISOU  339  NZ  LYS A  63    10594  14059  13717   -708  -3238   1707       N1+
ATOM    340  N   CYS A  64      -6.470   2.424 -22.416  1.00 86.11           N  
ANISOU  340  N   CYS A  64     8774  11742  12203   -595  -2355   1597       N  
ATOM    341  CA  CYS A  64      -5.908   3.767 -22.311  1.00 80.85           C  
ANISOU  341  CA  CYS A  64     8179  11021  11521   -473  -2298   1695       C  
ATOM    342  C   CYS A  64      -4.627   3.840 -21.481  1.00 78.29           C  
ANISOU  342  C   CYS A  64     8042  10616  11088   -452  -2083   1626       C  
ATOM    343  O   CYS A  64      -4.486   3.134 -20.479  1.00 73.48           O  
ANISOU  343  O   CYS A  64     7441   9958  10520   -486  -1920   1525       O  
ATOM    344  CB  CYS A  64      -6.954   4.717 -21.729  1.00 79.64           C  
ANISOU  344  CB  CYS A  64     7814  10805  11640   -358  -2269   1787       C  
ATOM    345  SG  CYS A  64      -8.574   4.552 -22.499  1.00108.91           S  
ANISOU  345  SG  CYS A  64    11260  14597  15525   -380  -2507   1859       S  
ATOM    346  N   PRO A  65      -3.690   4.710 -21.900  1.00 79.86           N  
ANISOU  346  N   PRO A  65     8390  10802  11151   -397  -2084   1687       N  
ATOM    347  CA  PRO A  65      -2.416   4.927 -21.205  1.00 75.23           C  
ANISOU  347  CA  PRO A  65     7980  10142  10462   -371  -1898   1630       C  
ATOM    348  C   PRO A  65      -2.607   5.336 -19.747  1.00 71.10           C  
ANISOU  348  C   PRO A  65     7382   9511  10123   -292  -1692   1601       C  
ATOM    349  O   PRO A  65      -3.639   5.908 -19.383  1.00 69.05           O  
ANISOU  349  O   PRO A  65     6941   9218  10077   -221  -1692   1659       O  
ATOM    350  CB  PRO A  65      -1.764   6.068 -22.001  1.00 73.64           C  
ANISOU  350  CB  PRO A  65     7882   9942  10156   -309  -1968   1743       C  
ATOM    351  CG  PRO A  65      -2.865   6.669 -22.817  1.00 75.15           C  
ANISOU  351  CG  PRO A  65     7919  10181  10454   -269  -2160   1879       C  
ATOM    352  CD  PRO A  65      -3.801   5.548 -23.107  1.00 78.11           C  
ANISOU  352  CD  PRO A  65     8173  10639  10864   -361  -2274   1823       C  
ATOM    353  N   ARG A  66      -1.607   5.042 -18.924  1.00 68.37           N  
ANISOU  353  N   ARG A  66     7174   9114   9691   -303  -1519   1507       N  
ATOM    354  CA  ARG A  66      -1.690   5.311 -17.496  1.00 64.85           C  
ANISOU  354  CA  ARG A  66     6679   8579   9380   -240  -1316   1461       C  
ATOM    355  C   ARG A  66      -1.833   6.805 -17.198  1.00 60.37           C  
ANISOU  355  C   ARG A  66     6057   7935   8945   -109  -1271   1542       C  
ATOM    356  O   ARG A  66      -2.491   7.186 -16.229  1.00 55.28           O  
ANISOU  356  O   ARG A  66     5286   7233   8484    -43  -1154   1531       O  
ATOM    357  CB  ARG A  66      -0.490   4.703 -16.762  1.00 66.92           C  
ANISOU  357  CB  ARG A  66     7116   8812   9498   -280  -1163   1350       C  
ATOM    358  CG  ARG A  66      -0.480   3.175 -16.768  1.00 74.08           C  
ANISOU  358  CG  ARG A  66     8051   9767  10330   -400  -1173   1261       C  
ATOM    359  CD  ARG A  66       0.759   2.594 -16.094  1.00 81.34           C  
ANISOU  359  CD  ARG A  66     9143  10653  11109   -432  -1034   1164       C  
ATOM    360  NE  ARG A  66       0.771   1.130 -16.143  1.00 89.50           N  
ANISOU  360  NE  ARG A  66    10202  11719  12086   -544  -1049   1085       N  
ATOM    361  CZ  ARG A  66       1.779   0.368 -15.723  1.00 92.96           C  
ANISOU  361  CZ  ARG A  66    10782  12135  12403   -589   -961   1001       C  
ATOM    362  NH1 ARG A  66       2.872   0.926 -15.221  1.00 93.10           N1+
ANISOU  362  NH1 ARG A  66    10928  12109  12336   -534   -855    982       N1+
ATOM    363  NH2 ARG A  66       1.701  -0.954 -15.808  1.00 93.24           N  
ANISOU  363  NH2 ARG A  66    10826  12187  12413   -689   -982    936       N  
ATOM    364  N   ARG A  67      -1.245   7.648 -18.044  1.00 62.60           N  
ANISOU  364  N   ARG A  67     6430   8215   9142    -72  -1359   1624       N  
ATOM    365  CA  ARG A  67      -1.286   9.091 -17.819  1.00 67.75           C  
ANISOU  365  CA  ARG A  67     7042   8777   9923     51  -1319   1704       C  
ATOM    366  C   ARG A  67      -2.716   9.620 -17.924  1.00 70.21           C  
ANISOU  366  C   ARG A  67     7126   9079  10471    119  -1401   1794       C  
ATOM    367  O   ARG A  67      -3.084  10.599 -17.267  1.00 71.14           O  
ANISOU  367  O   ARG A  67     7151   9104  10774    226  -1313   1820       O  
ATOM    368  CB  ARG A  67      -0.357   9.832 -18.790  1.00 75.40           C  
ANISOU  368  CB  ARG A  67     8156   9745  10748     64  -1405   1789       C  
ATOM    369  CG  ARG A  67       1.124   9.428 -18.718  1.00 85.56           C  
ANISOU  369  CG  ARG A  67     9660  11035  11814      5  -1320   1704       C  
ATOM    370  CD  ARG A  67       1.756   9.649 -17.328  1.00 93.36           C  
ANISOU  370  CD  ARG A  67    10698  11928  12845     49  -1103   1599       C  
ATOM    371  NE  ARG A  67       1.745  11.047 -16.889  1.00 97.73           N  
ANISOU  371  NE  ARG A  67    11212  12372  13549    164  -1034   1650       N  
ATOM    372  CZ  ARG A  67       2.669  11.954 -17.210  1.00 94.97           C  
ANISOU  372  CZ  ARG A  67    10974  11966  13144    199  -1025   1696       C  
ATOM    373  NH1 ARG A  67       3.691  11.624 -17.992  1.00 91.43           N1+
ANISOU  373  NH1 ARG A  67    10684  11569  12484    129  -1076   1701       N1+
ATOM    374  NH2 ARG A  67       2.564  13.197 -16.753  1.00 92.99           N  
ANISOU  374  NH2 ARG A  67    10672  11602  13058    303   -959   1734       N  
ATOM    375  N   VAL A  68      -3.521   8.959 -18.750  1.00 70.11           N  
ANISOU  375  N   VAL A  68     7020   9160  10458     56  -1572   1835       N  
ATOM    376  CA  VAL A  68      -4.928   9.309 -18.906  1.00 69.38           C  
ANISOU  376  CA  VAL A  68     6696   9073  10594    109  -1669   1916       C  
ATOM    377  C   VAL A  68      -5.715   8.991 -17.635  1.00 65.77           C  
ANISOU  377  C   VAL A  68     6085   8573  10333    129  -1506   1831       C  
ATOM    378  O   VAL A  68      -6.463   9.828 -17.123  1.00 58.66           O  
ANISOU  378  O   VAL A  68     5027   7603   9658    233  -1452   1870       O  
ATOM    379  CB  VAL A  68      -5.553   8.558 -20.100  1.00 68.51           C  
ANISOU  379  CB  VAL A  68     6527   9087  10418     21  -1900   1963       C  
ATOM    380  CG1 VAL A  68      -7.071   8.608 -20.036  1.00 66.19           C  
ANISOU  380  CG1 VAL A  68     5970   8804  10376     55  -1978   2011       C  
ATOM    381  CG2 VAL A  68      -5.043   9.137 -21.407  1.00 66.01           C  
ANISOU  381  CG2 VAL A  68     6321   8817   9943     26  -2077   2082       C  
ATOM    382  N   ASN A  69      -5.525   7.775 -17.131  1.00 65.21           N  
ANISOU  382  N   ASN A  69     6061   8540  10176     30  -1422   1717       N  
ATOM    383  CA  ASN A  69      -6.231   7.304 -15.947  1.00 62.59           C  
ANISOU  383  CA  ASN A  69     5598   8183  10001     28  -1261   1639       C  
ATOM    384  C   ASN A  69      -5.990   8.205 -14.743  1.00 63.46           C  
ANISOU  384  C   ASN A  69     5710   8192  10210    135  -1049   1602       C  
ATOM    385  O   ASN A  69      -6.921   8.525 -13.996  1.00 63.51           O  
ANISOU  385  O   ASN A  69     5539   8162  10431    197   -954   1596       O  
ATOM    386  CB  ASN A  69      -5.819   5.867 -15.639  1.00 58.69           C  
ANISOU  386  CB  ASN A  69     5197   7735   9365   -100  -1203   1532       C  
ATOM    387  CG  ASN A  69      -5.961   4.955 -16.842  1.00 61.39           C  
ANISOU  387  CG  ASN A  69     5554   8173   9597   -211  -1409   1545       C  
ATOM    388  ND2 ASN A  69      -5.203   3.866 -16.854  1.00 63.60           N  
ANISOU  388  ND2 ASN A  69     5981   8482   9701   -316  -1383   1457       N  
ATOM    389  OD1 ASN A  69      -6.743   5.228 -17.752  1.00 60.90           O  
ANISOU  389  OD1 ASN A  69     5372   8159   9611   -202  -1593   1629       O  
ATOM    390  N   ARG A  70      -4.739   8.628 -14.575  1.00 60.18           N  
ANISOU  390  N   ARG A  70     5492   7733   9642    156   -976   1573       N  
ATOM    391  CA  ARG A  70      -4.378   9.553 -13.510  1.00 59.17           C  
ANISOU  391  CA  ARG A  70     5387   7508   9586    255   -789   1529       C  
ATOM    392  C   ARG A  70      -5.143  10.865 -13.640  1.00 63.84           C  
ANISOU  392  C   ARG A  70     5823   8029  10405    382   -822   1616       C  
ATOM    393  O   ARG A  70      -5.561  11.443 -12.640  1.00 65.89           O  
ANISOU  393  O   ARG A  70     5986   8220  10829    465   -668   1571       O  
ATOM    394  CB  ARG A  70      -2.871   9.809 -13.508  1.00 54.39           C  
ANISOU  394  CB  ARG A  70     5015   6871   8778    249   -741   1492       C  
ATOM    395  CG  ARG A  70      -2.048   8.566 -13.205  1.00 60.65           C  
ANISOU  395  CG  ARG A  70     5960   7717   9367    139   -682   1395       C  
ATOM    396  CD  ARG A  70      -0.590   8.893 -12.903  1.00 63.74           C  
ANISOU  396  CD  ARG A  70     6558   8066   9595    148   -595   1340       C  
ATOM    397  NE  ARG A  70       0.015   7.871 -12.050  1.00 68.10           N  
ANISOU  397  NE  ARG A  70     7211   8640  10024     80   -470   1230       N  
ATOM    398  CZ  ARG A  70       0.747   6.855 -12.498  1.00 67.15           C  
ANISOU  398  CZ  ARG A  70     7219   8573   9721    -18   -522   1198       C  
ATOM    399  NH1 ARG A  70       0.982   6.729 -13.800  1.00 65.41           N1+
ANISOU  399  NH1 ARG A  70     7050   8399   9405    -62   -691   1257       N1+
ATOM    400  NH2 ARG A  70       1.254   5.972 -11.640  1.00 63.65           N  
ANISOU  400  NH2 ARG A  70     6857   8139   9190    -68   -405   1108       N  
ATOM    401  N   GLU A  71      -5.326  11.324 -14.877  1.00 66.61           N  
ANISOU  401  N   GLU A  71     6150   8396  10761    398  -1025   1742       N  
ATOM    402  CA  GLU A  71      -6.115  12.521 -15.144  1.00 67.31           C  
ANISOU  402  CA  GLU A  71     6080   8417  11076    518  -1090   1849       C  
ATOM    403  C   GLU A  71      -7.551  12.302 -14.704  1.00 64.42           C  
ANISOU  403  C   GLU A  71     5463   8064  10949    544  -1070   1843       C  
ATOM    404  O   GLU A  71      -8.135  13.135 -14.009  1.00 60.69           O  
ANISOU  404  O   GLU A  71     4854   7507  10699    653   -963   1836       O  
ATOM    405  CB  GLU A  71      -6.097  12.854 -16.634  1.00 73.40           C  
ANISOU  405  CB  GLU A  71     6875   9229  11783    512  -1334   1999       C  
ATOM    406  CG  GLU A  71      -5.198  14.013 -17.020  1.00 76.40           C  
ANISOU  406  CG  GLU A  71     7388   9526  12117    582  -1348   2075       C  
ATOM    407  CD  GLU A  71      -5.304  14.354 -18.498  1.00 76.16           C  
ANISOU  407  CD  GLU A  71     7365   9545  12027    578  -1592   2244       C  
ATOM    408  OE1 GLU A  71      -6.382  14.817 -18.935  1.00 71.82           O  
ANISOU  408  OE1 GLU A  71     6631   8990  11666    642  -1720   2355       O  
ATOM    409  OE2 GLU A  71      -4.308  14.150 -19.225  1.00 77.46           O1-
ANISOU  409  OE2 GLU A  71     7720   9758  11954    510  -1656   2267       O1-
ATOM    410  N   VAL A  72      -8.110  11.171 -15.125  1.00 64.49           N  
ANISOU  410  N   VAL A  72     5407   8178  10918    441  -1171   1840       N  
ATOM    411  CA  VAL A  72      -9.475  10.800 -14.775  1.00 65.77           C  
ANISOU  411  CA  VAL A  72     5323   8365  11300    444  -1162   1833       C  
ATOM    412  C   VAL A  72      -9.665  10.715 -13.261  1.00 61.97           C  
ANISOU  412  C   VAL A  72     4788   7835  10923    472   -896   1713       C  
ATOM    413  O   VAL A  72     -10.604  11.297 -12.714  1.00 62.83           O  
ANISOU  413  O   VAL A  72     4699   7895  11278    562   -818   1717       O  
ATOM    414  CB  VAL A  72      -9.877   9.457 -15.415  1.00 62.98           C  
ANISOU  414  CB  VAL A  72     4938   8130  10861    305  -1300   1826       C  
ATOM    415  CG1 VAL A  72     -11.210   8.988 -14.866  1.00 61.81           C  
ANISOU  415  CG1 VAL A  72     4541   8002  10944    295  -1251   1799       C  
ATOM    416  CG2 VAL A  72      -9.939   9.590 -16.927  1.00 62.24           C  
ANISOU  416  CG2 VAL A  72     4857   8100  10691    284  -1577   1946       C  
ATOM    417  N   VAL A  73      -8.763  10.002 -12.594  1.00 54.75           N  
ANISOU  417  N   VAL A  73     4050   6935   9816    399   -756   1608       N  
ATOM    418  CA  VAL A  73      -8.835   9.834 -11.143  1.00 53.18           C  
ANISOU  418  CA  VAL A  73     3830   6708   9670    414   -502   1495       C  
ATOM    419  C   VAL A  73      -8.663  11.173 -10.419  1.00 54.68           C  
ANISOU  419  C   VAL A  73     4011   6791   9974    553   -361   1470       C  
ATOM    420  O   VAL A  73      -9.353  11.454  -9.438  1.00 59.79           O  
ANISOU  420  O   VAL A  73     4519   7407  10793    614   -194   1413       O  
ATOM    421  CB  VAL A  73      -7.824   8.768 -10.652  1.00 44.37           C  
ANISOU  421  CB  VAL A  73     2918   5632   8307    306   -406   1403       C  
ATOM    422  CG1 VAL A  73      -7.579   8.874  -9.155  1.00 52.47           C  
ANISOU  422  CG1 VAL A  73     3978   6621   9337    341   -144   1296       C  
ATOM    423  CG2 VAL A  73      -8.312   7.378 -11.019  1.00 47.89           C  
ANISOU  423  CG2 VAL A  73     3312   6165   8717    174   -488   1403       C  
ATOM    424  N   GLU A  74      -7.765  12.009 -10.928  1.00 53.93           N  
ANISOU  424  N   GLU A  74     4059   6640   9793    603   -426   1509       N  
ATOM    425  CA  GLU A  74      -7.573  13.344 -10.373  1.00 59.66           C  
ANISOU  425  CA  GLU A  74     4778   7249  10640    733   -315   1489       C  
ATOM    426  C   GLU A  74      -8.842  14.177 -10.478  1.00 59.57           C  
ANISOU  426  C   GLU A  74     4515   7184  10936    844   -349   1555       C  
ATOM    427  O   GLU A  74      -9.307  14.749  -9.494  1.00 59.13           O  
ANISOU  427  O   GLU A  74     4351   7065  11053    931   -174   1482       O  
ATOM    428  CB  GLU A  74      -6.433  14.062 -11.093  1.00 64.92           C  
ANISOU  428  CB  GLU A  74     5629   7863  11174    755   -409   1543       C  
ATOM    429  CG  GLU A  74      -6.089  15.422 -10.503  1.00 71.44           C  
ANISOU  429  CG  GLU A  74     6470   8555  12118    879   -290   1510       C  
ATOM    430  CD  GLU A  74      -5.404  15.321  -9.153  1.00 75.75           C  
ANISOU  430  CD  GLU A  74     7126   9080  12574    876    -57   1347       C  
ATOM    431  OE1 GLU A  74      -5.236  16.367  -8.488  1.00 78.04           O  
ANISOU  431  OE1 GLU A  74     7410   9265  12977    975     66   1288       O  
ATOM    432  OE2 GLU A  74      -5.023  14.197  -8.761  1.00 76.63           O1-
ANISOU  432  OE2 GLU A  74     7332   9280  12504    773      0   1278       O1-
ATOM    433  N   TYR A  75      -9.381  14.240 -11.691  1.00 63.50           N  
ANISOU  433  N   TYR A  75     4922   7710  11495    842   -577   1692       N  
ATOM    434  CA  TYR A  75     -10.629  14.935 -11.992  1.00 68.98           C  
ANISOU  434  CA  TYR A  75     5365   8364  12482    941   -658   1780       C  
ATOM    435  C   TYR A  75     -11.736  14.432 -11.066  1.00 70.58           C  
ANISOU  435  C   TYR A  75     5366   8595  12856    938   -511   1696       C  
ATOM    436  O   TYR A  75     -12.566  15.201 -10.586  1.00 71.89           O  
ANISOU  436  O   TYR A  75     5421   8690  13205   1023   -418   1660       O  
ATOM    437  CB  TYR A  75     -10.976  14.677 -13.467  1.00 73.48           C  
ANISOU  437  CB  TYR A  75     5905   9005  13008    892   -942   1925       C  
ATOM    438  CG  TYR A  75     -12.223  15.342 -14.033  1.00 80.53           C  
ANISOU  438  CG  TYR A  75     6658   9869  14071    948  -1051   1993       C  
ATOM    439  CD1 TYR A  75     -12.148  16.553 -14.719  1.00 81.02           C  
ANISOU  439  CD1 TYR A  75     6766   9846  14173   1032  -1149   2091       C  
ATOM    440  CD2 TYR A  75     -13.466  14.725 -13.937  1.00 84.82           C  
ANISOU  440  CD2 TYR A  75     7025  10473  14731    910  -1063   1967       C  
ATOM    441  CE1 TYR A  75     -13.282  17.142 -15.262  1.00 81.52           C  
ANISOU  441  CE1 TYR A  75     6696   9886  14391   1083  -1255   2160       C  
ATOM    442  CE2 TYR A  75     -14.602  15.308 -14.473  1.00 86.07           C  
ANISOU  442  CE2 TYR A  75     7049  10609  15046    963  -1170   2031       C  
ATOM    443  CZ  TYR A  75     -14.507  16.513 -15.133  1.00 84.26           C  
ANISOU  443  CZ  TYR A  75     6862  10296  14855   1051  -1268   2128       C  
ATOM    444  OH  TYR A  75     -15.649  17.078 -15.660  1.00 83.05           O  
ANISOU  444  OH  TYR A  75     6569  10122  14863   1105  -1376   2196       O  
ATOM    445  N   MET A  76     -11.718  13.133 -10.797  1.00 69.24           N  
ANISOU  445  N   MET A  76     5228   8527  12554    811   -470   1636       N  
ATOM    446  CA  MET A  76     -12.709  12.504  -9.935  1.00 66.07           C  
ANISOU  446  CA  MET A  76     4644   8166  12296    786   -326   1566       C  
ATOM    447  C   MET A  76     -12.553  12.903  -8.477  1.00 66.18           C  
ANISOU  447  C   MET A  76     4671   8122  12353    849    -38   1436       C  
ATOM    448  O   MET A  76     -13.531  13.231  -7.805  1.00 68.60           O  
ANISOU  448  O   MET A  76     4835   8402  12829    901     89   1382       O  
ATOM    449  CB  MET A  76     -12.582  10.994 -10.041  1.00 61.60           C  
ANISOU  449  CB  MET A  76     4145   7710  11551    624   -356   1537       C  
ATOM    450  CG  MET A  76     -13.677  10.227  -9.346  1.00 60.35           C  
ANISOU  450  CG  MET A  76     3786   7600  11546    577   -240   1492       C  
ATOM    451  SD  MET A  76     -13.409   8.470  -9.613  1.00115.12           S  
ANISOU  451  SD  MET A  76    10824  14644  18270    382   -301   1469       S  
ATOM    452  CE  MET A  76     -12.519   8.521 -11.171  1.00 54.06           C  
ANISOU  452  CE  MET A  76     3275   6936  10331    345   -589   1556       C  
ATOM    453  N   VAL A  77     -11.318  12.851  -7.990  1.00 61.71           N  
ANISOU  453  N   VAL A  77     4347   7543  11557    822     65   1359       N  
ATOM    454  CA  VAL A  77     -11.024  13.183  -6.605  1.00 60.64           C  
ANISOU  454  CA  VAL A  77     4258   7367  11414    870    330   1225       C  
ATOM    455  C   VAL A  77     -11.379  14.626  -6.282  1.00 68.34           C  
ANISOU  455  C   VAL A  77     5121   8226  12620   1030    405   1208       C  
ATOM    456  O   VAL A  77     -12.027  14.900  -5.273  1.00 75.01           O  
ANISOU  456  O   VAL A  77     5862   9051  13587   1081    598   1113       O  
ATOM    457  CB  VAL A  77      -9.545  12.913  -6.281  1.00 58.47           C  
ANISOU  457  CB  VAL A  77     4271   7100  10845    813    388   1157       C  
ATOM    458  CG1 VAL A  77      -9.091  13.721  -5.082  1.00 55.04           C  
ANISOU  458  CG1 VAL A  77     3900   6598  10416    898    612   1032       C  
ATOM    459  CG2 VAL A  77      -9.344  11.434  -6.035  1.00 59.15           C  
ANISOU  459  CG2 VAL A  77     4437   7292  10744    670    418   1128       C  
ATOM    460  N   GLN A  78     -10.976  15.543  -7.156  1.00 72.71           N  
ANISOU  460  N   GLN A  78     5724   8699  13204   1097    250   1293       N  
ATOM    461  CA  GLN A  78     -11.228  16.966  -6.943  1.00 80.51           C  
ANISOU  461  CA  GLN A  78     6671   9557  14363   1230    300   1270       C  
ATOM    462  C   GLN A  78     -12.702  17.346  -7.056  1.00 81.33           C  
ANISOU  462  C   GLN A  78     6585   9642  14674   1272    271   1291       C  
ATOM    463  O   GLN A  78     -13.163  18.259  -6.374  1.00 83.51           O  
ANISOU  463  O   GLN A  78     6809   9835  15087   1360    402   1211       O  
ATOM    464  CB  GLN A  78     -10.389  17.810  -7.910  1.00 88.91           C  
ANISOU  464  CB  GLN A  78     7855  10537  15390   1275    135   1372       C  
ATOM    465  CG  GLN A  78      -9.043  18.287  -7.352  1.00 94.02           C  
ANISOU  465  CG  GLN A  78     8699  11117  15909   1300    252   1286       C  
ATOM    466  CD  GLN A  78      -8.021  17.169  -7.173  1.00 97.78           C  
ANISOU  466  CD  GLN A  78     9397  11697  16057   1161    277   1229       C  
ATOM    467  NE2 GLN A  78      -6.769  17.552  -6.944  1.00 96.89           N  
ANISOU  467  NE2 GLN A  78     9494  11537  15784   1158    327   1170       N  
ATOM    468  OE1 GLN A  78      -8.348  15.984  -7.242  1.00 99.75           O  
ANISOU  468  OE1 GLN A  78     9624  12063  16212   1059    251   1237       O  
ATOM    469  N   HIS A  79     -13.442  16.649  -7.913  1.00 81.49           N  
ANISOU  469  N   HIS A  79     6503   9742  14718   1207     97   1393       N  
ATOM    470  CA  HIS A  79     -14.847  16.984  -8.142  1.00 87.76           C  
ANISOU  470  CA  HIS A  79     7112  10521  15712   1246     45   1424       C  
ATOM    471  C   HIS A  79     -15.797  16.369  -7.107  1.00 89.67           C  
ANISOU  471  C   HIS A  79     7218  10819  16033   1217    232   1318       C  
ATOM    472  O   HIS A  79     -16.660  17.055  -6.563  1.00 89.98           O  
ANISOU  472  O   HIS A  79     7142  10802  16243   1294    336   1262       O  
ATOM    473  CB  HIS A  79     -15.283  16.575  -9.555  1.00 91.38           C  
ANISOU  473  CB  HIS A  79     7519  11040  16160   1191   -234   1574       C  
ATOM    474  CG  HIS A  79     -14.659  17.387 -10.650  1.00 94.03           C  
ANISOU  474  CG  HIS A  79     7962  11317  16448   1233   -426   1696       C  
ATOM    475  CD2 HIS A  79     -15.074  17.647 -11.913  1.00 94.05           C  
ANISOU  475  CD2 HIS A  79     7934  11329  16471   1235   -665   1834       C  
ATOM    476  ND1 HIS A  79     -13.452  18.039 -10.505  1.00 95.33           N  
ANISOU  476  ND1 HIS A  79     8295  11405  16523   1276   -376   1683       N  
ATOM    477  CE1 HIS A  79     -13.153  18.665 -11.629  1.00 92.46           C  
ANISOU  477  CE1 HIS A  79     7999  11003  16129   1299   -571   1814       C  
ATOM    478  NE2 HIS A  79     -14.122  18.444 -12.500  1.00 91.99           N  
ANISOU  478  NE2 HIS A  79     7825  10999  16127   1275   -748   1909       N  
ATOM    479  N   PHE A  80     -15.632  15.075  -6.838  1.00 89.07           N  
ANISOU  479  N   PHE A  80     7159  10853  15832   1102    277   1293       N  
ATOM    480  CA  PHE A  80     -16.567  14.341  -5.985  1.00 82.93           C  
ANISOU  480  CA  PHE A  80     6256  10140  15114   1052    434   1216       C  
ATOM    481  C   PHE A  80     -16.125  14.261  -4.530  1.00 83.04           C  
ANISOU  481  C   PHE A  80     6345  10159  15047   1057    719   1072       C  
ATOM    482  O   PHE A  80     -16.306  13.234  -3.878  1.00 80.43           O  
ANISOU  482  O   PHE A  80     6000   9914  14646    968    842   1025       O  
ATOM    483  CB  PHE A  80     -16.793  12.931  -6.531  1.00 75.72           C  
ANISOU  483  CB  PHE A  80     5306   9340  14123    912    317   1273       C  
ATOM    484  CG  PHE A  80     -17.378  12.906  -7.909  1.00 76.11           C  
ANISOU  484  CG  PHE A  80     5274   9407  14239    895     40   1398       C  
ATOM    485  CD1 PHE A  80     -18.751  12.895  -8.091  1.00 80.49           C  
ANISOU  485  CD1 PHE A  80     5638   9973  14971    903     -6   1416       C  
ATOM    486  CD2 PHE A  80     -16.556  12.901  -9.025  1.00 75.53           C  
ANISOU  486  CD2 PHE A  80     5318   9342  14039    871   -176   1495       C  
ATOM    487  CE1 PHE A  80     -19.293  12.876  -9.364  1.00 84.35           C  
ANISOU  487  CE1 PHE A  80     6057  10485  15508    887   -266   1526       C  
ATOM    488  CE2 PHE A  80     -17.088  12.883 -10.301  1.00 77.95           C  
ANISOU  488  CE2 PHE A  80     5565   9676  14377    852   -434   1606       C  
ATOM    489  CZ  PHE A  80     -18.459  12.869 -10.472  1.00 83.48           C  
ANISOU  489  CZ  PHE A  80     6077  10390  15252    860   -480   1620       C  
ATOM    490  N   LYS A  81     -15.553  15.349  -4.026  1.00 88.07           N  
ANISOU  490  N   LYS A  81     7071  10705  15688   1158    822   1003       N  
ATOM    491  CA  LYS A  81     -15.124  15.417  -2.631  1.00 92.27           C  
ANISOU  491  CA  LYS A  81     7687  11241  16129   1172   1088    853       C  
ATOM    492  C   LYS A  81     -16.252  15.150  -1.615  1.00 94.77           C  
ANISOU  492  C   LYS A  81     7873  11606  16528   1163   1279    765       C  
ATOM    493  O   LYS A  81     -16.147  14.216  -0.816  1.00 93.33           O  
ANISOU  493  O   LYS A  81     7730  11514  16218   1080   1429    709       O  
ATOM    494  CB  LYS A  81     -14.434  16.756  -2.339  1.00 96.31           C  
ANISOU  494  CB  LYS A  81     8303  11635  16655   1285   1145    786       C  
ATOM    495  CG  LYS A  81     -14.350  17.673  -3.547  1.00101.98           C  
ANISOU  495  CG  LYS A  81     9012  12253  17481   1353    922    902       C  
ATOM    496  CD  LYS A  81     -14.176  19.134  -3.149  1.00106.70           C  
ANISOU  496  CD  LYS A  81     9648  12716  18176   1474    999    826       C  
ATOM    497  CE  LYS A  81     -15.457  19.713  -2.566  1.00110.57           C  
ANISOU  497  CE  LYS A  81     9973  13173  18865   1540   1106    759       C  
ATOM    498  NZ  LYS A  81     -15.328  21.172  -2.290  1.00112.42           N1+
ANISOU  498  NZ  LYS A  81    10236  13266  19214   1655   1158    693       N1+
ATOM    499  N   PRO A  82     -17.339  15.949  -1.646  1.00 96.57           N  
ANISOU  499  N   PRO A  82     7948  11778  16968   1245   1276    759       N  
ATOM    500  CA  PRO A  82     -18.305  15.767  -0.556  1.00 98.36           C  
ANISOU  500  CA  PRO A  82     8064  12050  17256   1243   1484    660       C  
ATOM    501  C   PRO A  82     -19.128  14.499  -0.727  1.00 98.47           C  
ANISOU  501  C   PRO A  82     7958  12169  17286   1131   1454    719       C  
ATOM    502  O   PRO A  82     -19.647  13.958   0.248  1.00 96.53           O  
ANISOU  502  O   PRO A  82     7667  11992  17016   1088   1643    646       O  
ATOM    503  CB  PRO A  82     -19.207  16.993  -0.691  1.00100.55           C  
ANISOU  503  CB  PRO A  82     8205  12229  17771   1363   1462    650       C  
ATOM    504  CG  PRO A  82     -19.208  17.279  -2.151  1.00100.30           C  
ANISOU  504  CG  PRO A  82     8139  12143  17827   1382   1184    799       C  
ATOM    505  CD  PRO A  82     -17.825  16.924  -2.645  1.00 97.21           C  
ANISOU  505  CD  PRO A  82     7938  11762  17234   1331   1087    848       C  
ATOM    506  N   GLN A  83     -19.238  14.030  -1.963  1.00100.93           N  
ANISOU  506  N   GLN A  83     8224  12495  17630   1080   1215    848       N  
ATOM    507  CA  GLN A  83     -20.053  12.864  -2.256  1.00106.21           C  
ANISOU  507  CA  GLN A  83     8772  13253  18330    971   1157    904       C  
ATOM    508  C   GLN A  83     -19.390  11.559  -1.803  1.00106.06           C  
ANISOU  508  C   GLN A  83     8866  13327  18104    839   1243    888       C  
ATOM    509  O   GLN A  83     -19.968  10.811  -1.010  1.00109.55           O  
ANISOU  509  O   GLN A  83     9252  13836  18536    772   1398    844       O  
ATOM    510  CB  GLN A  83     -20.409  12.819  -3.748  1.00110.12           C  
ANISOU  510  CB  GLN A  83     9187  13738  18917    958    860   1038       C  
ATOM    511  CG  GLN A  83     -21.250  11.616  -4.163  1.00114.66           C  
ANISOU  511  CG  GLN A  83     9637  14401  19528    839    772   1090       C  
ATOM    512  CD  GLN A  83     -22.534  11.468  -3.353  1.00118.54           C  
ANISOU  512  CD  GLN A  83     9952  14917  20169    840    936   1029       C  
ATOM    513  NE2 GLN A  83     -22.827  10.241  -2.928  1.00116.32           N  
ANISOU  513  NE2 GLN A  83     9645  14722  19831    717   1020   1013       N  
ATOM    514  OE1 GLN A  83     -23.250  12.443  -3.113  1.00121.45           O  
ANISOU  514  OE1 GLN A  83    10211  15228  20707    947    988    998       O  
ATOM    515  N   ILE A  84     -18.181  11.287  -2.293  1.00 99.76           N  
ANISOU  515  N   ILE A  84     8229  12531  17144    801   1145    929       N  
ATOM    516  CA  ILE A  84     -17.559   9.979  -2.079  1.00 92.64           C  
ANISOU  516  CA  ILE A  84     7429  11712  16059    667   1183    936       C  
ATOM    517  C   ILE A  84     -16.051   9.992  -1.838  1.00 85.20           C  
ANISOU  517  C   ILE A  84     6699  10762  14910    663   1230    910       C  
ATOM    518  O   ILE A  84     -15.388   8.997  -2.120  1.00 79.44           O  
ANISOU  518  O   ILE A  84     6059  10085  14042    557   1174    952       O  
ATOM    519  CB  ILE A  84     -17.795   9.040  -3.287  1.00 92.95           C  
ANISOU  519  CB  ILE A  84     7411  11794  16110    561    943   1046       C  
ATOM    520  CG1 ILE A  84     -17.225   9.660  -4.567  1.00 92.41           C  
ANISOU  520  CG1 ILE A  84     7391  11680  16042    610    692   1132       C  
ATOM    521  CG2 ILE A  84     -19.276   8.706  -3.452  1.00 95.48           C  
ANISOU  521  CG2 ILE A  84     7526  12143  16612    532    908   1066       C  
ATOM    522  CD1 ILE A  84     -17.330   8.765  -5.788  1.00 92.75           C  
ANISOU  522  CD1 ILE A  84     7408  11776  16057    503    443   1228       C  
ATOM    523  N   PHE A  85     -15.502  11.091  -1.326  1.00 84.47           N  
ANISOU  523  N   PHE A  85     6691  10604  14800    774   1330    837       N  
ATOM    524  CA  PHE A  85     -14.048  11.168  -1.126  1.00 79.69           C  
ANISOU  524  CA  PHE A  85     6286   9987  14005    777   1368    807       C  
ATOM    525  C   PHE A  85     -13.602  11.881   0.146  1.00 76.42           C  
ANISOU  525  C   PHE A  85     5976   9548  13512    850   1602    669       C  
ATOM    526  O   PHE A  85     -12.454  11.728   0.570  1.00 68.55           O  
ANISOU  526  O   PHE A  85     5152   8564  12331    832   1677    624       O  
ATOM    527  CB  PHE A  85     -13.351  11.809  -2.336  1.00 75.78           C  
ANISOU  527  CB  PHE A  85     5841   9423  13527    828   1142    892       C  
ATOM    528  CG  PHE A  85     -12.983  10.830  -3.414  1.00 68.07           C  
ANISOU  528  CG  PHE A  85     4903   8502  12458    717    931   1001       C  
ATOM    529  CD1 PHE A  85     -12.008   9.873  -3.191  1.00 59.21           C  
ANISOU  529  CD1 PHE A  85     4004   7435  11059    605    952    975       C  
ATOM    530  CD2 PHE A  85     -13.610  10.869  -4.651  1.00 69.22           C  
ANISOU  530  CD2 PHE A  85     4923   8643  12734    714    693   1114       C  
ATOM    531  CE1 PHE A  85     -11.671   8.964  -4.177  1.00 58.99           C  
ANISOU  531  CE1 PHE A  85     4059   7451  10904    494    752   1050       C  
ATOM    532  CE2 PHE A  85     -13.275   9.966  -5.644  1.00 66.12           C  
ANISOU  532  CE2 PHE A  85     4607   8306  12208    602    489   1191       C  
ATOM    533  CZ  PHE A  85     -12.304   9.010  -5.406  1.00 62.61           C  
ANISOU  533  CZ  PHE A  85     4384   7910  11494    490    523   1152       C  
ATOM    534  N   GLY A  86     -14.504  12.650   0.748  1.00 78.52           N  
ANISOU  534  N   GLY A  86     6140   9781  13912    929   1713    596       N  
ATOM    535  CA  GLY A  86     -14.143  13.501   1.866  1.00 77.76           C  
ANISOU  535  CA  GLY A  86     6137   9654  13756   1008   1909    454       C  
ATOM    536  C   GLY A  86     -12.974  14.382   1.472  1.00 79.77           C  
ANISOU  536  C   GLY A  86     6531   9817  13961   1079   1831    441       C  
ATOM    537  O   GLY A  86     -12.877  14.823   0.325  1.00 82.79           O  
ANISOU  537  O   GLY A  86     6880  10130  14447   1116   1629    539       O  
ATOM    538  N   ASP A  87     -12.066  14.621   2.409  1.00 79.96           N  
ANISOU  538  N   ASP A  87     6720   9846  13816   1094   1985    323       N  
ATOM    539  CA  ASP A  87     -10.878  15.409   2.112  1.00 81.46           C  
ANISOU  539  CA  ASP A  87     7055   9950  13947   1152   1924    299       C  
ATOM    540  C   ASP A  87      -9.614  14.550   2.142  1.00 72.55           C  
ANISOU  540  C   ASP A  87     6098   8880  12586   1071   1927    312       C  
ATOM    541  O   ASP A  87      -8.503  15.070   2.266  1.00 70.09           O  
ANISOU  541  O   ASP A  87     5957   8522  12154   1100   1928    253       O  
ATOM    542  CB  ASP A  87     -10.753  16.573   3.094  1.00 91.36           C  
ANISOU  542  CB  ASP A  87     8369  11141  15202   1244   2076    139       C  
ATOM    543  CG  ASP A  87     -10.693  16.112   4.533  1.00 99.57           C  
ANISOU  543  CG  ASP A  87     9489  12284  16058   1202   2305      8       C  
ATOM    544  OD1 ASP A  87     -11.301  15.065   4.847  1.00102.94           O  
ANISOU  544  OD1 ASP A  87     9854  12817  16440   1121   2369     44       O  
ATOM    545  OD2 ASP A  87     -10.038  16.793   5.348  1.00102.21           O1-
ANISOU  545  OD2 ASP A  87     9953  12594  16288   1246   2413   -128       O1-
ATOM    546  N   ARG A  88      -9.790  13.237   2.028  1.00 64.28           N  
ANISOU  546  N   ARG A  88     5042   7936  11446    955   1907    385       N  
ATOM    547  CA  ARG A  88      -8.660  12.318   2.008  1.00 64.07           C  
ANISOU  547  CA  ARG A  88     5252   7970  11123    843   1850    401       C  
ATOM    548  C   ARG A  88      -7.828  12.534   0.746  1.00 64.36           C  
ANISOU  548  C   ARG A  88     5407   7946  11101    833   1604    485       C  
ATOM    549  O   ARG A  88      -8.319  13.089  -0.236  1.00 66.19           O  
ANISOU  549  O   ARG A  88     5518   8116  11517    884   1453    567       O  
ATOM    550  CB  ARG A  88      -9.148  10.869   2.063  1.00 65.60           C  
ANISOU  550  CB  ARG A  88     5404   8268  11254    716   1859    469       C  
ATOM    551  CG  ARG A  88     -10.000  10.518   3.274  1.00 68.27           C  
ANISOU  551  CG  ARG A  88     5623   8677  11639    708   2107    408       C  
ATOM    552  CD  ARG A  88     -10.530   9.100   3.140  1.00 68.40           C  
ANISOU  552  CD  ARG A  88     5582   8777  11630    576   2088    499       C  
ATOM    553  NE  ARG A  88     -11.512   8.746   4.158  1.00 67.69           N  
ANISOU  553  NE  ARG A  88     5388   8753  11579    554   2283    458       N  
ATOM    554  CZ  ARG A  88     -12.811   9.005   4.060  1.00 68.42           C  
ANISOU  554  CZ  ARG A  88     5291   8836  11871    582   2279    466       C  
ATOM    555  NH1 ARG A  88     -13.283   9.633   2.992  1.00 69.12           N1+
ANISOU  555  NH1 ARG A  88     5248   8851  12165    642   2104    520       N1+
ATOM    556  NH2 ARG A  88     -13.638   8.644   5.032  1.00 69.28           N  
ANISOU  556  NH2 ARG A  88     5344   9011  11969    551   2447    424       N  
ATOM    557  N   LYS A  89      -6.568  12.108   0.769  1.00 61.54           N  
ANISOU  557  N   LYS A  89     5283   7611  10488    769   1563    467       N  
ATOM    558  CA  LYS A  89      -5.746  12.165  -0.436  1.00 57.12           C  
ANISOU  558  CA  LYS A  89     4842   7011   9850    743   1340    549       C  
ATOM    559  C   LYS A  89      -5.367  10.764  -0.890  1.00 49.60           C  
ANISOU  559  C   LYS A  89     3989   6141   8717    608   1238    617       C  
ATOM    560  O   LYS A  89      -4.361  10.209  -0.468  1.00 40.74           O  
ANISOU  560  O   LYS A  89     3054   5055   7372    549   1274    574       O  
ATOM    561  CB  LYS A  89      -4.506  13.033  -0.223  1.00 61.13           C  
ANISOU  561  CB  LYS A  89     5531   7451  10243    795   1354    471       C  
ATOM    562  CG  LYS A  89      -4.813  14.400   0.385  1.00 69.55           C  
ANISOU  562  CG  LYS A  89     6514   8428  11484    926   1479    377       C  
ATOM    563  CD  LYS A  89      -3.694  15.398   0.121  1.00 73.28           C  
ANISOU  563  CD  LYS A  89     7132   8802  11910    978   1420    340       C  
ATOM    564  CE  LYS A  89      -3.747  16.570   1.091  1.00 77.86           C  
ANISOU  564  CE  LYS A  89     7679   9304  12599   1088   1591    196       C  
ATOM    565  NZ  LYS A  89      -3.345  16.154   2.467  1.00 82.58           N1+
ANISOU  565  NZ  LYS A  89     8379   9984  13013   1057   1786     54       N1+
ATOM    566  N   PRO A  90      -6.189  10.175  -1.757  1.00 42.78           N  
ANISOU  566  N   PRO A  90     2992   5304   7958    558   1108    720       N  
ATOM    567  CA  PRO A  90      -5.882   8.802  -2.147  1.00 41.66           C  
ANISOU  567  CA  PRO A  90     2935   5233   7660    427   1021    770       C  
ATOM    568  C   PRO A  90      -4.679   8.759  -3.065  1.00 52.01           C  
ANISOU  568  C   PRO A  90     4436   6524   8800    393    852    801       C  
ATOM    569  O   PRO A  90      -4.236   9.777  -3.601  1.00 39.70           O  
ANISOU  569  O   PRO A  90     2917   4899   7269    465    773    812       O  
ATOM    570  CB  PRO A  90      -7.136   8.361  -2.898  1.00 49.85           C  
ANISOU  570  CB  PRO A  90     3762   6296   8883    393    914    860       C  
ATOM    571  CG  PRO A  90      -7.723   9.629  -3.429  1.00 51.39           C  
ANISOU  571  CG  PRO A  90     3814   6419   9291    510    846    893       C  
ATOM    572  CD  PRO A  90      -7.366  10.717  -2.456  1.00 49.48           C  
ANISOU  572  CD  PRO A  90     3614   6119   9069    618   1019    793       C  
ATOM    573  N   VAL A  91      -4.154   7.558  -3.238  1.00 49.38           N  
ANISOU  573  N   VAL A  91     4217   6246   8297    281    803    816       N  
ATOM    574  CA  VAL A  91      -2.977   7.350  -4.044  1.00 45.58           C  
ANISOU  574  CA  VAL A  91     3920   5758   7640    238    662    835       C  
ATOM    575  C   VAL A  91      -3.294   6.282  -5.100  1.00 40.99           C  
ANISOU  575  C   VAL A  91     3307   5222   7044    135    494    912       C  
ATOM    576  O   VAL A  91      -4.020   5.330  -4.821  1.00 39.57           O  
ANISOU  576  O   VAL A  91     3037   5087   6909     65    533    923       O  
ATOM    577  CB  VAL A  91      -1.806   6.967  -3.136  1.00 47.84           C  
ANISOU  577  CB  VAL A  91     4404   6059   7716    210    776    755       C  
ATOM    578  CG1 VAL A  91      -0.810   6.216  -3.899  1.00 56.43           C  
ANISOU  578  CG1 VAL A  91     5649   7162   8630    129    644    778       C  
ATOM    579  CG2 VAL A  91      -1.172   8.231  -2.510  1.00 35.69           C  
ANISOU  579  CG2 VAL A  91     2933   4462   6165    313    871    677       C  
ATOM    580  N   TYR A  92      -2.769   6.456  -6.312  1.00 36.36           N  
ANISOU  580  N   TYR A  92     2792   4624   6398    122    311    962       N  
ATOM    581  CA  TYR A  92      -3.201   5.679  -7.479  1.00 45.63           C  
ANISOU  581  CA  TYR A  92     3914   5841   7581     40    128   1031       C  
ATOM    582  C   TYR A  92      -2.029   5.213  -8.354  1.00 45.77           C  
ANISOU  582  C   TYR A  92     4122   5875   7395    -25     -1   1035       C  
ATOM    583  O   TYR A  92      -1.057   5.944  -8.549  1.00 34.28           O  
ANISOU  583  O   TYR A  92     2795   4383   5845     21    -15   1025       O  
ATOM    584  CB  TYR A  92      -4.171   6.532  -8.295  1.00 38.22           C  
ANISOU  584  CB  TYR A  92     2803   4887   6833    105      6   1111       C  
ATOM    585  CG  TYR A  92      -4.732   5.897  -9.540  1.00 45.19           C  
ANISOU  585  CG  TYR A  92     3610   5820   7738     30   -200   1184       C  
ATOM    586  CD1 TYR A  92      -5.290   4.632  -9.508  1.00 39.24           C  
ANISOU  586  CD1 TYR A  92     2792   5120   6995    -75   -211   1173       C  
ATOM    587  CD2 TYR A  92      -4.757   6.595 -10.743  1.00 47.28           C  
ANISOU  587  CD2 TYR A  92     3861   6081   8023     66   -384   1265       C  
ATOM    588  CE1 TYR A  92      -5.820   4.061 -10.641  1.00 45.20           C  
ANISOU  588  CE1 TYR A  92     3476   5924   7775   -147   -404   1225       C  
ATOM    589  CE2 TYR A  92      -5.290   6.037 -11.880  1.00 49.04           C  
ANISOU  589  CE2 TYR A  92     4016   6363   8254     -2   -580   1326       C  
ATOM    590  CZ  TYR A  92      -5.822   4.769 -11.825  1.00 49.71           C  
ANISOU  590  CZ  TYR A  92     4039   6502   8347   -109   -591   1298       C  
ATOM    591  OH  TYR A  92      -6.349   4.201 -12.956  1.00 41.38           O  
ANISOU  591  OH  TYR A  92     2916   5508   7300   -182   -792   1344       O  
ATOM    592  N   ASP A  93      -2.121   3.995  -8.881  1.00 35.03           N  
ANISOU  592  N   ASP A  93     2773   4562   5973   -134    -89   1043       N  
ATOM    593  CA  ASP A  93      -1.013   3.426  -9.649  1.00 39.83           C  
ANISOU  593  CA  ASP A  93     3559   5188   6388   -201   -193   1030       C  
ATOM    594  C   ASP A  93      -1.121   3.693 -11.156  1.00 44.38           C  
ANISOU  594  C   ASP A  93     4120   5790   6953   -214   -404   1096       C  
ATOM    595  O   ASP A  93      -0.242   3.313 -11.927  1.00 46.21           O  
ANISOU  595  O   ASP A  93     4492   6043   7024   -266   -497   1086       O  
ATOM    596  CB  ASP A  93      -0.847   1.922  -9.356  1.00 33.19           C  
ANISOU  596  CB  ASP A  93     2770   4375   5467   -313   -162    987       C  
ATOM    597  CG  ASP A  93      -1.942   1.049  -9.997  1.00 44.35           C  
ANISOU  597  CG  ASP A  93     4038   5828   6983   -397   -272   1020       C  
ATOM    598  OD1 ASP A  93      -3.005   1.570 -10.413  1.00 48.63           O  
ANISOU  598  OD1 ASP A  93     4410   6383   7683   -364   -344   1074       O  
ATOM    599  OD2 ASP A  93      -1.733  -0.180 -10.081  1.00 40.26           O1-
ANISOU  599  OD2 ASP A  93     3574   5325   6399   -497   -291    989       O1-
ATOM    600  N   GLY A  94      -2.203   4.343 -11.570  1.00 49.48           N  
ANISOU  600  N   GLY A  94     4594   6439   7767   -165   -480   1166       N  
ATOM    601  CA  GLY A  94      -2.386   4.684 -12.970  1.00 51.77           C  
ANISOU  601  CA  GLY A  94     4861   6761   8047   -169   -687   1244       C  
ATOM    602  C   GLY A  94      -3.140   3.618 -13.738  1.00 54.39           C  
ANISOU  602  C   GLY A  94     5105   7163   8397   -271   -829   1256       C  
ATOM    603  O   GLY A  94      -3.427   3.780 -14.921  1.00 54.78           O  
ANISOU  603  O   GLY A  94     5122   7257   8435   -285  -1015   1319       O  
ATOM    604  N   LYS A  95      -3.459   2.517 -13.065  1.00 53.69           N  
ANISOU  604  N   LYS A  95     4980   7084   8336   -346   -743   1198       N  
ATOM    605  CA  LYS A  95      -4.198   1.430 -13.691  1.00 49.36           C  
ANISOU  605  CA  LYS A  95     4340   6589   7824   -452   -865   1195       C  
ATOM    606  C   LYS A  95      -5.461   1.124 -12.918  1.00 47.36           C  
ANISOU  606  C   LYS A  95     3880   6331   7785   -460   -780   1199       C  
ATOM    607  O   LYS A  95      -6.439   1.862 -12.994  1.00 48.12           O  
ANISOU  607  O   LYS A  95     3799   6427   8056   -395   -813   1258       O  
ATOM    608  CB  LYS A  95      -3.341   0.170 -13.780  1.00 57.37           C  
ANISOU  608  CB  LYS A  95     5512   7617   8670   -562   -861   1118       C  
ATOM    609  CG  LYS A  95      -2.234   0.249 -14.807  1.00 67.66           C  
ANISOU  609  CG  LYS A  95     6995   8945   9768   -579   -978   1108       C  
ATOM    610  CD  LYS A  95      -1.424  -1.038 -14.839  1.00 72.66           C  
ANISOU  610  CD  LYS A  95     7769   9580  10257   -682   -962   1022       C  
ATOM    611  CE  LYS A  95      -0.678  -1.258 -13.535  1.00 73.47           C  
ANISOU  611  CE  LYS A  95     7969   9623  10321   -662   -760    973       C  
ATOM    612  NZ  LYS A  95       0.169  -2.480 -13.594  1.00 73.98           N1+
ANISOU  612  NZ  LYS A  95     8172   9680  10256   -753   -752    896       N1+
ATOM    613  N   LYS A  96      -5.431   0.033 -12.161  1.00 50.30           N  
ANISOU  613  N   LYS A  96     4271   6694   8148   -539   -665   1142       N  
ATOM    614  CA  LYS A  96      -6.628  -0.435 -11.476  1.00 54.03           C  
ANISOU  614  CA  LYS A  96     4547   7166   8816   -570   -581   1147       C  
ATOM    615  C   LYS A  96      -6.596  -0.234  -9.962  1.00 50.21           C  
ANISOU  615  C   LYS A  96     4061   6642   8374   -519   -332   1123       C  
ATOM    616  O   LYS A  96      -7.612  -0.410  -9.297  1.00 52.15           O  
ANISOU  616  O   LYS A  96     4135   6889   8790   -525   -233   1134       O  
ATOM    617  CB  LYS A  96      -6.901  -1.907 -11.820  1.00 56.96           C  
ANISOU  617  CB  LYS A  96     4899   7559   9185   -714   -650   1113       C  
ATOM    618  CG  LYS A  96      -7.221  -2.134 -13.300  1.00 61.90           C  
ANISOU  618  CG  LYS A  96     5482   8239   9799   -772   -902   1128       C  
ATOM    619  CD  LYS A  96      -7.487  -3.598 -13.632  1.00 63.78           C  
ANISOU  619  CD  LYS A  96     5699   8489  10046   -918   -969   1077       C  
ATOM    620  CE  LYS A  96      -8.957  -3.952 -13.469  1.00 69.59           C  
ANISOU  620  CE  LYS A  96     6179   9236  11024   -964   -981   1102       C  
ATOM    621  NZ  LYS A  96      -9.857  -3.155 -14.365  1.00 71.45           N1+
ANISOU  621  NZ  LYS A  96     6247   9524  11375   -917  -1161   1162       N1+
ATOM    622  N   ASN A  97      -5.449   0.157  -9.419  1.00 50.51           N  
ANISOU  622  N   ASN A  97     4284   6652   8257   -468   -230   1089       N  
ATOM    623  CA  ASN A  97      -5.284   0.174  -7.958  1.00 50.59           C  
ANISOU  623  CA  ASN A  97     4322   6636   8263   -436      3   1054       C  
ATOM    624  C   ASN A  97      -5.241   1.547  -7.285  1.00 40.50           C  
ANISOU  624  C   ASN A  97     3026   5330   7031   -302    119   1049       C  
ATOM    625  O   ASN A  97      -4.423   2.397  -7.624  1.00 37.83           O  
ANISOU  625  O   ASN A  97     2802   4968   6601   -235     74   1044       O  
ATOM    626  CB  ASN A  97      -4.056  -0.653  -7.555  1.00 53.63           C  
ANISOU  626  CB  ASN A  97     4922   7010   8446   -493     62   1005       C  
ATOM    627  CG  ASN A  97      -4.027  -2.004  -8.238  1.00 58.82           C  
ANISOU  627  CG  ASN A  97     5605   7680   9064   -622    -51    999       C  
ATOM    628  ND2 ASN A  97      -4.533  -3.027  -7.555  1.00 52.31           N  
ANISOU  628  ND2 ASN A  97     4720   6850   8304   -700     45    998       N  
ATOM    629  OD1 ASN A  97      -3.575  -2.123  -9.383  1.00 66.97           O  
ANISOU  629  OD1 ASN A  97     6708   8725  10013   -653   -221    994       O  
ATOM    630  N   ILE A  98      -6.120   1.749  -6.312  1.00 43.25           N  
ANISOU  630  N   ILE A  98     3230   5678   7525   -267    278   1045       N  
ATOM    631  CA  ILE A  98      -6.114   2.985  -5.541  1.00 49.09           C  
ANISOU  631  CA  ILE A  98     3949   6387   8316   -142    413   1019       C  
ATOM    632  C   ILE A  98      -6.145   2.691  -4.033  1.00 49.60           C  
ANISOU  632  C   ILE A  98     4028   6462   8356   -143    656    968       C  
ATOM    633  O   ILE A  98      -6.823   1.761  -3.584  1.00 47.11           O  
ANISOU  633  O   ILE A  98     3624   6177   8100   -219    731    981       O  
ATOM    634  CB  ILE A  98      -7.266   3.921  -5.972  1.00 54.05           C  
ANISOU  634  CB  ILE A  98     4357   7002   9177    -62    356   1065       C  
ATOM    635  CG1 ILE A  98      -7.159   5.278  -5.285  1.00 56.61           C  
ANISOU  635  CG1 ILE A  98     4672   7278   9559     74    482   1029       C  
ATOM    636  CG2 ILE A  98      -8.600   3.297  -5.680  1.00 58.71           C  
ANISOU  636  CG2 ILE A  98     4728   7624   9955   -111    407   1087       C  
ATOM    637  CD1 ILE A  98      -8.266   6.230  -5.676  1.00 61.26           C  
ANISOU  637  CD1 ILE A  98     5041   7840  10395    164    430   1075       C  
ATOM    638  N   TYR A  99      -5.381   3.468  -3.266  1.00 46.70           N  
ANISOU  638  N   TYR A  99     3779   6073   7894    -63    775    910       N  
ATOM    639  CA  TYR A  99      -5.270   3.266  -1.828  1.00 39.17           C  
ANISOU  639  CA  TYR A  99     2867   5140   6876    -58   1000    856       C  
ATOM    640  C   TYR A  99      -5.624   4.521  -1.055  1.00 45.55           C  
ANISOU  640  C   TYR A  99     3599   5928   7781     63   1146    802       C  
ATOM    641  O   TYR A  99      -5.346   5.638  -1.499  1.00 41.48           O  
ANISOU  641  O   TYR A  99     3093   5362   7303    153   1080    788       O  
ATOM    642  CB  TYR A  99      -3.855   2.842  -1.433  1.00 39.42           C  
ANISOU  642  CB  TYR A  99     3143   5175   6662    -89   1025    816       C  
ATOM    643  CG  TYR A  99      -3.373   1.608  -2.147  1.00 45.82           C  
ANISOU  643  CG  TYR A  99     4045   5995   7371   -203    893    854       C  
ATOM    644  CD1 TYR A  99      -3.564   0.341  -1.601  1.00 46.73           C  
ANISOU  644  CD1 TYR A  99     4166   6137   7452   -300    966    874       C  
ATOM    645  CD2 TYR A  99      -2.739   1.704  -3.375  1.00 35.43           C  
ANISOU  645  CD2 TYR A  99     2808   4656   5997   -214    699    870       C  
ATOM    646  CE1 TYR A  99      -3.128  -0.795  -2.266  1.00 44.75           C  
ANISOU  646  CE1 TYR A  99     3996   5882   7127   -402    846    900       C  
ATOM    647  CE2 TYR A  99      -2.301   0.574  -4.043  1.00 43.73           C  
ANISOU  647  CE2 TYR A  99     3941   5715   6958   -316    584    889       C  
ATOM    648  CZ  TYR A  99      -2.494  -0.670  -3.484  1.00 41.46           C  
ANISOU  648  CZ  TYR A  99     3656   5445   6653   -408    656    899       C  
ATOM    649  OH  TYR A  99      -2.053  -1.785  -4.150  1.00 37.87           O  
ANISOU  649  OH  TYR A  99     3281   4985   6125   -506    544    909       O  
ATOM    650  N   THR A 100      -6.217   4.316   0.118  1.00 42.89           N  
ANISOU  650  N   THR A 100     3188   5627   7480     63   1350    771       N  
ATOM    651  CA  THR A 100      -6.568   5.396   1.019  1.00 45.83           C  
ANISOU  651  CA  THR A 100     3491   5990   7933    172   1522    699       C  
ATOM    652  C   THR A 100      -6.188   5.002   2.433  1.00 47.03           C  
ANISOU  652  C   THR A 100     3748   6195   7925    152   1736    638       C  
ATOM    653  O   THR A 100      -6.170   3.819   2.759  1.00 50.35           O  
ANISOU  653  O   THR A 100     4211   6664   8257     52   1774    678       O  
ATOM    654  CB  THR A 100      -8.060   5.662   0.982  1.00 57.14           C  
ANISOU  654  CB  THR A 100     4657   7423   9629    204   1569    726       C  
ATOM    655  CG2 THR A 100      -8.335   7.087   1.364  1.00 64.09           C  
ANISOU  655  CG2 THR A 100     5457   8257  10637    343   1661    656       C  
ATOM    656  OG1 THR A 100      -8.547   5.437  -0.343  1.00 61.48           O  
ANISOU  656  OG1 THR A 100     5101   7954  10304    170   1353    812       O  
ATOM    657  N   VAL A 101      -5.898   5.992   3.274  1.00 42.55           N  
ANISOU  657  N   VAL A 101     3223   5619   7325    247   1873    541       N  
ATOM    658  CA  VAL A 101      -5.391   5.738   4.622  1.00 46.98           C  
ANISOU  658  CA  VAL A 101     3911   6240   7699    236   2064    473       C  
ATOM    659  C   VAL A 101      -6.503   5.343   5.613  1.00 56.00           C  
ANISOU  659  C   VAL A 101     4908   7452   8919    216   2278    472       C  
ATOM    660  O   VAL A 101      -6.259   4.622   6.586  1.00 61.16           O  
ANISOU  660  O   VAL A 101     5654   8176   9410    160   2415    468       O  
ATOM    661  CB  VAL A 101      -4.583   6.948   5.143  1.00 47.40           C  
ANISOU  661  CB  VAL A 101     4076   6262   7671    340   2122    355       C  
ATOM    662  CG1 VAL A 101      -5.503   8.128   5.446  1.00 48.56           C  
ANISOU  662  CG1 VAL A 101     4047   6376   8028    451   2235    285       C  
ATOM    663  CG2 VAL A 101      -3.764   6.564   6.364  1.00 50.78           C  
ANISOU  663  CG2 VAL A 101     4682   6760   7852    313   2262    291       C  
ATOM    664  N   THR A 102      -7.718   5.819   5.353  1.00 52.69           N  
ANISOU  664  N   THR A 102     4259   7013   8750    261   2305    482       N  
ATOM    665  CA  THR A 102      -8.907   5.405   6.091  1.00 53.40           C  
ANISOU  665  CA  THR A 102     4173   7163   8955    234   2493    495       C  
ATOM    666  C   THR A 102      -9.991   5.044   5.077  1.00 53.03           C  
ANISOU  666  C   THR A 102     3907   7089   9152    195   2366    590       C  
ATOM    667  O   THR A 102      -9.909   5.434   3.912  1.00 53.02           O  
ANISOU  667  O   THR A 102     3878   7025   9244    222   2157    625       O  
ATOM    668  CB  THR A 102      -9.426   6.525   7.024  1.00 57.56           C  
ANISOU  668  CB  THR A 102     4622   7696   9551    346   2681    376       C  
ATOM    669  CG2 THR A 102      -8.412   6.821   8.126  1.00 49.23           C  
ANISOU  669  CG2 THR A 102     3781   6684   8241    374   2809    270       C  
ATOM    670  OG1 THR A 102      -9.660   7.718   6.262  1.00 55.17           O  
ANISOU  670  OG1 THR A 102     4210   7302   9448    456   2581    347       O  
ATOM    671  N   ALA A 103     -11.006   4.308   5.516  1.00 50.48           N  
ANISOU  671  N   ALA A 103     3453   6819   8910    128   2471    628       N  
ATOM    672  CA  ALA A 103     -12.043   3.816   4.611  1.00 51.40           C  
ANISOU  672  CA  ALA A 103     3376   6918   9236     73   2339    712       C  
ATOM    673  C   ALA A 103     -12.890   4.927   3.994  1.00 55.63           C  
ANISOU  673  C   ALA A 103     3730   7398  10009    179   2256    689       C  
ATOM    674  O   ALA A 103     -13.184   5.934   4.638  1.00 56.45           O  
ANISOU  674  O   ALA A 103     3808   7491  10147    283   2370    599       O  
ATOM    675  CB  ALA A 103     -12.935   2.803   5.323  1.00 52.97           C  
ANISOU  675  CB  ALA A 103     3518   7179   9429    -25   2455    740       C  
ATOM    676  N   LEU A 104     -13.273   4.726   2.738  1.00 55.60           N  
ANISOU  676  N   LEU A 104     3604   7360  10161    151   2045    772       N  
ATOM    677  CA  LEU A 104     -14.162   5.636   2.025  1.00 57.75           C  
ANISOU  677  CA  LEU A 104     3697   7581  10664    240   1931    777       C  
ATOM    678  C   LEU A 104     -15.595   5.319   2.418  1.00 62.62           C  
ANISOU  678  C   LEU A 104     4140   8230  11421    211   2008    774       C  
ATOM    679  O   LEU A 104     -15.920   4.159   2.665  1.00 67.14           O  
ANISOU  679  O   LEU A 104     4702   8853  11953     93   2049    812       O  
ATOM    680  CB  LEU A 104     -14.006   5.462   0.513  1.00 53.86           C  
ANISOU  680  CB  LEU A 104     3154   7055  10255    210   1657    873       C  
ATOM    681  CG  LEU A 104     -12.869   6.216  -0.170  1.00 56.67           C  
ANISOU  681  CG  LEU A 104     3661   7358  10515    277   1515    874       C  
ATOM    682  CD1 LEU A 104     -11.556   5.816   0.431  1.00 59.15           C  
ANISOU  682  CD1 LEU A 104     4254   7690  10533    234   1586    826       C  
ATOM    683  CD2 LEU A 104     -12.857   5.945  -1.663  1.00 55.65           C  
ANISOU  683  CD2 LEU A 104     3517   7213  10416    231   1224    964       C  
ATOM    684  N   PRO A 105     -16.465   6.342   2.464  1.00 64.99           N  
ANISOU  684  N   PRO A 105     4301   8497  11896    318   2027    732       N  
ATOM    685  CA  PRO A 105     -17.863   6.131   2.873  1.00 68.79           C  
ANISOU  685  CA  PRO A 105     4604   9010  12523    300   2112    723       C  
ATOM    686  C   PRO A 105     -18.650   5.398   1.791  1.00 68.94           C  
ANISOU  686  C   PRO A 105     4473   9029  12693    219   1916    817       C  
ATOM    687  O   PRO A 105     -19.721   5.840   1.386  1.00 68.80           O  
ANISOU  687  O   PRO A 105     4273   8990  12878    265   1850    827       O  
ATOM    688  CB  PRO A 105     -18.394   7.556   3.045  1.00 62.16           C  
ANISOU  688  CB  PRO A 105     3672   8116  11831    450   2153    652       C  
ATOM    689  CG  PRO A 105     -17.569   8.371   2.106  1.00 64.58           C  
ANISOU  689  CG  PRO A 105     4043   8344  12151    527   1975    677       C  
ATOM    690  CD  PRO A 105     -16.195   7.751   2.118  1.00 62.15           C  
ANISOU  690  CD  PRO A 105     3940   8060  11615    460   1967    693       C  
ATOM    691  N   ILE A 106     -18.111   4.270   1.346  1.00 72.46           N  
ANISOU  691  N   ILE A 106     4999   9500  13034     96   1824    881       N  
ATOM    692  CA  ILE A 106     -18.622   3.566   0.185  1.00 74.78           C  
ANISOU  692  CA  ILE A 106     5185   9791  13438     12   1603    961       C  
ATOM    693  C   ILE A 106     -19.069   2.162   0.584  1.00 77.12           C  
ANISOU  693  C   ILE A 106     5463  10137  13701   -135   1675    985       C  
ATOM    694  O   ILE A 106     -19.879   1.536  -0.097  1.00 77.59           O  
ANISOU  694  O   ILE A 106     5392  10202  13887   -209   1546   1029       O  
ATOM    695  CB  ILE A 106     -17.539   3.514  -0.924  1.00 75.86           C  
ANISOU  695  CB  ILE A 106     5434   9902  13489     -4   1385   1014       C  
ATOM    696  CG1 ILE A 106     -18.127   3.920  -2.275  1.00 73.96           C  
ANISOU  696  CG1 ILE A 106     5057   9632  13411     27   1124   1070       C  
ATOM    697  CG2 ILE A 106     -16.853   2.159  -0.973  1.00 76.41           C  
ANISOU  697  CG2 ILE A 106     5627  10002  13404   -151   1366   1050       C  
ATOM    698  CD1 ILE A 106     -18.615   5.341  -2.295  1.00 72.41           C  
ANISOU  698  CD1 ILE A 106     4767   9388  13358    181   1127   1046       C  
ATOM    699  N   GLY A 107     -18.542   1.680   1.705  1.00 78.86           N  
ANISOU  699  N   GLY A 107     5820  10393  13749   -177   1880    957       N  
ATOM    700  CA  GLY A 107     -18.931   0.391   2.245  1.00 83.58           C  
ANISOU  700  CA  GLY A 107     6418  11032  14306   -311   1975    985       C  
ATOM    701  C   GLY A 107     -18.455  -0.812   1.450  1.00 84.04           C  
ANISOU  701  C   GLY A 107     6542  11079  14309   -446   1813   1051       C  
ATOM    702  O   GLY A 107     -17.463  -1.453   1.799  1.00 85.80           O  
ANISOU  702  O   GLY A 107     6946  11308  14347   -507   1862   1065       O  
ATOM    703  N   ASN A 108     -19.165  -1.121   0.374  1.00 80.85           N  
ANISOU  703  N   ASN A 108     5997  10659  14065   -492   1614   1086       N  
ATOM    704  CA  ASN A 108     -18.944  -2.367  -0.337  1.00 78.10           C  
ANISOU  704  CA  ASN A 108     5688  10300  13687   -633   1468   1133       C  
ATOM    705  C   ASN A 108     -19.624  -2.303  -1.695  1.00 80.96           C  
ANISOU  705  C   ASN A 108     5899  10648  14215   -644   1210   1154       C  
ATOM    706  O   ASN A 108     -20.139  -3.299  -2.193  1.00 84.16           O  
ANISOU  706  O   ASN A 108     6241  11053  14683   -759   1109   1174       O  
ATOM    707  CB  ASN A 108     -19.533  -3.511   0.484  1.00 77.97           C  
ANISOU  707  CB  ASN A 108     5651  10305  13668   -748   1620   1146       C  
ATOM    708  CG  ASN A 108     -18.915  -4.845   0.155  1.00 76.97           C  
ANISOU  708  CG  ASN A 108     5646  10158  13443   -891   1540   1184       C  
ATOM    709  ND2 ASN A 108     -19.664  -5.688  -0.547  1.00 75.90           N  
ANISOU  709  ND2 ASN A 108     5398  10008  13433   -993   1408   1202       N  
ATOM    710  OD1 ASN A 108     -17.780  -5.125   0.541  1.00 76.23           O  
ANISOU  710  OD1 ASN A 108     5746  10056  13162   -909   1598   1193       O  
ATOM    711  N   GLU A 109     -19.602  -1.121  -2.298  1.00 80.65           N  
ANISOU  711  N   GLU A 109     5811  10595  14239   -522   1098   1148       N  
ATOM    712  CA  GLU A 109     -20.510  -0.804  -3.390  1.00 82.45           C  
ANISOU  712  CA  GLU A 109     5866  10818  14641   -501    885   1168       C  
ATOM    713  C   GLU A 109     -19.802  -0.316  -4.655  1.00 78.43           C  
ANISOU  713  C   GLU A 109     5418  10294  14088   -463    630   1198       C  
ATOM    714  O   GLU A 109     -18.915   0.532  -4.593  1.00 74.76           O  
ANISOU  714  O   GLU A 109     5059   9810  13535   -370    646   1197       O  
ATOM    715  CB  GLU A 109     -21.493   0.262  -2.902  1.00 88.27           C  
ANISOU  715  CB  GLU A 109     6446  11552  15539   -377    991   1142       C  
ATOM    716  CG  GLU A 109     -22.943  -0.019  -3.208  1.00 98.68           C  
ANISOU  716  CG  GLU A 109     7547  12886  17062   -412    933   1150       C  
ATOM    717  CD  GLU A 109     -23.343   0.486  -4.574  1.00105.50           C  
ANISOU  717  CD  GLU A 109     8309  13739  18037   -370    655   1185       C  
ATOM    718  OE1 GLU A 109     -22.753   0.019  -5.570  1.00106.73           O  
ANISOU  718  OE1 GLU A 109     8547  13900  18108   -434    447   1214       O  
ATOM    719  OE2 GLU A 109     -24.240   1.354  -4.650  1.00107.17           O1-
ANISOU  719  OE2 GLU A 109     8365  13941  18416   -272    643   1183       O1-
ATOM    720  N   ARG A 110     -20.203  -0.854  -5.803  1.00 81.74           N  
ANISOU  720  N   ARG A 110     5773  10726  14560   -538    396   1224       N  
ATOM    721  CA  ARG A 110     -19.720  -0.361  -7.092  1.00 86.12           C  
ANISOU  721  CA  ARG A 110     6367  11280  15074   -502    134   1258       C  
ATOM    722  C   ARG A 110     -20.367   0.987  -7.404  1.00 84.55           C  
ANISOU  722  C   ARG A 110     6044  11066  15014   -355     72   1278       C  
ATOM    723  O   ARG A 110     -21.486   1.034  -7.921  1.00 86.45           O  
ANISOU  723  O   ARG A 110     6119  11320  15407   -353    -37   1291       O  
ATOM    724  CB  ARG A 110     -20.052  -1.356  -8.214  1.00 95.37           C  
ANISOU  724  CB  ARG A 110     7507  12479  16250   -628    -98   1267       C  
ATOM    725  CG  ARG A 110     -18.972  -2.389  -8.513  1.00101.45           C  
ANISOU  725  CG  ARG A 110     8455  13251  16839   -750   -159   1257       C  
ATOM    726  CD  ARG A 110     -17.810  -1.770  -9.274  1.00108.17           C  
ANISOU  726  CD  ARG A 110     9452  14105  17544   -698   -309   1283       C  
ATOM    727  NE  ARG A 110     -16.642  -2.649  -9.303  1.00113.59           N  
ANISOU  727  NE  ARG A 110    10322  14786  18050   -799   -313   1266       N  
ATOM    728  CZ  ARG A 110     -15.384  -2.226  -9.432  1.00116.73           C  
ANISOU  728  CZ  ARG A 110    10879  15178  18296   -762   -335   1281       C  
ATOM    729  NH1 ARG A 110     -15.120  -0.929  -9.540  1.00118.75           N1+
ANISOU  729  NH1 ARG A 110    11152  15427  18540   -621   -351   1308       N1+
ATOM    730  NH2 ARG A 110     -14.385  -3.100  -9.446  1.00114.81           N  
ANISOU  730  NH2 ARG A 110    10845  14922  17854   -850   -332   1246       N  
ATOM    731  N   VAL A 111     -19.672   2.079  -7.090  1.00 78.37           N  
ANISOU  731  N   VAL A 111     5340  10251  14185   -231    142   1280       N  
ATOM    732  CA  VAL A 111     -20.187   3.419  -7.381  1.00 75.16           C  
ANISOU  732  CA  VAL A 111     4835   9812  13909    -84     85   1301       C  
ATOM    733  C   VAL A 111     -19.753   3.895  -8.765  1.00 71.54           C  
ANISOU  733  C   VAL A 111     4427   9353  13401    -53   -197   1367       C  
ATOM    734  O   VAL A 111     -18.617   3.668  -9.171  1.00 71.29           O  
ANISOU  734  O   VAL A 111     4558   9331  13199    -91   -276   1384       O  
ATOM    735  CB  VAL A 111     -19.743   4.448  -6.324  1.00 61.33           C  
ANISOU  735  CB  VAL A 111     3139   8014  12149     42    307   1261       C  
ATOM    736  CG1 VAL A 111     -20.630   4.366  -5.102  1.00 62.94           C  
ANISOU  736  CG1 VAL A 111     3235   8223  12456     51    557   1200       C  
ATOM    737  CG2 VAL A 111     -18.287   4.234  -5.954  1.00 58.69           C  
ANISOU  737  CG2 VAL A 111     3014   7677  11607     17    386   1245       C  
ATOM    738  N   ASP A 112     -20.655   4.563  -9.481  1.00 69.56           N  
ANISOU  738  N   ASP A 112     4042   9096  13292     15   -346   1408       N  
ATOM    739  CA  ASP A 112     -20.366   5.015 -10.841  1.00 69.63           C  
ANISOU  739  CA  ASP A 112     4097   9113  13245     42   -623   1481       C  
ATOM    740  C   ASP A 112     -20.314   6.540 -10.967  1.00 70.80           C  
ANISOU  740  C   ASP A 112     4238   9197  13464    206   -641   1525       C  
ATOM    741  O   ASP A 112     -19.439   7.094 -11.639  1.00 68.58           O  
ANISOU  741  O   ASP A 112     4087   8901  13069    249   -768   1578       O  
ATOM    742  CB  ASP A 112     -21.395   4.440 -11.815  1.00 70.80           C  
ANISOU  742  CB  ASP A 112     4116   9316  13469    -31   -832   1506       C  
ATOM    743  CG  ASP A 112     -21.472   2.928 -11.750  1.00 71.95           C  
ANISOU  743  CG  ASP A 112     4269   9512  13556   -198   -824   1457       C  
ATOM    744  OD1 ASP A 112     -22.557   2.370 -12.017  1.00 73.92           O  
ANISOU  744  OD1 ASP A 112     4371   9794  13923   -258   -888   1445       O  
ATOM    745  OD2 ASP A 112     -20.445   2.295 -11.429  1.00 74.65           O1-
ANISOU  745  OD2 ASP A 112     4766   9858  13740   -269   -752   1430       O1-
ATOM    746  N   LYS A 127     -16.817   7.600 -17.437  1.00 75.65           N  
ANISOU  746  N   LYS A 127     5533   9975  13234    161  -1858   1911       N  
ATOM    747  CA  LYS A 127     -17.201   6.204 -17.240  1.00 85.29           C  
ANISOU  747  CA  LYS A 127     6698  11259  14448     23  -1841   1826       C  
ATOM    748  C   LYS A 127     -16.225   5.476 -16.320  1.00 89.01           C  
ANISOU  748  C   LYS A 127     7274  11720  14827    -45  -1661   1752       C  
ATOM    749  O   LYS A 127     -15.277   4.840 -16.784  1.00 93.55           O  
ANISOU  749  O   LYS A 127     8006  12340  15198   -133  -1739   1738       O  
ATOM    750  CB  LYS A 127     -17.286   5.476 -18.584  1.00 89.81           C  
ANISOU  750  CB  LYS A 127     7324  11932  14866    -83  -2094   1837       C  
ATOM    751  CG  LYS A 127     -17.914   4.088 -18.504  1.00 90.79           C  
ANISOU  751  CG  LYS A 127     7365  12112  15020   -222  -2099   1746       C  
ATOM    752  CD  LYS A 127     -18.499   3.657 -19.844  1.00 89.67           C  
ANISOU  752  CD  LYS A 127     7203  12061  14806   -289  -2355   1756       C  
ATOM    753  CE  LYS A 127     -19.883   3.049 -19.662  1.00 90.14           C  
ANISOU  753  CE  LYS A 127     7050  12139  15061   -336  -2353   1708       C  
ATOM    754  NZ  LYS A 127     -20.532   2.682 -20.951  1.00 92.63           N1+
ANISOU  754  NZ  LYS A 127     7327  12546  15320   -393  -2604   1711       N1+
ATOM    755  N   VAL A 128     -16.459   5.575 -15.013  1.00 84.68           N  
ANISOU  755  N   VAL A 128     6641  11112  14420     -5  -1416   1701       N  
ATOM    756  CA  VAL A 128     -15.562   4.985 -14.025  1.00 76.73           C  
ANISOU  756  CA  VAL A 128     5729  10092  13335    -56  -1221   1636       C  
ATOM    757  C   VAL A 128     -16.327   4.419 -12.839  1.00 74.98           C  
ANISOU  757  C   VAL A 128     5376   9854  13259    -88   -999   1563       C  
ATOM    758  O   VAL A 128     -17.282   5.033 -12.359  1.00 77.29           O  
ANISOU  758  O   VAL A 128     5521  10110  13735     -4   -907   1560       O  
ATOM    759  CB  VAL A 128     -14.561   6.025 -13.484  1.00 74.53           C  
ANISOU  759  CB  VAL A 128     5556   9747  13015     59  -1100   1655       C  
ATOM    760  CG1 VAL A 128     -13.746   5.440 -12.348  1.00 73.47           C  
ANISOU  760  CG1 VAL A 128     5571   9592  12753     12   -861   1558       C  
ATOM    761  CG2 VAL A 128     -13.645   6.494 -14.581  1.00 77.52           C  
ANISOU  761  CG2 VAL A 128     6103  10139  13211     77  -1293   1724       C  
ATOM    762  N   SER A 129     -15.906   3.248 -12.369  1.00 72.15           N  
ANISOU  762  N   SER A 129     5079   9521  12816   -211   -909   1506       N  
ATOM    763  CA  SER A 129     -16.451   2.692 -11.138  1.00 72.32           C  
ANISOU  763  CA  SER A 129     5013   9525  12940   -245   -668   1444       C  
ATOM    764  C   SER A 129     -15.368   2.396 -10.101  1.00 64.74           C  
ANISOU  764  C   SER A 129     4190   8545  11863   -267   -455   1404       C  
ATOM    765  O   SER A 129     -14.222   2.089 -10.446  1.00 61.56           O  
ANISOU  765  O   SER A 129     4031   8145  11215   -309   -509   1382       O  
ATOM    766  CB  SER A 129     -17.269   1.434 -11.423  1.00 80.08           C  
ANISOU  766  CB  SER A 129     5913  10551  13964   -384   -734   1414       C  
ATOM    767  OG  SER A 129     -16.462   0.437 -12.017  1.00 84.14           O  
ANISOU  767  OG  SER A 129     6565  11097  14307   -510   -851   1398       O  
ATOM    768  N   ILE A 130     -15.744   2.516  -8.831  1.00 60.10           N  
ANISOU  768  N   ILE A 130     3543   7930  11361   -229   -199   1360       N  
ATOM    769  CA  ILE A 130     -14.874   2.153  -7.718  1.00 52.50           C  
ANISOU  769  CA  ILE A 130     2750   6952  10245   -252     28   1303       C  
ATOM    770  C   ILE A 130     -15.589   1.151  -6.808  1.00 59.92           C  
ANISOU  770  C   ILE A 130     3580   7910  11275   -346    205   1276       C  
ATOM    771  O   ILE A 130     -16.787   1.285  -6.533  1.00 60.27           O  
ANISOU  771  O   ILE A 130     3467   7956  11478   -322    259   1264       O  
ATOM    772  CB  ILE A 130     -14.446   3.390  -6.885  1.00 57.53           C  
ANISOU  772  CB  ILE A 130     3449   7542  10867   -105    201   1272       C  
ATOM    773  CG1 ILE A 130     -13.719   4.407  -7.763  1.00 59.31           C  
ANISOU  773  CG1 ILE A 130     3794   7735  11004    -14     35   1304       C  
ATOM    774  CG2 ILE A 130     -13.538   2.984  -5.731  1.00 50.48           C  
ANISOU  774  CG2 ILE A 130     2757   6644   9779   -132    423   1204       C  
ATOM    775  CD1 ILE A 130     -13.146   5.586  -6.989  1.00 56.42           C  
ANISOU  775  CD1 ILE A 130     3517   7311  10609    119    194   1262       C  
ATOM    776  N   LYS A 131     -14.864   0.131  -6.364  1.00 52.13           N  
ANISOU  776  N   LYS A 131     2758   6930  10121   -450    289   1247       N  
ATOM    777  CA  LYS A 131     -15.398  -0.783  -5.371  1.00 59.68           C  
ANISOU  777  CA  LYS A 131     3649   7895  11131   -534    484   1230       C  
ATOM    778  C   LYS A 131     -14.269  -1.324  -4.519  1.00 55.29           C  
ANISOU  778  C   LYS A 131     3328   7330  10350   -574    642   1200       C  
ATOM    779  O   LYS A 131     -13.160  -1.554  -5.004  1.00 53.93           O  
ANISOU  779  O   LYS A 131     3377   7146   9968   -597    534   1185       O  
ATOM    780  CB  LYS A 131     -16.234  -1.897  -6.014  1.00 66.48           C  
ANISOU  780  CB  LYS A 131     4419   8772  12070   -663    350   1237       C  
ATOM    781  CG  LYS A 131     -15.706  -3.308  -5.835  1.00 71.49           C  
ANISOU  781  CG  LYS A 131     5171   9400  12591   -812    379   1229       C  
ATOM    782  CD  LYS A 131     -16.692  -4.325  -6.406  1.00 77.40           C  
ANISOU  782  CD  LYS A 131     5806  10154  13446   -929    262   1221       C  
ATOM    783  CE  LYS A 131     -16.007  -5.650  -6.722  1.00 81.01           C  
ANISOU  783  CE  LYS A 131     6399  10593  13789  -1074    194   1209       C  
ATOM    784  NZ  LYS A 131     -14.888  -5.491  -7.704  1.00 79.99           N1+
ANISOU  784  NZ  LYS A 131     6406  10467  13521  -1077      2   1211       N1+
ATOM    785  N   TRP A 132     -14.554  -1.492  -3.235  1.00 51.78           N  
ANISOU  785  N   TRP A 132     2846   6894   9933   -576    898   1187       N  
ATOM    786  CA  TRP A 132     -13.541  -1.897  -2.277  1.00 57.48           C  
ANISOU  786  CA  TRP A 132     3796   7614  10430   -596   1063   1160       C  
ATOM    787  C   TRP A 132     -13.009  -3.291  -2.586  1.00 55.06           C  
ANISOU  787  C   TRP A 132     3619   7296  10006   -740    984   1177       C  
ATOM    788  O   TRP A 132     -13.745  -4.165  -3.040  1.00 50.58           O  
ANISOU  788  O   TRP A 132     2916   6727   9575   -848    907   1207       O  
ATOM    789  CB  TRP A 132     -14.093  -1.822  -0.850  1.00 60.70           C  
ANISOU  789  CB  TRP A 132     4135   8046  10883   -573   1348   1144       C  
ATOM    790  CG  TRP A 132     -13.124  -2.287   0.181  1.00 57.50           C  
ANISOU  790  CG  TRP A 132     3937   7651  10260   -601   1521   1133       C  
ATOM    791  CD1 TRP A 132     -12.045  -1.607   0.654  1.00 56.68           C  
ANISOU  791  CD1 TRP A 132     4037   7544   9952   -514   1579   1084       C  
ATOM    792  CD2 TRP A 132     -13.143  -3.544   0.865  1.00 59.63           C  
ANISOU  792  CD2 TRP A 132     4271   7930  10455   -719   1631   1162       C  
ATOM    793  CE2 TRP A 132     -12.043  -3.555   1.744  1.00 59.56           C  
ANISOU  793  CE2 TRP A 132     4474   7933  10225   -699   1767   1148       C  
ATOM    794  CE3 TRP A 132     -13.985  -4.660   0.820  1.00 63.43           C  
ANISOU  794  CE3 TRP A 132     4670   8407  11022   -836   1615   1192       C  
ATOM    795  NE1 TRP A 132     -11.386  -2.362   1.594  1.00 59.32           N  
ANISOU  795  NE1 TRP A 132     4537   7896  10105   -571   1722   1088       N  
ATOM    796  CZ2 TRP A 132     -11.759  -4.642   2.571  1.00 60.02           C  
ANISOU  796  CZ2 TRP A 132     4647   8000  10156   -791   1889   1182       C  
ATOM    797  CZ3 TRP A 132     -13.702  -5.737   1.638  1.00 65.85           C  
ANISOU  797  CZ3 TRP A 132     5098   8715  11208   -928   1739   1220       C  
ATOM    798  CH2 TRP A 132     -12.597  -5.722   2.502  1.00 63.48           C  
ANISOU  798  CH2 TRP A 132     5001   8427  10690   -903   1870   1220       C  
ATOM    799  N   LEU A 133     -11.717  -3.481  -2.356  1.00 54.60           N  
ANISOU  799  N   LEU A 133     3818   7223   9705   -739    998   1153       N  
ATOM    800  CA  LEU A 133     -11.087  -4.767  -2.596  1.00 58.84           C  
ANISOU  800  CA  LEU A 133     4495   7737  10124   -863    933   1163       C  
ATOM    801  C   LEU A 133     -10.721  -5.390  -1.259  1.00 60.27           C  
ANISOU  801  C   LEU A 133     4781   7921  10199   -899   1161   1176       C  
ATOM    802  O   LEU A 133     -11.410  -6.279  -0.761  1.00 63.35           O  
ANISOU  802  O   LEU A 133     5069   8310  10692   -993   1265   1218       O  
ATOM    803  CB  LEU A 133      -9.829  -4.599  -3.452  1.00 60.38           C  
ANISOU  803  CB  LEU A 133     4905   7912  10123   -840    756   1131       C  
ATOM    804  CG  LEU A 133      -9.604  -5.616  -4.569  1.00 63.53           C  
ANISOU  804  CG  LEU A 133     5348   8290  10500   -953    551   1129       C  
ATOM    805  CD1 LEU A 133      -9.579  -7.034  -4.026  1.00 62.45           C  
ANISOU  805  CD1 LEU A 133     5247   8124  10357  -1080    638   1147       C  
ATOM    806  CD2 LEU A 133     -10.680  -5.466  -5.635  1.00 69.06           C  
ANISOU  806  CD2 LEU A 133     5836   9009  11395   -975    375   1144       C  
ATOM    807  N   ALA A 134      -9.640  -4.895  -0.673  1.00 56.61           N  
ANISOU  807  N   ALA A 134     4518   7462   9531   -823   1237   1144       N  
ATOM    808  CA  ALA A 134      -9.069  -5.514   0.509  1.00 53.65           C  
ANISOU  808  CA  ALA A 134     4283   7093   9007   -856   1419   1160       C  
ATOM    809  C   ALA A 134      -8.451  -4.490   1.450  1.00 52.67           C  
ANISOU  809  C   ALA A 134     4271   7002   8739   -737   1566   1114       C  
ATOM    810  O   ALA A 134      -8.364  -3.301   1.145  1.00 43.77           O  
ANISOU  810  O   ALA A 134     3127   5877   7625   -628   1520   1066       O  
ATOM    811  CB  ALA A 134      -8.016  -6.548   0.105  1.00 45.63           C  
ANISOU  811  CB  ALA A 134     3462   6034   7839   -938   1307   1168       C  
ATOM    812  N   ILE A 135      -8.028  -4.982   2.605  1.00 49.17           N  
ANISOU  812  N   ILE A 135     3943   6581   8159   -761   1739   1132       N  
ATOM    813  CA  ILE A 135      -7.249  -4.205   3.543  1.00 50.25           C  
ANISOU  813  CA  ILE A 135     4225   6753   8116   -665   1866   1082       C  
ATOM    814  C   ILE A 135      -5.814  -4.671   3.413  1.00 46.12           C  
ANISOU  814  C   ILE A 135     3947   6203   7374   -683   1772   1075       C  
ATOM    815  O   ILE A 135      -5.550  -5.865   3.402  1.00 51.65           O  
ANISOU  815  O   ILE A 135     4714   6878   8034   -782   1747   1129       O  
ATOM    816  CB  ILE A 135      -7.714  -4.476   4.979  1.00 52.85           C  
ANISOU  816  CB  ILE A 135     4525   7140   8416   -682   2125   1110       C  
ATOM    817  CG1 ILE A 135      -9.135  -3.950   5.184  1.00 58.63           C  
ANISOU  817  CG1 ILE A 135     5003   7902   9370   -656   2243   1107       C  
ATOM    818  CG2 ILE A 135      -6.752  -3.856   5.981  1.00 54.04           C  
ANISOU  818  CG2 ILE A 135     4859   7333   8339   -600   2243   1055       C  
ATOM    819  CD1 ILE A 135      -9.787  -4.452   6.454  1.00 66.86           C  
ANISOU  819  CD1 ILE A 135     6029   9002  10371   -694   2448   1127       C  
ATOM    820  N   VAL A 136      -4.878  -3.745   3.293  1.00 40.16           N  
ANISOU  820  N   VAL A 136     3321   5445   6492   -589   1719   1007       N  
ATOM    821  CA  VAL A 136      -3.484  -4.140   3.375  1.00 39.86           C  
ANISOU  821  CA  VAL A 136     3513   5391   6242   -599   1662    995       C  
ATOM    822  C   VAL A 136      -2.887  -3.625   4.683  1.00 39.79           C  
ANISOU  822  C   VAL A 136     3624   5434   6061   -531   1830    956       C  
ATOM    823  O   VAL A 136      -3.145  -2.496   5.109  1.00 41.37           O  
ANISOU  823  O   VAL A 136     3775   5664   6281   -439   1920    893       O  
ATOM    824  CB  VAL A 136      -2.678  -3.758   2.104  1.00 46.31           C  
ANISOU  824  CB  VAL A 136     4409   6160   7025   -572   1443    955       C  
ATOM    825  CG1 VAL A 136      -3.562  -3.009   1.124  1.00 49.30           C  
ANISOU  825  CG1 VAL A 136     4615   6528   7591   -537   1342    946       C  
ATOM    826  CG2 VAL A 136      -1.405  -2.984   2.445  1.00 43.31           C  
ANISOU  826  CG2 VAL A 136     4211   5785   6459   -487   1447    888       C  
ATOM    827  N   SER A 137      -2.116  -4.484   5.334  1.00 39.66           N  
ANISOU  827  N   SER A 137     3761   5427   5883   -580   1873    991       N  
ATOM    828  CA  SER A 137      -1.629  -4.203   6.670  1.00 42.68           C  
ANISOU  828  CA  SER A 137     4255   5873   6089   -534   2036    968       C  
ATOM    829  C   SER A 137      -0.164  -3.831   6.598  1.00 46.18           C  
ANISOU  829  C   SER A 137     4896   6303   6347   -481   1941    908       C  
ATOM    830  O   SER A 137       0.641  -4.582   6.040  1.00 51.56           O  
ANISOU  830  O   SER A 137     5684   6937   6970   -529   1810    936       O  
ATOM    831  CB  SER A 137      -1.838  -5.428   7.569  1.00 41.69           C  
ANISOU  831  CB  SER A 137     4158   5776   5908   -624   2161   1068       C  
ATOM    832  OG  SER A 137      -1.127  -5.304   8.789  1.00 43.76           O  
ANISOU  832  OG  SER A 137     4567   6103   5956   -588   2284   1055       O  
ATOM    833  N   TRP A 138       0.179  -2.660   7.131  1.00 45.19           N  
ANISOU  833  N   TRP A 138     4813   6214   6143   -383   2007    817       N  
ATOM    834  CA  TRP A 138       1.583  -2.268   7.202  1.00 45.04           C  
ANISOU  834  CA  TRP A 138     4978   6189   5948   -335   1933    754       C  
ATOM    835  C   TRP A 138       2.165  -2.757   8.507  1.00 46.27           C  
ANISOU  835  C   TRP A 138     5268   6409   5901   -347   2051    772       C  
ATOM    836  O   TRP A 138       3.380  -2.918   8.636  1.00 49.15           O  
ANISOU  836  O   TRP A 138     5795   6769   6109   -338   1981    754       O  
ATOM    837  CB  TRP A 138       1.773  -0.761   7.031  1.00 43.80           C  
ANISOU  837  CB  TRP A 138     4806   6022   5813   -228   1920    642       C  
ATOM    838  CG  TRP A 138       1.767  -0.339   5.584  1.00 43.55           C  
ANISOU  838  CG  TRP A 138     4716   5916   5915   -215   1743    634       C  
ATOM    839  CD1 TRP A 138       1.813  -1.160   4.491  1.00 35.76           C  
ANISOU  839  CD1 TRP A 138     3720   4881   4985   -286   1591    698       C  
ATOM    840  CD2 TRP A 138       1.705   1.006   5.074  1.00 44.13           C  
ANISOU  840  CD2 TRP A 138     4736   5955   6076   -127   1700    562       C  
ATOM    841  CE2 TRP A 138       1.716   0.919   3.666  1.00 37.12           C  
ANISOU  841  CE2 TRP A 138     3812   5008   5285   -151   1518    598       C  
ATOM    842  CE3 TRP A 138       1.639   2.271   5.673  1.00 40.06           C  
ANISOU  842  CE3 TRP A 138     4200   5450   5570    -31   1799    469       C  
ATOM    843  NE1 TRP A 138       1.786  -0.411   3.336  1.00 36.57           N  
ANISOU  843  NE1 TRP A 138     3771   4935   5189   -249   1455    672       N  
ATOM    844  CZ2 TRP A 138       1.655   2.049   2.849  1.00 36.20           C  
ANISOU  844  CZ2 TRP A 138     3641   4845   5270    -82   1432    563       C  
ATOM    845  CZ3 TRP A 138       1.577   3.386   4.864  1.00 36.29           C  
ANISOU  845  CZ3 TRP A 138     3664   4913   5214     39   1714    428       C  
ATOM    846  CH2 TRP A 138       1.592   3.270   3.465  1.00 39.26           C  
ANISOU  846  CH2 TRP A 138     4006   5231   5679     13   1531    484       C  
ATOM    847  N   ARG A 139       1.280  -3.001   9.468  1.00 46.58           N  
ANISOU  847  N   ARG A 139     5235   6515   5948   -368   2232    812       N  
ATOM    848  CA  ARG A 139       1.646  -3.699  10.689  1.00 50.76           C  
ANISOU  848  CA  ARG A 139     5880   7114   6291   -400   2350    866       C  
ATOM    849  C   ARG A 139       2.274  -5.039  10.319  1.00 45.30           C  
ANISOU  849  C   ARG A 139     5282   6369   5561   -484   2235    970       C  
ATOM    850  O   ARG A 139       3.361  -5.376  10.792  1.00 36.72           O  
ANISOU  850  O   ARG A 139     4359   5297   4295   -480   2201    980       O  
ATOM    851  CB  ARG A 139       0.407  -3.917  11.560  1.00 59.23           C  
ANISOU  851  CB  ARG A 139     6832   8258   7416   -431   2559    917       C  
ATOM    852  CG  ARG A 139       0.576  -4.975  12.638  1.00 68.42           C  
ANISOU  852  CG  ARG A 139     8098   9482   8417   -497   2626   1007       C  
ATOM    853  CD  ARG A 139       1.153  -4.390  13.912  1.00 72.92           C  
ANISOU  853  CD  ARG A 139     8794  10158   8752   -437   2692    924       C  
ATOM    854  NE  ARG A 139       0.265  -3.388  14.494  1.00 72.75           N  
ANISOU  854  NE  ARG A 139     8665  10208   8769   -381   2828    827       N  
ATOM    855  CZ  ARG A 139       0.468  -2.802  15.667  1.00 65.94           C  
ANISOU  855  CZ  ARG A 139     7872   9452   7729   -333   2908    741       C  
ATOM    856  NH1 ARG A 139       1.529  -3.122  16.398  1.00 63.46           N1+
ANISOU  856  NH1 ARG A 139     7732   9194   7186   -338   2860    747       N1+
ATOM    857  NH2 ARG A 139      -0.391  -1.897  16.106  1.00 67.18           N  
ANISOU  857  NH2 ARG A 139     7918   9663   7945   -281   3030    647       N  
ATOM    858  N   MET A 140       1.598  -5.782   9.442  1.00 46.81           N  
ANISOU  858  N   MET A 140     5363   6492   5930   -559   2166   1040       N  
ATOM    859  CA  MET A 140       2.075  -7.094   9.012  1.00 42.64           C  
ANISOU  859  CA  MET A 140     4904   5897   5400   -644   2060   1131       C  
ATOM    860  C   MET A 140       3.421  -7.002   8.294  1.00 45.10           C  
ANISOU  860  C   MET A 140     5353   6154   5628   -612   1879   1075       C  
ATOM    861  O   MET A 140       4.296  -7.848   8.500  1.00 43.61           O  
ANISOU  861  O   MET A 140     5293   5941   5335   -643   1830   1125       O  
ATOM    862  CB  MET A 140       1.037  -7.791   8.123  1.00 45.28           C  
ANISOU  862  CB  MET A 140     5079   6167   5958   -728   2013   1190       C  
ATOM    863  CG  MET A 140       1.512  -9.135   7.546  1.00 50.26           C  
ANISOU  863  CG  MET A 140     5772   6710   6613   -818   1891   1265       C  
ATOM    864  SD  MET A 140       0.276 -10.051   6.591  1.00 61.87           S  
ANISOU  864  SD  MET A 140     7058   8106   8346   -932   1839   1327       S  
ATOM    865  CE  MET A 140       0.001  -8.952   5.205  1.00 64.32           C  
ANISOU  865  CE  MET A 140     7262   8399   8777   -876   1686   1215       C  
ATOM    866  N   LEU A 141       3.586  -5.977   7.455  1.00 43.01           N  
ANISOU  866  N   LEU A 141     5058   5869   5416   -550   1784    977       N  
ATOM    867  CA  LEU A 141       4.863  -5.762   6.767  1.00 42.37           C  
ANISOU  867  CA  LEU A 141     5100   5742   5256   -518   1626    917       C  
ATOM    868  C   LEU A 141       6.001  -5.501   7.769  1.00 31.54           C  
ANISOU  868  C   LEU A 141     3891   4421   3673   -465   1666    882       C  
ATOM    869  O   LEU A 141       7.081  -6.076   7.659  1.00 43.98           O  
ANISOU  869  O   LEU A 141     5590   5965   5155   -478   1575    895       O  
ATOM    870  CB  LEU A 141       4.748  -4.645   5.719  1.00 31.11           C  
ANISOU  870  CB  LEU A 141     3604   4288   3928   -462   1531    832       C  
ATOM    871  CG  LEU A 141       6.031  -4.112   5.076  1.00 29.47           C  
ANISOU  871  CG  LEU A 141     3513   4046   3637   -415   1396    758       C  
ATOM    872  CD1 LEU A 141       6.887  -5.222   4.452  1.00 28.51           C  
ANISOU  872  CD1 LEU A 141     3486   3869   3479   -476   1270    794       C  
ATOM    873  CD2 LEU A 141       5.690  -3.057   4.033  1.00 35.37           C  
ANISOU  873  CD2 LEU A 141     4170   4765   4502   -371   1316    702       C  
ATOM    874  N   HIS A 142       5.751  -4.655   8.757  1.00 40.63           N  
ANISOU  874  N   HIS A 142     5036   5651   4749   -407   1802    834       N  
ATOM    875  CA  HIS A 142       6.731  -4.446   9.819  1.00 48.19           C  
ANISOU  875  CA  HIS A 142     6142   6672   5497   -364   1847    800       C  
ATOM    876  C   HIS A 142       7.162  -5.749  10.520  1.00 50.71           C  
ANISOU  876  C   HIS A 142     6562   7005   5699   -423   1865    914       C  
ATOM    877  O   HIS A 142       8.360  -6.009  10.694  1.00 47.13           O  
ANISOU  877  O   HIS A 142     6246   6547   5116   -409   1783    909       O  
ATOM    878  CB  HIS A 142       6.200  -3.463  10.853  1.00 49.31           C  
ANISOU  878  CB  HIS A 142     6250   6905   5581   -304   2012    731       C  
ATOM    879  CG  HIS A 142       7.190  -3.134  11.923  1.00 54.36           C  
ANISOU  879  CG  HIS A 142     7039   7620   5997   -258   2049    676       C  
ATOM    880  CD2 HIS A 142       8.261  -2.306  11.921  1.00 54.37           C  
ANISOU  880  CD2 HIS A 142     7134   7619   5904   -194   1973    566       C  
ATOM    881  ND1 HIS A 142       7.154  -3.710  13.176  1.00 60.01           N  
ANISOU  881  ND1 HIS A 142     7821   8425   6553   -281   2171    741       N  
ATOM    882  CE1 HIS A 142       8.155  -3.246  13.900  1.00 59.21           C  
ANISOU  882  CE1 HIS A 142     7847   8383   6269   -232   2146    663       C  
ATOM    883  NE2 HIS A 142       8.845  -2.395  13.159  1.00 56.70           N  
ANISOU  883  NE2 HIS A 142     7548   8008   5989   -179   2041    557       N  
ATOM    884  N   GLU A 143       6.188  -6.567  10.913  1.00 47.97           N  
ANISOU  884  N   GLU A 143     6142   6672   5410   -490   1970   1022       N  
ATOM    885  CA  GLU A 143       6.499  -7.819  11.597  1.00 44.83           C  
ANISOU  885  CA  GLU A 143     5833   6280   4919   -550   1997   1149       C  
ATOM    886  C   GLU A 143       7.267  -8.810  10.727  1.00 44.02           C  
ANISOU  886  C   GLU A 143     5790   6070   4866   -595   1830   1197       C  
ATOM    887  O   GLU A 143       8.152  -9.512  11.213  1.00 38.93           O  
ANISOU  887  O   GLU A 143     5270   5420   4100   -604   1795   1257       O  
ATOM    888  CB  GLU A 143       5.241  -8.488  12.137  1.00 51.64           C  
ANISOU  888  CB  GLU A 143     6592   7170   5857   -620   2138   1254       C  
ATOM    889  CG  GLU A 143       5.538  -9.793  12.890  1.00 62.57           C  
ANISOU  889  CG  GLU A 143     8064   8556   7155   -686   2115   1369       C  
ATOM    890  CD  GLU A 143       6.292  -9.583  14.207  1.00 67.85           C  
ANISOU  890  CD  GLU A 143     8864   9333   7582   -644   2131   1346       C  
ATOM    891  OE1 GLU A 143       6.500  -8.412  14.604  1.00 69.54           O  
ANISOU  891  OE1 GLU A 143     9096   9628   7698   -567   2170   1230       O  
ATOM    892  OE2 GLU A 143       6.667 -10.594  14.849  1.00 66.22           O1-
ANISOU  892  OE2 GLU A 143     8738   9128   7292   -691   2102   1444       O1-
ATOM    893  N   ALA A 144       6.918  -8.873   9.446  1.00 44.23           N  
ANISOU  893  N   ALA A 144     5724   6012   5069   -624   1727   1170       N  
ATOM    894  CA  ALA A 144       7.632  -9.735   8.513  1.00 43.51           C  
ANISOU  894  CA  ALA A 144     5682   5818   5032   -664   1570   1190       C  
ATOM    895  C   ALA A 144       9.117  -9.417   8.550  1.00 45.29           C  
ANISOU  895  C   ALA A 144     6053   6044   5110   -601   1472   1125       C  
ATOM    896  O   ALA A 144       9.954 -10.310   8.480  1.00 50.50           O  
ANISOU  896  O   ALA A 144     6803   6649   5735   -624   1393   1171       O  
ATOM    897  CB  ALA A 144       7.097  -9.551   7.104  1.00 42.03           C  
ANISOU  897  CB  ALA A 144     5380   5564   5024   -688   1468   1138       C  
ATOM    898  N   LEU A 145       9.436  -8.134   8.676  1.00 43.20           N  
ANISOU  898  N   LEU A 145     5805   5836   4773   -522   1480   1016       N  
ATOM    899  CA  LEU A 145      10.821  -7.695   8.597  1.00 41.37           C  
ANISOU  899  CA  LEU A 145     5691   5601   4425   -464   1381    938       C  
ATOM    900  C   LEU A 145      11.647  -8.062   9.832  1.00 43.75           C  
ANISOU  900  C   LEU A 145     6123   5960   4539   -444   1418    981       C  
ATOM    901  O   LEU A 145      12.852  -8.271   9.732  1.00 48.84           O  
ANISOU  901  O   LEU A 145     6868   6578   5111   -423   1314    961       O  
ATOM    902  CB  LEU A 145      10.897  -6.195   8.300  1.00 38.82           C  
ANISOU  902  CB  LEU A 145     5339   5307   4102   -391   1374    808       C  
ATOM    903  CG  LEU A 145      11.204  -5.836   6.841  1.00 46.98           C  
ANISOU  903  CG  LEU A 145     6341   6265   5246   -387   1236    744       C  
ATOM    904  CD1 LEU A 145      10.270  -6.548   5.861  1.00 46.48           C  
ANISOU  904  CD1 LEU A 145     6170   6140   5351   -458   1198    802       C  
ATOM    905  CD2 LEU A 145      11.155  -4.328   6.634  1.00 50.03           C  
ANISOU  905  CD2 LEU A 145     6690   6674   5646   -316   1246    635       C  
ATOM    906  N   VAL A 146      11.010  -8.153  10.993  1.00 38.03           N  
ANISOU  906  N   VAL A 146     5395   5319   3734   -452   1562   1043       N  
ATOM    907  CA  VAL A 146      11.756  -8.526  12.198  1.00 45.54           C  
ANISOU  907  CA  VAL A 146     6475   6338   4491   -435   1592   1097       C  
ATOM    908  C   VAL A 146      11.521  -9.961  12.679  1.00 49.88           C  
ANISOU  908  C   VAL A 146     7034   6866   5053   -507   1598   1251       C  
ATOM    909  O   VAL A 146      12.167 -10.404  13.616  1.00 53.48           O  
ANISOU  909  O   VAL A 146     7570   7373   5376   -501   1563   1293       O  
ATOM    910  CB  VAL A 146      11.557  -7.515  13.363  1.00 66.05           C  
ANISOU  910  CB  VAL A 146     9074   9071   6950   -382   1687   1015       C  
ATOM    911  CG1 VAL A 146      12.427  -6.281  13.146  1.00 66.35           C  
ANISOU  911  CG1 VAL A 146     9163   9122   6923   -303   1632    864       C  
ATOM    912  CG2 VAL A 146      10.088  -7.135  13.520  1.00 61.95           C  
ANISOU  912  CG2 VAL A 146     8427   8591   6521   -401   1839   1017       C  
ATOM    913  N   SER A 147      10.626 -10.691  12.017  1.00 58.60           N  
ANISOU  913  N   SER A 147     8050   7891   6326   -578   1628   1331       N  
ATOM    914  CA  SER A 147      10.342 -12.081  12.392  1.00 66.43           C  
ANISOU  914  CA  SER A 147     9041   8841   7360   -656   1627   1472       C  
ATOM    915  C   SER A 147      10.963 -13.139  11.459  1.00 65.35           C  
ANISOU  915  C   SER A 147     8939   8560   7331   -695   1508   1529       C  
ATOM    916  O   SER A 147      11.712 -14.006  11.912  1.00 68.03           O  
ANISOU  916  O   SER A 147     9363   8871   7613   -703   1442   1601       O  
ATOM    917  CB  SER A 147       8.830 -12.315  12.518  1.00 67.16           C  
ANISOU  917  CB  SER A 147     9001   8944   7571   -723   1751   1527       C  
ATOM    918  OG  SER A 147       8.187 -12.240  11.255  1.00 66.98           O  
ANISOU  918  OG  SER A 147     8867   8835   7746   -754   1742   1508       O  
ATOM    919  N   GLY A 148      10.637 -13.085  10.170  1.00 55.59           N  
ANISOU  919  N   GLY A 148     7621   7238   6264   -720   1446   1472       N  
ATOM    920  CA  GLY A 148      11.140 -14.070   9.223  1.00 49.10           C  
ANISOU  920  CA  GLY A 148     6812   6284   5560   -762   1315   1487       C  
ATOM    921  C   GLY A 148      10.150 -15.165   8.841  1.00 50.22           C  
ANISOU  921  C   GLY A 148     6862   6336   5885   -864   1342   1582       C  
ATOM    922  O   GLY A 148      10.206 -15.715   7.731  1.00 54.71           O  
ANISOU  922  O   GLY A 148     7394   6798   6596   -906   1236   1546       O  
ATOM    923  N   GLN A 149       9.222 -15.465   9.746  1.00 40.75           N  
ANISOU  923  N   GLN A 149     5620   5182   4683   -907   1487   1695       N  
ATOM    924  CA  GLN A 149       8.372 -16.652   9.620  1.00 48.39           C  
ANISOU  924  CA  GLN A 149     6511   6062   5811  -1009   1504   1787       C  
ATOM    925  C   GLN A 149       7.365 -16.652   8.457  1.00 46.45           C  
ANISOU  925  C   GLN A 149     6112   5754   5781  -1072   1493   1749       C  
ATOM    926  O   GLN A 149       6.800 -17.695   8.128  1.00 42.63           O  
ANISOU  926  O   GLN A 149     5568   5175   5455  -1162   1479   1808       O  
ATOM    927  CB  GLN A 149       7.660 -16.949  10.943  1.00 57.07           C  
ANISOU  927  CB  GLN A 149     7607   7241   6836  -1038   1621   1866       C  
ATOM    928  CG  GLN A 149       6.694 -15.872  11.376  1.00 68.89           C  
ANISOU  928  CG  GLN A 149     9013   8865   8298  -1015   1748   1817       C  
ATOM    929  CD  GLN A 149       7.054 -15.292  12.728  1.00 80.84           C  
ANISOU  929  CD  GLN A 149    10615  10517   9583   -956   1816   1811       C  
ATOM    930  NE2 GLN A 149       6.074 -14.687  13.404  1.00 79.10           N  
ANISOU  930  NE2 GLN A 149    10319  10402   9332   -957   1950   1793       N  
ATOM    931  OE1 GLN A 149       8.202 -15.392  13.165  1.00 86.85           O  
ANISOU  931  OE1 GLN A 149    11507  11292  10200   -912   1745   1817       O  
ATOM    932  N   ILE A 150       7.129 -15.498   7.842  1.00 39.49           N  
ANISOU  932  N   ILE A 150     5169   4931   4906  -1024   1463   1620       N  
ATOM    933  CA  ILE A 150       6.298 -15.462   6.642  1.00 39.65           C  
ANISOU  933  CA  ILE A 150     5051   4901   5115  -1074   1400   1557       C  
ATOM    934  C   ILE A 150       6.999 -14.654   5.564  1.00 43.38           C  
ANISOU  934  C   ILE A 150     5548   5370   5564  -1014   1257   1412       C  
ATOM    935  O   ILE A 150       7.823 -13.786   5.866  1.00 47.97           O  
ANISOU  935  O   ILE A 150     6216   6013   5996   -926   1247   1352       O  
ATOM    936  CB  ILE A 150       4.887 -14.865   6.889  1.00 43.58           C  
ANISOU  936  CB  ILE A 150     5395   5471   5692  -1093   1524   1567       C  
ATOM    937  CG1 ILE A 150       4.966 -13.349   7.093  1.00 42.63           C  
ANISOU  937  CG1 ILE A 150     5273   5461   5462   -991   1559   1469       C  
ATOM    938  CG2 ILE A 150       4.181 -15.586   8.046  1.00 47.32           C  
ANISOU  938  CG2 ILE A 150     5843   5964   6173  -1153   1691   1716       C  
ATOM    939  CD1 ILE A 150       3.667 -12.609   6.805  1.00 41.45           C  
ANISOU  939  CD1 ILE A 150     4950   5357   5441   -995   1620   1433       C  
ATOM    940  N   PRO A 151       6.696 -14.949   4.297  1.00 40.86           N  
ANISOU  940  N   PRO A 151     5155   4978   5390  -1064   1145   1356       N  
ATOM    941  CA  PRO A 151       7.310 -14.140   3.242  1.00 36.05           C  
ANISOU  941  CA  PRO A 151     4568   4376   4751  -1009   1017   1228       C  
ATOM    942  C   PRO A 151       6.902 -12.677   3.373  1.00 30.27           C  
ANISOU  942  C   PRO A 151     3782   3747   3973   -936   1067   1170       C  
ATOM    943  O   PRO A 151       5.792 -12.386   3.810  1.00 31.33           O  
ANISOU  943  O   PRO A 151     3806   3929   4170   -950   1171   1209       O  
ATOM    944  CB  PRO A 151       6.733 -14.742   1.959  1.00 30.75           C  
ANISOU  944  CB  PRO A 151     3804   3630   4251  -1090    911   1192       C  
ATOM    945  CG  PRO A 151       6.352 -16.144   2.329  1.00 32.06           C  
ANISOU  945  CG  PRO A 151     3952   3710   4520  -1184    952   1292       C  
ATOM    946  CD  PRO A 151       5.903 -16.070   3.759  1.00 41.63           C  
ANISOU  946  CD  PRO A 151     5159   4983   5674  -1174   1121   1403       C  
ATOM    947  N   VAL A 152       7.809 -11.773   3.023  1.00 35.02           N  
ANISOU  947  N   VAL A 152     4457   4376   4473   -858    998   1080       N  
ATOM    948  CA  VAL A 152       7.481 -10.358   2.941  1.00 37.16           C  
ANISOU  948  CA  VAL A 152     4675   4720   4723   -788   1022   1015       C  
ATOM    949  C   VAL A 152       6.227 -10.157   2.089  1.00 31.04           C  
ANISOU  949  C   VAL A 152     3738   3941   4114   -827    995   1006       C  
ATOM    950  O   VAL A 152       6.223 -10.497   0.922  1.00 33.21           O  
ANISOU  950  O   VAL A 152     3986   4166   4465   -869    870    974       O  
ATOM    951  CB  VAL A 152       8.641  -9.572   2.340  1.00 36.85           C  
ANISOU  951  CB  VAL A 152     4727   4682   4591   -719    921    919       C  
ATOM    952  CG1 VAL A 152       8.192  -8.175   1.953  1.00 39.80           C  
ANISOU  952  CG1 VAL A 152     5027   5105   4991   -660    921    855       C  
ATOM    953  CG2 VAL A 152       9.797  -9.525   3.326  1.00 35.72           C  
ANISOU  953  CG2 VAL A 152     4724   4563   4285   -667    958    919       C  
ATOM    954  N   PRO A 153       5.147  -9.637   2.696  1.00 31.04           N  
ANISOU  954  N   PRO A 153     3628   3998   4170   -816   1114   1035       N  
ATOM    955  CA  PRO A 153       3.854  -9.493   2.004  1.00 31.05           C  
ANISOU  955  CA  PRO A 153     3455   3998   4345   -854   1095   1039       C  
ATOM    956  C   PRO A 153       3.917  -8.436   0.899  1.00 48.98           C  
ANISOU  956  C   PRO A 153     5690   6278   6642   -801    977    958       C  
ATOM    957  O   PRO A 153       4.031  -7.232   1.171  1.00 43.91           O  
ANISOU  957  O   PRO A 153     5052   5682   5951   -714   1017    915       O  
ATOM    958  CB  PRO A 153       2.906  -9.042   3.116  1.00 32.37           C  
ANISOU  958  CB  PRO A 153     3530   4231   4536   -832   1272   1081       C  
ATOM    959  CG  PRO A 153       3.818  -8.362   4.143  1.00 31.83           C  
ANISOU  959  CG  PRO A 153     3596   4218   4281   -747   1355   1052       C  
ATOM    960  CD  PRO A 153       5.106  -9.144   4.089  1.00 30.84           C  
ANISOU  960  CD  PRO A 153     3632   4045   4040   -764   1273   1060       C  
ATOM    961  N   LEU A 154       3.838  -8.903  -0.345  1.00 45.81           N  
ANISOU  961  N   LEU A 154     5256   5830   6318   -856    832    939       N  
ATOM    962  CA  LEU A 154       4.083  -8.064  -1.502  1.00 40.91           C  
ANISOU  962  CA  LEU A 154     4630   5216   5697   -816    700    873       C  
ATOM    963  C   LEU A 154       2.962  -7.065  -1.770  1.00 38.06           C  
ANISOU  963  C   LEU A 154     4113   4896   5452   -779    708    874       C  
ATOM    964  O   LEU A 154       3.200  -6.030  -2.380  1.00 35.60           O  
ANISOU  964  O   LEU A 154     3806   4600   5120   -715    640    833       O  
ATOM    965  CB  LEU A 154       4.347  -8.935  -2.733  1.00 46.62           C  
ANISOU  965  CB  LEU A 154     5375   5888   6451   -891    546    848       C  
ATOM    966  CG  LEU A 154       5.547  -9.882  -2.585  1.00 44.55           C  
ANISOU  966  CG  LEU A 154     5266   5574   6089   -918    527    836       C  
ATOM    967  CD1 LEU A 154       5.451 -11.049  -3.551  1.00 39.53           C  
ANISOU  967  CD1 LEU A 154     4615   4876   5528  -1015    415    820       C  
ATOM    968  CD2 LEU A 154       6.862  -9.138  -2.778  1.00 41.93           C  
ANISOU  968  CD2 LEU A 154     5067   5253   5610   -841    484    775       C  
ATOM    969  N   GLU A 155       1.747  -7.369  -1.317  1.00 36.36           N  
ANISOU  969  N   GLU A 155     3756   4694   5367   -818    793    926       N  
ATOM    970  CA  GLU A 155       0.631  -6.428  -1.452  1.00 38.34           C  
ANISOU  970  CA  GLU A 155     3840   4981   5745   -776    815    930       C  
ATOM    971  C   GLU A 155       0.835  -5.204  -0.571  1.00 40.31           C  
ANISOU  971  C   GLU A 155     4116   5272   5930   -667    935    902       C  
ATOM    972  O   GLU A 155       0.393  -4.113  -0.917  1.00 39.99           O  
ANISOU  972  O   GLU A 155     3989   5246   5958   -599    914    880       O  
ATOM    973  CB  GLU A 155      -0.700  -7.083  -1.083  1.00 43.26           C  
ANISOU  973  CB  GLU A 155     4297   5610   6531   -847    895    989       C  
ATOM    974  CG  GLU A 155      -0.998  -8.359  -1.834  1.00 50.18           C  
ANISOU  974  CG  GLU A 155     5135   6438   7492   -965    791   1011       C  
ATOM    975  CD  GLU A 155      -0.481  -9.599  -1.120  1.00 63.25           C  
ANISOU  975  CD  GLU A 155     6895   8052   9086  -1034    862   1050       C  
ATOM    976  OE1 GLU A 155       0.554  -9.510  -0.421  1.00 61.03           O  
ANISOU  976  OE1 GLU A 155     6769   7773   8645   -987    923   1045       O  
ATOM    977  OE2 GLU A 155      -1.123 -10.665  -1.252  1.00 72.44           O1-
ANISOU  977  OE2 GLU A 155     7979   9175  10369  -1137    855   1090       O1-
ATOM    978  N   SER A 156       1.494  -5.401   0.572  1.00 31.80           N  
ANISOU  978  N   SER A 156     3154   4208   4721   -650   1058    904       N  
ATOM    979  CA  SER A 156       1.794  -4.318   1.503  1.00 37.25           C  
ANISOU  979  CA  SER A 156     3887   4939   5327   -553   1176    862       C  
ATOM    980  C   SER A 156       2.931  -3.453   0.978  1.00 36.92           C  
ANISOU  980  C   SER A 156     3964   4881   5183   -483   1078    794       C  
ATOM    981  O   SER A 156       2.895  -2.229   1.096  1.00 35.87           O  
ANISOU  981  O   SER A 156     3806   4761   5061   -398   1108    747       O  
ATOM    982  CB  SER A 156       2.163  -4.869   2.882  1.00 32.04           C  
ANISOU  982  CB  SER A 156     3321   4311   4543   -564   1326    888       C  
ATOM    983  OG  SER A 156       1.075  -5.565   3.460  1.00 43.44           O  
ANISOU  983  OG  SER A 156     4650   5773   6081   -626   1441    958       O  
ATOM    984  N   VAL A 157       3.944  -4.097   0.408  1.00 29.11           N  
ANISOU  984  N   VAL A 157     3098   3858   4104   -521    967    787       N  
ATOM    985  CA  VAL A 157       5.048  -3.369  -0.200  1.00 31.95           C  
ANISOU  985  CA  VAL A 157     3565   4200   4375   -468    870    728       C  
ATOM    986  C   VAL A 157       4.524  -2.569  -1.382  1.00 36.32           C  
ANISOU  986  C   VAL A 157     4021   4742   5037   -444    761    720       C  
ATOM    987  O   VAL A 157       4.955  -1.443  -1.637  1.00 33.78           O  
ANISOU  987  O   VAL A 157     3727   4415   4693   -371    734    679       O  
ATOM    988  CB  VAL A 157       6.158  -4.315  -0.691  1.00 26.71           C  
ANISOU  988  CB  VAL A 157     3035   3501   3613   -520    772    722       C  
ATOM    989  CG1 VAL A 157       7.209  -3.546  -1.488  1.00 25.48           C  
ANISOU  989  CG1 VAL A 157     2968   3329   3385   -473    669    663       C  
ATOM    990  CG2 VAL A 157       6.796  -5.050   0.484  1.00 26.66           C  
ANISOU  990  CG2 VAL A 157     3135   3502   3494   -533    866    739       C  
ATOM    991  N   GLN A 158       3.575  -3.156  -2.098  1.00 28.62           N  
ANISOU  991  N   GLN A 158     2928   3762   4184   -508    695    763       N  
ATOM    992  CA  GLN A 158       3.057  -2.518  -3.291  1.00 33.98           C  
ANISOU  992  CA  GLN A 158     3515   4438   4960   -493    569    768       C  
ATOM    993  C   GLN A 158       2.314  -1.243  -2.916  1.00 35.45           C  
ANISOU  993  C   GLN A 158     3587   4637   5243   -405    642    766       C  
ATOM    994  O   GLN A 158       2.504  -0.213  -3.549  1.00 34.99           O  
ANISOU  994  O   GLN A 158     3527   4567   5199   -343    572    752       O  
ATOM    995  CB  GLN A 158       2.162  -3.475  -4.079  1.00 31.27           C  
ANISOU  995  CB  GLN A 158     3062   4091   4728   -586    478    808       C  
ATOM    996  CG  GLN A 158       1.461  -2.855  -5.269  1.00 37.25           C  
ANISOU  996  CG  GLN A 158     3704   4859   5590   -574    342    823       C  
ATOM    997  CD  GLN A 158       0.723  -3.891  -6.100  1.00 49.44           C  
ANISOU  997  CD  GLN A 158     5158   6405   7223   -676    232    847       C  
ATOM    998  NE2 GLN A 158      -0.585  -3.703  -6.273  1.00 49.67           N  
ANISOU  998  NE2 GLN A 158     5001   6452   7420   -683    217    884       N  
ATOM    999  OE1 GLN A 158       1.323  -4.859  -6.570  1.00 56.97           O  
ANISOU  999  OE1 GLN A 158     6204   7340   8103   -749    160    825       O  
ATOM   1000  N   ALA A 159       1.488  -1.310  -1.875  1.00 31.99           N  
ANISOU 1000  N   ALA A 159     3058   4222   4875   -397    791    780       N  
ATOM   1001  CA  ALA A 159       0.766  -0.125  -1.402  1.00 33.38           C  
ANISOU 1001  CA  ALA A 159     3121   4408   5153   -308    883    765       C  
ATOM   1002  C   ALA A 159       1.718   0.983  -0.938  1.00 30.87           C  
ANISOU 1002  C   ALA A 159     2917   4078   4733   -215    931    700       C  
ATOM   1003  O   ALA A 159       1.477   2.162  -1.169  1.00 31.20           O  
ANISOU 1003  O   ALA A 159     2898   4100   4856   -135    921    680       O  
ATOM   1004  CB  ALA A 159      -0.200  -0.497  -0.296  1.00 33.03           C  
ANISOU 1004  CB  ALA A 159     2970   4398   5182   -325   1053    785       C  
ATOM   1005  N   LEU A 160       2.806   0.603  -0.292  1.00 29.91           N  
ANISOU 1005  N   LEU A 160     2957   3964   4444   -226    976    666       N  
ATOM   1006  CA  LEU A 160       3.779   1.587   0.149  1.00 36.41           C  
ANISOU 1006  CA  LEU A 160     3891   4776   5168   -148   1012    595       C  
ATOM   1007  C   LEU A 160       4.485   2.255  -1.039  1.00 36.55           C  
ANISOU 1007  C   LEU A 160     3960   4749   5178   -123    861    585       C  
ATOM   1008  O   LEU A 160       4.694   3.471  -1.039  1.00 28.22           O  
ANISOU 1008  O   LEU A 160     2905   3667   4152    -44    871    544       O  
ATOM   1009  CB  LEU A 160       4.782   0.953   1.117  1.00 28.52           C  
ANISOU 1009  CB  LEU A 160     3046   3802   3989   -171   1083    566       C  
ATOM   1010  CG  LEU A 160       6.002   1.774   1.539  1.00 36.97           C  
ANISOU 1010  CG  LEU A 160     4251   4863   4935   -107   1097    486       C  
ATOM   1011  CD1 LEU A 160       5.597   3.096   2.172  1.00 28.49           C  
ANISOU 1011  CD1 LEU A 160     3115   3789   3921    -16   1202    422       C  
ATOM   1012  CD2 LEU A 160       6.860   0.962   2.494  1.00 36.60           C  
ANISOU 1012  CD2 LEU A 160     4339   4850   4718   -138   1154    475       C  
ATOM   1013  N   ASP A 161       4.848   1.457  -2.043  1.00 35.13           N  
ANISOU 1013  N   ASP A 161     3825   4561   4963   -192    726    620       N  
ATOM   1014  CA  ASP A 161       5.502   1.972  -3.250  1.00 31.95           C  
ANISOU 1014  CA  ASP A 161     3474   4128   4538   -181    583    621       C  
ATOM   1015  C   ASP A 161       4.606   2.956  -4.021  1.00 30.33           C  
ANISOU 1015  C   ASP A 161     3134   3905   4483   -132    521    658       C  
ATOM   1016  O   ASP A 161       5.043   4.032  -4.406  1.00 27.35           O  
ANISOU 1016  O   ASP A 161     2784   3494   4113    -71    484    646       O  
ATOM   1017  CB  ASP A 161       5.926   0.828  -4.177  1.00 31.29           C  
ANISOU 1017  CB  ASP A 161     3451   4048   4390   -270    461    644       C  
ATOM   1018  CG  ASP A 161       6.795   1.309  -5.346  1.00 37.73           C  
ANISOU 1018  CG  ASP A 161     4346   4844   5145   -263    331    637       C  
ATOM   1019  OD1 ASP A 161       7.814   1.994  -5.096  1.00 39.39           O  
ANISOU 1019  OD1 ASP A 161     4657   5033   5276   -215    357    593       O  
ATOM   1020  OD2 ASP A 161       6.462   1.005  -6.514  1.00 33.25           O1-
ANISOU 1020  OD2 ASP A 161     3740   4285   4607   -307    205    674       O1-
ATOM   1021  N   VAL A 162       3.354   2.569  -4.231  1.00 28.73           N  
ANISOU 1021  N   VAL A 162     2782   3722   4410   -161    507    708       N  
ATOM   1022  CA  VAL A 162       2.395   3.395  -4.949  1.00 38.25           C  
ANISOU 1022  CA  VAL A 162     3843   4915   5775   -116    438    754       C  
ATOM   1023  C   VAL A 162       2.235   4.758  -4.264  1.00 37.52           C  
ANISOU 1023  C   VAL A 162     3705   4788   5761     -6    542    721       C  
ATOM   1024  O   VAL A 162       2.181   5.795  -4.929  1.00 39.47           O  
ANISOU 1024  O   VAL A 162     3919   4997   6083     55    470    744       O  
ATOM   1025  CB  VAL A 162       1.037   2.657  -5.075  1.00 37.46           C  
ANISOU 1025  CB  VAL A 162     3575   4847   5811   -170    425    804       C  
ATOM   1026  CG1 VAL A 162      -0.024   3.528  -5.733  1.00 32.36           C  
ANISOU 1026  CG1 VAL A 162     2759   4190   5346   -115    354    856       C  
ATOM   1027  CG2 VAL A 162       1.219   1.385  -5.878  1.00 30.64           C  
ANISOU 1027  CG2 VAL A 162     2755   4004   4881   -279    306    826       C  
ATOM   1028  N   ALA A 163       2.188   4.742  -2.934  1.00 33.74           N  
ANISOU 1028  N   ALA A 163     3234   4322   5262     17    711    665       N  
ATOM   1029  CA  ALA A 163       2.041   5.956  -2.131  1.00 34.15           C  
ANISOU 1029  CA  ALA A 163     3248   4344   5382    118    832    609       C  
ATOM   1030  C   ALA A 163       3.228   6.906  -2.264  1.00 34.98           C  
ANISOU 1030  C   ALA A 163     3485   4399   5408    172    804    559       C  
ATOM   1031  O   ALA A 163       3.065   8.129  -2.320  1.00 30.86           O  
ANISOU 1031  O   ALA A 163     2911   3821   4992    257    817    542       O  
ATOM   1032  CB  ALA A 163       1.808   5.602  -0.669  1.00 31.73           C  
ANISOU 1032  CB  ALA A 163     2941   4081   5036    118   1021    554       C  
ATOM   1033  N   MET A 164       4.422   6.337  -2.311  1.00 30.12           N  
ANISOU 1033  N   MET A 164     3032   3796   4618    123    768    537       N  
ATOM   1034  CA  MET A 164       5.626   7.140  -2.324  1.00 30.55           C  
ANISOU 1034  CA  MET A 164     3211   3806   4590    163    754    482       C  
ATOM   1035  C   MET A 164       5.985   7.649  -3.715  1.00 28.61           C  
ANISOU 1035  C   MET A 164     2983   3517   4372    165    599    539       C  
ATOM   1036  O   MET A 164       6.780   8.574  -3.846  1.00 27.22           O  
ANISOU 1036  O   MET A 164     2876   3289   4180    210    588    508       O  
ATOM   1037  CB  MET A 164       6.784   6.352  -1.707  1.00 29.01           C  
ANISOU 1037  CB  MET A 164     3176   3644   4205    115    787    430       C  
ATOM   1038  CG  MET A 164       6.553   6.005  -0.239  1.00 27.36           C  
ANISOU 1038  CG  MET A 164     2970   3482   3946    121    947    376       C  
ATOM   1039  SD  MET A 164       8.012   5.340   0.577  1.00 35.77           S  
ANISOU 1039  SD  MET A 164     4224   4579   4789     87    978    315       S  
ATOM   1040  CE  MET A 164       8.934   6.838   0.851  1.00 27.49           C  
ANISOU 1040  CE  MET A 164     3242   3476   3728    170   1000    214       C  
ATOM   1041  N   ARG A 165       5.398   7.057  -4.751  1.00 29.90           N  
ANISOU 1041  N   ARG A 165     3083   3705   4574    114    480    623       N  
ATOM   1042  CA  ARG A 165       5.717   7.460  -6.120  1.00 29.09           C  
ANISOU 1042  CA  ARG A 165     3003   3578   4472    109    328    687       C  
ATOM   1043  C   ARG A 165       4.531   8.132  -6.812  1.00 29.61           C  
ANISOU 1043  C   ARG A 165     2910   3625   4716    153    258    768       C  
ATOM   1044  O   ARG A 165       4.560   8.386  -8.015  1.00 39.11           O  
ANISOU 1044  O   ARG A 165     4111   4823   5926    143    119    842       O  
ATOM   1045  CB  ARG A 165       6.222   6.264  -6.948  1.00 26.74           C  
ANISOU 1045  CB  ARG A 165     2787   3329   4044     11    220    712       C  
ATOM   1046  CG  ARG A 165       5.138   5.275  -7.376  1.00 33.47           C  
ANISOU 1046  CG  ARG A 165     3532   4230   4953    -53    159    764       C  
ATOM   1047  CD  ARG A 165       5.742   3.968  -7.918  1.00 26.61           C  
ANISOU 1047  CD  ARG A 165     2760   3402   3950   -152     84    755       C  
ATOM   1048  NE  ARG A 165       6.767   4.243  -8.916  1.00 25.84           N  
ANISOU 1048  NE  ARG A 165     2776   3297   3747   -163    -15    761       N  
ATOM   1049  CZ  ARG A 165       8.052   3.961  -8.766  1.00 24.65           C  
ANISOU 1049  CZ  ARG A 165     2771   3138   3457   -183      8    706       C  
ATOM   1050  NH1 ARG A 165       8.476   3.354  -7.663  1.00 26.58           N1+
ANISOU 1050  NH1 ARG A 165     3070   3382   3646   -194    114    647       N1+
ATOM   1051  NH2 ARG A 165       8.911   4.273  -9.721  1.00 25.76           N  
ANISOU 1051  NH2 ARG A 165     2999   3275   3515   -193    -75    716       N  
ATOM   1052  N   HIS A 166       3.496   8.426  -6.044  1.00 30.12           N  
ANISOU 1052  N   HIS A 166     2839   3682   4922    202    355    755       N  
ATOM   1053  CA  HIS A 166       2.272   8.998  -6.588  1.00 31.61           C  
ANISOU 1053  CA  HIS A 166     2854   3853   5303    249    296    830       C  
ATOM   1054  C   HIS A 166       2.451  10.423  -7.115  1.00 32.09           C  
ANISOU 1054  C   HIS A 166     2904   3832   5457    336    246    867       C  
ATOM   1055  O   HIS A 166       1.997  10.751  -8.217  1.00 32.81           O  
ANISOU 1055  O   HIS A 166     2927   3915   5623    346    105    967       O  
ATOM   1056  CB  HIS A 166       1.170   8.971  -5.531  1.00 32.79           C  
ANISOU 1056  CB  HIS A 166     2859   4013   5588    284    436    795       C  
ATOM   1057  CG  HIS A 166      -0.099   9.626  -5.970  1.00 38.97           C  
ANISOU 1057  CG  HIS A 166     3445   4770   6592    345    389    863       C  
ATOM   1058  CD2 HIS A 166      -0.584  10.869  -5.741  1.00 35.64           C  
ANISOU 1058  CD2 HIS A 166     2921   4276   6343    453    437    859       C  
ATOM   1059  ND1 HIS A 166      -1.032   8.984  -6.754  1.00 35.27           N  
ANISOU 1059  ND1 HIS A 166     2854   4348   6198    295    272    944       N  
ATOM   1060  CE1 HIS A 166      -2.045   9.802  -6.980  1.00 38.90           C  
ANISOU 1060  CE1 HIS A 166     3142   4772   6866    372    247    994       C  
ATOM   1061  NE2 HIS A 166      -1.799  10.949  -6.375  1.00 38.77           N  
ANISOU 1061  NE2 HIS A 166     3134   4679   6918    471    349    945       N  
ATOM   1062  N   LEU A 167       3.101  11.268  -6.321  1.00 35.41           N  
ANISOU 1062  N   LEU A 167     3390   4191   5875    399    358    788       N  
ATOM   1063  CA  LEU A 167       3.375  12.641  -6.729  1.00 36.88           C  
ANISOU 1063  CA  LEU A 167     3575   4280   6156    479    325    815       C  
ATOM   1064  C   LEU A 167       4.307  12.679  -7.944  1.00 36.83           C  
ANISOU 1064  C   LEU A 167     3688   4270   6034    435    180    887       C  
ATOM   1065  O   LEU A 167       4.025  13.374  -8.918  1.00 41.29           O  
ANISOU 1065  O   LEU A 167     4204   4796   6689    468     68    991       O  
ATOM   1066  CB  LEU A 167       3.971  13.447  -5.571  1.00 35.39           C  
ANISOU 1066  CB  LEU A 167     3443   4027   5978    542    479    693       C  
ATOM   1067  CG  LEU A 167       3.470  14.886  -5.393  1.00 40.39           C  
ANISOU 1067  CG  LEU A 167     3973   4550   6825    656    524    688       C  
ATOM   1068  CD1 LEU A 167       4.471  15.728  -4.605  1.00 39.91           C  
ANISOU 1068  CD1 LEU A 167     4017   4414   6734    699    628    570       C  
ATOM   1069  CD2 LEU A 167       3.129  15.562  -6.716  1.00 35.25           C  
ANISOU 1069  CD2 LEU A 167     3258   3842   6293    687    367    831       C  
ATOM   1070  N   ALA A 168       5.409  11.929  -7.881  1.00 37.29           N  
ANISOU 1070  N   ALA A 168     3900   4372   5896    362    185    837       N  
ATOM   1071  CA  ALA A 168       6.339  11.803  -9.013  1.00 29.15           C  
ANISOU 1071  CA  ALA A 168     2986   3353   4736    309     63    894       C  
ATOM   1072  C   ALA A 168       5.616  11.406 -10.295  1.00 36.26           C  
ANISOU 1072  C   ALA A 168     3820   4307   5652    270    -98   1013       C  
ATOM   1073  O   ALA A 168       5.959  11.874 -11.385  1.00 35.58           O  
ANISOU 1073  O   ALA A 168     3773   4208   5538    266   -210   1099       O  
ATOM   1074  CB  ALA A 168       7.424  10.784  -8.704  1.00 27.61           C  
ANISOU 1074  CB  ALA A 168     2937   3211   4342    231     94    816       C  
ATOM   1075  N   SER A 169       4.614  10.542 -10.154  1.00 30.32           N  
ANISOU 1075  N   SER A 169     2965   3617   4940    237   -108   1019       N  
ATOM   1076  CA  SER A 169       3.890  10.004 -11.298  1.00 36.30           C  
ANISOU 1076  CA  SER A 169     3652   4437   5703    188   -265   1114       C  
ATOM   1077  C   SER A 169       3.027  11.053 -11.980  1.00 41.07           C  
ANISOU 1077  C   SER A 169     4128   5001   6476    262   -357   1226       C  
ATOM   1078  O   SER A 169       2.643  10.886 -13.139  1.00 41.95           O  
ANISOU 1078  O   SER A 169     4207   5160   6572    230   -516   1322       O  
ATOM   1079  CB  SER A 169       3.035   8.812 -10.884  1.00 35.58           C  
ANISOU 1079  CB  SER A 169     3474   4413   5631    131   -244   1084       C  
ATOM   1080  OG  SER A 169       3.844   7.680 -10.623  1.00 34.13           O  
ANISOU 1080  OG  SER A 169     3416   4273   5278     47   -210   1012       O  
ATOM   1081  N   MET A 170       2.736  12.134 -11.262  1.00 41.06           N  
ANISOU 1081  N   MET A 170     4056   4911   6634    361   -261   1211       N  
ATOM   1082  CA  MET A 170       1.978  13.244 -11.825  1.00 42.82           C  
ANISOU 1082  CA  MET A 170     4156   5072   7041    446   -338   1318       C  
ATOM   1083  C   MET A 170       2.905  14.328 -12.369  1.00 42.52           C  
ANISOU 1083  C   MET A 170     4221   4953   6979    486   -373   1371       C  
ATOM   1084  O   MET A 170       2.584  15.000 -13.334  1.00 45.96           O  
ANISOU 1084  O   MET A 170     4611   5364   7487    520   -498   1500       O  
ATOM   1085  CB  MET A 170       1.052  13.851 -10.773  1.00 36.02           C  
ANISOU 1085  CB  MET A 170     3141   4147   6397    539   -211   1271       C  
ATOM   1086  CG  MET A 170       0.100  12.860 -10.117  1.00 60.05           C  
ANISOU 1086  CG  MET A 170     6070   7263   9483    504   -149   1220       C  
ATOM   1087  SD  MET A 170      -1.189  12.251 -11.225  1.00 84.23           S  
ANISOU 1087  SD  MET A 170     8967  10405  12630    464   -337   1342       S  
ATOM   1088  CE  MET A 170      -1.984  11.032 -10.181  1.00 95.89           C  
ANISOU 1088  CE  MET A 170    10347  11951  14135    406   -212   1251       C  
ATOM   1089  N   ARG A 171       4.055  14.498 -11.735  1.00 44.38           N  
ANISOU 1089  N   ARG A 171     4594   5149   7119    480   -263   1275       N  
ATOM   1090  CA  ARG A 171       4.966  15.574 -12.097  1.00 42.95           C  
ANISOU 1090  CA  ARG A 171     4504   4877   6937    516   -270   1311       C  
ATOM   1091  C   ARG A 171       5.876  15.194 -13.260  1.00 44.20           C  
ANISOU 1091  C   ARG A 171     4799   5093   6901    434   -386   1380       C  
ATOM   1092  O   ARG A 171       6.343  16.058 -13.997  1.00 43.87           O  
ANISOU 1092  O   ARG A 171     4804   4995   6870    455   -444   1471       O  
ATOM   1093  CB  ARG A 171       5.824  15.962 -10.890  1.00 39.58           C  
ANISOU 1093  CB  ARG A 171     4158   4382   6500    542   -104   1168       C  
ATOM   1094  CG  ARG A 171       5.029  16.436  -9.692  1.00 47.35           C  
ANISOU 1094  CG  ARG A 171     5022   5308   7662    625     29   1082       C  
ATOM   1095  CD  ARG A 171       5.160  17.935  -9.490  1.00 59.84           C  
ANISOU 1095  CD  ARG A 171     6576   6743   9418    723     77   1083       C  
ATOM   1096  NE  ARG A 171       5.155  18.303  -8.074  1.00 66.57           N  
ANISOU 1096  NE  ARG A 171     7408   7543  10343    777    251    926       N  
ATOM   1097  CZ  ARG A 171       6.190  18.129  -7.254  1.00 69.49           C  
ANISOU 1097  CZ  ARG A 171     7904   7919  10581    746    352    793       C  
ATOM   1098  NH1 ARG A 171       7.316  17.575  -7.700  1.00 67.38           N1+
ANISOU 1098  NH1 ARG A 171     7785   7701  10118    663    300    799       N1+
ATOM   1099  NH2 ARG A 171       6.099  18.500  -5.984  1.00 71.06           N  
ANISOU 1099  NH2 ARG A 171     8078   8079  10842    798    504    651       N  
ATOM   1100  N   TYR A 172       6.141  13.902 -13.418  1.00 43.03           N  
ANISOU 1100  N   TYR A 172     4717   5055   6579    340   -411   1335       N  
ATOM   1101  CA  TYR A 172       7.118  13.470 -14.399  1.00 30.90           C  
ANISOU 1101  CA  TYR A 172     3318   3576   4844    260   -493   1368       C  
ATOM   1102  C   TYR A 172       6.591  12.373 -15.292  1.00 34.15           C  
ANISOU 1102  C   TYR A 172     3711   4109   5156    182   -624   1414       C  
ATOM   1103  O   TYR A 172       5.498  11.848 -15.087  1.00 36.31           O  
ANISOU 1103  O   TYR A 172     3863   4422   5512    181   -648   1413       O  
ATOM   1104  CB  TYR A 172       8.386  12.965 -13.714  1.00 31.93           C  
ANISOU 1104  CB  TYR A 172     3591   3711   4832    214   -384   1238       C  
ATOM   1105  CG  TYR A 172       8.971  13.908 -12.684  1.00 36.67           C  
ANISOU 1105  CG  TYR A 172     4216   4202   5514    280   -249   1160       C  
ATOM   1106  CD1 TYR A 172       9.395  15.185 -13.041  1.00 42.46           C  
ANISOU 1106  CD1 TYR A 172     4969   4837   6327    331   -256   1222       C  
ATOM   1107  CD2 TYR A 172       9.118  13.516 -11.360  1.00 31.12           C  
ANISOU 1107  CD2 TYR A 172     3521   3495   4807    287   -117   1024       C  
ATOM   1108  CE1 TYR A 172       9.943  16.043 -12.110  1.00 45.32           C  
ANISOU 1108  CE1 TYR A 172     5353   5095   6771    386   -137   1137       C  
ATOM   1109  CE2 TYR A 172       9.665  14.370 -10.420  1.00 38.49           C  
ANISOU 1109  CE2 TYR A 172     4481   4339   5804    344     -1    939       C  
ATOM   1110  CZ  TYR A 172      10.077  15.631 -10.801  1.00 50.08           C  
ANISOU 1110  CZ  TYR A 172     5965   5705   7360    391    -12    989       C  
ATOM   1111  OH  TYR A 172      10.616  16.487  -9.868  1.00 60.23           O  
ANISOU 1111  OH  TYR A 172     7272   6894   8717    443    100    892       O  
ATOM   1112  N   THR A 173       7.404  12.012 -16.275  1.00 31.16           N  
ANISOU 1112  N   THR A 173     3452   3789   4599    112   -702   1444       N  
ATOM   1113  CA  THR A 173       7.086  10.923 -17.177  1.00 32.55           C  
ANISOU 1113  CA  THR A 173     3634   4084   4651     27   -825   1464       C  
ATOM   1114  C   THR A 173       7.642   9.624 -16.615  1.00 30.09           C  
ANISOU 1114  C   THR A 173     3398   3819   4216    -48   -753   1327       C  
ATOM   1115  O   THR A 173       8.858   9.463 -16.525  1.00 28.26           O  
ANISOU 1115  O   THR A 173     3299   3580   3860    -79   -692   1264       O  
ATOM   1116  CB  THR A 173       7.735  11.151 -18.536  1.00 32.33           C  
ANISOU 1116  CB  THR A 173     3707   4103   4474    -15   -935   1555       C  
ATOM   1117  CG2 THR A 173       7.362  10.039 -19.489  1.00 31.59           C  
ANISOU 1117  CG2 THR A 173     3617   4137   4248   -103  -1067   1563       C  
ATOM   1118  OG1 THR A 173       7.315  12.419 -19.056  1.00 42.63           O  
ANISOU 1118  OG1 THR A 173     4953   5353   5893     58  -1001   1700       O  
ATOM   1119  N   PRO A 174       6.754   8.693 -16.232  1.00 30.10           N  
ANISOU 1119  N   PRO A 174     3309   3864   4263    -78   -759   1285       N  
ATOM   1120  CA  PRO A 174       7.192   7.415 -15.659  1.00 32.11           C  
ANISOU 1120  CA  PRO A 174     3626   4153   4421   -148   -692   1167       C  
ATOM   1121  C   PRO A 174       7.671   6.419 -16.716  1.00 32.71           C  
ANISOU 1121  C   PRO A 174     3791   4315   4321   -246   -793   1151       C  
ATOM   1122  O   PRO A 174       7.038   6.256 -17.751  1.00 31.52           O  
ANISOU 1122  O   PRO A 174     3595   4229   4151   -279   -932   1217       O  
ATOM   1123  CB  PRO A 174       5.922   6.881 -14.970  1.00 35.73           C  
ANISOU 1123  CB  PRO A 174     3937   4622   5017   -145   -669   1151       C  
ATOM   1124  CG  PRO A 174       4.942   8.029 -14.961  1.00 34.29           C  
ANISOU 1124  CG  PRO A 174     3615   4395   5017    -56   -692   1242       C  
ATOM   1125  CD  PRO A 174       5.296   8.865 -16.141  1.00 31.40           C  
ANISOU 1125  CD  PRO A 174     3297   4031   4602    -39   -807   1344       C  
ATOM   1126  N   VAL A 175       8.787   5.755 -16.442  1.00 31.66           N  
ANISOU 1126  N   VAL A 175     3784   4183   4062   -291   -724   1057       N  
ATOM   1127  CA  VAL A 175       9.352   4.766 -17.351  1.00 26.64           C  
ANISOU 1127  CA  VAL A 175     3240   3619   3262   -381   -797   1017       C  
ATOM   1128  C   VAL A 175       9.948   3.603 -16.547  1.00 40.72           C  
ANISOU 1128  C   VAL A 175     5085   5392   4996   -426   -706    897       C  
ATOM   1129  O   VAL A 175      11.007   3.747 -15.926  1.00 38.76           O  
ANISOU 1129  O   VAL A 175     4925   5098   4702   -406   -605    841       O  
ATOM   1130  CB  VAL A 175      10.459   5.386 -18.204  1.00 37.84           C  
ANISOU 1130  CB  VAL A 175     4778   5047   4552   -383   -819   1047       C  
ATOM   1131  CG1 VAL A 175      11.160   4.311 -19.001  1.00 45.15           C  
ANISOU 1131  CG1 VAL A 175     5805   6044   5306   -474   -865    979       C  
ATOM   1132  CG2 VAL A 175       9.894   6.462 -19.129  1.00 33.82           C  
ANISOU 1132  CG2 VAL A 175     4219   4553   4077   -346   -924   1185       C  
ATOM   1133  N   GLY A 176       9.283   2.448 -16.556  1.00 25.77           N  
ANISOU 1133  N   GLY A 176     3141   3535   3117   -488   -744    859       N  
ATOM   1134  CA  GLY A 176       9.690   1.369 -15.676  1.00 24.89           C  
ANISOU 1134  CA  GLY A 176     3070   3398   2990   -523   -654    764       C  
ATOM   1135  C   GLY A 176       9.594   1.899 -14.257  1.00 27.27           C  
ANISOU 1135  C   GLY A 176     3334   3635   3392   -452   -520    759       C  
ATOM   1136  O   GLY A 176       8.601   2.531 -13.909  1.00 29.51           O  
ANISOU 1136  O   GLY A 176     3503   3906   3804   -403   -511    814       O  
ATOM   1137  N   ARG A 177      10.627   1.698 -13.450  1.00 28.70           N  
ANISOU 1137  N   ARG A 177     3610   3779   3517   -441   -418    692       N  
ATOM   1138  CA  ARG A 177      10.594   2.225 -12.092  1.00 26.20           C  
ANISOU 1138  CA  ARG A 177     3269   3412   3273   -375   -291    678       C  
ATOM   1139  C   ARG A 177      11.264   3.599 -11.992  1.00 29.02           C  
ANISOU 1139  C   ARG A 177     3667   3729   3630   -302   -253    692       C  
ATOM   1140  O   ARG A 177      11.589   4.067 -10.902  1.00 31.74           O  
ANISOU 1140  O   ARG A 177     4026   4032   4002   -250   -147    655       O  
ATOM   1141  CB  ARG A 177      11.190   1.220 -11.099  1.00 30.46           C  
ANISOU 1141  CB  ARG A 177     3872   3937   3765   -401   -203    604       C  
ATOM   1142  CG  ARG A 177      10.399  -0.100 -11.024  1.00 43.54           C  
ANISOU 1142  CG  ARG A 177     5472   5614   5456   -471   -224    598       C  
ATOM   1143  CD  ARG A 177      10.718  -0.941  -9.778  1.00 57.30           C  
ANISOU 1143  CD  ARG A 177     7251   7331   7187   -481   -117    554       C  
ATOM   1144  NE  ARG A 177      10.116  -0.398  -8.556  1.00 68.16           N  
ANISOU 1144  NE  ARG A 177     8561   8693   8642   -424     -7    572       N  
ATOM   1145  CZ  ARG A 177       9.905  -1.098  -7.438  1.00 68.78           C  
ANISOU 1145  CZ  ARG A 177     8631   8765   8735   -436     86    562       C  
ATOM   1146  NH1 ARG A 177      10.237  -2.383  -7.381  1.00 68.39           N1+
ANISOU 1146  NH1 ARG A 177     8632   8709   8643   -501     78    542       N1+
ATOM   1147  NH2 ARG A 177       9.354  -0.514  -6.374  1.00 60.11           N  
ANISOU 1147  NH2 ARG A 177     7475   7667   7697   -382    193    572       N  
ATOM   1148  N   SER A 178      11.459   4.247 -13.136  1.00 28.98           N  
ANISOU 1148  N   SER A 178     3681   3737   3592   -301   -340    746       N  
ATOM   1149  CA  SER A 178      12.123   5.549 -13.161  1.00 29.23           C  
ANISOU 1149  CA  SER A 178     3753   3720   3632   -241   -310    769       C  
ATOM   1150  C   SER A 178      11.211   6.687 -13.617  1.00 24.05           C  
ANISOU 1150  C   SER A 178     3000   3044   3093   -185   -362    870       C  
ATOM   1151  O   SER A 178      10.089   6.447 -14.056  1.00 24.99           O  
ANISOU 1151  O   SER A 178     3021   3200   3273   -197   -439    926       O  
ATOM   1152  CB  SER A 178      13.385   5.484 -14.014  1.00 22.30           C  
ANISOU 1152  CB  SER A 178     2998   2859   2617   -281   -343    753       C  
ATOM   1153  OG  SER A 178      14.292   4.560 -13.447  1.00 28.77           O  
ANISOU 1153  OG  SER A 178     3898   3679   3353   -315   -284    656       O  
ATOM   1154  N   PHE A 179      11.697   7.920 -13.476  1.00 24.07           N  
ANISOU 1154  N   PHE A 179     3025   2983   3139   -124   -321    891       N  
ATOM   1155  CA  PHE A 179      10.945   9.124 -13.831  1.00 25.25           C  
ANISOU 1155  CA  PHE A 179     3086   3089   3418    -59   -361    990       C  
ATOM   1156  C   PHE A 179      11.800  10.085 -14.672  1.00 27.20           C  
ANISOU 1156  C   PHE A 179     3408   3303   3622    -49   -396   1053       C  
ATOM   1157  O   PHE A 179      12.970  10.307 -14.374  1.00 27.53           O  
ANISOU 1157  O   PHE A 179     3547   3310   3605    -53   -327    994       O  
ATOM   1158  CB  PHE A 179      10.474   9.844 -12.572  1.00 25.49           C  
ANISOU 1158  CB  PHE A 179     3039   3046   3599     22   -250    953       C  
ATOM   1159  CG  PHE A 179       9.449   9.081 -11.790  1.00 25.73           C  
ANISOU 1159  CG  PHE A 179     2974   3109   3694     19   -210    917       C  
ATOM   1160  CD1 PHE A 179       8.114   9.121 -12.158  1.00 26.96           C  
ANISOU 1160  CD1 PHE A 179     2992   3285   3966     35   -278    993       C  
ATOM   1161  CD2 PHE A 179       9.818   8.323 -10.685  1.00 24.85           C  
ANISOU 1161  CD2 PHE A 179     2905   3009   3529      0   -106    815       C  
ATOM   1162  CE1 PHE A 179       7.158   8.421 -11.448  1.00 33.84           C  
ANISOU 1162  CE1 PHE A 179     3766   4185   4907     27   -233    963       C  
ATOM   1163  CE2 PHE A 179       8.869   7.615  -9.976  1.00 27.65           C  
ANISOU 1163  CE2 PHE A 179     3172   3393   3940     -9    -60    794       C  
ATOM   1164  CZ  PHE A 179       7.532   7.664 -10.357  1.00 26.43           C  
ANISOU 1164  CZ  PHE A 179     2876   3257   3911      2   -119    865       C  
ATOM   1165  N   PHE A 180      11.222  10.658 -15.721  1.00 26.55           N  
ANISOU 1165  N   PHE A 180     3281   3233   3575    -37   -504   1177       N  
ATOM   1166  CA  PHE A 180      11.968  11.603 -16.543  1.00 26.89           C  
ANISOU 1166  CA  PHE A 180     3392   3243   3583    -29   -535   1258       C  
ATOM   1167  C   PHE A 180      11.161  12.841 -16.831  1.00 28.33           C  
ANISOU 1167  C   PHE A 180     3481   3359   3926     47   -582   1384       C  
ATOM   1168  O   PHE A 180       9.936  12.833 -16.745  1.00 33.51           O  
ANISOU 1168  O   PHE A 180     4013   4023   4696     82   -629   1427       O  
ATOM   1169  CB  PHE A 180      12.435  10.947 -17.854  1.00 26.95           C  
ANISOU 1169  CB  PHE A 180     3484   3350   3404   -114   -633   1297       C  
ATOM   1170  CG  PHE A 180      13.338   9.776 -17.645  1.00 25.64           C  
ANISOU 1170  CG  PHE A 180     3414   3235   3092   -184   -585   1172       C  
ATOM   1171  CD1 PHE A 180      14.711   9.951 -17.559  1.00 24.77           C  
ANISOU 1171  CD1 PHE A 180     3412   3096   2902   -201   -511   1118       C  
ATOM   1172  CD2 PHE A 180      12.815   8.503 -17.494  1.00 25.36           C  
ANISOU 1172  CD2 PHE A 180     3352   3268   3017   -232   -612   1108       C  
ATOM   1173  CE1 PHE A 180      15.551   8.867 -17.337  1.00 24.98           C  
ANISOU 1173  CE1 PHE A 180     3517   3162   2809   -258   -468   1002       C  
ATOM   1174  CE2 PHE A 180      13.644   7.415 -17.272  1.00 29.96           C  
ANISOU 1174  CE2 PHE A 180     4018   3883   3484   -291   -568    995       C  
ATOM   1175  CZ  PHE A 180      15.014   7.596 -17.181  1.00 23.40           C  
ANISOU 1175  CZ  PHE A 180     3293   3024   2574   -300   -496    942       C  
ATOM   1176  N   SER A 181      11.856  13.916 -17.167  1.00 30.58           N  
ANISOU 1176  N   SER A 181     4216   3872   3532    443    356    239       N  
ATOM   1177  CA  SER A 181      11.186  15.102 -17.681  1.00 34.72           C  
ANISOU 1177  CA  SER A 181     4775   4399   4017    522    323    221       C  
ATOM   1178  C   SER A 181      11.962  15.608 -18.882  1.00 26.85           C  
ANISOU 1178  C   SER A 181     3866   3278   3057    453    297    193       C  
ATOM   1179  O   SER A 181      13.172  15.385 -18.979  1.00 19.90           O  
ANISOU 1179  O   SER A 181     3023   2324   2216    380    302    173       O  
ATOM   1180  CB  SER A 181      11.064  16.186 -16.604  1.00 41.67           C  
ANISOU 1180  CB  SER A 181     5692   5300   4840    670    292    182       C  
ATOM   1181  OG  SER A 181      12.334  16.570 -16.125  1.00 45.93           O  
ANISOU 1181  OG  SER A 181     6313   5731   5407    658    277    140       O  
ATOM   1182  N   PRO A 182      11.262  16.280 -19.807  1.00 29.99           N  
ANISOU 1182  N   PRO A 182     4291   3670   3433    476    267    195       N  
ATOM   1183  CA  PRO A 182      11.917  16.770 -21.021  1.00 27.43           C  
ANISOU 1183  CA  PRO A 182     4044   3242   3134    398    238    181       C  
ATOM   1184  C   PRO A 182      13.067  17.703 -20.673  1.00 25.17           C  
ANISOU 1184  C   PRO A 182     3863   2856   2843    390    196    145       C  
ATOM   1185  O   PRO A 182      12.993  18.402 -19.668  1.00 27.80           O  
ANISOU 1185  O   PRO A 182     4241   3181   3142    490    164    121       O  
ATOM   1186  CB  PRO A 182      10.798  17.511 -21.779  1.00 28.67           C  
ANISOU 1186  CB  PRO A 182     4224   3416   3252    460    202    185       C  
ATOM   1187  CG  PRO A 182       9.628  17.553 -20.868  1.00 29.12           C  
ANISOU 1187  CG  PRO A 182     4217   3597   3251    591    206    189       C  
ATOM   1188  CD  PRO A 182       9.806  16.505 -19.816  1.00 32.85           C  
ANISOU 1188  CD  PRO A 182     4598   4144   3739    569    259    214       C  
ATOM   1189  N   PRO A 183      14.134  17.665 -21.477  1.00 24.94           N  
ANISOU 1189  N   PRO A 183     3866   2769   2840    272    193    143       N  
ATOM   1190  CA  PRO A 183      15.347  18.471 -21.319  1.00 27.68           C  
ANISOU 1190  CA  PRO A 183     4302   3039   3176    219    150    124       C  
ATOM   1191  C   PRO A 183      15.045  19.941 -21.057  1.00 31.22           C  
ANISOU 1191  C   PRO A 183     4879   3406   3577    291     59    111       C  
ATOM   1192  O   PRO A 183      14.374  20.588 -21.858  1.00 29.11           O  
ANISOU 1192  O   PRO A 183     4669   3105   3286    307     10    120       O  
ATOM   1193  CB  PRO A 183      16.025  18.345 -22.686  1.00 20.17           C  
ANISOU 1193  CB  PRO A 183     3349   2080   2233     84    150    140       C  
ATOM   1194  CG  PRO A 183      15.571  17.007 -23.201  1.00 23.25           C  
ANISOU 1194  CG  PRO A 183     3632   2544   2658     72    212    151       C  
ATOM   1195  CD  PRO A 183      14.171  16.831 -22.695  1.00 23.84           C  
ANISOU 1195  CD  PRO A 183     3672   2654   2731    178    224    164       C  
ATOM   1196  N   GLU A 184      15.554  20.445 -19.941  1.00 30.27           N  
ANISOU 1196  N   GLU A 184     4814   3246   3440    340     26     86       N  
ATOM   1197  CA  GLU A 184      15.482  21.850 -19.596  1.00 34.30           C  
ANISOU 1197  CA  GLU A 184     5477   3656   3900    408    -87     66       C  
ATOM   1198  C   GLU A 184      16.845  22.153 -19.021  1.00 36.77           C  
ANISOU 1198  C   GLU A 184     5845   3912   4216    325   -115     59       C  
ATOM   1199  O   GLU A 184      17.269  21.508 -18.059  1.00 34.37           O  
ANISOU 1199  O   GLU A 184     5470   3657   3934    352    -57     41       O  
ATOM   1200  CB  GLU A 184      14.451  22.066 -18.499  1.00 49.45           C  
ANISOU 1200  CB  GLU A 184     7389   5618   5780    608   -103     32       C  
ATOM   1201  CG  GLU A 184      13.556  23.257 -18.697  1.00 63.19           C  
ANISOU 1201  CG  GLU A 184     9254   7301   7453    736   -215      7       C  
ATOM   1202  CD  GLU A 184      12.182  22.834 -19.157  1.00 77.00           C  
ANISOU 1202  CD  GLU A 184    10908   9165   9182    824   -172     13       C  
ATOM   1203  OE1 GLU A 184      11.265  22.777 -18.306  1.00 79.54           O  
ANISOU 1203  OE1 GLU A 184    11171   9596   9455    992   -165    -13       O  
ATOM   1204  OE2 GLU A 184      12.026  22.541 -20.366  1.00 80.58           O1-
ANISOU 1204  OE2 GLU A 184    11335   9617   9662    723   -146     45       O1-
ATOM   1205  N   GLY A 185      17.540  23.123 -19.601  1.00 33.74           N  
ANISOU 1205  N   GLY A 185     5587   3429   3804    216   -207     78       N  
ATOM   1206  CA  GLY A 185      18.871  23.464 -19.133  1.00 22.69           C  
ANISOU 1206  CA  GLY A 185     4236   1988   2395    111   -243     82       C  
ATOM   1207  C   GLY A 185      19.941  22.505 -19.623  1.00 25.39           C  
ANISOU 1207  C   GLY A 185     4452   2432   2763    -42   -151    101       C  
ATOM   1208  O   GLY A 185      21.051  22.516 -19.104  1.00 31.51           O  
ANISOU 1208  O   GLY A 185     5224   3220   3530   -114   -153     97       O  
ATOM   1209  N   TYR A 186      19.607  21.659 -20.600  1.00 26.18           N  
ANISOU 1209  N   TYR A 186     4448   2612   2887    -77    -77    116       N  
ATOM   1210  CA  TYR A 186      20.591  20.769 -21.225  1.00 23.82           C  
ANISOU 1210  CA  TYR A 186     4036   2421   2594   -201     -8    125       C  
ATOM   1211  C   TYR A 186      20.085  20.259 -22.562  1.00 22.28           C  
ANISOU 1211  C   TYR A 186     3780   2278   2408   -239     27    147       C  
ATOM   1212  O   TYR A 186      18.894  20.289 -22.829  1.00 22.77           O  
ANISOU 1212  O   TYR A 186     3856   2309   2488   -156     25    150       O  
ATOM   1213  CB  TYR A 186      20.945  19.583 -20.319  1.00 22.76           C  
ANISOU 1213  CB  TYR A 186     3792   2363   2492   -139     80     85       C  
ATOM   1214  CG  TYR A 186      19.823  18.577 -20.099  1.00 28.68           C  
ANISOU 1214  CG  TYR A 186     4466   3146   3286    -22    145     72       C  
ATOM   1215  CD1 TYR A 186      19.723  17.435 -20.890  1.00 18.56           C  
ANISOU 1215  CD1 TYR A 186     3088   1938   2025    -49    202     74       C  
ATOM   1216  CD2 TYR A 186      18.883  18.756 -19.082  1.00 27.36           C  
ANISOU 1216  CD2 TYR A 186     4322   2947   3128    114    139     61       C  
ATOM   1217  CE1 TYR A 186      18.714  16.511 -20.690  1.00 23.51           C  
ANISOU 1217  CE1 TYR A 186     3656   2590   2685     31    245     76       C  
ATOM   1218  CE2 TYR A 186      17.868  17.836 -18.871  1.00 18.70           C  
ANISOU 1218  CE2 TYR A 186     3144   1906   2056    194    194     66       C  
ATOM   1219  CZ  TYR A 186      17.790  16.713 -19.673  1.00 28.33           C  
ANISOU 1219  CZ  TYR A 186     4281   3183   3302    140    244     78       C  
ATOM   1220  OH  TYR A 186      16.793  15.788 -19.465  1.00 28.83           O  
ANISOU 1220  OH  TYR A 186     4274   3296   3384    194    282     95       O  
ATOM   1221  N   TYR A 187      20.994  19.774 -23.396  1.00 22.47           N  
ANISOU 1221  N   TYR A 187     3728   2398   2411   -356     57    157       N  
ATOM   1222  CA  TYR A 187      20.605  19.191 -24.678  1.00 19.88           C  
ANISOU 1222  CA  TYR A 187     3334   2131   2089   -385     89    171       C  
ATOM   1223  C   TYR A 187      21.708  18.269 -25.138  1.00 22.43           C  
ANISOU 1223  C   TYR A 187     3541   2596   2385   -452    138    152       C  
ATOM   1224  O   TYR A 187      22.840  18.692 -25.334  1.00 27.84           O  
ANISOU 1224  O   TYR A 187     4218   3349   3010   -566    114    166       O  
ATOM   1225  CB  TYR A 187      20.321  20.278 -25.723  1.00 20.49           C  
ANISOU 1225  CB  TYR A 187     3501   2155   2131   -469     16    221       C  
ATOM   1226  CG  TYR A 187      20.002  19.733 -27.106  1.00 25.68           C  
ANISOU 1226  CG  TYR A 187     4088   2882   2788   -505     48    236       C  
ATOM   1227  CD1 TYR A 187      19.080  18.698 -27.283  1.00 21.85           C  
ANISOU 1227  CD1 TYR A 187     3530   2418   2355   -403    108    211       C  
ATOM   1228  CD2 TYR A 187      20.626  20.255 -28.232  1.00 26.89           C  
ANISOU 1228  CD2 TYR A 187     4248   3086   2883   -649     10    280       C  
ATOM   1229  CE1 TYR A 187      18.800  18.193 -28.543  1.00 21.28           C  
ANISOU 1229  CE1 TYR A 187     3400   2403   2282   -429    128    221       C  
ATOM   1230  CE2 TYR A 187      20.350  19.769 -29.503  1.00 28.27           C  
ANISOU 1230  CE2 TYR A 187     4356   3333   3052   -672     38    291       C  
ATOM   1231  CZ  TYR A 187      19.444  18.741 -29.657  1.00 30.78           C  
ANISOU 1231  CZ  TYR A 187     4608   3657   3428   -555     96    256       C  
ATOM   1232  OH  TYR A 187      19.191  18.266 -30.925  1.00 29.33           O  
ANISOU 1232  OH  TYR A 187     4366   3540   3239   -575    114    264       O  
ATOM   1233  N   HIS A 188      21.380  16.995 -25.273  1.00 24.97           N  
ANISOU 1233  N   HIS A 188     3777   2971   2741   -377    197    118       N  
ATOM   1234  CA  HIS A 188      22.368  15.997 -25.639  1.00 22.58           C  
ANISOU 1234  CA  HIS A 188     3373   2802   2404   -396    230     81       C  
ATOM   1235  C   HIS A 188      21.783  15.079 -26.708  1.00 25.96           C  
ANISOU 1235  C   HIS A 188     3746   3270   2847   -363    249     72       C  
ATOM   1236  O   HIS A 188      21.225  14.018 -26.384  1.00 22.02           O  
ANISOU 1236  O   HIS A 188     3224   2748   2392   -272    271     44       O  
ATOM   1237  CB  HIS A 188      22.784  15.183 -24.407  1.00 20.88           C  
ANISOU 1237  CB  HIS A 188     3129   2596   2207   -316    262     29       C  
ATOM   1238  CG  HIS A 188      23.595  15.955 -23.410  1.00 21.13           C  
ANISOU 1238  CG  HIS A 188     3199   2615   2215   -351    245     28       C  
ATOM   1239  CD2 HIS A 188      23.419  16.156 -22.081  1.00 21.96           C  
ANISOU 1239  CD2 HIS A 188     3352   2640   2353   -286    246     16       C  
ATOM   1240  ND1 HIS A 188      24.768  16.600 -23.739  1.00 23.98           N  
ANISOU 1240  ND1 HIS A 188     3545   3065   2501   -470    219     41       N  
ATOM   1241  CE1 HIS A 188      25.274  17.173 -22.664  1.00 26.69           C  
ANISOU 1241  CE1 HIS A 188     3933   3368   2838   -481    200     38       C  
ATOM   1242  NE2 HIS A 188      24.472  16.921 -21.642  1.00 29.34           N  
ANISOU 1242  NE2 HIS A 188     4310   3597   3241   -361    217     18       N  
ATOM   1243  N   PRO A 189      21.886  15.494 -27.983  1.00 24.00           N  
ANISOU 1243  N   PRO A 189     3484   3077   2558   -442    230    102       N  
ATOM   1244  CA  PRO A 189      21.420  14.638 -29.073  1.00 24.25           C  
ANISOU 1244  CA  PRO A 189     3462   3154   2597   -408    241     89       C  
ATOM   1245  C   PRO A 189      22.367  13.464 -29.279  1.00 22.80           C  
ANISOU 1245  C   PRO A 189     3189   3107   2366   -367    253     25       C  
ATOM   1246  O   PRO A 189      23.577  13.584 -29.075  1.00 21.64           O  
ANISOU 1246  O   PRO A 189     2998   3076   2149   -407    254      3       O  
ATOM   1247  CB  PRO A 189      21.429  15.579 -30.294  1.00 19.50           C  
ANISOU 1247  CB  PRO A 189     2874   2585   1950   -514    212    141       C  
ATOM   1248  CG  PRO A 189      22.476  16.581 -29.982  1.00 20.14           C  
ANISOU 1248  CG  PRO A 189     2976   2710   1967   -628    185    170       C  
ATOM   1249  CD  PRO A 189      22.414  16.781 -28.473  1.00 19.85           C  
ANISOU 1249  CD  PRO A 189     3000   2570   1974   -575    187    155       C  
ATOM   1250  N   LEU A 190      21.806  12.338 -29.700  1.00 24.09           N  
ANISOU 1250  N   LEU A 190     3333   3263   2559   -284    252     -7       N  
ATOM   1251  CA  LEU A 190      22.572  11.112 -29.880  1.00 24.05           C  
ANISOU 1251  CA  LEU A 190     3268   3363   2506   -210    240    -81       C  
ATOM   1252  C   LEU A 190      22.807  10.782 -31.360  1.00 30.06           C  
ANISOU 1252  C   LEU A 190     3968   4248   3204   -208    219   -100       C  
ATOM   1253  O   LEU A 190      23.592   9.889 -31.683  1.00 29.08           O  
ANISOU 1253  O   LEU A 190     3788   4248   3010   -135    197   -171       O  
ATOM   1254  CB  LEU A 190      21.837   9.958 -29.202  1.00 22.22           C  
ANISOU 1254  CB  LEU A 190     3079   3022   2341   -112    226   -107       C  
ATOM   1255  CG  LEU A 190      21.664  10.143 -27.696  1.00 21.20           C  
ANISOU 1255  CG  LEU A 190     2996   2799   2261   -101    247    -94       C  
ATOM   1256  CD1 LEU A 190      20.772   9.066 -27.106  1.00 20.57           C  
ANISOU 1256  CD1 LEU A 190     2957   2617   2240    -35    228    -95       C  
ATOM   1257  CD2 LEU A 190      23.033  10.101 -27.066  1.00 18.40           C  
ANISOU 1257  CD2 LEU A 190     2609   2539   1843    -90    253   -147       C  
ATOM   1258  N   GLY A 191      22.132  11.516 -32.242  1.00 26.74           N  
ANISOU 1258  N   GLY A 191     3560   3799   2800   -275    221    -40       N  
ATOM   1259  CA  GLY A 191      22.047  11.155 -33.644  1.00 28.63           C  
ANISOU 1259  CA  GLY A 191     3752   4127   2999   -262    202    -51       C  
ATOM   1260  C   GLY A 191      20.839  10.260 -33.875  1.00 31.39           C  
ANISOU 1260  C   GLY A 191     4145   4352   3428   -181    181    -60       C  
ATOM   1261  O   GLY A 191      20.280   9.696 -32.925  1.00 26.36           O  
ANISOU 1261  O   GLY A 191     3560   3598   2858   -132    177    -66       O  
ATOM   1262  N   GLY A 192      20.422  10.136 -35.134  1.00 31.84           N  
ANISOU 1262  N   GLY A 192     4181   4443   3474   -177    164    -54       N  
ATOM   1263  CA  GLY A 192      19.325   9.250 -35.490  1.00 29.96           C  
ANISOU 1263  CA  GLY A 192     3981   4102   3300   -111    132    -60       C  
ATOM   1264  C   GLY A 192      18.015   9.596 -34.797  1.00 32.19           C  
ANISOU 1264  C   GLY A 192     4331   4221   3681   -139    152      2       C  
ATOM   1265  O   GLY A 192      17.251   8.710 -34.410  1.00 33.60           O  
ANISOU 1265  O   GLY A 192     4544   4310   3911    -93    126      0       O  
ATOM   1266  N   GLY A 193      17.767  10.888 -34.627  1.00 18.51           N  
ANISOU 1266  N   GLY A 193     2616   2458   1959   -213    186     57       N  
ATOM   1267  CA  GLY A 193      16.519  11.351 -34.060  1.00 32.20           C  
ANISOU 1267  CA  GLY A 193     4403   4071   3761   -219    200    108       C  
ATOM   1268  C   GLY A 193      16.361  11.027 -32.583  1.00 27.84           C  
ANISOU 1268  C   GLY A 193     3876   3457   3246   -186    211    105       C  
ATOM   1269  O   GLY A 193      15.249  11.057 -32.063  1.00 26.57           O  
ANISOU 1269  O   GLY A 193     3738   3226   3132   -169    217    140       O  
ATOM   1270  N   ARG A 194      17.465  10.716 -31.906  1.00 26.00           N  
ANISOU 1270  N   ARG A 194     3629   3268   2981   -173    212     65       N  
ATOM   1271  CA  ARG A 194      17.410  10.395 -30.482  1.00 28.01           C  
ANISOU 1271  CA  ARG A 194     3908   3470   3266   -142    222     61       C  
ATOM   1272  C   ARG A 194      18.142  11.421 -29.619  1.00 24.37           C  
ANISOU 1272  C   ARG A 194     3460   3017   2783   -173    247     65       C  
ATOM   1273  O   ARG A 194      19.119  12.033 -30.060  1.00 22.32           O  
ANISOU 1273  O   ARG A 194     3181   2831   2468   -223    248     55       O  
ATOM   1274  CB  ARG A 194      17.981   9.002 -30.228  1.00 29.84           C  
ANISOU 1274  CB  ARG A 194     4132   3721   3484    -84    188      5       C  
ATOM   1275  CG  ARG A 194      17.678   8.007 -31.325  1.00 31.02           C  
ANISOU 1275  CG  ARG A 194     4278   3879   3628    -52    137    -17       C  
ATOM   1276  CD  ARG A 194      17.453   6.650 -30.747  1.00 27.86           C  
ANISOU 1276  CD  ARG A 194     3922   3417   3247     -2     81    -37       C  
ATOM   1277  NE  ARG A 194      18.231   5.593 -31.388  1.00 37.28           N  
ANISOU 1277  NE  ARG A 194     5124   4655   4387     71     11   -115       N  
ATOM   1278  CZ  ARG A 194      17.714   4.654 -32.179  1.00 49.88           C  
ANISOU 1278  CZ  ARG A 194     6755   6211   5987    104    -64   -126       C  
ATOM   1279  NH1 ARG A 194      16.415   4.648 -32.446  1.00 60.71           N1+
ANISOU 1279  NH1 ARG A 194     8144   7506   7417     52    -69    -56       N1+
ATOM   1280  NH2 ARG A 194      18.495   3.720 -32.711  1.00 47.77           N  
ANISOU 1280  NH2 ARG A 194     6506   5988   5656    197   -143   -211       N  
ATOM   1281  N   GLU A 195      17.676  11.596 -28.383  1.00 19.58           N  
ANISOU 1281  N   GLU A 195     2884   2345   2211   -147    262     82       N  
ATOM   1282  CA  GLU A 195      18.349  12.480 -27.441  1.00 20.00           C  
ANISOU 1282  CA  GLU A 195     2961   2391   2246   -163    274     80       C  
ATOM   1283  C   GLU A 195      18.290  11.952 -25.981  1.00 22.08           C  
ANISOU 1283  C   GLU A 195     3232   2621   2536   -107    288     68       C  
ATOM   1284  O   GLU A 195      17.464  11.099 -25.643  1.00 23.84           O  
ANISOU 1284  O   GLU A 195     3449   2817   2792    -69    285     81       O  
ATOM   1285  CB  GLU A 195      17.757  13.891 -27.531  1.00 20.40           C  
ANISOU 1285  CB  GLU A 195     3066   2389   2298   -190    265    124       C  
ATOM   1286  CG  GLU A 195      16.614  14.112 -26.548  1.00 29.27           C  
ANISOU 1286  CG  GLU A 195     4218   3448   3455   -122    271    146       C  
ATOM   1287  CD  GLU A 195      15.710  15.287 -26.896  1.00 32.21           C  
ANISOU 1287  CD  GLU A 195     4646   3772   3820   -112    245    177       C  
ATOM   1288  OE1 GLU A 195      16.188  16.444 -26.910  1.00 35.35           O  
ANISOU 1288  OE1 GLU A 195     5112   4134   4187   -147    211    182       O  
ATOM   1289  OE2 GLU A 195      14.500  15.047 -27.122  1.00 33.27           O1-
ANISOU 1289  OE2 GLU A 195     4763   3906   3972    -67    250    197       O1-
ATOM   1290  N   VAL A 196      19.160  12.471 -25.120  1.00 17.50           N  
ANISOU 1290  N   VAL A 196     2666   2048   1935   -112    296     49       N  
ATOM   1291  CA  VAL A 196      19.201  12.046 -23.716  1.00 17.32           C  
ANISOU 1291  CA  VAL A 196     2651   1999   1931    -58    309     35       C  
ATOM   1292  C   VAL A 196      18.210  12.822 -22.857  1.00 17.33           C  
ANISOU 1292  C   VAL A 196     2684   1944   1955    -20    316     73       C  
ATOM   1293  O   VAL A 196      18.194  14.051 -22.884  1.00 26.10           O  
ANISOU 1293  O   VAL A 196     3839   3026   3051    -34    301     86       O  
ATOM   1294  CB  VAL A 196      20.617  12.213 -23.110  1.00 28.47           C  
ANISOU 1294  CB  VAL A 196     4058   3453   3305    -69    314     -9       C  
ATOM   1295  CG1 VAL A 196      20.637  11.831 -21.621  1.00 27.39           C  
ANISOU 1295  CG1 VAL A 196     3933   3284   3189     -8    329    -23       C  
ATOM   1296  CG2 VAL A 196      21.616  11.386 -23.866  1.00 17.56           C  
ANISOU 1296  CG2 VAL A 196     2630   2164   1879    -78    305    -60       C  
ATOM   1297  N   TRP A 197      17.358  12.112 -22.120  1.00 17.58           N  
ANISOU 1297  N   TRP A 197     2700   1968   2013     28    326     93       N  
ATOM   1298  CA  TRP A 197      16.601  12.741 -21.035  1.00 18.60           C  
ANISOU 1298  CA  TRP A 197     2841   2085   2142     88    334    117       C  
ATOM   1299  C   TRP A 197      17.199  12.310 -19.697  1.00 17.25           C  
ANISOU 1299  C   TRP A 197     2666   1917   1971    123    349     95       C  
ATOM   1300  O   TRP A 197      17.529  11.135 -19.505  1.00 17.12           O  
ANISOU 1300  O   TRP A 197     2630   1911   1963    112    351     84       O  
ATOM   1301  CB  TRP A 197      15.128  12.339 -21.059  1.00 23.87           C  
ANISOU 1301  CB  TRP A 197     3471   2781   2817    113    337    167       C  
ATOM   1302  CG  TRP A 197      14.320  12.914 -22.184  1.00 22.57           C  
ANISOU 1302  CG  TRP A 197     3311   2617   2649    102    324    188       C  
ATOM   1303  CD1 TRP A 197      14.775  13.313 -23.418  1.00 25.03           C  
ANISOU 1303  CD1 TRP A 197     3649   2903   2960     51    309    175       C  
ATOM   1304  CD2 TRP A 197      12.904  13.147 -22.185  1.00 20.69           C  
ANISOU 1304  CD2 TRP A 197     3043   2422   2395    146    323    228       C  
ATOM   1305  CE2 TRP A 197      12.574  13.688 -23.452  1.00 21.88           C  
ANISOU 1305  CE2 TRP A 197     3215   2553   2543    125    305    231       C  
ATOM   1306  CE3 TRP A 197      11.886  12.949 -21.245  1.00 18.33           C  
ANISOU 1306  CE3 TRP A 197     2693   2200   2073    202    334    263       C  
ATOM   1307  NE1 TRP A 197      13.733  13.784 -24.173  1.00 17.82           N  
ANISOU 1307  NE1 TRP A 197     2737   1994   2040     62    297    202       N  
ATOM   1308  CZ2 TRP A 197      11.266  14.043 -23.795  1.00 22.15           C  
ANISOU 1308  CZ2 TRP A 197     3228   2632   2557    168    298    259       C  
ATOM   1309  CZ3 TRP A 197      10.587  13.305 -21.584  1.00 23.28           C  
ANISOU 1309  CZ3 TRP A 197     3284   2894   2668    242    328    293       C  
ATOM   1310  CH2 TRP A 197      10.287  13.845 -22.851  1.00 23.91           C  
ANISOU 1310  CH2 TRP A 197     3392   2942   2750    230    309    287       C  
ATOM   1311  N   PHE A 198      17.337  13.257 -18.778  1.00 17.39           N  
ANISOU 1311  N   PHE A 198     2713   1918   1974    170    349     85       N  
ATOM   1312  CA  PHE A 198      17.813  12.960 -17.426  1.00 24.80           C  
ANISOU 1312  CA  PHE A 198     3648   2863   2911    215    364     66       C  
ATOM   1313  C   PHE A 198      16.636  12.751 -16.498  1.00 24.27           C  
ANISOU 1313  C   PHE A 198     3545   2837   2838    282    376    105       C  
ATOM   1314  O   PHE A 198      15.593  13.378 -16.666  1.00 28.84           O  
ANISOU 1314  O   PHE A 198     4118   3442   3399    323    367    132       O  
ATOM   1315  CB  PHE A 198      18.667  14.100 -16.877  1.00 22.30           C  
ANISOU 1315  CB  PHE A 198     3386   2510   2577    231    348     32       C  
ATOM   1316  CG  PHE A 198      20.036  14.167 -17.475  1.00 28.70           C  
ANISOU 1316  CG  PHE A 198     4209   3320   3376    152    340     -2       C  
ATOM   1317  CD1 PHE A 198      20.872  13.065 -17.446  1.00 29.99           C  
ANISOU 1317  CD1 PHE A 198     4334   3523   3539    134    360    -36       C  
ATOM   1318  CD2 PHE A 198      20.485  15.330 -18.079  1.00 29.67           C  
ANISOU 1318  CD2 PHE A 198     4384   3415   3474     95    303      0       C  
ATOM   1319  CE1 PHE A 198      22.141  13.121 -18.004  1.00 31.33           C  
ANISOU 1319  CE1 PHE A 198     4495   3734   3676     73    353    -72       C  
ATOM   1320  CE2 PHE A 198      21.743  15.396 -18.639  1.00 29.08           C  
ANISOU 1320  CE2 PHE A 198     4301   3379   3371      6    296    -20       C  
ATOM   1321  CZ  PHE A 198      22.574  14.295 -18.608  1.00 28.71           C  
ANISOU 1321  CZ  PHE A 198     4193   3401   3315      1    326    -59       C  
ATOM   1322  N   GLY A 199      16.808  11.863 -15.528  1.00 17.45           N  
ANISOU 1322  N   GLY A 199     2656   1996   1978    295    393    108       N  
ATOM   1323  CA  GLY A 199      15.788  11.619 -14.523  1.00 23.09           C  
ANISOU 1323  CA  GLY A 199     3322   2780   2670    347    405    154       C  
ATOM   1324  C   GLY A 199      16.320  10.790 -13.363  1.00 26.48           C  
ANISOU 1324  C   GLY A 199     3744   3217   3100    355    417    150       C  
ATOM   1325  O   GLY A 199      17.512  10.834 -13.042  1.00 17.42           O  
ANISOU 1325  O   GLY A 199     2635   2020   1964    361    419     94       O  
ATOM   1326  N   PHE A 200      15.448  10.020 -12.727  1.00 27.86           N  
ANISOU 1326  N   PHE A 200     3866   3464   3255    347    420    212       N  
ATOM   1327  CA  PHE A 200      15.895   9.206 -11.603  1.00 18.11           C  
ANISOU 1327  CA  PHE A 200     2633   2233   2015    348    423    216       C  
ATOM   1328  C   PHE A 200      15.135   7.892 -11.484  1.00 18.55           C  
ANISOU 1328  C   PHE A 200     2660   2332   2057    265    398    298       C  
ATOM   1329  O   PHE A 200      13.976   7.791 -11.893  1.00 21.47           O  
ANISOU 1329  O   PHE A 200     2977   2777   2405    226    391    367       O  
ATOM   1330  CB  PHE A 200      15.838  10.008 -10.295  1.00 18.30           C  
ANISOU 1330  CB  PHE A 200     2633   2314   2007    451    448    204       C  
ATOM   1331  CG  PHE A 200      14.450  10.400  -9.868  1.00 21.45           C  
ANISOU 1331  CG  PHE A 200     2951   2849   2349    503    457    265       C  
ATOM   1332  CD1 PHE A 200      13.796  11.469 -10.463  1.00 23.19           C  
ANISOU 1332  CD1 PHE A 200     3164   3100   2549    563    450    255       C  
ATOM   1333  CD2 PHE A 200      13.802   9.712  -8.847  1.00 19.52           C  
ANISOU 1333  CD2 PHE A 200     2636   2721   2058    497    465    333       C  
ATOM   1334  CE1 PHE A 200      12.509  11.842 -10.054  1.00 20.62           C  
ANISOU 1334  CE1 PHE A 200     2753   2930   2150    636    453    299       C  
ATOM   1335  CE2 PHE A 200      12.522  10.071  -8.436  1.00 20.30           C  
ANISOU 1335  CE2 PHE A 200     2638   2993   2084    551    474    390       C  
ATOM   1336  CZ  PHE A 200      11.875  11.133  -9.038  1.00 22.89           C  
ANISOU 1336  CZ  PHE A 200     2950   3363   2384    630    469    367       C  
ATOM   1337  N   HIS A 201      15.817   6.882 -10.956  1.00 18.53           N  
ANISOU 1337  N   HIS A 201     2701   2278   2061    233    374    291       N  
ATOM   1338  CA  HIS A 201      15.167   5.653 -10.528  1.00 20.19           C  
ANISOU 1338  CA  HIS A 201     2906   2520   2247    148    333    378       C  
ATOM   1339  C   HIS A 201      14.673   5.770  -9.073  1.00 23.64           C  
ANISOU 1339  C   HIS A 201     3278   3070   2636    180    360    432       C  
ATOM   1340  O   HIS A 201      15.376   6.296  -8.199  1.00 20.26           O  
ANISOU 1340  O   HIS A 201     2855   2635   2206    269    394    376       O  
ATOM   1341  CB  HIS A 201      16.120   4.468 -10.615  1.00 19.08           C  
ANISOU 1341  CB  HIS A 201     2865   2261   2124    108    271    342       C  
ATOM   1342  CG  HIS A 201      15.598   3.244  -9.925  1.00 27.79           C  
ANISOU 1342  CG  HIS A 201     3992   3374   3194     19    210    433       C  
ATOM   1343  CD2 HIS A 201      15.607   2.891  -8.612  1.00 21.48           C  
ANISOU 1343  CD2 HIS A 201     3187   2613   2363     17    209    472       C  
ATOM   1344  ND1 HIS A 201      14.922   2.250 -10.590  1.00 28.14           N  
ANISOU 1344  ND1 HIS A 201     4073   3389   3230    -97    130    507       N  
ATOM   1345  CE1 HIS A 201      14.558   1.312  -9.722  1.00 23.81           C  
ANISOU 1345  CE1 HIS A 201     3550   2855   2643   -180     73    593       C  
ATOM   1346  NE2 HIS A 201      14.957   1.681  -8.523  1.00 27.17           N  
ANISOU 1346  NE2 HIS A 201     3946   3326   3053   -112    124    575       N  
ATOM   1347  N   GLN A 202      13.469   5.264  -8.818  1.00 21.51           N  
ANISOU 1347  N   GLN A 202     2940   2917   2315    103    343    545       N  
ATOM   1348  CA  GLN A 202      12.949   5.184  -7.445  1.00 21.10           C  
ANISOU 1348  CA  GLN A 202     2813   3006   2199    115    361    613       C  
ATOM   1349  C   GLN A 202      12.260   3.838  -7.198  1.00 27.87           C  
ANISOU 1349  C   GLN A 202     3667   3908   3013    -46    296    740       C  
ATOM   1350  O   GLN A 202      11.435   3.386  -8.003  1.00 25.62           O  
ANISOU 1350  O   GLN A 202     3364   3653   2716   -154    256    814       O  
ATOM   1351  CB  GLN A 202      11.977   6.332  -7.154  1.00 21.48           C  
ANISOU 1351  CB  GLN A 202     2738   3237   2188    211    414    630       C  
ATOM   1352  CG  GLN A 202      11.243   6.188  -5.816  1.00 34.49           C  
ANISOU 1352  CG  GLN A 202     4277   5084   3742    221    430    714       C  
ATOM   1353  CD  GLN A 202      10.260   7.327  -5.527  1.00 35.70           C  
ANISOU 1353  CD  GLN A 202     4304   5447   3815    351    471    717       C  
ATOM   1354  NE2 GLN A 202       9.177   7.006  -4.842  1.00 28.73           N  
ANISOU 1354  NE2 GLN A 202     3289   4803   2826    313    474    826       N  
ATOM   1355  OE1 GLN A 202      10.474   8.473  -5.920  1.00 37.54           O  
ANISOU 1355  OE1 GLN A 202     4560   5634   4069    483    491    624       O  
ATOM   1356  N   SER A 203      12.611   3.192  -6.093  1.00 22.39           N  
ANISOU 1356  N   SER A 203     2999   3214   2294    -70    276    770       N  
ATOM   1357  CA  SER A 203      11.916   1.981  -5.687  1.00 27.16           C  
ANISOU 1357  CA  SER A 203     3604   3874   2841   -238    202    909       C  
ATOM   1358  C   SER A 203      11.942   1.845  -4.171  1.00 27.31           C  
ANISOU 1358  C   SER A 203     3578   4000   2800   -222    221    956       C  
ATOM   1359  O   SER A 203      12.787   2.439  -3.504  1.00 32.76           O  
ANISOU 1359  O   SER A 203     4280   4654   3513    -84    273    861       O  
ATOM   1360  CB  SER A 203      12.550   0.752  -6.339  1.00 23.52           C  
ANISOU 1360  CB  SER A 203     3312   3201   2426   -340     94    900       C  
ATOM   1361  OG  SER A 203      13.941   0.722  -6.085  1.00 28.76           O  
ANISOU 1361  OG  SER A 203     4081   3707   3138   -237     95    775       O  
ATOM   1362  N   VAL A 204      11.004   1.072  -3.630  1.00 25.35           N  
ANISOU 1362  N   VAL A 204     3271   3893   2467   -374    174   1110       N  
ATOM   1363  CA  VAL A 204      10.997   0.757  -2.201  1.00 26.04           C  
ANISOU 1363  CA  VAL A 204     3320   4089   2486   -390    176   1175       C  
ATOM   1364  C   VAL A 204      11.200  -0.738  -2.008  1.00 26.83           C  
ANISOU 1364  C   VAL A 204     3560   4060   2575   -575     51   1265       C  
ATOM   1365  O   VAL A 204      10.513  -1.552  -2.623  1.00 27.71           O  
ANISOU 1365  O   VAL A 204     3705   4164   2661   -756    -40   1374       O  
ATOM   1366  CB  VAL A 204       9.703   1.232  -1.490  1.00 42.58           C  
ANISOU 1366  CB  VAL A 204     5204   6517   4457   -400    229   1290       C  
ATOM   1367  CG1 VAL A 204       9.578   0.595  -0.120  1.00 47.22           C  
ANISOU 1367  CG1 VAL A 204     5756   7227   4958   -477    206   1396       C  
ATOM   1368  CG2 VAL A 204       9.708   2.732  -1.336  1.00 42.03           C  
ANISOU 1368  CG2 VAL A 204     5029   6556   4387   -168    335   1178       C  
ATOM   1369  N   ARG A 205      12.150  -1.086  -1.145  1.00 34.33           N  
ANISOU 1369  N   ARG A 205     4603   4902   3538   -528     35   1216       N  
ATOM   1370  CA  ARG A 205      12.547  -2.472  -0.944  1.00 35.95           C  
ANISOU 1370  CA  ARG A 205     4982   4940   3736   -670   -101   1272       C  
ATOM   1371  C   ARG A 205      12.710  -2.802   0.533  1.00 34.59           C  
ANISOU 1371  C   ARG A 205     4799   4842   3499   -686   -104   1330       C  
ATOM   1372  O   ARG A 205      13.165  -1.972   1.326  1.00 27.26           O  
ANISOU 1372  O   ARG A 205     3794   3987   2577   -520      0   1250       O  
ATOM   1373  CB  ARG A 205      13.863  -2.757  -1.678  1.00 40.98           C  
ANISOU 1373  CB  ARG A 205     5808   5294   4468   -576   -150   1112       C  
ATOM   1374  CG  ARG A 205      13.731  -2.879  -3.195  1.00 58.12           C  
ANISOU 1374  CG  ARG A 205     8037   7358   6690   -608   -197   1078       C  
ATOM   1375  CD  ARG A 205      15.099  -2.939  -3.874  1.00 68.62           C  
ANISOU 1375  CD  ARG A 205     9510   8466   8095   -473   -220    901       C  
ATOM   1376  NE  ARG A 205      16.125  -3.470  -2.977  1.00 75.56           N  
ANISOU 1376  NE  ARG A 205    10505   9237   8967   -414   -262    840       N  
ATOM   1377  CZ  ARG A 205      16.558  -4.727  -2.977  1.00 78.76           C  
ANISOU 1377  CZ  ARG A 205    11102   9469   9352   -478   -416    845       C  
ATOM   1378  NH1 ARG A 205      16.067  -5.606  -3.841  1.00 78.47           N1+
ANISOU 1378  NH1 ARG A 205    11173   9337   9304   -608   -553    910       N1+
ATOM   1379  NH2 ARG A 205      17.493  -5.104  -2.113  1.00 81.86           N  
ANISOU 1379  NH2 ARG A 205    11591   9778   9734   -403   -445    781       N  
ATOM   1380  N   PRO A 206      12.328  -4.022   0.916  1.00 33.21           N  
ANISOU 1380  N   PRO A 206     4710   4648   3259   -893   -233   1476       N  
ATOM   1381  CA  PRO A 206      12.589  -4.468   2.283  1.00 31.87           C  
ANISOU 1381  CA  PRO A 206     4562   4518   3030   -921   -254   1533       C  
ATOM   1382  C   PRO A 206      14.082  -4.714   2.426  1.00 33.42           C  
ANISOU 1382  C   PRO A 206     4944   4450   3303   -778   -283   1368       C  
ATOM   1383  O   PRO A 206      14.681  -5.355   1.566  1.00 34.85           O  
ANISOU 1383  O   PRO A 206     5308   4395   3537   -788   -385   1298       O  
ATOM   1384  CB  PRO A 206      11.823  -5.785   2.369  1.00 31.90           C  
ANISOU 1384  CB  PRO A 206     4650   4522   2948  -1208   -418   1734       C  
ATOM   1385  CG  PRO A 206      11.696  -6.248   0.934  1.00 31.86           C  
ANISOU 1385  CG  PRO A 206     4767   4342   2997  -1287   -517   1719       C  
ATOM   1386  CD  PRO A 206      11.569  -5.010   0.134  1.00 30.54           C  
ANISOU 1386  CD  PRO A 206     4452   4262   2891  -1122   -372   1609       C  
ATOM   1387  N   ALA A 207      14.678  -4.164   3.473  1.00 28.45           N  
ANISOU 1387  N   ALA A 207     4261   3876   2672   -631   -193   1299       N  
ATOM   1388  CA  ALA A 207      16.068  -4.418   3.795  1.00 33.42           C  
ANISOU 1388  CA  ALA A 207     5048   4293   3355   -501   -217   1153       C  
ATOM   1389  C   ALA A 207      16.160  -5.072   5.193  1.00 40.32           C  
ANISOU 1389  C   ALA A 207     5962   5202   4156   -562   -264   1238       C  
ATOM   1390  O   ALA A 207      15.173  -5.613   5.677  1.00 30.08           O  
ANISOU 1390  O   ALA A 207     4615   4046   2767   -753   -319   1424       O  
ATOM   1391  CB  ALA A 207      16.859  -3.142   3.721  1.00 26.06           C  
ANISOU 1391  CB  ALA A 207     4037   3370   2496   -263    -75    976       C  
ATOM   1392  N   MET A 208      17.328  -5.018   5.831  1.00 27.89           N  
ANISOU 1392  N   MET A 208     4469   3513   2614   -409   -243   1108       N  
ATOM   1393  CA  MET A 208      17.598  -5.880   6.981  1.00 35.87           C  
ANISOU 1393  CA  MET A 208     5581   4485   3564   -473   -325   1172       C  
ATOM   1394  C   MET A 208      16.652  -5.664   8.170  1.00 41.38           C  
ANISOU 1394  C   MET A 208     6101   5459   4164   -557   -266   1334       C  
ATOM   1395  O   MET A 208      16.101  -6.629   8.694  1.00 38.91           O  
ANISOU 1395  O   MET A 208     5844   5176   3763   -759   -378   1501       O  
ATOM   1396  CB  MET A 208      19.070  -5.817   7.428  1.00 32.36           C  
ANISOU 1396  CB  MET A 208     5250   3876   3170   -274   -308    988       C  
ATOM   1397  CG  MET A 208      19.443  -6.929   8.401  1.00 28.85           C  
ANISOU 1397  CG  MET A 208     4969   3327   2664   -346   -431   1041       C  
ATOM   1398  SD  MET A 208      21.210  -7.272   8.642  1.00 28.22           S  
ANISOU 1398  SD  MET A 208     5091   3002   2628   -138   -475    820       S  
ATOM   1399  CE  MET A 208      21.472  -8.652   7.492  1.00 28.90           C  
ANISOU 1399  CE  MET A 208     5462   2812   2707   -231   -708    802       C  
ATOM   1400  N   TRP A 209      16.450  -4.417   8.584  1.00 29.09           N  
ANISOU 1400  N   TRP A 209     4335   4107   2609   -405   -105   1289       N  
ATOM   1401  CA  TRP A 209      15.471  -4.142   9.639  1.00 35.79           C  
ANISOU 1401  CA  TRP A 209     4989   5264   3347   -461    -47   1436       C  
ATOM   1402  C   TRP A 209      14.317  -3.246   9.174  1.00 37.04           C  
ANISOU 1402  C   TRP A 209     4924   5682   3467   -458     41   1494       C  
ATOM   1403  O   TRP A 209      13.260  -3.233   9.792  1.00 34.32           O  
ANISOU 1403  O   TRP A 209     4413   5625   3002   -555     58   1649       O  
ATOM   1404  CB  TRP A 209      16.156  -3.549  10.879  1.00 32.04           C  
ANISOU 1404  CB  TRP A 209     4458   4848   2867   -270     45   1348       C  
ATOM   1405  CG  TRP A 209      17.321  -4.374  11.340  1.00 39.27           C  
ANISOU 1405  CG  TRP A 209     5587   5517   3817   -252    -37   1277       C  
ATOM   1406  CD1 TRP A 209      17.287  -5.461  12.185  1.00 37.49           C  
ANISOU 1406  CD1 TRP A 209     5463   5266   3515   -399   -144   1396       C  
ATOM   1407  CD2 TRP A 209      18.690  -4.208  10.967  1.00 45.26           C  
ANISOU 1407  CD2 TRP A 209     6487   6028   4681    -79    -29   1071       C  
ATOM   1408  CE2 TRP A 209      19.445  -5.212  11.608  1.00 45.22           C  
ANISOU 1408  CE2 TRP A 209     6666   5858   4658   -108   -132   1061       C  
ATOM   1409  CE3 TRP A 209      19.374  -3.291  10.140  1.00 48.99           C  
ANISOU 1409  CE3 TRP A 209     6948   6413   5252     95     49    895       C  
ATOM   1410  NE1 TRP A 209      18.552  -5.970  12.355  1.00 37.42           N  
ANISOU 1410  NE1 TRP A 209     5660   4998   3561   -309   -205   1266       N  
ATOM   1411  CZ2 TRP A 209      20.827  -5.343  11.470  1.00 49.37           C  
ANISOU 1411  CZ2 TRP A 209     7349   6156   5253     44   -153    877       C  
ATOM   1412  CZ3 TRP A 209      20.754  -3.418   9.991  1.00 47.65           C  
ANISOU 1412  CZ3 TRP A 209     6926   6028   5150    225     30    723       C  
ATOM   1413  CH2 TRP A 209      21.462  -4.437  10.652  1.00 45.27           C  
ANISOU 1413  CH2 TRP A 209     6793   5585   4823    207    -68    711       C  
ATOM   1414  N   LYS A 210      14.522  -2.521   8.076  1.00 32.73           N  
ANISOU 1414  N   LYS A 210     4377   5047   3011   -347     90   1370       N  
ATOM   1415  CA  LYS A 210      13.604  -1.462   7.666  1.00 35.60           C  
ANISOU 1415  CA  LYS A 210     4542   5637   3347   -280    184   1380       C  
ATOM   1416  C   LYS A 210      13.279  -1.530   6.182  1.00 39.90           C  
ANISOU 1416  C   LYS A 210     5132   6081   3948   -357    147   1373       C  
ATOM   1417  O   LYS A 210      14.014  -2.134   5.412  1.00 28.23           O  
ANISOU 1417  O   LYS A 210     3837   4335   2552   -394     71   1307       O  
ATOM   1418  CB  LYS A 210      14.235  -0.094   7.951  1.00 38.92           C  
ANISOU 1418  CB  LYS A 210     4894   6073   3821     -4    305   1207       C  
ATOM   1419  CG  LYS A 210      15.057  -0.029   9.247  1.00 49.95           C  
ANISOU 1419  CG  LYS A 210     6315   7453   5211    116    334   1148       C  
ATOM   1420  CD  LYS A 210      15.289   1.401   9.721  1.00 52.19           C  
ANISOU 1420  CD  LYS A 210     6486   7838   5505    370    445   1022       C  
ATOM   1421  CE  LYS A 210      14.188   1.866  10.672  1.00 52.15           C  
ANISOU 1421  CE  LYS A 210     6268   8187   5361    413    493   1124       C  
ATOM   1422  NZ  LYS A 210      12.828   1.901  10.053  1.00 52.07           N1+
ANISOU 1422  NZ  LYS A 210     6118   8400   5267    304    487   1247       N1+
ATOM   1423  N   MET A 211      12.169  -0.916   5.791  1.00 29.27           N  
ANISOU 1423  N   MET A 211     3613   4963   2546   -369    196   1436       N  
ATOM   1424  CA  MET A 211      11.937  -0.588   4.397  1.00 28.67           C  
ANISOU 1424  CA  MET A 211     3552   4807   2534   -371    196   1389       C  
ATOM   1425  C   MET A 211      12.943   0.495   4.000  1.00 29.31           C  
ANISOU 1425  C   MET A 211     3676   4735   2724   -135    275   1182       C  
ATOM   1426  O   MET A 211      13.293   1.360   4.806  1.00 30.08           O  
ANISOU 1426  O   MET A 211     3707   4908   2815     44    353   1103       O  
ATOM   1427  CB  MET A 211      10.515  -0.074   4.179  1.00 29.64           C  
ANISOU 1427  CB  MET A 211     3467   5236   2558   -410    237   1494       C  
ATOM   1428  CG  MET A 211       9.434  -1.096   4.467  1.00 52.16           C  
ANISOU 1428  CG  MET A 211     6254   8277   5287   -672    156   1715       C  
ATOM   1429  SD  MET A 211       9.680  -2.695   3.658  1.00 39.47           S  
ANISOU 1429  SD  MET A 211     4890   6376   3731   -945    -18   1800       S  
ATOM   1430  CE  MET A 211       9.464  -2.309   1.932  1.00 31.13           C  
ANISOU 1430  CE  MET A 211     3861   5201   2764   -924    -16   1723       C  
ATOM   1431  N   MET A 212      13.407   0.434   2.761  1.00 26.10           N  
ANISOU 1431  N   MET A 212     3383   4121   2411   -142    245   1102       N  
ATOM   1432  CA  MET A 212      14.354   1.402   2.229  1.00 28.09           C  
ANISOU 1432  CA  MET A 212     3679   4233   2759     42    305    924       C  
ATOM   1433  C   MET A 212      13.851   1.952   0.902  1.00 25.63           C  
ANISOU 1433  C   MET A 212     3335   3921   2481     40    319    903       C  
ATOM   1434  O   MET A 212      13.262   1.226   0.103  1.00 26.84           O  
ANISOU 1434  O   MET A 212     3516   4054   2628   -114    254    986       O  
ATOM   1435  CB  MET A 212      15.715   0.758   1.974  1.00 23.85           C  
ANISOU 1435  CB  MET A 212     3332   3429   2303     53    251    820       C  
ATOM   1436  CG  MET A 212      16.432   0.283   3.196  1.00 24.17           C  
ANISOU 1436  CG  MET A 212     3431   3430   2324     83    237    806       C  
ATOM   1437  SD  MET A 212      17.351   1.580   4.042  1.00 33.90           S  
ANISOU 1437  SD  MET A 212     4611   4683   3588    322    347    658       S  
ATOM   1438  CE  MET A 212      18.451   0.565   5.025  1.00 23.50           C  
ANISOU 1438  CE  MET A 212     3433   3227   2270    320    291    625       C  
ATOM   1439  N   LEU A 213      14.103   3.238   0.687  1.00 23.46           N  
ANISOU 1439  N   LEU A 213     3012   3659   2240    210    395    792       N  
ATOM   1440  CA  LEU A 213      13.862   3.900  -0.576  1.00 22.96           C  
ANISOU 1440  CA  LEU A 213     2941   3561   2220    235    409    745       C  
ATOM   1441  C   LEU A 213      15.195   3.956  -1.321  1.00 23.20           C  
ANISOU 1441  C   LEU A 213     3113   3351   2352    280    398    611       C  
ATOM   1442  O   LEU A 213      16.189   4.507  -0.823  1.00 22.63           O  
ANISOU 1442  O   LEU A 213     3077   3209   2311    400    431    507       O  
ATOM   1443  CB  LEU A 213      13.327   5.317  -0.343  1.00 24.55           C  
ANISOU 1443  CB  LEU A 213     3023   3923   2382    397    478    705       C  
ATOM   1444  CG  LEU A 213      13.070   6.232  -1.547  1.00 32.13           C  
ANISOU 1444  CG  LEU A 213     3978   4853   3378    451    493    647       C  
ATOM   1445  CD1 LEU A 213      11.830   5.806  -2.291  1.00 27.35           C  
ANISOU 1445  CD1 LEU A 213     3298   4369   2726    328    469    757       C  
ATOM   1446  CD2 LEU A 213      12.958   7.691  -1.125  1.00 37.28           C  
ANISOU 1446  CD2 LEU A 213     4571   5594   3998    650    537    569       C  
ATOM   1447  N   ASN A 214      15.214   3.357  -2.505  1.00 28.44           N  
ANISOU 1447  N   ASN A 214     3848   3902   3054    180    345    617       N  
ATOM   1448  CA  ASN A 214      16.398   3.331  -3.345  1.00 20.76           C  
ANISOU 1448  CA  ASN A 214     2991   2740   2157    216    327    498       C  
ATOM   1449  C   ASN A 214      16.225   4.391  -4.427  1.00 22.46           C  
ANISOU 1449  C   ASN A 214     3168   2960   2405    267    367    446       C  
ATOM   1450  O   ASN A 214      15.269   4.347  -5.203  1.00 20.58           O  
ANISOU 1450  O   ASN A 214     2887   2777   2156    198    354    512       O  
ATOM   1451  CB  ASN A 214      16.568   1.935  -3.949  1.00 29.90           C  
ANISOU 1451  CB  ASN A 214     4265   3771   3324     91    226    529       C  
ATOM   1452  CG  ASN A 214      17.763   1.823  -4.900  1.00 29.01           C  
ANISOU 1452  CG  ASN A 214     4259   3496   3267    141    199    401       C  
ATOM   1453  ND2 ASN A 214      17.671   0.890  -5.814  1.00 24.85           N  
ANISOU 1453  ND2 ASN A 214     3817   2879   2745     55    110    419       N  
ATOM   1454  OD1 ASN A 214      18.751   2.551  -4.801  1.00 34.63           O  
ANISOU 1454  OD1 ASN A 214     4974   4177   4006    253    250    291       O  
ATOM   1455  N   ILE A 215      17.145   5.352  -4.441  1.00 20.06           N  
ANISOU 1455  N   ILE A 215     2883   2602   2137    382    410    335       N  
ATOM   1456  CA  ILE A 215      17.128   6.462  -5.380  1.00 21.89           C  
ANISOU 1456  CA  ILE A 215     3098   2823   2396    431    438    282       C  
ATOM   1457  C   ILE A 215      18.465   6.493  -6.119  1.00 25.55           C  
ANISOU 1457  C   ILE A 215     3648   3152   2910    441    427    178       C  
ATOM   1458  O   ILE A 215      19.526   6.443  -5.490  1.00 29.10           O  
ANISOU 1458  O   ILE A 215     4138   3552   3366    491    433    110       O  
ATOM   1459  CB  ILE A 215      16.994   7.804  -4.637  1.00 27.69           C  
ANISOU 1459  CB  ILE A 215     3779   3635   3108    560    486    250       C  
ATOM   1460  CG1 ILE A 215      15.759   7.822  -3.733  1.00 26.40           C  
ANISOU 1460  CG1 ILE A 215     3511   3650   2871    584    500    340       C  
ATOM   1461  CG2 ILE A 215      16.947   8.950  -5.630  1.00 25.53           C  
ANISOU 1461  CG2 ILE A 215     3513   3332   2855    600    492    203       C  
ATOM   1462  CD1 ILE A 215      14.474   8.033  -4.487  1.00 30.44           C  
ANISOU 1462  CD1 ILE A 215     3949   4270   3347    549    496    408       C  
ATOM   1463  N   ASP A 216      18.419   6.566  -7.446  1.00 25.99           N  
ANISOU 1463  N   ASP A 216     3721   3166   2990    396    411    164       N  
ATOM   1464  CA  ASP A 216      19.627   6.724  -8.244  1.00 18.78           C  
ANISOU 1464  CA  ASP A 216     2863   2169   2105    407    403     70       C  
ATOM   1465  C   ASP A 216      19.366   7.739  -9.363  1.00 24.47           C  
ANISOU 1465  C   ASP A 216     3562   2895   2839    402    418     60       C  
ATOM   1466  O   ASP A 216      18.235   7.856  -9.846  1.00 23.15           O  
ANISOU 1466  O   ASP A 216     3358   2771   2668    370    416    124       O  
ATOM   1467  CB  ASP A 216      20.068   5.386  -8.835  1.00 19.00           C  
ANISOU 1467  CB  ASP A 216     2957   2129   2134    352    341     55       C  
ATOM   1468  CG  ASP A 216      21.514   5.412  -9.370  1.00 24.41           C  
ANISOU 1468  CG  ASP A 216     3685   2770   2821    390    333    -57       C  
ATOM   1469  OD1 ASP A 216      21.974   4.370  -9.888  1.00 25.54           O  
ANISOU 1469  OD1 ASP A 216     3887   2867   2951    378    272    -91       O  
ATOM   1470  OD2 ASP A 216      22.199   6.458  -9.271  1.00 18.02           O1-
ANISOU 1470  OD2 ASP A 216     2853   1980   2015    433    376   -111       O1-
ATOM   1471  N   VAL A 217      20.390   8.485  -9.776  1.00 17.06           N  
ANISOU 1471  N   VAL A 217     2648   1923   1911    424    428    -15       N  
ATOM   1472  CA  VAL A 217      20.193   9.346 -10.938  1.00 26.25           C  
ANISOU 1472  CA  VAL A 217     3807   3083   3084    398    429    -17       C  
ATOM   1473  C   VAL A 217      20.237   8.472 -12.167  1.00 24.45           C  
ANISOU 1473  C   VAL A 217     3591   2835   2863    333    398    -18       C  
ATOM   1474  O   VAL A 217      20.914   7.438 -12.189  1.00 24.59           O  
ANISOU 1474  O   VAL A 217     3639   2830   2874    326    370    -53       O  
ATOM   1475  CB  VAL A 217      21.183  10.526 -11.040  1.00 19.74           C  
ANISOU 1475  CB  VAL A 217     3006   2238   2255    416    436    -77       C  
ATOM   1476  CG1 VAL A 217      20.913  11.526  -9.917  1.00 20.14           C  
ANISOU 1476  CG1 VAL A 217     3061   2296   2297    494    446    -74       C  
ATOM   1477  CG2 VAL A 217      22.593  10.040 -10.972  1.00 26.72           C  
ANISOU 1477  CG2 VAL A 217     3908   3116   3129    409    432   -147       C  
ATOM   1478  N   SER A 218      19.473   8.864 -13.175  1.00 23.77           N  
ANISOU 1478  N   SER A 218     3488   2758   2785    298    394     18       N  
ATOM   1479  CA  SER A 218      19.382   8.067 -14.387  1.00 19.91           C  
ANISOU 1479  CA  SER A 218     3010   2253   2302    242    361     21       C  
ATOM   1480  C   SER A 218      19.296   8.951 -15.619  1.00 21.50           C  
ANISOU 1480  C   SER A 218     3201   2459   2507    216    366     16       C  
ATOM   1481  O   SER A 218      18.970  10.140 -15.524  1.00 19.90           O  
ANISOU 1481  O   SER A 218     2993   2265   2305    234    386     29       O  
ATOM   1482  CB  SER A 218      18.168   7.136 -14.327  1.00 25.52           C  
ANISOU 1482  CB  SER A 218     3710   2971   3016    202    334    100       C  
ATOM   1483  OG  SER A 218      18.320   6.067 -15.254  1.00 38.90           O  
ANISOU 1483  OG  SER A 218     5442   4625   4712    159    277     90       O  
ATOM   1484  N   ALA A 219      19.584   8.352 -16.771  1.00 19.07           N  
ANISOU 1484  N   ALA A 219     2903   2145   2198    180    337     -5       N  
ATOM   1485  CA  ALA A 219      19.488   9.021 -18.067  1.00 25.80           C  
ANISOU 1485  CA  ALA A 219     3744   3009   3049    144    337     -4       C  
ATOM   1486  C   ALA A 219      19.130   7.975 -19.108  1.00 31.02           C  
ANISOU 1486  C   ALA A 219     4410   3663   3715    116    296      3       C  
ATOM   1487  O   ALA A 219      19.716   6.904 -19.116  1.00 33.75           O  
ANISOU 1487  O   ALA A 219     4781   3997   4045    132    257    -36       O  
ATOM   1488  CB  ALA A 219      20.810   9.680 -18.424  1.00 19.98           C  
ANISOU 1488  CB  ALA A 219     3008   2302   2284    135    345    -64       C  
ATOM   1489  N   THR A 220      18.165   8.272 -19.971  1.00 28.69           N  
ANISOU 1489  N   THR A 220     4099   3368   3434     83    295     49       N  
ATOM   1490  CA  THR A 220      17.772   7.329 -21.012  1.00 24.38           C  
ANISOU 1490  CA  THR A 220     3562   2810   2893     56    249     58       C  
ATOM   1491  C   THR A 220      17.525   8.069 -22.328  1.00 24.45           C  
ANISOU 1491  C   THR A 220     3551   2838   2902     29    258     64       C  
ATOM   1492  O   THR A 220      17.406   9.301 -22.348  1.00 23.72           O  
ANISOU 1492  O   THR A 220     3446   2757   2808     25    293     76       O  
ATOM   1493  CB  THR A 220      16.556   6.439 -20.582  1.00 29.00           C  
ANISOU 1493  CB  THR A 220     4152   3372   3493     26    218    132       C  
ATOM   1494  CG2 THR A 220      15.290   7.234 -20.511  1.00 27.31           C  
ANISOU 1494  CG2 THR A 220     3892   3197   3288     10    253    202       C  
ATOM   1495  OG1 THR A 220      16.369   5.379 -21.521  1.00 32.70           O  
ANISOU 1495  OG1 THR A 220     4654   3807   3962     -2    149    132       O  
ATOM   1496  N   ALA A 221      17.509   7.324 -23.429  1.00 28.15           N  
ANISOU 1496  N   ALA A 221     4026   3304   3366     16    216     49       N  
ATOM   1497  CA  ALA A 221      17.310   7.919 -24.749  1.00 19.30           C  
ANISOU 1497  CA  ALA A 221     2885   2207   2241     -9    221     53       C  
ATOM   1498  C   ALA A 221      15.831   7.994 -25.096  1.00 19.36           C  
ANISOU 1498  C   ALA A 221     2882   2195   2279    -37    220    123       C  
ATOM   1499  O   ALA A 221      15.087   7.031 -24.920  1.00 21.87           O  
ANISOU 1499  O   ALA A 221     3210   2489   2612    -52    183    160       O  
ATOM   1500  CB  ALA A 221      18.060   7.145 -25.788  1.00 17.58           C  
ANISOU 1500  CB  ALA A 221     2671   2017   1992      8    175     -5       C  
ATOM   1501  N   PHE A 222      15.415   9.166 -25.567  1.00 20.00           N  
ANISOU 1501  N   PHE A 222     2948   2290   2361    -48    251    144       N  
ATOM   1502  CA  PHE A 222      14.058   9.399 -26.057  1.00 20.22           C  
ANISOU 1502  CA  PHE A 222     2959   2320   2404    -61    251    199       C  
ATOM   1503  C   PHE A 222      14.157   9.879 -27.505  1.00 26.63           C  
ANISOU 1503  C   PHE A 222     3770   3138   3210    -82    245    186       C  
ATOM   1504  O   PHE A 222      15.203  10.368 -27.929  1.00 25.22           O  
ANISOU 1504  O   PHE A 222     3599   2976   3007    -92    250    147       O  
ATOM   1505  CB  PHE A 222      13.377  10.499 -25.242  1.00 20.74           C  
ANISOU 1505  CB  PHE A 222     3018   2401   2463    -29    284    229       C  
ATOM   1506  CG  PHE A 222      12.739  10.021 -23.959  1.00 31.80           C  
ANISOU 1506  CG  PHE A 222     4393   3830   3861     -9    291    266       C  
ATOM   1507  CD1 PHE A 222      11.360  10.008 -23.823  1.00 30.95           C  
ANISOU 1507  CD1 PHE A 222     4239   3778   3740     -5    293    325       C  
ATOM   1508  CD2 PHE A 222      13.516   9.610 -22.885  1.00 33.70           C  
ANISOU 1508  CD2 PHE A 222     4646   4059   4101      4    295    246       C  
ATOM   1509  CE1 PHE A 222      10.760   9.584 -22.652  1.00 32.75           C  
ANISOU 1509  CE1 PHE A 222     4427   4066   3949      2    299    370       C  
ATOM   1510  CE2 PHE A 222      12.920   9.185 -21.705  1.00 31.05           C  
ANISOU 1510  CE2 PHE A 222     4282   3760   3754     15    300    288       C  
ATOM   1511  CZ  PHE A 222      11.541   9.168 -21.590  1.00 33.26           C  
ANISOU 1511  CZ  PHE A 222     4510   4112   4016      9    302    354       C  
ATOM   1512  N   TYR A 223      13.064   9.764 -28.254  1.00 26.60           N  
ANISOU 1512  N   TYR A 223     3752   3136   3219    -95    234    223       N  
ATOM   1513  CA  TYR A 223      13.019  10.334 -29.584  1.00 26.73           C  
ANISOU 1513  CA  TYR A 223     3770   3159   3229   -111    231    216       C  
ATOM   1514  C   TYR A 223      12.704  11.811 -29.499  1.00 22.34           C  
ANISOU 1514  C   TYR A 223     3234   2597   2657    -99    253    231       C  
ATOM   1515  O   TYR A 223      11.793  12.229 -28.779  1.00 25.22           O  
ANISOU 1515  O   TYR A 223     3597   2967   3020    -62    263    259       O  
ATOM   1516  CB  TYR A 223      11.990   9.619 -30.455  1.00 26.65           C  
ANISOU 1516  CB  TYR A 223     3742   3148   3237   -125    204    245       C  
ATOM   1517  CG  TYR A 223      12.369   8.191 -30.733  1.00 26.65           C  
ANISOU 1517  CG  TYR A 223     3751   3131   3243   -132    153    223       C  
ATOM   1518  CD1 TYR A 223      13.357   7.890 -31.659  1.00 25.39           C  
ANISOU 1518  CD1 TYR A 223     3599   2988   3062   -119    128    167       C  
ATOM   1519  CD2 TYR A 223      11.761   7.141 -30.055  1.00 24.17           C  
ANISOU 1519  CD2 TYR A 223     3445   2794   2944   -150    116    259       C  
ATOM   1520  CE1 TYR A 223      13.727   6.595 -31.909  1.00 24.10           C  
ANISOU 1520  CE1 TYR A 223     3460   2806   2891    -96     61    132       C  
ATOM   1521  CE2 TYR A 223      12.122   5.825 -30.309  1.00 26.21           C  
ANISOU 1521  CE2 TYR A 223     3744   3013   3202   -152     41    235       C  
ATOM   1522  CZ  TYR A 223      13.104   5.562 -31.234  1.00 27.06           C  
ANISOU 1522  CZ  TYR A 223     3870   3126   3288   -112     11    164       C  
ATOM   1523  OH  TYR A 223      13.471   4.262 -31.493  1.00 36.57           O  
ANISOU 1523  OH  TYR A 223     5129   4288   4478    -85    -82    127       O  
ATOM   1524  N   LYS A 224      13.505  12.596 -30.206  1.00 24.78           N  
ANISOU 1524  N   LYS A 224     3568   2906   2942   -129    249    212       N  
ATOM   1525  CA  LYS A 224      13.231  14.009 -30.421  1.00 23.26           C  
ANISOU 1525  CA  LYS A 224     3425   2685   2728   -131    241    228       C  
ATOM   1526  C   LYS A 224      11.848  14.145 -31.032  1.00 18.03           C  
ANISOU 1526  C   LYS A 224     2756   2019   2074   -101    235    255       C  
ATOM   1527  O   LYS A 224      11.488  13.400 -31.931  1.00 32.24           O  
ANISOU 1527  O   LYS A 224     4520   3839   3890   -118    232    261       O  
ATOM   1528  CB  LYS A 224      14.268  14.597 -31.386  1.00 24.49           C  
ANISOU 1528  CB  LYS A 224     3601   2856   2849   -203    225    220       C  
ATOM   1529  CG  LYS A 224      15.693  14.586 -30.847  1.00 35.50           C  
ANISOU 1529  CG  LYS A 224     4989   4283   4215   -241    230    195       C  
ATOM   1530  CD  LYS A 224      16.729  14.622 -31.967  1.00 42.84           C  
ANISOU 1530  CD  LYS A 224     5888   5293   5096   -316    220    187       C  
ATOM   1531  CE  LYS A 224      17.104  16.040 -32.374  1.00 41.45           C  
ANISOU 1531  CE  LYS A 224     5774   5103   4874   -402    188    224       C  
ATOM   1532  NZ  LYS A 224      18.442  16.046 -33.029  1.00 39.85           N1+
ANISOU 1532  NZ  LYS A 224     5519   5021   4602   -492    183    221       N1+
ATOM   1533  N   ALA A 225      11.072  15.089 -30.531  1.00 18.31           N  
ANISOU 1533  N   ALA A 225     2830   2036   2091    -45    224    266       N  
ATOM   1534  CA  ALA A 225       9.814  15.450 -31.147  1.00 25.80           C  
ANISOU 1534  CA  ALA A 225     3778   2995   3029     -3    212    283       C  
ATOM   1535  C   ALA A 225      10.138  16.395 -32.312  1.00 28.43           C  
ANISOU 1535  C   ALA A 225     4179   3281   3340    -43    180    281       C  
ATOM   1536  O   ALA A 225      10.584  17.524 -32.108  1.00 33.73           O  
ANISOU 1536  O   ALA A 225     4939   3898   3980    -45    142    276       O  
ATOM   1537  CB  ALA A 225       8.918  16.136 -30.135  1.00 28.65           C  
ANISOU 1537  CB  ALA A 225     4155   3376   3356     97    203    283       C  
ATOM   1538  N   GLN A 226       9.938  15.915 -33.534  1.00 21.50           N  
ANISOU 1538  N   GLN A 226     3269   2423   2478    -81    184    289       N  
ATOM   1539  CA  GLN A 226      10.311  16.659 -34.722  1.00 23.88           C  
ANISOU 1539  CA  GLN A 226     3621   2697   2755   -134    156    295       C  
ATOM   1540  C   GLN A 226       9.512  16.063 -35.873  1.00 23.59           C  
ANISOU 1540  C   GLN A 226     3536   2691   2737   -131    164    303       C  
ATOM   1541  O   GLN A 226       8.945  14.976 -35.737  1.00 19.32           O  
ANISOU 1541  O   GLN A 226     2924   2188   2229   -109    186    305       O  
ATOM   1542  CB  GLN A 226      11.816  16.534 -34.975  1.00 21.32           C  
ANISOU 1542  CB  GLN A 226     3290   2394   2417   -225    158    289       C  
ATOM   1543  CG  GLN A 226      12.266  15.107 -35.264  1.00 23.36           C  
ANISOU 1543  CG  GLN A 226     3458   2718   2700   -238    188    270       C  
ATOM   1544  CD  GLN A 226      13.766  15.002 -35.501  1.00 26.35           C  
ANISOU 1544  CD  GLN A 226     3814   3157   3042   -305    188    254       C  
ATOM   1545  NE2 GLN A 226      14.322  13.812 -35.300  1.00 23.11           N  
ANISOU 1545  NE2 GLN A 226     3343   2799   2640   -285    201    220       N  
ATOM   1546  OE1 GLN A 226      14.415  15.982 -35.850  1.00 29.60           O  
ANISOU 1546  OE1 GLN A 226     4265   3575   3407   -375    166    273       O  
ATOM   1547  N   PRO A 227       9.431  16.779 -37.001  1.00 18.98           N  
ANISOU 1547  N   PRO A 227     2996   2086   2130   -158    138    312       N  
ATOM   1548  CA  PRO A 227       8.653  16.177 -38.097  1.00 18.86           C  
ANISOU 1548  CA  PRO A 227     2931   2100   2134   -148    146    316       C  
ATOM   1549  C   PRO A 227       9.270  14.862 -38.585  1.00 18.52           C  
ANISOU 1549  C   PRO A 227     2811   2109   2118   -186    165    304       C  
ATOM   1550  O   PRO A 227      10.475  14.620 -38.441  1.00 18.47           O  
ANISOU 1550  O   PRO A 227     2791   2128   2098   -229    169    290       O  
ATOM   1551  CB  PRO A 227       8.663  17.251 -39.196  1.00 19.24           C  
ANISOU 1551  CB  PRO A 227     3051   2115   2145   -179    111    329       C  
ATOM   1552  CG  PRO A 227       9.416  18.425 -38.664  1.00 21.06           C  
ANISOU 1552  CG  PRO A 227     3381   2288   2333   -216     71    338       C  
ATOM   1553  CD  PRO A 227       9.726  18.206 -37.214  1.00 19.51           C  
ANISOU 1553  CD  PRO A 227     3174   2089   2148   -185     87    324       C  
ATOM   1554  N   VAL A 228       8.431  13.996 -39.134  1.00 18.40           N  
ANISOU 1554  N   VAL A 228     2747   2113   2133   -163    166    306       N  
ATOM   1555  CA  VAL A 228       8.892  12.696 -39.590  1.00 18.78           C  
ANISOU 1555  CA  VAL A 228     2744   2193   2201   -177    158    288       C  
ATOM   1556  C   VAL A 228       9.978  12.809 -40.672  1.00 18.34           C  
ANISOU 1556  C   VAL A 228     2680   2180   2110   -212    149    267       C  
ATOM   1557  O   VAL A 228      10.922  12.002 -40.724  1.00 18.34           O  
ANISOU 1557  O   VAL A 228     2648   2226   2097   -213    140    235       O  
ATOM   1558  CB  VAL A 228       7.708  11.792 -40.006  1.00 18.24           C  
ANISOU 1558  CB  VAL A 228     2640   2125   2166   -156    142    301       C  
ATOM   1559  CG1 VAL A 228       8.208  10.596 -40.781  1.00 18.24           C  
ANISOU 1559  CG1 VAL A 228     2616   2139   2175   -160    107    274       C  
ATOM   1560  CG2 VAL A 228       6.925  11.334 -38.731  1.00 18.29           C  
ANISOU 1560  CG2 VAL A 228     2627   2132   2190   -144    147    328       C  
ATOM   1561  N   ILE A 229       9.880  13.845 -41.495  1.00 18.56           N  
ANISOU 1561  N   ILE A 229     2739   2205   2108   -238    146    285       N  
ATOM   1562  CA  ILE A 229      10.880  14.049 -42.545  1.00 21.71           C  
ANISOU 1562  CA  ILE A 229     3119   2674   2456   -288    137    280       C  
ATOM   1563  C   ILE A 229      12.255  14.369 -41.977  1.00 22.31           C  
ANISOU 1563  C   ILE A 229     3191   2801   2484   -342    142    277       C  
ATOM   1564  O   ILE A 229      13.274  13.925 -42.520  1.00 24.65           O  
ANISOU 1564  O   ILE A 229     3429   3204   2733   -361    139    255       O  
ATOM   1565  CB  ILE A 229      10.424  15.117 -43.567  1.00 21.63           C  
ANISOU 1565  CB  ILE A 229     3153   2646   2419   -319    124    312       C  
ATOM   1566  CG1 ILE A 229       9.247  14.555 -44.352  1.00 18.95           C  
ANISOU 1566  CG1 ILE A 229     2791   2289   2118   -262    120    305       C  
ATOM   1567  CG2 ILE A 229      11.564  15.525 -44.490  1.00 20.58           C  
ANISOU 1567  CG2 ILE A 229     2999   2605   2214   -398    113    325       C  
ATOM   1568  CD1 ILE A 229       9.024  15.187 -45.685  1.00 27.42           C  
ANISOU 1568  CD1 ILE A 229     3881   3376   3161   -285    106    322       C  
ATOM   1569  N   GLU A 230      12.291  15.120 -40.876  1.00 21.81           N  
ANISOU 1569  N   GLU A 230     3186   2677   2425   -359    145    294       N  
ATOM   1570  CA  GLU A 230      13.565  15.431 -40.222  1.00 23.92           C  
ANISOU 1570  CA  GLU A 230     3452   2988   2649   -417    146    294       C  
ATOM   1571  C   GLU A 230      14.130  14.216 -39.493  1.00 21.86           C  
ANISOU 1571  C   GLU A 230     3130   2771   2404   -369    164    247       C  
ATOM   1572  O   GLU A 230      15.331  13.977 -39.503  1.00 23.21           O  
ANISOU 1572  O   GLU A 230     3254   3041   2523   -397    165    226       O  
ATOM   1573  CB  GLU A 230      13.411  16.595 -39.250  1.00 33.39           C  
ANISOU 1573  CB  GLU A 230     4746   4094   3846   -439    129    321       C  
ATOM   1574  CG  GLU A 230      12.950  17.870 -39.908  1.00 52.84           C  
ANISOU 1574  CG  GLU A 230     7302   6496   6280   -482     86    363       C  
ATOM   1575  CD  GLU A 230      12.918  19.029 -38.938  1.00 71.41           C  
ANISOU 1575  CD  GLU A 230     9769   8747   8615   -492     43    381       C  
ATOM   1576  OE1 GLU A 230      13.457  18.880 -37.812  1.00 72.97           O  
ANISOU 1576  OE1 GLU A 230     9961   8943   8820   -484     55    366       O  
ATOM   1577  OE2 GLU A 230      12.350  20.084 -39.304  1.00 77.31           O1-
ANISOU 1577  OE2 GLU A 230    10623   9413   9339   -497    -12    406       O1-
ATOM   1578  N   PHE A 231      13.254  13.468 -38.840  1.00 18.56           N  
ANISOU 1578  N   PHE A 231     2714   2289   2048   -299    170    234       N  
ATOM   1579  CA  PHE A 231      13.620  12.177 -38.289  1.00 19.30           C  
ANISOU 1579  CA  PHE A 231     2769   2406   2158   -252    167    194       C  
ATOM   1580  C   PHE A 231      14.270  11.356 -39.394  1.00 20.69           C  
ANISOU 1580  C   PHE A 231     2892   2675   2295   -232    143    153       C  
ATOM   1581  O   PHE A 231      15.410  10.919 -39.249  1.00 21.41           O  
ANISOU 1581  O   PHE A 231     2946   2851   2337   -219    136    111       O  
ATOM   1582  CB  PHE A 231      12.374  11.461 -37.757  1.00 18.11           C  
ANISOU 1582  CB  PHE A 231     2629   2181   2071   -205    162    206       C  
ATOM   1583  CG  PHE A 231      12.633  10.067 -37.245  1.00 24.63           C  
ANISOU 1583  CG  PHE A 231     3441   3005   2912   -168    136    173       C  
ATOM   1584  CD1 PHE A 231      13.084   9.858 -35.951  1.00 23.48           C  
ANISOU 1584  CD1 PHE A 231     3307   2844   2772   -161    145    165       C  
ATOM   1585  CD2 PHE A 231      12.395   8.958 -38.047  1.00 25.97           C  
ANISOU 1585  CD2 PHE A 231     3602   3178   3090   -137     88    151       C  
ATOM   1586  CE1 PHE A 231      13.308   8.566 -35.474  1.00 22.62           C  
ANISOU 1586  CE1 PHE A 231     3205   2720   2672   -128    105    136       C  
ATOM   1587  CE2 PHE A 231      12.617   7.659 -37.568  1.00 25.39           C  
ANISOU 1587  CE2 PHE A 231     3545   3080   3023   -101     36    121       C  
ATOM   1588  CZ  PHE A 231      13.074   7.466 -36.280  1.00 19.84           C  
ANISOU 1588  CZ  PHE A 231     2858   2357   2322    -99     44    115       C  
ATOM   1589  N   MET A 232      13.550  11.174 -40.504  1.00 20.91           N  
ANISOU 1589  N   MET A 232     2912   2700   2335   -217    128    160       N  
ATOM   1590  CA  MET A 232      14.078  10.401 -41.634  1.00 18.96           C  
ANISOU 1590  CA  MET A 232     2615   2546   2043   -177     95    115       C  
ATOM   1591  C   MET A 232      15.445  10.895 -42.116  1.00 23.80           C  
ANISOU 1591  C   MET A 232     3172   3310   2559   -215    104    101       C  
ATOM   1592  O   MET A 232      16.351  10.099 -42.355  1.00 22.90           O  
ANISOU 1592  O   MET A 232     3007   3309   2386   -158     79     42       O  
ATOM   1593  CB  MET A 232      13.117  10.406 -42.817  1.00 18.97           C  
ANISOU 1593  CB  MET A 232     2617   2524   2065   -167     81    132       C  
ATOM   1594  CG  MET A 232      13.594   9.503 -43.946  1.00 22.49           C  
ANISOU 1594  CG  MET A 232     3017   3064   2465   -103     37     78       C  
ATOM   1595  SD  MET A 232      12.636   9.680 -45.461  1.00 24.80           S  
ANISOU 1595  SD  MET A 232     3303   3350   2770    -97     24     98       S  
ATOM   1596  CE  MET A 232      13.242  11.275 -45.997  1.00 19.68           C  
ANISOU 1596  CE  MET A 232     2634   2791   2054   -198     71    148       C  
ATOM   1597  N   CYS A 233      15.599  12.204 -42.257  1.00 19.61           N  
ANISOU 1597  N   CYS A 233     2656   2794   2002   -310    129    156       N  
ATOM   1598  CA  CYS A 233      16.881  12.738 -42.708  1.00 25.47           C  
ANISOU 1598  CA  CYS A 233     3339   3700   2639   -380    133    163       C  
ATOM   1599  C   CYS A 233      18.023  12.433 -41.745  1.00 33.19           C  
ANISOU 1599  C   CYS A 233     4283   4756   3574   -375    139    127       C  
ATOM   1600  O   CYS A 233      19.118  12.080 -42.181  1.00 36.03           O  
ANISOU 1600  O   CYS A 233     4555   5300   3836   -363    130     90       O  
ATOM   1601  CB  CYS A 233      16.790  14.236 -42.991  1.00 25.95           C  
ANISOU 1601  CB  CYS A 233     3449   3736   2676   -507    136    242       C  
ATOM   1602  SG  CYS A 233      15.911  14.588 -44.534  1.00 33.97           S  
ANISOU 1602  SG  CYS A 233     4473   4742   3691   -518    122    275       S  
ATOM   1603  N   GLU A 234      17.764  12.546 -40.443  1.00 28.41           N  
ANISOU 1603  N   GLU A 234     3738   4027   3031   -373    152    134       N  
ATOM   1604  CA  GLU A 234      18.752  12.156 -39.451  1.00 26.65           C  
ANISOU 1604  CA  GLU A 234     3489   3861   2777   -353    158     94       C  
ATOM   1605  C   GLU A 234      19.144  10.684 -39.609  1.00 26.20           C  
ANISOU 1605  C   GLU A 234     3383   3876   2696   -228    128      8       C  
ATOM   1606  O   GLU A 234      20.330  10.362 -39.622  1.00 33.67           O  
ANISOU 1606  O   GLU A 234     4259   4983   3549   -203    120    -41       O  
ATOM   1607  CB  GLU A 234      18.258  12.408 -38.009  1.00 28.09           C  
ANISOU 1607  CB  GLU A 234     3747   3888   3038   -353    174    111       C  
ATOM   1608  CG  GLU A 234      18.218  13.865 -37.566  1.00 31.97           C  
ANISOU 1608  CG  GLU A 234     4301   4319   3529   -455    182    176       C  
ATOM   1609  CD  GLU A 234      18.116  14.013 -36.037  1.00 37.71           C  
ANISOU 1609  CD  GLU A 234     5081   4944   4303   -434    194    174       C  
ATOM   1610  OE1 GLU A 234      18.829  13.283 -35.312  1.00 33.15           O  
ANISOU 1610  OE1 GLU A 234     4468   4412   3714   -393    203    129       O  
ATOM   1611  OE2 GLU A 234      17.328  14.857 -35.561  1.00 39.25           O1-
ANISOU 1611  OE2 GLU A 234     5355   5020   4539   -447    189    213       O1-
ATOM   1612  N   VAL A 235      18.169   9.782 -39.716  1.00 24.48           N  
ANISOU 1612  N   VAL A 235     3206   3546   2548   -148    100    -13       N  
ATOM   1613  CA  VAL A 235      18.525   8.357 -39.719  1.00 27.08           C  
ANISOU 1613  CA  VAL A 235     3527   3907   2855    -25     44    -97       C  
ATOM   1614  C   VAL A 235      19.155   7.902 -41.040  1.00 26.84           C  
ANISOU 1614  C   VAL A 235     3424   4047   2726     42      5   -153       C  
ATOM   1615  O   VAL A 235      19.862   6.904 -41.076  1.00 31.74           O  
ANISOU 1615  O   VAL A 235     4026   4752   3283    157    -49   -238       O  
ATOM   1616  CB  VAL A 235      17.356   7.412 -39.329  1.00 30.57           C  
ANISOU 1616  CB  VAL A 235     4049   4173   3392     26      2    -96       C  
ATOM   1617  CG1 VAL A 235      16.611   7.928 -38.090  1.00 29.42           C  
ANISOU 1617  CG1 VAL A 235     3956   3893   3329    -38     44    -33       C  
ATOM   1618  CG2 VAL A 235      16.419   7.220 -40.474  1.00 28.74           C  
ANISOU 1618  CG2 VAL A 235     3826   3906   3189     37    -25    -79       C  
ATOM   1619  N   LEU A 236      18.912   8.646 -42.111  1.00 25.99           N  
ANISOU 1619  N   LEU A 236     3279   3998   2597    -19     27   -108       N  
ATOM   1620  CA  LEU A 236      19.471   8.308 -43.426  1.00 30.34           C  
ANISOU 1620  CA  LEU A 236     3747   4734   3045     43     -5   -154       C  
ATOM   1621  C   LEU A 236      20.636   9.217 -43.795  1.00 34.45           C  
ANISOU 1621  C   LEU A 236     4163   5485   3442    -44     32   -129       C  
ATOM   1622  O   LEU A 236      21.235   9.051 -44.854  1.00 34.45           O  
ANISOU 1622  O   LEU A 236     4069   5691   3330     -3     13   -161       O  
ATOM   1623  CB  LEU A 236      18.391   8.392 -44.510  1.00 25.89           C  
ANISOU 1623  CB  LEU A 236     3207   4100   2532     39    -16   -121       C  
ATOM   1624  CG  LEU A 236      17.634   7.119 -44.906  1.00 28.88           C  
ANISOU 1624  CG  LEU A 236     3639   4377   2958    165    -92   -177       C  
ATOM   1625  CD1 LEU A 236      17.700   6.062 -43.841  1.00 26.33           C  
ANISOU 1625  CD1 LEU A 236     3383   3953   2668    243   -145   -230       C  
ATOM   1626  CD2 LEU A 236      16.185   7.419 -45.259  1.00 27.21           C  
ANISOU 1626  CD2 LEU A 236     3486   4001   2852    113    -80   -112       C  
ATOM   1627  N   ASP A 237      20.952  10.173 -42.917  1.00 35.73           N  
ANISOU 1627  N   ASP A 237     4341   5621   3615   -168     78    -69       N  
ATOM   1628  CA  ASP A 237      22.038  11.135 -43.156  1.00 40.31           C  
ANISOU 1628  CA  ASP A 237     4834   6407   4075   -292    103    -24       C  
ATOM   1629  C   ASP A 237      21.845  11.864 -44.486  1.00 38.48           C  
ANISOU 1629  C   ASP A 237     4562   6266   3793   -380    106     40       C  
ATOM   1630  O   ASP A 237      22.705  11.838 -45.356  1.00 36.80           O  
ANISOU 1630  O   ASP A 237     4230   6311   3443   -386     97     29       O  
ATOM   1631  CB  ASP A 237      23.405  10.442 -43.119  1.00 47.68           C  
ANISOU 1631  CB  ASP A 237     5650   7596   4869   -208     86   -107       C  
ATOM   1632  CG  ASP A 237      24.558  11.417 -42.931  1.00 66.54           C  
ANISOU 1632  CG  ASP A 237     7954  10188   7142   -359    113    -51       C  
ATOM   1633  OD1 ASP A 237      24.577  12.485 -43.580  1.00 76.52           O  
ANISOU 1633  OD1 ASP A 237     9198  11512   8364   -520    126     45       O  
ATOM   1634  OD2 ASP A 237      25.458  11.110 -42.121  1.00 74.50           O1-
ANISOU 1634  OD2 ASP A 237     8919  11293   8092   -325    115    -99       O1-
ATOM   1635  N   ILE A 238      20.702  12.513 -44.634  1.00 35.52           N  
ANISOU 1635  N   ILE A 238     4284   5692   3519   -442    114    105       N  
ATOM   1636  CA  ILE A 238      20.417  13.285 -45.830  1.00 37.48           C  
ANISOU 1636  CA  ILE A 238     4519   5991   3730   -532    112    172       C  
ATOM   1637  C   ILE A 238      20.511  14.753 -45.443  1.00 41.63           C  
ANISOU 1637  C   ILE A 238     5114   6455   4250   -721    117    277       C  
ATOM   1638  O   ILE A 238      19.778  15.212 -44.557  1.00 42.54           O  
ANISOU 1638  O   ILE A 238     5347   6348   4467   -738    120    301       O  
ATOM   1639  CB  ILE A 238      19.010  12.964 -46.360  1.00 31.82           C  
ANISOU 1639  CB  ILE A 238     3875   5094   3123   -456    103    165       C  
ATOM   1640  CG1 ILE A 238      18.942  11.501 -46.805  1.00 29.42           C  
ANISOU 1640  CG1 ILE A 238     3522   4840   2816   -279     72     65       C  
ATOM   1641  CG2 ILE A 238      18.640  13.910 -47.496  1.00 29.95           C  
ANISOU 1641  CG2 ILE A 238     3645   4878   2855   -557    100    240       C  
ATOM   1642  CD1 ILE A 238      17.541  11.031 -47.170  1.00 26.05           C  
ANISOU 1642  CD1 ILE A 238     3170   4225   2502   -206     55     57       C  
ATOM   1643  N   ARG A 239      21.414  15.488 -46.087  1.00 35.70           N  
ANISOU 1643  N   ARG A 239     4291   5905   3369   -861    108    339       N  
ATOM   1644  CA  ARG A 239      21.697  16.858 -45.666  1.00 40.00           C  
ANISOU 1644  CA  ARG A 239     4912   6398   3887  -1058     88    443       C  
ATOM   1645  C   ARG A 239      20.730  17.889 -46.251  1.00 37.15           C  
ANISOU 1645  C   ARG A 239     4677   5868   3571  -1148     56    524       C  
ATOM   1646  O   ARG A 239      20.516  18.955 -45.665  1.00 34.33           O  
ANISOU 1646  O   ARG A 239     4452   5352   3241  -1258     21    590       O  
ATOM   1647  CB  ARG A 239      23.154  17.231 -45.964  1.00 44.38           C  
ANISOU 1647  CB  ARG A 239     5341   7252   4270  -1201     78    490       C  
ATOM   1648  CG  ARG A 239      24.151  16.681 -44.941  1.00 54.51           C  
ANISOU 1648  CG  ARG A 239     6550   8651   5512  -1158     97    431       C  
ATOM   1649  CD  ARG A 239      25.545  17.281 -45.113  1.00 65.95           C  
ANISOU 1649  CD  ARG A 239     7883  10393   6783  -1337     82    499       C  
ATOM   1650  NE  ARG A 239      26.441  16.895 -44.024  1.00 76.92           N  
ANISOU 1650  NE  ARG A 239     9218  11868   8139  -1305     98    446       N  
ATOM   1651  CZ  ARG A 239      26.724  17.661 -42.973  1.00 85.48           C  
ANISOU 1651  CZ  ARG A 239    10388  12843   9248  -1428     82    499       C  
ATOM   1652  NH1 ARG A 239      26.191  18.872 -42.865  1.00 86.87           N1+
ANISOU 1652  NH1 ARG A 239    10719  12813   9475  -1589     37    603       N1+
ATOM   1653  NH2 ARG A 239      27.547  17.220 -42.028  1.00 88.11           N  
ANISOU 1653  NH2 ARG A 239    10662  13269   9549  -1383    100    442       N  
ATOM   1654  N   ASN A 240      20.138  17.551 -47.393  1.00 26.16           N  
ANISOU 1654  N   ASN A 240     3253   4504   2183  -1086     60    511       N  
ATOM   1655  CA  ASN A 240      19.243  18.446 -48.108  1.00 25.00           C  
ANISOU 1655  CA  ASN A 240     3213   4220   2064  -1156     29    579       C  
ATOM   1656  C   ASN A 240      18.162  17.631 -48.813  1.00 34.85           C  
ANISOU 1656  C   ASN A 240     4451   5399   3392   -994     50    516       C  
ATOM   1657  O   ASN A 240      18.380  17.094 -49.901  1.00 36.01           O  
ANISOU 1657  O   ASN A 240     4490   5716   3477   -953     57    495       O  
ATOM   1658  CB  ASN A 240      20.047  19.277 -49.123  1.00 28.73           C  
ANISOU 1658  CB  ASN A 240     3635   4891   2389  -1345     -6    677       C  
ATOM   1659  CG  ASN A 240      19.202  20.292 -49.856  1.00 30.07           C  
ANISOU 1659  CG  ASN A 240     3937   4913   2575  -1432    -54    754       C  
ATOM   1660  ND2 ASN A 240      19.834  21.065 -50.737  1.00 37.95           N  
ANISOU 1660  ND2 ASN A 240     4909   6067   3443  -1617    -96    854       N  
ATOM   1661  OD1 ASN A 240      17.992  20.390 -49.634  1.00 38.26           O  
ANISOU 1661  OD1 ASN A 240     5097   5711   3730  -1336    -59    727       O  
ATOM   1662  N   ILE A 241      16.989  17.554 -48.198  1.00 33.30           N  
ANISOU 1662  N   ILE A 241     4362   4965   3324   -903     54    488       N  
ATOM   1663  CA  ILE A 241      15.916  16.699 -48.692  1.00 31.05           C  
ANISOU 1663  CA  ILE A 241     4069   4607   3121   -755     70    430       C  
ATOM   1664  C   ILE A 241      15.338  17.230 -50.004  1.00 35.26           C  
ANISOU 1664  C   ILE A 241     4623   5141   3632   -791     51    472       C  
ATOM   1665  O   ILE A 241      14.633  16.521 -50.713  1.00 37.31           O  
ANISOU 1665  O   ILE A 241     4852   5392   3933   -684     59    429       O  
ATOM   1666  CB  ILE A 241      14.804  16.538 -47.620  1.00 25.74           C  
ANISOU 1666  CB  ILE A 241     3493   3713   2575   -667     79    401       C  
ATOM   1667  CG1 ILE A 241      13.807  15.439 -48.002  1.00 23.52           C  
ANISOU 1667  CG1 ILE A 241     3185   3382   2370   -527     90    342       C  
ATOM   1668  CG2 ILE A 241      14.099  17.863 -47.369  1.00 28.12           C  
ANISOU 1668  CG2 ILE A 241     3936   3852   2897   -735     48    461       C  
ATOM   1669  CD1 ILE A 241      14.412  14.046 -48.032  1.00 29.99           C  
ANISOU 1669  CD1 ILE A 241     3904   4316   3175   -433     93    269       C  
ATOM   1670  N   ASP A 242      15.653  18.480 -50.328  1.00 36.10           N  
ANISOU 1670  N   ASP A 242     4792   5255   3668   -947     15    560       N  
ATOM   1671  CA  ASP A 242      15.087  19.124 -51.504  1.00 33.81           C  
ANISOU 1671  CA  ASP A 242     4548   4945   3354   -994    -13    609       C  
ATOM   1672  C   ASP A 242      16.038  19.021 -52.684  1.00 33.86           C  
ANISOU 1672  C   ASP A 242     4422   5211   3231  -1071    -13    641       C  
ATOM   1673  O   ASP A 242      15.713  19.448 -53.775  1.00 34.08           O  
ANISOU 1673  O   ASP A 242     4463   5263   3222  -1114    -33    683       O  
ATOM   1674  CB  ASP A 242      14.793  20.601 -51.229  1.00 38.91           C  
ANISOU 1674  CB  ASP A 242     5368   5428   3989  -1122    -76    691       C  
ATOM   1675  CG  ASP A 242      13.778  20.808 -50.117  1.00 46.56           C  
ANISOU 1675  CG  ASP A 242     6465   6160   5065  -1025    -84    654       C  
ATOM   1676  OD1 ASP A 242      12.784  20.050 -50.045  1.00 47.62           O  
ANISOU 1676  OD1 ASP A 242     6580   6225   5290   -872    -47    588       O  
ATOM   1677  OD2 ASP A 242      13.973  21.747 -49.317  1.00 49.55           O1-
ANISOU 1677  OD2 ASP A 242     6965   6434   5429  -1106   -136    695       O1-
ATOM   1678  N   GLU A 243      17.220  18.466 -52.447  1.00 34.69           N  
ANISOU 1678  N   GLU A 243     4396   5526   3256  -1084      7    620       N  
ATOM   1679  CA  GLU A 243      18.246  18.360 -53.474  1.00 41.02           C  
ANISOU 1679  CA  GLU A 243     5047   6632   3907  -1151      7    649       C  
ATOM   1680  C   GLU A 243      17.815  17.460 -54.636  1.00 46.20           C  
ANISOU 1680  C   GLU A 243     5611   7381   4562  -1002     23    584       C  
ATOM   1681  O   GLU A 243      17.863  17.856 -55.806  1.00 48.42           O  
ANISOU 1681  O   GLU A 243     5851   7783   4762  -1068      8    636       O  
ATOM   1682  CB  GLU A 243      19.531  17.823 -52.848  1.00 47.31           C  
ANISOU 1682  CB  GLU A 243     5715   7643   4618  -1152     25    616       C  
ATOM   1683  CG  GLU A 243      20.693  17.655 -53.806  1.00 56.72           C  
ANISOU 1683  CG  GLU A 243     6719   9206   5624  -1207     25    636       C  
ATOM   1684  CD  GLU A 243      21.492  18.927 -53.988  1.00 71.20           C  
ANISOU 1684  CD  GLU A 243     8555  11170   7328  -1476    -10    778       C  
ATOM   1685  OE1 GLU A 243      20.884  19.976 -54.284  1.00 76.57           O  
ANISOU 1685  OE1 GLU A 243     9377  11680   8037  -1610    -52    871       O  
ATOM   1686  OE2 GLU A 243      22.731  18.881 -53.829  1.00 77.45           O1-
ANISOU 1686  OE2 GLU A 243     9211  12238   7980  -1557     -7    798       O1-
ATOM   1687  N   GLN A 244      17.397  16.246 -54.298  1.00 46.31           N  
ANISOU 1687  N   GLN A 244     5601   7334   4663   -806     43    474       N  
ATOM   1688  CA  GLN A 244      17.034  15.246 -55.289  1.00 46.27           C  
ANISOU 1688  CA  GLN A 244     5519   7404   4658   -646     41    399       C  
ATOM   1689  C   GLN A 244      15.622  14.737 -55.036  1.00 37.38           C  
ANISOU 1689  C   GLN A 244     4499   6009   3694   -522     41    349       C  
ATOM   1690  O   GLN A 244      15.416  13.874 -54.182  1.00 33.65           O  
ANISOU 1690  O   GLN A 244     4046   5441   3298   -415     41    280       O  
ATOM   1691  CB  GLN A 244      18.015  14.075 -55.219  1.00 56.36           C  
ANISOU 1691  CB  GLN A 244     6657   8903   5853   -515     38    305       C  
ATOM   1692  CG  GLN A 244      19.384  14.361 -55.818  1.00 65.75           C  
ANISOU 1692  CG  GLN A 244     7689  10446   6847   -600     37    340       C  
ATOM   1693  CD  GLN A 244      20.261  13.126 -55.867  1.00 69.26           C  
ANISOU 1693  CD  GLN A 244     7995  11127   7195   -421     22    224       C  
ATOM   1694  NE2 GLN A 244      20.852  12.860 -57.031  1.00 74.20           N  
ANISOU 1694  NE2 GLN A 244     8472  12052   7669   -368      7    205       N  
ATOM   1695  OE1 GLN A 244      20.396  12.411 -54.876  1.00 63.90           O  
ANISOU 1695  OE1 GLN A 244     7344  10365   6569   -322     17    150       O  
ATOM   1696  N   PRO A 245      14.632  15.265 -55.767  1.00 32.63           N  
ANISOU 1696  N   PRO A 245     3966   5292   3138   -542     35    386       N  
ATOM   1697  CA  PRO A 245      13.280  14.769 -55.496  1.00 33.59           C  
ANISOU 1697  CA  PRO A 245     4174   5188   3402   -430     34    341       C  
ATOM   1698  C   PRO A 245      13.003  13.400 -56.139  1.00 32.77           C  
ANISOU 1698  C   PRO A 245     4002   5131   3318   -262     15    252       C  
ATOM   1699  O   PRO A 245      12.209  13.322 -57.081  1.00 34.93           O  
ANISOU 1699  O   PRO A 245     4287   5367   3619   -216      4    247       O  
ATOM   1700  CB  PRO A 245      12.409  15.822 -56.164  1.00 36.28           C  
ANISOU 1700  CB  PRO A 245     4601   5422   3761   -502     28    407       C  
ATOM   1701  CG  PRO A 245      13.223  16.142 -57.410  1.00 39.53           C  
ANISOU 1701  CG  PRO A 245     4922   6058   4041   -570     19    446       C  
ATOM   1702  CD  PRO A 245      14.626  16.289 -56.827  1.00 38.52           C  
ANISOU 1702  CD  PRO A 245     4721   6103   3810   -663     23    470       C  
ATOM   1703  N   LYS A 246      13.651  12.343 -55.649  1.00 31.00           N  
ANISOU 1703  N   LYS A 246     3721   4980   3076   -167     -1    179       N  
ATOM   1704  CA  LYS A 246      13.385  10.990 -56.157  1.00 37.23           C  
ANISOU 1704  CA  LYS A 246     4480   5783   3883      2    -48     87       C  
ATOM   1705  C   LYS A 246      13.113   9.967 -55.044  1.00 31.83           C  
ANISOU 1705  C   LYS A 246     3852   4958   3284     86    -77     29       C  
ATOM   1706  O   LYS A 246      13.527  10.166 -53.907  1.00 32.52           O  
ANISOU 1706  O   LYS A 246     3961   5012   3383     33    -55     43       O  
ATOM   1707  CB  LYS A 246      14.494  10.520 -57.109  1.00 40.16           C  
ANISOU 1707  CB  LYS A 246     4721   6432   4107     79    -75     37       C  
ATOM   1708  CG  LYS A 246      15.854  10.191 -56.494  1.00 36.43           C  
ANISOU 1708  CG  LYS A 246     4168   6144   3529    100    -81     -3       C  
ATOM   1709  CD  LYS A 246      16.761   9.654 -57.618  1.00 33.60           C  
ANISOU 1709  CD  LYS A 246     3670   6085   3011    214   -117    -65       C  
ATOM   1710  CE  LYS A 246      18.169   9.356 -57.166  1.00 30.31           C  
ANISOU 1710  CE  LYS A 246     3148   5912   2457    250   -125   -111       C  
ATOM   1711  NZ  LYS A 246      19.032   9.113 -58.354  1.00 32.65           N1+
ANISOU 1711  NZ  LYS A 246     3286   6550   2569    339   -151   -153       N1+
ATOM   1712  N   PRO A 247      12.383   8.883 -55.363  1.00 28.52           N  
ANISOU 1712  N   PRO A 247     3465   4447   2922    206   -136    -29       N  
ATOM   1713  CA  PRO A 247      12.031   7.946 -54.281  1.00 29.08           C  
ANISOU 1713  CA  PRO A 247     3607   4368   3074    255   -176    -65       C  
ATOM   1714  C   PRO A 247      13.276   7.362 -53.618  1.00 26.03           C  
ANISOU 1714  C   PRO A 247     3186   4092   2612    312   -203   -124       C  
ATOM   1715  O   PRO A 247      14.351   7.397 -54.213  1.00 22.87           O  
ANISOU 1715  O   PRO A 247     2694   3909   2089    355   -207   -159       O  
ATOM   1716  CB  PRO A 247      11.237   6.846 -55.007  1.00 24.73           C  
ANISOU 1716  CB  PRO A 247     3093   3740   2564    369   -261   -116       C  
ATOM   1717  CG  PRO A 247      10.731   7.508 -56.268  1.00 24.84           C  
ANISOU 1717  CG  PRO A 247     3074   3798   2566    349   -234    -84       C  
ATOM   1718  CD  PRO A 247      11.794   8.493 -56.657  1.00 22.29           C  
ANISOU 1718  CD  PRO A 247     2663   3673   2132    286   -175    -55       C  
ATOM   1719  N   LEU A 248      13.126   6.854 -52.399  1.00 21.78           N  
ANISOU 1719  N   LEU A 248     2714   3424   2138    313   -220   -133       N  
ATOM   1720  CA  LEU A 248      14.234   6.266 -51.652  1.00 23.03           C  
ANISOU 1720  CA  LEU A 248     2855   3662   2233    374   -249   -194       C  
ATOM   1721  C   LEU A 248      14.700   4.988 -52.312  1.00 26.06           C  
ANISOU 1721  C   LEU A 248     3233   4127   2544    553   -360   -302       C  
ATOM   1722  O   LEU A 248      13.910   4.281 -52.937  1.00 25.62           O  
ANISOU 1722  O   LEU A 248     3232   3973   2531    623   -434   -327       O  
ATOM   1723  CB  LEU A 248      13.795   5.918 -50.227  1.00 21.62           C  
ANISOU 1723  CB  LEU A 248     2765   3301   2147    338   -255   -176       C  
ATOM   1724  CG  LEU A 248      13.279   7.066 -49.356  1.00 24.42           C  
ANISOU 1724  CG  LEU A 248     3142   3563   2574    192   -162    -83       C  
ATOM   1725  CD1 LEU A 248      12.695   6.526 -48.052  1.00 21.40           C  
ANISOU 1725  CD1 LEU A 248     2839   3014   2278    177   -180    -70       C  
ATOM   1726  CD2 LEU A 248      14.395   8.066 -49.073  1.00 21.08           C  
ANISOU 1726  CD2 LEU A 248     2656   3282   2073    118    -96    -61       C  
ATOM   1727  N   THR A 249      15.981   4.679 -52.153  1.00 28.44           N  
ANISOU 1727  N   THR A 249     3471   4608   2726    635   -383   -372       N  
ATOM   1728  CA  THR A 249      16.469   3.359 -52.507  1.00 32.80           C  
ANISOU 1728  CA  THR A 249     4043   5218   3201    836   -511   -493       C  
ATOM   1729  C   THR A 249      15.805   2.354 -51.579  1.00 33.77           C  
ANISOU 1729  C   THR A 249     4317   5088   3426    866   -599   -512       C  
ATOM   1730  O   THR A 249      15.232   2.721 -50.546  1.00 34.04           O  
ANISOU 1730  O   THR A 249     4405   4963   3565    735   -543   -435       O  
ATOM   1731  CB  THR A 249      17.995   3.240 -52.335  1.00 37.85           C  
ANISOU 1731  CB  THR A 249     4584   6116   3682    927   -518   -570       C  
ATOM   1732  CG2 THR A 249      18.741   4.287 -53.190  1.00 32.52           C  
ANISOU 1732  CG2 THR A 249     3744   5729   2885    862   -431   -532       C  
ATOM   1733  OG1 THR A 249      18.334   3.406 -50.953  1.00 36.14           O  
ANISOU 1733  OG1 THR A 249     4400   5829   3502    851   -477   -547       O  
ATOM   1734  N   ASP A 250      15.888   1.083 -51.939  1.00 37.83           N  
ANISOU 1734  N   ASP A 250     4905   5570   3898   1040   -749   -612       N  
ATOM   1735  CA  ASP A 250      15.348   0.031 -51.088  1.00 41.66           C  
ANISOU 1735  CA  ASP A 250     5550   5819   4461   1062   -862   -627       C  
ATOM   1736  C   ASP A 250      16.087  -0.064 -49.754  1.00 37.26           C  
ANISOU 1736  C   ASP A 250     5013   5258   3888   1047   -847   -641       C  
ATOM   1737  O   ASP A 250      15.467  -0.296 -48.717  1.00 41.66           O  
ANISOU 1737  O   ASP A 250     5667   5618   4544    954   -856   -586       O  
ATOM   1738  CB  ASP A 250      15.361  -1.313 -51.819  1.00 49.50           C  
ANISOU 1738  CB  ASP A 250     6642   6771   5396   1261  -1056   -738       C  
ATOM   1739  CG  ASP A 250      14.400  -1.337 -53.001  1.00 62.67           C  
ANISOU 1739  CG  ASP A 250     8320   8385   7108   1260  -1085   -715       C  
ATOM   1740  OD1 ASP A 250      13.245  -1.776 -52.818  1.00 65.67           O  
ANISOU 1740  OD1 ASP A 250     8815   8535   7599   1182  -1146   -658       O  
ATOM   1741  OD2 ASP A 250      14.795  -0.900 -54.107  1.00 68.74           O1-
ANISOU 1741  OD2 ASP A 250     8973   9352   7792   1329  -1047   -746       O1-
ATOM   1742  N   SER A 251      17.406   0.112 -49.779  1.00 33.76           N  
ANISOU 1742  N   SER A 251     4469   5047   3311   1137   -823   -713       N  
ATOM   1743  CA  SER A 251      18.190   0.091 -48.540  1.00 38.30           C  
ANISOU 1743  CA  SER A 251     5050   5642   3862   1127   -800   -730       C  
ATOM   1744  C   SER A 251      17.749   1.221 -47.631  1.00 28.48           C  
ANISOU 1744  C   SER A 251     3778   4317   2726    908   -649   -603       C  
ATOM   1745  O   SER A 251      17.524   1.013 -46.439  1.00 32.69           O  
ANISOU 1745  O   SER A 251     4391   4699   3330    851   -651   -574       O  
ATOM   1746  CB  SER A 251      19.691   0.217 -48.812  1.00 42.79           C  
ANISOU 1746  CB  SER A 251     5486   6521   4252   1249   -788   -822       C  
ATOM   1747  OG  SER A 251      20.127  -0.823 -49.658  1.00 58.29           O  
ANISOU 1747  OG  SER A 251     7470   8582   6094   1483   -937   -955       O  
ATOM   1748  N   GLN A 252      17.636   2.416 -48.209  1.00 26.92           N  
ANISOU 1748  N   GLN A 252     3474   4224   2531    795   -530   -529       N  
ATOM   1749  CA  GLN A 252      17.184   3.594 -47.476  1.00 26.74           C  
ANISOU 1749  CA  GLN A 252     3435   4126   2598    603   -402   -414       C  
ATOM   1750  C   GLN A 252      15.843   3.351 -46.805  1.00 29.24           C  
ANISOU 1750  C   GLN A 252     3867   4181   3060    526   -415   -348       C  
ATOM   1751  O   GLN A 252      15.684   3.623 -45.617  1.00 31.96           O  
ANISOU 1751  O   GLN A 252     4246   4432   3465    443   -370   -301       O  
ATOM   1752  CB  GLN A 252      17.089   4.800 -48.400  1.00 28.68           C  
ANISOU 1752  CB  GLN A 252     3587   4489   2823    505   -311   -347       C  
ATOM   1753  CG  GLN A 252      18.406   5.505 -48.604  1.00 28.96           C  
ANISOU 1753  CG  GLN A 252     3494   4787   2724    483   -256   -356       C  
ATOM   1754  CD  GLN A 252      18.289   6.639 -49.586  1.00 34.75           C  
ANISOU 1754  CD  GLN A 252     4149   5628   3426    374   -188   -281       C  
ATOM   1755  NE2 GLN A 252      19.142   7.641 -49.427  1.00 40.08           N  
ANISOU 1755  NE2 GLN A 252     4742   6464   4024    259   -121   -231       N  
ATOM   1756  OE1 GLN A 252      17.432   6.627 -50.475  1.00 32.72           O  
ANISOU 1756  OE1 GLN A 252     3914   5306   3212    383   -203   -263       O  
ATOM   1757  N   ARG A 253      14.889   2.818 -47.560  1.00 26.59           N  
ANISOU 1757  N   ARG A 253     3585   3746   2772    556   -481   -345       N  
ATOM   1758  CA  ARG A 253      13.553   2.567 -47.027  1.00 25.72           C  
ANISOU 1758  CA  ARG A 253     3566   3423   2784    471   -499   -274       C  
ATOM   1759  C   ARG A 253      13.566   1.516 -45.930  1.00 29.63           C  
ANISOU 1759  C   ARG A 253     4166   3789   3302    496   -589   -295       C  
ATOM   1760  O   ARG A 253      12.893   1.668 -44.911  1.00 31.75           O  
ANISOU 1760  O   ARG A 253     4472   3942   3648    390   -555   -221       O  
ATOM   1761  CB  ARG A 253      12.605   2.120 -48.139  1.00 26.29           C  
ANISOU 1761  CB  ARG A 253     3672   3431   2887    500   -566   -271       C  
ATOM   1762  CG  ARG A 253      11.155   1.998 -47.698  1.00 27.80           C  
ANISOU 1762  CG  ARG A 253     3928   3444   3189    391   -573   -183       C  
ATOM   1763  CD  ARG A 253      10.301   1.325 -48.760  1.00 37.72           C  
ANISOU 1763  CD  ARG A 253     5231   4634   4468    428   -669   -190       C  
ATOM   1764  NE  ARG A 253      10.561  -0.109 -48.837  1.00 45.15           N  
ANISOU 1764  NE  ARG A 253     6281   5498   5377    536   -842   -263       N  
ATOM   1765  CZ  ARG A 253      11.123  -0.710 -49.879  1.00 48.08           C  
ANISOU 1765  CZ  ARG A 253     6664   5933   5671    689   -940   -360       C  
ATOM   1766  NH1 ARG A 253      11.476  -0.001 -50.944  1.00 48.97           N1+
ANISOU 1766  NH1 ARG A 253     6670   6205   5733    737   -869   -385       N1+
ATOM   1767  NH2 ARG A 253      11.320  -2.020 -49.860  1.00 53.44           N  
ANISOU 1767  NH2 ARG A 253     7469   6519   6316    796  -1120   -430       N  
ATOM   1768  N   VAL A 254      14.318   0.439 -46.147  1.00 30.59           N  
ANISOU 1768  N   VAL A 254     4340   3936   3347    644   -716   -398       N  
ATOM   1769  CA  VAL A 254      14.453  -0.616 -45.139  1.00 30.70           C  
ANISOU 1769  CA  VAL A 254     4474   3823   3367    679   -826   -427       C  
ATOM   1770  C   VAL A 254      15.030  -0.051 -43.838  1.00 32.50           C  
ANISOU 1770  C   VAL A 254     4668   4081   3602    613   -728   -401       C  
ATOM   1771  O   VAL A 254      14.492  -0.268 -42.751  1.00 35.32           O  
ANISOU 1771  O   VAL A 254     5093   4301   4027    526   -733   -341       O  
ATOM   1772  CB  VAL A 254      15.329  -1.782 -45.675  1.00 36.34           C  
ANISOU 1772  CB  VAL A 254     5255   4581   3970    886   -990   -564       C  
ATOM   1773  CG1 VAL A 254      15.907  -2.626 -44.546  1.00 27.00           C  
ANISOU 1773  CG1 VAL A 254     4179   3321   2760    942  -1084   -613       C  
ATOM   1774  CG2 VAL A 254      14.529  -2.640 -46.659  1.00 37.53           C  
ANISOU 1774  CG2 VAL A 254     5503   4621   4137    943  -1134   -582       C  
ATOM   1775  N   ARG A 255      16.118   0.696 -43.969  1.00 22.77           N  
ANISOU 1775  N   ARG A 255     3323   3040   2291    647   -641   -440       N  
ATOM   1776  CA  ARG A 255      16.773   1.331 -42.839  1.00 26.00           C  
ANISOU 1776  CA  ARG A 255     3688   3495   2694    587   -548   -420       C  
ATOM   1777  C   ARG A 255      15.829   2.285 -42.104  1.00 29.81           C  
ANISOU 1777  C   ARG A 255     4161   3877   3286    417   -436   -299       C  
ATOM   1778  O   ARG A 255      15.780   2.305 -40.878  1.00 29.36           O  
ANISOU 1778  O   ARG A 255     4139   3745   3269    364   -412   -267       O  
ATOM   1779  CB  ARG A 255      18.008   2.084 -43.337  1.00 36.66           C  
ANISOU 1779  CB  ARG A 255     4905   5091   3932    625   -477   -466       C  
ATOM   1780  CG  ARG A 255      18.744   2.863 -42.274  1.00 49.79           C  
ANISOU 1780  CG  ARG A 255     6516   6821   5582    551   -380   -441       C  
ATOM   1781  CD  ARG A 255      20.070   3.380 -42.799  1.00 60.53           C  
ANISOU 1781  CD  ARG A 255     7744   8450   6804    591   -340   -492       C  
ATOM   1782  NE  ARG A 255      21.049   3.506 -41.723  1.00 71.78           N  
ANISOU 1782  NE  ARG A 255     9145   9945   8183    590   -310   -518       N  
ATOM   1783  CZ  ARG A 255      21.791   2.498 -41.272  1.00 78.44           C  
ANISOU 1783  CZ  ARG A 255    10025  10823   8957    734   -395   -621       C  
ATOM   1784  NH1 ARG A 255      21.664   1.288 -41.804  1.00 80.78           N1+
ANISOU 1784  NH1 ARG A 255    10397  11078   9219    893   -529   -708       N1+
ATOM   1785  NH2 ARG A 255      22.659   2.697 -40.289  1.00 82.71           N  
ANISOU 1785  NH2 ARG A 255    10536  11433   9457    726   -358   -641       N  
ATOM   1786  N   PHE A 256      15.077   3.071 -42.867  1.00 30.51           N  
ANISOU 1786  N   PHE A 256     4205   3973   3413    345   -374   -238       N  
ATOM   1787  CA  PHE A 256      14.135   4.023 -42.307  1.00 27.93           C  
ANISOU 1787  CA  PHE A 256     3871   3570   3173    213   -281   -136       C  
ATOM   1788  C   PHE A 256      13.015   3.278 -41.593  1.00 28.86           C  
ANISOU 1788  C   PHE A 256     4073   3524   3369    171   -335    -87       C  
ATOM   1789  O   PHE A 256      12.607   3.640 -40.477  1.00 25.50           O  
ANISOU 1789  O   PHE A 256     3655   3044   2989     96   -284    -28       O  
ATOM   1790  CB  PHE A 256      13.581   4.906 -43.425  1.00 21.81           C  
ANISOU 1790  CB  PHE A 256     3042   2839   2406    170   -227    -97       C  
ATOM   1791  CG  PHE A 256      12.425   5.773 -43.014  1.00 24.18           C  
ANISOU 1791  CG  PHE A 256     3349   3055   2783     67   -157     -5       C  
ATOM   1792  CD1 PHE A 256      12.495   6.566 -41.878  1.00 25.00           C  
ANISOU 1792  CD1 PHE A 256     3450   3142   2907      4    -87     36       C  
ATOM   1793  CD2 PHE A 256      11.271   5.817 -43.789  1.00 27.12           C  
ANISOU 1793  CD2 PHE A 256     3729   3378   3198     46   -167     32       C  
ATOM   1794  CE1 PHE A 256      11.427   7.382 -41.511  1.00 27.28           C  
ANISOU 1794  CE1 PHE A 256     3745   3371   3248    -62    -34    107       C  
ATOM   1795  CE2 PHE A 256      10.185   6.628 -43.424  1.00 23.05           C  
ANISOU 1795  CE2 PHE A 256     3212   2809   2736    -28   -107    106       C  
ATOM   1796  CZ  PHE A 256      10.266   7.411 -42.288  1.00 23.77           C  
ANISOU 1796  CZ  PHE A 256     3302   2891   2838    -74    -44    140       C  
ATOM   1797  N   THR A 257      12.535   2.222 -42.239  1.00 21.19           N  
ANISOU 1797  N   THR A 257     3164   2484   2402    218   -448   -109       N  
ATOM   1798  CA  THR A 257      11.458   1.400 -41.678  1.00 30.55           C  
ANISOU 1798  CA  THR A 257     4434   3523   3649    156   -524    -51       C  
ATOM   1799  C   THR A 257      11.768   0.822 -40.286  1.00 30.13           C  
ANISOU 1799  C   THR A 257     4444   3404   3599    138   -560    -44       C  
ATOM   1800  O   THR A 257      10.973   0.964 -39.355  1.00 23.90           O  
ANISOU 1800  O   THR A 257     3660   2561   2860     35   -527     40       O  
ATOM   1801  CB  THR A 257      11.077   0.258 -42.643  1.00 30.72           C  
ANISOU 1801  CB  THR A 257     4536   3474   3662    214   -672    -85       C  
ATOM   1802  CG2 THR A 257       9.866  -0.497 -42.142  1.00 28.42           C  
ANISOU 1802  CG2 THR A 257     4327   3044   3428    111   -754     -1       C  
ATOM   1803  OG1 THR A 257      10.782   0.814 -43.932  1.00 34.39           O  
ANISOU 1803  OG1 THR A 257     4937   4007   4123    234   -633    -90       O  
ATOM   1804  N   LYS A 258      12.924   0.178 -40.150  1.00 28.91           N  
ANISOU 1804  N   LYS A 258     4332   3271   3381    245   -630   -137       N  
ATOM   1805  CA  LYS A 258      13.289  -0.477 -38.901  1.00 30.33           C  
ANISOU 1805  CA  LYS A 258     4587   3380   3556    243   -682   -142       C  
ATOM   1806  C   LYS A 258      13.377   0.539 -37.767  1.00 37.92           C  
ANISOU 1806  C   LYS A 258     5477   4385   4547    163   -541    -88       C  
ATOM   1807  O   LYS A 258      13.207   0.203 -36.595  1.00 37.57           O  
ANISOU 1807  O   LYS A 258     5480   4272   4525    113   -556    -48       O  
ATOM   1808  CB  LYS A 258      14.619  -1.217 -39.045  1.00 37.08           C  
ANISOU 1808  CB  LYS A 258     5490   4279   4319    402   -775   -269       C  
ATOM   1809  CG  LYS A 258      14.628  -2.268 -40.149  1.00 48.51           C  
ANISOU 1809  CG  LYS A 258     7025   5687   5720    517   -938   -343       C  
ATOM   1810  CD  LYS A 258      15.917  -3.089 -40.157  1.00 62.76           C  
ANISOU 1810  CD  LYS A 258     8891   7539   7417    702  -1053   -481       C  
ATOM   1811  CE  LYS A 258      16.031  -3.972 -38.911  1.00 77.55           C  
ANISOU 1811  CE  LYS A 258    10901   9271   9294    694  -1155   -481       C  
ATOM   1812  NZ  LYS A 258      15.032  -5.087 -38.877  1.00 82.94           N1+
ANISOU 1812  NZ  LYS A 258    11755   9742  10017    637  -1329   -429       N1+
ATOM   1813  N   GLU A 259      13.623   1.789 -38.139  1.00 31.29           N  
ANISOU 1813  N   GLU A 259     4531   3656   3703    149   -415    -83       N  
ATOM   1814  CA  GLU A 259      13.769   2.873 -37.189  1.00 25.98           C  
ANISOU 1814  CA  GLU A 259     3799   3023   3049     87   -294    -40       C  
ATOM   1815  C   GLU A 259      12.427   3.474 -36.748  1.00 23.67           C  
ANISOU 1815  C   GLU A 259     3488   2682   2824    -17   -234     63       C  
ATOM   1816  O   GLU A 259      12.268   3.835 -35.592  1.00 20.19           O  
ANISOU 1816  O   GLU A 259     3040   2228   2404    -61   -185    105       O  
ATOM   1817  CB  GLU A 259      14.676   3.954 -37.784  1.00 29.55           C  
ANISOU 1817  CB  GLU A 259     4166   3610   3452    108   -210    -76       C  
ATOM   1818  CG  GLU A 259      15.635   4.548 -36.798  1.00 45.08           C  
ANISOU 1818  CG  GLU A 259     6103   5634   5392    101   -147    -92       C  
ATOM   1819  CD  GLU A 259      16.382   3.487 -36.025  1.00 54.52           C  
ANISOU 1819  CD  GLU A 259     7354   6808   6556    173   -219   -154       C  
ATOM   1820  OE1 GLU A 259      17.169   2.747 -36.656  1.00 54.00           O  
ANISOU 1820  OE1 GLU A 259     7298   6803   6419    276   -294   -241       O  
ATOM   1821  OE2 GLU A 259      16.166   3.384 -34.793  1.00 57.46           O1-
ANISOU 1821  OE2 GLU A 259     7761   7106   6965    136   -206   -120       O1-
ATOM   1822  N   ILE A 260      11.460   3.599 -37.654  1.00 24.73           N  
ANISOU 1822  N   ILE A 260     3608   2804   2983    -46   -240    101       N  
ATOM   1823  CA  ILE A 260      10.211   4.282 -37.292  1.00 24.11           C  
ANISOU 1823  CA  ILE A 260     3495   2718   2948   -126   -179    188       C  
ATOM   1824  C   ILE A 260       9.096   3.326 -36.876  1.00 22.69           C  
ANISOU 1824  C   ILE A 260     3353   2471   2796   -191   -251    256       C  
ATOM   1825  O   ILE A 260       8.113   3.735 -36.245  1.00 21.89           O  
ANISOU 1825  O   ILE A 260     3213   2392   2712   -255   -206    331       O  
ATOM   1826  CB  ILE A 260       9.676   5.206 -38.421  1.00 28.58           C  
ANISOU 1826  CB  ILE A 260     4013   3328   3520   -130   -128    201       C  
ATOM   1827  CG1 ILE A 260       8.688   6.223 -37.832  1.00 26.00           C  
ANISOU 1827  CG1 ILE A 260     3646   3020   3214   -177    -50    268       C  
ATOM   1828  CG2 ILE A 260       8.995   4.377 -39.489  1.00 19.34           C  
ANISOU 1828  CG2 ILE A 260     2866   2123   2361   -127   -208    204       C  
ATOM   1829  CD1 ILE A 260       8.421   7.428 -38.673  1.00 24.95           C  
ANISOU 1829  CD1 ILE A 260     3481   2926   3073   -168      7    271       C  
ATOM   1830  N   LYS A 261       9.249   2.058 -37.241  1.00 27.53           N  
ANISOU 1830  N   LYS A 261     4044   3014   3400   -175   -375    230       N  
ATOM   1831  CA  LYS A 261       8.259   1.038 -36.918  1.00 28.68           C  
ANISOU 1831  CA  LYS A 261     4248   3087   3564   -260   -474    303       C  
ATOM   1832  C   LYS A 261       8.002   1.022 -35.412  1.00 35.51           C  
ANISOU 1832  C   LYS A 261     5104   3956   4431   -333   -446    370       C  
ATOM   1833  O   LYS A 261       8.939   0.990 -34.604  1.00 33.42           O  
ANISOU 1833  O   LYS A 261     4863   3683   4151   -293   -433    329       O  
ATOM   1834  CB  LYS A 261       8.758  -0.319 -37.389  1.00 31.44           C  
ANISOU 1834  CB  LYS A 261     4718   3337   3891   -213   -636    248       C  
ATOM   1835  CG  LYS A 261       7.683  -1.354 -37.632  1.00 45.90           C  
ANISOU 1835  CG  LYS A 261     6624   5080   5735   -306   -769    320       C  
ATOM   1836  CD  LYS A 261       8.294  -2.589 -38.292  1.00 54.22           C  
ANISOU 1836  CD  LYS A 261     7819   6024   6758   -222   -948    242       C  
ATOM   1837  CE  LYS A 261       7.268  -3.682 -38.519  1.00 62.66           C  
ANISOU 1837  CE  LYS A 261     8992   6979   7835   -329  -1111    318       C  
ATOM   1838  NZ  LYS A 261       6.704  -4.177 -37.232  1.00 68.25           N1+
ANISOU 1838  NZ  LYS A 261     9742   7645   8546   -479  -1155    428       N1+
ATOM   1839  N   GLY A 262       6.729   1.102 -35.042  1.00 32.68           N  
ANISOU 1839  N   GLY A 262     4700   3635   4083   -437   -431    472       N  
ATOM   1840  CA  GLY A 262       6.338   1.061 -33.649  1.00 21.44           C  
ANISOU 1840  CA  GLY A 262     3252   2246   2649   -512   -409    547       C  
ATOM   1841  C   GLY A 262       6.188   2.413 -32.974  1.00 27.46           C  
ANISOU 1841  C   GLY A 262     3909   3120   3406   -483   -264    557       C  
ATOM   1842  O   GLY A 262       5.584   2.510 -31.909  1.00 35.83           O  
ANISOU 1842  O   GLY A 262     4921   4247   4447   -540   -236    629       O  
ATOM   1843  N   LEU A 263       6.739   3.464 -33.564  1.00 21.26           N  
ANISOU 1843  N   LEU A 263     3092   2359   2628   -395   -183    488       N  
ATOM   1844  CA  LEU A 263       6.620   4.776 -32.935  1.00 26.71           C  
ANISOU 1844  CA  LEU A 263     3710   3131   3306   -359    -71    492       C  
ATOM   1845  C   LEU A 263       5.242   5.399 -33.158  1.00 29.62           C  
ANISOU 1845  C   LEU A 263     4001   3591   3661   -382    -32    552       C  
ATOM   1846  O   LEU A 263       4.533   5.044 -34.100  1.00 28.07           O  
ANISOU 1846  O   LEU A 263     3799   3396   3472   -415    -72    575       O  
ATOM   1847  CB  LEU A 263       7.695   5.724 -33.442  1.00 23.49           C  
ANISOU 1847  CB  LEU A 263     3311   2714   2901   -278    -15    410       C  
ATOM   1848  CG  LEU A 263       9.133   5.281 -33.217  1.00 27.50           C  
ANISOU 1848  CG  LEU A 263     3872   3174   3404   -239    -40    341       C  
ATOM   1849  CD1 LEU A 263      10.040   6.509 -33.284  1.00 24.63           C  
ANISOU 1849  CD1 LEU A 263     3489   2843   3026   -189     35    290       C  
ATOM   1850  CD2 LEU A 263       9.263   4.559 -31.882  1.00 19.74           C  
ANISOU 1850  CD2 LEU A 263     2915   2168   2417   -267    -68    367       C  
ATOM   1851  N   LYS A 264       4.865   6.322 -32.277  1.00 28.69           N  
ANISOU 1851  N   LYS A 264     3825   3560   3515   -351     39    571       N  
ATOM   1852  CA  LYS A 264       3.645   7.089 -32.459  1.00 23.18           C  
ANISOU 1852  CA  LYS A 264     3052   2972   2785   -334     77    606       C  
ATOM   1853  C   LYS A 264       3.959   8.348 -33.242  1.00 25.05           C  
ANISOU 1853  C   LYS A 264     3306   3186   3024   -246    124    541       C  
ATOM   1854  O   LYS A 264       5.024   8.949 -33.067  1.00 23.41           O  
ANISOU 1854  O   LYS A 264     3145   2922   2826   -199    150    487       O  
ATOM   1855  CB  LYS A 264       3.021   7.478 -31.116  1.00 27.38           C  
ANISOU 1855  CB  LYS A 264     3512   3628   3263   -321    116    652       C  
ATOM   1856  CG  LYS A 264       2.440   6.312 -30.322  1.00 39.95           C  
ANISOU 1856  CG  LYS A 264     5066   5281   4831   -433     68    744       C  
ATOM   1857  CD  LYS A 264       1.479   6.797 -29.228  1.00 48.30           C  
ANISOU 1857  CD  LYS A 264     6013   6529   5810   -415    110    800       C  
ATOM   1858  CE  LYS A 264       2.160   7.774 -28.265  1.00 57.57           C  
ANISOU 1858  CE  LYS A 264     7196   7707   6970   -301    170    742       C  
ATOM   1859  NZ  LYS A 264       1.195   8.574 -27.447  1.00 62.41           N1+
ANISOU 1859  NZ  LYS A 264     7702   8517   7492   -224    212    765       N1+
ATOM   1860  N   VAL A 265       3.031   8.750 -34.107  1.00 19.88           N  
ANISOU 1860  N   VAL A 265     2619   2579   2356   -231    128    552       N  
ATOM   1861  CA  VAL A 265       3.147  10.021 -34.802  1.00 19.59           C  
ANISOU 1861  CA  VAL A 265     2609   2526   2310   -151    161    501       C  
ATOM   1862  C   VAL A 265       1.818  10.759 -34.731  1.00 23.43           C  
ANISOU 1862  C   VAL A 265     3034   3129   2740    -96    180    523       C  
ATOM   1863  O   VAL A 265       0.769  10.161 -34.459  1.00 22.33           O  
ANISOU 1863  O   VAL A 265     2814   3098   2570   -136    169    581       O  
ATOM   1864  CB  VAL A 265       3.606   9.864 -36.285  1.00 27.07           C  
ANISOU 1864  CB  VAL A 265     3598   3393   3293   -166    138    467       C  
ATOM   1865  CG1 VAL A 265       4.951   9.135 -36.377  1.00 18.90           C  
ANISOU 1865  CG1 VAL A 265     2614   2276   2292   -195    113    433       C  
ATOM   1866  CG2 VAL A 265       2.546   9.144 -37.106  1.00 30.80           C  
ANISOU 1866  CG2 VAL A 265     4031   3899   3771   -209    103    505       C  
ATOM   1867  N   GLU A 266       1.868  12.064 -34.957  1.00 20.65           N  
ANISOU 1867  N   GLU A 266     2722   2763   2360     -4    198    477       N  
ATOM   1868  CA  GLU A 266       0.671  12.889 -34.909  1.00 24.25           C  
ANISOU 1868  CA  GLU A 266     3137   3331   2748     85    204    476       C  
ATOM   1869  C   GLU A 266       0.569  13.688 -36.201  1.00 25.97           C  
ANISOU 1869  C   GLU A 266     3414   3488   2966    128    192    437       C  
ATOM   1870  O   GLU A 266       1.590  14.039 -36.807  1.00 25.60           O  
ANISOU 1870  O   GLU A 266     3451   3319   2957    109    185    406       O  
ATOM   1871  CB  GLU A 266       0.707  13.819 -33.689  1.00 24.09           C  
ANISOU 1871  CB  GLU A 266     3128   3356   2667    188    215    452       C  
ATOM   1872  CG  GLU A 266       1.900  14.738 -33.674  1.00 29.75           C  
ANISOU 1872  CG  GLU A 266     3965   3933   3405    221    206    399       C  
ATOM   1873  CD  GLU A 266       1.963  15.627 -32.442  1.00 45.29           C  
ANISOU 1873  CD  GLU A 266     5962   5930   5316    326    200    371       C  
ATOM   1874  OE1 GLU A 266       2.378  16.800 -32.588  1.00 52.66           O  
ANISOU 1874  OE1 GLU A 266     7005   6775   6229    393    167    326       O  
ATOM   1875  OE2 GLU A 266       1.622  15.153 -31.332  1.00 49.39           O1-
ANISOU 1875  OE2 GLU A 266     6402   6557   5808    338    219    398       O1-
ATOM   1876  N   VAL A 267      -0.656  13.975 -36.626  1.00 29.54           N  
ANISOU 1876  N   VAL A 267     3816   4040   3368    183    187    442       N  
ATOM   1877  CA  VAL A 267      -0.863  14.601 -37.926  1.00 31.92           C  
ANISOU 1877  CA  VAL A 267     4171   4287   3670    217    171    411       C  
ATOM   1878  C   VAL A 267      -1.089  16.099 -37.819  1.00 34.77           C  
ANISOU 1878  C   VAL A 267     4610   4638   3962    353    149    358       C  
ATOM   1879  O   VAL A 267      -1.663  16.574 -36.846  1.00 34.50           O  
ANISOU 1879  O   VAL A 267     4548   4705   3854    453    145    346       O  
ATOM   1880  CB  VAL A 267      -2.029  13.964 -38.695  1.00 33.60           C  
ANISOU 1880  CB  VAL A 267     4296   4597   3873    191    168    442       C  
ATOM   1881  CG1 VAL A 267      -1.685  12.538 -39.081  1.00 35.38           C  
ANISOU 1881  CG1 VAL A 267     4490   4781   4172     54    159    487       C  
ATOM   1882  CG2 VAL A 267      -3.303  14.020 -37.869  1.00 39.47           C  
ANISOU 1882  CG2 VAL A 267     4929   5540   4526    253    175    466       C  
ATOM   1883  N   THR A 268      -0.654  16.823 -38.851  1.00 38.21           N  
ANISOU 1883  N   THR A 268     5149   4957   4411    360    124    328       N  
ATOM   1884  CA  THR A 268      -0.669  18.283 -38.869  1.00 38.10           C  
ANISOU 1884  CA  THR A 268     5257   4883   4335    471     75    280       C  
ATOM   1885  C   THR A 268      -1.698  18.893 -39.824  1.00 40.88           C  
ANISOU 1885  C   THR A 268     5632   5267   4636    558     44    253       C  
ATOM   1886  O   THR A 268      -1.978  20.090 -39.751  1.00 40.71           O  
ANISOU 1886  O   THR A 268     5714   5212   4540    681    -14    207       O  
ATOM   1887  CB  THR A 268       0.717  18.847 -39.258  1.00 37.17           C  
ANISOU 1887  CB  THR A 268     5269   4600   4254    398     49    274       C  
ATOM   1888  CG2 THR A 268       1.819  18.176 -38.453  1.00 35.68           C  
ANISOU 1888  CG2 THR A 268     5053   4386   4117    308     82    295       C  
ATOM   1889  OG1 THR A 268       0.955  18.631 -40.655  1.00 39.37           O  
ANISOU 1889  OG1 THR A 268     5560   4826   4572    320     51    286       O  
ATOM   1890  N   HIS A 269      -2.260  18.079 -40.715  1.00 42.08           N  
ANISOU 1890  N   HIS A 269     5695   5472   4819    503     72    278       N  
ATOM   1891  CA  HIS A 269      -3.162  18.588 -41.751  1.00 42.18           C  
ANISOU 1891  CA  HIS A 269     5728   5508   4791    576     46    253       C  
ATOM   1892  C   HIS A 269      -4.590  18.849 -41.269  1.00 54.59           C  
ANISOU 1892  C   HIS A 269     7219   7261   6260    718     38    229       C  
ATOM   1893  O   HIS A 269      -5.394  19.444 -41.983  1.00 53.79           O  
ANISOU 1893  O   HIS A 269     7144   7190   6102    814      8    193       O  
ATOM   1894  CB  HIS A 269      -3.178  17.649 -42.960  1.00 37.59           C  
ANISOU 1894  CB  HIS A 269     5090   4912   4281    466     72    284       C  
ATOM   1895  CG  HIS A 269      -3.689  16.273 -42.657  1.00 38.51           C  
ANISOU 1895  CG  HIS A 269     5059   5145   4428    390    108    333       C  
ATOM   1896  CD2 HIS A 269      -4.840  15.652 -43.014  1.00 38.18           C  
ANISOU 1896  CD2 HIS A 269     4908   5231   4365    386    115    357       C  
ATOM   1897  ND1 HIS A 269      -2.969  15.356 -41.926  1.00 36.38           N  
ANISOU 1897  ND1 HIS A 269     4752   4861   4211    292    129    370       N  
ATOM   1898  CE1 HIS A 269      -3.657  14.228 -41.837  1.00 35.09           C  
ANISOU 1898  CE1 HIS A 269     4476   4798   4058    225    137    418       C  
ATOM   1899  NE2 HIS A 269      -4.796  14.383 -42.487  1.00 30.18           N  
ANISOU 1899  NE2 HIS A 269     3804   4269   3392    273    130    415       N  
ATOM   1900  N   CYS A 270      -4.912  18.394 -40.064  1.00 65.89           N  
ANISOU 1900  N   CYS A 270     8547   8831   7658    734     63    249       N  
ATOM   1901  CA  CYS A 270      -6.228  18.664 -39.501  1.00 79.02           C  
ANISOU 1901  CA  CYS A 270    10112  10712   9199    877     55    228       C  
ATOM   1902  C   CYS A 270      -6.139  19.846 -38.540  1.00 88.56           C  
ANISOU 1902  C   CYS A 270    11413  11919  10315   1049      4    163       C  
ATOM   1903  O   CYS A 270      -5.129  20.028 -37.860  1.00 91.49           O  
ANISOU 1903  O   CYS A 270    11863  12174  10727   1017     -3    164       O  
ATOM   1904  CB  CYS A 270      -6.807  17.418 -38.827  1.00 80.16           C  
ANISOU 1904  CB  CYS A 270    10066  11052   9337    784    106    300       C  
ATOM   1905  SG  CYS A 270      -7.182  16.065 -39.988  1.00 58.56           S  
ANISOU 1905  SG  CYS A 270     7235   8330   6684    604    132    371       S  
ATOM   1906  N   GLY A 271      -7.192  20.655 -38.508  1.00 94.11           N  
ANISOU 1906  N   GLY A 271    12114  12753  10890   1243    -41    101       N  
ATOM   1907  CA  GLY A 271      -7.178  21.909 -37.775  1.00 99.59           C  
ANISOU 1907  CA  GLY A 271    12933  13426  11481   1443   -121     20       C  
ATOM   1908  C   GLY A 271      -6.858  21.782 -36.298  1.00103.00           C  
ANISOU 1908  C   GLY A 271    13315  13937  11885   1473   -108     28       C  
ATOM   1909  O   GLY A 271      -7.758  21.801 -35.458  1.00104.45           O  
ANISOU 1909  O   GLY A 271    13375  14366  11946   1609   -106      8       O  
ATOM   1910  N   GLN A 272      -5.569  21.653 -35.986  1.00104.24           N  
ANISOU 1910  N   GLN A 272    13559  13902  12144   1347    -98     57       N  
ATOM   1911  CA  GLN A 272      -5.094  21.516 -34.605  1.00105.26           C  
ANISOU 1911  CA  GLN A 272    13657  14072  12264   1359    -84     67       C  
ATOM   1912  C   GLN A 272      -5.709  20.325 -33.863  1.00102.00           C  
ANISOU 1912  C   GLN A 272    13016  13907  11834   1294     -2    133       C  
ATOM   1913  O   GLN A 272      -5.603  20.228 -32.639  1.00100.94           O  
ANISOU 1913  O   GLN A 272    12826  13870  11658   1335      9    138       O  
ATOM   1914  CB  GLN A 272      -5.297  22.815 -33.806  1.00108.11           C  
ANISOU 1914  CB  GLN A 272    14136  14444  12497   1600   -181    -25       C  
ATOM   1915  CG  GLN A 272      -4.379  23.963 -34.219  1.00110.73           C  
ANISOU 1915  CG  GLN A 272    14728  14489  12855   1622   -283    -71       C  
ATOM   1916  CD  GLN A 272      -4.448  25.146 -33.268  1.00114.88           C  
ANISOU 1916  CD  GLN A 272    15389  14999  13260   1849   -397   -158       C  
ATOM   1917  NE2 GLN A 272      -3.755  26.227 -33.612  1.00115.54           N  
ANISOU 1917  NE2 GLN A 272    15721  14832  13347   1871   -514   -196       N  
ATOM   1918  OE1 GLN A 272      -5.116  25.088 -32.236  1.00117.95           O  
ANISOU 1918  OE1 GLN A 272    15664  15604  13547   2001   -391   -188       O  
ATOM   1919  N   MET A 273      -6.345  19.420 -34.604  1.00 98.69           N  
ANISOU 1919  N   MET A 273    12470  13588  11441   1183     46    189       N  
ATOM   1920  CA  MET A 273      -6.909  18.215 -34.010  1.00 93.16           C  
ANISOU 1920  CA  MET A 273    11565  13106  10726   1077    107    272       C  
ATOM   1921  C   MET A 273      -5.776  17.292 -33.582  1.00 88.16           C  
ANISOU 1921  C   MET A 273    10943  12335  10217    888    146    337       C  
ATOM   1922  O   MET A 273      -5.763  16.787 -32.458  1.00 90.54           O  
ANISOU 1922  O   MET A 273    11153  12755  10492    858    170    378       O  
ATOM   1923  CB  MET A 273      -7.857  17.511 -34.983  1.00 89.83           C  
ANISOU 1923  CB  MET A 273    11027  12803  10299    994    129    318       C  
ATOM   1924  CG  MET A 273      -9.103  18.323 -35.314  1.00 89.86           C  
ANISOU 1924  CG  MET A 273    10987  12996  10159   1190     95    255       C  
ATOM   1925  SD  MET A 273     -10.049  18.857 -33.866  1.00133.57           S  
ANISOU 1925  SD  MET A 273    16387  18873  15488   1409     79    217       S  
ATOM   1926  CE  MET A 273     -11.062  17.418 -33.524  1.00 76.14           C  
ANISOU 1926  CE  MET A 273     8832  11936   8162   1234    143    346       C  
ATOM   1927  N   LYS A 274      -4.827  17.086 -34.487  1.00 78.86           N  
ANISOU 1927  N   LYS A 274     9877  10921   9165    769    146    342       N  
ATOM   1928  CA  LYS A 274      -3.570  16.430 -34.149  1.00 69.92           C  
ANISOU 1928  CA  LYS A 274     8790   9635   8141    628    168    376       C  
ATOM   1929  C   LYS A 274      -3.770  14.998 -33.648  1.00 59.95           C  
ANISOU 1929  C   LYS A 274     7393   8481   6904    479    203    464       C  
ATOM   1930  O   LYS A 274      -3.180  14.588 -32.648  1.00 59.55           O  
ANISOU 1930  O   LYS A 274     7331   8423   6873    433    218    489       O  
ATOM   1931  CB  LYS A 274      -2.812  17.272 -33.123  1.00 72.74           C  
ANISOU 1931  CB  LYS A 274     9239   9923   8476    723    149    329       C  
ATOM   1932  CG  LYS A 274      -1.311  17.148 -33.191  1.00 77.11           C  
ANISOU 1932  CG  LYS A 274     9903  10259   9135    616    152    329       C  
ATOM   1933  CD  LYS A 274      -0.663  18.283 -32.419  1.00 82.58           C  
ANISOU 1933  CD  LYS A 274    10718  10866   9794    726    112    273       C  
ATOM   1934  CE  LYS A 274      -0.770  19.592 -33.183  1.00 83.41           C  
ANISOU 1934  CE  LYS A 274    10966  10870   9856    832     42    212       C  
ATOM   1935  NZ  LYS A 274       0.076  19.563 -34.409  1.00 82.78           N1+
ANISOU 1935  NZ  LYS A 274    10975  10616   9862    703     38    224       N1+
ATOM   1936  N   ARG A 275      -4.608  14.249 -34.362  1.00 52.43           N  
ANISOU 1936  N   ARG A 275     6349   7622   5950    398    206    514       N  
ATOM   1937  CA  ARG A 275      -4.852  12.841 -34.066  1.00 43.22           C  
ANISOU 1937  CA  ARG A 275     5080   6535   4807    230    213    609       C  
ATOM   1938  C   ARG A 275      -3.559  12.032 -34.151  1.00 36.41           C  
ANISOU 1938  C   ARG A 275     4307   5462   4066    100    206    625       C  
ATOM   1939  O   ARG A 275      -2.734  12.231 -35.052  1.00 37.68           O  
ANISOU 1939  O   ARG A 275     4577   5438   4304     94    198    580       O  
ATOM   1940  CB  ARG A 275      -5.926  12.290 -35.008  1.00 44.54           C  
ANISOU 1940  CB  ARG A 275     5161   6808   4954    164    199    653       C  
ATOM   1941  CG  ARG A 275      -6.050  10.778 -35.075  1.00 52.04           C  
ANISOU 1941  CG  ARG A 275     6055   7767   5949    -41    175    754       C  
ATOM   1942  CD  ARG A 275      -7.227  10.389 -35.979  1.00 60.26           C  
ANISOU 1942  CD  ARG A 275     7009   8932   6953    -95    154    796       C  
ATOM   1943  NE  ARG A 275      -7.352   8.943 -36.173  1.00 65.01           N  
ANISOU 1943  NE  ARG A 275     7587   9514   7600   -302    105    894       N  
ATOM   1944  CZ  ARG A 275      -8.451   8.340 -36.622  1.00 69.09           C  
ANISOU 1944  CZ  ARG A 275     8005  10176   8069   -400     73    966       C  
ATOM   1945  NH1 ARG A 275      -9.530   9.053 -36.917  1.00 70.12           N1+
ANISOU 1945  NH1 ARG A 275     8034  10507   8102   -301     98    947       N1+
ATOM   1946  NH2 ARG A 275      -8.479   7.022 -36.770  1.00 71.10           N  
ANISOU 1946  NH2 ARG A 275     8270  10380   8366   -597      5   1058       N  
ATOM   1947  N   LYS A 276      -3.377  11.144 -33.183  1.00 30.36           N  
ANISOU 1947  N   LYS A 276     3494   4740   3303      3    205    687       N  
ATOM   1948  CA  LYS A 276      -2.172  10.338 -33.085  1.00 33.20           C  
ANISOU 1948  CA  LYS A 276     3936   4921   3758    -99    190    695       C  
ATOM   1949  C   LYS A 276      -2.371   8.944 -33.671  1.00 32.75           C  
ANISOU 1949  C   LYS A 276     3868   4829   3745   -260    140    764       C  
ATOM   1950  O   LYS A 276      -3.475   8.416 -33.679  1.00 39.21           O  
ANISOU 1950  O   LYS A 276     4589   5797   4512   -333    119    838       O  
ATOM   1951  CB  LYS A 276      -1.742  10.223 -31.619  1.00 33.03           C  
ANISOU 1951  CB  LYS A 276     3896   4942   3712    -98    205    714       C  
ATOM   1952  CG  LYS A 276      -1.310  11.537 -30.981  1.00 39.57           C  
ANISOU 1952  CG  LYS A 276     4767   5761   4506     60    236    639       C  
ATOM   1953  CD  LYS A 276      -0.953  11.323 -29.512  1.00 52.24           C  
ANISOU 1953  CD  LYS A 276     6342   7420   6085     59    250    663       C  
ATOM   1954  CE  LYS A 276      -0.652  12.632 -28.799  1.00 57.13           C  
ANISOU 1954  CE  LYS A 276     7004   8046   6658    226    266    590       C  
ATOM   1955  NZ  LYS A 276      -0.707  12.469 -27.324  1.00 59.84           N1+
ANISOU 1955  NZ  LYS A 276     7278   8513   6944    248    282    619       N1+
ATOM   1956  N   TYR A 277      -1.293   8.348 -34.159  1.00 25.16           N  
ANISOU 1956  N   TYR A 277     3009   3679   2872   -313    110    740       N  
ATOM   1957  CA  TYR A 277      -1.358   7.002 -34.695  1.00 22.37           C  
ANISOU 1957  CA  TYR A 277     2678   3261   2559   -447     38    792       C  
ATOM   1958  C   TYR A 277      -0.072   6.289 -34.369  1.00 24.94           C  
ANISOU 1958  C   TYR A 277     3102   3431   2943   -483      3    769       C  
ATOM   1959  O   TYR A 277       0.956   6.930 -34.136  1.00 24.41           O  
ANISOU 1959  O   TYR A 277     3086   3290   2897   -402     43    700       O  
ATOM   1960  CB  TYR A 277      -1.415   7.046 -36.222  1.00 32.04           C  
ANISOU 1960  CB  TYR A 277     3944   4404   3825   -431     18    753       C  
ATOM   1961  CG  TYR A 277      -2.601   7.716 -36.848  1.00 25.41           C  
ANISOU 1961  CG  TYR A 277     3028   3690   2937   -386     43    758       C  
ATOM   1962  CD1 TYR A 277      -3.721   6.979 -37.214  1.00 34.13           C  
ANISOU 1962  CD1 TYR A 277     4063   4892   4013   -483     -2    832       C  
ATOM   1963  CD2 TYR A 277      -2.586   9.070 -37.130  1.00 25.77           C  
ANISOU 1963  CD2 TYR A 277     3081   3749   2959   -249     98    689       C  
ATOM   1964  CE1 TYR A 277      -4.803   7.579 -37.840  1.00 37.85           C  
ANISOU 1964  CE1 TYR A 277     4459   5489   4434   -433     20    831       C  
ATOM   1965  CE2 TYR A 277      -3.672   9.686 -37.752  1.00 33.11           C  
ANISOU 1965  CE2 TYR A 277     3954   4790   3839   -190    112    683       C  
ATOM   1966  CZ  TYR A 277      -4.774   8.931 -38.106  1.00 37.33           C  
ANISOU 1966  CZ  TYR A 277     4404   5436   4344   -277     79    751       C  
ATOM   1967  OH  TYR A 277      -5.852   9.524 -38.720  1.00 45.00           O  
ANISOU 1967  OH  TYR A 277     5309   6532   5256   -212     92    741       O  
ATOM   1968  N   ARG A 278      -0.109   4.964 -34.420  1.00 22.35           N  
ANISOU 1968  N   ARG A 278     2810   3048   2633   -604    -84    824       N  
ATOM   1969  CA  ARG A 278       1.105   4.171 -34.300  1.00 27.59           C  
ANISOU 1969  CA  ARG A 278     3584   3554   3345   -620   -141    789       C  
ATOM   1970  C   ARG A 278       1.519   3.634 -35.664  1.00 26.42           C  
ANISOU 1970  C   ARG A 278     3518   3278   3244   -612   -208    740       C  
ATOM   1971  O   ARG A 278       0.699   3.146 -36.419  1.00 23.34           O  
ANISOU 1971  O   ARG A 278     3119   2897   2853   -673   -264    781       O  
ATOM   1972  CB  ARG A 278       0.895   3.008 -33.326  1.00 28.16           C  
ANISOU 1972  CB  ARG A 278     3672   3631   3396   -749   -219    878       C  
ATOM   1973  CG  ARG A 278       2.191   2.365 -32.866  1.00 39.27           C  
ANISOU 1973  CG  ARG A 278     5192   4895   4835   -736   -268    832       C  
ATOM   1974  CD  ARG A 278       1.947   1.297 -31.805  1.00 52.44           C  
ANISOU 1974  CD  ARG A 278     6885   6565   6473   -866   -350    926       C  
ATOM   1975  NE  ARG A 278       0.908   1.682 -30.847  1.00 62.54           N  
ANISOU 1975  NE  ARG A 278     8036   8039   7689   -927   -294   1021       N  
ATOM   1976  CZ  ARG A 278       1.112   2.423 -29.760  1.00 62.94           C  
ANISOU 1976  CZ  ARG A 278     8022   8181   7710   -864   -205   1011       C  
ATOM   1977  NH1 ARG A 278       2.324   2.888 -29.484  1.00 52.51           N1+
ANISOU 1977  NH1 ARG A 278     6759   6765   6426   -752   -159    916       N1+
ATOM   1978  NH2 ARG A 278       0.094   2.704 -28.953  1.00 68.98           N  
ANISOU 1978  NH2 ARG A 278     8659   9150   8400   -910   -165   1096       N  
ATOM   1979  N   VAL A 279       2.808   3.708 -35.959  1.00 24.57           N  
ANISOU 1979  N   VAL A 279     3358   2939   3041   -534   -206    652       N  
ATOM   1980  CA  VAL A 279       3.342   3.241 -37.224  1.00 25.13           C  
ANISOU 1980  CA  VAL A 279     3497   2912   3139   -499   -268    592       C  
ATOM   1981  C   VAL A 279       3.585   1.735 -37.228  1.00 30.32           C  
ANISOU 1981  C   VAL A 279     4256   3462   3803   -557   -411    605       C  
ATOM   1982  O   VAL A 279       4.337   1.217 -36.399  1.00 28.28           O  
ANISOU 1982  O   VAL A 279     4055   3151   3539   -558   -447    592       O  
ATOM   1983  CB  VAL A 279       4.656   3.941 -37.513  1.00 22.49           C  
ANISOU 1983  CB  VAL A 279     3185   2547   2811   -392   -213    494       C  
ATOM   1984  CG1 VAL A 279       5.268   3.426 -38.815  1.00 22.21           C  
ANISOU 1984  CG1 VAL A 279     3206   2447   2786   -341   -279    427       C  
ATOM   1985  CG2 VAL A 279       4.418   5.438 -37.549  1.00 20.35           C  
ANISOU 1985  CG2 VAL A 279     2846   2355   2529   -343   -100    486       C  
ATOM   1986  N   CYS A 280       2.951   1.027 -38.156  1.00 26.39           N  
ANISOU 1986  N   CYS A 280     3791   2923   3313   -602   -503    628       N  
ATOM   1987  CA  CYS A 280       3.191  -0.406 -38.264  1.00 34.71           C  
ANISOU 1987  CA  CYS A 280     4972   3850   4367   -648   -669    634       C  
ATOM   1988  C   CYS A 280       4.008  -0.754 -39.506  1.00 36.83           C  
ANISOU 1988  C   CYS A 280     5318   4031   4643   -533   -737    528       C  
ATOM   1989  O   CYS A 280       4.563  -1.849 -39.588  1.00 39.67           O  
ANISOU 1989  O   CYS A 280     5804   4276   4993   -512   -879    492       O  
ATOM   1990  CB  CYS A 280       1.883  -1.207 -38.219  1.00 36.93           C  
ANISOU 1990  CB  CYS A 280     5260   4135   4635   -807   -768    753       C  
ATOM   1991  SG  CYS A 280       0.718  -0.817 -39.549  1.00 54.53           S  
ANISOU 1991  SG  CYS A 280     7414   6431   6874   -824   -748    776       S  
ATOM   1992  N   ASN A 281       4.092   0.174 -40.461  1.00 34.31           N  
ANISOU 1992  N   ASN A 281     4930   3772   4334   -450   -644    475       N  
ATOM   1993  CA  ASN A 281       4.953  -0.030 -41.625  1.00 30.09           C  
ANISOU 1993  CA  ASN A 281     4444   3196   3793   -329   -692    371       C  
ATOM   1994  C   ASN A 281       5.268   1.227 -42.446  1.00 28.36           C  
ANISOU 1994  C   ASN A 281     4135   3069   3573   -248   -564    320       C  
ATOM   1995  O   ASN A 281       4.740   2.308 -42.202  1.00 27.81           O  
ANISOU 1995  O   ASN A 281     3980   3075   3512   -278   -446    360       O  
ATOM   1996  CB  ASN A 281       4.365  -1.105 -42.549  1.00 37.94           C  
ANISOU 1996  CB  ASN A 281     5521   4103   4791   -352   -846    381       C  
ATOM   1997  CG  ASN A 281       5.435  -1.947 -43.214  1.00 42.91           C  
ANISOU 1997  CG  ASN A 281     6260   4653   5391   -223   -972    272       C  
ATOM   1998  ND2 ASN A 281       5.031  -3.079 -43.771  1.00 45.78           N  
ANISOU 1998  ND2 ASN A 281     6737   4907   5752   -238  -1146    276       N  
ATOM   1999  OD1 ASN A 281       6.612  -1.582 -43.230  1.00 44.74           O  
ANISOU 1999  OD1 ASN A 281     6473   4932   5594   -108   -921    183       O  
ATOM   2000  N   VAL A 282       6.156   1.059 -43.416  1.00 25.82           N  
ANISOU 2000  N   VAL A 282     3839   2744   3227   -139   -600    229       N  
ATOM   2001  CA  VAL A 282       6.450   2.086 -44.393  1.00 31.51           C  
ANISOU 2001  CA  VAL A 282     4487   3550   3936    -77   -508    188       C  
ATOM   2002  C   VAL A 282       6.242   1.463 -45.779  1.00 32.31           C  
ANISOU 2002  C   VAL A 282     4620   3625   4030    -20   -601    148       C  
ATOM   2003  O   VAL A 282       6.784   0.399 -46.079  1.00 33.30           O  
ANISOU 2003  O   VAL A 282     4827   3697   4129     50   -729     89       O  
ATOM   2004  CB  VAL A 282       7.885   2.607 -44.235  1.00 26.19           C  
ANISOU 2004  CB  VAL A 282     3787   2946   3218      0   -450    116       C  
ATOM   2005  CG1 VAL A 282       8.209   3.647 -45.312  1.00 21.52           C  
ANISOU 2005  CG1 VAL A 282     3125   2451   2602     40   -370     88       C  
ATOM   2006  CG2 VAL A 282       8.090   3.192 -42.819  1.00 20.08           C  
ANISOU 2006  CG2 VAL A 282     2992   2185   2453    -54   -369    154       C  
ATOM   2007  N   THR A 283       5.430   2.111 -46.605  1.00 27.40           N  
ANISOU 2007  N   THR A 283     3943   3039   3428    -40   -548    177       N  
ATOM   2008  CA  THR A 283       5.082   1.566 -47.920  1.00 21.37           C  
ANISOU 2008  CA  THR A 283     3206   2252   2663      8   -632    147       C  
ATOM   2009  C   THR A 283       6.309   1.472 -48.811  1.00 21.50           C  
ANISOU 2009  C   THR A 283     3221   2324   2622    143   -658     45       C  
ATOM   2010  O   THR A 283       7.216   2.285 -48.693  1.00 28.68           O  
ANISOU 2010  O   THR A 283     4072   3329   3497    174   -566     15       O  
ATOM   2011  CB  THR A 283       4.007   2.433 -48.625  1.00 21.04           C  
ANISOU 2011  CB  THR A 283     3094   2252   2646    -33   -553    195       C  
ATOM   2012  CG2 THR A 283       2.725   2.450 -47.813  1.00 21.14           C  
ANISOU 2012  CG2 THR A 283     3090   2249   2693   -153   -538    291       C  
ATOM   2013  OG1 THR A 283       4.484   3.777 -48.781  1.00 25.81           O  
ANISOU 2013  OG1 THR A 283     3627   2948   3232     -8   -423    181       O  
ATOM   2014  N   ARG A 284       6.342   0.465 -49.682  1.00 28.99           N  
ANISOU 2014  N   ARG A 284     4236   3226   3552    222   -794     -9       N  
ATOM   2015  CA  ARG A 284       7.344   0.394 -50.748  1.00 28.05           C  
ANISOU 2015  CA  ARG A 284     4096   3197   3363    369   -822   -109       C  
ATOM   2016  C   ARG A 284       7.103   1.494 -51.789  1.00 26.68           C  
ANISOU 2016  C   ARG A 284     3823   3127   3187    368   -712    -97       C  
ATOM   2017  O   ARG A 284       8.041   2.056 -52.349  1.00 21.93           O  
ANISOU 2017  O   ARG A 284     3152   2659   2520    437   -658   -146       O  
ATOM   2018  CB  ARG A 284       7.295  -0.966 -51.451  1.00 35.95           C  
ANISOU 2018  CB  ARG A 284     5206   4112   4341    468  -1013   -173       C  
ATOM   2019  CG  ARG A 284       7.910  -2.118 -50.685  1.00 46.56           C  
ANISOU 2019  CG  ARG A 284     6670   5367   5652    523  -1157   -221       C  
ATOM   2020  CD  ARG A 284       7.646  -3.450 -51.401  1.00 60.36           C  
ANISOU 2020  CD  ARG A 284     8558   6995   7381    612  -1375   -274       C  
ATOM   2021  NE  ARG A 284       6.292  -3.944 -51.147  1.00 72.00           N  
ANISOU 2021  NE  ARG A 284    10111   8314   8931    458  -1450   -172       N  
ATOM   2022  CZ  ARG A 284       5.533  -4.577 -52.039  1.00 78.51           C  
ANISOU 2022  CZ  ARG A 284    11007   9052   9770    465  -1577   -168       C  
ATOM   2023  NH1 ARG A 284       5.982  -4.799 -53.269  1.00 83.34           N1+
ANISOU 2023  NH1 ARG A 284    11624   9711  10329    635  -1644   -270       N1+
ATOM   2024  NH2 ARG A 284       4.316  -4.984 -51.701  1.00 76.11           N  
ANISOU 2024  NH2 ARG A 284    10761   8631   9526    298  -1640    -60       N  
ATOM   2025  N   ARG A 285       5.838   1.800 -52.043  1.00 23.62           N  
ANISOU 2025  N   ARG A 285     3427   2688   2860    284   -684    -27       N  
ATOM   2026  CA  ARG A 285       5.470   2.781 -53.058  1.00 23.33           C  
ANISOU 2026  CA  ARG A 285     3316   2727   2823    285   -596    -14       C  
ATOM   2027  C   ARG A 285       5.526   4.220 -52.524  1.00 25.83           C  
ANISOU 2027  C   ARG A 285     3564   3107   3142    210   -445     37       C  
ATOM   2028  O   ARG A 285       5.211   4.462 -51.358  1.00 24.15           O  
ANISOU 2028  O   ARG A 285     3361   2854   2962    132   -404     87       O  
ATOM   2029  CB  ARG A 285       4.065   2.449 -53.607  1.00 24.89           C  
ANISOU 2029  CB  ARG A 285     3537   2846   3074    241   -644     30       C  
ATOM   2030  CG  ARG A 285       4.080   1.269 -54.588  1.00 27.12           C  
ANISOU 2030  CG  ARG A 285     3886   3080   3341    336   -797    -32       C  
ATOM   2031  CD  ARG A 285       2.836   0.350 -54.534  1.00 39.95           C  
ANISOU 2031  CD  ARG A 285     5586   4575   5019    262   -911     21       C  
ATOM   2032  NE  ARG A 285       1.669   0.857 -55.260  1.00 57.70           N  
ANISOU 2032  NE  ARG A 285     7785   6836   7303    212   -864     68       N  
ATOM   2033  CZ  ARG A 285       1.311   0.496 -56.500  1.00 67.54           C  
ANISOU 2033  CZ  ARG A 285     9046   8067   8546    276   -935     34       C  
ATOM   2034  NH1 ARG A 285       2.044  -0.386 -57.188  1.00 65.29           N1+
ANISOU 2034  NH1 ARG A 285     8828   7758   8221    406  -1064    -53       N1+
ATOM   2035  NH2 ARG A 285       0.214   1.022 -57.059  1.00 22.65           N  
ANISOU 2035  NH2 ARG A 285     3312   2401   2893    226   -883     81       N  
ATOM   2036  N   PRO A 286       5.948   5.174 -53.376  1.00 23.13           N  
ANISOU 2036  N   PRO A 286     3164   2866   2759    233   -374     24       N  
ATOM   2037  CA  PRO A 286       5.808   6.604 -53.071  1.00 19.98           C  
ANISOU 2037  CA  PRO A 286     2730   2501   2362    159   -257     77       C  
ATOM   2038  C   PRO A 286       4.330   6.944 -52.874  1.00 22.30           C  
ANISOU 2038  C   PRO A 286     3035   2721   2716    101   -232    137       C  
ATOM   2039  O   PRO A 286       3.479   6.238 -53.414  1.00 19.95           O  
ANISOU 2039  O   PRO A 286     2752   2379   2450    115   -293    138       O  
ATOM   2040  CB  PRO A 286       6.303   7.302 -54.342  1.00 27.60           C  
ANISOU 2040  CB  PRO A 286     3647   3571   3268    191   -227     58       C  
ATOM   2041  CG  PRO A 286       6.954   6.247 -55.208  1.00 25.31           C  
ANISOU 2041  CG  PRO A 286     3345   3341   2931    300   -315    -17       C  
ATOM   2042  CD  PRO A 286       6.497   4.910 -54.723  1.00 21.94           C  
ANISOU 2042  CD  PRO A 286     2985   2799   2550    333   -418    -39       C  
ATOM   2043  N   ALA A 287       4.027   7.998 -52.113  1.00 19.41           N  
ANISOU 2043  N   ALA A 287     2665   2352   2357     44   -154    183       N  
ATOM   2044  CA  ALA A 287       2.652   8.487 -51.977  1.00 22.11           C  
ANISOU 2044  CA  ALA A 287     3005   2665   2731     13   -126    229       C  
ATOM   2045  C   ALA A 287       1.965   8.682 -53.339  1.00 23.49           C  
ANISOU 2045  C   ALA A 287     3168   2852   2906     45   -134    222       C  
ATOM   2046  O   ALA A 287       0.752   8.479 -53.475  1.00 19.51           O  
ANISOU 2046  O   ALA A 287     2655   2329   2429     36   -149    247       O  
ATOM   2047  CB  ALA A 287       2.629   9.789 -51.202  1.00 19.09           C  
ANISOU 2047  CB  ALA A 287     2630   2293   2331    -15    -51    258       C  
ATOM   2048  N   SER A 288       2.747   9.103 -54.331  1.00 19.42           N  
ANISOU 2048  N   SER A 288     2644   2385   2351     78   -124    193       N  
ATOM   2049  CA  SER A 288       2.241   9.255 -55.694  1.00 21.25           C  
ANISOU 2049  CA  SER A 288     2864   2634   2577    114   -135    182       C  
ATOM   2050  C   SER A 288       1.673   7.955 -56.292  1.00 24.80           C  
ANISOU 2050  C   SER A 288     3313   3052   3060    154   -218    158       C  
ATOM   2051  O   SER A 288       0.699   7.988 -57.029  1.00 19.85           O  
ANISOU 2051  O   SER A 288     2679   2411   2451    166   -228    166       O  
ATOM   2052  CB  SER A 288       3.331   9.803 -56.604  1.00 25.66           C  
ANISOU 2052  CB  SER A 288     3403   3274   3071    133   -117    160       C  
ATOM   2053  OG  SER A 288       2.978   9.568 -57.951  1.00 32.65           O  
ANISOU 2053  OG  SER A 288     4271   4185   3951    185   -147    137       O  
ATOM   2054  N   HIS A 289       2.292   6.822 -55.977  1.00 20.04           N  
ANISOU 2054  N   HIS A 289     2726   2429   2458    177   -290    127       N  
ATOM   2055  CA  HIS A 289       1.872   5.541 -56.525  1.00 20.47           C  
ANISOU 2055  CA  HIS A 289     2809   2433   2536    217   -400    101       C  
ATOM   2056  C   HIS A 289       0.980   4.717 -55.580  1.00 29.86           C  
ANISOU 2056  C   HIS A 289     4034   3537   3774    146   -458    146       C  
ATOM   2057  O   HIS A 289       0.276   3.823 -56.045  1.00 22.36           O  
ANISOU 2057  O   HIS A 289     3115   2533   2848    144   -552    149       O  
ATOM   2058  CB  HIS A 289       3.086   4.684 -56.890  1.00 22.54           C  
ANISOU 2058  CB  HIS A 289     3089   2724   2752    308   -480     27       C  
ATOM   2059  CG  HIS A 289       4.014   5.313 -57.882  1.00 30.30           C  
ANISOU 2059  CG  HIS A 289     4017   3830   3665    375   -438    -15       C  
ATOM   2060  CD2 HIS A 289       5.234   4.910 -58.329  1.00 21.37           C  
ANISOU 2060  CD2 HIS A 289     2865   2797   2459    469   -479    -83       C  
ATOM   2061  ND1 HIS A 289       3.741   6.493 -58.544  1.00 28.20           N  
ANISOU 2061  ND1 HIS A 289     3710   3618   3387    347   -351     16       N  
ATOM   2062  CE1 HIS A 289       4.745   6.791 -59.345  1.00 22.41           C  
ANISOU 2062  CE1 HIS A 289     2928   3009   2575    400   -339    -19       C  
ATOM   2063  NE2 HIS A 289       5.664   5.846 -59.228  1.00 21.36           N  
ANISOU 2063  NE2 HIS A 289     2796   2921   2400    479   -411    -81       N  
ATOM   2064  N   GLN A 290       1.025   4.994 -54.269  1.00 20.48           N  
ANISOU 2064  N   GLN A 290     2845   2344   2594     80   -411    186       N  
ATOM   2065  CA  GLN A 290       0.277   4.197 -53.271  1.00 20.82           C  
ANISOU 2065  CA  GLN A 290     2913   2330   2667     -3   -467    241       C  
ATOM   2066  C   GLN A 290      -1.244   4.370 -53.362  1.00 24.09           C  
ANISOU 2066  C   GLN A 290     3290   2761   3102    -68   -455    303       C  
ATOM   2067  O   GLN A 290      -1.757   5.489 -53.259  1.00 22.86           O  
ANISOU 2067  O   GLN A 290     3082   2668   2935    -71   -357    324       O  
ATOM   2068  CB  GLN A 290       0.740   4.532 -51.841  1.00 20.58           C  
ANISOU 2068  CB  GLN A 290     2878   2310   2631    -48   -412    267       C  
ATOM   2069  CG  GLN A 290       0.036   3.719 -50.742  1.00 21.02           C  
ANISOU 2069  CG  GLN A 290     2953   2328   2707   -146   -469    332       C  
ATOM   2070  CD  GLN A 290       0.380   2.230 -50.807  1.00 23.66           C  
ANISOU 2070  CD  GLN A 290     3376   2567   3047   -148   -621    314       C  
ATOM   2071  NE2 GLN A 290      -0.640   1.383 -50.826  1.00 22.36           N  
ANISOU 2071  NE2 GLN A 290     3240   2357   2899   -233   -717    372       N  
ATOM   2072  OE1 GLN A 290       1.551   1.856 -50.864  1.00 24.92           O  
ANISOU 2072  OE1 GLN A 290     3582   2698   3187    -73   -661    248       O  
ATOM   2073  N   THR A 291      -1.955   3.259 -53.544  1.00 21.62           N  
ANISOU 2073  N   THR A 291     3011   2396   2809   -118   -567    332       N  
ATOM   2074  CA  THR A 291      -3.412   3.278 -53.635  1.00 21.98           C  
ANISOU 2074  CA  THR A 291     3009   2480   2861   -194   -569    397       C  
ATOM   2075  C   THR A 291      -4.073   2.643 -52.406  1.00 30.49           C  
ANISOU 2075  C   THR A 291     4081   3568   3936   -325   -613    484       C  
ATOM   2076  O   THR A 291      -3.445   1.889 -51.673  1.00 22.83           O  
ANISOU 2076  O   THR A 291     3172   2531   2969   -360   -680    491       O  
ATOM   2077  CB  THR A 291      -3.942   2.562 -54.915  1.00 29.84           C  
ANISOU 2077  CB  THR A 291     4034   3430   3873   -176   -669    381       C  
ATOM   2078  CG2 THR A 291      -3.393   3.203 -56.193  1.00 24.47           C  
ANISOU 2078  CG2 THR A 291     3347   2765   3187    -49   -624    303       C  
ATOM   2079  OG1 THR A 291      -3.584   1.175 -54.892  1.00 30.41           O  
ANISOU 2079  OG1 THR A 291     4206   3393   3956   -199   -827    375       O  
ATOM   2080  N   PHE A 292      -5.340   2.973 -52.185  1.00 27.09           N  
ANISOU 2080  N   PHE A 292     3570   3235   3486   -395   -576    550       N  
ATOM   2081  CA  PHE A 292      -6.146   2.383 -51.122  1.00 24.36           C  
ANISOU 2081  CA  PHE A 292     3193   2943   3119   -538   -620    649       C  
ATOM   2082  C   PHE A 292      -7.592   2.417 -51.619  1.00 25.81           C  
ANISOU 2082  C   PHE A 292     3297   3232   3279   -599   -628    704       C  
ATOM   2083  O   PHE A 292      -7.931   3.231 -52.484  1.00 23.89           O  
ANISOU 2083  O   PHE A 292     3011   3036   3031   -509   -559    659       O  
ATOM   2084  CB  PHE A 292      -5.991   3.155 -49.785  1.00 23.40           C  
ANISOU 2084  CB  PHE A 292     3011   2913   2965   -543   -514    672       C  
ATOM   2085  CG  PHE A 292      -6.587   4.540 -49.808  1.00 32.83           C  
ANISOU 2085  CG  PHE A 292     4111   4240   4122   -468   -386    656       C  
ATOM   2086  CD1 PHE A 292      -7.906   4.753 -49.421  1.00 23.72           C  
ANISOU 2086  CD1 PHE A 292     2852   3250   2913   -524   -362    722       C  
ATOM   2087  CD2 PHE A 292      -5.827   5.632 -50.230  1.00 28.99           C  
ANISOU 2087  CD2 PHE A 292     3646   3725   3642   -340   -301    576       C  
ATOM   2088  CE1 PHE A 292      -8.458   6.029 -49.450  1.00 25.99           C  
ANISOU 2088  CE1 PHE A 292     3065   3659   3150   -426   -261    692       C  
ATOM   2089  CE2 PHE A 292      -6.371   6.917 -50.269  1.00 22.77           C  
ANISOU 2089  CE2 PHE A 292     2802   3035   2813   -263   -208    557       C  
ATOM   2090  CZ  PHE A 292      -7.690   7.117 -49.894  1.00 22.89           C  
ANISOU 2090  CZ  PHE A 292     2723   3203   2772   -291   -191    607       C  
ATOM   2091  N   PRO A 293      -8.446   1.528 -51.096  1.00 29.18           N  
ANISOU 2091  N   PRO A 293     3704   3701   3681   -758   -717    805       N  
ATOM   2092  CA  PRO A 293      -9.864   1.595 -51.475  1.00 26.08           C  
ANISOU 2092  CA  PRO A 293     3212   3449   3247   -828   -719    865       C  
ATOM   2093  C   PRO A 293     -10.609   2.706 -50.724  1.00 31.77           C  
ANISOU 2093  C   PRO A 293     3786   4389   3897   -804   -584    890       C  
ATOM   2094  O   PRO A 293     -10.826   2.595 -49.526  1.00 33.32           O  
ANISOU 2094  O   PRO A 293     3927   4686   4046   -891   -573    960       O  
ATOM   2095  CB  PRO A 293     -10.395   0.216 -51.078  1.00 27.40           C  
ANISOU 2095  CB  PRO A 293     3417   3591   3401  -1031   -878    977       C  
ATOM   2096  CG  PRO A 293      -9.481  -0.234 -49.958  1.00 27.37           C  
ANISOU 2096  CG  PRO A 293     3488   3506   3407  -1072   -910    995       C  
ATOM   2097  CD  PRO A 293      -8.139   0.378 -50.224  1.00 29.39           C  
ANISOU 2097  CD  PRO A 293     3809   3649   3710   -888   -836    870       C  
ATOM   2098  N   LEU A 294     -10.967   3.777 -51.426  1.00 25.60           N  
ANISOU 2098  N   LEU A 294     2949   3678   3098   -675   -491    826       N  
ATOM   2099  CA  LEU A 294     -11.670   4.905 -50.829  1.00 27.30           C  
ANISOU 2099  CA  LEU A 294     3044   4095   3233   -610   -378    826       C  
ATOM   2100  C   LEU A 294     -13.151   4.594 -50.757  1.00 31.42           C  
ANISOU 2100  C   LEU A 294     3436   4828   3676   -714   -406    911       C  
ATOM   2101  O   LEU A 294     -13.803   4.407 -51.793  1.00 32.00           O  
ANISOU 2101  O   LEU A 294     3495   4912   3754   -721   -442    908       O  
ATOM   2102  CB  LEU A 294     -11.486   6.147 -51.699  1.00 26.26           C  
ANISOU 2102  CB  LEU A 294     2930   3941   3108   -428   -293    723       C  
ATOM   2103  CG  LEU A 294     -11.599   7.577 -51.152  1.00 34.38           C  
ANISOU 2103  CG  LEU A 294     3913   5079   4070   -291   -185    674       C  
ATOM   2104  CD1 LEU A 294     -11.806   8.537 -52.304  1.00 41.40           C  
ANISOU 2104  CD1 LEU A 294     4826   5951   4955   -152   -145    595       C  
ATOM   2105  CD2 LEU A 294     -12.674   7.774 -50.105  1.00 34.78           C  
ANISOU 2105  CD2 LEU A 294     3828   5375   4013   -319   -158    732       C  
ATOM   2106  N   GLN A 295     -13.688   4.580 -49.541  1.00 28.27           N  
ANISOU 2106  N   GLN A 295     2931   4616   3193   -792   -387    987       N  
ATOM   2107  CA  GLN A 295     -15.090   4.273 -49.331  1.00 32.19           C  
ANISOU 2107  CA  GLN A 295     3277   5365   3588   -909   -412   1082       C  
ATOM   2108  C   GLN A 295     -15.975   5.490 -49.565  1.00 29.33           C  
ANISOU 2108  C   GLN A 295     2793   5219   3133   -751   -314   1024       C  
ATOM   2109  O   GLN A 295     -15.729   6.565 -49.036  1.00 34.42           O  
ANISOU 2109  O   GLN A 295     3421   5919   3737   -594   -224    957       O  
ATOM   2110  CB  GLN A 295     -15.300   3.742 -47.911  1.00 45.86           C  
ANISOU 2110  CB  GLN A 295     4932   7241   5250  -1061   -435   1194       C  
ATOM   2111  CG  GLN A 295     -16.735   3.359 -47.591  1.00 56.86           C  
ANISOU 2111  CG  GLN A 295     6149   8938   6516  -1214   -467   1314       C  
ATOM   2112  CD  GLN A 295     -16.962   3.179 -46.101  1.00 69.53           C  
ANISOU 2112  CD  GLN A 295     7647  10749   8023  -1322   -456   1412       C  
ATOM   2113  NE2 GLN A 295     -18.210   3.336 -45.665  1.00 71.14           N  
ANISOU 2113  NE2 GLN A 295     7647  11307   8074  -1380   -434   1488       N  
ATOM   2114  OE1 GLN A 295     -16.022   2.916 -45.349  1.00 76.06           O  
ANISOU 2114  OE1 GLN A 295     8564  11433   8901  -1346   -466   1418       O  
ATOM   2115  N   LEU A 296     -17.023   5.300 -50.349  1.00 35.36           N  
ANISOU 2115  N   LEU A 296     3478   6103   3854   -790   -344   1049       N  
ATOM   2116  CA  LEU A 296     -17.965   6.367 -50.657  1.00 35.42           C  
ANISOU 2116  CA  LEU A 296     3370   6328   3759   -635   -267    991       C  
ATOM   2117  C   LEU A 296     -19.128   6.380 -49.657  1.00 39.00           C  
ANISOU 2117  C   LEU A 296     3618   7152   4049   -703   -251   1076       C  
ATOM   2118  O   LEU A 296     -19.352   5.405 -48.944  1.00 45.44           O  
ANISOU 2118  O   LEU A 296     4376   8054   4835   -915   -314   1202       O  
ATOM   2119  CB  LEU A 296     -18.502   6.202 -52.084  1.00 30.42           C  
ANISOU 2119  CB  LEU A 296     2751   5649   3158   -626   -304    964       C  
ATOM   2120  CG  LEU A 296     -17.485   6.088 -53.229  1.00 31.89           C  
ANISOU 2120  CG  LEU A 296     3117   5510   3490   -566   -331    887       C  
ATOM   2121  CD1 LEU A 296     -18.203   6.232 -54.589  1.00 31.15           C  
ANISOU 2121  CD1 LEU A 296     3007   5430   3397   -510   -343    846       C  
ATOM   2122  CD2 LEU A 296     -16.348   7.105 -53.092  1.00 27.78           C  
ANISOU 2122  CD2 LEU A 296     2704   4836   3016   -389   -252    783       C  
ATOM   2123  N   GLU A 297     -19.849   7.497 -49.612  1.00 33.60           N  
ANISOU 2123  N   GLU A 297     2829   6693   3246   -516   -176   1005       N  
ATOM   2124  CA  GLU A 297     -21.039   7.648 -48.786  1.00 42.79           C  
ANISOU 2124  CA  GLU A 297     3773   8261   4223   -534   -155   1064       C  
ATOM   2125  C   GLU A 297     -22.009   6.492 -49.001  1.00 41.95           C  
ANISOU 2125  C   GLU A 297     3542   8329   4067   -787   -236   1205       C  
ATOM   2126  O   GLU A 297     -22.624   6.017 -48.061  1.00 50.05           O  
ANISOU 2126  O   GLU A 297     4414   9629   4975   -937   -255   1321       O  
ATOM   2127  CB  GLU A 297     -21.732   8.974 -49.107  1.00 50.99           C  
ANISOU 2127  CB  GLU A 297     4743   9486   5145   -266    -87    943       C  
ATOM   2128  CG  GLU A 297     -23.063   9.171 -48.403  1.00 61.96           C  
ANISOU 2128  CG  GLU A 297     5885  11342   6315   -249    -69    987       C  
ATOM   2129  CD  GLU A 297     -22.909   9.567 -46.948  1.00 67.59           C  
ANISOU 2129  CD  GLU A 297     6522  12233   6924   -186    -30    996       C  
ATOM   2130  OE1 GLU A 297     -21.881  10.195 -46.606  1.00 67.63           O  
ANISOU 2130  OE1 GLU A 297     6678  12010   7007    -52      1    914       O  
ATOM   2131  OE2 GLU A 297     -23.822   9.255 -46.150  1.00 70.94           O1-
ANISOU 2131  OE2 GLU A 297     6731  13039   7182   -274    -33   1087       O1-
ATOM   2132  N   SER A 298     -22.126   6.032 -50.240  1.00 40.09           N  
ANISOU 2132  N   SER A 298     3378   7936   3917   -843   -290   1199       N  
ATOM   2133  CA  SER A 298     -23.001   4.913 -50.556  1.00 42.62           C  
ANISOU 2133  CA  SER A 298     3610   8382   4201  -1094   -388   1333       C  
ATOM   2134  C   SER A 298     -22.507   3.599 -49.943  1.00 53.16           C  
ANISOU 2134  C   SER A 298     5017   9583   5599  -1372   -496   1473       C  
ATOM   2135  O   SER A 298     -23.300   2.710 -49.640  1.00 57.86           O  
ANISOU 2135  O   SER A 298     5503  10369   6112  -1619   -580   1622       O  
ATOM   2136  CB  SER A 298     -23.103   4.747 -52.067  1.00 43.78           C  
ANISOU 2136  CB  SER A 298     3849   8343   4442  -1067   -430   1279       C  
ATOM   2137  OG  SER A 298     -21.853   4.366 -52.599  1.00 34.47           O  
ANISOU 2137  OG  SER A 298     2895   6758   3444  -1062   -472   1234       O  
ATOM   2138  N   GLY A 299     -21.194   3.473 -49.776  1.00 54.23           N  
ANISOU 2138  N   GLY A 299     5340   9393   5872  -1335   -503   1427       N  
ATOM   2139  CA  GLY A 299     -20.609   2.230 -49.310  1.00 48.78           C  
ANISOU 2139  CA  GLY A 299     4757   8524   5252  -1568   -621   1538       C  
ATOM   2140  C   GLY A 299     -19.855   1.474 -50.394  1.00 48.60           C  
ANISOU 2140  C   GLY A 299     4948   8127   5389  -1603   -726   1505       C  
ATOM   2141  O   GLY A 299     -19.226   0.455 -50.114  1.00 50.05           O  
ANISOU 2141  O   GLY A 299     5264   8112   5641  -1758   -841   1571       O  
ATOM   2142  N   GLN A 300     -19.920   1.958 -51.634  1.00 41.63           N  
ANISOU 2142  N   GLN A 300     4105   7154   4559  -1449   -696   1400       N  
ATOM   2143  CA  GLN A 300     -19.062   1.426 -52.685  1.00 33.21           C  
ANISOU 2143  CA  GLN A 300     3239   5741   3639  -1422   -778   1339       C  
ATOM   2144  C   GLN A 300     -17.642   1.902 -52.417  1.00 31.65           C  
ANISOU 2144  C   GLN A 300     3173   5321   3531  -1263   -715   1236       C  
ATOM   2145  O   GLN A 300     -17.426   2.786 -51.594  1.00 31.71           O  
ANISOU 2145  O   GLN A 300     3120   5436   3493  -1155   -602   1201       O  
ATOM   2146  CB  GLN A 300     -19.510   1.907 -54.072  1.00 32.78           C  
ANISOU 2146  CB  GLN A 300     3178   5672   3606  -1289   -751   1251       C  
ATOM   2147  CG  GLN A 300     -20.933   1.536 -54.474  1.00 34.28           C  
ANISOU 2147  CG  GLN A 300     3229   6093   3704  -1424   -805   1337       C  
ATOM   2148  CD  GLN A 300     -21.547   2.579 -55.393  1.00 50.68           C  
ANISOU 2148  CD  GLN A 300     5225   8285   5745  -1225   -706   1233       C  
ATOM   2149  NE2 GLN A 300     -21.967   2.159 -56.589  1.00 49.43           N  
ANISOU 2149  NE2 GLN A 300     5102   8054   5627  -1251   -777   1224       N  
ATOM   2150  OE1 GLN A 300     -21.632   3.754 -55.036  1.00 47.87           O  
ANISOU 2150  OE1 GLN A 300     4789   8073   5324  -1041   -576   1156       O  
ATOM   2151  N   THR A 301     -16.667   1.326 -53.110  1.00 46.44           N  
ANISOU 2151  N   THR A 301     5225   6897   5521  -1242   -795   1187       N  
ATOM   2152  CA  THR A 301     -15.291   1.792 -52.979  1.00 40.07           C  
ANISOU 2152  CA  THR A 301     4534   5899   4791  -1088   -735   1086       C  
ATOM   2153  C   THR A 301     -14.658   2.017 -54.341  1.00 33.61           C  
ANISOU 2153  C   THR A 301     3824   4888   4059   -935   -736    971       C  
ATOM   2154  O   THR A 301     -14.916   1.274 -55.277  1.00 40.62           O  
ANISOU 2154  O   THR A 301     4768   5686   4982   -986   -842    980       O  
ATOM   2155  CB  THR A 301     -14.429   0.817 -52.157  1.00 45.10           C  
ANISOU 2155  CB  THR A 301     5284   6383   5468  -1207   -832   1138       C  
ATOM   2156  CG2 THR A 301     -14.761   0.922 -50.678  1.00 43.64           C  
ANISOU 2156  CG2 THR A 301     4992   6389   5199  -1307   -789   1228       C  
ATOM   2157  OG1 THR A 301     -14.694  -0.518 -52.586  1.00 52.72           O  
ANISOU 2157  OG1 THR A 301     6338   7237   6458  -1377  -1013   1213       O  
ATOM   2158  N   VAL A 302     -13.853   3.067 -54.446  1.00 27.17           N  
ANISOU 2158  N   VAL A 302     3035   4022   3268   -752   -622    868       N  
ATOM   2159  CA  VAL A 302     -13.064   3.342 -55.643  1.00 26.18           C  
ANISOU 2159  CA  VAL A 302     3008   3726   3214   -610   -615    763       C  
ATOM   2160  C   VAL A 302     -11.595   3.363 -55.257  1.00 29.60           C  
ANISOU 2160  C   VAL A 302     3545   4005   3697   -549   -603    711       C  
ATOM   2161  O   VAL A 302     -11.255   3.687 -54.118  1.00 28.28           O  
ANISOU 2161  O   VAL A 302     3355   3884   3506   -562   -549    731       O  
ATOM   2162  CB  VAL A 302     -13.401   4.718 -56.251  1.00 25.59           C  
ANISOU 2162  CB  VAL A 302     2874   3741   3107   -447   -493    687       C  
ATOM   2163  CG1 VAL A 302     -14.839   4.769 -56.686  1.00 26.43           C  
ANISOU 2163  CG1 VAL A 302     2871   4018   3154   -481   -498    723       C  
ATOM   2164  CG2 VAL A 302     -13.123   5.822 -55.246  1.00 32.20           C  
ANISOU 2164  CG2 VAL A 302     3673   4664   3897   -367   -379    665       C  
ATOM   2165  N   GLU A 303     -10.717   3.024 -56.191  1.00 27.97           N  
ANISOU 2165  N   GLU A 303     3443   3633   3551   -476   -655    643       N  
ATOM   2166  CA  GLU A 303      -9.287   3.086 -55.910  1.00 33.75           C  
ANISOU 2166  CA  GLU A 303     4259   4250   4316   -405   -641    586       C  
ATOM   2167  C   GLU A 303      -8.833   4.535 -55.960  1.00 32.76           C  
ANISOU 2167  C   GLU A 303     4101   4172   4173   -276   -497    523       C  
ATOM   2168  O   GLU A 303      -9.177   5.257 -56.886  1.00 31.59           O  
ANISOU 2168  O   GLU A 303     3930   4056   4018   -192   -448    482       O  
ATOM   2169  CB  GLU A 303      -8.490   2.263 -56.921  1.00 36.84           C  
ANISOU 2169  CB  GLU A 303     4759   4484   4752   -351   -748    527       C  
ATOM   2170  CG  GLU A 303      -8.683   0.767 -56.807  1.00 52.53           C  
ANISOU 2170  CG  GLU A 303     6829   6375   6756   -468   -926    579       C  
ATOM   2171  CD  GLU A 303      -7.788   0.146 -55.752  1.00 64.58           C  
ANISOU 2171  CD  GLU A 303     8431   7821   8285   -511   -982    593       C  
ATOM   2172  OE1 GLU A 303      -6.550   0.299 -55.858  1.00 71.86           O  
ANISOU 2172  OE1 GLU A 303     9408   8677   9220   -395   -962    512       O  
ATOM   2173  OE2 GLU A 303      -8.322  -0.488 -54.815  1.00 59.09           O1-
ANISOU 2173  OE2 GLU A 303     7737   7143   7572   -665  -1047    688       O1-
ATOM   2174  N   CYS A 304      -8.059   4.958 -54.968  1.00 32.00           N  
ANISOU 2174  N   CYS A 304     4016   4074   4069   -264   -440    518       N  
ATOM   2175  CA  CYS A 304      -7.510   6.308 -54.965  1.00 29.56           C  
ANISOU 2175  CA  CYS A 304     3702   3787   3741   -156   -328    464       C  
ATOM   2176  C   CYS A 304      -6.025   6.274 -54.591  1.00 28.70           C  
ANISOU 2176  C   CYS A 304     3662   3590   3654   -129   -322    427       C  
ATOM   2177  O   CYS A 304      -5.606   5.393 -53.839  1.00 21.76           O  
ANISOU 2177  O   CYS A 304     2812   2666   2790   -194   -380    453       O  
ATOM   2178  CB  CYS A 304      -8.281   7.173 -53.965  1.00 25.98           C  
ANISOU 2178  CB  CYS A 304     3173   3467   3230   -158   -250    497       C  
ATOM   2179  SG  CYS A 304      -8.046   8.926 -54.226  1.00 30.62           S  
ANISOU 2179  SG  CYS A 304     3777   4078   3780    -19   -146    432       S  
ATOM   2180  N   THR A 305      -5.229   7.204 -55.117  1.00 20.94           N  
ANISOU 2180  N   THR A 305     2705   2587   2665    -40   -261    370       N  
ATOM   2181  CA  THR A 305      -3.862   7.347 -54.633  1.00 20.54           C  
ANISOU 2181  CA  THR A 305     2697   2492   2616    -23   -242    343       C  
ATOM   2182  C   THR A 305      -3.822   8.213 -53.387  1.00 22.04           C  
ANISOU 2182  C   THR A 305     2871   2725   2778    -35   -169    365       C  
ATOM   2183  O   THR A 305      -4.709   9.051 -53.166  1.00 25.99           O  
ANISOU 2183  O   THR A 305     3335   3293   3245    -15   -121    380       O  
ATOM   2184  CB  THR A 305      -2.852   7.925 -55.673  1.00 23.04           C  
ANISOU 2184  CB  THR A 305     3043   2789   2922     53   -218    285       C  
ATOM   2185  CG2 THR A 305      -2.896   7.144 -56.969  1.00 20.35           C  
ANISOU 2185  CG2 THR A 305     2713   2421   2598     90   -290    253       C  
ATOM   2186  OG1 THR A 305      -3.128   9.308 -55.916  1.00 22.88           O  
ANISOU 2186  OG1 THR A 305     3018   2806   2870     89   -142    281       O  
ATOM   2187  N   VAL A 306      -2.788   8.011 -52.576  1.00 20.19           N  
ANISOU 2187  N   VAL A 306     2666   2458   2549    -53   -168    360       N  
ATOM   2188  CA  VAL A 306      -2.622   8.813 -51.373  1.00 20.05           C  
ANISOU 2188  CA  VAL A 306     2642   2472   2506    -57   -106    376       C  
ATOM   2189  C   VAL A 306      -2.462  10.298 -51.709  1.00 19.80           C  
ANISOU 2189  C   VAL A 306     2632   2452   2440      6    -42    349       C  
ATOM   2190  O   VAL A 306      -3.149  11.160 -51.134  1.00 19.97           O  
ANISOU 2190  O   VAL A 306     2641   2521   2424     33     -5    360       O  
ATOM   2191  CB  VAL A 306      -1.448   8.292 -50.512  1.00 34.00           C  
ANISOU 2191  CB  VAL A 306     4440   4194   4285    -85   -121    370       C  
ATOM   2192  CG1 VAL A 306      -1.102   9.286 -49.408  1.00 19.69           C  
ANISOU 2192  CG1 VAL A 306     2630   2404   2445    -76    -55    375       C  
ATOM   2193  CG2 VAL A 306      -1.802   6.917 -49.925  1.00 20.33           C  
ANISOU 2193  CG2 VAL A 306     2705   2444   2577   -158   -198    410       C  
ATOM   2194  N   ALA A 307      -1.568  10.584 -52.653  1.00 19.55           N  
ANISOU 2194  N   ALA A 307     2636   2385   2407     32    -42    313       N  
ATOM   2195  CA  ALA A 307      -1.335  11.957 -53.124  1.00 29.14           C  
ANISOU 2195  CA  ALA A 307     3891   3597   3583     69     -3    298       C  
ATOM   2196  C   ALA A 307      -2.620  12.610 -53.630  1.00 27.76           C  
ANISOU 2196  C   ALA A 307     3711   3450   3386    116      6    299       C  
ATOM   2197  O   ALA A 307      -2.922  13.758 -53.287  1.00 19.86           O  
ANISOU 2197  O   ALA A 307     2751   2454   2343    155     28    296       O  
ATOM   2198  CB  ALA A 307      -0.251  11.992 -54.204  1.00 19.34           C  
ANISOU 2198  CB  ALA A 307     2669   2346   2333     70    -12    273       C  
ATOM   2199  N   GLN A 308      -3.385  11.872 -54.422  1.00 19.83           N  
ANISOU 2199  N   GLN A 308     2666   2465   2405    121    -22    299       N  
ATOM   2200  CA  GLN A 308      -4.630  12.420 -54.974  1.00 23.74           C  
ANISOU 2200  CA  GLN A 308     3146   3001   2874    173    -15    295       C  
ATOM   2201  C   GLN A 308      -5.697  12.648 -53.913  1.00 23.95           C  
ANISOU 2201  C   GLN A 308     3128   3107   2865    188      0    315       C  
ATOM   2202  O   GLN A 308      -6.410  13.653 -53.947  1.00 20.82           O  
ANISOU 2202  O   GLN A 308     2746   2750   2414    263     17    298       O  
ATOM   2203  CB  GLN A 308      -5.203  11.512 -56.059  1.00 20.21           C  
ANISOU 2203  CB  GLN A 308     2660   2561   2459    168    -54    291       C  
ATOM   2204  CG  GLN A 308      -4.554  11.666 -57.427  1.00 28.18           C  
ANISOU 2204  CG  GLN A 308     3704   3529   3475    198    -63    259       C  
ATOM   2205  CD  GLN A 308      -4.827  10.455 -58.294  1.00 34.12           C  
ANISOU 2205  CD  GLN A 308     4425   4273   4267    191   -121    252       C  
ATOM   2206  NE2 GLN A 308      -3.846  10.057 -59.101  1.00 19.97           N  
ANISOU 2206  NE2 GLN A 308     2651   2454   2484    208   -147    223       N  
ATOM   2207  OE1 GLN A 308      -5.901   9.856 -58.204  1.00 36.20           O  
ANISOU 2207  OE1 GLN A 308     4646   4565   4543    171   -149    273       O  
ATOM   2208  N   TYR A 309      -5.820  11.693 -52.996  1.00 20.65           N  
ANISOU 2208  N   TYR A 309     2658   2724   2467    123    -14    352       N  
ATOM   2209  CA  TYR A 309      -6.715  11.846 -51.851  1.00 21.15           C  
ANISOU 2209  CA  TYR A 309     2659   2895   2481    128      3    381       C  
ATOM   2210  C   TYR A 309      -6.435  13.124 -51.068  1.00 26.13           C  
ANISOU 2210  C   TYR A 309     3339   3529   3059    203     38    355       C  
ATOM   2211  O   TYR A 309      -7.366  13.852 -50.744  1.00 21.69           O  
ANISOU 2211  O   TYR A 309     2751   3062   2427    283     49    343       O  
ATOM   2212  CB  TYR A 309      -6.630  10.643 -50.918  1.00 22.93           C  
ANISOU 2212  CB  TYR A 309     2837   3142   2733     25    -24    434       C  
ATOM   2213  CG  TYR A 309      -7.473  10.757 -49.660  1.00 25.33           C  
ANISOU 2213  CG  TYR A 309     3062   3586   2975     18     -5    473       C  
ATOM   2214  CD1 TYR A 309      -8.851  10.625 -49.719  1.00 29.19           C  
ANISOU 2214  CD1 TYR A 309     3455   4226   3409     15    -12    503       C  
ATOM   2215  CD2 TYR A 309      -6.888  10.957 -48.411  1.00 29.54           C  
ANISOU 2215  CD2 TYR A 309     3606   4122   3495     13     17    482       C  
ATOM   2216  CE1 TYR A 309      -9.636  10.705 -48.581  1.00 25.97           C  
ANISOU 2216  CE1 TYR A 309     2953   3991   2925     10      4    542       C  
ATOM   2217  CE2 TYR A 309      -7.674  11.037 -47.243  1.00 22.51           C  
ANISOU 2217  CE2 TYR A 309     2631   3386   2537     14     33    519       C  
ATOM   2218  CZ  TYR A 309      -9.049  10.914 -47.349  1.00 29.01           C  
ANISOU 2218  CZ  TYR A 309     3349   4379   3295     13     27    549       C  
ATOM   2219  OH  TYR A 309      -9.860  10.991 -46.248  1.00 29.02           O  
ANISOU 2219  OH  TYR A 309     3244   4575   3207     18     42    588       O  
ATOM   2220  N   PHE A 310      -5.166  13.406 -50.776  1.00 20.71           N  
ANISOU 2220  N   PHE A 310     2725   2748   2396    186     46    344       N  
ATOM   2221  CA  PHE A 310      -4.852  14.570 -49.937  1.00 23.74           C  
ANISOU 2221  CA  PHE A 310     3170   3120   2731    245     62    324       C  
ATOM   2222  C   PHE A 310      -5.179  15.883 -50.640  1.00 23.42           C  
ANISOU 2222  C   PHE A 310     3210   3052   2637    340     51    285       C  
ATOM   2223  O   PHE A 310      -5.539  16.874 -50.002  1.00 28.54           O  
ANISOU 2223  O   PHE A 310     3903   3723   3218    428     42    261       O  
ATOM   2224  CB  PHE A 310      -3.417  14.527 -49.382  1.00 20.37           C  
ANISOU 2224  CB  PHE A 310     2796   2608   2336    189     69    328       C  
ATOM   2225  CG  PHE A 310      -3.305  13.745 -48.097  1.00 20.92           C  
ANISOU 2225  CG  PHE A 310     2810   2720   2421    142     77    358       C  
ATOM   2226  CD1 PHE A 310      -3.208  14.398 -46.878  1.00 20.57           C  
ANISOU 2226  CD1 PHE A 310     2782   2697   2335    181     91    356       C  
ATOM   2227  CD2 PHE A 310      -3.359  12.358 -48.105  1.00 20.31           C  
ANISOU 2227  CD2 PHE A 310     2670   2656   2390     63     59    390       C  
ATOM   2228  CE1 PHE A 310      -3.137  13.687 -45.690  1.00 20.61           C  
ANISOU 2228  CE1 PHE A 310     2733   2750   2349    137    100    387       C  
ATOM   2229  CE2 PHE A 310      -3.287  11.633 -46.916  1.00 25.72           C  
ANISOU 2229  CE2 PHE A 310     3316   3376   3083      9     57    426       C  
ATOM   2230  CZ  PHE A 310      -3.179  12.299 -45.706  1.00 25.03           C  
ANISOU 2230  CZ  PHE A 310     3232   3322   2955     45     84    426       C  
ATOM   2231  N   LYS A 311      -5.097  15.863 -51.960  1.00 20.90           N  
ANISOU 2231  N   LYS A 311     2914   2686   2340    330     41    275       N  
ATOM   2232  CA  LYS A 311      -5.480  17.011 -52.768  1.00 27.92           C  
ANISOU 2232  CA  LYS A 311     3886   3544   3178    411     20    242       C  
ATOM   2233  C   LYS A 311      -7.005  17.211 -52.773  1.00 27.20           C  
ANISOU 2233  C   LYS A 311     3741   3564   3029    513     15    219       C  
ATOM   2234  O   LYS A 311      -7.484  18.299 -52.473  1.00 23.60           O  
ANISOU 2234  O   LYS A 311     3351   3121   2494    623     -9    183       O  
ATOM   2235  CB  LYS A 311      -4.927  16.875 -54.192  1.00 29.28           C  
ANISOU 2235  CB  LYS A 311     4088   3651   3387    367     13    242       C  
ATOM   2236  CG  LYS A 311      -5.268  18.044 -55.118  1.00 31.13           C  
ANISOU 2236  CG  LYS A 311     4420   3841   3568    435    -16    216       C  
ATOM   2237  CD  LYS A 311      -4.839  19.371 -54.482  1.00 45.37           C  
ANISOU 2237  CD  LYS A 311     6359   5572   5309    468    -52    206       C  
ATOM   2238  CE  LYS A 311      -5.214  20.571 -55.354  1.00 50.95           C  
ANISOU 2238  CE  LYS A 311     7192   6215   5951    537   -105    182       C  
ATOM   2239  NZ  LYS A 311      -4.121  20.909 -56.301  1.00 54.82           N1+
ANISOU 2239  NZ  LYS A 311     7758   6622   6450    437   -123    214       N1+
ATOM   2240  N   GLN A 312      -7.759  16.163 -53.106  1.00 32.28           N  
ANISOU 2240  N   GLN A 312     4270   4295   3700    479     27    239       N  
ATOM   2241  CA  GLN A 312      -9.216  16.259 -53.164  1.00 33.11           C  
ANISOU 2241  CA  GLN A 312     4300   4541   3741    560     24    224       C  
ATOM   2242  C   GLN A 312      -9.795  16.522 -51.792  1.00 30.45           C  
ANISOU 2242  C   GLN A 312     3908   4335   3328    620     31    224       C  
ATOM   2243  O   GLN A 312     -10.762  17.249 -51.653  1.00 38.72           O  
ANISOU 2243  O   GLN A 312     4942   5492   4279    748     19    185       O  
ATOM   2244  CB  GLN A 312      -9.854  14.974 -53.701  1.00 28.24           C  
ANISOU 2244  CB  GLN A 312     3566   3996   3168    480     25    262       C  
ATOM   2245  CG  GLN A 312      -9.306  14.460 -55.002  1.00 33.69           C  
ANISOU 2245  CG  GLN A 312     4291   4576   3935    424     11    261       C  
ATOM   2246  CD  GLN A 312      -9.663  12.991 -55.245  1.00 42.48           C  
ANISOU 2246  CD  GLN A 312     5311   5727   5101    322    -11    306       C  
ATOM   2247  NE2 GLN A 312      -9.173  12.437 -56.350  1.00 38.42           N  
ANISOU 2247  NE2 GLN A 312     4827   5123   4650    289    -35    299       N  
ATOM   2248  OE1 GLN A 312     -10.358  12.364 -54.442  1.00 46.81           O  
ANISOU 2248  OE1 GLN A 312     5769   6388   5629    272    -17    348       O  
ATOM   2249  N   LYS A 313      -9.219  15.905 -50.774  1.00 32.18           N  
ANISOU 2249  N   LYS A 313     4090   4557   3579    537     47    265       N  
ATOM   2250  CA  LYS A 313      -9.821  15.974 -49.452  1.00 30.60           C  
ANISOU 2250  CA  LYS A 313     3811   4512   3304    581     56    275       C  
ATOM   2251  C   LYS A 313      -9.366  17.178 -48.638  1.00 33.67           C  
ANISOU 2251  C   LYS A 313     4303   4856   3635    692     43    229       C  
ATOM   2252  O   LYS A 313     -10.182  17.848 -47.995  1.00 32.05           O  
ANISOU 2252  O   LYS A 313     4071   4786   3321    827     31    193       O  
ATOM   2253  CB  LYS A 313      -9.573  14.682 -48.667  1.00 27.47           C  
ANISOU 2253  CB  LYS A 313     3321   4159   2959    437     70    347       C  
ATOM   2254  CG  LYS A 313      -9.968  14.771 -47.192  1.00 26.47           C  
ANISOU 2254  CG  LYS A 313     3117   4188   2754    469     83    366       C  
ATOM   2255  CD  LYS A 313     -11.380  14.310 -46.958  1.00 30.54           C  
ANISOU 2255  CD  LYS A 313     3470   4950   3183    466     85    402       C  
ATOM   2256  CE  LYS A 313     -11.693  14.280 -45.465  1.00 41.64           C  
ANISOU 2256  CE  LYS A 313     4781   6536   4506    481     99    432       C  
ATOM   2257  NZ  LYS A 313     -11.718  12.891 -44.921  1.00 44.97           N1+
ANISOU 2257  NZ  LYS A 313     5103   7019   4965    291     95    534       N1+
ATOM   2258  N   TYR A 314      -8.066  17.451 -48.651  1.00 33.24           N  
ANISOU 2258  N   TYR A 314     4365   4624   3641    641     38    228       N  
ATOM   2259  CA  TYR A 314      -7.534  18.490 -47.770  1.00 32.18           C  
ANISOU 2259  CA  TYR A 314     4337   4432   3459    720     14    196       C  
ATOM   2260  C   TYR A 314      -6.974  19.665 -48.530  1.00 33.27           C  
ANISOU 2260  C   TYR A 314     4649   4408   3584    767    -35    156       C  
ATOM   2261  O   TYR A 314      -6.376  20.558 -47.927  1.00 30.46           O  
ANISOU 2261  O   TYR A 314     4414   3966   3195    809    -75    135       O  
ATOM   2262  CB  TYR A 314      -6.462  17.925 -46.850  1.00 26.39           C  
ANISOU 2262  CB  TYR A 314     3594   3645   2786    614     38    235       C  
ATOM   2263  CG  TYR A 314      -7.007  16.879 -45.914  1.00 32.54           C  
ANISOU 2263  CG  TYR A 314     4221   4580   3562    567     71    279       C  
ATOM   2264  CD1 TYR A 314      -7.852  17.233 -44.858  1.00 30.13           C  
ANISOU 2264  CD1 TYR A 314     3850   4442   3157    672     69    267       C  
ATOM   2265  CD2 TYR A 314      -6.694  15.538 -46.086  1.00 25.87           C  
ANISOU 2265  CD2 TYR A 314     3303   3725   2800    419     90    336       C  
ATOM   2266  CE1 TYR A 314      -8.361  16.274 -44.001  1.00 28.34           C  
ANISOU 2266  CE1 TYR A 314     3475   4379   2914    608     96    322       C  
ATOM   2267  CE2 TYR A 314      -7.197  14.574 -45.224  1.00 31.79           C  
ANISOU 2267  CE2 TYR A 314     3930   4608   3540    354    104    390       C  
ATOM   2268  CZ  TYR A 314      -8.032  14.950 -44.189  1.00 28.32           C  
ANISOU 2268  CZ  TYR A 314     3414   4345   3001    437    111    390       C  
ATOM   2269  OH  TYR A 314      -8.535  13.996 -43.345  1.00 28.38           O  
ANISOU 2269  OH  TYR A 314     3291   4504   2986    352    121    457       O  
ATOM   2270  N   ASN A 315      -7.155  19.638 -49.850  1.00 30.59           N  
ANISOU 2270  N   ASN A 315     4329   4025   3268    748    -41    153       N  
ATOM   2271  CA  ASN A 315      -6.633  20.673 -50.740  1.00 39.86           C  
ANISOU 2271  CA  ASN A 315     5667   5049   4428    764    -92    131       C  
ATOM   2272  C   ASN A 315      -5.153  20.902 -50.510  1.00 36.88           C  
ANISOU 2272  C   ASN A 315     5384   4536   4094    655   -102    161       C  
ATOM   2273  O   ASN A 315      -4.648  22.019 -50.588  1.00 37.09           O  
ANISOU 2273  O   ASN A 315     5570   4446   4077    672   -166    150       O  
ATOM   2274  CB  ASN A 315      -7.456  21.938 -50.589  1.00 43.87           C  
ANISOU 2274  CB  ASN A 315     6282   5566   4821    943   -163     66       C  
ATOM   2275  CG  ASN A 315      -8.940  21.629 -50.517  1.00 54.52           C  
ANISOU 2275  CG  ASN A 315     7499   7109   6106   1062   -145     34       C  
ATOM   2276  ND2 ASN A 315      -9.480  21.594 -49.295  1.00 66.48           N  
ANISOU 2276  ND2 ASN A 315     8937   8768   7555   1148   -139     18       N  
ATOM   2277  OD1 ASN A 315      -9.594  21.397 -51.541  1.00 48.51           O  
ANISOU 2277  OD1 ASN A 315     6695   6387   5348   1073   -135     26       O  
ATOM   2278  N   LEU A 316      -4.475  19.801 -50.215  1.00 32.44           N  
ANISOU 2278  N   LEU A 316     4723   3994   3609    537    -48    203       N  
ATOM   2279  CA  LEU A 316      -3.055  19.809 -49.933  1.00 32.98           C  
ANISOU 2279  CA  LEU A 316     4843   3974   3715    429    -46    232       C  
ATOM   2280  C   LEU A 316      -2.358  19.049 -51.034  1.00 32.83           C  
ANISOU 2280  C   LEU A 316     4780   3936   3759    321    -21    259       C  
ATOM   2281  O   LEU A 316      -2.600  17.855 -51.238  1.00 29.49           O  
ANISOU 2281  O   LEU A 316     4241   3576   3388    289     15    269       O  
ATOM   2282  CB  LEU A 316      -2.773  19.148 -48.589  1.00 31.45           C  
ANISOU 2282  CB  LEU A 316     4574   3830   3546    404    -12    246       C  
ATOM   2283  CG  LEU A 316      -1.307  18.868 -48.258  1.00 38.95           C  
ANISOU 2283  CG  LEU A 316     5542   4716   4540    290      1    274       C  
ATOM   2284  CD1 LEU A 316      -0.489  20.141 -48.284  1.00 47.20           C  
ANISOU 2284  CD1 LEU A 316     6740   5652   5540    273    -53    274       C  
ATOM   2285  CD2 LEU A 316      -1.211  18.229 -46.900  1.00 36.61           C  
ANISOU 2285  CD2 LEU A 316     5175   4473   4262    284     31    283       C  
ATOM   2286  N   GLN A 317      -1.516  19.768 -51.757  1.00 29.65           N  
ANISOU 2286  N   GLN A 317     4476   3452   3338    266    -51    271       N  
ATOM   2287  CA  GLN A 317      -0.660  19.192 -52.763  1.00 29.58           C  
ANISOU 2287  CA  GLN A 317     4427   3448   3366    169    -33    295       C  
ATOM   2288  C   GLN A 317       0.652  18.871 -52.061  1.00 31.16           C  
ANISOU 2288  C   GLN A 317     4611   3645   3582     78    -17    319       C  
ATOM   2289  O   GLN A 317       1.335  19.777 -51.595  1.00 28.13           O  
ANISOU 2289  O   GLN A 317     4323   3205   3159     40    -49    335       O  
ATOM   2290  CB  GLN A 317      -0.421  20.244 -53.825  1.00 24.68           C  
ANISOU 2290  CB  GLN A 317     3918   2766   2694    146    -80    308       C  
ATOM   2291  CG  GLN A 317       0.487  19.827 -54.944  1.00 33.42           C  
ANISOU 2291  CG  GLN A 317     4981   3904   3811     51    -66    335       C  
ATOM   2292  CD  GLN A 317       0.889  21.022 -55.795  1.00 43.48           C  
ANISOU 2292  CD  GLN A 317     6380   5122   5019     -4   -122    367       C  
ATOM   2293  NE2 GLN A 317       1.804  21.837 -55.278  1.00 50.59           N  
ANISOU 2293  NE2 GLN A 317     7376   5973   5874    -90   -163    404       N  
ATOM   2294  OE1 GLN A 317       0.367  21.221 -56.889  1.00 37.30           O  
ANISOU 2294  OE1 GLN A 317     5614   4338   4222     23   -136    362       O  
ATOM   2295  N   LEU A 318       0.997  17.591 -51.972  1.00 29.79           N  
ANISOU 2295  N   LEU A 318     4327   3529   3463     47     20    318       N  
ATOM   2296  CA  LEU A 318       2.191  17.171 -51.237  1.00 26.14           C  
ANISOU 2296  CA  LEU A 318     3840   3078   3012    -20     34    329       C  
ATOM   2297  C   LEU A 318       3.477  17.741 -51.834  1.00 27.42           C  
ANISOU 2297  C   LEU A 318     4044   3244   3132   -109     19    354       C  
ATOM   2298  O   LEU A 318       3.638  17.770 -53.058  1.00 32.77           O  
ANISOU 2298  O   LEU A 318     4710   3952   3790   -131     11    361       O  
ATOM   2299  CB  LEU A 318       2.301  15.650 -51.229  1.00 19.50           C  
ANISOU 2299  CB  LEU A 318     2893   2292   2226    -24     55    317       C  
ATOM   2300  CG  LEU A 318       1.157  14.822 -50.661  1.00 26.17           C  
ANISOU 2300  CG  LEU A 318     3680   3154   3111     22     62    312       C  
ATOM   2301  CD1 LEU A 318       1.511  13.348 -50.790  1.00 19.15           C  
ANISOU 2301  CD1 LEU A 318     2722   2290   2266     -2     52    304       C  
ATOM   2302  CD2 LEU A 318       0.886  15.186 -49.198  1.00 21.84           C  
ANISOU 2302  CD2 LEU A 318     3147   2600   2551     41     73    319       C  
ATOM   2303  N   LYS A 319       4.394  18.172 -50.971  1.00 24.50           N  
ANISOU 2303  N   LYS A 319     3713   2859   2738   -166     13    371       N  
ATOM   2304  CA  LYS A 319       5.718  18.601 -51.409  1.00 27.16           C  
ANISOU 2304  CA  LYS A 319     4065   3233   3022   -273     -1    404       C  
ATOM   2305  C   LYS A 319       6.598  17.419 -51.806  1.00 23.38           C  
ANISOU 2305  C   LYS A 319     3464   2870   2552   -295     29    389       C  
ATOM   2306  O   LYS A 319       7.461  17.544 -52.677  1.00 26.06           O  
ANISOU 2306  O   LYS A 319     3773   3294   2835   -361     22    409       O  
ATOM   2307  CB  LYS A 319       6.442  19.409 -50.325  1.00 38.35           C  
ANISOU 2307  CB  LYS A 319     5561   4604   4407   -334    -25    428       C  
ATOM   2308  CG  LYS A 319       5.934  20.821 -50.140  1.00 47.18           C  
ANISOU 2308  CG  LYS A 319     6838   5607   5484   -328    -90    447       C  
ATOM   2309  CD  LYS A 319       6.809  21.594 -49.159  1.00 55.39           C  
ANISOU 2309  CD  LYS A 319     7964   6597   6485   -403   -130    475       C  
ATOM   2310  CE  LYS A 319       6.186  22.941 -48.782  1.00 62.85           C  
ANISOU 2310  CE  LYS A 319     9091   7403   7387   -363   -218    479       C  
ATOM   2311  NZ  LYS A 319       5.999  23.846 -49.961  1.00 68.53           N1+
ANISOU 2311  NZ  LYS A 319     9919   8070   8049   -410   -288    513       N1+
ATOM   2312  N   TYR A 320       6.378  16.274 -51.176  1.00 21.85           N  
ANISOU 2312  N   TYR A 320     3201   2686   2414   -235     53    353       N  
ATOM   2313  CA  TYR A 320       7.230  15.111 -51.416  1.00 20.91           C  
ANISOU 2313  CA  TYR A 320     2988   2662   2294   -231     60    324       C  
ATOM   2314  C   TYR A 320       6.443  13.872 -51.806  1.00 23.38           C  
ANISOU 2314  C   TYR A 320     3249   2972   2663   -150     52    287       C  
ATOM   2315  O   TYR A 320       6.496  12.858 -51.104  1.00 19.45           O  
ANISOU 2315  O   TYR A 320     2721   2467   2201   -120     46    262       O  
ATOM   2316  CB  TYR A 320       8.042  14.805 -50.158  1.00 21.19           C  
ANISOU 2316  CB  TYR A 320     3012   2706   2332   -251     72    316       C  
ATOM   2317  CG  TYR A 320       8.785  16.002 -49.648  1.00 25.61           C  
ANISOU 2317  CG  TYR A 320     3633   3257   2840   -337     69    356       C  
ATOM   2318  CD1 TYR A 320       9.952  16.437 -50.269  1.00 25.57           C  
ANISOU 2318  CD1 TYR A 320     3605   3355   2754   -425     60    382       C  
ATOM   2319  CD2 TYR A 320       8.307  16.723 -48.568  1.00 32.02           C  
ANISOU 2319  CD2 TYR A 320     4526   3968   3672   -334     65    370       C  
ATOM   2320  CE1 TYR A 320      10.630  17.552 -49.813  1.00 31.67           C  
ANISOU 2320  CE1 TYR A 320     4445   4115   3474   -529     41    431       C  
ATOM   2321  CE2 TYR A 320       8.985  17.836 -48.087  1.00 31.13           C  
ANISOU 2321  CE2 TYR A 320     4490   3827   3509   -415     42    406       C  
ATOM   2322  CZ  TYR A 320      10.143  18.246 -48.711  1.00 32.17           C  
ANISOU 2322  CZ  TYR A 320     4609   4046   3568   -522     27    441       C  
ATOM   2323  OH  TYR A 320      10.807  19.355 -48.241  1.00 28.59           O  
ANISOU 2323  OH  TYR A 320     4243   3560   3061   -624    -11    488       O  
ATOM   2324  N   PRO A 321       5.732  13.933 -52.943  1.00 24.82           N  
ANISOU 2324  N   PRO A 321     3428   3155   2848   -121     42    286       N  
ATOM   2325  CA  PRO A 321       4.936  12.766 -53.342  1.00 19.37           C  
ANISOU 2325  CA  PRO A 321     2698   2453   2209    -54     21    255       C  
ATOM   2326  C   PRO A 321       5.833  11.583 -53.731  1.00 29.94           C  
ANISOU 2326  C   PRO A 321     3980   3864   3533    -20    -11    212       C  
ATOM   2327  O   PRO A 321       5.336  10.461 -53.869  1.00 19.46           O  
ANISOU 2327  O   PRO A 321     2638   2510   2245     31    -53    184       O  
ATOM   2328  CB  PRO A 321       4.149  13.285 -54.561  1.00 19.50           C  
ANISOU 2328  CB  PRO A 321     2726   2464   2217    -35     17    263       C  
ATOM   2329  CG  PRO A 321       5.029  14.339 -55.155  1.00 19.85           C  
ANISOU 2329  CG  PRO A 321     2793   2560   2190    -93     25    289       C  
ATOM   2330  CD  PRO A 321       5.706  14.999 -53.970  1.00 21.74           C  
ANISOU 2330  CD  PRO A 321     3074   2778   2408   -155     39    314       C  
ATOM   2331  N   HIS A 322       7.131  11.830 -53.887  1.00 19.78           N  
ANISOU 2331  N   HIS A 322     2664   2674   2178    -47     -4    206       N  
ATOM   2332  CA  HIS A 322       8.075  10.757 -54.159  1.00 20.05           C  
ANISOU 2332  CA  HIS A 322     2642   2803   2175     10    -41    152       C  
ATOM   2333  C   HIS A 322       8.473   9.974 -52.908  1.00 27.16           C  
ANISOU 2333  C   HIS A 322     3551   3668   3099     26    -58    127       C  
ATOM   2334  O   HIS A 322       8.990   8.858 -53.016  1.00 20.17           O  
ANISOU 2334  O   HIS A 322     2645   2824   2196    101   -112     70       O  
ATOM   2335  CB  HIS A 322       9.337  11.285 -54.855  1.00 20.95           C  
ANISOU 2335  CB  HIS A 322     2696   3081   2183    -20    -29    154       C  
ATOM   2336  CG  HIS A 322      10.031  12.379 -54.102  1.00 22.89           C  
ANISOU 2336  CG  HIS A 322     2960   3347   2389   -129     11    206       C  
ATOM   2337  CD2 HIS A 322      11.168  12.373 -53.363  1.00 20.92           C  
ANISOU 2337  CD2 HIS A 322     2681   3179   2089   -163     19    200       C  
ATOM   2338  ND1 HIS A 322       9.566  13.675 -54.074  1.00 20.68           N  
ANISOU 2338  ND1 HIS A 322     2747   2997   2113   -216     33    269       N  
ATOM   2339  CE1 HIS A 322      10.376  14.419 -53.342  1.00 21.49           C  
ANISOU 2339  CE1 HIS A 322     2869   3123   2173   -305     47    305       C  
ATOM   2340  NE2 HIS A 322      11.356  13.651 -52.900  1.00 22.31           N  
ANISOU 2340  NE2 HIS A 322     2906   3325   2245   -280     46    266       N  
ATOM   2341  N   LEU A 323       8.242  10.558 -51.731  1.00 19.60           N  
ANISOU 2341  N   LEU A 323     2634   2636   2175    -33    -20    165       N  
ATOM   2342  CA  LEU A 323       8.552   9.889 -50.467  1.00 19.78           C  
ANISOU 2342  CA  LEU A 323     2670   2622   2224    -26    -31    149       C  
ATOM   2343  C   LEU A 323       7.457   8.874 -50.140  1.00 23.78           C  
ANISOU 2343  C   LEU A 323     3204   3029   2802      6    -75    147       C  
ATOM   2344  O   LEU A 323       6.321   9.010 -50.610  1.00 21.75           O  
ANISOU 2344  O   LEU A 323     2957   2727   2581      3    -76    171       O  
ATOM   2345  CB  LEU A 323       8.696  10.913 -49.323  1.00 20.15           C  
ANISOU 2345  CB  LEU A 323     2749   2634   2274    -97     20    192       C  
ATOM   2346  CG  LEU A 323       9.958  11.764 -49.465  1.00 21.72           C  
ANISOU 2346  CG  LEU A 323     2927   2933   2393   -152     43    202       C  
ATOM   2347  CD1 LEU A 323      10.174  12.698 -48.281  1.00 19.44           C  
ANISOU 2347  CD1 LEU A 323     2685   2595   2106   -219     75    239       C  
ATOM   2348  CD2 LEU A 323      11.168  10.871 -49.695  1.00 20.50           C  
ANISOU 2348  CD2 LEU A 323     2708   2904   2179   -107     17    146       C  
ATOM   2349  N   PRO A 324       7.791   7.855 -49.332  1.00 22.76           N  
ANISOU 2349  N   PRO A 324     3092   2870   2686     29   -119    121       N  
ATOM   2350  CA  PRO A 324       6.791   6.831 -49.023  1.00 24.04           C  
ANISOU 2350  CA  PRO A 324     3289   2941   2906     32   -180    133       C  
ATOM   2351  C   PRO A 324       5.807   7.301 -47.962  1.00 27.10           C  
ANISOU 2351  C   PRO A 324     3685   3275   3336    -34   -135    197       C  
ATOM   2352  O   PRO A 324       5.905   8.430 -47.473  1.00 27.94           O  
ANISOU 2352  O   PRO A 324     3783   3401   3431    -63    -64    221       O  
ATOM   2353  CB  PRO A 324       7.633   5.672 -48.485  1.00 22.14           C  
ANISOU 2353  CB  PRO A 324     3078   2687   2647     76   -254     85       C  
ATOM   2354  CG  PRO A 324       8.826   6.349 -47.863  1.00 22.28           C  
ANISOU 2354  CG  PRO A 324     3068   2777   2618     68   -193     70       C  
ATOM   2355  CD  PRO A 324       9.099   7.563 -48.718  1.00 19.53           C  
ANISOU 2355  CD  PRO A 324     2673   2517   2231     48   -127     82       C  
ATOM   2356  N   CYS A 325       4.856   6.434 -47.627  1.00 20.27           N  
ANISOU 2356  N   CYS A 325     2838   2353   2510    -58   -188    226       N  
ATOM   2357  CA  CYS A 325       3.882   6.740 -46.604  1.00 19.33           C  
ANISOU 2357  CA  CYS A 325     2707   2222   2414   -116   -153    288       C  
ATOM   2358  C   CYS A 325       4.123   5.873 -45.387  1.00 25.04           C  
ANISOU 2358  C   CYS A 325     3457   2910   3147   -151   -194    303       C  
ATOM   2359  O   CYS A 325       4.751   4.818 -45.468  1.00 26.53           O  
ANISOU 2359  O   CYS A 325     3690   3056   3333   -130   -276    269       O  
ATOM   2360  CB  CYS A 325       2.473   6.441 -47.097  1.00 23.69           C  
ANISOU 2360  CB  CYS A 325     3242   2770   2988   -144   -182    329       C  
ATOM   2361  SG  CYS A 325       2.013   7.226 -48.644  1.00 35.40           S  
ANISOU 2361  SG  CYS A 325     4703   4283   4463    -99   -154    310       S  
ATOM   2362  N   LEU A 326       3.584   6.316 -44.263  1.00 24.19           N  
ANISOU 2362  N   LEU A 326     3327   2823   3043   -194   -146    353       N  
ATOM   2363  CA  LEU A 326       3.510   5.480 -43.083  1.00 24.98           C  
ANISOU 2363  CA  LEU A 326     3443   2897   3149   -245   -187    388       C  
ATOM   2364  C   LEU A 326       2.186   4.739 -43.104  1.00 25.76           C  
ANISOU 2364  C   LEU A 326     3529   2999   3259   -319   -245    456       C  
ATOM   2365  O   LEU A 326       1.127   5.357 -43.168  1.00 24.53           O  
ANISOU 2365  O   LEU A 326     3313   2914   3094   -336   -199    497       O  
ATOM   2366  CB  LEU A 326       3.574   6.348 -41.829  1.00 20.59           C  
ANISOU 2366  CB  LEU A 326     2859   2385   2580   -252   -107    411       C  
ATOM   2367  CG  LEU A 326       4.778   7.274 -41.722  1.00 21.39           C  
ANISOU 2367  CG  LEU A 326     2972   2491   2664   -201    -48    359       C  
ATOM   2368  CD1 LEU A 326       4.662   8.147 -40.479  1.00 18.90           C  
ANISOU 2368  CD1 LEU A 326     2639   2208   2334   -203     16    383       C  
ATOM   2369  CD2 LEU A 326       6.055   6.444 -41.701  1.00 19.04           C  
ANISOU 2369  CD2 LEU A 326     2715   2157   2362   -181    -97    307       C  
ATOM   2370  N   GLN A 327       2.241   3.417 -43.062  1.00 20.85           N  
ANISOU 2370  N   GLN A 327     2967   2307   2648   -363   -358    469       N  
ATOM   2371  CA  GLN A 327       1.050   2.649 -42.732  1.00 23.82           C  
ANISOU 2371  CA  GLN A 327     3336   2692   3023   -473   -426    558       C  
ATOM   2372  C   GLN A 327       0.888   2.660 -41.225  1.00 24.03           C  
ANISOU 2372  C   GLN A 327     3334   2766   3030   -540   -397    619       C  
ATOM   2373  O   GLN A 327       1.825   2.345 -40.500  1.00 27.49           O  
ANISOU 2373  O   GLN A 327     3823   3152   3469   -525   -413    594       O  
ATOM   2374  CB  GLN A 327       1.165   1.206 -43.199  1.00 22.30           C  
ANISOU 2374  CB  GLN A 327     3246   2386   2842   -509   -585    556       C  
ATOM   2375  CG  GLN A 327      -0.107   0.434 -42.982  1.00 45.32           C  
ANISOU 2375  CG  GLN A 327     6158   5312   5749   -652   -670    663       C  
ATOM   2376  CD  GLN A 327      -0.024  -0.967 -43.517  1.00 51.84           C  
ANISOU 2376  CD  GLN A 327     7113   6000   6583   -690   -854    663       C  
ATOM   2377  NE2 GLN A 327      -1.169  -1.629 -43.614  1.00 56.03           N  
ANISOU 2377  NE2 GLN A 327     7648   6535   7105   -827   -945    758       N  
ATOM   2378  OE1 GLN A 327       1.057  -1.454 -43.851  1.00 53.73           O  
ANISOU 2378  OE1 GLN A 327     7451   6138   6826   -593   -924    576       O  
ATOM   2379  N   VAL A 328      -0.300   3.028 -40.761  1.00 27.87           N  
ANISOU 2379  N   VAL A 328     3731   3370   3490   -604   -354    697       N  
ATOM   2380  CA  VAL A 328      -0.593   3.082 -39.333  1.00 28.62           C  
ANISOU 2380  CA  VAL A 328     3776   3547   3550   -665   -323    762       C  
ATOM   2381  C   VAL A 328      -1.848   2.263 -39.026  1.00 33.42           C  
ANISOU 2381  C   VAL A 328     4341   4234   4124   -815   -396    879       C  
ATOM   2382  O   VAL A 328      -2.568   1.864 -39.939  1.00 37.81           O  
ANISOU 2382  O   VAL A 328     4895   4790   4683   -862   -454    905       O  
ATOM   2383  CB  VAL A 328      -0.787   4.541 -38.872  1.00 27.41           C  
ANISOU 2383  CB  VAL A 328     3534   3512   3366   -578   -191    741       C  
ATOM   2384  CG1 VAL A 328       0.516   5.324 -39.002  1.00 22.86           C  
ANISOU 2384  CG1 VAL A 328     3010   2859   2816   -465   -134    645       C  
ATOM   2385  CG2 VAL A 328      -1.895   5.214 -39.684  1.00 24.32           C  
ANISOU 2385  CG2 VAL A 328     3068   3221   2951   -551   -155    749       C  
ATOM   2386  N   GLY A 329      -2.116   2.015 -37.748  1.00 38.61           N  
ANISOU 2386  N   GLY A 329     4958   4972   4741   -898   -396    955       N  
ATOM   2387  CA  GLY A 329      -3.265   1.209 -37.362  1.00 44.41           C  
ANISOU 2387  CA  GLY A 329     5643   5807   5425  -1069   -472   1084       C  
ATOM   2388  C   GLY A 329      -3.106  -0.243 -37.792  1.00 49.33           C  
ANISOU 2388  C   GLY A 329     6402   6267   6076  -1188   -644   1122       C  
ATOM   2389  O   GLY A 329      -1.986  -0.736 -37.875  1.00 50.85           O  
ANISOU 2389  O   GLY A 329     6726   6284   6312  -1135   -705   1054       O  
ATOM   2390  N   GLN A 330      -4.215  -0.924 -38.077  1.00 52.54           N  
ANISOU 2390  N   GLN A 330     6782   6733   6448  -1342   -734   1227       N  
ATOM   2391  CA  GLN A 330      -4.162  -2.326 -38.497  1.00 59.20           C  
ANISOU 2391  CA  GLN A 330     7776   7407   7310  -1466   -927   1271       C  
ATOM   2392  C   GLN A 330      -3.574  -2.480 -39.893  1.00 64.80           C  
ANISOU 2392  C   GLN A 330     8595   7944   8083  -1345   -980   1159       C  
ATOM   2393  O   GLN A 330      -3.731  -1.605 -40.736  1.00 62.61           O  
ANISOU 2393  O   GLN A 330     8244   7722   7824  -1232   -880   1093       O  
ATOM   2394  CB  GLN A 330      -5.553  -2.960 -38.472  1.00 64.61           C  
ANISOU 2394  CB  GLN A 330     8401   8214   7933  -1683  -1017   1424       C  
ATOM   2395  CG  GLN A 330      -6.057  -3.359 -37.091  1.00 71.81           C  
ANISOU 2395  CG  GLN A 330     9251   9265   8768  -1863  -1042   1566       C  
ATOM   2396  CD  GLN A 330      -7.156  -4.415 -37.159  1.00 76.19           C  
ANISOU 2396  CD  GLN A 330     9815   9871   9264  -2124  -1203   1729       C  
ATOM   2397  NE2 GLN A 330      -7.746  -4.730 -36.010  1.00 78.73           N  
ANISOU 2397  NE2 GLN A 330    10056  10361   9498  -2308  -1224   1874       N  
ATOM   2398  OE1 GLN A 330      -7.465  -4.943 -38.231  1.00 76.70           O  
ANISOU 2398  OE1 GLN A 330     9957   9830   9355  -2166  -1313   1729       O  
ATOM   2399  N   GLU A 331      -2.915  -3.610 -40.138  1.00 77.59           N  
ANISOU 2399  N   GLU A 331    10395   9360   9726  -1365  -1149   1137       N  
ATOM   2400  CA  GLU A 331      -2.327  -3.890 -41.446  1.00 89.26           C  
ANISOU 2400  CA  GLU A 331    11981  10686  11248  -1239  -1222   1026       C  
ATOM   2401  C   GLU A 331      -3.369  -4.396 -42.439  1.00 92.50           C  
ANISOU 2401  C   GLU A 331    12404  11087  11656  -1334  -1326   1083       C  
ATOM   2402  O   GLU A 331      -3.058  -5.206 -43.310  1.00 97.72           O  
ANISOU 2402  O   GLU A 331    13209  11584  12337  -1298  -1479   1034       O  
ATOM   2403  CB  GLU A 331      -1.196  -4.918 -41.327  1.00 98.73           C  
ANISOU 2403  CB  GLU A 331    13378  11680  12457  -1189  -1380    964       C  
ATOM   2404  CG  GLU A 331       0.041  -4.433 -40.584  1.00107.30           C  
ANISOU 2404  CG  GLU A 331    14462  12760  13546  -1059  -1283    876       C  
ATOM   2405  CD  GLU A 331      -0.129  -4.448 -39.075  1.00117.74           C  
ANISOU 2405  CD  GLU A 331    15745  14150  14839  -1178  -1248    971       C  
ATOM   2406  OE1 GLU A 331      -1.035  -3.755 -38.565  1.00121.58           O  
ANISOU 2406  OE1 GLU A 331    16077  14813  15304  -1262  -1131   1057       O  
ATOM   2407  OE2 GLU A 331       0.645  -5.156 -38.396  1.00121.84           O1-
ANISOU 2407  OE2 GLU A 331    16388  14557  15349  -1177  -1343    955       O1-
ATOM   2408  N   GLN A 332      -4.602  -3.916 -42.298  1.00 88.88           N  
ANISOU 2408  N   GLN A 332    11792  10815  11164  -1444  -1249   1181       N  
ATOM   2409  CA  GLN A 332      -5.708  -4.327 -43.155  1.00 83.64           C  
ANISOU 2409  CA  GLN A 332    11113  10178  10487  -1553  -1336   1249       C  
ATOM   2410  C   GLN A 332      -6.668  -3.170 -43.369  1.00 73.47           C  
ANISOU 2410  C   GLN A 332     9620   9122   9173  -1529  -1165   1266       C  
ATOM   2411  O   GLN A 332      -7.542  -3.236 -44.231  1.00 74.52           O  
ANISOU 2411  O   GLN A 332     9713   9302   9298  -1574  -1196   1294       O  
ATOM   2412  CB  GLN A 332      -6.477  -5.499 -42.537  1.00 91.72           C  
ANISOU 2412  CB  GLN A 332    12196  11193  11461  -1813  -1513   1410       C  
ATOM   2413  CG  GLN A 332      -5.759  -6.838 -42.574  1.00 95.63           C  
ANISOU 2413  CG  GLN A 332    12937  11425  11973  -1856  -1745   1402       C  
ATOM   2414  CD  GLN A 332      -5.420  -7.347 -41.190  1.00 99.28           C  
ANISOU 2414  CD  GLN A 332    13456  11865  12399  -1971  -1800   1479       C  
ATOM   2415  NE2 GLN A 332      -5.085  -8.629 -41.095  1.00102.10           N  
ANISOU 2415  NE2 GLN A 332    14037  12007  12749  -2062  -2038   1510       N  
ATOM   2416  OE1 GLN A 332      -5.464  -6.597 -40.213  1.00 99.23           O  
ANISOU 2416  OE1 GLN A 332    13305  12031  12367  -1972  -1639   1507       O  
ATOM   2417  N   LYS A 333      -6.516  -2.116 -42.575  1.00 64.91           N  
ANISOU 2417  N   LYS A 333     8413   8181   8067  -1449   -994   1244       N  
ATOM   2418  CA  LYS A 333      -7.386  -0.947 -42.700  1.00 65.32           C  
ANISOU 2418  CA  LYS A 333     8285   8454   8079  -1394   -842   1245       C  
ATOM   2419  C   LYS A 333      -6.861   0.080 -43.710  1.00 57.76           C  
ANISOU 2419  C   LYS A 333     7325   7450   7170  -1182   -734   1106       C  
ATOM   2420  O   LYS A 333      -7.459   1.147 -43.878  1.00 51.68           O  
ANISOU 2420  O   LYS A 333     6432   6834   6368  -1105   -614   1086       O  
ATOM   2421  CB  LYS A 333      -7.614  -0.294 -41.337  1.00 71.32           C  
ANISOU 2421  CB  LYS A 333     8918   9408   8774  -1408   -730   1293       C  
ATOM   2422  CG  LYS A 333      -8.491  -1.113 -40.407  1.00 78.39           C  
ANISOU 2422  CG  LYS A 333     9755  10439   9590  -1636   -813   1455       C  
ATOM   2423  CD  LYS A 333      -8.335  -0.658 -38.958  1.00 82.43           C  
ANISOU 2423  CD  LYS A 333    10181  11093  10046  -1631   -724   1487       C  
ATOM   2424  CE  LYS A 333      -9.094  -1.575 -38.000  1.00 85.22           C  
ANISOU 2424  CE  LYS A 333    10485  11582  10314  -1878   -820   1659       C  
ATOM   2425  NZ  LYS A 333      -8.708  -1.349 -36.576  1.00 84.02           N1+
ANISOU 2425  NZ  LYS A 333    10287  11518  10119  -1876   -758   1686       N1+
ATOM   2426  N   HIS A 334      -5.747  -0.261 -44.368  1.00 52.69           N  
ANISOU 2426  N   HIS A 334     6820   6605   6593  -1090   -789   1013       N  
ATOM   2427  CA  HIS A 334      -5.184   0.524 -45.472  1.00 47.00           C  
ANISOU 2427  CA  HIS A 334     6112   5833   5913   -915   -716    893       C  
ATOM   2428  C   HIS A 334      -5.089   2.003 -45.173  1.00 38.39           C  
ANISOU 2428  C   HIS A 334     4922   4861   4805   -797   -544    846       C  
ATOM   2429  O   HIS A 334      -5.497   2.821 -46.002  1.00 29.40           O  
ANISOU 2429  O   HIS A 334     3731   3778   3663   -716   -476    805       O  
ATOM   2430  CB  HIS A 334      -6.013   0.362 -46.755  1.00 45.23           C  
ANISOU 2430  CB  HIS A 334     5874   5613   5696   -924   -763    896       C  
ATOM   2431  CG  HIS A 334      -5.974  -1.015 -47.334  1.00 53.99           C  
ANISOU 2431  CG  HIS A 334     7115   6570   6830  -1003   -951    916       C  
ATOM   2432  CD2 HIS A 334      -6.908  -1.995 -47.367  1.00 55.33           C  
ANISOU 2432  CD2 HIS A 334     7308   6738   6979  -1174  -1087   1020       C  
ATOM   2433  ND1 HIS A 334      -4.867  -1.517 -47.986  1.00 59.80           N  
ANISOU 2433  ND1 HIS A 334     7984   7131   7605   -898  -1032    821       N  
ATOM   2434  CE1 HIS A 334      -5.121  -2.750 -48.391  1.00 61.94           C  
ANISOU 2434  CE1 HIS A 334     8371   7283   7882   -983  -1218    856       C  
ATOM   2435  NE2 HIS A 334      -6.351  -3.064 -48.026  1.00 60.03           N  
ANISOU 2435  NE2 HIS A 334     8071   7132   7607  -1164  -1259    982       N  
ATOM   2436  N   THR A 335      -4.586   2.362 -43.999  1.00 33.96           N  
ANISOU 2436  N   THR A 335     4343   4333   4226   -786   -484    850       N  
ATOM   2437  CA  THR A 335      -4.423   3.782 -43.724  1.00 34.09           C  
ANISOU 2437  CA  THR A 335     4292   4437   4223   -665   -343    797       C  
ATOM   2438  C   THR A 335      -2.948   4.219 -43.838  1.00 32.65           C  
ANISOU 2438  C   THR A 335     4191   4135   4081   -554   -305    701       C  
ATOM   2439  O   THR A 335      -2.055   3.665 -43.190  1.00 37.45           O  
ANISOU 2439  O   THR A 335     4861   4663   4704   -572   -342    693       O  
ATOM   2440  CB  THR A 335      -5.223   4.244 -42.459  1.00 38.11           C  
ANISOU 2440  CB  THR A 335     4688   5130   4661   -705   -281    866       C  
ATOM   2441  CG2 THR A 335      -5.595   3.070 -41.600  1.00 24.85           C  
ANISOU 2441  CG2 THR A 335     3003   3480   2957   -872   -370    973       C  
ATOM   2442  OG1 THR A 335      -4.479   5.200 -41.700  1.00 37.35           O  
ANISOU 2442  OG1 THR A 335     4593   5041   4558   -603   -191    813       O  
ATOM   2443  N   TYR A 336      -2.719   5.179 -44.733  1.00 26.69           N  
ANISOU 2443  N   TYR A 336     3433   3374   3334   -447   -242    633       N  
ATOM   2444  CA  TYR A 336      -1.386   5.574 -45.161  1.00 22.91           C  
ANISOU 2444  CA  TYR A 336     3020   2805   2882   -359   -218    550       C  
ATOM   2445  C   TYR A 336      -1.240   7.048 -44.944  1.00 21.81           C  
ANISOU 2445  C   TYR A 336     2851   2719   2716   -280   -113    518       C  
ATOM   2446  O   TYR A 336      -2.108   7.807 -45.353  1.00 24.14           O  
ANISOU 2446  O   TYR A 336     3104   3083   2987   -246    -75    522       O  
ATOM   2447  CB  TYR A 336      -1.194   5.276 -46.658  1.00 23.31           C  
ANISOU 2447  CB  TYR A 336     3109   2792   2957   -318   -265    502       C  
ATOM   2448  CG  TYR A 336      -1.372   3.816 -46.985  1.00 23.51           C  
ANISOU 2448  CG  TYR A 336     3186   2744   3003   -382   -395    525       C  
ATOM   2449  CD1 TYR A 336      -0.505   2.867 -46.453  1.00 26.24           C  
ANISOU 2449  CD1 TYR A 336     3609   3004   3357   -400   -475    513       C  
ATOM   2450  CD2 TYR A 336      -2.409   3.378 -47.798  1.00 23.19           C  
ANISOU 2450  CD2 TYR A 336     3131   2714   2967   -423   -452    557       C  
ATOM   2451  CE1 TYR A 336      -0.647   1.530 -46.734  1.00 22.45           C  
ANISOU 2451  CE1 TYR A 336     3208   2435   2888   -452   -620    530       C  
ATOM   2452  CE2 TYR A 336      -2.570   2.020 -48.076  1.00 22.74           C  
ANISOU 2452  CE2 TYR A 336     3145   2570   2925   -490   -595    582       C  
ATOM   2453  CZ  TYR A 336      -1.677   1.108 -47.538  1.00 22.99           C  
ANISOU 2453  CZ  TYR A 336     3270   2501   2962   -502   -685    567       C  
ATOM   2454  OH  TYR A 336      -1.804  -0.241 -47.781  1.00 34.91           O  
ANISOU 2454  OH  TYR A 336     4882   3904   4480   -561   -854    588       O  
ATOM   2455  N   LEU A 337      -0.154   7.457 -44.292  1.00 20.10           N  
ANISOU 2455  N   LEU A 337     2669   2470   2500   -250    -78    486       N  
ATOM   2456  CA  LEU A 337       0.109   8.877 -44.090  1.00 23.17           C  
ANISOU 2456  CA  LEU A 337     3058   2883   2861   -182     -2    457       C  
ATOM   2457  C   LEU A 337       1.381   9.313 -44.803  1.00 22.76           C  
ANISOU 2457  C   LEU A 337     3061   2769   2819   -145      9    399       C  
ATOM   2458  O   LEU A 337       2.449   8.750 -44.571  1.00 29.67           O  
ANISOU 2458  O   LEU A 337     3964   3604   3706   -157    -12    377       O  
ATOM   2459  CB  LEU A 337       0.212   9.197 -42.595  1.00 23.54           C  
ANISOU 2459  CB  LEU A 337     3091   2969   2885   -184     32    478       C  
ATOM   2460  CG  LEU A 337      -0.981   8.742 -41.749  1.00 20.45           C  
ANISOU 2460  CG  LEU A 337     2626   2680   2465   -230     23    544       C  
ATOM   2461  CD1 LEU A 337      -0.773   9.084 -40.254  1.00 20.53           C  
ANISOU 2461  CD1 LEU A 337     2618   2738   2445   -219     58    559       C  
ATOM   2462  CD2 LEU A 337      -2.271   9.360 -42.276  1.00 20.85           C  
ANISOU 2462  CD2 LEU A 337     2617   2830   2473   -191     41    555       C  
ATOM   2463  N   PRO A 338       1.271  10.326 -45.678  1.00 19.75           N  
ANISOU 2463  N   PRO A 338     2692   2392   2419   -101     36    378       N  
ATOM   2464  CA  PRO A 338       2.456  10.949 -46.281  1.00 19.43           C  
ANISOU 2464  CA  PRO A 338     2695   2322   2367    -86     50    340       C  
ATOM   2465  C   PRO A 338       3.361  11.457 -45.166  1.00 25.37           C  
ANISOU 2465  C   PRO A 338     3473   3064   3103    -95     77    336       C  
ATOM   2466  O   PRO A 338       2.840  11.948 -44.156  1.00 25.38           O  
ANISOU 2466  O   PRO A 338     3474   3079   3091    -82     98    355       O  
ATOM   2467  CB  PRO A 338       1.883  12.154 -47.035  1.00 19.48           C  
ANISOU 2467  CB  PRO A 338     2722   2334   2344    -50     71    337       C  
ATOM   2468  CG  PRO A 338       0.419  11.911 -47.144  1.00 24.28           C  
ANISOU 2468  CG  PRO A 338     3287   2982   2955    -31     63    359       C  
ATOM   2469  CD  PRO A 338       0.029  11.055 -45.984  1.00 19.73           C  
ANISOU 2469  CD  PRO A 338     2667   2438   2391    -65     55    391       C  
ATOM   2470  N   LEU A 339       4.675  11.338 -45.337  1.00 23.35           N  
ANISOU 2470  N   LEU A 339     3233   2801   2839   -111     73    310       N  
ATOM   2471  CA  LEU A 339       5.624  11.698 -44.284  1.00 24.08           C  
ANISOU 2471  CA  LEU A 339     3345   2888   2915   -127     94    305       C  
ATOM   2472  C   LEU A 339       5.466  13.138 -43.824  1.00 24.69           C  
ANISOU 2472  C   LEU A 339     3469   2949   2963   -120    120    320       C  
ATOM   2473  O   LEU A 339       5.586  13.444 -42.634  1.00 23.88           O  
ANISOU 2473  O   LEU A 339     3383   2837   2855   -115    133    326       O  
ATOM   2474  CB  LEU A 339       7.061  11.490 -44.759  1.00 18.51           C  
ANISOU 2474  CB  LEU A 339     2637   2212   2185   -143     85    273       C  
ATOM   2475  CG  LEU A 339       7.421  10.070 -45.202  1.00 18.58           C  
ANISOU 2475  CG  LEU A 339     2619   2237   2205   -120     38    239       C  
ATOM   2476  CD1 LEU A 339       8.914   9.964 -45.468  1.00 18.72           C  
ANISOU 2476  CD1 LEU A 339     2619   2321   2171   -115     32    198       C  
ATOM   2477  CD2 LEU A 339       6.967   9.020 -44.181  1.00 18.59           C  
ANISOU 2477  CD2 LEU A 339     2624   2195   2244   -120      9    249       C  
ATOM   2478  N   GLU A 340       5.181  14.018 -44.775  1.00 18.78           N  
ANISOU 2478  N   GLU A 340     2753   2193   2190   -113    115    322       N  
ATOM   2479  CA  GLU A 340       5.229  15.449 -44.517  1.00 19.53           C  
ANISOU 2479  CA  GLU A 340     2927   2251   2244   -109    111    331       C  
ATOM   2480  C   GLU A 340       4.089  15.932 -43.616  1.00 19.26           C  
ANISOU 2480  C   GLU A 340     2910   2208   2199    -37    110    334       C  
ATOM   2481  O   GLU A 340       4.175  16.998 -43.041  1.00 26.33           O  
ANISOU 2481  O   GLU A 340     3882   3066   3058    -13     92    331       O  
ATOM   2482  CB  GLU A 340       5.255  16.225 -45.835  1.00 20.89           C  
ANISOU 2482  CB  GLU A 340     3144   2411   2384   -127     90    337       C  
ATOM   2483  CG  GLU A 340       4.009  16.050 -46.676  1.00 28.03           C  
ANISOU 2483  CG  GLU A 340     4025   3323   3300    -75     86    333       C  
ATOM   2484  CD  GLU A 340       4.193  16.532 -48.106  1.00 31.61           C  
ANISOU 2484  CD  GLU A 340     4507   3774   3728   -100     69    338       C  
ATOM   2485  OE1 GLU A 340       3.772  17.675 -48.417  1.00 34.87           O  
ANISOU 2485  OE1 GLU A 340     5005   4142   4102    -83     41    345       O  
ATOM   2486  OE2 GLU A 340       4.743  15.760 -48.924  1.00 32.15           O1-
ANISOU 2486  OE2 GLU A 340     4517   3890   3807   -130     74    331       O1-
ATOM   2487  N   VAL A 341       3.031  15.144 -43.478  1.00 19.24           N  
ANISOU 2487  N   VAL A 341     2837   2253   2218     -3    121    339       N  
ATOM   2488  CA  VAL A 341       1.932  15.555 -42.608  1.00 23.41           C  
ANISOU 2488  CA  VAL A 341     3356   2824   2716     71    123    342       C  
ATOM   2489  C   VAL A 341       2.131  15.003 -41.176  1.00 25.71           C  
ANISOU 2489  C   VAL A 341     3605   3147   3015     63    140    354       C  
ATOM   2490  O   VAL A 341       1.248  15.118 -40.341  1.00 31.56           O  
ANISOU 2490  O   VAL A 341     4310   3959   3724    120    146    362       O  
ATOM   2491  CB  VAL A 341       0.534  15.109 -43.162  1.00 19.84           C  
ANISOU 2491  CB  VAL A 341     2834   2444   2259    106    122    352       C  
ATOM   2492  CG1 VAL A 341       0.304  15.598 -44.593  1.00 21.46           C  
ANISOU 2492  CG1 VAL A 341     3078   2617   2457    119    106    337       C  
ATOM   2493  CG2 VAL A 341       0.368  13.595 -43.098  1.00 19.66           C  
ANISOU 2493  CG2 VAL A 341     2725   2462   2284     39    127    381       C  
ATOM   2494  N   CYS A 342       3.293  14.416 -40.901  1.00 20.53           N  
ANISOU 2494  N   CYS A 342     2951   2456   2393     -1    147    354       N  
ATOM   2495  CA  CYS A 342       3.521  13.712 -39.635  1.00 20.68           C  
ANISOU 2495  CA  CYS A 342     2932   2500   2426    -17    161    367       C  
ATOM   2496  C   CYS A 342       4.669  14.241 -38.779  1.00 25.77           C  
ANISOU 2496  C   CYS A 342     3628   3101   3062    -24    167    351       C  
ATOM   2497  O   CYS A 342       5.747  14.544 -39.297  1.00 25.21           O  
ANISOU 2497  O   CYS A 342     3601   2985   2991    -64    161    336       O  
ATOM   2498  CB  CYS A 342       3.785  12.232 -39.897  1.00 18.86           C  
ANISOU 2498  CB  CYS A 342     2655   2271   2241    -80    148    379       C  
ATOM   2499  SG  CYS A 342       2.460  11.366 -40.709  1.00 27.70           S  
ANISOU 2499  SG  CYS A 342     3714   3437   3374    -97    124    410       S  
ATOM   2500  N   ASN A 343       4.425  14.307 -37.465  1.00 21.97           N  
ANISOU 2500  N   ASN A 343     3132   2651   2565     11    178    359       N  
ATOM   2501  CA  ASN A 343       5.443  14.587 -36.446  1.00 25.62           C  
ANISOU 2501  CA  ASN A 343     3631   3079   3024      5    185    346       C  
ATOM   2502  C   ASN A 343       5.622  13.393 -35.536  1.00 24.08           C  
ANISOU 2502  C   ASN A 343     3376   2916   2856    -27    199    363       C  
ATOM   2503  O   ASN A 343       4.658  12.695 -35.238  1.00 22.96           O  
ANISOU 2503  O   ASN A 343     3171   2839   2714    -27    201    395       O  
ATOM   2504  CB  ASN A 343       5.018  15.749 -35.538  1.00 21.78           C  
ANISOU 2504  CB  ASN A 343     3190   2599   2487     93    174    334       C  
ATOM   2505  CG  ASN A 343       5.027  17.083 -36.247  1.00 29.68           C  
ANISOU 2505  CG  ASN A 343     4292   3535   3450    126    134    314       C  
ATOM   2506  ND2 ASN A 343       4.130  17.972 -35.841  1.00 36.83           N  
ANISOU 2506  ND2 ASN A 343     5234   4460   4298    237    105    297       N  
ATOM   2507  OD1 ASN A 343       5.825  17.315 -37.144  1.00 35.38           O  
ANISOU 2507  OD1 ASN A 343     5061   4198   4182     57    121    314       O  
ATOM   2508  N   ILE A 344       6.846  13.172 -35.072  1.00 26.50           N  
ANISOU 2508  N   ILE A 344     3707   3185   3178    -60    204    345       N  
ATOM   2509  CA  ILE A 344       7.091  12.194 -34.017  1.00 25.06           C  
ANISOU 2509  CA  ILE A 344     3491   3020   3013    -79    210    356       C  
ATOM   2510  C   ILE A 344       6.466  12.729 -32.717  1.00 18.73           C  
ANISOU 2510  C   ILE A 344     2674   2265   2179    -22    226    372       C  
ATOM   2511  O   ILE A 344       6.747  13.848 -32.320  1.00 18.83           O  
ANISOU 2511  O   ILE A 344     2736   2254   2163     28    227    349       O  
ATOM   2512  CB  ILE A 344       8.606  11.966 -33.786  1.00 21.78           C  
ANISOU 2512  CB  ILE A 344     3105   2564   2606   -108    210    322       C  
ATOM   2513  CG1 ILE A 344       9.307  11.572 -35.088  1.00 18.00           C  
ANISOU 2513  CG1 ILE A 344     2631   2074   2135   -142    192    297       C  
ATOM   2514  CG2 ILE A 344       8.836  10.903 -32.703  1.00 19.11           C  
ANISOU 2514  CG2 ILE A 344     2745   2233   2284   -121    207    330       C  
ATOM   2515  CD1 ILE A 344       9.092  10.127 -35.477  1.00 18.03           C  
ANISOU 2515  CD1 ILE A 344     2609   2079   2164   -158    157    299       C  
ATOM   2516  N   VAL A 345       5.602  11.944 -32.082  1.00 19.96           N  
ANISOU 2516  N   VAL A 345     2762   2494   2328    -30    228    413       N  
ATOM   2517  CA  VAL A 345       4.977  12.344 -30.820  1.00 21.57           C  
ANISOU 2517  CA  VAL A 345     2929   2782   2486     30    244    431       C  
ATOM   2518  C   VAL A 345       6.045  12.516 -29.715  1.00 23.52           C  
ANISOU 2518  C   VAL A 345     3213   2986   2738     44    255    406       C  
ATOM   2519  O   VAL A 345       6.900  11.649 -29.527  1.00 22.63           O  
ANISOU 2519  O   VAL A 345     3111   2827   2663    -17    252    404       O  
ATOM   2520  CB  VAL A 345       3.889  11.317 -30.386  1.00 26.24           C  
ANISOU 2520  CB  VAL A 345     3425   3489   3058    -15    240    498       C  
ATOM   2521  CG1 VAL A 345       3.445  11.526 -28.911  1.00 20.42           C  
ANISOU 2521  CG1 VAL A 345     2630   2866   2263     36    258    521       C  
ATOM   2522  CG2 VAL A 345       2.695  11.369 -31.334  1.00 21.83           C  
ANISOU 2522  CG2 VAL A 345     2818   3000   2476    -14    230    521       C  
ATOM   2523  N   ALA A 346       6.001  13.647 -29.015  1.00 22.07           N  
ANISOU 2523  N   ALA A 346     3058   2814   2512    134    259    381       N  
ATOM   2524  CA  ALA A 346       6.911  13.910 -27.888  1.00 28.96           C  
ANISOU 2524  CA  ALA A 346     3967   3653   3385    157    266    358       C  
ATOM   2525  C   ALA A 346       6.833  12.850 -26.798  1.00 27.53           C  
ANISOU 2525  C   ALA A 346     3719   3536   3207    127    284    394       C  
ATOM   2526  O   ALA A 346       5.775  12.299 -26.535  1.00 33.22           O  
ANISOU 2526  O   ALA A 346     4357   4366   3898    119    288    444       O  
ATOM   2527  CB  ALA A 346       6.623  15.286 -27.279  1.00 28.28           C  
ANISOU 2527  CB  ALA A 346     3929   3578   3240    278    247    326       C  
ATOM   2528  N   GLY A 347       7.966  12.560 -26.177  1.00 24.83           N  
ANISOU 2528  N   GLY A 347     3410   3132   2892    101    290    374       N  
ATOM   2529  CA  GLY A 347       7.985  11.789 -24.950  1.00 23.92           C  
ANISOU 2529  CA  GLY A 347     3251   3066   2770     89    302    402       C  
ATOM   2530  C   GLY A 347       8.014  10.279 -25.058  1.00 31.16           C  
ANISOU 2530  C   GLY A 347     4144   3979   3718    -11    284    443       C  
ATOM   2531  O   GLY A 347       7.604   9.587 -24.127  1.00 30.68           O  
ANISOU 2531  O   GLY A 347     4036   3984   3637    -37    282    492       O  
ATOM   2532  N   GLN A 348       8.494   9.751 -26.175  1.00 28.29           N  
ANISOU 2532  N   GLN A 348     3816   3538   3393    -65    260    425       N  
ATOM   2533  CA  GLN A 348       8.580   8.305 -26.316  1.00 26.21           C  
ANISOU 2533  CA  GLN A 348     3561   3246   3153   -146    216    453       C  
ATOM   2534  C   GLN A 348      10.000   7.869 -26.033  1.00 26.95           C  
ANISOU 2534  C   GLN A 348     3713   3260   3268   -143    204    398       C  
ATOM   2535  O   GLN A 348      10.943   8.405 -26.625  1.00 26.24           O  
ANISOU 2535  O   GLN A 348     3656   3129   3186   -115    215    337       O  
ATOM   2536  CB  GLN A 348       8.195   7.867 -27.730  1.00 22.37           C  
ANISOU 2536  CB  GLN A 348     3081   2732   2685   -188    180    459       C  
ATOM   2537  CG  GLN A 348       6.821   8.301 -28.182  1.00 23.64           C  
ANISOU 2537  CG  GLN A 348     3182   2977   2823   -188    191    506       C  
ATOM   2538  CD  GLN A 348       6.584   7.988 -29.667  1.00 26.25           C  
ANISOU 2538  CD  GLN A 348     3529   3268   3178   -219    159    500       C  
ATOM   2539  NE2 GLN A 348       6.541   9.026 -30.487  1.00 18.98           N  
ANISOU 2539  NE2 GLN A 348     2614   2345   2255   -169    186    465       N  
ATOM   2540  OE1 GLN A 348       6.448   6.827 -30.060  1.00 19.46           O  
ANISOU 2540  OE1 GLN A 348     2685   2374   2334   -287    100    526       O  
ATOM   2541  N   ARG A 349      10.167   6.909 -25.126  1.00 26.05           N  
ANISOU 2541  N   ARG A 349     3611   3136   3151   -174    176    421       N  
ATOM   2542  CA  ARG A 349      11.502   6.402 -24.838  1.00 31.35           C  
ANISOU 2542  CA  ARG A 349     4341   3739   3832   -158    155    361       C  
ATOM   2543  C   ARG A 349      11.980   5.504 -25.965  1.00 30.59           C  
ANISOU 2543  C   ARG A 349     4296   3581   3747   -174     89    324       C  
ATOM   2544  O   ARG A 349      11.184   4.831 -26.619  1.00 35.87           O  
ANISOU 2544  O   ARG A 349     4971   4236   4422   -223     37    366       O  
ATOM   2545  CB  ARG A 349      11.565   5.626 -23.523  1.00 42.76           C  
ANISOU 2545  CB  ARG A 349     5798   5182   5265   -179    134    393       C  
ATOM   2546  CG  ARG A 349      13.007   5.414 -23.059  1.00 53.15           C  
ANISOU 2546  CG  ARG A 349     7167   6445   6582   -133    129    316       C  
ATOM   2547  CD  ARG A 349      13.131   4.362 -21.984  1.00 64.50           C  
ANISOU 2547  CD  ARG A 349     8644   7854   8008   -159     81    342       C  
ATOM   2548  NE  ARG A 349      12.812   3.026 -22.469  1.00 70.76           N  
ANISOU 2548  NE  ARG A 349     9500   8585   8800   -222    -22    372       N  
ATOM   2549  CZ  ARG A 349      12.887   1.933 -21.720  1.00 77.04           C  
ANISOU 2549  CZ  ARG A 349    10362   9330   9581   -262    -98    401       C  
ATOM   2550  NH1 ARG A 349      13.271   2.021 -20.456  1.00 79.36           N1+
ANISOU 2550  NH1 ARG A 349    10652   9641   9863   -243    -68    403       N1+
ATOM   2551  NH2 ARG A 349      12.580   0.753 -22.233  1.00 84.38           N  
ANISOU 2551  NH2 ARG A 349    11373  10184  10505   -323   -216    430       N  
ATOM   2552  N   CYS A 350      13.287   5.491 -26.181  1.00 29.76           N  
ANISOU 2552  N   CYS A 350     4224   3449   3634   -127     84    243       N  
ATOM   2553  CA  CYS A 350      13.868   4.602 -27.167  1.00 33.76           C  
ANISOU 2553  CA  CYS A 350     4777   3917   4131   -111     12    190       C  
ATOM   2554  C   CYS A 350      14.152   3.241 -26.532  1.00 40.74           C  
ANISOU 2554  C   CYS A 350     5737   4737   5004   -112    -77    183       C  
ATOM   2555  O   CYS A 350      15.056   3.102 -25.704  1.00 43.55           O  
ANISOU 2555  O   CYS A 350     6116   5088   5343    -71    -73    138       O  
ATOM   2556  CB  CYS A 350      15.130   5.229 -27.765  1.00 37.82           C  
ANISOU 2556  CB  CYS A 350     5277   4474   4620    -57     44    107       C  
ATOM   2557  SG  CYS A 350      15.934   4.233 -29.049  1.00 55.35           S  
ANISOU 2557  SG  CYS A 350     7533   6696   6800     -1    -44     24       S  
ATOM   2558  N   ILE A 351      13.347   2.248 -26.907  1.00 45.78           N  
ANISOU 2558  N   ILE A 351     6422   5322   5649   -164   -166    230       N  
ATOM   2559  CA  ILE A 351      13.564   0.862 -26.492  1.00 51.73           C  
ANISOU 2559  CA  ILE A 351     7282   5987   6385   -173   -288    227       C  
ATOM   2560  C   ILE A 351      14.473   0.143 -27.497  1.00 55.40           C  
ANISOU 2560  C   ILE A 351     7822   6409   6819    -84   -381    124       C  
ATOM   2561  O   ILE A 351      15.243  -0.744 -27.120  1.00 53.76           O  
ANISOU 2561  O   ILE A 351     7705   6143   6577    -28   -471     66       O  
ATOM   2562  CB  ILE A 351      12.220   0.088 -26.294  1.00 64.68           C  
ANISOU 2562  CB  ILE A 351     8952   7589   8035   -295   -363    344       C  
ATOM   2563  CG1 ILE A 351      12.467  -1.362 -25.861  1.00 66.68           C  
ANISOU 2563  CG1 ILE A 351     9345   7726   8263   -320   -516    348       C  
ATOM   2564  CG2 ILE A 351      11.379   0.109 -27.569  1.00 62.61           C  
ANISOU 2564  CG2 ILE A 351     8669   7330   7787   -331   -387    372       C  
ATOM   2565  CD1 ILE A 351      13.263  -1.526 -24.572  1.00 68.41           C  
ANISOU 2565  CD1 ILE A 351     9598   7930   8463   -286   -508    322       C  
ATOM   2566  N   LYS A 352      14.385   0.533 -28.770  1.00 53.81           N  
ANISOU 2566  N   LYS A 352     7580   6244   6620    -59   -365     97       N  
ATOM   2567  CA  LYS A 352      15.286   0.015 -29.796  1.00 53.00           C  
ANISOU 2567  CA  LYS A 352     7522   6144   6473     46   -440     -9       C  
ATOM   2568  C   LYS A 352      16.729   0.252 -29.368  1.00 53.75           C  
ANISOU 2568  C   LYS A 352     7599   6307   6518    145   -406   -107       C  
ATOM   2569  O   LYS A 352      17.028   1.242 -28.700  1.00 54.01           O  
ANISOU 2569  O   LYS A 352     7556   6404   6562    124   -292    -94       O  
ATOM   2570  CB  LYS A 352      15.030   0.683 -31.152  1.00 53.89           C  
ANISOU 2570  CB  LYS A 352     7564   6322   6591     54   -396    -18       C  
ATOM   2571  CG  LYS A 352      13.746   0.261 -31.862  1.00 55.87           C  
ANISOU 2571  CG  LYS A 352     7841   6511   6877    -17   -455     54       C  
ATOM   2572  CD  LYS A 352      13.581   1.032 -33.187  1.00 58.13           C  
ANISOU 2572  CD  LYS A 352     8052   6870   7166      1   -399     38       C  
ATOM   2573  CE  LYS A 352      12.140   1.014 -33.697  1.00 56.61           C  
ANISOU 2573  CE  LYS A 352     7850   6643   7018    -88   -412    127       C  
ATOM   2574  NZ  LYS A 352      11.680  -0.366 -34.020  1.00 61.33           N1+
ANISOU 2574  NZ  LYS A 352     8558   7133   7611   -104   -570    139       N1+
ATOM   2575  N   LYS A 353      17.623  -0.655 -29.746  1.00 54.71           N  
ANISOU 2575  N   LYS A 353     7792   6421   6575    258   -513   -209       N  
ATOM   2576  CA  LYS A 353      19.004  -0.585 -29.283  1.00 56.10           C  
ANISOU 2576  CA  LYS A 353     7950   6678   6686    360   -496   -307       C  
ATOM   2577  C   LYS A 353      19.778   0.591 -29.886  1.00 56.20           C  
ANISOU 2577  C   LYS A 353     7829   6861   6665    383   -379   -347       C  
ATOM   2578  O   LYS A 353      19.561   0.975 -31.045  1.00 55.39           O  
ANISOU 2578  O   LYS A 353     7672   6817   6555    378   -362   -345       O  
ATOM   2579  CB  LYS A 353      19.735  -1.900 -29.560  1.00 57.93           C  
ANISOU 2579  CB  LYS A 353     8299   6874   6838    500   -658   -417       C  
ATOM   2580  CG  LYS A 353      20.060  -2.145 -31.022  1.00 61.73           C  
ANISOU 2580  CG  LYS A 353     8767   7431   7258    604   -720   -498       C  
ATOM   2581  CD  LYS A 353      21.187  -3.153 -31.159  1.00 69.68           C  
ANISOU 2581  CD  LYS A 353     9855   8470   8150    792   -857   -643       C  
ATOM   2582  CE  LYS A 353      22.380  -2.760 -30.291  1.00 73.75           C  
ANISOU 2582  CE  LYS A 353    10307   9105   8610    851   -784   -707       C  
ATOM   2583  NZ  LYS A 353      23.453  -3.797 -30.285  1.00 78.37           N1+
ANISOU 2583  NZ  LYS A 353    10979   9727   9073   1051   -926   -856       N1+
ATOM   2584  N   LEU A 354      20.675   1.164 -29.088  1.00 52.46           N  
ANISOU 2584  N   LEU A 354     7303   6466   6164    397   -306   -377       N  
ATOM   2585  CA  LEU A 354      21.535   2.246 -29.558  1.00 51.14           C  
ANISOU 2585  CA  LEU A 354     7016   6466   5948    398   -212   -407       C  
ATOM   2586  C   LEU A 354      22.662   1.695 -30.410  1.00 53.98           C  
ANISOU 2586  C   LEU A 354     7351   6969   6191    531   -278   -526       C  
ATOM   2587  O   LEU A 354      23.140   0.589 -30.175  1.00 59.32           O  
ANISOU 2587  O   LEU A 354     8106   7620   6813    648   -384   -610       O  
ATOM   2588  CB  LEU A 354      22.142   3.013 -28.384  1.00 43.07           C  
ANISOU 2588  CB  LEU A 354     5953   5482   4930    362   -126   -397       C  
ATOM   2589  CG  LEU A 354      21.194   3.731 -27.426  1.00 40.98           C  
ANISOU 2589  CG  LEU A 354     5697   5117   4759    256    -54   -293       C  
ATOM   2590  CD1 LEU A 354      21.995   4.551 -26.428  1.00 36.11           C  
ANISOU 2590  CD1 LEU A 354     5036   4555   4128    240     21   -302       C  
ATOM   2591  CD2 LEU A 354      20.198   4.599 -28.192  1.00 37.61           C  
ANISOU 2591  CD2 LEU A 354     5230   4677   4381    171     -4   -214       C  
ATOM   2592  N   THR A 355      23.102   2.476 -31.389  1.00 50.75           N  
ANISOU 2592  N   THR A 355     6833   6720   5729    516   -224   -535       N  
ATOM   2593  CA  THR A 355      24.279   2.110 -32.162  1.00 52.22           C  
ANISOU 2593  CA  THR A 355     6958   7106   5779    643   -270   -647       C  
ATOM   2594  C   THR A 355      25.541   2.306 -31.324  1.00 57.12           C  
ANISOU 2594  C   THR A 355     7524   7859   6320    682   -237   -707       C  
ATOM   2595  O   THR A 355      25.471   2.490 -30.105  1.00 55.50           O  
ANISOU 2595  O   THR A 355     7359   7555   6175    632   -199   -673       O  
ATOM   2596  CB  THR A 355      24.384   2.914 -33.474  1.00 53.78           C  
ANISOU 2596  CB  THR A 355     7041   7464   5930    598   -221   -626       C  
ATOM   2597  CG2 THR A 355      23.077   2.836 -34.259  1.00 53.51           C  
ANISOU 2597  CG2 THR A 355     7056   7293   5982    550   -241   -561       C  
ATOM   2598  OG1 THR A 355      24.685   4.282 -33.181  1.00 56.26           O  
ANISOU 2598  OG1 THR A 355     7265   7859   6251    460   -105   -556       O  
ATOM   2599  N   ASP A 356      26.694   2.263 -31.978  1.00 67.86           N  
ANISOU 2599  N   ASP A 356    10529   7597   7657   1065    230    973       N  
ATOM   2600  CA  ASP A 356      27.963   2.344 -31.270  1.00 73.08           C  
ANISOU 2600  CA  ASP A 356    11191   8200   8375    921    348    965       C  
ATOM   2601  C   ASP A 356      28.316   3.772 -30.887  1.00 72.20           C  
ANISOU 2601  C   ASP A 356    11172   7965   8296    887    455    981       C  
ATOM   2602  O   ASP A 356      28.653   4.046 -29.735  1.00 72.96           O  
ANISOU 2602  O   ASP A 356    11228   8018   8475    811    505    956       O  
ATOM   2603  CB  ASP A 356      29.077   1.706 -32.097  1.00 80.42           C  
ANISOU 2603  CB  ASP A 356    12150   9150   9256    845    407    971       C  
ATOM   2604  CG  ASP A 356      28.953   0.195 -32.162  1.00 85.72           C  
ANISOU 2604  CG  ASP A 356    12716   9935   9918    846    318    942       C  
ATOM   2605  OD1 ASP A 356      28.474  -0.401 -31.171  1.00 81.41           O  
ANISOU 2605  OD1 ASP A 356    12061   9436   9437    845    251    912       O  
ATOM   2606  OD2 ASP A 356      29.326  -0.394 -33.201  1.00 91.31           O1-
ANISOU 2606  OD2 ASP A 356    13455  10685  10554    849    316    948       O1-
ATOM   2607  N   ASN A 357      28.240   4.679 -31.854  1.00 73.58           N  
ANISOU 2607  N   ASN A 357    11473   8081   8402    943    491   1021       N  
ATOM   2608  CA  ASN A 357      28.449   6.091 -31.572  1.00 75.47           C  
ANISOU 2608  CA  ASN A 357    11812   8199   8666    926    586   1038       C  
ATOM   2609  C   ASN A 357      27.416   6.566 -30.561  1.00 71.54           C  
ANISOU 2609  C   ASN A 357    11268   7686   8227    994    528   1020       C  
ATOM   2610  O   ASN A 357      27.763   7.119 -29.510  1.00 67.26           O  
ANISOU 2610  O   ASN A 357    10715   7078   7763    922    594    997       O  
ATOM   2611  CB  ASN A 357      28.373   6.929 -32.851  1.00 79.73           C  
ANISOU 2611  CB  ASN A 357    12500   8682   9110    998    619   1089       C  
ATOM   2612  CG  ASN A 357      27.993   6.109 -34.073  1.00 82.42           C  
ANISOU 2612  CG  ASN A 357    12848   9114   9355   1079    536   1107       C  
ATOM   2613  ND2 ASN A 357      28.960   5.376 -34.613  1.00 84.00           N  
ANISOU 2613  ND2 ASN A 357    13044   9345   9526    998    583   1103       N  
ATOM   2614  OD1 ASN A 357      26.848   6.141 -34.531  1.00 83.33           O  
ANISOU 2614  OD1 ASN A 357    12968   9270   9422   1214    431   1119       O  
ATOM   2615  N   GLN A 358      26.150   6.316 -30.888  1.00 68.60           N  
ANISOU 2615  N   GLN A 358    10862   7381   7821   1132    405   1026       N  
ATOM   2616  CA  GLN A 358      25.030   6.670 -30.026  1.00 60.82           C  
ANISOU 2616  CA  GLN A 358     9820   6399   6888   1215    338   1006       C  
ATOM   2617  C   GLN A 358      25.311   6.334 -28.575  1.00 55.43           C  
ANISOU 2617  C   GLN A 358     9037   5716   6307   1125    361    961       C  
ATOM   2618  O   GLN A 358      25.145   7.185 -27.700  1.00 56.71           O  
ANISOU 2618  O   GLN A 358     9215   5805   6525   1121    402    948       O  
ATOM   2619  CB  GLN A 358      23.750   5.977 -30.494  1.00 54.02           C  
ANISOU 2619  CB  GLN A 358     8882   5652   5991   1346    190    997       C  
ATOM   2620  CG  GLN A 358      23.107   6.634 -31.702  1.00 49.82           C  
ANISOU 2620  CG  GLN A 358     8454   5108   5368   1471    153   1036       C  
ATOM   2621  CD  GLN A 358      21.835   5.929 -32.134  1.00 57.03           C  
ANISOU 2621  CD  GLN A 358     9274   6141   6252   1594      2   1014       C  
ATOM   2622  NE2 GLN A 358      21.089   6.551 -33.041  1.00 62.95           N  
ANISOU 2622  NE2 GLN A 358    10101   6885   6930   1718    -44   1041       N  
ATOM   2623  OE1 GLN A 358      21.523   4.838 -31.655  1.00 57.00           O  
ANISOU 2623  OE1 GLN A 358     9131   6235   6291   1575    -71    971       O  
ATOM   2624  N   THR A 359      25.771   5.110 -28.328  1.00 54.91           N  
ANISOU 2624  N   THR A 359     8875   5729   6260   1052    337    937       N  
ATOM   2625  CA  THR A 359      26.038   4.654 -26.963  1.00 56.14           C  
ANISOU 2625  CA  THR A 359     8933   5893   6505    969    351    895       C  
ATOM   2626  C   THR A 359      27.188   5.421 -26.307  1.00 57.63           C  
ANISOU 2626  C   THR A 359     9176   5976   6743    838    487    884       C  
ATOM   2627  O   THR A 359      27.076   5.878 -25.170  1.00 60.84           O  
ANISOU 2627  O   THR A 359     9560   6336   7220    812    514    853       O  
ATOM   2628  CB  THR A 359      26.320   3.141 -26.910  1.00 52.61           C  
ANISOU 2628  CB  THR A 359     8379   5551   6061    922    297    876       C  
ATOM   2629  CG2 THR A 359      26.705   2.726 -25.509  1.00 48.21           C  
ANISOU 2629  CG2 THR A 359     7720   5004   5593    823    321    828       C  
ATOM   2630  OG1 THR A 359      25.141   2.424 -27.293  1.00 54.89           O  
ANISOU 2630  OG1 THR A 359     8593   5941   6322   1037    165    870       O  
ATOM   2631  N   SER A 360      28.288   5.556 -27.037  1.00 62.78           N  
ANISOU 2631  N   SER A 360     9898   6594   7362    755    572    901       N  
ATOM   2632  CA  SER A 360      29.435   6.332 -26.586  1.00 65.70           C  
ANISOU 2632  CA  SER A 360    10318   6870   7777    624    704    882       C  
ATOM   2633  C   SER A 360      29.026   7.766 -26.263  1.00 63.24           C  
ANISOU 2633  C   SER A 360    10093   6450   7484    664    749    886       C  
ATOM   2634  O   SER A 360      29.306   8.261 -25.168  1.00 60.82           O  
ANISOU 2634  O   SER A 360     9769   6087   7251    593    802    845       O  
ATOM   2635  CB  SER A 360      30.516   6.335 -27.667  1.00 72.23           C  
ANISOU 2635  CB  SER A 360    11212   7680   8551    554    784    904       C  
ATOM   2636  OG  SER A 360      30.707   5.032 -28.185  1.00 75.95           O  
ANISOU 2636  OG  SER A 360    11618   8254   8987    549    730    907       O  
ATOM   2637  N   THR A 361      28.374   8.418 -27.231  1.00 59.65           N  
ANISOU 2637  N   THR A 361     9736   5969   6961    778    727    933       N  
ATOM   2638  CA  THR A 361      27.840   9.768 -27.061  1.00 54.75           C  
ANISOU 2638  CA  THR A 361     9208   5249   6347    842    757    945       C  
ATOM   2639  C   THR A 361      27.074   9.866 -25.748  1.00 50.13           C  
ANISOU 2639  C   THR A 361     8545   4664   5837    874    714    903       C  
ATOM   2640  O   THR A 361      27.285  10.788 -24.963  1.00 53.97           O  
ANISOU 2640  O   THR A 361     9069   5059   6377    829    785    876       O  
ATOM   2641  CB  THR A 361      26.895  10.166 -28.225  1.00 38.40           C  
ANISOU 2641  CB  THR A 361     7220   3182   4187    997    695    999       C  
ATOM   2642  CG2 THR A 361      26.678  11.667 -28.272  1.00 33.87           C  
ANISOU 2642  CG2 THR A 361     6776   2484   3609   1042    758   1022       C  
ATOM   2643  OG1 THR A 361      27.460   9.751 -29.471  1.00 55.10           O  
ANISOU 2643  OG1 THR A 361     9387   5326   6224    983    710   1034       O  
ATOM   2644  N   MET A 362      26.205   8.892 -25.498  1.00 44.03           N  
ANISOU 2644  N   MET A 362     7663   3997   5070    949    600    892       N  
ATOM   2645  CA  MET A 362      25.398   8.907 -24.283  1.00 52.01           C  
ANISOU 2645  CA  MET A 362     8595   5018   6149    991    556    851       C  
ATOM   2646  C   MET A 362      26.237   8.766 -23.016  1.00 56.80           C  
ANISOU 2646  C   MET A 362     9151   5594   6836    851    627    797       C  
ATOM   2647  O   MET A 362      25.967   9.417 -22.015  1.00 56.24           O  
ANISOU 2647  O   MET A 362     9081   5466   6822    851    656    760       O  
ATOM   2648  CB  MET A 362      24.329   7.819 -24.328  1.00 53.04           C  
ANISOU 2648  CB  MET A 362     8608   5276   6270   1093    423    846       C  
ATOM   2649  CG  MET A 362      23.470   7.776 -23.084  1.00 54.36           C  
ANISOU 2649  CG  MET A 362     8686   5462   6508   1141    383    800       C  
ATOM   2650  SD  MET A 362      21.909   6.930 -23.343  1.00 59.58           S  
ANISOU 2650  SD  MET A 362     9224   6261   7155   1298    226    793       S  
ATOM   2651  CE  MET A 362      20.832   8.111 -22.560  1.00 71.34           C  
ANISOU 2651  CE  MET A 362    10723   7690   8692   1406    228    767       C  
ATOM   2652  N   ILE A 363      27.259   7.920 -23.058  1.00 61.28           N  
ANISOU 2652  N   ILE A 363     9676   6201   7408    732    656    788       N  
ATOM   2653  CA  ILE A 363      28.106   7.724 -21.883  1.00 62.29           C  
ANISOU 2653  CA  ILE A 363     9750   6309   7610    594    717    731       C  
ATOM   2654  C   ILE A 363      28.884   8.989 -21.489  1.00 59.36           C  
ANISOU 2654  C   ILE A 363     9459   5819   7275    499    836    702       C  
ATOM   2655  O   ILE A 363      28.988   9.307 -20.306  1.00 61.63           O  
ANISOU 2655  O   ILE A 363     9719   6068   7628    443    869    644       O  
ATOM   2656  CB  ILE A 363      29.052   6.519 -22.062  1.00 62.87           C  
ANISOU 2656  CB  ILE A 363     9739   6471   7680    486    714    719       C  
ATOM   2657  CG1 ILE A 363      28.231   5.260 -22.354  1.00 65.04           C  
ANISOU 2657  CG1 ILE A 363     9895   6891   7926    567    585    723       C  
ATOM   2658  CG2 ILE A 363      29.890   6.318 -20.819  1.00 58.16           C  
ANISOU 2658  CG2 ILE A 363     9032   5907   7159    338    752    633       C  
ATOM   2659  CD1 ILE A 363      29.034   4.102 -22.906  1.00 65.15           C  
ANISOU 2659  CD1 ILE A 363     9842   6996   7917    492    570    719       C  
ATOM   2660  N   LYS A 364      29.407   9.718 -22.475  1.00 56.32           N  
ANISOU 2660  N   LYS A 364     9177   5376   6847    483    900    736       N  
ATOM   2661  CA  LYS A 364      30.124  10.967 -22.202  1.00 55.45           C  
ANISOU 2661  CA  LYS A 364     9150   5150   6770    396   1014    709       C  
ATOM   2662  C   LYS A 364      29.229  12.010 -21.539  1.00 51.41           C  
ANISOU 2662  C   LYS A 364     8686   4561   6285    478   1011    695       C  
ATOM   2663  O   LYS A 364      29.699  12.848 -20.770  1.00 52.23           O  
ANISOU 2663  O   LYS A 364     8818   4583   6443    396   1089    644       O  
ATOM   2664  CB  LYS A 364      30.712  11.556 -23.486  1.00 59.12           C  
ANISOU 2664  CB  LYS A 364     9725   5564   7173    384   1082    757       C  
ATOM   2665  CG  LYS A 364      31.553  10.582 -24.273  1.00 68.01           C  
ANISOU 2665  CG  LYS A 364    10813   6763   8265    318   1089    772       C  
ATOM   2666  CD  LYS A 364      32.279  11.280 -25.417  1.00 77.89           C  
ANISOU 2666  CD  LYS A 364    12179   7950   9465    286   1182    808       C  
ATOM   2667  CE  LYS A 364      32.625  10.292 -26.523  1.00 78.81           C  
ANISOU 2667  CE  LYS A 364    12279   8148   9515    293   1157    845       C  
ATOM   2668  NZ  LYS A 364      33.051   8.978 -25.960  1.00 76.90           N1+
ANISOU 2668  NZ  LYS A 364    11897   8009   9313    219   1117    805       N1+
ATOM   2669  N   ALA A 365      27.938  11.959 -21.846  1.00 46.31           N  
ANISOU 2669  N   ALA A 365     8045   3947   5604    640    920    733       N  
ATOM   2670  CA  ALA A 365      26.993  12.920 -21.296  1.00 45.44           C  
ANISOU 2670  CA  ALA A 365     7976   3772   5517    737    911    721       C  
ATOM   2671  C   ALA A 365      26.433  12.487 -19.942  1.00 50.30           C  
ANISOU 2671  C   ALA A 365     8486   4425   6199    747    868    660       C  
ATOM   2672  O   ALA A 365      26.002  13.327 -19.148  1.00 51.09           O  
ANISOU 2672  O   ALA A 365     8612   4460   6341    776    894    623       O  
ATOM   2673  CB  ALA A 365      25.858  13.160 -22.283  1.00 47.00           C  
ANISOU 2673  CB  ALA A 365     8223   3987   5648    911    834    784       C  
ATOM   2674  N   THR A 366      26.441  11.183 -19.676  1.00 50.36           N  
ANISOU 2674  N   THR A 366     8381   4538   6215    726    808    648       N  
ATOM   2675  CA  THR A 366      25.733  10.656 -18.507  1.00 57.47           C  
ANISOU 2675  CA  THR A 366     9183   5486   7166    762    759    599       C  
ATOM   2676  C   THR A 366      26.618  10.080 -17.407  1.00 59.55           C  
ANISOU 2676  C   THR A 366     9334   5811   7483    599    786    518       C  
ATOM   2677  O   THR A 366      26.258  10.125 -16.231  1.00 63.51           O  
ANISOU 2677  O   THR A 366     9754   6348   8028    586    774    448       O  
ATOM   2678  CB  THR A 366      24.690   9.587 -18.909  1.00 52.76           C  
ANISOU 2678  CB  THR A 366     8484   5022   6539    882    634    626       C  
ATOM   2679  CG2 THR A 366      23.807  10.111 -20.024  1.00 52.44           C  
ANISOU 2679  CG2 THR A 366     8512   4972   6439   1032    583    686       C  
ATOM   2680  OG1 THR A 366      25.353   8.392 -19.341  1.00 51.73           O  
ANISOU 2680  OG1 THR A 366     8269   5001   6385    797    601    632       O  
ATOM   2681  N   ALA A 367      27.764   9.524 -17.782  1.00 58.60           N  
ANISOU 2681  N   ALA A 367     9193   5720   7352    476    815    521       N  
ATOM   2682  CA  ALA A 367      28.639   8.929 -16.785  1.00 60.11           C  
ANISOU 2682  CA  ALA A 367     9261   5992   7587    326    825    440       C  
ATOM   2683  C   ALA A 367      29.264  10.007 -15.909  1.00 58.05           C  
ANISOU 2683  C   ALA A 367     9059   5622   7377    231    921    375       C  
ATOM   2684  O   ALA A 367      29.429  11.165 -16.316  1.00 52.57           O  
ANISOU 2684  O   ALA A 367     8518   4772   6685    239   1006    401       O  
ATOM   2685  CB  ALA A 367      29.706   8.057 -17.430  1.00 58.58           C  
ANISOU 2685  CB  ALA A 367     9024   5861   7373    229    830    455       C  
ATOM   2686  N   ARG A 368      29.572   9.621 -14.680  1.00 50.67           N  
ANISOU 2686  N   ARG A 368     8004   4767   6480    144    905    289       N  
ATOM   2687  CA  ARG A 368      30.258  10.507 -13.768  1.00 48.23           C  
ANISOU 2687  CA  ARG A 368     7729   4377   6218     38    985    209       C  
ATOM   2688  C   ARG A 368      30.935   9.681 -12.693  1.00 46.61           C  
ANISOU 2688  C   ARG A 368     7372   4301   6035    -76    951    125       C  
ATOM   2689  O   ARG A 368      30.470   8.585 -12.356  1.00 40.89           O  
ANISOU 2689  O   ARG A 368     6526   3716   5294    -41    862    125       O  
ATOM   2690  CB  ARG A 368      29.298  11.542 -13.170  1.00 53.23           C  
ANISOU 2690  CB  ARG A 368     8435   4920   6871    128   1005    188       C  
ATOM   2691  CG  ARG A 368      27.865  11.077 -12.994  1.00 51.53           C  
ANISOU 2691  CG  ARG A 368     8155   4788   6637    279    914    210       C  
ATOM   2692  CD  ARG A 368      26.912  12.195 -13.381  1.00 59.24           C  
ANISOU 2692  CD  ARG A 368     9265   5632   7611    420    940    250       C  
ATOM   2693  NE  ARG A 368      27.319  12.840 -14.627  1.00 71.17           N  
ANISOU 2693  NE  ARG A 368    10933   7011   9096    436    999    329       N  
ATOM   2694  CZ  ARG A 368      26.596  13.745 -15.288  1.00 75.44           C  
ANISOU 2694  CZ  ARG A 368    11579   7471   9614    561   1004    382       C  
ATOM   2695  NH1 ARG A 368      25.409  14.124 -14.829  1.00 78.81           N1+
ANISOU 2695  NH1 ARG A 368    12002   7890  10052    693    967    369       N1+
ATOM   2696  NH2 ARG A 368      27.061  14.273 -16.413  1.00 71.76           N  
ANISOU 2696  NH2 ARG A 368    11201   6959   9107    549   1038    442       N  
ATOM   2697  N   SER A 369      32.048  10.201 -12.180  1.00 45.93           N  
ANISOU 2697  N   SER A 369     7297   4168   5986   -214   1020     53       N  
ATOM   2698  CA  SER A 369      32.798   9.537 -11.122  1.00 24.90           C  
ANISOU 2698  CA  SER A 369     4500   1620   3340   -323    988    -34       C  
ATOM   2699  C   SER A 369      31.862   9.184  -9.967  1.00 24.38           C  
ANISOU 2699  C   SER A 369     4355   1642   3265   -260    919    -74       C  
ATOM   2700  O   SER A 369      30.795   9.784  -9.819  1.00 24.81           O  
ANISOU 2700  O   SER A 369     4468   1639   3318   -158    922    -60       O  
ATOM   2701  CB  SER A 369      33.940  10.439 -10.631  1.00 32.04           C  
ANISOU 2701  CB  SER A 369     5442   2443   4290   -467   1076   -121       C  
ATOM   2702  OG  SER A 369      33.457  11.596  -9.941  1.00 27.96           O  
ANISOU 2702  OG  SER A 369     5010   1817   3797   -448   1124   -170       O  
ATOM   2703  N   ALA A 370      32.249   8.192  -9.172  1.00 23.53           N  
ANISOU 2703  N   ALA A 370     4116   1673   3150   -315    858   -120       N  
ATOM   2704  CA  ALA A 370      31.521   7.873  -7.946  1.00 23.17           C  
ANISOU 2704  CA  ALA A 370     4000   1711   3092   -278    806   -167       C  
ATOM   2705  C   ALA A 370      31.228   9.102  -7.051  1.00 24.17           C  
ANISOU 2705  C   ALA A 370     4197   1746   3239   -281    862   -240       C  
ATOM   2706  O   ALA A 370      30.084   9.296  -6.643  1.00 24.26           O  
ANISOU 2706  O   ALA A 370     4219   1758   3242   -182    848   -235       O  
ATOM   2707  CB  ALA A 370      32.216   6.751  -7.172  1.00 22.36           C  
ANISOU 2707  CB  ALA A 370     3768   1754   2975   -353    745   -211       C  
ATOM   2708  N   PRO A 371      32.241   9.950  -6.778  1.00 25.01           N  
ANISOU 2708  N   PRO A 371     4353   1773   3377   -393    929   -311       N  
ATOM   2709  CA  PRO A 371      31.949  11.120  -5.941  1.00 28.47           C  
ANISOU 2709  CA  PRO A 371     4865   2118   3836   -396    984   -387       C  
ATOM   2710  C   PRO A 371      30.960  12.078  -6.605  1.00 32.47           C  
ANISOU 2710  C   PRO A 371     5501   2482   4354   -280   1033   -329       C  
ATOM   2711  O   PRO A 371      30.109  12.661  -5.919  1.00 29.60           O  
ANISOU 2711  O   PRO A 371     5171   2083   3993   -211   1044   -365       O  
ATOM   2712  CB  PRO A 371      33.318  11.808  -5.799  1.00 32.93           C  
ANISOU 2712  CB  PRO A 371     5460   2613   4439   -549   1051   -467       C  
ATOM   2713  CG  PRO A 371      34.320  10.732  -6.042  1.00 29.16           C  
ANISOU 2713  CG  PRO A 371     4872   2255   3953   -630   1004   -462       C  
ATOM   2714  CD  PRO A 371      33.684   9.842  -7.077  1.00 28.25           C  
ANISOU 2714  CD  PRO A 371     4738   2186   3808   -528    957   -342       C  
ATOM   2715  N   ASP A 372      31.069  12.244  -7.921  1.00 28.63           N  
ANISOU 2715  N   ASP A 372     5092   1916   3871   -253   1062   -242       N  
ATOM   2716  CA  ASP A 372      30.141  13.111  -8.627  1.00 27.80           C  
ANISOU 2716  CA  ASP A 372     5117   1678   3768   -128   1100   -178       C  
ATOM   2717  C   ASP A 372      28.718  12.546  -8.541  1.00 27.21           C  
ANISOU 2717  C   ASP A 372     4985   1689   3665     27   1021   -134       C  
ATOM   2718  O   ASP A 372      27.765  13.282  -8.272  1.00 27.92           O  
ANISOU 2718  O   ASP A 372     5134   1712   3764    130   1037   -141       O  
ATOM   2719  CB  ASP A 372      30.572  13.324 -10.084  1.00 31.44           C  
ANISOU 2719  CB  ASP A 372     5677   2047   4224   -127   1143    -87       C  
ATOM   2720  CG  ASP A 372      31.856  14.150 -10.210  1.00 41.63           C  
ANISOU 2720  CG  ASP A 372     7049   3218   5553   -277   1248   -132       C  
ATOM   2721  OD1 ASP A 372      32.167  14.941  -9.296  1.00 44.40           O  
ANISOU 2721  OD1 ASP A 372     7426   3503   5940   -349   1298   -227       O  
ATOM   2722  OD2 ASP A 372      32.556  14.016 -11.237  1.00 48.89           O1-
ANISOU 2722  OD2 ASP A 372     8005   4106   6466   -325   1283    -76       O1-
ATOM   2723  N   ARG A 373      28.577  11.241  -8.745  1.00 26.00           N  
ANISOU 2723  N   ARG A 373     4712   1684   3482     42    939    -94       N  
ATOM   2724  CA  ARG A 373      27.254  10.628  -8.705  1.00 28.32           C  
ANISOU 2724  CA  ARG A 373     4938   2065   3755    175    867    -57       C  
ATOM   2725  C   ARG A 373      26.681  10.732  -7.292  1.00 34.39           C  
ANISOU 2725  C   ARG A 373     5649   2886   4531    185    862   -140       C  
ATOM   2726  O   ARG A 373      25.511  11.097  -7.096  1.00 29.52           O  
ANISOU 2726  O   ARG A 373     5044   2254   3918    304    857   -138       O  
ATOM   2727  CB  ARG A 373      27.299   9.169  -9.152  1.00 24.24           C  
ANISOU 2727  CB  ARG A 373     4306   1694   3212    171    786     -8       C  
ATOM   2728  CG  ARG A 373      25.956   8.465  -8.954  1.00 40.28           C  
ANISOU 2728  CG  ARG A 373     6249   3827   5230    286    715     13       C  
ATOM   2729  CD  ARG A 373      25.967   7.036  -9.454  1.00 36.25           C  
ANISOU 2729  CD  ARG A 373     5635   3444   4696    280    638     60       C  
ATOM   2730  NE  ARG A 373      26.213   6.980 -10.886  1.00 42.66           N  
ANISOU 2730  NE  ARG A 373     6507   4211   5492    309    631    137       N  
ATOM   2731  CZ  ARG A 373      25.263   6.883 -11.805  1.00 41.22           C  
ANISOU 2731  CZ  ARG A 373     6341   4028   5294    432    589    200       C  
ATOM   2732  NH1 ARG A 373      23.995   6.814 -11.438  1.00 41.71           N1+
ANISOU 2732  NH1 ARG A 373     6350   4135   5363    536    550    191       N1+
ATOM   2733  NH2 ARG A 373      25.586   6.857 -13.091  1.00 40.14           N  
ANISOU 2733  NH2 ARG A 373     6271   3850   5131    453    586    267       N  
ATOM   2734  N   GLN A 374      27.542  10.438  -6.323  1.00 30.59           N  
ANISOU 2734  N   GLN A 374     5108   2466   4048     62    865   -216       N  
ATOM   2735  CA  GLN A 374      27.218  10.526  -4.912  1.00 26.80           C  
ANISOU 2735  CA  GLN A 374     4582   2039   3562     50    866   -302       C  
ATOM   2736  C   GLN A 374      26.642  11.903  -4.561  1.00 33.06           C  
ANISOU 2736  C   GLN A 374     5482   2699   4380    110    934   -347       C  
ATOM   2737  O   GLN A 374      25.659  12.009  -3.821  1.00 31.92           O  
ANISOU 2737  O   GLN A 374     5311   2588   4230    188    929   -380       O  
ATOM   2738  CB  GLN A 374      28.473  10.209  -4.083  1.00 26.88           C  
ANISOU 2738  CB  GLN A 374     4541   2110   3563    -99    864   -379       C  
ATOM   2739  CG  GLN A 374      28.295  10.252  -2.578  1.00 33.08           C  
ANISOU 2739  CG  GLN A 374     5282   2959   4326   -124    861   -474       C  
ATOM   2740  CD  GLN A 374      29.607  10.028  -1.815  1.00 31.29           C  
ANISOU 2740  CD  GLN A 374     5013   2789   4087   -266    851   -554       C  
ATOM   2741  NE2 GLN A 374      29.558  10.223  -0.514  1.00 30.69           N  
ANISOU 2741  NE2 GLN A 374     4920   2756   3985   -292    854   -645       N  
ATOM   2742  OE1 GLN A 374      30.644   9.697  -2.395  1.00 36.29           O  
ANISOU 2742  OE1 GLN A 374     5627   3429   4731   -346    841   -538       O  
ATOM   2743  N   GLU A 375      27.226  12.963  -5.108  1.00 30.91           N  
ANISOU 2743  N   GLU A 375     5335   2272   4138     76   1003   -349       N  
ATOM   2744  CA  GLU A 375      26.706  14.294  -4.825  1.00 28.91           C  
ANISOU 2744  CA  GLU A 375     5197   1875   3912    136   1071   -390       C  
ATOM   2745  C   GLU A 375      25.351  14.519  -5.499  1.00 40.28           C  
ANISOU 2745  C   GLU A 375     6675   3278   5354    317   1054   -315       C  
ATOM   2746  O   GLU A 375      24.456  15.137  -4.920  1.00 29.97           O  
ANISOU 2746  O   GLU A 375     5393   1935   4059    408   1075   -355       O  
ATOM   2747  CB  GLU A 375      27.702  15.374  -5.245  1.00 47.44           C  
ANISOU 2747  CB  GLU A 375     7678   4053   6294     45   1157   -411       C  
ATOM   2748  CG  GLU A 375      28.773  15.658  -4.207  1.00 61.09           C  
ANISOU 2748  CG  GLU A 375     9389   5785   8036   -113   1192   -531       C  
ATOM   2749  CD  GLU A 375      28.195  16.186  -2.897  1.00 69.06           C  
ANISOU 2749  CD  GLU A 375    10399   6796   9045    -86   1207   -633       C  
ATOM   2750  OE1 GLU A 375      27.744  17.351  -2.873  1.00 69.71           O  
ANISOU 2750  OE1 GLU A 375    10601   6727   9156    -29   1274   -657       O  
ATOM   2751  OE2 GLU A 375      28.186  15.432  -1.897  1.00 69.51           O1-
ANISOU 2751  OE2 GLU A 375    10341   7001   9066   -119   1156   -688       O1-
ATOM   2752  N   GLU A 376      25.204  14.007  -6.719  1.00 28.76           N  
ANISOU 2752  N   GLU A 376     5215   1833   3881    372   1014   -212       N  
ATOM   2753  CA  GLU A 376      23.960  14.159  -7.469  1.00 34.87           C  
ANISOU 2753  CA  GLU A 376     6016   2582   4650    548    984   -140       C  
ATOM   2754  C   GLU A 376      22.795  13.473  -6.768  1.00 28.65           C  
ANISOU 2754  C   GLU A 376     5097   1935   3855    635    925   -163       C  
ATOM   2755  O   GLU A 376      21.715  14.040  -6.688  1.00 29.45           O  
ANISOU 2755  O   GLU A 376     5221   1999   3970    770    929   -167       O  
ATOM   2756  CB  GLU A 376      24.102  13.653  -8.919  1.00 28.73           C  
ANISOU 2756  CB  GLU A 376     5259   1808   3848    582    944    -30       C  
ATOM   2757  CG  GLU A 376      24.786  14.630  -9.865  1.00 41.90           C  
ANISOU 2757  CG  GLU A 376     7099   3301   5522    564   1017     17       C  
ATOM   2758  CD  GLU A 376      24.853  14.122 -11.316  1.00 49.15           C  
ANISOU 2758  CD  GLU A 376     8044   4228   6401    609    978    127       C  
ATOM   2759  OE1 GLU A 376      24.285  13.053 -11.605  1.00 52.11           O  
ANISOU 2759  OE1 GLU A 376     8305   4743   6751    666    890    162       O  
ATOM   2760  OE2 GLU A 376      25.470  14.794 -12.173  1.00 54.64           O1-
ANISOU 2760  OE2 GLU A 376     8881   4790   7092    587   1040    177       O1-
ATOM   2761  N   ILE A 377      23.020  12.259  -6.270  1.00 27.45           N  
ANISOU 2761  N   ILE A 377     4808   1942   3682    559    873   -178       N  
ATOM   2762  CA  ILE A 377      22.001  11.547  -5.485  1.00 36.32           C  
ANISOU 2762  CA  ILE A 377     5803   3200   4797    616    831   -206       C  
ATOM   2763  C   ILE A 377      21.570  12.357  -4.279  1.00 27.91           C  
ANISOU 2763  C   ILE A 377     4758   2100   3745    635    887   -299       C  
ATOM   2764  O   ILE A 377      20.378  12.544  -4.028  1.00 28.41           O  
ANISOU 2764  O   ILE A 377     4790   2185   3821    756    884   -311       O  
ATOM   2765  CB  ILE A 377      22.499  10.219  -4.898  1.00 31.62           C  
ANISOU 2765  CB  ILE A 377     5080   2760   4173    507    786   -220       C  
ATOM   2766  CG1 ILE A 377      23.078   9.306  -5.969  1.00 35.20           C  
ANISOU 2766  CG1 ILE A 377     5505   3257   4613    469    733   -142       C  
ATOM   2767  CG2 ILE A 377      21.357   9.520  -4.164  1.00 32.06           C  
ANISOU 2767  CG2 ILE A 377     5017   2943   4222    569    755   -240       C  
ATOM   2768  CD1 ILE A 377      22.076   8.840  -6.937  1.00 43.64           C  
ANISOU 2768  CD1 ILE A 377     6537   4364   5682    590    676    -70       C  
ATOM   2769  N   SER A 378      22.556  12.823  -3.526  1.00 39.10           N  
ANISOU 2769  N   SER A 378     6224   3472   5160    515    936   -371       N  
ATOM   2770  CA  SER A 378      22.279  13.567  -2.304  1.00 38.33           C  
ANISOU 2770  CA  SER A 378     6150   3345   5067    516    990   -471       C  
ATOM   2771  C   SER A 378      21.521  14.854  -2.620  1.00 39.10           C  
ANISOU 2771  C   SER A 378     6361   3292   5202    645   1042   -475       C  
ATOM   2772  O   SER A 378      20.542  15.178  -1.953  1.00 39.49           O  
ANISOU 2772  O   SER A 378     6389   3356   5259    737   1060   -522       O  
ATOM   2773  CB  SER A 378      23.569  13.862  -1.538  1.00 37.26           C  
ANISOU 2773  CB  SER A 378     6051   3184   4924    358   1027   -553       C  
ATOM   2774  OG  SER A 378      23.281  14.631  -0.383  1.00 57.02           O  
ANISOU 2774  OG  SER A 378     8586   5654   7426    364   1079   -657       O  
ATOM   2775  N   ARG A 379      21.956  15.567  -3.656  1.00 37.38           N  
ANISOU 2775  N   ARG A 379     6267   2930   5006    657   1068   -421       N  
ATOM   2776  CA  ARG A 379      21.277  16.795  -4.058  1.00 44.35           C  
ANISOU 2776  CA  ARG A 379     7276   3653   5921    789   1115   -412       C  
ATOM   2777  C   ARG A 379      19.853  16.514  -4.522  1.00 38.70           C  
ANISOU 2777  C   ARG A 379     6499   2997   5207    972   1061   -357       C  
ATOM   2778  O   ARG A 379      18.922  17.247  -4.197  1.00 39.48           O  
ANISOU 2778  O   ARG A 379     6628   3044   5329   1097   1088   -392       O  
ATOM   2779  CB  ARG A 379      22.051  17.509  -5.170  1.00 51.02           C  
ANISOU 2779  CB  ARG A 379     8274   4333   6780    763   1154   -349       C  
ATOM   2780  CG  ARG A 379      23.247  18.308  -4.679  1.00 59.78           C  
ANISOU 2780  CG  ARG A 379     9480   5323   7909    611   1236   -425       C  
ATOM   2781  CD  ARG A 379      23.867  19.137  -5.794  1.00 67.24           C  
ANISOU 2781  CD  ARG A 379    10562   6119   8867    588   1277   -354       C  
ATOM   2782  NE  ARG A 379      22.861  19.768  -6.648  1.00 68.85           N  
ANISOU 2782  NE  ARG A 379    10823   6272   9067    757   1253   -270       N  
ATOM   2783  CZ  ARG A 379      22.653  19.448  -7.923  1.00 64.12           C  
ANISOU 2783  CZ  ARG A 379    10239   5684   8441    830   1207   -155       C  
ATOM   2784  NH1 ARG A 379      23.385  18.500  -8.506  1.00 55.99           N1+
ANISOU 2784  NH1 ARG A 379     9174   4710   7389    748   1185   -109       N1+
ATOM   2785  NH2 ARG A 379      21.714  20.079  -8.617  1.00 62.50           N  
ANISOU 2785  NH2 ARG A 379    10082   5438   8228    985   1180    -91       N  
ATOM   2786  N   LEU A 380      19.699  15.456  -5.303  1.00 31.38           N  
ANISOU 2786  N   LEU A 380     5484   2180   4259    988    985   -277       N  
ATOM   2787  CA  LEU A 380      18.392  15.019  -5.757  1.00 38.58           C  
ANISOU 2787  CA  LEU A 380     6310   3174   5173   1145    921   -233       C  
ATOM   2788  C   LEU A 380      17.496  14.750  -4.549  1.00 37.91           C  
ANISOU 2788  C   LEU A 380     6106   3201   5097   1179    926   -314       C  
ATOM   2789  O   LEU A 380      16.352  15.211  -4.467  1.00 32.40           O  
ANISOU 2789  O   LEU A 380     5392   2494   4424   1327    929   -331       O  
ATOM   2790  CB  LEU A 380      18.561  13.751  -6.581  1.00 33.63           C  
ANISOU 2790  CB  LEU A 380     5591   2668   4519   1113    840   -156       C  
ATOM   2791  CG  LEU A 380      17.305  13.031  -7.038  1.00 34.85           C  
ANISOU 2791  CG  LEU A 380     5626   2940   4675   1244    761   -119       C  
ATOM   2792  CD1 LEU A 380      16.479  13.961  -7.886  1.00 35.94           C  
ANISOU 2792  CD1 LEU A 380     5853   2973   4828   1426    752    -77       C  
ATOM   2793  CD2 LEU A 380      17.689  11.767  -7.798  1.00 28.74           C  
ANISOU 2793  CD2 LEU A 380     4774   2273   3873   1182    689    -54       C  
ATOM   2794  N   MET A 381      18.054  14.016  -3.600  1.00 32.76           N  
ANISOU 2794  N   MET A 381     5371   2653   4422   1041    931   -365       N  
ATOM   2795  CA  MET A 381      17.362  13.666  -2.377  1.00 37.24           C  
ANISOU 2795  CA  MET A 381     5831   3333   4984   1047    946   -440       C  
ATOM   2796  C   MET A 381      16.928  14.890  -1.583  1.00 44.68           C  
ANISOU 2796  C   MET A 381     6850   4178   5949   1111   1022   -525       C  
ATOM   2797  O   MET A 381      15.762  15.022  -1.216  1.00 48.56           O  
ANISOU 2797  O   MET A 381     7281   4711   6458   1229   1031   -557       O  
ATOM   2798  CB  MET A 381      18.260  12.794  -1.517  1.00 40.01           C  
ANISOU 2798  CB  MET A 381     6119   3787   5295    880    943   -475       C  
ATOM   2799  CG  MET A 381      17.472  11.904  -0.634  1.00 50.96           C  
ANISOU 2799  CG  MET A 381     7368   5332   6664    887    931   -507       C  
ATOM   2800  SD  MET A 381      16.302  10.997  -1.650  1.00 56.58           S  
ANISOU 2800  SD  MET A 381     7959   6141   7399   1003    857   -424       S  
ATOM   2801  CE  MET A 381      15.179  10.503  -0.355  1.00 29.08           C  
ANISOU 2801  CE  MET A 381     4343   2796   3911   1030    890   -495       C  
ATOM   2802  N   LYS A 382      17.869  15.786  -1.319  1.00 47.45           N  
ANISOU 2802  N   LYS A 382     7330   4397   6301   1032   1080   -569       N  
ATOM   2803  CA  LYS A 382      17.560  17.016  -0.604  1.00 51.77           C  
ANISOU 2803  CA  LYS A 382     7968   4831   6872   1086   1157   -656       C  
ATOM   2804  C   LYS A 382      16.496  17.843  -1.331  1.00 50.49           C  
ANISOU 2804  C   LYS A 382     7865   4568   6752   1281   1162   -621       C  
ATOM   2805  O   LYS A 382      15.649  18.475  -0.700  1.00 51.51           O  
ANISOU 2805  O   LYS A 382     7997   4673   6902   1383   1204   -687       O  
ATOM   2806  CB  LYS A 382      18.833  17.836  -0.392  1.00 60.20           C  
ANISOU 2806  CB  LYS A 382     9172   5760   7941    958   1214   -703       C  
ATOM   2807  CG  LYS A 382      19.931  17.093   0.379  1.00 64.28           C  
ANISOU 2807  CG  LYS A 382     9630   6378   8416    772   1203   -749       C  
ATOM   2808  CD  LYS A 382      19.552  16.853   1.839  1.00 66.03           C  
ANISOU 2808  CD  LYS A 382     9775   6710   8603    750   1223   -850       C  
ATOM   2809  CE  LYS A 382      20.661  16.112   2.593  1.00 63.74           C  
ANISOU 2809  CE  LYS A 382     9433   6522   8262    577   1202   -892       C  
ATOM   2810  NZ  LYS A 382      20.398  16.016   4.061  1.00 57.48           N1+
ANISOU 2810  NZ  LYS A 382     8596   5821   7423    552   1230   -995       N1+
ATOM   2811  N   ASN A 383      16.521  17.804  -2.658  1.00 49.31           N  
ANISOU 2811  N   ASN A 383     7759   4367   6610   1340   1116   -517       N  
ATOM   2812  CA  ASN A 383      15.608  18.606  -3.465  1.00 57.67           C  
ANISOU 2812  CA  ASN A 383     8890   5321   7700   1533   1110   -473       C  
ATOM   2813  C   ASN A 383      14.244  17.985  -3.783  1.00 62.85           C  
ANISOU 2813  C   ASN A 383     9404   6110   8365   1689   1041   -444       C  
ATOM   2814  O   ASN A 383      13.354  18.676  -4.278  1.00 68.69           O  
ANISOU 2814  O   ASN A 383    10168   6800   9130   1848   1020   -422       O  
ATOM   2815  CB  ASN A 383      16.296  19.038  -4.763  1.00 64.32           C  
ANISOU 2815  CB  ASN A 383     9861   6043   8536   1520   1091   -373       C  
ATOM   2816  CG  ASN A 383      17.424  20.022  -4.522  1.00 65.42           C  
ANISOU 2816  CG  ASN A 383    10135   6043   8680   1384   1160   -405       C  
ATOM   2817  ND2 ASN A 383      17.660  20.893  -5.493  1.00 66.47           N  
ANISOU 2817  ND2 ASN A 383    10380   6061   8814   1404   1156   -333       N  
ATOM   2818  OD1 ASN A 383      18.068  20.009  -3.469  1.00 63.66           O  
ANISOU 2818  OD1 ASN A 383     9912   5819   8456   1261   1216   -498       O  
ATOM   2819  N   ALA A 384      14.074  16.691  -3.522  1.00 59.12           N  
ANISOU 2819  N   ALA A 384     8765   5825   7873   1624    990   -440       N  
ATOM   2820  CA  ALA A 384      12.760  16.066  -3.690  1.00 47.56           C  
ANISOU 2820  CA  ALA A 384     7147   4497   6426   1752    932   -431       C  
ATOM   2821  C   ALA A 384      11.837  16.365  -2.497  1.00 45.71           C  
ANISOU 2821  C   ALA A 384     6838   4314   6217   1814    988   -534       C  
ATOM   2822  O   ALA A 384      10.616  16.383  -2.638  1.00 42.10           O  
ANISOU 2822  O   ALA A 384     6291   3914   5792   1966    964   -544       O  
ATOM   2823  CB  ALA A 384      12.892  14.563  -3.914  1.00 36.02           C  
ANISOU 2823  CB  ALA A 384     5542   3206   4939   1657    863   -388       C  
ATOM   2824  N   SER A 385      12.431  16.614  -1.334  1.00 48.29           N  
ANISOU 2824  N   SER A 385     7199   4622   6525   1698   1062   -614       N  
ATOM   2825  CA  SER A 385      11.673  16.887  -0.114  1.00 52.37           C  
ANISOU 2825  CA  SER A 385     7656   5189   7053   1739   1127   -718       C  
ATOM   2826  C   SER A 385      10.557  15.876   0.148  1.00 49.05           C  
ANISOU 2826  C   SER A 385     7037   4959   6642   1787   1097   -727       C  
ATOM   2827  O   SER A 385       9.402  16.270   0.287  1.00 52.38           O  
ANISOU 2827  O   SER A 385     7399   5399   7103   1936   1113   -768       O  
ATOM   2828  CB  SER A 385      11.066  18.294  -0.163  1.00 61.49           C  
ANISOU 2828  CB  SER A 385     8918   6192   8252   1902   1175   -758       C  
ATOM   2829  OG  SER A 385      12.053  19.298  -0.032  1.00 66.24           O  
ANISOU 2829  OG  SER A 385     9701   6618   8848   1835   1231   -782       O  
ATOM   2830  N   TYR A 386      10.891  14.589   0.215  1.00 45.62           N  
ANISOU 2830  N   TYR A 386     6498   4660   6175   1662   1056   -693       N  
ATOM   2831  CA  TYR A 386       9.864  13.557   0.363  1.00 41.88           C  
ANISOU 2831  CA  TYR A 386     5837   4361   5715   1693   1030   -695       C  
ATOM   2832  C   TYR A 386       8.944  13.776   1.563  1.00 45.77           C  
ANISOU 2832  C   TYR A 386     6252   4920   6219   1741   1110   -796       C  
ATOM   2833  O   TYR A 386       7.746  13.486   1.495  1.00 45.60           O  
ANISOU 2833  O   TYR A 386     6095   4993   6237   1844   1102   -812       O  
ATOM   2834  CB  TYR A 386      10.482  12.162   0.412  1.00 37.77           C  
ANISOU 2834  CB  TYR A 386     5239   3960   5153   1535    990   -650       C  
ATOM   2835  CG  TYR A 386      10.842  11.639  -0.952  1.00 38.40           C  
ANISOU 2835  CG  TYR A 386     5323   4031   5236   1534    896   -550       C  
ATOM   2836  CD1 TYR A 386       9.877  11.097  -1.789  1.00 39.23           C  
ANISOU 2836  CD1 TYR A 386     5312   4215   5376   1633    828   -511       C  
ATOM   2837  CD2 TYR A 386      12.148  11.705  -1.413  1.00 38.31           C  
ANISOU 2837  CD2 TYR A 386     5429   3933   5192   1433    877   -500       C  
ATOM   2838  CE1 TYR A 386      10.210  10.635  -3.055  1.00 43.97           C  
ANISOU 2838  CE1 TYR A 386     5926   4809   5972   1636    741   -424       C  
ATOM   2839  CE2 TYR A 386      12.493  11.249  -2.664  1.00 37.90           C  
ANISOU 2839  CE2 TYR A 386     5389   3874   5139   1434    799   -412       C  
ATOM   2840  CZ  TYR A 386      11.528  10.716  -3.484  1.00 45.10           C  
ANISOU 2840  CZ  TYR A 386     6196   4864   6078   1536    731   -373       C  
ATOM   2841  OH  TYR A 386      11.894  10.258  -4.731  1.00 42.90           O  
ANISOU 2841  OH  TYR A 386     5935   4578   5788   1536    652   -289       O  
ATOM   2842  N   ASN A 387       9.493  14.317   2.647  1.00 47.77           N  
ANISOU 2842  N   ASN A 387     6590   5124   6438   1667   1189   -869       N  
ATOM   2843  CA  ASN A 387       8.710  14.522   3.861  1.00 52.67           C  
ANISOU 2843  CA  ASN A 387     7149   5808   7056   1701   1275   -969       C  
ATOM   2844  C   ASN A 387       7.733  15.689   3.767  1.00 55.19           C  
ANISOU 2844  C   ASN A 387     7490   6044   7434   1891   1312  -1023       C  
ATOM   2845  O   ASN A 387       7.021  15.982   4.730  1.00 57.99           O  
ANISOU 2845  O   ASN A 387     7798   6443   7794   1938   1391  -1113       O  
ATOM   2846  CB  ASN A 387       9.622  14.674   5.086  1.00 53.88           C  
ANISOU 2846  CB  ASN A 387     7385   5946   7141   1560   1343  -1036       C  
ATOM   2847  CG  ASN A 387      10.388  13.399   5.404  1.00 54.21           C  
ANISOU 2847  CG  ASN A 387     7375   6101   7119   1389   1312   -995       C  
ATOM   2848  ND2 ASN A 387      11.679  13.535   5.689  1.00 53.90           N  
ANISOU 2848  ND2 ASN A 387     7446   6003   7030   1262   1309  -1000       N  
ATOM   2849  OD1 ASN A 387       9.826  12.305   5.382  1.00 55.18           O  
ANISOU 2849  OD1 ASN A 387     7362   6361   7242   1372   1291   -961       O  
ATOM   2850  N   LEU A 388       7.695  16.346   2.609  1.00 52.19           N  
ANISOU 2850  N   LEU A 388     7187   5546   7096   2005   1258   -966       N  
ATOM   2851  CA  LEU A 388       6.767  17.453   2.392  1.00 53.58           C  
ANISOU 2851  CA  LEU A 388     7392   5635   7329   2206   1280  -1005       C  
ATOM   2852  C   LEU A 388       5.735  17.087   1.341  1.00 50.39           C  
ANISOU 2852  C   LEU A 388     6866   5302   6977   2354   1196   -950       C  
ATOM   2853  O   LEU A 388       4.802  17.839   1.087  1.00 52.40           O  
ANISOU 2853  O   LEU A 388     7086   5537   7287   2483   1169   -971       O  
ATOM   2854  CB  LEU A 388       7.514  18.726   1.993  1.00 56.41           C  
ANISOU 2854  CB  LEU A 388     7953   5788   7694   2215   1280   -990       C  
ATOM   2855  CG  LEU A 388       8.353  19.351   3.106  1.00 56.14           C  
ANISOU 2855  CG  LEU A 388     8037   5672   7622   2098   1368  -1074       C  
ATOM   2856  CD1 LEU A 388       9.161  20.525   2.580  1.00 52.01           C  
ANISOU 2856  CD1 LEU A 388     7697   4956   7109   2076   1353  -1046       C  
ATOM   2857  CD2 LEU A 388       7.459  19.781   4.268  1.00 59.95           C  
ANISOU 2857  CD2 LEU A 388     8450   6212   8117   2151   1437  -1189       C  
ATOM   2858  N   ASP A 389       5.931  15.929   0.724  1.00 50.87           N  
ANISOU 2858  N   ASP A 389     6837   5469   7022   2272   1119   -875       N  
ATOM   2859  CA  ASP A 389       4.952  15.350  -0.181  1.00 47.91           C  
ANISOU 2859  CA  ASP A 389     6317   5196   6690   2385   1034   -834       C  
ATOM   2860  C   ASP A 389       3.675  15.125   0.625  1.00 49.30           C  
ANISOU 2860  C   ASP A 389     6314   5509   6908   2455   1085   -925       C  
ATOM   2861  O   ASP A 389       3.657  14.324   1.563  1.00 52.19           O  
ANISOU 2861  O   ASP A 389     6584   5994   7250   2328   1140   -965       O  
ATOM   2862  CB  ASP A 389       5.500  14.029  -0.728  1.00 44.63           C  
ANISOU 2862  CB  ASP A 389     5836   4879   6243   2245    960   -755       C  
ATOM   2863  CG  ASP A 389       4.567  13.352  -1.724  1.00 45.95           C  
ANISOU 2863  CG  ASP A 389     5853   5154   6450   2344    863   -716       C  
ATOM   2864  OD1 ASP A 389       3.347  13.618  -1.725  1.00 48.04           O  
ANISOU 2864  OD1 ASP A 389     6006   5476   6770   2497    860   -767       O  
ATOM   2865  OD2 ASP A 389       5.066  12.521  -2.507  1.00 37.34           O1-
ANISOU 2865  OD2 ASP A 389     4751   4099   5336   2266    787   -640       O1-
ATOM   2866  N   PRO A 390       2.597  15.829   0.259  1.00 44.33           N  
ANISOU 2866  N   PRO A 390     5629   4872   6344   2611   1053   -950       N  
ATOM   2867  CA  PRO A 390       1.358  15.761   1.038  1.00 49.73           C  
ANISOU 2867  CA  PRO A 390     6140   5675   7080   2663   1107  -1042       C  
ATOM   2868  C   PRO A 390       0.714  14.374   0.982  1.00 52.16           C  
ANISOU 2868  C   PRO A 390     6236   6180   7405   2629   1085  -1042       C  
ATOM   2869  O   PRO A 390      -0.096  14.046   1.847  1.00 57.60           O  
ANISOU 2869  O   PRO A 390     6780   6985   8120   2617   1159  -1120       O  
ATOM   2870  CB  PRO A 390       0.465  16.810   0.369  1.00 45.62           C  
ANISOU 2870  CB  PRO A 390     5617   5087   6630   2818   1048  -1040       C  
ATOM   2871  CG  PRO A 390       0.957  16.882  -1.028  1.00 47.83           C  
ANISOU 2871  CG  PRO A 390     5992   5289   6894   2850    932   -929       C  
ATOM   2872  CD  PRO A 390       2.442  16.633  -0.965  1.00 45.93           C  
ANISOU 2872  CD  PRO A 390     5910   4967   6576   2719    955   -882       C  
ATOM   2873  N   TYR A 391       1.075  13.577  -0.018  1.00 47.11           N  
ANISOU 2873  N   TYR A 391     5578   5573   6748   2604    990   -959       N  
ATOM   2874  CA  TYR A 391       0.596  12.202  -0.109  1.00 46.51           C  
ANISOU 2874  CA  TYR A 391     5309   5675   6688   2534    961   -955       C  
ATOM   2875  C   TYR A 391       1.327  11.310   0.875  1.00 44.38           C  
ANISOU 2875  C   TYR A 391     5041   5462   6361   2312   1033   -955       C  
ATOM   2876  O   TYR A 391       0.713  10.544   1.611  1.00 45.95           O  
ANISOU 2876  O   TYR A 391     5088   5796   6573   2246   1093  -1005       O  
ATOM   2877  CB  TYR A 391       0.736  11.674  -1.535  1.00 40.77           C  
ANISOU 2877  CB  TYR A 391     4569   4959   5964   2558    823   -865       C  
ATOM   2878  CG  TYR A 391      -0.162  12.428  -2.489  1.00 54.88           C  
ANISOU 2878  CG  TYR A 391     6332   6712   7809   2715    733   -849       C  
ATOM   2879  CD1 TYR A 391      -1.483  12.039  -2.681  1.00 58.03           C  
ANISOU 2879  CD1 TYR A 391     6527   7243   8278   2768    696   -887       C  
ATOM   2880  CD2 TYR A 391       0.295  13.552  -3.164  1.00 53.65           C  
ANISOU 2880  CD2 TYR A 391     6361   6389   7635   2791    690   -795       C  
ATOM   2881  CE1 TYR A 391      -2.319  12.736  -3.532  1.00 61.14           C  
ANISOU 2881  CE1 TYR A 391     6902   7611   8718   2905    613   -869       C  
ATOM   2882  CE2 TYR A 391      -0.533  14.254  -4.018  1.00 59.93           C  
ANISOU 2882  CE2 TYR A 391     7142   7156   8474   2926    609   -774       C  
ATOM   2883  CZ  TYR A 391      -1.840  13.841  -4.199  1.00 62.48           C  
ANISOU 2883  CZ  TYR A 391     7261   7618   8861   2988    567   -811       C  
ATOM   2884  OH  TYR A 391      -2.669  14.531  -5.052  1.00 64.05           O  
ANISOU 2884  OH  TYR A 391     7446   7795   9096   3128    484   -790       O  
ATOM   2885  N   ILE A 392       2.645  11.424   0.883  1.00 38.93           N  
ANISOU 2885  N   ILE A 392     4522   4665   5603   2199   1030   -900       N  
ATOM   2886  CA  ILE A 392       3.471  10.732   1.856  1.00 44.00           C  
ANISOU 2886  CA  ILE A 392     5193   5343   6180   2002   1093   -901       C  
ATOM   2887  C   ILE A 392       3.080  11.133   3.273  1.00 41.21           C  
ANISOU 2887  C   ILE A 392     4824   5017   5815   1994   1222  -1000       C  
ATOM   2888  O   ILE A 392       3.159  10.326   4.202  1.00 44.13           O  
ANISOU 2888  O   ILE A 392     5139   5484   6146   1863   1285  -1021       O  
ATOM   2889  CB  ILE A 392       4.956  11.009   1.586  1.00 43.47           C  
ANISOU 2889  CB  ILE A 392     5318   5146   6052   1907   1065   -838       C  
ATOM   2890  CG1 ILE A 392       5.388  10.255   0.338  1.00 43.25           C  
ANISOU 2890  CG1 ILE A 392     5282   5129   6023   1873    952   -740       C  
ATOM   2891  CG2 ILE A 392       5.824  10.589   2.749  1.00 44.49           C  
ANISOU 2891  CG2 ILE A 392     5498   5296   6110   1732   1136   -859       C  
ATOM   2892  CD1 ILE A 392       6.838  10.439   0.007  1.00 50.61           C  
ANISOU 2892  CD1 ILE A 392     6384   5946   6901   1774    927   -679       C  
ATOM   2893  N   GLN A 393       2.631  12.373   3.436  1.00 40.12           N  
ANISOU 2893  N   GLN A 393     4741   4795   5708   2141   1262  -1062       N  
ATOM   2894  CA  GLN A 393       2.188  12.832   4.741  1.00 48.28           C  
ANISOU 2894  CA  GLN A 393     5760   5852   6731   2151   1386  -1165       C  
ATOM   2895  C   GLN A 393       0.839  12.232   5.127  1.00 50.76           C  
ANISOU 2895  C   GLN A 393     5859   6331   7098   2196   1433  -1224       C  
ATOM   2896  O   GLN A 393       0.645  11.843   6.283  1.00 42.35           O  
ANISOU 2896  O   GLN A 393     4741   5351   5998   2109   1537  -1281       O  
ATOM   2897  CB  GLN A 393       2.147  14.360   4.810  1.00 53.39           C  
ANISOU 2897  CB  GLN A 393     6541   6347   7398   2294   1419  -1218       C  
ATOM   2898  CG  GLN A 393       3.523  14.995   4.933  1.00 56.02           C  
ANISOU 2898  CG  GLN A 393     7091   6524   7670   2207   1424  -1195       C  
ATOM   2899  CD  GLN A 393       3.454  16.444   5.366  1.00 62.03           C  
ANISOU 2899  CD  GLN A 393     7981   7143   8444   2318   1491  -1273       C  
ATOM   2900  NE2 GLN A 393       4.564  17.159   5.219  1.00 59.66           N  
ANISOU 2900  NE2 GLN A 393     7873   6683   8112   2269   1484  -1253       N  
ATOM   2901  OE1 GLN A 393       2.413  16.917   5.828  1.00 68.43           O  
ANISOU 2901  OE1 GLN A 393     8705   7995   9301   2406   1527  -1350       O  
ATOM   2902  N   GLU A 394      -0.073  12.151   4.154  1.00 50.88           N  
ANISOU 2902  N   GLU A 394     5748   6392   7192   2328   1357  -1211       N  
ATOM   2903  CA  GLU A 394      -1.397  11.557   4.350  1.00 51.20           C  
ANISOU 2903  CA  GLU A 394     5560   6595   7299   2374   1390  -1270       C  
ATOM   2904  C   GLU A 394      -1.292  10.167   4.949  1.00 51.57           C  
ANISOU 2904  C   GLU A 394     5509   6775   7311   2181   1434  -1255       C  
ATOM   2905  O   GLU A 394      -2.141   9.756   5.742  1.00 48.33           O  
ANISOU 2905  O   GLU A 394     4956   6484   6923   2159   1530  -1324       O  
ATOM   2906  CB  GLU A 394      -2.158  11.465   3.029  1.00 49.62           C  
ANISOU 2906  CB  GLU A 394     5254   6418   7181   2479   1263  -1224       C  
ATOM   2907  CG  GLU A 394      -3.407  12.334   2.967  1.00 59.75           C  
ANISOU 2907  CG  GLU A 394     6462   7691   8549   2614   1269  -1267       C  
ATOM   2908  CD  GLU A 394      -4.610  11.736   3.684  1.00 64.21           C  
ANISOU 2908  CD  GLU A 394     6822   8411   9161   2584   1352  -1326       C  
ATOM   2909  OE1 GLU A 394      -5.447  11.083   3.021  1.00 59.63           O  
ANISOU 2909  OE1 GLU A 394     6080   7936   8641   2599   1284  -1308       O  
ATOM   2910  OE2 GLU A 394      -4.733  11.940   4.910  1.00 70.80           O1-
ANISOU 2910  OE2 GLU A 394     7667   9263   9971   2543   1486  -1391       O1-
ATOM   2911  N   PHE A 395      -0.239   9.455   4.568  1.00 45.02           N  
ANISOU 2911  N   PHE A 395     4762   5918   6426   2042   1371  -1163       N  
ATOM   2912  CA  PHE A 395      -0.014   8.098   5.040  1.00 42.79           C  
ANISOU 2912  CA  PHE A 395     4411   5742   6106   1859   1401  -1133       C  
ATOM   2913  C   PHE A 395       0.993   8.026   6.177  1.00 45.51           C  
ANISOU 2913  C   PHE A 395     4894   6051   6346   1714   1482  -1131       C  
ATOM   2914  O   PHE A 395       1.481   6.945   6.500  1.00 50.18           O  
ANISOU 2914  O   PHE A 395     5478   6700   6888   1559   1491  -1085       O  
ATOM   2915  CB  PHE A 395       0.430   7.210   3.883  1.00 38.80           C  
ANISOU 2915  CB  PHE A 395     3888   5246   5608   1800   1276  -1038       C  
ATOM   2916  CG  PHE A 395      -0.687   6.815   2.982  1.00 39.52           C  
ANISOU 2916  CG  PHE A 395     3795   5430   5793   1893   1208  -1049       C  
ATOM   2917  CD1 PHE A 395      -1.190   7.705   2.056  1.00 40.42           C  
ANISOU 2917  CD1 PHE A 395     3901   5495   5963   2082   1129  -1060       C  
ATOM   2918  CD2 PHE A 395      -1.253   5.555   3.074  1.00 50.65           C  
ANISOU 2918  CD2 PHE A 395     5038   6974   7232   1794   1224  -1053       C  
ATOM   2919  CE1 PHE A 395      -2.231   7.342   1.225  1.00 55.05           C  
ANISOU 2919  CE1 PHE A 395     5575   7442   7897   2175   1056  -1079       C  
ATOM   2920  CE2 PHE A 395      -2.295   5.185   2.252  1.00 48.37           C  
ANISOU 2920  CE2 PHE A 395     4567   6777   7033   1874   1158  -1076       C  
ATOM   2921  CZ  PHE A 395      -2.786   6.078   1.324  1.00 52.89           C  
ANISOU 2921  CZ  PHE A 395     5125   7311   7658   2067   1069  -1092       C  
ATOM   2922  N   GLY A 396       1.296   9.176   6.775  1.00 44.55           N  
ANISOU 2922  N   GLY A 396     4900   5833   6193   1770   1537  -1184       N  
ATOM   2923  CA  GLY A 396       2.250   9.259   7.863  1.00 39.53           C  
ANISOU 2923  CA  GLY A 396     4402   5162   5456   1649   1607  -1198       C  
ATOM   2924  C   GLY A 396       3.600   8.609   7.611  1.00 40.24           C  
ANISOU 2924  C   GLY A 396     4600   5214   5478   1503   1536  -1108       C  
ATOM   2925  O   GLY A 396       4.232   8.103   8.539  1.00 38.29           O  
ANISOU 2925  O   GLY A 396     4405   4999   5145   1370   1586  -1107       O  
ATOM   2926  N   ILE A 397       4.057   8.613   6.359  1.00 39.66           N  
ANISOU 2926  N   ILE A 397     4560   5073   5436   1529   1420  -1033       N  
ATOM   2927  CA  ILE A 397       5.357   8.024   6.035  1.00 40.64           C  
ANISOU 2927  CA  ILE A 397     4781   5159   5501   1398   1352   -951       C  
ATOM   2928  C   ILE A 397       6.485   9.031   6.290  1.00 42.43           C  
ANISOU 2928  C   ILE A 397     5196   5249   5676   1380   1356   -965       C  
ATOM   2929  O   ILE A 397       6.323  10.226   6.029  1.00 36.03           O  
ANISOU 2929  O   ILE A 397     4455   4335   4900   1497   1362  -1002       O  
ATOM   2930  CB  ILE A 397       5.385   7.514   4.573  1.00 44.81           C  
ANISOU 2930  CB  ILE A 397     5263   5682   6081   1424   1232   -867       C  
ATOM   2931  CG1 ILE A 397       4.319   6.430   4.375  1.00 34.75           C  
ANISOU 2931  CG1 ILE A 397     3797   4548   4859   1420   1227   -863       C  
ATOM   2932  CG2 ILE A 397       6.771   6.989   4.186  1.00 32.98           C  
ANISOU 2932  CG2 ILE A 397     3869   4136   4526   1299   1164   -786       C  
ATOM   2933  CD1 ILE A 397       3.894   6.253   2.941  1.00 34.65           C  
ANISOU 2933  CD1 ILE A 397     3712   4538   4915   1507   1116   -816       C  
ATOM   2934  N   LYS A 398       7.607   8.549   6.827  1.00 40.36           N  
ANISOU 2934  N   LYS A 398     5015   4987   5333   1235   1356   -941       N  
ATOM   2935  CA  LYS A 398       8.807   9.370   7.003  1.00 45.08           C  
ANISOU 2935  CA  LYS A 398     5781   5465   5884   1193   1348   -954       C  
ATOM   2936  C   LYS A 398      10.032   8.775   6.287  1.00 45.91           C  
ANISOU 2936  C   LYS A 398     5943   5538   5962   1089   1258   -867       C  
ATOM   2937  O   LYS A 398      10.255   7.557   6.338  1.00 41.40           O  
ANISOU 2937  O   LYS A 398     5310   5059   5362    994   1231   -815       O  
ATOM   2938  CB  LYS A 398       9.114   9.547   8.491  1.00 54.94           C  
ANISOU 2938  CB  LYS A 398     7086   6741   7049   1121   1438  -1031       C  
ATOM   2939  CG  LYS A 398       9.009  10.982   8.986  1.00 62.56           C  
ANISOU 2939  CG  LYS A 398     8147   7603   8019   1203   1502  -1126       C  
ATOM   2940  CD  LYS A 398       7.850  11.165   9.960  1.00 71.71           C  
ANISOU 2940  CD  LYS A 398     9230   8839   9177   1269   1608  -1213       C  
ATOM   2941  CE  LYS A 398       6.504  11.086   9.256  1.00 81.62           C  
ANISOU 2941  CE  LYS A 398    10343  10140  10530   1401   1604  -1203       C  
ATOM   2942  NZ  LYS A 398       6.432  12.035   8.106  1.00 89.19           N1+
ANISOU 2942  NZ  LYS A 398    11352  10971  11566   1530   1542  -1184       N1+
ATOM   2943  N   VAL A 399      10.816   9.626   5.617  1.00 38.81           N  
ANISOU 2943  N   VAL A 399     5163   4506   5077   1108   1218   -852       N  
ATOM   2944  CA  VAL A 399      12.079   9.177   5.019  1.00 37.69           C  
ANISOU 2944  CA  VAL A 399     5084   4329   4908   1004   1145   -782       C  
ATOM   2945  C   VAL A 399      13.302   9.983   5.485  1.00 34.73           C  
ANISOU 2945  C   VAL A 399     4855   3853   4489    931   1164   -825       C  
ATOM   2946  O   VAL A 399      13.249  11.207   5.589  1.00 32.04           O  
ANISOU 2946  O   VAL A 399     4601   3403   4168    996   1204   -881       O  
ATOM   2947  CB  VAL A 399      12.028   9.083   3.443  1.00 55.22           C  
ANISOU 2947  CB  VAL A 399     7293   6502   7187   1067   1059   -697       C  
ATOM   2948  CG1 VAL A 399      10.606   8.998   2.952  1.00 54.35           C  
ANISOU 2948  CG1 VAL A 399     7065   6444   7140   1199   1051   -694       C  
ATOM   2949  CG2 VAL A 399      12.735  10.254   2.776  1.00 56.46           C  
ANISOU 2949  CG2 VAL A 399     7593   6498   7362   1102   1045   -691       C  
ATOM   2950  N   LYS A 400      14.391   9.271   5.773  1.00 30.10           N  
ANISOU 2950  N   LYS A 400     4288   3304   3843    797   1132   -801       N  
ATOM   2951  CA  LYS A 400      15.673   9.882   6.115  1.00 46.22           C  
ANISOU 2951  CA  LYS A 400     6450   5264   5846    711   1134   -839       C  
ATOM   2952  C   LYS A 400      16.323  10.579   4.923  1.00 44.65           C  
ANISOU 2952  C   LYS A 400     6337   4930   5697    727   1094   -799       C  
ATOM   2953  O   LYS A 400      16.302  10.075   3.800  1.00 42.49           O  
ANISOU 2953  O   LYS A 400     6029   4659   5458    747   1035   -713       O  
ATOM   2954  CB  LYS A 400      16.645   8.828   6.645  1.00 48.76           C  
ANISOU 2954  CB  LYS A 400     6755   5677   6095    574   1098   -818       C  
ATOM   2955  CG  LYS A 400      16.191   8.134   7.906  1.00 52.06           C  
ANISOU 2955  CG  LYS A 400     7117   6221   6444    542   1142   -853       C  
ATOM   2956  CD  LYS A 400      16.224   9.046   9.116  1.00 57.65           C  
ANISOU 2956  CD  LYS A 400     7896   6905   7102    540   1214   -965       C  
ATOM   2957  CE  LYS A 400      15.592   8.353  10.316  1.00 59.24           C  
ANISOU 2957  CE  LYS A 400     8041   7237   7232    525   1269   -992       C  
ATOM   2958  NZ  LYS A 400      15.908   6.887  10.300  1.00 56.11           N1+
ANISOU 2958  NZ  LYS A 400     7581   6947   6793    446   1219   -910       N1+
ATOM   2959  N   ASP A 401      16.938  11.722   5.197  1.00 49.71           N  
ANISOU 2959  N   ASP A 401     7095   5453   6339    710   1132   -864       N  
ATOM   2960  CA  ASP A 401      17.562  12.557   4.174  1.00 52.64           C  
ANISOU 2960  CA  ASP A 401     7569   5674   6756    720   1117   -835       C  
ATOM   2961  C   ASP A 401      18.916  12.031   3.695  1.00 44.23           C  
ANISOU 2961  C   ASP A 401     6525   4608   5672    593   1064   -789       C  
ATOM   2962  O   ASP A 401      19.332  12.314   2.575  1.00 46.50           O  
ANISOU 2962  O   ASP A 401     6865   4804   5997    601   1039   -730       O  
ATOM   2963  CB  ASP A 401      17.746  13.978   4.723  1.00 57.94           C  
ANISOU 2963  CB  ASP A 401     8363   6213   7440    735   1188   -932       C  
ATOM   2964  CG  ASP A 401      16.953  15.008   3.953  1.00 69.58           C  
ANISOU 2964  CG  ASP A 401     9899   7558   8982    883   1214   -918       C  
ATOM   2965  OD1 ASP A 401      16.041  14.611   3.199  1.00 76.35           O  
ANISOU 2965  OD1 ASP A 401    10684   8455   9871    989   1180   -849       O  
ATOM   2966  OD2 ASP A 401      17.239  16.216   4.105  1.00 75.36           O1-
ANISOU 2966  OD2 ASP A 401    10752   8145   9734    894   1267   -979       O1-
ATOM   2967  N   ASP A 402      19.601  11.277   4.550  1.00 36.81           N  
ANISOU 2967  N   ASP A 402     5546   3769   4670    480   1047   -816       N  
ATOM   2968  CA  ASP A 402      20.987  10.892   4.303  1.00 34.30           C  
ANISOU 2968  CA  ASP A 402     5249   3451   4332    355   1003   -797       C  
ATOM   2969  C   ASP A 402      21.116   9.430   3.896  1.00 34.57           C  
ANISOU 2969  C   ASP A 402     5184   3606   4346    320    933   -710       C  
ATOM   2970  O   ASP A 402      20.371   8.575   4.389  1.00 29.71           O  
ANISOU 2970  O   ASP A 402     4482   3104   3701    345    928   -695       O  
ATOM   2971  CB  ASP A 402      21.829  11.141   5.557  1.00 37.07           C  
ANISOU 2971  CB  ASP A 402     5636   3824   4625    253   1023   -898       C  
ATOM   2972  CG  ASP A 402      21.744  12.577   6.042  1.00 53.36           C  
ANISOU 2972  CG  ASP A 402     7801   5766   6706    277   1095   -998       C  
ATOM   2973  OD1 ASP A 402      22.627  13.389   5.689  1.00 60.36           O  
ANISOU 2973  OD1 ASP A 402     8775   6534   7624    220   1108  -1028       O  
ATOM   2974  OD2 ASP A 402      20.789  12.900   6.779  1.00 63.29           O1-
ANISOU 2974  OD2 ASP A 402     9054   7042   7951    350   1144  -1049       O1-
ATOM   2975  N   MET A 403      22.065   9.155   2.999  1.00 29.15           N  
ANISOU 2975  N   MET A 403     4512   2889   3675    261    888   -657       N  
ATOM   2976  CA  MET A 403      22.380   7.793   2.570  1.00 27.13           C  
ANISOU 2976  CA  MET A 403     4174   2734   3401    219    821   -580       C  
ATOM   2977  C   MET A 403      22.664   6.901   3.787  1.00 29.76           C  
ANISOU 2977  C   MET A 403     4452   3195   3662    149    806   -612       C  
ATOM   2978  O   MET A 403      23.300   7.346   4.745  1.00 25.44           O  
ANISOU 2978  O   MET A 403     3946   2647   3075     87    826   -693       O  
ATOM   2979  CB  MET A 403      23.585   7.816   1.634  1.00 28.94           C  
ANISOU 2979  CB  MET A 403     4441   2904   3651    150    789   -545       C  
ATOM   2980  CG  MET A 403      23.264   8.311   0.217  1.00 35.23           C  
ANISOU 2980  CG  MET A 403     5283   3598   4504    224    790   -479       C  
ATOM   2981  SD  MET A 403      24.645   8.164  -0.953  1.00 35.02           S  
ANISOU 2981  SD  MET A 403     5294   3518   4495    139    761   -427       S  
ATOM   2982  CE  MET A 403      25.683   9.498  -0.363  1.00105.20           C  
ANISOU 2982  CE  MET A 403    14287  12291  13393     50    825   -527       C  
ATOM   2983  N   THR A 404      22.168   5.665   3.776  1.00 25.91           N  
ANISOU 2983  N   THR A 404     3876   2813   3155    160    772   -552       N  
ATOM   2984  CA  THR A 404      22.421   4.773   4.904  1.00 27.19           C  
ANISOU 2984  CA  THR A 404     3999   3089   3242     99    759   -570       C  
ATOM   2985  C   THR A 404      23.904   4.439   4.966  1.00 27.59           C  
ANISOU 2985  C   THR A 404     4068   3155   3262     -1    708   -576       C  
ATOM   2986  O   THR A 404      24.553   4.232   3.937  1.00 24.65           O  
ANISOU 2986  O   THR A 404     3692   2748   2927    -24    668   -528       O  
ATOM   2987  CB  THR A 404      21.594   3.456   4.860  1.00 28.77           C  
ANISOU 2987  CB  THR A 404     4108   3391   3433    124    740   -499       C  
ATOM   2988  CG2 THR A 404      20.132   3.745   4.727  1.00 23.99           C  
ANISOU 2988  CG2 THR A 404     3464   2781   2868    221    787   -498       C  
ATOM   2989  OG1 THR A 404      22.013   2.649   3.764  1.00 44.05           O  
ANISOU 2989  OG1 THR A 404     6008   5331   5398    107    678   -420       O  
ATOM   2990  N   GLU A 405      24.450   4.399   6.171  1.00 24.01           N  
ANISOU 2990  N   GLU A 405     3631   2756   2736    -57    709   -641       N  
ATOM   2991  CA  GLU A 405      25.839   4.001   6.334  1.00 28.72           C  
ANISOU 2991  CA  GLU A 405     4229   3386   3298   -146    652   -654       C  
ATOM   2992  C   GLU A 405      25.883   2.494   6.489  1.00 22.97           C  
ANISOU 2992  C   GLU A 405     3436   2767   2524   -158    599   -583       C  
ATOM   2993  O   GLU A 405      25.017   1.910   7.134  1.00 41.82           O  
ANISOU 2993  O   GLU A 405     5799   5222   4870   -125    621   -563       O  
ATOM   2994  CB  GLU A 405      26.444   4.666   7.564  1.00 28.54           C  
ANISOU 2994  CB  GLU A 405     4254   3376   3213   -196    666   -764       C  
ATOM   2995  CG  GLU A 405      26.166   6.153   7.633  1.00 38.59           C  
ANISOU 2995  CG  GLU A 405     5598   4540   4525   -176    732   -845       C  
ATOM   2996  CD  GLU A 405      26.445   6.736   9.002  1.00 46.22           C  
ANISOU 2996  CD  GLU A 405     6610   5532   5419   -212    754   -960       C  
ATOM   2997  OE1 GLU A 405      25.833   6.274   9.993  1.00 54.72           O  
ANISOU 2997  OE1 GLU A 405     7674   6698   6421   -186    769   -970       O  
ATOM   2998  OE2 GLU A 405      27.277   7.660   9.083  1.00 48.38           O1-
ANISOU 2998  OE2 GLU A 405     6934   5738   5711   -269    760  -1043       O1-
ATOM   2999  N   VAL A 406      26.898   1.869   5.905  1.00 22.32           N  
ANISOU 2999  N   VAL A 406     3329   2700   2451   -205    537   -546       N  
ATOM   3000  CA  VAL A 406      27.040   0.412   5.941  1.00 23.61           C  
ANISOU 3000  CA  VAL A 406     3440   2953   2579   -214    483   -474       C  
ATOM   3001  C   VAL A 406      28.500   0.070   6.107  1.00 21.53           C  
ANISOU 3001  C   VAL A 406     3171   2726   2284   -281    418   -497       C  
ATOM   3002  O   VAL A 406      29.359   0.702   5.498  1.00 32.73           O  
ANISOU 3002  O   VAL A 406     4601   4087   3748   -320    408   -529       O  
ATOM   3003  CB  VAL A 406      26.633  -0.273   4.593  1.00 40.23           C  
ANISOU 3003  CB  VAL A 406     5499   5035   4750   -181    463   -380       C  
ATOM   3004  CG1 VAL A 406      26.429  -1.774   4.793  1.00 42.13           C  
ANISOU 3004  CG1 VAL A 406     5691   5363   4955   -181    427   -310       C  
ATOM   3005  CG2 VAL A 406      25.403   0.346   3.991  1.00 33.38           C  
ANISOU 3005  CG2 VAL A 406     4633   4107   3941   -111    515   -365       C  
ATOM   3006  N   THR A 407      28.790  -0.956   6.893  1.00 23.94           N  
ANISOU 3006  N   THR A 407     3458   3126   2514   -294    375   -478       N  
ATOM   3007  CA  THR A 407      30.148  -1.469   6.929  1.00 27.17           C  
ANISOU 3007  CA  THR A 407     3847   3579   2899   -342    300   -487       C  
ATOM   3008  C   THR A 407      30.269  -2.707   6.050  1.00 28.42           C  
ANISOU 3008  C   THR A 407     3956   3757   3087   -329    255   -391       C  
ATOM   3009  O   THR A 407      29.551  -3.694   6.236  1.00 29.53           O  
ANISOU 3009  O   THR A 407     4083   3938   3200   -297    256   -323       O  
ATOM   3010  CB  THR A 407      30.627  -1.782   8.362  1.00 26.09           C  
ANISOU 3010  CB  THR A 407     3727   3534   2651   -360    265   -535       C  
ATOM   3011  CG2 THR A 407      32.061  -2.334   8.343  1.00 22.03           C  
ANISOU 3011  CG2 THR A 407     3181   3071   2117   -398    177   -548       C  
ATOM   3012  OG1 THR A 407      30.610  -0.580   9.136  1.00 25.97           O  
ANISOU 3012  OG1 THR A 407     3759   3498   2609   -377    304   -639       O  
ATOM   3013  N   GLY A 408      31.175  -2.649   5.084  1.00 22.39           N  
ANISOU 3013  N   GLY A 408     3168   2960   2380   -358    223   -388       N  
ATOM   3014  CA  GLY A 408      31.455  -3.818   4.281  1.00 21.05           C  
ANISOU 3014  CA  GLY A 408     2954   2811   2234   -348    176   -309       C  
ATOM   3015  C   GLY A 408      32.834  -4.348   4.599  1.00 19.44           C  
ANISOU 3015  C   GLY A 408     2723   2668   1996   -384    104   -334       C  
ATOM   3016  O   GLY A 408      33.526  -3.824   5.485  1.00 20.47           O  
ANISOU 3016  O   GLY A 408     2865   2832   2080   -416     85   -415       O  
ATOM   3017  N   ARG A 409      33.236  -5.384   3.871  1.00 18.84           N  
ANISOU 3017  N   ARG A 409     2607   2608   1942   -374     59   -272       N  
ATOM   3018  CA  ARG A 409      34.548  -5.984   4.036  1.00 20.00           C  
ANISOU 3018  CA  ARG A 409     2717   2814   2067   -395    -14   -291       C  
ATOM   3019  C   ARG A 409      35.205  -6.164   2.671  1.00 19.63           C  
ANISOU 3019  C   ARG A 409     2629   2731   2099   -410    -25   -268       C  
ATOM   3020  O   ARG A 409      34.573  -6.630   1.717  1.00 17.75           O  
ANISOU 3020  O   ARG A 409     2387   2454   1904   -382     -7   -197       O  
ATOM   3021  CB  ARG A 409      34.434  -7.341   4.752  1.00 18.97           C  
ANISOU 3021  CB  ARG A 409     2588   2757   1865   -356    -64   -232       C  
ATOM   3022  CG  ARG A 409      33.891  -7.284   6.182  1.00 19.66           C  
ANISOU 3022  CG  ARG A 409     2722   2891   1855   -342    -53   -250       C  
ATOM   3023  CD  ARG A 409      33.422  -8.659   6.675  1.00 19.60           C  
ANISOU 3023  CD  ARG A 409     2732   2927   1786   -299    -73   -164       C  
ATOM   3024  NE  ARG A 409      32.197  -9.065   5.992  1.00 28.41           N  
ANISOU 3024  NE  ARG A 409     3848   3993   2952   -280    -17    -90       N  
ATOM   3025  CZ  ARG A 409      32.123 -10.026   5.073  1.00 24.48           C  
ANISOU 3025  CZ  ARG A 409     3323   3473   2504   -265    -35    -19       C  
ATOM   3026  NH1 ARG A 409      33.204 -10.717   4.736  1.00 21.20           N1+
ANISOU 3026  NH1 ARG A 409     2881   3079   2093   -262   -103     -7       N1+
ATOM   3027  NH2 ARG A 409      30.961 -10.307   4.498  1.00 17.88           N  
ANISOU 3027  NH2 ARG A 409     2482   2598   1714   -252     14     34       N  
ATOM   3028  N   VAL A 410      36.477  -5.809   2.580  1.00 18.80           N  
ANISOU 3028  N   VAL A 410     2490   2643   2012   -455    -55   -333       N  
ATOM   3029  CA  VAL A 410      37.217  -6.050   1.359  1.00 18.41           C  
ANISOU 3029  CA  VAL A 410     2397   2570   2029   -471    -62   -317       C  
ATOM   3030  C   VAL A 410      37.846  -7.433   1.430  1.00 19.32           C  
ANISOU 3030  C   VAL A 410     2465   2756   2118   -439   -138   -278       C  
ATOM   3031  O   VAL A 410      38.780  -7.652   2.205  1.00 19.84           O  
ANISOU 3031  O   VAL A 410     2498   2895   2144   -448   -198   -329       O  
ATOM   3032  CB  VAL A 410      38.292  -4.966   1.115  1.00 25.05           C  
ANISOU 3032  CB  VAL A 410     3215   3388   2914   -543    -43   -409       C  
ATOM   3033  CG1 VAL A 410      38.967  -5.175  -0.249  1.00 18.64           C  
ANISOU 3033  CG1 VAL A 410     2364   2545   2173   -561    -32   -387       C  
ATOM   3034  CG2 VAL A 410      37.664  -3.585   1.194  1.00 19.33           C  
ANISOU 3034  CG2 VAL A 410     2551   2585   2210   -570     32   -450       C  
ATOM   3035  N   LEU A 411      37.312  -8.372   0.646  1.00 18.43           N  
ANISOU 3035  N   LEU A 411     2352   2624   2027   -398   -139   -192       N  
ATOM   3036  CA  LEU A 411      37.838  -9.743   0.607  1.00 17.37           C  
ANISOU 3036  CA  LEU A 411     2183   2541   1876   -362   -205   -148       C  
ATOM   3037  C   LEU A 411      39.264  -9.770   0.098  1.00 26.89           C  
ANISOU 3037  C   LEU A 411     3324   3774   3119   -387   -240   -198       C  
ATOM   3038  O   LEU A 411      39.629  -8.964  -0.753  1.00 28.04           O  
ANISOU 3038  O   LEU A 411     3453   3875   3324   -431   -195   -232       O  
ATOM   3039  CB  LEU A 411      36.982 -10.622  -0.289  1.00 16.61           C  
ANISOU 3039  CB  LEU A 411     2099   2403   1808   -324   -190    -58       C  
ATOM   3040  CG  LEU A 411      35.518 -10.768   0.105  1.00 23.86           C  
ANISOU 3040  CG  LEU A 411     3066   3300   2701   -298   -154     -7       C  
ATOM   3041  CD1 LEU A 411      34.801 -11.681  -0.858  1.00 24.57           C  
ANISOU 3041  CD1 LEU A 411     3153   3353   2828   -269   -147     69       C  
ATOM   3042  CD2 LEU A 411      35.437 -11.319   1.512  1.00 25.73           C  
ANISOU 3042  CD2 LEU A 411     3326   3595   2854   -279   -187      0       C  
ATOM   3043  N   PRO A 412      40.085 -10.699   0.614  1.00 26.48           N  
ANISOU 3043  N   PRO A 412     3234   3795   3032   -356   -317   -201       N  
ATOM   3044  CA  PRO A 412      41.446 -10.808   0.071  1.00 27.47           C  
ANISOU 3044  CA  PRO A 412     3283   3955   3201   -374   -350   -251       C  
ATOM   3045  C   PRO A 412      41.412 -11.462  -1.321  1.00 25.12           C  
ANISOU 3045  C   PRO A 412     2969   3611   2963   -356   -328   -193       C  
ATOM   3046  O   PRO A 412      40.611 -12.368  -1.563  1.00 26.36           O  
ANISOU 3046  O   PRO A 412     3162   3745   3110   -308   -331   -112       O  
ATOM   3047  CB  PRO A 412      42.159 -11.699   1.094  1.00 25.92           C  
ANISOU 3047  CB  PRO A 412     3058   3849   2940   -325   -445   -262       C  
ATOM   3048  CG  PRO A 412      41.041 -12.548   1.692  1.00 22.53           C  
ANISOU 3048  CG  PRO A 412     2704   3410   2447   -268   -453   -172       C  
ATOM   3049  CD  PRO A 412      39.816 -11.683   1.682  1.00 20.83           C  
ANISOU 3049  CD  PRO A 412     2548   3132   2236   -300   -373   -159       C  
ATOM   3050  N   ALA A 413      42.237 -10.977  -2.242  1.00 29.84           N  
ANISOU 3050  N   ALA A 413     3519   4196   3625   -399   -298   -238       N  
ATOM   3051  CA  ALA A 413      42.222 -11.494  -3.613  1.00 28.79           C  
ANISOU 3051  CA  ALA A 413     3377   4020   3543   -385   -270   -190       C  
ATOM   3052  C   ALA A 413      43.023 -12.783  -3.709  1.00 25.61           C  
ANISOU 3052  C   ALA A 413     2919   3672   3139   -332   -338   -178       C  
ATOM   3053  O   ALA A 413      44.052 -12.929  -3.058  1.00 26.26           O  
ANISOU 3053  O   ALA A 413     2941   3828   3210   -328   -394   -236       O  
ATOM   3054  CB  ALA A 413      42.756 -10.462  -4.591  1.00 25.91           C  
ANISOU 3054  CB  ALA A 413     2993   3613   3239   -452   -199   -237       C  
ATOM   3055  N   PRO A 414      42.545 -13.730  -4.520  1.00 22.29           N  
ANISOU 3055  N   PRO A 414     2520   3217   2732   -288   -335   -106       N  
ATOM   3056  CA  PRO A 414      43.236 -15.019  -4.635  1.00 23.91           C  
ANISOU 3056  CA  PRO A 414     2683   3462   2938   -229   -397    -90       C  
ATOM   3057  C   PRO A 414      44.517 -14.853  -5.441  1.00 25.09           C  
ANISOU 3057  C   PRO A 414     2750   3639   3143   -253   -386   -153       C  
ATOM   3058  O   PRO A 414      44.591 -13.936  -6.246  1.00 25.47           O  
ANISOU 3058  O   PRO A 414     2796   3650   3232   -312   -314   -179       O  
ATOM   3059  CB  PRO A 414      42.240 -15.875  -5.421  1.00 29.07           C  
ANISOU 3059  CB  PRO A 414     3390   4055   3600   -192   -379     -6       C  
ATOM   3060  CG  PRO A 414      41.463 -14.885  -6.265  1.00 19.15           C  
ANISOU 3060  CG  PRO A 414     2172   2734   2371   -239   -301      2       C  
ATOM   3061  CD  PRO A 414      41.342 -13.652  -5.366  1.00 16.72           C  
ANISOU 3061  CD  PRO A 414     1876   2435   2042   -286   -280    -43       C  
ATOM   3062  N   ILE A 415      45.510 -15.708  -5.231  1.00 24.72           N  
ANISOU 3062  N   ILE A 415     2639   3655   3098   -205   -451   -176       N  
ATOM   3063  CA  ILE A 415      46.708 -15.666  -6.063  1.00 24.03           C  
ANISOU 3063  CA  ILE A 415     2464   3597   3068   -222   -434   -237       C  
ATOM   3064  C   ILE A 415      46.567 -16.641  -7.248  1.00 28.10           C  
ANISOU 3064  C   ILE A 415     2992   4072   3612   -177   -417   -184       C  
ATOM   3065  O   ILE A 415      45.905 -17.669  -7.146  1.00 24.15           O  
ANISOU 3065  O   ILE A 415     2544   3546   3086   -114   -453   -115       O  
ATOM   3066  CB  ILE A 415      47.983 -15.940  -5.246  1.00 29.29           C  
ANISOU 3066  CB  ILE A 415     3034   4364   3731   -195   -514   -311       C  
ATOM   3067  CG1 ILE A 415      47.802 -17.192  -4.398  1.00 41.49           C  
ANISOU 3067  CG1 ILE A 415     4608   5937   5218    -95   -608   -256       C  
ATOM   3068  CG2 ILE A 415      48.291 -14.753  -4.305  1.00 27.40           C  
ANISOU 3068  CG2 ILE A 415     2768   4167   3476   -262   -518   -389       C  
ATOM   3069  CD1 ILE A 415      48.764 -17.279  -3.210  1.00 47.65           C  
ANISOU 3069  CD1 ILE A 415     5321   6819   5963    -60   -702   -321       C  
ATOM   3070  N   LEU A 416      47.167 -16.297  -8.380  1.00 17.78           N  
ANISOU 3070  N   LEU A 416     1644   2755   2358   -215   -355   -219       N  
ATOM   3071  CA  LEU A 416      47.086 -17.163  -9.553  1.00 24.59           C  
ANISOU 3071  CA  LEU A 416     2519   3582   3242   -174   -335   -180       C  
ATOM   3072  C   LEU A 416      48.407 -17.868  -9.837  1.00 24.52           C  
ANISOU 3072  C   LEU A 416     2411   3635   3268   -135   -363   -234       C  
ATOM   3073  O   LEU A 416      49.480 -17.282  -9.702  1.00 26.18           O  
ANISOU 3073  O   LEU A 416     2531   3905   3511   -175   -353   -316       O  
ATOM   3074  CB  LEU A 416      46.592 -16.359 -10.759  1.00 22.81           C  
ANISOU 3074  CB  LEU A 416     2342   3289   3037   -232   -237   -165       C  
ATOM   3075  CG  LEU A 416      45.215 -15.824 -10.338  1.00 26.75           C  
ANISOU 3075  CG  LEU A 416     2933   3733   3499   -248   -227   -110       C  
ATOM   3076  CD1 LEU A 416      45.058 -14.354 -10.590  1.00 17.91           C  
ANISOU 3076  CD1 LEU A 416     1839   2577   2390   -327   -149   -135       C  
ATOM   3077  CD2 LEU A 416      44.086 -16.639 -10.959  1.00 27.62           C  
ANISOU 3077  CD2 LEU A 416     3115   3787   3593   -200   -231    -32       C  
ATOM   3078  N   GLN A 417      48.321 -19.143 -10.191  1.00 21.06           N  
ANISOU 3078  N   GLN A 417     1988   3184   2828    -56   -400   -192       N  
ATOM   3079  CA  GLN A 417      49.501 -19.931 -10.507  1.00 18.72           C  
ANISOU 3079  CA  GLN A 417     1603   2941   2567     -1   -429   -239       C  
ATOM   3080  C   GLN A 417      49.739 -19.960 -12.024  1.00 25.22           C  
ANISOU 3080  C   GLN A 417     2419   3735   3431    -21   -347   -250       C  
ATOM   3081  O   GLN A 417      48.864 -20.399 -12.756  1.00 19.17           O  
ANISOU 3081  O   GLN A 417     1733   2899   2650     -4   -323   -190       O  
ATOM   3082  CB  GLN A 417      49.302 -21.359 -10.019  1.00 18.76           C  
ANISOU 3082  CB  GLN A 417     1640   2941   2547    104   -514   -187       C  
ATOM   3083  CG  GLN A 417      50.483 -22.255 -10.301  1.00 19.57           C  
ANISOU 3083  CG  GLN A 417     1657   3094   2685    179   -551   -233       C  
ATOM   3084  CD  GLN A 417      51.713 -21.770  -9.574  1.00 39.04           C  
ANISOU 3084  CD  GLN A 417     4003   5663   5168    175   -592   -322       C  
ATOM   3085  NE2 GLN A 417      52.702 -21.275 -10.324  1.00 38.65           N  
ANISOU 3085  NE2 GLN A 417     3852   5659   5175    131   -536   -403       N  
ATOM   3086  OE1 GLN A 417      51.768 -21.821  -8.345  1.00 38.21           O  
ANISOU 3086  OE1 GLN A 417     3895   5601   5023    206   -672   -321       O  
ATOM   3087  N   TYR A 418      50.908 -19.490 -12.474  1.00 23.13           N  
ANISOU 3087  N   TYR A 418     2055   3523   3212    -58   -303   -331       N  
ATOM   3088  CA  TYR A 418      51.331 -19.587 -13.877  1.00 27.00           C  
ANISOU 3088  CA  TYR A 418     2527   3997   3735    -70   -222   -351       C  
ATOM   3089  C   TYR A 418      52.318 -20.752 -14.073  1.00 27.07           C  
ANISOU 3089  C   TYR A 418     2452   4059   3775     17   -264   -390       C  
ATOM   3090  O   TYR A 418      52.708 -21.414 -13.101  1.00 28.49           O  
ANISOU 3090  O   TYR A 418     2587   4287   3951     88   -360   -401       O  
ATOM   3091  CB  TYR A 418      51.891 -18.240 -14.392  1.00 22.19           C  
ANISOU 3091  CB  TYR A 418     1876   3398   3156   -180   -119   -411       C  
ATOM   3092  CG  TYR A 418      50.777 -17.258 -14.709  1.00 21.88           C  
ANISOU 3092  CG  TYR A 418     1951   3278   3087   -247    -55   -355       C  
ATOM   3093  CD1 TYR A 418      50.306 -17.116 -16.006  1.00 20.20           C  
ANISOU 3093  CD1 TYR A 418     1812   3001   2862   -264     26   -317       C  
ATOM   3094  CD2 TYR A 418      50.159 -16.509 -13.706  1.00 18.88           C  
ANISOU 3094  CD2 TYR A 418     1609   2884   2682   -283    -82   -340       C  
ATOM   3095  CE1 TYR A 418      49.275 -16.245 -16.315  1.00 18.26           C  
ANISOU 3095  CE1 TYR A 418     1671   2682   2584   -309     75   -264       C  
ATOM   3096  CE2 TYR A 418      49.099 -15.632 -14.004  1.00 22.51           C  
ANISOU 3096  CE2 TYR A 418     2173   3266   3115   -332    -26   -289       C  
ATOM   3097  CZ  TYR A 418      48.665 -15.508 -15.325  1.00 31.16           C  
ANISOU 3097  CZ  TYR A 418     3338   4300   4203   -341     50   -250       C  
ATOM   3098  OH  TYR A 418      47.629 -14.658 -15.683  1.00 22.47           O  
ANISOU 3098  OH  TYR A 418     2341   3125   3073   -375     99   -199       O  
ATOM   3099  N   GLY A 419      52.691 -21.021 -15.322  1.00 25.68           N  
ANISOU 3099  N   GLY A 419     2263   3871   3624     21   -195   -408       N  
ATOM   3100  CA  GLY A 419      53.499 -22.190 -15.646  1.00 25.86           C  
ANISOU 3100  CA  GLY A 419     2219   3929   3676    112   -227   -441       C  
ATOM   3101  C   GLY A 419      54.938 -21.861 -15.994  1.00 30.45           C  
ANISOU 3101  C   GLY A 419     2657   4596   4315     88   -178   -545       C  
ATOM   3102  O   GLY A 419      55.551 -20.991 -15.369  1.00 25.58           O  
ANISOU 3102  O   GLY A 419     1957   4040   3723     26   -175   -605       O  
ATOM   3103  N   GLY A 420      55.478 -22.543 -17.006  1.00 40.47           N  
ANISOU 3103  N   GLY A 420     3895   5871   5611    132   -135   -573       N  
ATOM   3104  CA  GLY A 420      56.860 -22.326 -17.417  1.00 41.31           C  
ANISOU 3104  CA  GLY A 420     3856   6062   5779    113    -79   -677       C  
ATOM   3105  C   GLY A 420      57.854 -22.796 -16.370  1.00 42.40           C  
ANISOU 3105  C   GLY A 420     3858   6298   5953    186   -181   -743       C  
ATOM   3106  O   GLY A 420      57.459 -23.329 -15.327  1.00 42.79           O  
ANISOU 3106  O   GLY A 420     3942   6344   5972    257   -296   -700       O  
ATOM   3107  N   ARG A 421      59.146 -22.598 -16.622  1.00 46.64           N  
ANISOU 3107  N   ARG A 421     4241   6926   6554    171   -140   -849       N  
ATOM   3108  CA  ARG A 421      60.150 -23.194 -15.743  1.00 52.52           C  
ANISOU 3108  CA  ARG A 421     4847   7773   7336    263   -246   -919       C  
ATOM   3109  C   ARG A 421      60.235 -22.505 -14.384  1.00 57.04           C  
ANISOU 3109  C   ARG A 421     5374   8400   7897    228   -329   -943       C  
ATOM   3110  O   ARG A 421      60.593 -23.131 -13.382  1.00 55.59           O  
ANISOU 3110  O   ARG A 421     5139   8277   7707    329   -457   -958       O  
ATOM   3111  CB  ARG A 421      61.519 -23.319 -16.425  1.00 57.35           C  
ANISOU 3111  CB  ARG A 421     5292   8475   8024    272   -185  -1034       C  
ATOM   3112  CG  ARG A 421      62.229 -22.029 -16.774  1.00 60.88           C  
ANISOU 3112  CG  ARG A 421     5634   8975   8521    125    -68  -1123       C  
ATOM   3113  CD  ARG A 421      63.530 -22.371 -17.490  1.00 67.92           C  
ANISOU 3113  CD  ARG A 421     6362   9954   9489    151     -5  -1232       C  
ATOM   3114  NE  ARG A 421      64.347 -21.199 -17.781  1.00 73.81           N  
ANISOU 3114  NE  ARG A 421     6987  10761  10296      6    112  -1330       N  
ATOM   3115  CZ  ARG A 421      65.356 -20.783 -17.022  1.00 80.28           C  
ANISOU 3115  CZ  ARG A 421     7713  11646  11142    -21     68  -1401       C  
ATOM   3116  NH1 ARG A 421      65.673 -21.441 -15.914  1.00 82.22           N1+
ANISOU 3116  NH1 ARG A 421     7924  11940  11373     92    -88  -1406       N1+
ATOM   3117  NH2 ARG A 421      66.048 -19.707 -17.369  1.00 82.70           N  
ANISOU 3117  NH2 ARG A 421     7969  11967  11488   -160    184  -1466       N  
ATOM   3118  N   ASN A 422      59.859 -21.230 -14.349  1.00 61.20           N  
ANISOU 3118  N   ASN A 422     5934   8903   8417     91   -258   -943       N  
ATOM   3119  CA  ASN A 422      59.854 -20.459 -13.104  1.00 60.28           C  
ANISOU 3119  CA  ASN A 422     5789   8830   8285     43   -325   -970       C  
ATOM   3120  C   ASN A 422      58.587 -20.653 -12.258  1.00 52.70           C  
ANISOU 3120  C   ASN A 422     4980   7799   7243     79   -407   -861       C  
ATOM   3121  O   ASN A 422      58.601 -20.379 -11.057  1.00 50.38           O  
ANISOU 3121  O   ASN A 422     4668   7551   6924     84   -495   -877       O  
ATOM   3122  CB  ASN A 422      60.076 -18.971 -13.402  1.00 59.95           C  
ANISOU 3122  CB  ASN A 422     5712   8788   8277   -124   -208  -1028       C  
ATOM   3123  CG  ASN A 422      59.220 -18.476 -14.554  1.00 60.63           C  
ANISOU 3123  CG  ASN A 422     5935   8760   8343   -201    -76   -955       C  
ATOM   3124  ND2 ASN A 422      58.326 -17.534 -14.266  1.00 51.68           N  
ANISOU 3124  ND2 ASN A 422     4908   7557   7171   -284    -49   -905       N  
ATOM   3125  OD1 ASN A 422      59.364 -18.933 -15.695  1.00 68.29           O  
ANISOU 3125  OD1 ASN A 422     6916   9706   9327   -181     -1   -945       O  
ATOM   3126  N   ARG A 423      57.511 -21.133 -12.892  1.00 45.87           N  
ANISOU 3126  N   ARG A 423     4262   6828   6339    103   -376   -757       N  
ATOM   3127  CA  ARG A 423      56.199 -21.299 -12.248  1.00 43.05           C  
ANISOU 3127  CA  ARG A 423     4052   6395   5911    125   -431   -652       C  
ATOM   3128  C   ARG A 423      55.806 -20.080 -11.402  1.00 41.34           C  
ANISOU 3128  C   ARG A 423     3858   6182   5670     29   -429   -660       C  
ATOM   3129  O   ARG A 423      55.621 -20.177 -10.185  1.00 43.42           O  
ANISOU 3129  O   ARG A 423     4132   6474   5891     66   -526   -648       O  
ATOM   3130  CB  ARG A 423      56.142 -22.594 -11.422  1.00 46.87           C  
ANISOU 3130  CB  ARG A 423     4556   6892   6362    266   -560   -611       C  
ATOM   3131  CG  ARG A 423      56.238 -23.870 -12.261  1.00 58.19           C  
ANISOU 3131  CG  ARG A 423     6009   8289   7813    365   -559   -584       C  
ATOM   3132  CD  ARG A 423      56.218 -25.139 -11.411  1.00 66.70           C  
ANISOU 3132  CD  ARG A 423     7115   9368   8859    506   -684   -541       C  
ATOM   3133  NE  ARG A 423      57.353 -25.201 -10.492  1.00 82.75           N  
ANISOU 3133  NE  ARG A 423     9018  11516  10907    567   -775   -618       N  
ATOM   3134  CZ  ARG A 423      58.515 -25.794 -10.763  1.00 91.52           C  
ANISOU 3134  CZ  ARG A 423    10006  12699  12070    649   -801   -692       C  
ATOM   3135  NH1 ARG A 423      58.706 -26.387 -11.935  1.00 93.88           N1+
ANISOU 3135  NH1 ARG A 423    10300  12961  12409    678   -736   -699       N1+
ATOM   3136  NH2 ARG A 423      59.489 -25.793  -9.857  1.00 92.34           N  
ANISOU 3136  NH2 ARG A 423     9988  12914  12182    707   -896   -764       N  
ATOM   3137  N   ALA A 424      55.693 -18.932 -12.061  1.00 33.28           N  
ANISOU 3137  N   ALA A 424     2849   5127   4670    -92   -316   -680       N  
ATOM   3138  CA  ALA A 424      55.419 -17.669 -11.380  1.00 28.89           C  
ANISOU 3138  CA  ALA A 424     2308   4566   4101   -192   -297   -701       C  
ATOM   3139  C   ALA A 424      54.014 -17.586 -10.780  1.00 29.53           C  
ANISOU 3139  C   ALA A 424     2535   4573   4113   -183   -331   -604       C  
ATOM   3140  O   ALA A 424      53.063 -18.213 -11.260  1.00 28.07           O  
ANISOU 3140  O   ALA A 424     2455   4313   3896   -137   -326   -513       O  
ATOM   3141  CB  ALA A 424      55.649 -16.498 -12.321  1.00 27.95           C  
ANISOU 3141  CB  ALA A 424     2180   4414   4024   -320   -157   -741       C  
ATOM   3142  N   ILE A 425      53.904 -16.799  -9.718  1.00 34.40           N  
ANISOU 3142  N   ILE A 425     3148   5213   4707   -229   -365   -632       N  
ATOM   3143  CA  ILE A 425      52.628 -16.510  -9.085  1.00 36.59           C  
ANISOU 3143  CA  ILE A 425     3551   5428   4923   -235   -383   -556       C  
ATOM   3144  C   ILE A 425      52.221 -15.113  -9.489  1.00 35.05           C  
ANISOU 3144  C   ILE A 425     3403   5173   4743   -353   -278   -567       C  
ATOM   3145  O   ILE A 425      53.069 -14.224  -9.615  1.00 36.89           O  
ANISOU 3145  O   ILE A 425     3556   5437   5024   -439   -224   -655       O  
ATOM   3146  CB  ILE A 425      52.761 -16.520  -7.559  1.00 39.48           C  
ANISOU 3146  CB  ILE A 425     3893   5862   5246   -204   -490   -583       C  
ATOM   3147  CG1 ILE A 425      53.239 -17.880  -7.091  1.00 34.28           C  
ANISOU 3147  CG1 ILE A 425     3194   5263   4568    -78   -599   -571       C  
ATOM   3148  CG2 ILE A 425      51.429 -16.200  -6.900  1.00 48.81           C  
ANISOU 3148  CG2 ILE A 425     5203   6980   6363   -213   -496   -508       C  
ATOM   3149  CD1 ILE A 425      52.201 -18.925  -7.250  1.00 33.59           C  
ANISOU 3149  CD1 ILE A 425     3224   5101   4439      2   -620   -456       C  
ATOM   3150  N   ALA A 426      50.927 -14.913  -9.698  1.00 30.28           N  
ANISOU 3150  N   ALA A 426     2926   4479   4101   -358   -246   -480       N  
ATOM   3151  CA  ALA A 426      50.414 -13.567  -9.874  1.00 29.80           C  
ANISOU 3151  CA  ALA A 426     2925   4354   4043   -454   -160   -483       C  
ATOM   3152  C   ALA A 426      49.627 -13.177  -8.634  1.00 30.67           C  
ANISOU 3152  C   ALA A 426     3092   4458   4102   -453   -212   -465       C  
ATOM   3153  O   ALA A 426      48.759 -13.930  -8.160  1.00 27.23           O  
ANISOU 3153  O   ALA A 426     2720   4009   3617   -382   -271   -393       O  
ATOM   3154  CB  ALA A 426      49.545 -13.488 -11.091  1.00 19.19           C  
ANISOU 3154  CB  ALA A 426     1680   2917   2693   -459    -81   -406       C  
ATOM   3155  N   THR A 427      49.928 -12.000  -8.102  1.00 32.36           N  
ANISOU 3155  N   THR A 427     3285   4680   4330   -537   -183   -534       N  
ATOM   3156  CA  THR A 427      49.165 -11.487  -6.976  1.00 27.39           C  
ANISOU 3156  CA  THR A 427     2717   4040   3652   -544   -217   -526       C  
ATOM   3157  C   THR A 427      48.393 -10.229  -7.399  1.00 19.79           C  
ANISOU 3157  C   THR A 427     1844   2979   2698   -619   -118   -509       C  
ATOM   3158  O   THR A 427      48.986  -9.187  -7.640  1.00 28.53           O  
ANISOU 3158  O   THR A 427     2924   4070   3848   -710    -48   -577       O  
ATOM   3159  CB  THR A 427      50.060 -11.303  -5.720  1.00 25.56           C  
ANISOU 3159  CB  THR A 427     2394   3906   3410   -557   -295   -623       C  
ATOM   3160  CG2 THR A 427      51.430 -10.824  -6.107  1.00 34.04           C  
ANISOU 3160  CG2 THR A 427     3346   5032   4555   -629   -260   -731       C  
ATOM   3161  OG1 THR A 427      49.461 -10.352  -4.829  1.00 37.57           O  
ANISOU 3161  OG1 THR A 427     3973   5404   4896   -602   -289   -641       O  
ATOM   3162  N   PRO A 428      47.058 -10.349  -7.526  1.00 22.87           N  
ANISOU 3162  N   PRO A 428     2341   3301   3049   -579   -108   -417       N  
ATOM   3163  CA  PRO A 428      46.168  -9.258  -7.934  1.00 20.75           C  
ANISOU 3163  CA  PRO A 428     2167   2935   2781   -624    -25   -388       C  
ATOM   3164  C   PRO A 428      46.320  -8.049  -7.037  1.00 27.08           C  
ANISOU 3164  C   PRO A 428     2971   3732   3585   -696     -6   -461       C  
ATOM   3165  O   PRO A 428      46.482  -8.199  -5.838  1.00 31.66           O  
ANISOU 3165  O   PRO A 428     3518   4377   4133   -683    -78   -501       O  
ATOM   3166  CB  PRO A 428      44.766  -9.859  -7.738  1.00 17.67           C  
ANISOU 3166  CB  PRO A 428     1859   2513   2341   -549    -60   -294       C  
ATOM   3167  CG  PRO A 428      44.960 -11.305  -7.948  1.00 17.37           C  
ANISOU 3167  CG  PRO A 428     1785   2521   2294   -475   -123   -255       C  
ATOM   3168  CD  PRO A 428      46.316 -11.610  -7.346  1.00 18.18           C  
ANISOU 3168  CD  PRO A 428     1781   2716   2411   -482   -177   -335       C  
ATOM   3169  N   ASN A 429      46.271  -6.861  -7.616  1.00 32.98           N  
ANISOU 3169  N   ASN A 429     3765   4401   4366   -769     91   -479       N  
ATOM   3170  CA  ASN A 429      46.381  -5.643  -6.833  1.00 32.28           C  
ANISOU 3170  CA  ASN A 429     3689   4290   4285   -843    119   -553       C  
ATOM   3171  C   ASN A 429      45.354  -4.669  -7.351  1.00 25.35           C  
ANISOU 3171  C   ASN A 429     2932   3293   3407   -858    204   -503       C  
ATOM   3172  O   ASN A 429      45.438  -4.231  -8.497  1.00 32.08           O  
ANISOU 3172  O   ASN A 429     3823   4074   4291   -888    289   -478       O  
ATOM   3173  CB  ASN A 429      47.780  -5.049  -6.966  1.00 37.21           C  
ANISOU 3173  CB  ASN A 429     4224   4944   4971   -942    160   -661       C  
ATOM   3174  CG  ASN A 429      48.115  -4.095  -5.840  1.00 45.58           C  
ANISOU 3174  CG  ASN A 429     5264   6020   6035  -1013    151   -763       C  
ATOM   3175  ND2 ASN A 429      49.044  -4.501  -4.988  1.00 45.38           N  
ANISOU 3175  ND2 ASN A 429     5127   6108   6008  -1018     68   -848       N  
ATOM   3176  OD1 ASN A 429      47.557  -3.000  -5.742  1.00 49.75           O  
ANISOU 3176  OD1 ASN A 429     5876   6459   6566  -1059    215   -770       O  
ATOM   3177  N   GLN A 430      44.375  -4.357  -6.517  1.00 23.36           N  
ANISOU 3177  N   GLN A 430     2742   3020   3115   -828    181   -486       N  
ATOM   3178  CA  GLN A 430      43.228  -3.553  -6.929  1.00 25.62           C  
ANISOU 3178  CA  GLN A 430     3142   3198   3394   -815    246   -430       C  
ATOM   3179  C   GLN A 430      42.527  -4.174  -8.138  1.00 23.25           C  
ANISOU 3179  C   GLN A 430     2887   2859   3087   -749    261   -327       C  
ATOM   3180  O   GLN A 430      42.217  -3.487  -9.101  1.00 26.79           O  
ANISOU 3180  O   GLN A 430     3409   3219   3553   -760    337   -293       O  
ATOM   3181  CB  GLN A 430      43.628  -2.093  -7.198  1.00 24.47           C  
ANISOU 3181  CB  GLN A 430     3039   2964   3294   -909    345   -488       C  
ATOM   3182  CG  GLN A 430      44.070  -1.334  -5.930  1.00 30.89           C  
ANISOU 3182  CG  GLN A 430     3825   3801   4110   -974    331   -595       C  
ATOM   3183  CD  GLN A 430      43.004  -1.339  -4.829  1.00 39.23           C  
ANISOU 3183  CD  GLN A 430     4926   4870   5110   -915    281   -581       C  
ATOM   3184  NE2 GLN A 430      43.448  -1.239  -3.579  1.00 42.98           N  
ANISOU 3184  NE2 GLN A 430     5353   5415   5562   -943    228   -667       N  
ATOM   3185  OE1 GLN A 430      41.801  -1.435  -5.102  1.00 33.78           O  
ANISOU 3185  OE1 GLN A 430     4310   4131   4394   -844    290   -498       O  
ATOM   3186  N   GLY A 431      42.299  -5.485  -8.077  1.00 21.71           N  
ANISOU 3186  N   GLY A 431     2653   2730   2864   -679    186   -281       N  
ATOM   3187  CA  GLY A 431      41.561  -6.187  -9.115  1.00 21.90           C  
ANISOU 3187  CA  GLY A 431     2715   2727   2877   -613    186   -192       C  
ATOM   3188  C   GLY A 431      42.294  -6.419 -10.433  1.00 17.28           C  
ANISOU 3188  C   GLY A 431     2115   2129   2320   -629    229   -181       C  
ATOM   3189  O   GLY A 431      41.679  -6.820 -11.409  1.00 21.98           O  
ANISOU 3189  O   GLY A 431     2755   2692   2904   -580    239   -113       O  
ATOM   3190  N   VAL A 432      43.604  -6.193 -10.458  1.00 19.03           N  
ANISOU 3190  N   VAL A 432     2270   2382   2579   -697    255   -252       N  
ATOM   3191  CA  VAL A 432      44.371  -6.292 -11.704  1.00 18.24           C  
ANISOU 3191  CA  VAL A 432     2155   2269   2507   -724    314   -250       C  
ATOM   3192  C   VAL A 432      45.783  -6.892 -11.501  1.00 28.82           C  
ANISOU 3192  C   VAL A 432     3370   3701   3880   -756    287   -324       C  
ATOM   3193  O   VAL A 432      46.463  -6.591 -10.518  1.00 37.33           O  
ANISOU 3193  O   VAL A 432     4380   4829   4975   -802    261   -403       O  
ATOM   3194  CB  VAL A 432      44.454  -4.897 -12.424  1.00 20.90           C  
ANISOU 3194  CB  VAL A 432     2570   2505   2866   -794    431   -257       C  
ATOM   3195  CG1 VAL A 432      45.084  -3.867 -11.530  1.00 37.75           C  
ANISOU 3195  CG1 VAL A 432     4677   4633   5034   -885    461   -347       C  
ATOM   3196  CG2 VAL A 432      45.266  -4.997 -13.687  1.00 22.21           C  
ANISOU 3196  CG2 VAL A 432     2725   2659   3054   -826    503   -255       C  
ATOM   3197  N   TRP A 433      46.201  -7.767 -12.414  1.00 26.92           N  
ANISOU 3197  N   TRP A 433     3096   3486   3645   -724    288   -301       N  
ATOM   3198  CA  TRP A 433      47.594  -8.220 -12.483  1.00 25.21           C  
ANISOU 3198  CA  TRP A 433     2762   3348   3469   -755    284   -373       C  
ATOM   3199  C   TRP A 433      48.101  -8.249 -13.944  1.00 29.12           C  
ANISOU 3199  C   TRP A 433     3265   3814   3984   -775    374   -360       C  
ATOM   3200  O   TRP A 433      47.427  -7.749 -14.843  1.00 28.06           O  
ANISOU 3200  O   TRP A 433     3236   3595   3830   -776    443   -300       O  
ATOM   3201  CB  TRP A 433      47.747  -9.581 -11.805  1.00 25.69           C  
ANISOU 3201  CB  TRP A 433     2749   3500   3513   -674    168   -372       C  
ATOM   3202  CG  TRP A 433      47.077 -10.729 -12.534  1.00 24.89           C  
ANISOU 3202  CG  TRP A 433     2688   3386   3382   -585    137   -289       C  
ATOM   3203  CD1 TRP A 433      47.686 -11.651 -13.341  1.00 21.70           C  
ANISOU 3203  CD1 TRP A 433     2237   3015   2994   -550    136   -289       C  
ATOM   3204  CD2 TRP A 433      45.688 -11.091 -12.497  1.00 22.22           C  
ANISOU 3204  CD2 TRP A 433     2439   3004   3000   -522    102   -205       C  
ATOM   3205  CE2 TRP A 433      45.531 -12.234 -13.312  1.00 19.43           C  
ANISOU 3205  CE2 TRP A 433     2090   2655   2638   -457     79   -160       C  
ATOM   3206  CE3 TRP A 433      44.563 -10.559 -11.863  1.00 16.85           C  
ANISOU 3206  CE3 TRP A 433     1831   2282   2290   -516     91   -170       C  
ATOM   3207  NE1 TRP A 433      46.766 -12.557 -13.807  1.00 21.02           N  
ANISOU 3207  NE1 TRP A 433     2211   2903   2874   -473    101   -212       N  
ATOM   3208  CZ2 TRP A 433      44.297 -12.845 -13.514  1.00 18.93           C  
ANISOU 3208  CZ2 TRP A 433     2096   2557   2540   -395     45    -85       C  
ATOM   3209  CZ3 TRP A 433      43.339 -11.174 -12.059  1.00 17.74           C  
ANISOU 3209  CZ3 TRP A 433     2006   2364   2369   -450     58    -93       C  
ATOM   3210  CH2 TRP A 433      43.215 -12.303 -12.881  1.00 18.13           C  
ANISOU 3210  CH2 TRP A 433     2054   2419   2413   -394     35    -53       C  
ATOM   3211  N   ASP A 434      49.281  -8.812 -14.194  1.00 33.91           N  
ANISOU 3211  N   ASP A 434     3764   4493   4628   -788    376   -418       N  
ATOM   3212  CA  ASP A 434      49.811  -8.825 -15.566  1.00 29.47           C  
ANISOU 3212  CA  ASP A 434     3208   3908   4082   -812    472   -411       C  
ATOM   3213  C   ASP A 434      50.662 -10.049 -15.936  1.00 31.26           C  
ANISOU 3213  C   ASP A 434     3330   4219   4326   -763    437   -440       C  
ATOM   3214  O   ASP A 434      51.142 -10.769 -15.062  1.00 37.01           O  
ANISOU 3214  O   ASP A 434     3960   5032   5070   -725    344   -484       O  
ATOM   3215  CB  ASP A 434      50.567  -7.524 -15.893  1.00 32.36           C  
ANISOU 3215  CB  ASP A 434     3571   4233   4493   -936    597   -470       C  
ATOM   3216  CG  ASP A 434      51.724  -7.256 -14.941  1.00 42.09           C  
ANISOU 3216  CG  ASP A 434     4664   5545   5785  -1007    578   -588       C  
ATOM   3217  OD1 ASP A 434      52.715  -8.011 -14.971  1.00 37.96           O  
ANISOU 3217  OD1 ASP A 434     4014   5114   5295   -995    551   -647       O  
ATOM   3218  OD2 ASP A 434      51.649  -6.278 -14.168  1.00 55.08           O1-
ANISOU 3218  OD2 ASP A 434     6323   7162   7444  -1074    589   -629       O1-
ATOM   3219  N   MET A 435      50.850 -10.250 -17.239  1.00 35.02           N  
ANISOU 3219  N   MET A 435     3837   4670   4798   -760    515   -414       N  
ATOM   3220  CA  MET A 435      51.581 -11.397 -17.795  1.00 38.37           C  
ANISOU 3220  CA  MET A 435     4181   5162   5237   -707    499   -437       C  
ATOM   3221  C   MET A 435      53.101 -11.243 -17.767  1.00 39.65           C  
ANISOU 3221  C   MET A 435     4199   5399   5468   -773    548   -545       C  
ATOM   3222  O   MET A 435      53.830 -12.158 -18.166  1.00 36.65           O  
ANISOU 3222  O   MET A 435     3734   5083   5109   -729    537   -577       O  
ATOM   3223  CB  MET A 435      51.178 -11.613 -19.259  1.00 34.35           C  
ANISOU 3223  CB  MET A 435     3766   4596   4688   -680    571   -374       C  
ATOM   3224  CG  MET A 435      49.781 -12.137 -19.465  1.00 37.71           C  
ANISOU 3224  CG  MET A 435     4306   4971   5051   -595    507   -279       C  
ATOM   3225  SD  MET A 435      49.618 -13.820 -18.882  1.00 47.15           S  
ANISOU 3225  SD  MET A 435     5439   6232   6243   -481    367   -271       S  
ATOM   3226  CE  MET A 435      50.757 -14.703 -19.944  1.00 19.79           C  
ANISOU 3226  CE  MET A 435     1899   2819   2802   -456    413   -318       C  
ATOM   3227  N   ARG A 436      53.579 -10.085 -17.325  1.00 37.84           N  
ANISOU 3227  N   ARG A 436     3939   5161   5278   -881    606   -605       N  
ATOM   3228  CA  ARG A 436      54.998  -9.774 -17.420  1.00 45.44           C  
ANISOU 3228  CA  ARG A 436     4765   6188   6313   -964    674   -715       C  
ATOM   3229  C   ARG A 436      55.856 -10.754 -16.614  1.00 47.49           C  
ANISOU 3229  C   ARG A 436     4860   6575   6609   -905    561   -792       C  
ATOM   3230  O   ARG A 436      55.786 -10.798 -15.387  1.00 50.58           O  
ANISOU 3230  O   ARG A 436     5208   7011   6999   -886    455   -820       O  
ATOM   3231  CB  ARG A 436      55.251  -8.337 -16.973  1.00 57.23           C  
ANISOU 3231  CB  ARG A 436     6261   7641   7844  -1095    748   -770       C  
ATOM   3232  CG  ARG A 436      56.579  -7.780 -17.425  1.00 74.63           C  
ANISOU 3232  CG  ARG A 436     8356   9877  10122  -1211    867   -871       C  
ATOM   3233  CD  ARG A 436      56.387  -6.519 -18.252  1.00 85.24           C  
ANISOU 3233  CD  ARG A 436     9821  11101  11466  -1321   1030   -841       C  
ATOM   3234  NE  ARG A 436      55.615  -5.511 -17.533  1.00 90.58           N  
ANISOU 3234  NE  ARG A 436    10596  11695  12127  -1363   1020   -819       N  
ATOM   3235  CZ  ARG A 436      56.125  -4.705 -16.609  1.00 98.56           C  
ANISOU 3235  CZ  ARG A 436    11536  12722  13192  -1459   1021   -913       C  
ATOM   3236  NH1 ARG A 436      57.411  -4.790 -16.288  1.00102.41           N1+
ANISOU 3236  NH1 ARG A 436    11854  13308  13748  -1513   1019  -1033       N1+
ATOM   3237  NH2 ARG A 436      55.350  -3.815 -16.004  1.00100.70           N  
ANISOU 3237  NH2 ARG A 436    11909  12910  13443  -1488   1014   -890       N  
ATOM   3238  N   GLY A 437      56.656 -11.548 -17.318  1.00 44.49           N  
ANISOU 3238  N   GLY A 437     4395   6253   6256   -870    584   -824       N  
ATOM   3239  CA  GLY A 437      57.521 -12.521 -16.677  1.00 38.89           C  
ANISOU 3239  CA  GLY A 437     3531   5664   5583   -799    481   -897       C  
ATOM   3240  C   GLY A 437      56.866 -13.875 -16.489  1.00 36.86           C  
ANISOU 3240  C   GLY A 437     3315   5414   5275   -652    359   -824       C  
ATOM   3241  O   GLY A 437      57.451 -14.776 -15.894  1.00 42.03           O  
ANISOU 3241  O   GLY A 437     3865   6157   5949   -571    259   -867       O  
ATOM   3242  N   LYS A 438      55.654 -14.030 -17.009  1.00 32.81           N  
ANISOU 3242  N   LYS A 438     2959   4809   4700   -614    368   -715       N  
ATOM   3243  CA  LYS A 438      54.891 -15.246 -16.770  1.00 30.17           C  
ANISOU 3243  CA  LYS A 438     2677   4467   4318   -489    257   -643       C  
ATOM   3244  C   LYS A 438      54.597 -16.060 -18.036  1.00 28.40           C  
ANISOU 3244  C   LYS A 438     2516   4204   4069   -429    297   -591       C  
ATOM   3245  O   LYS A 438      54.380 -15.510 -19.110  1.00 25.77           O  
ANISOU 3245  O   LYS A 438     2257   3813   3721   -480    406   -565       O  
ATOM   3246  CB  LYS A 438      53.612 -14.895 -16.005  1.00 30.92           C  
ANISOU 3246  CB  LYS A 438     2887   4500   4360   -484    199   -568       C  
ATOM   3247  CG  LYS A 438      53.909 -13.993 -14.800  1.00 33.13           C  
ANISOU 3247  CG  LYS A 438     3113   4815   4659   -550    170   -627       C  
ATOM   3248  CD  LYS A 438      52.694 -13.714 -13.936  1.00 36.41           C  
ANISOU 3248  CD  LYS A 438     3632   5180   5021   -536    110   -561       C  
ATOM   3249  CE  LYS A 438      53.040 -12.744 -12.815  1.00 38.44           C  
ANISOU 3249  CE  LYS A 438     3840   5470   5295   -608     92   -631       C  
ATOM   3250  NZ  LYS A 438      53.445 -11.423 -13.361  1.00 41.98           N1+
ANISOU 3250  NZ  LYS A 438     4288   5878   5783   -734    218   -679       N1+
ATOM   3251  N   GLN A 439      54.614 -17.379 -17.893  1.00 26.72           N  
ANISOU 3251  N   GLN A 439     2279   4022   3851   -318    207   -578       N  
ATOM   3252  CA  GLN A 439      54.260 -18.284 -18.968  1.00 28.54           C  
ANISOU 3252  CA  GLN A 439     2573   4215   4055   -251    226   -534       C  
ATOM   3253  C   GLN A 439      52.935 -18.898 -18.604  1.00 27.29           C  
ANISOU 3253  C   GLN A 439     2529   3997   3845   -185    139   -442       C  
ATOM   3254  O   GLN A 439      52.668 -19.107 -17.424  1.00 27.34           O  
ANISOU 3254  O   GLN A 439     2525   4019   3845   -155     43   -429       O  
ATOM   3255  CB  GLN A 439      55.263 -19.428 -19.051  1.00 35.80           C  
ANISOU 3255  CB  GLN A 439     3380   5206   5014   -167    186   -592       C  
ATOM   3256  CG  GLN A 439      56.660 -19.041 -18.742  1.00 48.91           C  
ANISOU 3256  CG  GLN A 439     4879   6962   6742   -208    213   -700       C  
ATOM   3257  CD  GLN A 439      57.263 -18.245 -19.844  1.00 58.96           C  
ANISOU 3257  CD  GLN A 439     6129   8233   8040   -303    365   -744       C  
ATOM   3258  NE2 GLN A 439      57.377 -16.939 -19.629  1.00 63.45           N  
ANISOU 3258  NE2 GLN A 439     6693   8792   8624   -422    433   -768       N  
ATOM   3259  OE1 GLN A 439      57.619 -18.787 -20.893  1.00 61.48           O  
ANISOU 3259  OE1 GLN A 439     6443   8555   8362   -272    428   -757       O  
ATOM   3260  N   PHE A 440      52.124 -19.225 -19.605  1.00 20.06           N  
ANISOU 3260  N   PHE A 440     1719   3014   2887   -162    170   -383       N  
ATOM   3261  CA  PHE A 440      50.862 -19.913 -19.340  1.00 21.82           C  
ANISOU 3261  CA  PHE A 440     2039   3182   3068   -101     91   -304       C  
ATOM   3262  C   PHE A 440      51.065 -21.203 -18.549  1.00 25.75           C  
ANISOU 3262  C   PHE A 440     2492   3711   3581     -7    -18   -308       C  
ATOM   3263  O   PHE A 440      52.068 -21.899 -18.713  1.00 25.61           O  
ANISOU 3263  O   PHE A 440     2389   3743   3598     42    -26   -362       O  
ATOM   3264  CB  PHE A 440      50.142 -20.247 -20.633  1.00 18.75           C  
ANISOU 3264  CB  PHE A 440     1750   2734   2639    -81    134   -261       C  
ATOM   3265  CG  PHE A 440      49.604 -19.045 -21.366  1.00 27.54           C  
ANISOU 3265  CG  PHE A 440     2947   3799   3718   -155    223   -231       C  
ATOM   3266  CD1 PHE A 440      48.941 -18.042 -20.685  1.00 20.38           C  
ANISOU 3266  CD1 PHE A 440     2082   2864   2798   -206    219   -199       C  
ATOM   3267  CD2 PHE A 440      49.758 -18.928 -22.748  1.00 22.88           C  
ANISOU 3267  CD2 PHE A 440     2401   3190   3102   -165    313   -234       C  
ATOM   3268  CE1 PHE A 440      48.437 -16.931 -21.366  1.00 23.15           C  
ANISOU 3268  CE1 PHE A 440     2519   3162   3116   -262    300   -167       C  
ATOM   3269  CE2 PHE A 440      49.266 -17.822 -23.422  1.00 20.38           C  
ANISOU 3269  CE2 PHE A 440     2174   2824   2745   -223    393   -199       C  
ATOM   3270  CZ  PHE A 440      48.608 -16.821 -22.736  1.00 18.50           C  
ANISOU 3270  CZ  PHE A 440     1979   2552   2499   -269    386   -164       C  
ATOM   3271  N   TYR A 441      50.103 -21.517 -17.690  1.00 22.05           N  
ANISOU 3271  N   TYR A 441     2084   3210   3085     22    -96   -249       N  
ATOM   3272  CA  TYR A 441      50.140 -22.759 -16.937  1.00 24.90           C  
ANISOU 3272  CA  TYR A 441     2430   3581   3450    113   -195   -235       C  
ATOM   3273  C   TYR A 441      50.293 -23.954 -17.875  1.00 26.45           C  
ANISOU 3273  C   TYR A 441     2640   3754   3656    185   -194   -238       C  
ATOM   3274  O   TYR A 441      51.119 -24.845 -17.646  1.00 27.49           O  
ANISOU 3274  O   TYR A 441     2708   3922   3817    259   -238   -273       O  
ATOM   3275  CB  TYR A 441      48.881 -22.897 -16.080  1.00 28.03           C  
ANISOU 3275  CB  TYR A 441     2914   3929   3809    120   -256   -161       C  
ATOM   3276  CG  TYR A 441      48.849 -24.157 -15.257  1.00 23.87           C  
ANISOU 3276  CG  TYR A 441     2392   3399   3279    209   -349   -135       C  
ATOM   3277  CD1 TYR A 441      49.461 -24.213 -14.005  1.00 30.23           C  
ANISOU 3277  CD1 TYR A 441     3139   4262   4085    239   -417   -154       C  
ATOM   3278  CD2 TYR A 441      48.199 -25.288 -15.720  1.00 22.45           C  
ANISOU 3278  CD2 TYR A 441     2281   3156   3092    264   -370    -92       C  
ATOM   3279  CE1 TYR A 441      49.419 -25.369 -13.239  1.00 29.02           C  
ANISOU 3279  CE1 TYR A 441     3007   4099   3919    328   -502   -121       C  
ATOM   3280  CE2 TYR A 441      48.155 -26.438 -14.972  1.00 22.88           C  
ANISOU 3280  CE2 TYR A 441     2355   3195   3145    343   -447    -63       C  
ATOM   3281  CZ  TYR A 441      48.767 -26.475 -13.733  1.00 27.03           C  
ANISOU 3281  CZ  TYR A 441     2832   3774   3666    378   -512    -73       C  
ATOM   3282  OH  TYR A 441      48.717 -27.628 -12.996  1.00 26.94           O  
ANISOU 3282  OH  TYR A 441     2854   3738   3643    463   -586    -35       O  
ATOM   3283  N   ASN A 442      49.495 -23.972 -18.936  1.00 25.04           N  
ANISOU 3283  N   ASN A 442     2546   3516   3451    168   -146   -205       N  
ATOM   3284  CA  ASN A 442      49.744 -24.902 -20.026  1.00 21.06           C  
ANISOU 3284  CA  ASN A 442     2053   2994   2953    221   -124   -225       C  
ATOM   3285  C   ASN A 442      49.659 -24.195 -21.368  1.00 22.44           C  
ANISOU 3285  C   ASN A 442     2265   3155   3104    166    -23   -236       C  
ATOM   3286  O   ASN A 442      48.568 -23.890 -21.850  1.00 21.24           O  
ANISOU 3286  O   ASN A 442     2208   2951   2911    140     -9   -187       O  
ATOM   3287  CB  ASN A 442      48.782 -26.095 -19.993  1.00 21.52           C  
ANISOU 3287  CB  ASN A 442     2194   2986   2996    282   -189   -174       C  
ATOM   3288  CG  ASN A 442      49.233 -27.229 -20.920  1.00 27.91           C  
ANISOU 3288  CG  ASN A 442     3002   3781   3821    352   -181   -209       C  
ATOM   3289  ND2 ASN A 442      48.283 -27.996 -21.416  1.00 23.80           N  
ANISOU 3289  ND2 ASN A 442     2571   3192   3281    375   -201   -176       N  
ATOM   3290  OD1 ASN A 442      50.428 -27.400 -21.184  1.00 30.73           O  
ANISOU 3290  OD1 ASN A 442     3275   4191   4210    382   -155   -271       O  
ATOM   3291  N   GLY A 443      50.817 -23.936 -21.966  1.00 22.24           N  
ANISOU 3291  N   GLY A 443     2165   3181   3104    152     48   -301       N  
ATOM   3292  CA  GLY A 443      50.881 -23.239 -23.236  1.00 21.37           C  
ANISOU 3292  CA  GLY A 443     2093   3061   2966    100    156   -312       C  
ATOM   3293  C   GLY A 443      50.877 -24.157 -24.441  1.00 23.54           C  
ANISOU 3293  C   GLY A 443     2408   3315   3220    155    182   -326       C  
ATOM   3294  O   GLY A 443      51.592 -25.164 -24.467  1.00 23.74           O  
ANISOU 3294  O   GLY A 443     2374   3366   3280    224    157   -371       O  
ATOM   3295  N   ILE A 444      50.080 -23.803 -25.446  1.00 24.42           N  
ANISOU 3295  N   ILE A 444     2624   3382   3273    130    229   -291       N  
ATOM   3296  CA  ILE A 444      50.026 -24.578 -26.682  1.00 25.13           C  
ANISOU 3296  CA  ILE A 444     2764   3453   3330    176    258   -309       C  
ATOM   3297  C   ILE A 444      51.079 -24.132 -27.693  1.00 26.71           C  
ANISOU 3297  C   ILE A 444     2931   3695   3524    147    379   -364       C  
ATOM   3298  O   ILE A 444      51.189 -22.952 -28.006  1.00 29.15           O  
ANISOU 3298  O   ILE A 444     3259   4007   3809     72    463   -353       O  
ATOM   3299  CB  ILE A 444      48.654 -24.448 -27.373  1.00 26.92           C  
ANISOU 3299  CB  ILE A 444     3122   3620   3487    170    245   -252       C  
ATOM   3300  CG1 ILE A 444      47.524 -24.880 -26.433  1.00 18.46           C  
ANISOU 3300  CG1 ILE A 444     2083   2507   2423    189    136   -201       C  
ATOM   3301  CG2 ILE A 444      48.637 -25.261 -28.684  1.00 19.76           C  
ANISOU 3301  CG2 ILE A 444     2269   2700   2539    218    272   -282       C  
ATOM   3302  CD1 ILE A 444      47.711 -26.266 -25.848  1.00 18.54           C  
ANISOU 3302  CD1 ILE A 444     2055   2509   2480    260     57   -219       C  
ATOM   3303  N   GLU A 445      51.839 -25.076 -28.227  1.00 29.00           N  
ANISOU 3303  N   GLU A 445     3175   4010   3833    207    396   -423       N  
ATOM   3304  CA  GLU A 445      52.739 -24.741 -29.318  1.00 27.12           C  
ANISOU 3304  CA  GLU A 445     2916   3809   3579    182    522   -475       C  
ATOM   3305  C   GLU A 445      51.962 -24.682 -30.646  1.00 27.05           C  
ANISOU 3305  C   GLU A 445     3044   3756   3477    182    569   -445       C  
ATOM   3306  O   GLU A 445      51.202 -25.585 -30.972  1.00 22.34           O  
ANISOU 3306  O   GLU A 445     2517   3121   2850    242    503   -432       O  
ATOM   3307  CB  GLU A 445      53.890 -25.733 -29.406  1.00 23.38           C  
ANISOU 3307  CB  GLU A 445     2335   3386   3162    251    529   -556       C  
ATOM   3308  CG  GLU A 445      54.818 -25.456 -30.587  1.00 62.56           C  
ANISOU 3308  CG  GLU A 445     7273   8390   8107    226    670   -616       C  
ATOM   3309  CD  GLU A 445      56.134 -26.198 -30.479  1.00 67.04           C  
ANISOU 3309  CD  GLU A 445     7698   9025   8749    284    687   -708       C  
ATOM   3310  OE1 GLU A 445      56.310 -26.945 -29.493  1.00 71.20           O  
ANISOU 3310  OE1 GLU A 445     8153   9562   9336    350    581   -720       O  
ATOM   3311  OE2 GLU A 445      56.990 -26.036 -31.375  1.00 67.01           O1-
ANISOU 3311  OE2 GLU A 445     7655   9065   8741    266    808   -767       O1-
ATOM   3312  N   ILE A 446      52.146 -23.607 -31.402  1.00 24.43           N  
ANISOU 3312  N   ILE A 446     2756   3430   3097    114    684   -436       N  
ATOM   3313  CA  ILE A 446      51.389 -23.418 -32.630  1.00 26.90           C  
ANISOU 3313  CA  ILE A 446     3209   3705   3307    116    725   -401       C  
ATOM   3314  C   ILE A 446      52.342 -23.500 -33.820  1.00 27.01           C  
ANISOU 3314  C   ILE A 446     3219   3755   3289    116    853   -458       C  
ATOM   3315  O   ILE A 446      53.135 -22.590 -34.052  1.00 26.00           O  
ANISOU 3315  O   ILE A 446     3060   3654   3166     47    973   -473       O  
ATOM   3316  CB  ILE A 446      50.639 -22.079 -32.619  1.00 22.52           C  
ANISOU 3316  CB  ILE A 446     2743   3112   2702     48    752   -327       C  
ATOM   3317  CG1 ILE A 446      49.653 -22.042 -31.456  1.00 21.40           C  
ANISOU 3317  CG1 ILE A 446     2604   2937   2590     53    629   -276       C  
ATOM   3318  CG2 ILE A 446      49.876 -21.886 -33.907  1.00 22.73           C  
ANISOU 3318  CG2 ILE A 446     2917   3105   2613     64    787   -291       C  
ATOM   3319  CD1 ILE A 446      49.085 -20.659 -31.182  1.00 21.07           C  
ANISOU 3319  CD1 ILE A 446     2621   2862   2521    -14    656   -214       C  
ATOM   3320  N   LYS A 447      52.280 -24.612 -34.549  1.00 24.42           N  
ANISOU 3320  N   LYS A 447     2920   3425   2931    192    832   -495       N  
ATOM   3321  CA  LYS A 447      53.178 -24.822 -35.689  1.00 29.81           C  
ANISOU 3321  CA  LYS A 447     3600   4147   3581    202    953   -557       C  
ATOM   3322  C   LYS A 447      52.468 -24.655 -37.042  1.00 27.69           C  
ANISOU 3322  C   LYS A 447     3491   3849   3181    211    999   -529       C  
ATOM   3323  O   LYS A 447      53.101 -24.359 -38.045  1.00 26.95           O  
ANISOU 3323  O   LYS A 447     3427   3781   3032    193   1128   -556       O  
ATOM   3324  CB  LYS A 447      53.845 -26.201 -35.617  1.00 28.25           C  
ANISOU 3324  CB  LYS A 447     3313   3976   3444    287    916   -638       C  
ATOM   3325  CG  LYS A 447      54.520 -26.505 -34.287  1.00 34.79           C  
ANISOU 3325  CG  LYS A 447     3989   4836   4394    301    853   -667       C  
ATOM   3326  CD  LYS A 447      55.216 -27.858 -34.317  1.00 42.80           C  
ANISOU 3326  CD  LYS A 447     4926   5873   5463    399    822   -745       C  
ATOM   3327  CE  LYS A 447      55.495 -28.386 -32.915  1.00 49.42           C  
ANISOU 3327  CE  LYS A 447     5653   6721   6403    441    711   -752       C  
ATOM   3328  NZ  LYS A 447      56.304 -29.643 -32.947  1.00 54.62           N1+
ANISOU 3328  NZ  LYS A 447     6232   7402   7120    544    690   -831       N1+
ATOM   3329  N   VAL A 448      51.154 -24.853 -37.074  1.00 27.76           N  
ANISOU 3329  N   VAL A 448     3602   3809   3137    241    893   -476       N  
ATOM   3330  CA  VAL A 448      50.430 -24.792 -38.343  1.00 31.37           C  
ANISOU 3330  CA  VAL A 448     4209   4247   3466    263    914   -456       C  
ATOM   3331  C   VAL A 448      49.255 -23.826 -38.237  1.00 31.81           C  
ANISOU 3331  C   VAL A 448     4366   4260   3461    233    869   -366       C  
ATOM   3332  O   VAL A 448      48.260 -24.119 -37.579  1.00 29.54           O  
ANISOU 3332  O   VAL A 448     4085   3942   3198    253    742   -335       O  
ATOM   3333  CB  VAL A 448      49.943 -26.190 -38.790  1.00 30.72           C  
ANISOU 3333  CB  VAL A 448     4158   4152   3364    348    825   -503       C  
ATOM   3334  CG1 VAL A 448      49.311 -26.119 -40.166  1.00 31.15           C  
ANISOU 3334  CG1 VAL A 448     4360   4198   3276    372    850   -496       C  
ATOM   3335  CG2 VAL A 448      51.100 -27.175 -38.799  1.00 30.67           C  
ANISOU 3335  CG2 VAL A 448     4048   4180   3427    390    863   -593       C  
ATOM   3336  N   TRP A 449      49.383 -22.673 -38.890  1.00 32.56           N  
ANISOU 3336  N   TRP A 449     4542   4352   3479    185    978   -324       N  
ATOM   3337  CA  TRP A 449      48.415 -21.585 -38.742  1.00 32.96           C  
ANISOU 3337  CA  TRP A 449     4685   4360   3480    156    951   -237       C  
ATOM   3338  C   TRP A 449      48.334 -20.754 -40.006  1.00 32.96           C  
ANISOU 3338  C   TRP A 449     4831   4350   3344    147   1057   -198       C  
ATOM   3339  O   TRP A 449      49.297 -20.659 -40.752  1.00 30.72           O  
ANISOU 3339  O   TRP A 449     4554   4092   3027    127   1190   -231       O  
ATOM   3340  CB  TRP A 449      48.795 -20.687 -37.561  1.00 24.41           C  
ANISOU 3340  CB  TRP A 449     3517   3267   2491     82    973   -209       C  
ATOM   3341  CG  TRP A 449      50.184 -20.146 -37.663  1.00 28.83           C  
ANISOU 3341  CG  TRP A 449     4009   3857   3087     15   1125   -245       C  
ATOM   3342  CD1 TRP A 449      51.351 -20.846 -37.500  1.00 25.81           C  
ANISOU 3342  CD1 TRP A 449     3498   3528   2782     16   1167   -328       C  
ATOM   3343  CD2 TRP A 449      50.566 -18.799 -37.966  1.00 26.02           C  
ANISOU 3343  CD2 TRP A 449     3709   3480   2697    -64   1258   -206       C  
ATOM   3344  CE2 TRP A 449      51.975 -18.754 -37.963  1.00 34.15           C  
ANISOU 3344  CE2 TRP A 449     4629   4556   3791   -119   1381   -272       C  
ATOM   3345  CE3 TRP A 449      49.855 -17.629 -38.240  1.00 32.54           C  
ANISOU 3345  CE3 TRP A 449     4667   4249   3446    -92   1288   -122       C  
ATOM   3346  NE1 TRP A 449      52.430 -20.017 -37.681  1.00 32.28           N  
ANISOU 3346  NE1 TRP A 449     4276   4368   3620    -63   1319   -347       N  
ATOM   3347  CZ2 TRP A 449      52.685 -17.585 -38.215  1.00 27.83           C  
ANISOU 3347  CZ2 TRP A 449     3847   3743   2984   -213   1538   -259       C  
ATOM   3348  CZ3 TRP A 449      50.562 -16.469 -38.486  1.00 32.22           C  
ANISOU 3348  CZ3 TRP A 449     4657   4188   3397   -179   1442   -102       C  
ATOM   3349  CH2 TRP A 449      51.959 -16.454 -38.472  1.00 34.84           C  
ANISOU 3349  CH2 TRP A 449     4877   4563   3796   -244   1569   -171       C  
ATOM   3350  N   ALA A 450      47.184 -20.136 -40.237  1.00 38.28           N  
ANISOU 3350  N   ALA A 450     5622   4985   3937    166   1001   -126       N  
ATOM   3351  CA  ALA A 450      46.979 -19.364 -41.449  1.00 26.56           C  
ANISOU 3351  CA  ALA A 450     4297   3486   2309    174   1085    -78       C  
ATOM   3352  C   ALA A 450      46.546 -17.941 -41.147  1.00 30.30           C  
ANISOU 3352  C   ALA A 450     4844   3907   2761    131   1115     11       C  
ATOM   3353  O   ALA A 450      46.146 -17.614 -40.026  1.00 25.51           O  
ANISOU 3353  O   ALA A 450     4173   3276   2242    107   1045     36       O  
ATOM   3354  CB  ALA A 450      45.954 -20.043 -42.330  1.00 26.69           C  
ANISOU 3354  CB  ALA A 450     4415   3510   2216    262    986    -83       C  
ATOM   3355  N   ILE A 451      46.659 -17.093 -42.164  1.00 33.06           N  
ANISOU 3355  N   ILE A 451     5335   4235   2991    124   1228     59       N  
ATOM   3356  CA  ILE A 451      46.165 -15.729 -42.118  1.00 33.63           C  
ANISOU 3356  CA  ILE A 451     5516   4246   3017    100   1262    152       C  
ATOM   3357  C   ILE A 451      45.150 -15.549 -43.233  1.00 31.49           C  
ANISOU 3357  C   ILE A 451     5423   3961   2581    186   1217    206       C  
ATOM   3358  O   ILE A 451      45.459 -15.749 -44.411  1.00 29.46           O  
ANISOU 3358  O   ILE A 451     5261   3726   2207    215   1290    195       O  
ATOM   3359  CB  ILE A 451      47.279 -14.689 -42.375  1.00 35.30           C  
ANISOU 3359  CB  ILE A 451     5759   4428   3223      8   1460    173       C  
ATOM   3360  CG1 ILE A 451      48.457 -14.900 -41.442  1.00 38.72           C  
ANISOU 3360  CG1 ILE A 451     6009   4891   3811    -77   1519    102       C  
ATOM   3361  CG2 ILE A 451      46.734 -13.277 -42.195  1.00 32.34           C  
ANISOU 3361  CG2 ILE A 451     5499   3974   2816    -17   1490    269       C  
ATOM   3362  CD1 ILE A 451      48.048 -14.869 -40.012  1.00 44.17           C  
ANISOU 3362  CD1 ILE A 451     6585   5570   4627    -95   1402    102       C  
ATOM   3363  N   ALA A 452      43.936 -15.166 -42.873  1.00 32.64           N  
ANISOU 3363  N   ALA A 452     5613   4076   2711    232   1096    260       N  
ATOM   3364  CA  ALA A 452      42.989 -14.731 -43.885  1.00 34.25           C  
ANISOU 3364  CA  ALA A 452     5993   4264   2757    314   1059    322       C  
ATOM   3365  C   ALA A 452      42.752 -13.241 -43.685  1.00 33.03           C  
ANISOU 3365  C   ALA A 452     5938   4032   2579    291   1120    418       C  
ATOM   3366  O   ALA A 452      42.169 -12.814 -42.668  1.00 28.85           O  
ANISOU 3366  O   ALA A 452     5355   3471   2136    280   1046    444       O  
ATOM   3367  CB  ALA A 452      41.691 -15.517 -43.785  1.00 34.94           C  
ANISOU 3367  CB  ALA A 452     6059   4383   2834    401    864    300       C  
ATOM   3368  N   CYS A 453      43.231 -12.451 -44.640  1.00 36.14           N  
ANISOU 3368  N   CYS A 453     6482   4392   2858    280   1263    470       N  
ATOM   3369  CA  CYS A 453      43.095 -11.005 -44.548  1.00 37.84           C  
ANISOU 3369  CA  CYS A 453     6814   4519   3044    255   1341    566       C  
ATOM   3370  C   CYS A 453      41.944 -10.464 -45.381  1.00 38.30           C  
ANISOU 3370  C   CYS A 453     7010   4551   2991    362   1241    631       C  
ATOM   3371  O   CYS A 453      42.071 -10.322 -46.583  1.00 37.14           O  
ANISOU 3371  O   CYS A 453     6960   4406   2747    396   1277    644       O  
ATOM   3372  CB  CYS A 453      44.380 -10.299 -44.966  1.00 31.97           C  
ANISOU 3372  CB  CYS A 453     6084   3738   2325    156   1529    569       C  
ATOM   3373  SG  CYS A 453      44.279  -8.538 -44.581  1.00 37.24           S  
ANISOU 3373  SG  CYS A 453     6814   4286   3049    104   1583    651       S  
ATOM   3374  N   PHE A 454      40.832 -10.145 -44.729  1.00 43.10           N  
ANISOU 3374  N   PHE A 454     7618   5136   3623    416   1115    666       N  
ATOM   3375  CA  PHE A 454      39.666  -9.620 -45.423  1.00 39.97           C  
ANISOU 3375  CA  PHE A 454     7324   4720   3141    524   1006    717       C  
ATOM   3376  C   PHE A 454      39.694  -8.105 -45.536  1.00 40.61           C  
ANISOU 3376  C   PHE A 454     7492   4702   3235    506   1080    790       C  
ATOM   3377  O   PHE A 454      38.744  -7.499 -46.023  1.00 44.99           O  
ANISOU 3377  O   PHE A 454     8133   5231   3729    596   1001    836       O  
ATOM   3378  CB  PHE A 454      38.380 -10.095 -44.750  1.00 36.50           C  
ANISOU 3378  CB  PHE A 454     6829   4317   2723    601    823    706       C  
ATOM   3379  CG  PHE A 454      38.146 -11.559 -44.905  1.00 37.28           C  
ANISOU 3379  CG  PHE A 454     6871   4509   2784    643    727    632       C  
ATOM   3380  CD1 PHE A 454      37.417 -12.046 -45.979  1.00 38.31           C  
ANISOU 3380  CD1 PHE A 454     7056   4691   2807    739    623    611       C  
ATOM   3381  CD2 PHE A 454      38.693 -12.459 -44.006  1.00 35.88           C  
ANISOU 3381  CD2 PHE A 454     6513   4367   2753    566    717    553       C  
ATOM   3382  CE1 PHE A 454      37.223 -13.408 -46.144  1.00 38.95           C  
ANISOU 3382  CE1 PHE A 454     7081   4854   2865    771    533    529       C  
ATOM   3383  CE2 PHE A 454      38.499 -13.821 -44.159  1.00 37.86           C  
ANISOU 3383  CE2 PHE A 454     6674   4692   3018    592    618    467       C  
ATOM   3384  CZ  PHE A 454      37.763 -14.296 -45.231  1.00 40.38           C  
ANISOU 3384  CZ  PHE A 454     7082   5057   3202    690    529    452       C  
ATOM   3385  N   ALA A 455      40.779  -7.492 -45.083  1.00 39.38           N  
ANISOU 3385  N   ALA A 455     7311   4492   3160    390   1231    795       N  
ATOM   3386  CA  ALA A 455      40.985  -6.067 -45.328  1.00 40.65           C  
ANISOU 3386  CA  ALA A 455     7567   4554   3327    362   1323    855       C  
ATOM   3387  C   ALA A 455      41.716  -5.933 -46.657  1.00 40.17           C  
ANISOU 3387  C   ALA A 455     7603   4488   3171    353   1434    864       C  
ATOM   3388  O   ALA A 455      42.489  -6.814 -47.025  1.00 41.73           O  
ANISOU 3388  O   ALA A 455     7755   4750   3352    316   1490    813       O  
ATOM   3389  CB  ALA A 455      41.794  -5.427 -44.204  1.00 33.31           C  
ANISOU 3389  CB  ALA A 455     6557   3565   2533    236   1429    845       C  
ATOM   3390  N   PRO A 456      41.470  -4.838 -47.388  1.00 36.97           N  
ANISOU 3390  N   PRO A 456     7336   4008   2704    391   1468    928       N  
ATOM   3391  CA  PRO A 456      42.123  -4.685 -48.697  1.00 48.22           C  
ANISOU 3391  CA  PRO A 456     8866   5425   4029    387   1574    944       C  
ATOM   3392  C   PRO A 456      43.650  -4.649 -48.574  1.00 52.27           C  
ANISOU 3392  C   PRO A 456     9320   5928   4614    244   1755    907       C  
ATOM   3393  O   PRO A 456      44.172  -4.186 -47.554  1.00 51.56           O  
ANISOU 3393  O   PRO A 456     9147   5794   4648    145   1818    893       O  
ATOM   3394  CB  PRO A 456      41.561  -3.362 -49.231  1.00 41.48           C  
ANISOU 3394  CB  PRO A 456     8167   4476   3118    446   1582   1024       C  
ATOM   3395  CG  PRO A 456      40.987  -2.657 -48.056  1.00 39.24           C  
ANISOU 3395  CG  PRO A 456     7841   4134   2936    440   1530   1042       C  
ATOM   3396  CD  PRO A 456      40.568  -3.720 -47.072  1.00 37.22           C  
ANISOU 3396  CD  PRO A 456     7435   3959   2747    446   1412    988       C  
ATOM   3397  N   GLN A 457      44.346  -5.157 -49.590  1.00 54.10           N  
ANISOU 3397  N   GLN A 457     9583   6204   4769    233   1833    885       N  
ATOM   3398  CA  GLN A 457      45.791  -5.357 -49.502  1.00 56.76           C  
ANISOU 3398  CA  GLN A 457     9834   6557   5176    104   1993    832       C  
ATOM   3399  C   GLN A 457      46.547  -4.052 -49.313  1.00 62.39           C  
ANISOU 3399  C   GLN A 457    10581   7167   5958      1   2139    863       C  
ATOM   3400  O   GLN A 457      47.559  -4.011 -48.617  1.00 58.48           O  
ANISOU 3400  O   GLN A 457     9967   6670   5581   -121   2239    812       O  
ATOM   3401  CB  GLN A 457      46.322  -6.116 -50.722  1.00 54.09           C  
ANISOU 3401  CB  GLN A 457     9532   6287   4731    124   2048    803       C  
ATOM   3402  CG  GLN A 457      47.837  -6.316 -50.709  1.00 60.15           C  
ANISOU 3402  CG  GLN A 457    10204   7078   5571     -4   2218    743       C  
ATOM   3403  CD  GLN A 457      48.316  -7.287 -51.772  1.00 69.12           C  
ANISOU 3403  CD  GLN A 457    11349   8301   6613     23   2257    697       C  
ATOM   3404  NE2 GLN A 457      49.627  -7.503 -51.827  1.00 72.78           N  
ANISOU 3404  NE2 GLN A 457    11722   8794   7137    -79   2404    639       N  
ATOM   3405  OE1 GLN A 457      47.518  -7.842 -52.532  1.00 69.07           O  
ANISOU 3405  OE1 GLN A 457    11424   8338   6483    134   2154    708       O  
ATOM   3406  N   LYS A 458      46.036  -2.990 -49.928  1.00 70.55           N  
ANISOU 3406  N   LYS A 458    11775   8113   6919     52   2147    940       N  
ATOM   3407  CA  LYS A 458      46.619  -1.662 -49.790  1.00 73.40           C  
ANISOU 3407  CA  LYS A 458    12193   8361   7336    -34   2279    973       C  
ATOM   3408  C   LYS A 458      46.502  -1.139 -48.356  1.00 71.38           C  
ANISOU 3408  C   LYS A 458    11842   8057   7223    -94   2253    958       C  
ATOM   3409  O   LYS A 458      47.296  -0.300 -47.932  1.00 75.81           O  
ANISOU 3409  O   LYS A 458    12384   8547   7874   -206   2373    948       O  
ATOM   3410  CB  LYS A 458      45.948  -0.686 -50.760  1.00 77.23           C  
ANISOU 3410  CB  LYS A 458    12882   8762   7700     56   2277   1062       C  
ATOM   3411  CG  LYS A 458      45.827  -1.211 -52.181  1.00 80.84           C  
ANISOU 3411  CG  LYS A 458    13447   9272   7998    139   2272   1083       C  
ATOM   3412  CD  LYS A 458      47.194  -1.440 -52.807  1.00 83.86           C  
ANISOU 3412  CD  LYS A 458    13811   9677   8377     36   2443   1047       C  
ATOM   3413  CE  LYS A 458      47.085  -2.158 -54.152  1.00 83.35           C  
ANISOU 3413  CE  LYS A 458    13832   9682   8154    118   2429   1053       C  
ATOM   3414  NZ  LYS A 458      46.255  -1.406 -55.135  1.00 81.74           N1+
ANISOU 3414  NZ  LYS A 458    13831   9418   7810    231   2392   1141       N1+
ATOM   3415  N   GLN A 459      45.517  -1.628 -47.609  1.00 64.14           N  
ANISOU 3415  N   GLN A 459    10865   7179   6327    -22   2097    953       N  
ATOM   3416  CA  GLN A 459      45.316  -1.164 -46.234  1.00 64.02           C  
ANISOU 3416  CA  GLN A 459    10763   7123   6439    -70   2063    940       C  
ATOM   3417  C   GLN A 459      45.982  -2.098 -45.216  1.00 57.71           C  
ANISOU 3417  C   GLN A 459     9769   6403   5756   -158   2065    857       C  
ATOM   3418  O   GLN A 459      45.853  -1.910 -44.005  1.00 50.70           O  
ANISOU 3418  O   GLN A 459     8790   5499   4975   -201   2028    835       O  
ATOM   3419  CB  GLN A 459      43.823  -1.011 -45.919  1.00 64.48           C  
ANISOU 3419  CB  GLN A 459    10868   7168   6463     57   1897    985       C  
ATOM   3420  CG  GLN A 459      43.527  -0.081 -44.751  1.00 70.92           C  
ANISOU 3420  CG  GLN A 459    11656   7906   7385     21   1885    993       C  
ATOM   3421  CD  GLN A 459      42.227  -0.414 -44.038  1.00 72.59           C  
ANISOU 3421  CD  GLN A 459    11827   8149   7604    120   1711   1002       C  
ATOM   3422  NE2 GLN A 459      41.927   0.330 -42.976  1.00 71.17           N  
ANISOU 3422  NE2 GLN A 459    11617   7909   7517     94   1695   1005       N  
ATOM   3423  OE1 GLN A 459      41.502  -1.329 -44.435  1.00 73.64           O  
ANISOU 3423  OE1 GLN A 459    11954   8361   7663    218   1593   1002       O  
ATOM   3424  N   CYS A 460      46.702  -3.098 -45.715  1.00 55.48           N  
ANISOU 3424  N   CYS A 460     9425   6206   5448   -183   2109    807       N  
ATOM   3425  CA  CYS A 460      47.338  -4.077 -44.850  1.00 49.77           C  
ANISOU 3425  CA  CYS A 460     8520   5566   4824   -252   2110    725       C  
ATOM   3426  C   CYS A 460      48.360  -4.882 -45.622  1.00 44.85           C  
ANISOU 3426  C   CYS A 460     7850   5017   4172   -289   2205    671       C  
ATOM   3427  O   CYS A 460      48.179  -6.077 -45.827  1.00 40.28           O  
ANISOU 3427  O   CYS A 460     7226   4530   3549   -233   2140    636       O  
ATOM   3428  CB  CYS A 460      46.287  -5.019 -44.274  1.00 54.18           C  
ANISOU 3428  CB  CYS A 460     9028   6189   5370   -160   1943    719       C  
ATOM   3429  SG  CYS A 460      46.832  -5.929 -42.816  1.00 54.08           S  
ANISOU 3429  SG  CYS A 460     8799   6248   5500   -242   1928    631       S  
ATOM   3430  N   ARG A 461      49.439  -4.233 -46.045  1.00 52.55           N  
ANISOU 3430  N   ARG A 461     8836   5954   5174   -385   2359    660       N  
ATOM   3431  CA  ARG A 461      50.369  -4.862 -46.979  1.00 60.47           C  
ANISOU 3431  CA  ARG A 461     9820   7021   6133   -410   2459    618       C  
ATOM   3432  C   ARG A 461      51.257  -5.902 -46.317  1.00 55.08           C  
ANISOU 3432  C   ARG A 461     8936   6437   5553   -475   2484    515       C  
ATOM   3433  O   ARG A 461      51.392  -5.935 -45.092  1.00 51.61           O  
ANISOU 3433  O   ARG A 461     8366   6006   5236   -531   2454    474       O  
ATOM   3434  CB  ARG A 461      51.216  -3.817 -47.703  1.00 73.92           C  
ANISOU 3434  CB  ARG A 461    11607   8651   7828   -488   2621    640       C  
ATOM   3435  CG  ARG A 461      52.470  -3.394 -46.963  1.00 82.85           C  
ANISOU 3435  CG  ARG A 461    12599   9770   9110   -640   2743    572       C  
ATOM   3436  CD  ARG A 461      53.087  -2.175 -47.633  1.00 89.34           C  
ANISOU 3436  CD  ARG A 461    13532  10495   9918   -711   2892    608       C  
ATOM   3437  NE  ARG A 461      52.115  -1.090 -47.697  1.00 93.60           N  
ANISOU 3437  NE  ARG A 461    14239  10921  10405   -655   2848    699       N  
ATOM   3438  CZ  ARG A 461      51.887  -0.236 -46.706  1.00 96.79           C  
ANISOU 3438  CZ  ARG A 461    14626  11249  10901   -697   2828    705       C  
ATOM   3439  NH1 ARG A 461      52.574  -0.327 -45.576  1.00 96.46           N1+
ANISOU 3439  NH1 ARG A 461    14409  11235  11006   -802   2846    625       N1+
ATOM   3440  NH2 ARG A 461      50.976   0.716 -46.845  1.00 99.94           N  
ANISOU 3440  NH2 ARG A 461    15181  11547  11244   -632   2788    786       N  
ATOM   3441  N   GLU A 462      51.862  -6.747 -47.146  1.00 53.52           N  
ANISOU 3441  N   GLU A 462     8716   6317   5303   -464   2538    470       N  
ATOM   3442  CA  GLU A 462      52.633  -7.886 -46.672  1.00 56.34           C  
ANISOU 3442  CA  GLU A 462     8888   6779   5740   -498   2551    368       C  
ATOM   3443  C   GLU A 462      53.669  -7.512 -45.612  1.00 61.15           C  
ANISOU 3443  C   GLU A 462     9326   7386   6520   -629   2627    302       C  
ATOM   3444  O   GLU A 462      53.902  -8.276 -44.680  1.00 65.12           O  
ANISOU 3444  O   GLU A 462     9667   7957   7118   -644   2581    231       O  
ATOM   3445  CB  GLU A 462      53.283  -8.629 -47.842  1.00 59.22           C  
ANISOU 3445  CB  GLU A 462     9263   7213   6025   -476   2627    328       C  
ATOM   3446  CG  GLU A 462      54.234  -7.788 -48.688  1.00 74.25           C  
ANISOU 3446  CG  GLU A 462    11222   9074   7914   -554   2792    342       C  
ATOM   3447  CD  GLU A 462      53.528  -6.798 -49.621  1.00 81.17           C  
ANISOU 3447  CD  GLU A 462    12323   9857   8663   -507   2799    450       C  
ATOM   3448  OE1 GLU A 462      52.277  -6.792 -49.684  1.00 80.98           O  
ANISOU 3448  OE1 GLU A 462    12406   9806   8554   -403   2668    513       O  
ATOM   3449  OE2 GLU A 462      54.235  -6.017 -50.293  1.00 82.76           O1-
ANISOU 3449  OE2 GLU A 462    12589  10008   8847   -571   2937    470       O1-
ATOM   3450  N   GLU A 463      54.257  -6.325 -45.730  1.00 59.45           N  
ANISOU 3450  N   GLU A 463     9150   7093   6344   -720   2737    323       N  
ATOM   3451  CA  GLU A 463      55.273  -5.885 -44.777  1.00 59.43           C  
ANISOU 3451  CA  GLU A 463     8988   7089   6502   -849   2808    253       C  
ATOM   3452  C   GLU A 463      54.674  -5.535 -43.404  1.00 56.60           C  
ANISOU 3452  C   GLU A 463     8574   6697   6235   -863   2708    257       C  
ATOM   3453  O   GLU A 463      55.262  -5.824 -42.359  1.00 52.04           O  
ANISOU 3453  O   GLU A 463     7816   6170   5787   -929   2697    177       O  
ATOM   3454  CB  GLU A 463      56.061  -4.699 -45.342  1.00 67.20           C  
ANISOU 3454  CB  GLU A 463    10041   7994   7497   -943   2958    269       C  
ATOM   3455  CG  GLU A 463      56.331  -4.768 -46.852  1.00 76.97           C  
ANISOU 3455  CG  GLU A 463    11405   9235   8608   -912   3053    302       C  
ATOM   3456  CD  GLU A 463      57.246  -5.922 -47.259  1.00 87.66           C  
ANISOU 3456  CD  GLU A 463    12626  10708   9972   -918   3105    214       C  
ATOM   3457  OE1 GLU A 463      57.818  -6.581 -46.362  1.00 92.19           O  
ANISOU 3457  OE1 GLU A 463    13001  11360  10667   -956   3081    123       O  
ATOM   3458  OE2 GLU A 463      57.399  -6.168 -48.481  1.00 86.80           O1-
ANISOU 3458  OE2 GLU A 463    12612  10618   9751   -878   3168    234       O1-
ATOM   3459  N   VAL A 464      53.505  -4.906 -43.424  1.00 52.43           N  
ANISOU 3459  N   VAL A 464     8198   6086   5636   -798   2632    349       N  
ATOM   3460  CA  VAL A 464      52.767  -4.568 -42.215  1.00 45.55           C  
ANISOU 3460  CA  VAL A 464     7299   5179   4831   -794   2530    364       C  
ATOM   3461  C   VAL A 464      52.239  -5.839 -41.547  1.00 46.73           C  
ANISOU 3461  C   VAL A 464     7345   5419   4992   -729   2406    331       C  
ATOM   3462  O   VAL A 464      52.315  -6.005 -40.330  1.00 48.84           O  
ANISOU 3462  O   VAL A 464     7479   5712   5368   -771   2358    284       O  
ATOM   3463  CB  VAL A 464      51.607  -3.630 -42.571  1.00 44.27           C  
ANISOU 3463  CB  VAL A 464     7333   4910   4577   -720   2479    471       C  
ATOM   3464  CG1 VAL A 464      50.549  -3.615 -41.484  1.00 41.35           C  
ANISOU 3464  CG1 VAL A 464     6947   4524   4241   -673   2341    494       C  
ATOM   3465  CG2 VAL A 464      52.139  -2.240 -42.842  1.00 46.77           C  
ANISOU 3465  CG2 VAL A 464     7733   5122   4918   -802   2599    493       C  
ATOM   3466  N   LEU A 465      51.714  -6.742 -42.364  1.00 54.09           N  
ANISOU 3466  N   LEU A 465     8342   6401   5809   -625   2355    351       N  
ATOM   3467  CA  LEU A 465      51.298  -8.066 -41.913  1.00 51.35           C  
ANISOU 3467  CA  LEU A 465     7907   6143   5460   -559   2253    311       C  
ATOM   3468  C   LEU A 465      52.448  -8.829 -41.253  1.00 46.58           C  
ANISOU 3468  C   LEU A 465     7091   5627   4979   -633   2303    199       C  
ATOM   3469  O   LEU A 465      52.284  -9.407 -40.179  1.00 41.73           O  
ANISOU 3469  O   LEU A 465     6357   5057   4443   -633   2230    157       O  
ATOM   3470  CB  LEU A 465      50.769  -8.867 -43.105  1.00 52.74           C  
ANISOU 3470  CB  LEU A 465     8193   6359   5488   -446   2215    335       C  
ATOM   3471  CG  LEU A 465      49.498  -9.668 -42.863  1.00 52.26           C  
ANISOU 3471  CG  LEU A 465     8171   6325   5360   -331   2058    358       C  
ATOM   3472  CD1 LEU A 465      48.583  -8.860 -41.982  1.00 51.98           C  
ANISOU 3472  CD1 LEU A 465     8174   6219   5359   -325   1974    421       C  
ATOM   3473  CD2 LEU A 465      48.814  -9.993 -44.175  1.00 46.73           C  
ANISOU 3473  CD2 LEU A 465     7623   5634   4497   -220   2011    400       C  
ATOM   3474  N   LYS A 466      53.611  -8.831 -41.901  1.00 48.19           N  
ANISOU 3474  N   LYS A 466     7245   5862   5203   -691   2424    148       N  
ATOM   3475  CA  LYS A 466      54.797  -9.467 -41.336  1.00 48.36           C  
ANISOU 3475  CA  LYS A 466     7054   5971   5349   -757   2472     34       C  
ATOM   3476  C   LYS A 466      55.257  -8.786 -40.043  1.00 45.65           C  
ANISOU 3476  C   LYS A 466     6581   5610   5155   -860   2472     -5       C  
ATOM   3477  O   LYS A 466      55.736  -9.448 -39.126  1.00 46.55           O  
ANISOU 3477  O   LYS A 466     6511   5799   5376   -882   2436    -90       O  
ATOM   3478  CB  LYS A 466      55.933  -9.537 -42.363  1.00 56.13           C  
ANISOU 3478  CB  LYS A 466     8018   6989   6319   -795   2604     -9       C  
ATOM   3479  CG  LYS A 466      55.784 -10.696 -43.352  1.00 68.95           C  
ANISOU 3479  CG  LYS A 466     9683   8680   7835   -695   2593    -25       C  
ATOM   3480  CD  LYS A 466      56.973 -10.817 -44.306  1.00 77.90           C  
ANISOU 3480  CD  LYS A 466    10779   9856   8963   -735   2727    -76       C  
ATOM   3481  CE  LYS A 466      56.756 -10.038 -45.606  1.00 82.41           C  
ANISOU 3481  CE  LYS A 466    11555  10357   9401   -725   2802     10       C  
ATOM   3482  NZ  LYS A 466      55.654 -10.601 -46.444  1.00 83.60           N1+
ANISOU 3482  NZ  LYS A 466    11866  10509   9390   -598   2719     68       N1+
ATOM   3483  N   ASN A 467      55.097  -7.470 -39.962  1.00 40.10           N  
ANISOU 3483  N   ASN A 467     5972   4805   4458   -916   2505     51       N  
ATOM   3484  CA  ASN A 467      55.413  -6.753 -38.729  1.00 41.66           C  
ANISOU 3484  CA  ASN A 467     6066   4978   4787  -1008   2494     14       C  
ATOM   3485  C   ASN A 467      54.544  -7.154 -37.519  1.00 42.16           C  
ANISOU 3485  C   ASN A 467     6073   5057   4889   -969   2359     18       C  
ATOM   3486  O   ASN A 467      55.055  -7.358 -36.413  1.00 41.85           O  
ANISOU 3486  O   ASN A 467     5861   5069   4970  -1024   2328    -60       O  
ATOM   3487  CB  ASN A 467      55.336  -5.247 -38.953  1.00 41.86           C  
ANISOU 3487  CB  ASN A 467     6226   4880   4800  -1066   2559     73       C  
ATOM   3488  CG  ASN A 467      55.426  -4.468 -37.660  1.00 48.10           C  
ANISOU 3488  CG  ASN A 467     6937   5632   5707  -1145   2530     41       C  
ATOM   3489  ND2 ASN A 467      54.274  -4.078 -37.111  1.00 42.50           N  
ANISOU 3489  ND2 ASN A 467     6316   4860   4972  -1097   2437    107       N  
ATOM   3490  OD1 ASN A 467      56.519  -4.227 -37.153  1.00 56.49           O  
ANISOU 3490  OD1 ASN A 467     7858   6725   6882  -1246   2585    -47       O  
ATOM   3491  N   PHE A 468      53.235  -7.244 -37.729  1.00 41.75           N  
ANISOU 3491  N   PHE A 468     6166   4962   4734   -872   2275    107       N  
ATOM   3492  CA  PHE A 468      52.302  -7.662 -36.678  1.00 37.40           C  
ANISOU 3492  CA  PHE A 468     5579   4424   4207   -824   2141    119       C  
ATOM   3493  C   PHE A 468      52.597  -9.109 -36.289  1.00 34.80           C  
ANISOU 3493  C   PHE A 468     5074   4211   3937   -765   2024     35       C  
ATOM   3494  O   PHE A 468      52.628  -9.456 -35.118  1.00 34.99           O  
ANISOU 3494  O   PHE A 468     4956   4276   4062   -767   1914    -14       O  
ATOM   3495  CB  PHE A 468      50.864  -7.493 -37.189  1.00 36.04           C  
ANISOU 3495  CB  PHE A 468     5596   4188   3908   -712   2051    227       C  
ATOM   3496  CG  PHE A 468      49.821  -8.274 -36.425  1.00 35.83           C  
ANISOU 3496  CG  PHE A 468     5513   4198   3903   -610   1839    228       C  
ATOM   3497  CD1 PHE A 468      49.053  -7.664 -35.456  1.00 30.39           C  
ANISOU 3497  CD1 PHE A 468     4833   3458   3256   -608   1753    261       C  
ATOM   3498  CD2 PHE A 468      49.559  -9.598 -36.735  1.00 36.33           C  
ANISOU 3498  CD2 PHE A 468     5526   4340   3936   -516   1732    199       C  
ATOM   3499  CE1 PHE A 468      48.074  -8.365 -34.795  1.00 34.29           C  
ANISOU 3499  CE1 PHE A 468     5280   3985   3764   -519   1572    265       C  
ATOM   3500  CE2 PHE A 468      48.585 -10.306 -36.064  1.00 33.52           C  
ANISOU 3500  CE2 PHE A 468     5126   4010   3600   -432   1550    202       C  
ATOM   3501  CZ  PHE A 468      47.840  -9.689 -35.096  1.00 33.87           C  
ANISOU 3501  CZ  PHE A 468     5175   4008   3687   -435   1472    236       C  
ATOM   3502  N   THR A 469      52.828  -9.937 -37.300  1.00 34.29           N  
ANISOU 3502  N   THR A 469     5031   4197   3802   -709   2053     20       N  
ATOM   3503  CA  THR A 469      53.177 -11.341 -37.124  1.00 38.19           C  
ANISOU 3503  CA  THR A 469     5376   4791   4341   -647   1963    -59       C  
ATOM   3504  C   THR A 469      54.468 -11.537 -36.308  1.00 39.33           C  
ANISOU 3504  C   THR A 469     5306   5007   4630   -728   2004   -167       C  
ATOM   3505  O   THR A 469      54.513 -12.371 -35.405  1.00 47.38           O  
ANISOU 3505  O   THR A 469     6184   6087   5730   -685   1873   -220       O  
ATOM   3506  CB  THR A 469      53.252 -12.059 -38.512  1.00 35.00           C  
ANISOU 3506  CB  THR A 469     5056   4418   3824   -580   2016    -58       C  
ATOM   3507  CG2 THR A 469      54.540 -12.837 -38.687  1.00 35.18           C  
ANISOU 3507  CG2 THR A 469     4924   4530   3912   -605   2092   -164       C  
ATOM   3508  OG1 THR A 469      52.140 -12.953 -38.646  1.00 38.32           O  
ANISOU 3508  OG1 THR A 469     5529   4850   4183   -456   1850    -30       O  
ATOM   3509  N   ASP A 470      55.505 -10.761 -36.614  1.00 33.85           N  
ANISOU 3509  N   ASP A 470     4590   4306   3967   -843   2184   -199       N  
ATOM   3510  CA  ASP A 470      56.768 -10.854 -35.888  1.00 35.90           C  
ANISOU 3510  CA  ASP A 470     4638   4639   4364   -927   2230   -310       C  
ATOM   3511  C   ASP A 470      56.567 -10.485 -34.422  1.00 38.41           C  
ANISOU 3511  C   ASP A 470     4860   4950   4783   -959   2118   -328       C  
ATOM   3512  O   ASP A 470      57.086 -11.149 -33.527  1.00 42.72           O  
ANISOU 3512  O   ASP A 470     5226   5578   5428   -947   2030   -409       O  
ATOM   3513  CB  ASP A 470      57.826  -9.946 -36.520  1.00 39.30           C  
ANISOU 3513  CB  ASP A 470     5074   5045   4814  -1034   2396   -333       C  
ATOM   3514  CG  ASP A 470      58.288 -10.447 -37.884  1.00 50.82           C  
ANISOU 3514  CG  ASP A 470     6583   6533   6193   -996   2485   -338       C  
ATOM   3515  OD1 ASP A 470      58.038 -11.631 -38.210  1.00 52.90           O  
ANISOU 3515  OD1 ASP A 470     6831   6859   6411   -902   2445   -358       O  
ATOM   3516  OD2 ASP A 470      58.906  -9.655 -38.629  1.00 57.04           O1-
ANISOU 3516  OD2 ASP A 470     7430   7278   6964  -1061   2597   -326       O1-
ATOM   3517  N   GLN A 471      55.795  -9.429 -34.196  1.00 31.60           N  
ANISOU 3517  N   GLN A 471     4129   3990   3889   -994   2120   -250       N  
ATOM   3518  CA  GLN A 471      55.507  -8.941 -32.857  1.00 34.41           C  
ANISOU 3518  CA  GLN A 471     4423   4327   4325  -1027   2025   -259       C  
ATOM   3519  C   GLN A 471      54.717  -9.959 -32.037  1.00 35.43           C  
ANISOU 3519  C   GLN A 471     4495   4501   4465   -911   1814   -255       C  
ATOM   3520  O   GLN A 471      55.072 -10.265 -30.900  1.00 31.91           O  
ANISOU 3520  O   GLN A 471     3897   4113   4114   -920   1726   -320       O  
ATOM   3521  CB  GLN A 471      54.730  -7.631 -32.944  1.00 41.34           C  
ANISOU 3521  CB  GLN A 471     5479   5079   5151  -1070   2076   -168       C  
ATOM   3522  CG  GLN A 471      55.580  -6.448 -33.330  1.00 50.17           C  
ANISOU 3522  CG  GLN A 471     6628   6137   6295  -1181   2218   -184       C  
ATOM   3523  CD  GLN A 471      56.746  -6.281 -32.388  1.00 61.38           C  
ANISOU 3523  CD  GLN A 471     7849   7618   7854  -1276   2222   -300       C  
ATOM   3524  NE2 GLN A 471      56.453  -6.212 -31.097  1.00 66.45           N  
ANISOU 3524  NE2 GLN A 471     8407   8274   8565  -1291   2126   -329       N  
ATOM   3525  OE1 GLN A 471      57.899  -6.229 -32.811  1.00 70.40           O  
ANISOU 3525  OE1 GLN A 471     8911   8799   9039  -1331   2306   -367       O  
ATOM   3526  N   LEU A 472      53.641 -10.464 -32.624  1.00 34.31           N  
ANISOU 3526  N   LEU A 472     4481   4333   4225   -803   1736   -179       N  
ATOM   3527  CA  LEU A 472      52.826 -11.493 -32.009  1.00 30.29           C  
ANISOU 3527  CA  LEU A 472     3933   3857   3717   -694   1550   -170       C  
ATOM   3528  C   LEU A 472      53.655 -12.716 -31.620  1.00 29.50           C  
ANISOU 3528  C   LEU A 472     3657   3861   3691   -659   1493   -261       C  
ATOM   3529  O   LEU A 472      53.485 -13.290 -30.547  1.00 31.01           O  
ANISOU 3529  O   LEU A 472     3752   4090   3942   -620   1360   -286       O  
ATOM   3530  CB  LEU A 472      51.730 -11.917 -32.980  1.00 32.06           C  
ANISOU 3530  CB  LEU A 472     4313   4047   3821   -593   1503    -93       C  
ATOM   3531  CG  LEU A 472      50.751 -12.912 -32.374  1.00 32.66           C  
ANISOU 3531  CG  LEU A 472     4365   4145   3898   -490   1318    -79       C  
ATOM   3532  CD1 LEU A 472      50.272 -12.393 -31.011  1.00 23.67           C  
ANISOU 3532  CD1 LEU A 472     3186   2985   2825   -516   1233    -67       C  
ATOM   3533  CD2 LEU A 472      49.586 -13.151 -33.314  1.00 24.20           C  
ANISOU 3533  CD2 LEU A 472     3449   3036   2710   -403   1272     -6       C  
ATOM   3534  N   ARG A 473      54.555 -13.111 -32.503  1.00 28.75           N  
ANISOU 3534  N   ARG A 473     3525   3810   3588   -667   1596   -310       N  
ATOM   3535  CA  ARG A 473      55.395 -14.260 -32.243  1.00 29.63           C  
ANISOU 3535  CA  ARG A 473     3473   4017   3768   -625   1552   -399       C  
ATOM   3536  C   ARG A 473      56.354 -14.054 -31.076  1.00 35.85           C  
ANISOU 3536  C   ARG A 473     4077   4864   4680   -690   1541   -483       C  
ATOM   3537  O   ARG A 473      56.577 -14.972 -30.296  1.00 39.19           O  
ANISOU 3537  O   ARG A 473     4377   5352   5163   -628   1423   -531       O  
ATOM   3538  CB  ARG A 473      56.156 -14.640 -33.501  1.00 29.68           C  
ANISOU 3538  CB  ARG A 473     3485   4057   3736   -622   1681   -436       C  
ATOM   3539  CG  ARG A 473      55.274 -15.341 -34.499  1.00 36.53           C  
ANISOU 3539  CG  ARG A 473     4493   4898   4489   -521   1641   -379       C  
ATOM   3540  CD  ARG A 473      55.984 -15.493 -35.822  1.00 39.51           C  
ANISOU 3540  CD  ARG A 473     4905   5299   4809   -530   1791   -408       C  
ATOM   3541  NE  ARG A 473      57.091 -16.431 -35.739  1.00 45.40           N  
ANISOU 3541  NE  ARG A 473     5481   6137   5633   -507   1805   -514       N  
ATOM   3542  CZ  ARG A 473      58.122 -16.428 -36.573  1.00 59.28           C  
ANISOU 3542  CZ  ARG A 473     7198   7937   7389   -545   1961   -572       C  
ATOM   3543  NH1 ARG A 473      58.184 -15.523 -37.546  1.00 61.99           N1+
ANISOU 3543  NH1 ARG A 473     7669   8234   7650   -615   2122   -530       N1+
ATOM   3544  NH2 ARG A 473      59.094 -17.321 -36.429  1.00 66.45           N  
ANISOU 3544  NH2 ARG A 473     7941   8933   8376   -512   1960   -673       N  
ATOM   3545  N   LYS A 474      56.934 -12.863 -30.964  1.00 28.52           N  
ANISOU 3545  N   LYS A 474     3133   3914   3790   -815   1662   -503       N  
ATOM   3546  CA  LYS A 474      57.819 -12.576 -29.850  1.00 40.98           C  
ANISOU 3546  CA  LYS A 474     4537   5551   5485   -885   1647   -592       C  
ATOM   3547  C   LYS A 474      57.025 -12.665 -28.554  1.00 37.82           C  
ANISOU 3547  C   LYS A 474     4125   5140   5105   -842   1477   -565       C  
ATOM   3548  O   LYS A 474      57.457 -13.289 -27.590  1.00 40.86           O  
ANISOU 3548  O   LYS A 474     4364   5601   5560   -808   1373   -627       O  
ATOM   3549  CB  LYS A 474      58.427 -11.183 -29.971  1.00 45.33           C  
ANISOU 3549  CB  LYS A 474     5094   6060   6068  -1038   1810   -613       C  
ATOM   3550  CG  LYS A 474      59.399 -10.859 -28.846  1.00 53.91           C  
ANISOU 3550  CG  LYS A 474     5989   7216   7279  -1120   1797   -721       C  
ATOM   3551  CD  LYS A 474      59.427  -9.371 -28.510  1.00 63.23           C  
ANISOU 3551  CD  LYS A 474     7218   8320   8488  -1260   1891   -716       C  
ATOM   3552  CE  LYS A 474      58.139  -8.933 -27.807  1.00 64.17           C  
ANISOU 3552  CE  LYS A 474     7463   8356   8562  -1225   1778   -629       C  
ATOM   3553  NZ  LYS A 474      58.311  -7.696 -26.984  1.00 58.94           N1+
ANISOU 3553  NZ  LYS A 474     6785   7648   7960  -1347   1816   -661       N1+
ATOM   3554  N   ILE A 475      55.851 -12.047 -28.555  1.00 31.16           N  
ANISOU 3554  N   ILE A 475     3440   4204   4195   -837   1451   -470       N  
ATOM   3555  CA  ILE A 475      54.988 -12.026 -27.380  1.00 33.22           C  
ANISOU 3555  CA  ILE A 475     3708   4446   4466   -802   1306   -438       C  
ATOM   3556  C   ILE A 475      54.467 -13.413 -27.018  1.00 32.72           C  
ANISOU 3556  C   ILE A 475     3614   4427   4391   -673   1148   -426       C  
ATOM   3557  O   ILE A 475      54.534 -13.813 -25.857  1.00 30.14           O  
ANISOU 3557  O   ILE A 475     3190   4146   4117   -647   1035   -458       O  
ATOM   3558  CB  ILE A 475      53.836 -11.033 -27.568  1.00 29.19           C  
ANISOU 3558  CB  ILE A 475     3377   3826   3887   -819   1324   -341       C  
ATOM   3559  CG1 ILE A 475      54.406  -9.619 -27.643  1.00 35.51           C  
ANISOU 3559  CG1 ILE A 475     4200   4575   4718   -954   1471   -360       C  
ATOM   3560  CG2 ILE A 475      52.843 -11.145 -26.434  1.00 23.97           C  
ANISOU 3560  CG2 ILE A 475     2728   3152   3230   -768   1174   -306       C  
ATOM   3561  CD1 ILE A 475      53.363  -8.534 -27.677  1.00 42.37           C  
ANISOU 3561  CD1 ILE A 475     5237   5330   5533   -973   1490   -272       C  
ATOM   3562  N   SER A 476      53.985 -14.151 -28.017  1.00 24.38           N  
ANISOU 3562  N   SER A 476     2642   3356   3264   -595   1144   -383       N  
ATOM   3563  CA  SER A 476      53.447 -15.490 -27.796  1.00 27.41           C  
ANISOU 3563  CA  SER A 476     3013   3767   3636   -479   1007   -371       C  
ATOM   3564  C   SER A 476      54.519 -16.429 -27.224  1.00 32.08           C  
ANISOU 3564  C   SER A 476     3431   4451   4307   -445    960   -460       C  
ATOM   3565  O   SER A 476      54.251 -17.217 -26.316  1.00 28.67           O  
ANISOU 3565  O   SER A 476     2948   4043   3901   -378    828   -462       O  
ATOM   3566  CB  SER A 476      52.858 -16.065 -29.098  1.00 29.93           C  
ANISOU 3566  CB  SER A 476     3452   4055   3867   -412   1027   -325       C  
ATOM   3567  OG  SER A 476      53.870 -16.507 -29.994  1.00 27.17           O  
ANISOU 3567  OG  SER A 476     3050   3752   3521   -412   1122   -384       O  
ATOM   3568  N   LYS A 477      55.735 -16.336 -27.754  1.00 30.07           N  
ANISOU 3568  N   LYS A 477     3087   4248   4092   -490   1071   -534       N  
ATOM   3569  CA  LYS A 477      56.851 -17.130 -27.239  1.00 29.13           C  
ANISOU 3569  CA  LYS A 477     2790   4225   4055   -457   1034   -628       C  
ATOM   3570  C   LYS A 477      57.144 -16.805 -25.775  1.00 33.42           C  
ANISOU 3570  C   LYS A 477     3222   4809   4669   -486    949   -666       C  
ATOM   3571  O   LYS A 477      57.451 -17.708 -24.983  1.00 31.72           O  
ANISOU 3571  O   LYS A 477     2905   4652   4495   -410    835   -704       O  
ATOM   3572  CB  LYS A 477      58.105 -16.904 -28.090  1.00 34.21           C  
ANISOU 3572  CB  LYS A 477     3351   4918   4730   -516   1188   -707       C  
ATOM   3573  CG  LYS A 477      59.350 -17.683 -27.647  1.00 39.67           C  
ANISOU 3573  CG  LYS A 477     3842   5718   5512   -477   1159   -816       C  
ATOM   3574  CD  LYS A 477      60.584 -17.219 -28.428  1.00 47.07           C  
ANISOU 3574  CD  LYS A 477     4688   6706   6490   -562   1331   -899       C  
ATOM   3575  CE  LYS A 477      61.793 -18.123 -28.189  1.00 50.85           C  
ANISOU 3575  CE  LYS A 477     4969   7299   7054   -502   1306  -1012       C  
ATOM   3576  NZ  LYS A 477      63.040 -17.592 -28.817  1.00 53.64           N1+
ANISOU 3576  NZ  LYS A 477     5207   7712   7463   -598   1477  -1105       N1+
ATOM   3577  N   ASP A 478      57.038 -15.525 -25.413  1.00 29.54           N  
ANISOU 3577  N   ASP A 478     2757   4280   4185   -592   1003   -657       N  
ATOM   3578  CA  ASP A 478      57.262 -15.107 -24.027  1.00 36.40           C  
ANISOU 3578  CA  ASP A 478     3533   5185   5112   -628    925   -697       C  
ATOM   3579  C   ASP A 478      56.202 -15.663 -23.082  1.00 33.44           C  
ANISOU 3579  C   ASP A 478     3212   4788   4706   -543    765   -634       C  
ATOM   3580  O   ASP A 478      56.449 -15.815 -21.895  1.00 36.32           O  
ANISOU 3580  O   ASP A 478     3486   5204   5111   -528    667   -671       O  
ATOM   3581  CB  ASP A 478      57.310 -13.582 -23.896  1.00 41.58           C  
ANISOU 3581  CB  ASP A 478     4224   5793   5782   -764   1025   -701       C  
ATOM   3582  CG  ASP A 478      58.507 -12.970 -24.609  1.00 57.91           C  
ANISOU 3582  CG  ASP A 478     6214   7890   7899   -869   1188   -779       C  
ATOM   3583  OD1 ASP A 478      59.480 -13.708 -24.890  1.00 60.72           O  
ANISOU 3583  OD1 ASP A 478     6441   8332   8299   -839   1205   -854       O  
ATOM   3584  OD2 ASP A 478      58.476 -11.748 -24.886  1.00 64.36           O1-
ANISOU 3584  OD2 ASP A 478     7099   8641   8712   -983   1305   -766       O1-
ATOM   3585  N   ALA A 479      55.028 -15.968 -23.620  1.00 32.46           N  
ANISOU 3585  N   ALA A 479     3235   4591   4508   -489    741   -542       N  
ATOM   3586  CA  ALA A 479      53.912 -16.452 -22.817  1.00 31.50           C  
ANISOU 3586  CA  ALA A 479     3175   4439   4355   -419    606   -477       C  
ATOM   3587  C   ALA A 479      53.840 -17.975 -22.751  1.00 26.33           C  
ANISOU 3587  C   ALA A 479     2492   3815   3698   -299    505   -474       C  
ATOM   3588  O   ALA A 479      52.940 -18.524 -22.135  1.00 27.63           O  
ANISOU 3588  O   ALA A 479     2707   3954   3839   -240    400   -422       O  
ATOM   3589  CB  ALA A 479      52.603 -15.897 -23.364  1.00 28.72           C  
ANISOU 3589  CB  ALA A 479     2991   3993   3930   -428    630   -384       C  
ATOM   3590  N   GLY A 480      54.770 -18.654 -23.405  1.00 27.69           N  
ANISOU 3590  N   GLY A 480     2588   4036   3896   -266    545   -532       N  
ATOM   3591  CA  GLY A 480      54.764 -20.104 -23.427  1.00 30.91           C  
ANISOU 3591  CA  GLY A 480     2976   4463   4306   -151    459   -534       C  
ATOM   3592  C   GLY A 480      53.855 -20.712 -24.480  1.00 32.89           C  
ANISOU 3592  C   GLY A 480     3356   4648   4492   -100    467   -474       C  
ATOM   3593  O   GLY A 480      53.587 -21.920 -24.452  1.00 31.13           O  
ANISOU 3593  O   GLY A 480     3144   4419   4265     -7    388   -464       O  
ATOM   3594  N   MET A 481      53.389 -19.880 -25.413  1.00 28.26           N  
ANISOU 3594  N   MET A 481     2871   4012   3853   -160    562   -437       N  
ATOM   3595  CA  MET A 481      52.493 -20.313 -26.480  1.00 24.23           C  
ANISOU 3595  CA  MET A 481     2490   3446   3271   -117    571   -385       C  
ATOM   3596  C   MET A 481      53.146 -19.976 -27.808  1.00 28.92           C  
ANISOU 3596  C   MET A 481     3102   4049   3838   -152    709   -416       C  
ATOM   3597  O   MET A 481      52.626 -19.152 -28.554  1.00 30.50           O  
ANISOU 3597  O   MET A 481     3412   4201   3976   -197    783   -369       O  
ATOM   3598  CB  MET A 481      51.154 -19.574 -26.381  1.00 23.76           C  
ANISOU 3598  CB  MET A 481     2556   3316   3155   -145    547   -302       C  
ATOM   3599  CG  MET A 481      50.059 -20.087 -27.323  1.00 20.63           C  
ANISOU 3599  CG  MET A 481     2285   2867   2684    -91    524   -249       C  
ATOM   3600  SD  MET A 481      48.669 -18.956 -27.527  1.00 26.64           S  
ANISOU 3600  SD  MET A 481     3189   3556   3376   -128    530   -162       S  
ATOM   3601  CE  MET A 481      49.325 -17.723 -28.661  1.00 20.56           C  
ANISOU 3601  CE  MET A 481     2474   2775   2565   -203    696   -166       C  
ATOM   3602  N   PRO A 482      54.302 -20.594 -28.101  1.00 29.47           N  
ANISOU 3602  N   PRO A 482     3065   4181   3951   -127    750   -493       N  
ATOM   3603  CA  PRO A 482      55.059 -20.147 -29.275  1.00 33.98           C  
ANISOU 3603  CA  PRO A 482     3640   4769   4502   -175    902   -530       C  
ATOM   3604  C   PRO A 482      54.338 -20.435 -30.593  1.00 34.60           C  
ANISOU 3604  C   PRO A 482     3864   4799   4483   -139    940   -486       C  
ATOM   3605  O   PRO A 482      53.904 -21.557 -30.863  1.00 27.60           O  
ANISOU 3605  O   PRO A 482     3008   3902   3574    -49    865   -484       O  
ATOM   3606  CB  PRO A 482      56.364 -20.947 -29.183  1.00 35.30           C  
ANISOU 3606  CB  PRO A 482     3649   5020   4744   -135    913   -628       C  
ATOM   3607  CG  PRO A 482      55.997 -22.188 -28.413  1.00 33.74           C  
ANISOU 3607  CG  PRO A 482     3424   4824   4570    -27    758   -622       C  
ATOM   3608  CD  PRO A 482      54.921 -21.769 -27.448  1.00 31.31           C  
ANISOU 3608  CD  PRO A 482     3181   4467   4247    -44    662   -548       C  
ATOM   3609  N   ILE A 483      54.173 -19.385 -31.382  1.00 37.37           N  
ANISOU 3609  N   ILE A 483     4312   5114   4774   -209   1053   -450       N  
ATOM   3610  CA  ILE A 483      53.693 -19.512 -32.741  1.00 37.97           C  
ANISOU 3610  CA  ILE A 483     4523   5157   4748   -181   1110   -418       C  
ATOM   3611  C   ILE A 483      54.943 -19.681 -33.586  1.00 39.15           C  
ANISOU 3611  C   ILE A 483     4608   5360   4907   -198   1245   -493       C  
ATOM   3612  O   ILE A 483      55.713 -18.737 -33.740  1.00 41.73           O  
ANISOU 3612  O   ILE A 483     4902   5700   5253   -290   1374   -514       O  
ATOM   3613  CB  ILE A 483      52.916 -18.258 -33.167  1.00 34.26           C  
ANISOU 3613  CB  ILE A 483     4199   4620   4200   -239   1168   -337       C  
ATOM   3614  CG1 ILE A 483      51.696 -18.078 -32.261  1.00 31.40           C  
ANISOU 3614  CG1 ILE A 483     3883   4211   3838   -220   1036   -272       C  
ATOM   3615  CG2 ILE A 483      52.493 -18.361 -34.624  1.00 35.64           C  
ANISOU 3615  CG2 ILE A 483     4517   4768   4257   -205   1229   -306       C  
ATOM   3616  CD1 ILE A 483      51.054 -16.715 -32.361  1.00 33.12           C  
ANISOU 3616  CD1 ILE A 483     4215   4364   4006   -280   1085   -200       C  
ATOM   3617  N   GLN A 484      55.158 -20.891 -34.100  1.00 34.25           N  
ANISOU 3617  N   GLN A 484     3966   4769   4279   -112   1219   -538       N  
ATOM   3618  CA  GLN A 484      56.413 -21.222 -34.771  1.00 41.90           C  
ANISOU 3618  CA  GLN A 484     4848   5800   5271   -114   1336   -624       C  
ATOM   3619  C   GLN A 484      56.410 -20.888 -36.260  1.00 45.31           C  
ANISOU 3619  C   GLN A 484     5405   6215   5594   -133   1475   -609       C  
ATOM   3620  O   GLN A 484      55.412 -21.084 -36.957  1.00 45.92           O  
ANISOU 3620  O   GLN A 484     5633   6245   5571    -87   1438   -554       O  
ATOM   3621  CB  GLN A 484      56.771 -22.702 -34.563  1.00 46.85           C  
ANISOU 3621  CB  GLN A 484     5382   6468   5951     -6   1248   -689       C  
ATOM   3622  CG  GLN A 484      56.723 -23.184 -33.105  1.00 46.17           C  
ANISOU 3622  CG  GLN A 484     5190   6395   5959     32   1099   -696       C  
ATOM   3623  CD  GLN A 484      57.890 -22.694 -32.250  1.00 51.61           C  
ANISOU 3623  CD  GLN A 484     5706   7154   6751    -23   1134   -760       C  
ATOM   3624  NE2 GLN A 484      58.178 -23.420 -31.175  1.00 44.60           N  
ANISOU 3624  NE2 GLN A 484     4705   6300   5942     40   1015   -792       N  
ATOM   3625  OE1 GLN A 484      58.523 -21.682 -32.552  1.00 63.56           O  
ANISOU 3625  OE1 GLN A 484     7189   8688   8271   -121   1265   -781       O  
ATOM   3626  N   GLY A 485      57.534 -20.368 -36.736  1.00 47.92           N  
ANISOU 3626  N   GLY A 485     5674   6588   5945   -203   1637   -662       N  
ATOM   3627  CA  GLY A 485      57.728 -20.147 -38.160  1.00 45.02           C  
ANISOU 3627  CA  GLY A 485     5414   6216   5475   -218   1786   -659       C  
ATOM   3628  C   GLY A 485      56.672 -19.304 -38.852  1.00 45.55           C  
ANISOU 3628  C   GLY A 485     5690   6204   5412   -242   1813   -555       C  
ATOM   3629  O   GLY A 485      55.999 -18.479 -38.233  1.00 51.38           O  
ANISOU 3629  O   GLY A 485     6479   6891   6154   -285   1765   -485       O  
ATOM   3630  N   GLN A 486      56.520 -19.539 -40.149  1.00 41.26           N  
ANISOU 3630  N   GLN A 486     5271   5656   4751   -206   1886   -546       N  
ATOM   3631  CA  GLN A 486      55.684 -18.712 -41.008  1.00 45.41           C  
ANISOU 3631  CA  GLN A 486     6001   6116   5136   -222   1936   -453       C  
ATOM   3632  C   GLN A 486      54.331 -19.373 -41.178  1.00 34.26           C  
ANISOU 3632  C   GLN A 486     4701   4670   3645   -121   1772   -405       C  
ATOM   3633  O   GLN A 486      54.234 -20.590 -41.075  1.00 30.95           O  
ANISOU 3633  O   GLN A 486     4225   4280   3255    -40   1671   -458       O  
ATOM   3634  CB  GLN A 486      56.359 -18.527 -42.384  1.00 53.46           C  
ANISOU 3634  CB  GLN A 486     7099   7155   6058   -245   2124   -472       C  
ATOM   3635  CG  GLN A 486      57.831 -18.124 -42.320  1.00 65.27           C  
ANISOU 3635  CG  GLN A 486     8456   8702   7643   -341   2297   -546       C  
ATOM   3636  CD  GLN A 486      58.092 -16.939 -41.388  1.00 77.54           C  
ANISOU 3636  CD  GLN A 486     9950  10225   9286   -457   2337   -519       C  
ATOM   3637  NE2 GLN A 486      57.357 -15.848 -41.596  1.00 80.45           N  
ANISOU 3637  NE2 GLN A 486    10483  10511   9574   -502   2367   -418       N  
ATOM   3638  OE1 GLN A 486      58.951 -17.006 -40.498  1.00 78.01           O  
ANISOU 3638  OE1 GLN A 486     9819  10336   9486   -503   2337   -594       O  
ATOM   3639  N   PRO A 487      53.281 -18.580 -41.454  1.00 36.58           N  
ANISOU 3639  N   PRO A 487     5155   4900   3842   -123   1746   -309       N  
ATOM   3640  CA  PRO A 487      51.974 -19.208 -41.663  1.00 35.43           C  
ANISOU 3640  CA  PRO A 487     5107   4731   3624    -28   1590   -274       C  
ATOM   3641  C   PRO A 487      52.042 -20.140 -42.869  1.00 34.42           C  
ANISOU 3641  C   PRO A 487     5044   4637   3399     45   1612   -321       C  
ATOM   3642  O   PRO A 487      52.832 -19.893 -43.776  1.00 39.59           O  
ANISOU 3642  O   PRO A 487     5736   5313   3993     18   1768   -343       O  
ATOM   3643  CB  PRO A 487      51.057 -18.014 -41.954  1.00 33.41           C  
ANISOU 3643  CB  PRO A 487     5015   4410   3270    -48   1599   -168       C  
ATOM   3644  CG  PRO A 487      51.958 -16.993 -42.545  1.00 39.09           C  
ANISOU 3644  CG  PRO A 487     5781   5118   3952   -132   1799   -153       C  
ATOM   3645  CD  PRO A 487      53.258 -17.148 -41.794  1.00 40.37           C  
ANISOU 3645  CD  PRO A 487     5749   5328   4262   -203   1869   -235       C  
ATOM   3646  N   CYS A 488      51.266 -21.215 -42.862  1.00 32.70           N  
ANISOU 3646  N   CYS A 488     4833   4422   3171    131   1464   -344       N  
ATOM   3647  CA  CYS A 488      51.256 -22.139 -43.994  1.00 33.51           C  
ANISOU 3647  CA  CYS A 488     5002   4552   3179    203   1472   -397       C  
ATOM   3648  C   CYS A 488      50.479 -21.539 -45.160  1.00 34.68           C  
ANISOU 3648  C   CYS A 488     5350   4677   3149    226   1499   -334       C  
ATOM   3649  O   CYS A 488      50.617 -21.966 -46.299  1.00 35.26           O  
ANISOU 3649  O   CYS A 488     5509   4776   3113    270   1553   -369       O  
ATOM   3650  CB  CYS A 488      50.640 -23.485 -43.593  1.00 32.29           C  
ANISOU 3650  CB  CYS A 488     4795   4398   3075    281   1304   -446       C  
ATOM   3651  SG  CYS A 488      48.889 -23.402 -43.039  1.00 39.83           S  
ANISOU 3651  SG  CYS A 488     5821   5302   4012    313   1110   -372       S  
ATOM   3652  N   PHE A 489      49.670 -20.530 -44.863  1.00 37.15           N  
ANISOU 3652  N   PHE A 489     5741   4943   3431    203   1461   -241       N  
ATOM   3653  CA  PHE A 489      48.719 -20.003 -45.821  1.00 35.02           C  
ANISOU 3653  CA  PHE A 489     5661   4648   2997    246   1444   -173       C  
ATOM   3654  C   PHE A 489      48.419 -18.565 -45.435  1.00 38.53           C  
ANISOU 3654  C   PHE A 489     6170   5038   3434    191   1484    -72       C  
ATOM   3655  O   PHE A 489      48.099 -18.282 -44.283  1.00 45.52           O  
ANISOU 3655  O   PHE A 489     6971   5896   4428    161   1407    -48       O  
ATOM   3656  CB  PHE A 489      47.451 -20.864 -45.779  1.00 32.50           C  
ANISOU 3656  CB  PHE A 489     5365   4330   2655    331   1250   -185       C  
ATOM   3657  CG  PHE A 489      46.336 -20.394 -46.685  1.00 37.75           C  
ANISOU 3657  CG  PHE A 489     6209   4979   3155    390   1197   -123       C  
ATOM   3658  CD1 PHE A 489      46.181 -20.933 -47.948  1.00 41.51           C  
ANISOU 3658  CD1 PHE A 489     6796   5487   3488    455   1202   -159       C  
ATOM   3659  CD2 PHE A 489      45.417 -19.449 -46.253  1.00 36.51           C  
ANISOU 3659  CD2 PHE A 489     6108   4778   2985    388   1132    -34       C  
ATOM   3660  CE1 PHE A 489      45.148 -20.515 -48.770  1.00 42.56           C  
ANISOU 3660  CE1 PHE A 489     7092   5614   3464    518   1140   -106       C  
ATOM   3661  CE2 PHE A 489      44.386 -19.033 -47.066  1.00 30.58           C  
ANISOU 3661  CE2 PHE A 489     5517   4018   2086    455   1072     20       C  
ATOM   3662  CZ  PHE A 489      44.244 -19.566 -48.316  1.00 38.53           C  
ANISOU 3662  CZ  PHE A 489     6630   5062   2946    521   1072    -15       C  
ATOM   3663  N   CYS A 490      48.540 -17.658 -46.396  1.00 32.04           N  
ANISOU 3663  N   CYS A 490     5501   4193   2479    177   1609    -14       N  
ATOM   3664  CA  CYS A 490      48.256 -16.255 -46.158  1.00 40.74           C  
ANISOU 3664  CA  CYS A 490     6690   5229   3561    130   1660     86       C  
ATOM   3665  C   CYS A 490      47.673 -15.683 -47.436  1.00 41.52           C  
ANISOU 3665  C   CYS A 490     7012   5304   3460    187   1698    158       C  
ATOM   3666  O   CYS A 490      48.371 -15.549 -48.423  1.00 47.94           O  
ANISOU 3666  O   CYS A 490     7902   6130   4183    172   1838    153       O  
ATOM   3667  CB  CYS A 490      49.537 -15.507 -45.761  1.00 37.47           C  
ANISOU 3667  CB  CYS A 490     6201   4800   3236     12   1839     79       C  
ATOM   3668  SG  CYS A 490      49.342 -13.731 -45.511  1.00 51.05           S  
ANISOU 3668  SG  CYS A 490     8037   6423   4937    -62   1932    194       S  
ATOM   3669  N   LYS A 491      46.384 -15.366 -47.420  1.00 41.73           N  
ANISOU 3669  N   LYS A 491     7133   5301   3424    256   1562    222       N  
ATOM   3670  CA  LYS A 491      45.704 -14.912 -48.622  1.00 41.01           C  
ANISOU 3670  CA  LYS A 491     7235   5195   3153    330   1550    286       C  
ATOM   3671  C   LYS A 491      44.695 -13.811 -48.334  1.00 41.17           C  
ANISOU 3671  C   LYS A 491     7333   5146   3162    354   1469    385       C  
ATOM   3672  O   LYS A 491      44.019 -13.816 -47.299  1.00 41.36           O  
ANISOU 3672  O   LYS A 491     7306   5158   3252    364   1371    397       O  
ATOM   3673  CB  LYS A 491      45.014 -16.081 -49.325  1.00 45.09           C  
ANISOU 3673  CB  LYS A 491     7789   5776   3568    435   1425    228       C  
ATOM   3674  CG  LYS A 491      45.968 -17.064 -50.007  1.00 55.78           C  
ANISOU 3674  CG  LYS A 491     9104   7190   4900    429   1510    133       C  
ATOM   3675  CD  LYS A 491      46.509 -16.537 -51.334  1.00 66.71           C  
ANISOU 3675  CD  LYS A 491    10586   8572   6188    418   1619    162       C  
ATOM   3676  CE  LYS A 491      47.608 -17.437 -51.900  1.00 69.53           C  
ANISOU 3676  CE  LYS A 491    10885   8990   6544    400   1726     65       C  
ATOM   3677  NZ  LYS A 491      47.229 -18.880 -51.868  1.00 69.54           N1+
ANISOU 3677  NZ  LYS A 491    10842   9049   6532    474   1615    -35       N1+
ATOM   3678  N   TYR A 492      44.618 -12.871 -49.271  1.00 36.72           N  
ANISOU 3678  N   TYR A 492     6894   4540   2521    366   1513    453       N  
ATOM   3679  CA  TYR A 492      43.642 -11.786 -49.272  1.00 36.30           C  
ANISOU 3679  CA  TYR A 492     6936   4418   2438    411   1440    545       C  
ATOM   3680  C   TYR A 492      42.323 -12.239 -49.878  1.00 38.56           C  
ANISOU 3680  C   TYR A 492     7292   4742   2616    540   1263    549       C  
ATOM   3681  O   TYR A 492      42.297 -13.009 -50.830  1.00 44.26           O  
ANISOU 3681  O   TYR A 492     8050   5523   3242    591   1236    504       O  
ATOM   3682  CB  TYR A 492      44.182 -10.591 -50.082  1.00 37.14           C  
ANISOU 3682  CB  TYR A 492     7152   4457   2503    373   1572    611       C  
ATOM   3683  CG  TYR A 492      45.389  -9.951 -49.442  1.00 42.86           C  
ANISOU 3683  CG  TYR A 492     7804   5134   3346    240   1736    608       C  
ATOM   3684  CD1 TYR A 492      45.247  -9.112 -48.341  1.00 40.33           C  
ANISOU 3684  CD1 TYR A 492     7444   4747   3135    188   1736    644       C  
ATOM   3685  CD2 TYR A 492      46.668 -10.214 -49.910  1.00 42.63           C  
ANISOU 3685  CD2 TYR A 492     7734   5133   3329    164   1887    560       C  
ATOM   3686  CE1 TYR A 492      46.343  -8.540 -47.734  1.00 44.41           C  
ANISOU 3686  CE1 TYR A 492     7883   5225   3767     61   1877    629       C  
ATOM   3687  CE2 TYR A 492      47.774  -9.647 -49.311  1.00 48.67           C  
ANISOU 3687  CE2 TYR A 492     8415   5864   4214     39   2029    546       C  
ATOM   3688  CZ  TYR A 492      47.606  -8.811 -48.223  1.00 48.94           C  
ANISOU 3688  CZ  TYR A 492     8411   5831   4354    -14   2020    578       C  
ATOM   3689  OH  TYR A 492      48.702  -8.240 -47.623  1.00 53.98           O  
ANISOU 3689  OH  TYR A 492     8958   6437   5114   -142   2153    554       O  
ATOM   3690  N   ALA A 493      41.225 -11.759 -49.317  1.00 43.41           N  
ANISOU 3690  N   ALA A 493     7916   5325   3252    590   1140    595       N  
ATOM   3691  CA  ALA A 493      39.910 -12.028 -49.874  1.00 43.34           C  
ANISOU 3691  CA  ALA A 493     7962   5351   3154    711    967    598       C  
ATOM   3692  C   ALA A 493      39.046 -10.807 -49.623  1.00 42.80           C  
ANISOU 3692  C   ALA A 493     7951   5212   3099    751    914    681       C  
ATOM   3693  O   ALA A 493      39.503  -9.852 -48.997  1.00 35.14           O  
ANISOU 3693  O   ALA A 493     6979   4167   2206    681   1011    728       O  
ATOM   3694  CB  ALA A 493      39.305 -13.261 -49.234  1.00 33.66           C  
ANISOU 3694  CB  ALA A 493     6632   4194   1962    745    826    523       C  
ATOM   3695  N   GLN A 494      37.815 -10.826 -50.130  1.00 46.93           N  
ANISOU 3695  N   GLN A 494     8521   5761   3550    862    763    690       N  
ATOM   3696  CA  GLN A 494      36.867  -9.727 -49.941  1.00 47.09           C  
ANISOU 3696  CA  GLN A 494     8590   5723   3579    919    697    758       C  
ATOM   3697  C   GLN A 494      35.441 -10.255 -49.856  1.00 42.57           C  
ANISOU 3697  C   GLN A 494     7971   5211   2992   1022    494    726       C  
ATOM   3698  O   GLN A 494      35.018 -11.088 -50.668  1.00 36.04           O  
ANISOU 3698  O   GLN A 494     7154   4458   2082   1085    404    675       O  
ATOM   3699  CB  GLN A 494      36.932  -8.715 -51.089  1.00 49.09           C  
ANISOU 3699  CB  GLN A 494     8999   5924   3731    960    765    825       C  
ATOM   3700  CG  GLN A 494      38.300  -8.145 -51.408  1.00 60.41           C  
ANISOU 3700  CG  GLN A 494    10492   7299   5164    862    968    855       C  
ATOM   3701  CD  GLN A 494      38.445  -7.755 -52.884  1.00 69.17           C  
ANISOU 3701  CD  GLN A 494    11752   8397   6131    912   1021    891       C  
ATOM   3702  NE2 GLN A 494      39.500  -8.252 -53.525  1.00 69.64           N  
ANISOU 3702  NE2 GLN A 494    11825   8485   6148    855   1138    860       N  
ATOM   3703  OE1 GLN A 494      37.615  -7.026 -53.438  1.00 67.66           O  
ANISOU 3703  OE1 GLN A 494    11664   8176   5869   1004    958    943       O  
ATOM   3704  N   GLY A 495      34.704  -9.758 -48.868  1.00 40.23           N  
ANISOU 3704  N   GLY A 495     7619   4885   2783   1035    424    750       N  
ATOM   3705  CA  GLY A 495      33.282 -10.019 -48.783  1.00 37.95           C  
ANISOU 3705  CA  GLY A 495     7283   4645   2491   1132    239    726       C  
ATOM   3706  C   GLY A 495      32.972 -11.332 -48.110  1.00 37.57           C  
ANISOU 3706  C   GLY A 495     7100   4673   2501   1119    133    644       C  
ATOM   3707  O   GLY A 495      33.790 -12.251 -48.104  1.00 41.04           O  
ANISOU 3707  O   GLY A 495     7506   5146   2940   1062    184    593       O  
ATOM   3708  N   ALA A 496      31.769 -11.409 -47.557  1.00 33.44           N  
ANISOU 3708  N   ALA A 496     6499   4178   2029   1174    -13    626       N  
ATOM   3709  CA  ALA A 496      31.327 -12.550 -46.773  1.00 34.21           C  
ANISOU 3709  CA  ALA A 496     6461   4338   2198   1160   -123    551       C  
ATOM   3710  C   ALA A 496      31.318 -13.839 -47.575  1.00 36.60           C  
ANISOU 3710  C   ALA A 496     6749   4723   2433   1180   -188    464       C  
ATOM   3711  O   ALA A 496      31.693 -14.908 -47.062  1.00 37.07           O  
ANISOU 3711  O   ALA A 496     6730   4817   2538   1131   -200    400       O  
ATOM   3712  CB  ALA A 496      29.945 -12.277 -46.192  1.00 36.39           C  
ANISOU 3712  CB  ALA A 496     6660   4630   2537   1220   -263    547       C  
ATOM   3713  N   ASP A 497      30.894 -13.730 -48.831  1.00 33.06           N  
ANISOU 3713  N   ASP A 497     6382   4303   1877   1254   -229    460       N  
ATOM   3714  CA  ASP A 497      30.742 -14.886 -49.709  1.00 40.35           C  
ANISOU 3714  CA  ASP A 497     7299   5305   2729   1283   -303    372       C  
ATOM   3715  C   ASP A 497      32.044 -15.641 -49.930  1.00 38.62           C  
ANISOU 3715  C   ASP A 497     7100   5090   2482   1215   -188    336       C  
ATOM   3716  O   ASP A 497      32.032 -16.805 -50.337  1.00 39.80           O  
ANISOU 3716  O   ASP A 497     7217   5302   2604   1219   -245    245       O  
ATOM   3717  CB  ASP A 497      30.147 -14.471 -51.061  1.00 52.16           C  
ANISOU 3717  CB  ASP A 497     8894   6822   4100   1377   -352    386       C  
ATOM   3718  CG  ASP A 497      28.817 -13.751 -50.918  1.00 69.00           C  
ANISOU 3718  CG  ASP A 497    11003   8958   6254   1456   -469    411       C  
ATOM   3719  OD1 ASP A 497      27.802 -14.416 -50.611  1.00 71.03           O  
ANISOU 3719  OD1 ASP A 497    11149   9276   6563   1483   -615    341       O  
ATOM   3720  OD2 ASP A 497      28.786 -12.517 -51.117  1.00 79.17           O1-
ANISOU 3720  OD2 ASP A 497    12383  10186   7513   1491   -413    497       O1-
ATOM   3721  N   SER A 498      33.168 -14.991 -49.666  1.00 33.23           N  
ANISOU 3721  N   SER A 498     6468   4345   1814   1149    -22    398       N  
ATOM   3722  CA  SER A 498      34.451 -15.641 -49.895  1.00 44.35           C  
ANISOU 3722  CA  SER A 498     7889   5760   3200   1084    104    361       C  
ATOM   3723  C   SER A 498      34.918 -16.461 -48.692  1.00 39.11           C  
ANISOU 3723  C   SER A 498     7111   5105   2643   1015    114    310       C  
ATOM   3724  O   SER A 498      35.887 -17.212 -48.778  1.00 40.90           O  
ANISOU 3724  O   SER A 498     7324   5349   2865    969    198    256       O  
ATOM   3725  CB  SER A 498      35.511 -14.615 -50.284  1.00 46.09           C  
ANISOU 3725  CB  SER A 498     8209   5915   3388   1037    288    440       C  
ATOM   3726  OG  SER A 498      35.791 -13.749 -49.201  1.00 46.66           O  
ANISOU 3726  OG  SER A 498     8251   5919   3560    978    360    503       O  
ATOM   3727  N   VAL A 499      34.236 -16.325 -47.564  1.00 39.54           N  
ANISOU 3727  N   VAL A 499     7083   5148   2794   1011     31    323       N  
ATOM   3728  CA  VAL A 499      34.695 -17.023 -46.371  1.00 33.69           C  
ANISOU 3728  CA  VAL A 499     6164   4396   2241    914     43    270       C  
ATOM   3729  C   VAL A 499      34.576 -18.538 -46.509  1.00 34.58           C  
ANISOU 3729  C   VAL A 499     6182   4565   2392    910    -43    156       C  
ATOM   3730  O   VAL A 499      35.559 -19.261 -46.350  1.00 28.36           O  
ANISOU 3730  O   VAL A 499     5331   3776   1668    847     34    104       O  
ATOM   3731  CB  VAL A 499      33.977 -16.548 -45.113  1.00 30.47           C  
ANISOU 3731  CB  VAL A 499     5658   3957   1962    895    -24    304       C  
ATOM   3732  CG1 VAL A 499      34.242 -17.511 -43.956  1.00 26.49           C  
ANISOU 3732  CG1 VAL A 499     4973   3457   1637    812    -46    237       C  
ATOM   3733  CG2 VAL A 499      34.433 -15.141 -44.773  1.00 28.22           C  
ANISOU 3733  CG2 VAL A 499     5446   3600   1676    869     95    405       C  
ATOM   3734  N   GLU A 500      33.377 -19.015 -46.815  1.00 28.96           N  
ANISOU 3734  N   GLU A 500     5461   3901   1643    977   -201    111       N  
ATOM   3735  CA  GLU A 500      33.164 -20.451 -46.931  1.00 32.22           C  
ANISOU 3735  CA  GLU A 500     5788   4358   2099    969   -288     -3       C  
ATOM   3736  C   GLU A 500      34.072 -21.194 -47.936  1.00 36.82           C  
ANISOU 3736  C   GLU A 500     6432   4965   2595    969   -215    -65       C  
ATOM   3737  O   GLU A 500      34.577 -22.262 -47.603  1.00 36.62           O  
ANISOU 3737  O   GLU A 500     6312   4938   2665    918   -203   -141       O  
ATOM   3738  CB  GLU A 500      31.688 -20.789 -47.173  1.00 31.83           C  
ANISOU 3738  CB  GLU A 500     5717   4359   2018   1038   -470    -49       C  
ATOM   3739  CG  GLU A 500      31.455 -22.278 -47.387  1.00 39.88           C  
ANISOU 3739  CG  GLU A 500     6660   5417   3075   1023   -555   -174       C  
ATOM   3740  CD  GLU A 500      29.993 -22.679 -47.344  1.00 44.97           C  
ANISOU 3740  CD  GLU A 500     7241   6108   3736   1063   -733   -231       C  
ATOM   3741  OE1 GLU A 500      29.708 -23.885 -47.516  1.00 42.31           O  
ANISOU 3741  OE1 GLU A 500     6843   5798   3435   1046   -808   -339       O  
ATOM   3742  OE2 GLU A 500      29.135 -21.799 -47.130  1.00 47.63           O1-
ANISOU 3742  OE2 GLU A 500     7586   6454   4058   1110   -795   -174       O1-
ATOM   3743  N   PRO A 501      34.278 -20.651 -49.157  1.00 36.06           N  
ANISOU 3743  N   PRO A 501     6499   4887   2315   1031   -163    -32       N  
ATOM   3744  CA  PRO A 501      35.154 -21.446 -50.025  1.00 33.53           C  
ANISOU 3744  CA  PRO A 501     6223   4592   1924   1026    -88   -102       C  
ATOM   3745  C   PRO A 501      36.588 -21.512 -49.508  1.00 31.18           C  
ANISOU 3745  C   PRO A 501     5867   4254   1725    938     78    -96       C  
ATOM   3746  O   PRO A 501      37.195 -22.578 -49.559  1.00 33.21           O  
ANISOU 3746  O   PRO A 501     6061   4525   2033    909    102   -183       O  
ATOM   3747  CB  PRO A 501      35.093 -20.710 -51.381  1.00 33.40           C  
ANISOU 3747  CB  PRO A 501     6372   4594   1725   1094    -53    -52       C  
ATOM   3748  CG  PRO A 501      33.858 -19.892 -51.323  1.00 33.59           C  
ANISOU 3748  CG  PRO A 501     6400   4614   1748   1146   -168      9       C  
ATOM   3749  CD  PRO A 501      33.665 -19.520 -49.881  1.00 32.07           C  
ANISOU 3749  CD  PRO A 501     6123   4383   1678   1108   -182     51       C  
ATOM   3750  N   MET A 502      37.116 -20.399 -49.017  1.00 30.88           N  
ANISOU 3750  N   MET A 502     5848   4169   1717    896    190     -1       N  
ATOM   3751  CA  MET A 502      38.483 -20.381 -48.497  1.00 41.29           C  
ANISOU 3751  CA  MET A 502     7099   5456   3133    809    346      0       C  
ATOM   3752  C   MET A 502      38.660 -21.311 -47.297  1.00 35.55           C  
ANISOU 3752  C   MET A 502     6186   4720   2600    749    299    -62       C  
ATOM   3753  O   MET A 502      39.663 -22.018 -47.182  1.00 35.98           O  
ANISOU 3753  O   MET A 502     6172   4779   2719    708    375   -120       O  
ATOM   3754  CB  MET A 502      38.887 -18.966 -48.096  1.00 41.82           C  
ANISOU 3754  CB  MET A 502     7212   5468   3208    768    460    109       C  
ATOM   3755  CG  MET A 502      40.297 -18.869 -47.547  1.00 30.07           C  
ANISOU 3755  CG  MET A 502     5645   3955   1825    673    620    104       C  
ATOM   3756  SD  MET A 502      40.583 -17.292 -46.732  1.00 42.19           S  
ANISOU 3756  SD  MET A 502     7195   5418   3417    608    721    215       S  
ATOM   3757  CE  MET A 502      40.950 -16.185 -48.071  1.00 31.54           C  
ANISOU 3757  CE  MET A 502     6068   4046   1870    634    868    296       C  
ATOM   3758  N   PHE A 503      37.681 -21.301 -46.403  1.00 33.14           N  
ANISOU 3758  N   PHE A 503     5804   4403   2385    750    175    -49       N  
ATOM   3759  CA  PHE A 503      37.759 -22.109 -45.195  1.00 26.87           C  
ANISOU 3759  CA  PHE A 503     4847   3593   1768    695    129    -94       C  
ATOM   3760  C   PHE A 503      37.643 -23.589 -45.520  1.00 27.01           C  
ANISOU 3760  C   PHE A 503     4820   3639   1804    713     56   -202       C  
ATOM   3761  O   PHE A 503      38.312 -24.414 -44.900  1.00 26.45           O  
ANISOU 3761  O   PHE A 503     4647   3554   1850    671     80   -252       O  
ATOM   3762  CB  PHE A 503      36.693 -21.686 -44.172  1.00 25.92           C  
ANISOU 3762  CB  PHE A 503     4665   3454   1731    690     24    -51       C  
ATOM   3763  CG  PHE A 503      37.066 -20.465 -43.371  1.00 30.63           C  
ANISOU 3763  CG  PHE A 503     5252   4007   2378    644    107     38       C  
ATOM   3764  CD1 PHE A 503      36.512 -20.249 -42.111  1.00 27.46           C  
ANISOU 3764  CD1 PHE A 503     4755   3582   2098    613     46     63       C  
ATOM   3765  CD2 PHE A 503      37.968 -19.535 -43.868  1.00 28.65           C  
ANISOU 3765  CD2 PHE A 503     5092   3737   2056    628    251     91       C  
ATOM   3766  CE1 PHE A 503      36.844 -19.148 -41.382  1.00 25.10           C  
ANISOU 3766  CE1 PHE A 503     4451   3243   1844    572    119    134       C  
ATOM   3767  CE2 PHE A 503      38.309 -18.421 -43.135  1.00 25.71           C  
ANISOU 3767  CE2 PHE A 503     4713   3320   1737    579    328    163       C  
ATOM   3768  CZ  PHE A 503      37.748 -18.221 -41.897  1.00 27.88           C  
ANISOU 3768  CZ  PHE A 503     4893   3572   2129    553    260    183       C  
ATOM   3769  N   ARG A 504      36.796 -23.915 -46.496  1.00 33.02           N  
ANISOU 3769  N   ARG A 504     5661   4437   2449    779    -36   -241       N  
ATOM   3770  CA  ARG A 504      36.682 -25.292 -46.993  1.00 30.86           C  
ANISOU 3770  CA  ARG A 504     5365   4186   2172    798   -100   -353       C  
ATOM   3771  C   ARG A 504      37.972 -25.789 -47.599  1.00 33.20           C  
ANISOU 3771  C   ARG A 504     5688   4489   2438    790     24   -402       C  
ATOM   3772  O   ARG A 504      38.352 -26.940 -47.386  1.00 33.04           O  
ANISOU 3772  O   ARG A 504     5593   4459   2500    774     15   -484       O  
ATOM   3773  CB  ARG A 504      35.566 -25.437 -48.025  1.00 32.24           C  
ANISOU 3773  CB  ARG A 504     5630   4409   2211    871   -220   -391       C  
ATOM   3774  CG  ARG A 504      34.171 -25.471 -47.421  1.00 39.07           C  
ANISOU 3774  CG  ARG A 504     6428   5279   3137    879   -375   -393       C  
ATOM   3775  CD  ARG A 504      33.114 -25.721 -48.502  1.00 43.28           C  
ANISOU 3775  CD  ARG A 504     7036   5870   3536    954   -501   -450       C  
ATOM   3776  NE  ARG A 504      31.768 -25.692 -47.937  1.00 44.08           N  
ANISOU 3776  NE  ARG A 504     7063   5985   3701    961   -646   -455       N  
ATOM   3777  CZ  ARG A 504      31.199 -26.716 -47.308  1.00 41.64           C  
ANISOU 3777  CZ  ARG A 504     6636   5666   3519    918   -733   -532       C  
ATOM   3778  NH1 ARG A 504      29.972 -26.596 -46.819  1.00 43.77           N1+
ANISOU 3778  NH1 ARG A 504     6835   5952   3842    921   -853   -535       N1+
ATOM   3779  NH2 ARG A 504      31.856 -27.859 -47.172  1.00 37.19           N  
ANISOU 3779  NH2 ARG A 504     6025   5073   3031    872   -698   -607       N  
ATOM   3780  N   HIS A 505      38.635 -24.925 -48.361  1.00 29.73           N  
ANISOU 3780  N   HIS A 505     5356   4061   1877    804    145   -351       N  
ATOM   3781  CA  HIS A 505      39.921 -25.273 -48.954  1.00 37.10           C  
ANISOU 3781  CA  HIS A 505     6312   5006   2778    793    285   -394       C  
ATOM   3782  C   HIS A 505      40.935 -25.549 -47.855  1.00 37.43           C  
ANISOU 3782  C   HIS A 505     6213   5016   2992    725    361   -401       C  
ATOM   3783  O   HIS A 505      41.659 -26.542 -47.893  1.00 41.30           O  
ANISOU 3783  O   HIS A 505     6645   5510   3537    721    395   -482       O  
ATOM   3784  CB  HIS A 505      40.423 -24.148 -49.856  1.00 31.53           C  
ANISOU 3784  CB  HIS A 505     5748   4312   1919    807    415   -323       C  
ATOM   3785  CG  HIS A 505      41.855 -24.291 -50.261  1.00 38.34           C  
ANISOU 3785  CG  HIS A 505     6612   5183   2772    777    588   -353       C  
ATOM   3786  CD2 HIS A 505      42.460 -25.148 -51.120  1.00 41.06           C  
ANISOU 3786  CD2 HIS A 505     6986   5560   3056    803    641   -442       C  
ATOM   3787  ND1 HIS A 505      42.853 -23.474 -49.773  1.00 42.28           N  
ANISOU 3787  ND1 HIS A 505     7076   5657   3331    711    735   -294       N  
ATOM   3788  CE1 HIS A 505      44.010 -23.821 -50.311  1.00 32.83           C  
ANISOU 3788  CE1 HIS A 505     5879   4482   2114    697    872   -346       C  
ATOM   3789  NE2 HIS A 505      43.799 -24.836 -51.129  1.00 40.31           N  
ANISOU 3789  NE2 HIS A 505     6866   5464   2987    755    820   -434       N  
ATOM   3790  N   LEU A 506      40.962 -24.655 -46.876  1.00 28.62           N  
ANISOU 3790  N   LEU A 506     5046   3871   1960    677    383   -319       N  
ATOM   3791  CA  LEU A 506      41.849 -24.753 -45.730  1.00 27.74           C  
ANISOU 3791  CA  LEU A 506     4799   3734   2008    614    443   -318       C  
ATOM   3792  C   LEU A 506      41.664 -26.084 -44.994  1.00 31.66           C  
ANISOU 3792  C   LEU A 506     5178   4217   2633    614    344   -393       C  
ATOM   3793  O   LEU A 506      42.639 -26.762 -44.652  1.00 29.78           O  
ANISOU 3793  O   LEU A 506     4857   3976   2482    597    400   -443       O  
ATOM   3794  CB  LEU A 506      41.562 -23.589 -44.782  1.00 30.98           C  
ANISOU 3794  CB  LEU A 506     5183   4113   2474    571    444   -222       C  
ATOM   3795  CG  LEU A 506      42.564 -22.441 -44.633  1.00 36.02           C  
ANISOU 3795  CG  LEU A 506     5833   4737   3115    516    599   -161       C  
ATOM   3796  CD1 LEU A 506      43.623 -22.496 -45.699  1.00 32.94           C  
ANISOU 3796  CD1 LEU A 506     5505   4374   2637    518    741   -194       C  
ATOM   3797  CD2 LEU A 506      41.859 -21.097 -44.651  1.00 37.68           C  
ANISOU 3797  CD2 LEU A 506     6137   4921   3258    517    596    -62       C  
ATOM   3798  N   LYS A 507      40.411 -26.458 -44.747  1.00 29.33           N  
ANISOU 3798  N   LYS A 507     4879   3914   2353    634    199   -400       N  
ATOM   3799  CA  LYS A 507      40.135 -27.696 -44.031  1.00 25.96           C  
ANISOU 3799  CA  LYS A 507     4354   3463   2047    628    108   -463       C  
ATOM   3800  C   LYS A 507      40.517 -28.896 -44.886  1.00 31.29           C  
ANISOU 3800  C   LYS A 507     5053   4149   2689    664    113   -567       C  
ATOM   3801  O   LYS A 507      40.977 -29.905 -44.364  1.00 31.76           O  
ANISOU 3801  O   LYS A 507     5032   4181   2854    657    107   -623       O  
ATOM   3802  CB  LYS A 507      38.664 -27.806 -43.618  1.00 29.18           C  
ANISOU 3802  CB  LYS A 507     4749   3860   2479    632    -39   -453       C  
ATOM   3803  CG  LYS A 507      38.413 -29.016 -42.701  1.00 37.75           C  
ANISOU 3803  CG  LYS A 507     5732   4907   3705    610   -117   -505       C  
ATOM   3804  CD  LYS A 507      36.958 -29.198 -42.311  1.00 37.42           C  
ANISOU 3804  CD  LYS A 507     5669   4857   3693    605   -252   -505       C  
ATOM   3805  CE  LYS A 507      36.782 -30.390 -41.374  1.00 38.47           C  
ANISOU 3805  CE  LYS A 507     5710   4940   3966    574   -310   -550       C  
ATOM   3806  NZ  LYS A 507      35.346 -30.664 -41.043  1.00 40.66           N1+
ANISOU 3806  NZ  LYS A 507     5961   5210   4277    560   -433   -562       N1+
ATOM   3807  N   ASN A 508      40.335 -28.773 -46.200  1.00 27.94           N  
ANISOU 3807  N   ASN A 508     4746   3761   2110    709    126   -593       N  
ATOM   3808  CA  ASN A 508      40.642 -29.864 -47.116  1.00 31.88           C  
ANISOU 3808  CA  ASN A 508     5282   4274   2559    748    131   -699       C  
ATOM   3809  C   ASN A 508      42.129 -30.085 -47.241  1.00 32.34           C  
ANISOU 3809  C   ASN A 508     5310   4336   2643    742    275   -729       C  
ATOM   3810  O   ASN A 508      42.588 -31.216 -47.364  1.00 31.62           O  
ANISOU 3810  O   ASN A 508     5183   4231   2598    762    278   -818       O  
ATOM   3811  CB  ASN A 508      40.071 -29.597 -48.513  1.00 40.23           C  
ANISOU 3811  CB  ASN A 508     6481   5378   3427    801    109   -718       C  
ATOM   3812  CG  ASN A 508      38.604 -29.922 -48.614  1.00 44.73           C  
ANISOU 3812  CG  ASN A 508     7067   5953   3974    822    -58   -745       C  
ATOM   3813  ND2 ASN A 508      37.919 -29.280 -49.556  1.00 50.53           N  
ANISOU 3813  ND2 ASN A 508     7916   6733   4549    869    -97   -725       N  
ATOM   3814  OD1 ASN A 508      38.086 -30.743 -47.859  1.00 40.78           O  
ANISOU 3814  OD1 ASN A 508     6478   5418   3597    798   -149   -786       O  
ATOM   3815  N   THR A 509      42.879 -28.992 -47.201  1.00 33.54           N  
ANISOU 3815  N   THR A 509     5471   4503   2769    715    396   -657       N  
ATOM   3816  CA  THR A 509      44.296 -29.041 -47.508  1.00 33.36           C  
ANISOU 3816  CA  THR A 509     5426   4499   2751    708    549   -688       C  
ATOM   3817  C   THR A 509      45.174 -29.181 -46.259  1.00 35.10           C  
ANISOU 3817  C   THR A 509     5497   4697   3143    666    589   -681       C  
ATOM   3818  O   THR A 509      46.202 -29.858 -46.287  1.00 32.53           O  
ANISOU 3818  O   THR A 509     5109   4379   2871    678    659   -747       O  
ATOM   3819  CB  THR A 509      44.701 -27.826 -48.348  1.00 41.56           C  
ANISOU 3819  CB  THR A 509     6570   5569   3651    699    677   -627       C  
ATOM   3820  CG2 THR A 509      45.892 -28.159 -49.199  1.00 47.08           C  
ANISOU 3820  CG2 THR A 509     7289   6301   4297    713    821   -692       C  
ATOM   3821  OG1 THR A 509      43.618 -27.480 -49.220  1.00 44.61           O  
ANISOU 3821  OG1 THR A 509     7094   5971   3884    741    603   -603       O  
ATOM   3822  N   TYR A 510      44.756 -28.551 -45.163  1.00 36.26           N  
ANISOU 3822  N   TYR A 510     5586   4819   3372    624    539   -605       N  
ATOM   3823  CA  TYR A 510      45.462 -28.669 -43.891  1.00 27.27           C  
ANISOU 3823  CA  TYR A 510     4307   3662   2390    588    554   -596       C  
ATOM   3824  C   TYR A 510      44.481 -29.168 -42.852  1.00 28.72           C  
ANISOU 3824  C   TYR A 510     4439   3805   2670    584    408   -581       C  
ATOM   3825  O   TYR A 510      43.888 -28.380 -42.120  1.00 28.42           O  
ANISOU 3825  O   TYR A 510     4386   3752   2658    549    367   -506       O  
ATOM   3826  CB  TYR A 510      46.025 -27.315 -43.447  1.00 27.04           C  
ANISOU 3826  CB  TYR A 510     4255   3644   2374    528    652   -518       C  
ATOM   3827  CG  TYR A 510      46.833 -26.591 -44.508  1.00 28.21           C  
ANISOU 3827  CG  TYR A 510     4477   3827   2413    518    808   -514       C  
ATOM   3828  CD1 TYR A 510      48.214 -26.746 -44.582  1.00 31.91           C  
ANISOU 3828  CD1 TYR A 510     4871   4324   2928    502    936   -564       C  
ATOM   3829  CD2 TYR A 510      46.222 -25.751 -45.424  1.00 34.47           C  
ANISOU 3829  CD2 TYR A 510     5414   4625   3059    525    829   -461       C  
ATOM   3830  CE1 TYR A 510      48.961 -26.093 -45.527  1.00 30.02           C  
ANISOU 3830  CE1 TYR A 510     4696   4116   2594    483   1091   -562       C  
ATOM   3831  CE2 TYR A 510      46.971 -25.086 -46.397  1.00 38.39           C  
ANISOU 3831  CE2 TYR A 510     5991   5147   3449    513    983   -451       C  
ATOM   3832  CZ  TYR A 510      48.338 -25.265 -46.432  1.00 39.86           C  
ANISOU 3832  CZ  TYR A 510     6098   5360   3688    486   1118   -502       C  
ATOM   3833  OH  TYR A 510      49.098 -24.622 -47.373  1.00 47.29           O  
ANISOU 3833  OH  TYR A 510     7113   6325   4528    465   1283   -495       O  
ATOM   3834  N   SER A 511      44.292 -30.480 -42.790  1.00 32.77           N  
ANISOU 3834  N   SER A 511     4926   4292   3234    618    335   -653       N  
ATOM   3835  CA  SER A 511      43.328 -31.031 -41.858  1.00 25.35           C  
ANISOU 3835  CA  SER A 511     3943   3306   2381    609    206   -642       C  
ATOM   3836  C   SER A 511      43.830 -30.861 -40.436  1.00 26.23           C  
ANISOU 3836  C   SER A 511     3942   3399   2624    576    211   -597       C  
ATOM   3837  O   SER A 511      43.050 -30.914 -39.499  1.00 25.66           O  
ANISOU 3837  O   SER A 511     3837   3295   2618    554    124   -559       O  
ATOM   3838  CB  SER A 511      42.999 -32.495 -42.175  1.00 26.93           C  
ANISOU 3838  CB  SER A 511     4155   3472   2604    649    134   -733       C  
ATOM   3839  OG  SER A 511      44.167 -33.271 -42.365  1.00 27.21           O  
ANISOU 3839  OG  SER A 511     4154   3506   2678    683    205   -801       O  
ATOM   3840  N   GLY A 512      45.125 -30.597 -40.282  1.00 31.24           N  
ANISOU 3840  N   GLY A 512     4517   4059   3292    570    316   -604       N  
ATOM   3841  CA  GLY A 512      45.683 -30.321 -38.970  1.00 28.31           C  
ANISOU 3841  CA  GLY A 512     4039   3684   3035    540    322   -566       C  
ATOM   3842  C   GLY A 512      45.863 -28.856 -38.615  1.00 33.34           C  
ANISOU 3842  C   GLY A 512     4666   4347   3657    483    383   -491       C  
ATOM   3843  O   GLY A 512      46.541 -28.552 -37.638  1.00 23.28           O  
ANISOU 3843  O   GLY A 512     3297   3080   2468    455    406   -473       O  
ATOM   3844  N   LEU A 513      45.267 -27.952 -39.395  1.00 23.83           N  
ANISOU 3844  N   LEU A 513     3559   3153   2343    468    406   -450       N  
ATOM   3845  CA  LEU A 513      45.344 -26.512 -39.117  1.00 23.58           C  
ANISOU 3845  CA  LEU A 513     3537   3131   2292    414    466   -376       C  
ATOM   3846  C   LEU A 513      44.965 -26.206 -37.665  1.00 22.49           C  
ANISOU 3846  C   LEU A 513     3323   2969   2253    379    397   -326       C  
ATOM   3847  O   LEU A 513      43.900 -26.610 -37.204  1.00 21.86           O  
ANISOU 3847  O   LEU A 513     3249   2861   2194    390    287   -310       O  
ATOM   3848  CB  LEU A 513      44.360 -25.765 -40.008  1.00 23.82           C  
ANISOU 3848  CB  LEU A 513     3698   3159   2195    422    453   -330       C  
ATOM   3849  CG  LEU A 513      44.752 -24.477 -40.714  1.00 24.48           C  
ANISOU 3849  CG  LEU A 513     3860   3256   2184    394    573   -282       C  
ATOM   3850  CD1 LEU A 513      43.545 -23.585 -40.782  1.00 29.91           C  
ANISOU 3850  CD1 LEU A 513     4637   3924   2804    397    513   -207       C  
ATOM   3851  CD2 LEU A 513      45.927 -23.775 -40.100  1.00 24.50           C  
ANISOU 3851  CD2 LEU A 513     3784   3269   2258    333    685   -269       C  
ATOM   3852  N   GLN A 514      45.816 -25.485 -36.944  1.00 22.34           N  
ANISOU 3852  N   GLN A 514     3231   2965   2294    332    465   -305       N  
ATOM   3853  CA  GLN A 514      45.510 -25.219 -35.539  1.00 25.08           C  
ANISOU 3853  CA  GLN A 514     3506   3293   2728    301    401   -264       C  
ATOM   3854  C   GLN A 514      44.744 -23.917 -35.363  1.00 27.50           C  
ANISOU 3854  C   GLN A 514     3871   3583   2994    261    401   -189       C  
ATOM   3855  O   GLN A 514      43.937 -23.797 -34.447  1.00 23.11           O  
ANISOU 3855  O   GLN A 514     3297   3005   2480    251    320   -151       O  
ATOM   3856  CB  GLN A 514      46.771 -25.189 -34.684  1.00 21.45           C  
ANISOU 3856  CB  GLN A 514     2927   2860   2364    275    451   -290       C  
ATOM   3857  CG  GLN A 514      47.544 -26.470 -34.658  1.00 21.86           C  
ANISOU 3857  CG  GLN A 514     2908   2925   2472    326    440   -362       C  
ATOM   3858  CD  GLN A 514      48.872 -26.294 -33.953  1.00 27.18           C  
ANISOU 3858  CD  GLN A 514     3458   3640   3229    305    497   -393       C  
ATOM   3859  NE2 GLN A 514      48.870 -26.469 -32.638  1.00 21.54           N  
ANISOU 3859  NE2 GLN A 514     2666   2920   2597    303    423   -378       N  
ATOM   3860  OE1 GLN A 514      49.889 -25.984 -34.581  1.00 29.62           O  
ANISOU 3860  OE1 GLN A 514     3741   3989   3526    290    608   -433       O  
ATOM   3861  N   LEU A 515      44.996 -22.950 -36.239  1.00 24.58           N  
ANISOU 3861  N   LEU A 515     3577   3220   2541    241    498   -166       N  
ATOM   3862  CA  LEU A 515      44.427 -21.622 -36.071  1.00 24.63           C  
ANISOU 3862  CA  LEU A 515     3644   3203   2512    205    515    -93       C  
ATOM   3863  C   LEU A 515      44.355 -20.818 -37.378  1.00 30.43           C  
ANISOU 3863  C   LEU A 515     4510   3934   3120    211    600    -63       C  
ATOM   3864  O   LEU A 515      45.249 -20.888 -38.217  1.00 23.19           O  
ANISOU 3864  O   LEU A 515     3613   3039   2161    208    702    -95       O  
ATOM   3865  CB  LEU A 515      45.249 -20.846 -35.043  1.00 22.11           C  
ANISOU 3865  CB  LEU A 515     3238   2885   2276    138    575    -81       C  
ATOM   3866  CG  LEU A 515      44.760 -19.423 -34.785  1.00 23.54           C  
ANISOU 3866  CG  LEU A 515     3480   3031   2432     96    603    -11       C  
ATOM   3867  CD1 LEU A 515      43.516 -19.448 -33.910  1.00 25.16           C  
ANISOU 3867  CD1 LEU A 515     3681   3213   2667    114    479     27       C  
ATOM   3868  CD2 LEU A 515      45.848 -18.558 -34.174  1.00 21.28           C  
ANISOU 3868  CD2 LEU A 515     3127   2749   2208     18    704    -16       C  
ATOM   3869  N   ILE A 516      43.275 -20.065 -37.548  1.00 22.15           N  
ANISOU 3869  N   ILE A 516     3552   2857   2007    226    557      0       N  
ATOM   3870  CA  ILE A 516      43.224 -19.051 -38.585  1.00 23.03           C  
ANISOU 3870  CA  ILE A 516     3797   2953   2000    229    642     48       C  
ATOM   3871  C   ILE A 516      43.130 -17.672 -37.953  1.00 27.00           C  
ANISOU 3871  C   ILE A 516     4321   3414   2524    179    686    116       C  
ATOM   3872  O   ILE A 516      42.180 -17.381 -37.234  1.00 24.60           O  
ANISOU 3872  O   ILE A 516     4010   3089   2250    190    596    151       O  
ATOM   3873  CB  ILE A 516      42.023 -19.216 -39.532  1.00 24.84           C  
ANISOU 3873  CB  ILE A 516     4143   3184   2113    305    558     66       C  
ATOM   3874  CG1 ILE A 516      41.951 -20.635 -40.099  1.00 25.69           C  
ANISOU 3874  CG1 ILE A 516     4231   3327   2204    354    496     -9       C  
ATOM   3875  CG2 ILE A 516      42.146 -18.233 -40.701  1.00 25.30           C  
ANISOU 3875  CG2 ILE A 516     4352   3229   2034    317    658    116       C  
ATOM   3876  CD1 ILE A 516      40.613 -20.986 -40.719  1.00 23.62           C  
ANISOU 3876  CD1 ILE A 516     4043   3072   1859    424    374     -9       C  
ATOM   3877  N   ILE A 517      44.122 -16.827 -38.207  1.00 30.33           N  
ANISOU 3877  N   ILE A 517     4767   3823   2935    121    830    129       N  
ATOM   3878  CA  ILE A 517      44.011 -15.425 -37.831  1.00 29.75           C  
ANISOU 3878  CA  ILE A 517     4745   3696   2862     74    887    196       C  
ATOM   3879  C   ILE A 517      43.323 -14.682 -38.982  1.00 32.18           C  
ANISOU 3879  C   ILE A 517     5233   3969   3024    123    913    263       C  
ATOM   3880  O   ILE A 517      43.825 -14.638 -40.114  1.00 34.51           O  
ANISOU 3880  O   ILE A 517     5616   4272   3224    131   1008    264       O  
ATOM   3881  CB  ILE A 517      45.381 -14.813 -37.483  1.00 32.56           C  
ANISOU 3881  CB  ILE A 517     5039   4046   3285    -24   1032    175       C  
ATOM   3882  CG1 ILE A 517      45.951 -15.503 -36.244  1.00 29.26           C  
ANISOU 3882  CG1 ILE A 517     4443   3667   3007    -58    983    111       C  
ATOM   3883  CG2 ILE A 517      45.265 -13.304 -37.236  1.00 31.06           C  
ANISOU 3883  CG2 ILE A 517     4927   3787   3087    -77   1106    242       C  
ATOM   3884  CD1 ILE A 517      47.392 -15.163 -35.951  1.00 33.20           C  
ANISOU 3884  CD1 ILE A 517     4850   4184   3580   -146   1110     65       C  
ATOM   3885  N   VAL A 518      42.143 -14.151 -38.682  1.00 29.12           N  
ANISOU 3885  N   VAL A 518     4900   3549   2617    165    823    319       N  
ATOM   3886  CA  VAL A 518      41.318 -13.454 -39.647  1.00 29.15           C  
ANISOU 3886  CA  VAL A 518     5071   3521   2485    231    817    387       C  
ATOM   3887  C   VAL A 518      41.444 -11.957 -39.426  1.00 29.86           C  
ANISOU 3887  C   VAL A 518     5242   3533   2568    188    913    459       C  
ATOM   3888  O   VAL A 518      41.215 -11.473 -38.329  1.00 33.44           O  
ANISOU 3888  O   VAL A 518     5634   3957   3114    153    885    471       O  
ATOM   3889  CB  VAL A 518      39.843 -13.843 -39.498  1.00 27.13           C  
ANISOU 3889  CB  VAL A 518     4817   3280   2210    317    646    396       C  
ATOM   3890  CG1 VAL A 518      38.998 -13.104 -40.522  1.00 25.21           C  
ANISOU 3890  CG1 VAL A 518     4745   3012   1821    400    630    463       C  
ATOM   3891  CG2 VAL A 518      39.676 -15.347 -39.627  1.00 23.83           C  
ANISOU 3891  CG2 VAL A 518     4315   2926   1812    350    549    318       C  
ATOM   3892  N   ILE A 519      41.814 -11.229 -40.470  1.00 30.22           N  
ANISOU 3892  N   ILE A 519     5436   3543   2503    189   1032    507       N  
ATOM   3893  CA  ILE A 519      42.004  -9.792 -40.357  1.00 31.51           C  
ANISOU 3893  CA  ILE A 519     5696   3619   2656    143   1142    579       C  
ATOM   3894  C   ILE A 519      40.841  -9.030 -40.993  1.00 27.87           C  
ANISOU 3894  C   ILE A 519     5409   3110   2072    242   1090    666       C  
ATOM   3895  O   ILE A 519      40.510  -9.236 -42.152  1.00 28.72           O  
ANISOU 3895  O   ILE A 519     5634   3236   2041    320   1077    689       O  
ATOM   3896  CB  ILE A 519      43.371  -9.391 -40.913  1.00 35.79           C  
ANISOU 3896  CB  ILE A 519     6276   4142   3182     53   1337    573       C  
ATOM   3897  CG1 ILE A 519      44.426 -10.139 -40.096  1.00 38.64           C  
ANISOU 3897  CG1 ILE A 519     6438   4558   3683    -34   1363    479       C  
ATOM   3898  CG2 ILE A 519      43.571  -7.869 -40.858  1.00 29.24           C  
ANISOU 3898  CG2 ILE A 519     5563   3206   2339     -3   1465    648       C  
ATOM   3899  CD1 ILE A 519      45.781  -9.621 -40.227  1.00 41.87           C  
ANISOU 3899  CD1 ILE A 519     6832   4949   4126   -145   1548    460       C  
ATOM   3900  N   LEU A 520      40.211  -8.178 -40.189  1.00 28.54           N  
ANISOU 3900  N   LEU A 520     5501   3136   2208    245   1052    709       N  
ATOM   3901  CA  LEU A 520      38.920  -7.581 -40.521  1.00 34.40           C  
ANISOU 3901  CA  LEU A 520     6367   3842   2861    357    961    780       C  
ATOM   3902  C   LEU A 520      38.987  -6.079 -40.688  1.00 38.95           C  
ANISOU 3902  C   LEU A 520     7034   4318   3446    339   1040    835       C  
ATOM   3903  O   LEU A 520      39.688  -5.399 -39.953  1.00 37.59           O  
ANISOU 3903  O   LEU A 520     6827   4089   3365    240   1139    833       O  
ATOM   3904  CB  LEU A 520      37.898  -7.878 -39.429  1.00 29.63           C  
ANISOU 3904  CB  LEU A 520     5643   3263   2352    392    805    755       C  
ATOM   3905  CG  LEU A 520      37.611  -9.359 -39.225  1.00 36.47           C  
ANISOU 3905  CG  LEU A 520     6366   4229   3262    413    679    674       C  
ATOM   3906  CD1 LEU A 520      36.562  -9.575 -38.148  1.00 35.22           C  
ANISOU 3906  CD1 LEU A 520     6099   4088   3194    442    539    657       C  
ATOM   3907  CD2 LEU A 520      37.167  -9.923 -40.558  1.00 38.67           C  
ANISOU 3907  CD2 LEU A 520     6739   4554   3399    507    626    676       C  
ATOM   3908  N   PRO A 521      38.219  -5.554 -41.644  1.00 43.54           N  
ANISOU 3908  N   PRO A 521     7728   4879   3937    438    989    877       N  
ATOM   3909  CA  PRO A 521      38.174  -4.109 -41.861  1.00 48.00           C  
ANISOU 3909  CA  PRO A 521     8392   5344   4501    438   1054    929       C  
ATOM   3910  C   PRO A 521      37.011  -3.488 -41.101  1.00 55.04           C  
ANISOU 3910  C   PRO A 521     9276   6202   5436    503    950    954       C  
ATOM   3911  O   PRO A 521      35.952  -3.252 -41.676  1.00 65.23           O  
ANISOU 3911  O   PRO A 521    10629   7497   6657    620    851    982       O  
ATOM   3912  CB  PRO A 521      37.965  -4.000 -43.371  1.00 42.24           C  
ANISOU 3912  CB  PRO A 521     7791   4621   3639    520   1052    958       C  
ATOM   3913  CG  PRO A 521      37.184  -5.250 -43.735  1.00 46.66           C  
ANISOU 3913  CG  PRO A 521     8310   5285   4132    612    906    925       C  
ATOM   3914  CD  PRO A 521      37.446  -6.298 -42.653  1.00 30.32           C  
ANISOU 3914  CD  PRO A 521     6097   3275   2149    552    876    870       C  
ATOM   3915  N   GLY A 522      37.213  -3.235 -39.814  1.00 54.42           N  
ANISOU 3915  N   GLY A 522     9113   6093   5472    429    971    939       N  
ATOM   3916  CA  GLY A 522      36.193  -2.613 -38.990  1.00 57.52           C  
ANISOU 3916  CA  GLY A 522     9490   6451   5915    481    887    957       C  
ATOM   3917  C   GLY A 522      34.997  -3.517 -38.792  1.00 59.08           C  
ANISOU 3917  C   GLY A 522     9622   6732   6096    581    716    941       C  
ATOM   3918  O   GLY A 522      35.109  -4.732 -38.945  1.00 58.47           O  
ANISOU 3918  O   GLY A 522     9485   6736   5994    582    668    907       O  
ATOM   3919  N   LYS A 523      33.856  -2.927 -38.445  1.00 58.66           N  
ANISOU 3919  N   LYS A 523     9575   6658   6057    664    625    960       N  
ATOM   3920  CA  LYS A 523      32.622  -3.690 -38.323  1.00 61.48           C  
ANISOU 3920  CA  LYS A 523     9863   7095   6401    763    459    939       C  
ATOM   3921  C   LYS A 523      32.191  -4.192 -39.690  1.00 61.05           C  
ANISOU 3921  C   LYS A 523     9866   7101   6229    854    392    937       C  
ATOM   3922  O   LYS A 523      32.121  -3.423 -40.651  1.00 72.34           O  
ANISOU 3922  O   LYS A 523    11413   8490   7584    903    426    974       O  
ATOM   3923  CB  LYS A 523      31.503  -2.869 -37.682  1.00 70.04           C  
ANISOU 3923  CB  LYS A 523    10935   8146   7530    832    387    955       C  
ATOM   3924  CG  LYS A 523      30.161  -3.603 -37.633  1.00 74.77           C  
ANISOU 3924  CG  LYS A 523    11454   8835   8121    935    216    926       C  
ATOM   3925  CD  LYS A 523      29.126  -2.851 -36.805  1.00 77.13           C  
ANISOU 3925  CD  LYS A 523    11718   9106   8482    990    157    932       C  
ATOM   3926  CE  LYS A 523      27.813  -3.619 -36.719  1.00 78.14           C  
ANISOU 3926  CE  LYS A 523    11745   9330   8614   1081     -7    893       C  
ATOM   3927  NZ  LYS A 523      26.948  -3.123 -35.607  1.00 80.28           N1+
ANISOU 3927  NZ  LYS A 523    11945   9586   8971   1110    -54    887       N1+
ATOM   3928  N   THR A 524      31.913  -5.486 -39.780  1.00 51.39           N  
ANISOU 3928  N   THR A 524     8565   5973   4989    876    296    892       N  
ATOM   3929  CA  THR A 524      31.607  -6.098 -41.065  1.00 53.18           C  
ANISOU 3929  CA  THR A 524     8838   6264   5105    950    234    875       C  
ATOM   3930  C   THR A 524      30.843  -7.409 -40.901  1.00 48.90           C  
ANISOU 3930  C   THR A 524     8186   5825   4569    992     85    814       C  
ATOM   3931  O   THR A 524      31.081  -8.154 -39.950  1.00 49.79           O  
ANISOU 3931  O   THR A 524     8199   5964   4756    934     71    783       O  
ATOM   3932  CB  THR A 524      32.894  -6.339 -41.896  1.00 44.86           C  
ANISOU 3932  CB  THR A 524     7855   5200   3988    885    361    878       C  
ATOM   3933  CG2 THR A 524      33.977  -7.001 -41.054  1.00 45.51           C  
ANISOU 3933  CG2 THR A 524     7857   5290   4143    767    443    849       C  
ATOM   3934  OG1 THR A 524      32.588  -7.183 -43.009  1.00 50.53           O  
ANISOU 3934  OG1 THR A 524     8599   5996   4606    952    288    847       O  
ATOM   3935  N   PRO A 525      29.903  -7.675 -41.823  1.00 42.59           N  
ANISOU 3935  N   PRO A 525     7405   5083   3695   1094    -27    794       N  
ATOM   3936  CA  PRO A 525      29.126  -8.916 -41.957  1.00 39.91           C  
ANISOU 3936  CA  PRO A 525     6971   4846   3347   1138   -172    724       C  
ATOM   3937  C   PRO A 525      29.981 -10.175 -42.084  1.00 32.16           C  
ANISOU 3937  C   PRO A 525     5958   3912   2348   1076   -149    676       C  
ATOM   3938  O   PRO A 525      29.455 -11.279 -41.932  1.00 30.42           O  
ANISOU 3938  O   PRO A 525     5646   3767   2147   1091   -262    610       O  
ATOM   3939  CB  PRO A 525      28.377  -8.715 -43.285  1.00 45.07           C  
ANISOU 3939  CB  PRO A 525     7699   5531   3893   1243   -243    722       C  
ATOM   3940  CG  PRO A 525      28.245  -7.254 -43.424  1.00 50.32           C  
ANISOU 3940  CG  PRO A 525     8462   6114   4543   1280   -182    793       C  
ATOM   3941  CD  PRO A 525      29.457  -6.642 -42.777  1.00 49.95           C  
ANISOU 3941  CD  PRO A 525     8453   5977   4547   1176    -22    838       C  
ATOM   3942  N   VAL A 526      31.262 -10.032 -42.409  1.00 31.09           N  
ANISOU 3942  N   VAL A 526     5898   3737   2179   1009     -6    700       N  
ATOM   3943  CA  VAL A 526      32.087 -11.224 -42.567  1.00 37.83           C  
ANISOU 3943  CA  VAL A 526     6725   4639   3011    958     22    649       C  
ATOM   3944  C   VAL A 526      32.411 -11.867 -41.216  1.00 31.85           C  
ANISOU 3944  C   VAL A 526     5793   3888   2421    859     21    597       C  
ATOM   3945  O   VAL A 526      32.610 -13.084 -41.147  1.00 28.04           O  
ANISOU 3945  O   VAL A 526     5209   3460   1985    823    -18    519       O  
ATOM   3946  CB  VAL A 526      33.385 -10.985 -43.390  1.00 48.22           C  
ANISOU 3946  CB  VAL A 526     8142   5922   4258    907    183    671       C  
ATOM   3947  CG1 VAL A 526      33.122 -10.059 -44.565  1.00 47.51           C  
ANISOU 3947  CG1 VAL A 526     8176   5800   4075    971    204    717       C  
ATOM   3948  CG2 VAL A 526      34.463 -10.426 -42.524  1.00 50.71           C  
ANISOU 3948  CG2 VAL A 526     8447   6170   4652    800    331    704       C  
ATOM   3949  N   TYR A 527      32.439 -11.061 -40.151  1.00 32.38           N  
ANISOU 3949  N   TYR A 527     5822   3896   2583    815     62    634       N  
ATOM   3950  CA  TYR A 527      32.667 -11.596 -38.804  1.00 29.81           C  
ANISOU 3950  CA  TYR A 527     5327   3579   2419    725     54    585       C  
ATOM   3951  C   TYR A 527      31.699 -12.739 -38.484  1.00 26.22           C  
ANISOU 3951  C   TYR A 527     4748   3196   2017    752    -95    516       C  
ATOM   3952  O   TYR A 527      32.123 -13.846 -38.172  1.00 25.38           O  
ANISOU 3952  O   TYR A 527     4540   3125   1978    695   -106    451       O  
ATOM   3953  CB  TYR A 527      32.582 -10.512 -37.713  1.00 26.62           C  
ANISOU 3953  CB  TYR A 527     4908   3108   2097    691     96    631       C  
ATOM   3954  CG  TYR A 527      32.748 -11.090 -36.309  1.00 23.43           C  
ANISOU 3954  CG  TYR A 527     4335   2720   1846    608     77    580       C  
ATOM   3955  CD1 TYR A 527      34.013 -11.213 -35.725  1.00 25.40           C  
ANISOU 3955  CD1 TYR A 527     4529   2953   2171    502    180    560       C  
ATOM   3956  CD2 TYR A 527      31.653 -11.532 -35.582  1.00 23.19           C  
ANISOU 3956  CD2 TYR A 527     4204   2727   1882    636    -43    551       C  
ATOM   3957  CE1 TYR A 527      34.179 -11.762 -34.456  1.00 20.66           C  
ANISOU 3957  CE1 TYR A 527     3784   2370   1697    435    157    516       C  
ATOM   3958  CE2 TYR A 527      31.807 -12.076 -34.304  1.00 24.87           C  
ANISOU 3958  CE2 TYR A 527     4275   2951   2222    562    -55    510       C  
ATOM   3959  CZ  TYR A 527      33.067 -12.192 -33.753  1.00 27.05           C  
ANISOU 3959  CZ  TYR A 527     4508   3209   2560    466     41    495       C  
ATOM   3960  OH  TYR A 527      33.205 -12.742 -32.489  1.00 27.62           O  
ANISOU 3960  OH  TYR A 527     4450   3297   2748    404     21    458       O  
ATOM   3961  N   ALA A 528      30.402 -12.454 -38.570  1.00 27.10           N  
ANISOU 3961  N   ALA A 528     4870   3326   2099    840   -206    527       N  
ATOM   3962  CA  ALA A 528      29.368 -13.458 -38.363  1.00 27.67           C  
ANISOU 3962  CA  ALA A 528     4829   3467   2217    867   -347    459       C  
ATOM   3963  C   ALA A 528      29.561 -14.647 -39.308  1.00 25.95           C  
ANISOU 3963  C   ALA A 528     4613   3307   1940    875   -387    394       C  
ATOM   3964  O   ALA A 528      29.339 -15.801 -38.933  1.00 29.63           O  
ANISOU 3964  O   ALA A 528     4963   3813   2483    838   -450    321       O  
ATOM   3965  CB  ALA A 528      27.991 -12.840 -38.563  1.00 32.52           C  
ANISOU 3965  CB  ALA A 528     5471   4099   2786    975   -454    482       C  
ATOM   3966  N   GLU A 529      29.987 -14.356 -40.530  1.00 30.76           N  
ANISOU 3966  N   GLU A 529     5361   3915   2412    923   -343    420       N  
ATOM   3967  CA  GLU A 529      30.213 -15.406 -41.506  1.00 31.43           C  
ANISOU 3967  CA  GLU A 529     5463   4053   2426    936   -372    356       C  
ATOM   3968  C   GLU A 529      31.410 -16.275 -41.122  1.00 26.68           C  
ANISOU 3968  C   GLU A 529     4788   3443   1905    834   -286    310       C  
ATOM   3969  O   GLU A 529      31.352 -17.500 -41.199  1.00 24.27           O  
ANISOU 3969  O   GLU A 529     4408   3178   1634    817   -343    231       O  
ATOM   3970  CB  GLU A 529      30.364 -14.814 -42.910  1.00 34.67           C  
ANISOU 3970  CB  GLU A 529     6053   4464   2655   1017   -340    400       C  
ATOM   3971  CG  GLU A 529      30.543 -15.846 -44.027  1.00 34.42           C  
ANISOU 3971  CG  GLU A 529     6057   4493   2529   1042   -373    331       C  
ATOM   3972  CD  GLU A 529      29.348 -16.778 -44.192  1.00 35.42           C  
ANISOU 3972  CD  GLU A 529     6102   4693   2663   1091   -545    246       C  
ATOM   3973  OE1 GLU A 529      28.337 -16.630 -43.464  1.00 42.43           O  
ANISOU 3973  OE1 GLU A 529     6902   5591   3629   1108   -639    243       O  
ATOM   3974  OE2 GLU A 529      29.419 -17.669 -45.060  1.00 37.02           O1-
ANISOU 3974  OE2 GLU A 529     6327   4945   2795   1110   -582    177       O1-
ATOM   3975  N   VAL A 530      32.487 -15.637 -40.686  1.00 28.17           N  
ANISOU 3975  N   VAL A 530     4996   3578   2131    769   -151    356       N  
ATOM   3976  CA  VAL A 530      33.646 -16.360 -40.164  1.00 27.29           C  
ANISOU 3976  CA  VAL A 530     4797   3461   2111    676    -72    313       C  
ATOM   3977  C   VAL A 530      33.277 -17.277 -38.979  1.00 28.62           C  
ANISOU 3977  C   VAL A 530     4806   3644   2425    630   -150    260       C  
ATOM   3978  O   VAL A 530      33.693 -18.443 -38.918  1.00 22.03           O  
ANISOU 3978  O   VAL A 530     3901   2833   1638    598   -161    194       O  
ATOM   3979  CB  VAL A 530      34.774 -15.373 -39.791  1.00 26.05           C  
ANISOU 3979  CB  VAL A 530     4673   3246   1977    611     80    369       C  
ATOM   3980  CG1 VAL A 530      35.815 -16.029 -38.911  1.00 23.71           C  
ANISOU 3980  CG1 VAL A 530     4254   2950   1806    519    138    324       C  
ATOM   3981  CG2 VAL A 530      35.415 -14.782 -41.072  1.00 24.71           C  
ANISOU 3981  CG2 VAL A 530     4660   3062   1666    637    185    408       C  
ATOM   3982  N   LYS A 531      32.477 -16.763 -38.051  1.00 21.78           N  
ANISOU 3982  N   LYS A 531     3889   2763   1625    631   -201    289       N  
ATOM   3983  CA  LYS A 531      32.051 -17.579 -36.915  1.00 20.81           C  
ANISOU 3983  CA  LYS A 531     3625   2651   1630    588   -268    246       C  
ATOM   3984  C   LYS A 531      31.054 -18.666 -37.317  1.00 21.02           C  
ANISOU 3984  C   LYS A 531     3609   2727   1650    626   -394    179       C  
ATOM   3985  O   LYS A 531      31.178 -19.791 -36.880  1.00 20.54           O  
ANISOU 3985  O   LYS A 531     3462   2675   1667    583   -421    123       O  
ATOM   3986  CB  LYS A 531      31.532 -16.722 -35.760  1.00 20.22           C  
ANISOU 3986  CB  LYS A 531     3505   2547   1629    572   -274    291       C  
ATOM   3987  CG  LYS A 531      32.605 -15.796 -35.161  1.00 23.96           C  
ANISOU 3987  CG  LYS A 531     3998   2969   2135    514   -150    339       C  
ATOM   3988  CD  LYS A 531      33.875 -16.554 -34.742  1.00 19.45           C  
ANISOU 3988  CD  LYS A 531     3358   2399   1631    437    -83    300       C  
ATOM   3989  CE  LYS A 531      34.867 -15.620 -34.058  1.00 27.44           C  
ANISOU 3989  CE  LYS A 531     4371   3370   2687    373     29    336       C  
ATOM   3990  NZ  LYS A 531      36.198 -16.243 -33.791  1.00 19.01           N1+
ANISOU 3990  NZ  LYS A 531     3239   2310   1672    309     99    297       N1+
ATOM   3991  N   ARG A 532      30.103 -18.356 -38.194  1.00 25.76           N  
ANISOU 3991  N   ARG A 532     4275   3358   2154    708   -470    182       N  
ATOM   3992  CA  ARG A 532      29.195 -19.394 -38.698  1.00 22.26           C  
ANISOU 3992  CA  ARG A 532     3792   2967   1698    740   -590    105       C  
ATOM   3993  C   ARG A 532      29.970 -20.538 -39.357  1.00 28.74           C  
ANISOU 3993  C   ARG A 532     4622   3801   2498    717   -569     40       C  
ATOM   3994  O   ARG A 532      29.718 -21.717 -39.111  1.00 25.35           O  
ANISOU 3994  O   ARG A 532     4110   3384   2137    684   -625    -32       O  
ATOM   3995  CB  ARG A 532      28.188 -18.817 -39.705  1.00 23.36           C  
ANISOU 3995  CB  ARG A 532     4014   3147   1717    844   -675    115       C  
ATOM   3996  CG  ARG A 532      27.291 -19.889 -40.336  1.00 23.97           C  
ANISOU 3996  CG  ARG A 532     4048   3286   1772    875   -803     22       C  
ATOM   3997  CD  ARG A 532      26.422 -19.372 -41.480  1.00 30.71           C  
ANISOU 3997  CD  ARG A 532     4991   4192   2485    988   -893     24       C  
ATOM   3998  NE  ARG A 532      27.123 -19.284 -42.768  1.00 32.69           N  
ANISOU 3998  NE  ARG A 532     5384   4452   2585   1034   -848     32       N  
ATOM   3999  CZ  ARG A 532      27.376 -20.326 -43.558  1.00 33.81           C  
ANISOU 3999  CZ  ARG A 532     5540   4627   2679   1030   -873    -47       C  
ATOM   4000  NH1 ARG A 532      27.012 -21.542 -43.182  1.00 37.45           N1+
ANISOU 4000  NH1 ARG A 532     5883   5107   3238    977   -939   -139       N1+
ATOM   4001  NH2 ARG A 532      28.004 -20.166 -44.721  1.00 32.39           N  
ANISOU 4001  NH2 ARG A 532     5496   4458   2354   1075   -824    -36       N  
ATOM   4002  N   VAL A 533      30.927 -20.181 -40.196  1.00 23.03           N  
ANISOU 4002  N   VAL A 533     4002   3069   1678    731   -479     64       N  
ATOM   4003  CA  VAL A 533      31.643 -21.180 -40.960  1.00 31.13           C  
ANISOU 4003  CA  VAL A 533     5050   4112   2668    723   -454      0       C  
ATOM   4004  C   VAL A 533      32.650 -21.934 -40.105  1.00 28.90           C  
ANISOU 4004  C   VAL A 533     4677   3798   2505    642   -387    -27       C  
ATOM   4005  O   VAL A 533      32.761 -23.157 -40.197  1.00 30.19           O  
ANISOU 4005  O   VAL A 533     4794   3970   2707    626   -420   -102       O  
ATOM   4006  CB  VAL A 533      32.340 -20.554 -42.161  1.00 30.34           C  
ANISOU 4006  CB  VAL A 533     5092   4015   2419    766   -371     32       C  
ATOM   4007  CG1 VAL A 533      33.178 -21.599 -42.878  1.00 24.85           C  
ANISOU 4007  CG1 VAL A 533     4412   3337   1693    753   -331    -39       C  
ATOM   4008  CG2 VAL A 533      31.305 -19.958 -43.088  1.00 25.46           C  
ANISOU 4008  CG2 VAL A 533     4573   3433   1669    861   -455     53       C  
ATOM   4009  N   GLY A 534      33.382 -21.205 -39.273  1.00 23.40           N  
ANISOU 4009  N   GLY A 534     3958   3065   1868    596   -296     32       N  
ATOM   4010  CA  GLY A 534      34.379 -21.824 -38.425  1.00 21.22           C  
ANISOU 4010  CA  GLY A 534     3595   2766   1702    529   -236     10       C  
ATOM   4011  C   GLY A 534      33.804 -22.560 -37.228  1.00 21.68           C  
ANISOU 4011  C   GLY A 534     3536   2813   1888    492   -310    -14       C  
ATOM   4012  O   GLY A 534      34.251 -23.667 -36.922  1.00 21.22           O  
ANISOU 4012  O   GLY A 534     3418   2747   1896    464   -313    -66       O  
ATOM   4013  N   ASP A 535      32.833 -21.951 -36.542  1.00 19.97           N  
ANISOU 4013  N   ASP A 535     3291   2593   1704    494   -363     24       N  
ATOM   4014  CA  ASP A 535      32.259 -22.549 -35.334  1.00 30.29           C  
ANISOU 4014  CA  ASP A 535     4491   3888   3129    454   -420      9       C  
ATOM   4015  C   ASP A 535      31.334 -23.722 -35.657  1.00 31.95           C  
ANISOU 4015  C   ASP A 535     4669   4118   3355    465   -522    -62       C  
ATOM   4016  O   ASP A 535      31.414 -24.769 -35.011  1.00 29.33           O  
ANISOU 4016  O   ASP A 535     4268   3766   3111    424   -540   -100       O  
ATOM   4017  CB  ASP A 535      31.447 -21.542 -34.513  1.00 28.23           C  
ANISOU 4017  CB  ASP A 535     4207   3620   2897    453   -442     64       C  
ATOM   4018  CG  ASP A 535      32.291 -20.433 -33.881  1.00 29.60           C  
ANISOU 4018  CG  ASP A 535     4396   3765   3087    424   -345    128       C  
ATOM   4019  OD1 ASP A 535      33.540 -20.538 -33.824  1.00 25.78           O  
ANISOU 4019  OD1 ASP A 535     3912   3267   2615    390   -262    126       O  
ATOM   4020  OD2 ASP A 535      31.667 -19.453 -33.403  1.00 24.08           O1-
ANISOU 4020  OD2 ASP A 535     3701   3056   2392    434   -353    174       O1-
ATOM   4021  N   THR A 536      30.443 -23.540 -36.634  1.00 25.47           N  
ANISOU 4021  N   THR A 536     3898   3334   2447    521   -591    -82       N  
ATOM   4022  CA  THR A 536      29.326 -24.476 -36.818  1.00 27.24           C  
ANISOU 4022  CA  THR A 536     4074   3581   2696    526   -701   -153       C  
ATOM   4023  C   THR A 536      29.382 -25.362 -38.070  1.00 28.24           C  
ANISOU 4023  C   THR A 536     4249   3731   2748    556   -738   -232       C  
ATOM   4024  O   THR A 536      28.889 -26.492 -38.052  1.00 25.48           O  
ANISOU 4024  O   THR A 536     3849   3381   2451    531   -801   -306       O  
ATOM   4025  CB  THR A 536      27.941 -23.752 -36.798  1.00 25.02           C  
ANISOU 4025  CB  THR A 536     3776   3335   2395    566   -785   -138       C  
ATOM   4026  CG2 THR A 536      27.806 -22.846 -35.564  1.00 22.42           C  
ANISOU 4026  CG2 THR A 536     3401   2982   2136    540   -748    -66       C  
ATOM   4027  OG1 THR A 536      27.773 -22.984 -38.000  1.00 34.96           O  
ANISOU 4027  OG1 THR A 536     5137   4630   3517    646   -803   -122       O  
ATOM   4028  N   LEU A 537      29.965 -24.862 -39.151  1.00 22.18           N  
ANISOU 4028  N   LEU A 537     3585   2983   1858    606   -696   -218       N  
ATOM   4029  CA  LEU A 537      29.974 -25.625 -40.392  1.00 29.60           C  
ANISOU 4029  CA  LEU A 537     4583   3953   2712    641   -733   -295       C  
ATOM   4030  C   LEU A 537      31.169 -26.583 -40.517  1.00 29.17           C  
ANISOU 4030  C   LEU A 537     4530   3868   2684    609   -660   -339       C  
ATOM   4031  O   LEU A 537      30.995 -27.732 -40.906  1.00 27.01           O  
ANISOU 4031  O   LEU A 537     4243   3595   2425    604   -708   -426       O  
ATOM   4032  CB  LEU A 537      29.889 -24.692 -41.608  1.00 29.01           C  
ANISOU 4032  CB  LEU A 537     4630   3919   2474    721   -732   -266       C  
ATOM   4033  CG  LEU A 537      29.725 -25.396 -42.952  1.00 35.65           C  
ANISOU 4033  CG  LEU A 537     5538   4803   3203    769   -786   -349       C  
ATOM   4034  CD1 LEU A 537      28.328 -26.002 -43.083  1.00 31.04           C  
ANISOU 4034  CD1 LEU A 537     4896   4260   2639    783   -933   -426       C  
ATOM   4035  CD2 LEU A 537      30.016 -24.443 -44.101  1.00 34.96           C  
ANISOU 4035  CD2 LEU A 537     5593   4745   2944    844   -746   -302       C  
ATOM   4036  N   LEU A 538      32.365 -26.111 -40.170  1.00 24.06           N  
ANISOU 4036  N   LEU A 538     3896   3194   2051    589   -545   -285       N  
ATOM   4037  CA  LEU A 538      33.591 -26.857 -40.441  1.00 25.78           C  
ANISOU 4037  CA  LEU A 538     4122   3394   2277    576   -467   -325       C  
ATOM   4038  C   LEU A 538      34.402 -27.244 -39.201  1.00 26.81           C  
ANISOU 4038  C   LEU A 538     4165   3480   2543    519   -412   -310       C  
ATOM   4039  O   LEU A 538      35.248 -28.134 -39.271  1.00 30.39           O  
ANISOU 4039  O   LEU A 538     4602   3915   3030    512   -373   -358       O  
ATOM   4040  CB  LEU A 538      34.489 -26.078 -41.412  1.00 24.99           C  
ANISOU 4040  CB  LEU A 538     4124   3314   2055    609   -368   -295       C  
ATOM   4041  CG  LEU A 538      33.885 -25.717 -42.773  1.00 27.73           C  
ANISOU 4041  CG  LEU A 538     4584   3708   2244    677   -410   -308       C  
ATOM   4042  CD1 LEU A 538      34.817 -24.803 -43.530  1.00 25.13           C  
ANISOU 4042  CD1 LEU A 538     4360   3387   1803    699   -290   -256       C  
ATOM   4043  CD2 LEU A 538      33.603 -26.963 -43.580  1.00 31.37           C  
ANISOU 4043  CD2 LEU A 538     5058   4190   2672    700   -478   -415       C  
ATOM   4044  N   GLY A 539      34.167 -26.573 -38.077  1.00 29.46           N  
ANISOU 4044  N   GLY A 539     4445   3799   2949    487   -410   -244       N  
ATOM   4045  CA  GLY A 539      34.895 -26.878 -36.851  1.00 22.67           C  
ANISOU 4045  CA  GLY A 539     3505   2903   2207    439   -367   -227       C  
ATOM   4046  C   GLY A 539      36.360 -26.462 -36.879  1.00 26.61           C  
ANISOU 4046  C   GLY A 539     4011   3401   2697    432   -251   -205       C  
ATOM   4047  O   GLY A 539      37.252 -27.290 -36.685  1.00 29.35           O  
ANISOU 4047  O   GLY A 539     4321   3733   3097    424   -216   -244       O  
ATOM   4048  N   MET A 540      36.608 -25.174 -37.109  1.00 23.28           N  
ANISOU 4048  N   MET A 540     3638   2994   2213    434   -189   -147       N  
ATOM   4049  CA  MET A 540      37.970 -24.647 -37.130  1.00 26.42           C  
ANISOU 4049  CA  MET A 540     4038   3394   2607    414    -69   -128       C  
ATOM   4050  C   MET A 540      38.097 -23.434 -36.231  1.00 30.15           C  
ANISOU 4050  C   MET A 540     4487   3853   3115    376    -27    -56       C  
ATOM   4051  O   MET A 540      37.218 -22.570 -36.195  1.00 29.32           O  
ANISOU 4051  O   MET A 540     4422   3744   2974    385    -59     -8       O  
ATOM   4052  CB  MET A 540      38.398 -24.268 -38.556  1.00 21.43           C  
ANISOU 4052  CB  MET A 540     3510   2786   1847    447     -2   -137       C  
ATOM   4053  CG  MET A 540      38.260 -25.408 -39.558  1.00 38.84           C  
ANISOU 4053  CG  MET A 540     5750   5007   4000    489    -42   -215       C  
ATOM   4054  SD  MET A 540      38.588 -24.897 -41.262  1.00 31.08           S  
ANISOU 4054  SD  MET A 540     4908   4059   2843    536     31   -220       S  
ATOM   4055  CE  MET A 540      37.466 -23.522 -41.340  1.00 86.50           C  
ANISOU 4055  CE  MET A 540    12002  11079   9787    556    -12   -133       C  
ATOM   4056  N   ALA A 541      39.213 -23.365 -35.522  1.00 30.72           N  
ANISOU 4056  N   ALA A 541     4495   3920   3257    336     44    -55       N  
ATOM   4057  CA  ALA A 541      39.455 -22.277 -34.591  1.00 29.78           C  
ANISOU 4057  CA  ALA A 541     4346   3789   3181    292     86      0       C  
ATOM   4058  C   ALA A 541      39.903 -21.033 -35.351  1.00 27.26           C  
ANISOU 4058  C   ALA A 541     4111   3469   2779    283    187     39       C  
ATOM   4059  O   ALA A 541      40.774 -21.112 -36.214  1.00 20.65           O  
ANISOU 4059  O   ALA A 541     3306   2646   1893    286    269     14       O  
ATOM   4060  CB  ALA A 541      40.493 -22.694 -33.532  1.00 18.72           C  
ANISOU 4060  CB  ALA A 541     2839   2389   1884    255    115    -22       C  
ATOM   4061  N   THR A 542      39.279 -19.898 -35.035  1.00 24.38           N  
ANISOU 4061  N   THR A 542     3783   3081   2397    274    184     99       N  
ATOM   4062  CA  THR A 542      39.574 -18.619 -35.667  1.00 26.33           C  
ANISOU 4062  CA  THR A 542     4125   3311   2567    265    279    148       C  
ATOM   4063  C   THR A 542      39.803 -17.567 -34.584  1.00 25.19           C  
ANISOU 4063  C   THR A 542     3946   3137   2489    209    322    189       C  
ATOM   4064  O   THR A 542      39.166 -17.596 -33.540  1.00 18.99           O  
ANISOU 4064  O   THR A 542     3100   2344   1770    202    249    199       O  
ATOM   4065  CB  THR A 542      38.392 -18.115 -36.560  1.00 24.99           C  
ANISOU 4065  CB  THR A 542     4074   3135   2288    329    228    189       C  
ATOM   4066  CG2 THR A 542      38.154 -19.028 -37.762  1.00 21.30           C  
ANISOU 4066  CG2 THR A 542     3658   2700   1734    386    188    144       C  
ATOM   4067  OG1 THR A 542      37.194 -18.056 -35.770  1.00 22.16           O  
ANISOU 4067  OG1 THR A 542     3678   2769   1973    347    121    207       O  
ATOM   4068  N   GLN A 543      40.719 -16.641 -34.838  1.00 25.09           N  
ANISOU 4068  N   GLN A 543     3971   3106   2457    164    444    209       N  
ATOM   4069  CA  GLN A 543      40.904 -15.492 -33.966  1.00 25.17           C  
ANISOU 4069  CA  GLN A 543     3968   3079   2516    108    493    246       C  
ATOM   4070  C   GLN A 543      40.847 -14.257 -34.820  1.00 22.71           C  
ANISOU 4070  C   GLN A 543     3794   2722   2112    111    580    304       C  
ATOM   4071  O   GLN A 543      41.715 -14.048 -35.660  1.00 27.77           O  
ANISOU 4071  O   GLN A 543     4486   3362   2703     89    690    300       O  
ATOM   4072  CB  GLN A 543      42.260 -15.538 -33.271  1.00 26.05           C  
ANISOU 4072  CB  GLN A 543     3976   3206   2717     33    571    203       C  
ATOM   4073  CG  GLN A 543      42.482 -14.338 -32.380  1.00 25.08           C  
ANISOU 4073  CG  GLN A 543     3840   3045   2644    -32    622    230       C  
ATOM   4074  CD  GLN A 543      41.321 -14.133 -31.421  1.00 26.72           C  
ANISOU 4074  CD  GLN A 543     4035   3234   2884     -9    519    260       C  
ATOM   4075  NE2 GLN A 543      40.608 -13.017 -31.569  1.00 19.39           N  
ANISOU 4075  NE2 GLN A 543     3203   2253   1910      3    534    318       N  
ATOM   4076  OE1 GLN A 543      41.049 -14.988 -30.579  1.00 18.41           O  
ANISOU 4076  OE1 GLN A 543     2891   2211   1893      2    430    233       O  
ATOM   4077  N   CYS A 544      39.820 -13.440 -34.638  1.00 24.19           N  
ANISOU 4077  N   CYS A 544     4048   2871   2273    142    537    360       N  
ATOM   4078  CA  CYS A 544      39.688 -12.260 -35.482  1.00 23.98           C  
ANISOU 4078  CA  CYS A 544     4170   2791   2150    159    614    425       C  
ATOM   4079  C   CYS A 544      40.387 -11.077 -34.858  1.00 29.25           C  
ANISOU 4079  C   CYS A 544     4844   3402   2869     77    724    448       C  
ATOM   4080  O   CYS A 544      40.442 -10.960 -33.635  1.00 29.31           O  
ANISOU 4080  O   CYS A 544     4754   3405   2976     32    699    429       O  
ATOM   4081  CB  CYS A 544      38.226 -11.926 -35.730  1.00 21.86           C  
ANISOU 4081  CB  CYS A 544     3981   2506   1817    249    512    473       C  
ATOM   4082  SG  CYS A 544      37.343 -13.200 -36.648  1.00 25.26           S  
ANISOU 4082  SG  CYS A 544     4421   3003   2172    344    385    439       S  
ATOM   4083  N   VAL A 545      40.922 -10.204 -35.707  1.00 26.38           N  
ANISOU 4083  N   VAL A 545     4600   2991   2434     56    850    488       N  
ATOM   4084  CA  VAL A 545      41.574  -8.985 -35.249  1.00 26.58           C  
ANISOU 4084  CA  VAL A 545     4650   2948   2501    -29    970    511       C  
ATOM   4085  C   VAL A 545      41.313  -7.825 -36.228  1.00 31.81           C  
ANISOU 4085  C   VAL A 545     5507   3530   3051     -1   1056    593       C  
ATOM   4086  O   VAL A 545      41.454  -7.968 -37.449  1.00 31.47           O  
ANISOU 4086  O   VAL A 545     5566   3493   2899     36   1103    616       O  
ATOM   4087  CB  VAL A 545      43.098  -9.202 -35.003  1.00 23.84           C  
ANISOU 4087  CB  VAL A 545     4200   2628   2229   -136   1082    446       C  
ATOM   4088  CG1 VAL A 545      43.791  -9.732 -36.253  1.00 35.49           C  
ANISOU 4088  CG1 VAL A 545     5719   4137   3627   -129   1162    431       C  
ATOM   4089  CG2 VAL A 545      43.760  -7.921 -34.547  1.00 25.31           C  
ANISOU 4089  CG2 VAL A 545     4410   2742   2464   -235   1208    461       C  
ATOM   4090  N   GLN A 546      40.902  -6.687 -35.677  1.00 33.34           N  
ANISOU 4090  N   GLN A 546     5756   3644   3266    -13   1073    640       N  
ATOM   4091  CA  GLN A 546      40.671  -5.476 -36.453  1.00 39.93           C  
ANISOU 4091  CA  GLN A 546     6782   4384   4005     13   1160    725       C  
ATOM   4092  C   GLN A 546      41.957  -5.028 -37.137  1.00 36.41           C  
ANISOU 4092  C   GLN A 546     6398   3902   3533    -79   1345    728       C  
ATOM   4093  O   GLN A 546      43.023  -5.045 -36.519  1.00 34.90           O  
ANISOU 4093  O   GLN A 546     6095   3723   3444   -193   1426    669       O  
ATOM   4094  CB  GLN A 546      40.195  -4.370 -35.521  1.00 46.83           C  
ANISOU 4094  CB  GLN A 546     7678   5175   4939     -3   1157    756       C  
ATOM   4095  CG  GLN A 546      39.056  -3.555 -36.056  1.00 60.93           C  
ANISOU 4095  CG  GLN A 546     9610   6899   6640    108   1106    832       C  
ATOM   4096  CD  GLN A 546      37.719  -4.198 -35.800  1.00 66.11           C  
ANISOU 4096  CD  GLN A 546    10233   7609   7275    223    935    838       C  
ATOM   4097  NE2 GLN A 546      37.422  -5.278 -36.526  1.00 58.60           N  
ANISOU 4097  NE2 GLN A 546     9260   6743   6260    287    853    817       N  
ATOM   4098  OE1 GLN A 546      36.950  -3.724 -34.960  1.00 72.96           O  
ANISOU 4098  OE1 GLN A 546    11077   8447   8195    251    871    848       O  
ATOM   4099  N   VAL A 547      41.859  -4.609 -38.399  1.00 35.63           N  
ANISOU 4099  N   VAL A 547     6431   3775   3331    -26   1379    770       N  
ATOM   4100  CA  VAL A 547      43.039  -4.175 -39.158  1.00 31.65           C  
ANISOU 4100  CA  VAL A 547     5959   3245   2820   -105   1531    756       C  
ATOM   4101  C   VAL A 547      43.810  -3.023 -38.490  1.00 37.30           C  
ANISOU 4101  C   VAL A 547     6650   3881   3642   -223   1641    741       C  
ATOM   4102  O   VAL A 547      45.046  -2.979 -38.547  1.00 37.73           O  
ANISOU 4102  O   VAL A 547     6644   3942   3748   -331   1764    693       O  
ATOM   4103  CB  VAL A 547      42.714  -3.879 -40.664  1.00 36.59           C  
ANISOU 4103  CB  VAL A 547     6739   3852   3313    -19   1538    807       C  
ATOM   4104  CG1 VAL A 547      41.525  -2.931 -40.814  1.00 34.11           C  
ANISOU 4104  CG1 VAL A 547     6539   3469   2954     80   1457    873       C  
ATOM   4105  CG2 VAL A 547      43.932  -3.337 -41.384  1.00 36.47           C  
ANISOU 4105  CG2 VAL A 547     6762   3801   3296   -107   1702    797       C  
ATOM   4106  N   LYS A 548      43.093  -2.121 -37.820  1.00 36.04           N  
ANISOU 4106  N   LYS A 548     6525   3651   3519   -202   1594    772       N  
ATOM   4107  CA  LYS A 548      43.738  -1.017 -37.107  1.00 41.17           C  
ANISOU 4107  CA  LYS A 548     7152   4222   4268   -309   1687    749       C  
ATOM   4108  C   LYS A 548      44.662  -1.537 -35.994  1.00 44.53           C  
ANISOU 4108  C   LYS A 548     7403   4700   4815   -430   1723    668       C  
ATOM   4109  O   LYS A 548      45.664  -0.909 -35.648  1.00 43.84           O  
ANISOU 4109  O   LYS A 548     7267   4581   4810   -546   1827    621       O  
ATOM   4110  CB  LYS A 548      42.693  -0.062 -36.524  1.00 44.82           C  
ANISOU 4110  CB  LYS A 548     7678   4607   4744   -251   1618    791       C  
ATOM   4111  CG  LYS A 548      41.823  -0.701 -35.455  1.00 55.70           C  
ANISOU 4111  CG  LYS A 548     8970   6033   6162   -206   1487    782       C  
ATOM   4112  CD  LYS A 548      40.974   0.313 -34.705  1.00 58.82           C  
ANISOU 4112  CD  LYS A 548     9405   6351   6595   -171   1440    806       C  
ATOM   4113  CE  LYS A 548      40.281  -0.334 -33.518  1.00 51.52           C  
ANISOU 4113  CE  LYS A 548     8376   5473   5725   -149   1327    788       C  
ATOM   4114  NZ  LYS A 548      39.600   0.668 -32.646  1.00 58.46           N1+
ANISOU 4114  NZ  LYS A 548     9278   6280   6656   -132   1297    798       N1+
ATOM   4115  N   ASN A 549      44.327  -2.695 -35.441  1.00 41.85           N  
ANISOU 4115  N   ASN A 549     6970   4445   4488   -401   1633    647       N  
ATOM   4116  CA  ASN A 549      45.159  -3.292 -34.406  1.00 35.10           C  
ANISOU 4116  CA  ASN A 549     5944   3650   3741   -504   1657    568       C  
ATOM   4117  C   ASN A 549      46.339  -4.047 -34.992  1.00 34.60           C  
ANISOU 4117  C   ASN A 549     5805   3659   3681   -563   1746    512       C  
ATOM   4118  O   ASN A 549      47.330  -4.298 -34.307  1.00 34.74           O  
ANISOU 4118  O   ASN A 549     5669   3726   3804   -659   1786    429       O  
ATOM   4119  CB  ASN A 549      44.318  -4.180 -33.501  1.00 35.48           C  
ANISOU 4119  CB  ASN A 549     5878   3771   3833   -432   1476    541       C  
ATOM   4120  CG  ASN A 549      43.322  -3.380 -32.686  1.00 38.44           C  
ANISOU 4120  CG  ASN A 549     6296   4078   4230   -398   1408    579       C  
ATOM   4121  ND2 ASN A 549      42.143  -3.948 -32.452  1.00 34.38           N  
ANISOU 4121  ND2 ASN A 549     5766   3603   3695   -290   1253    596       N  
ATOM   4122  OD1 ASN A 549      43.609  -2.252 -32.281  1.00 43.72           O  
ANISOU 4122  OD1 ASN A 549     7013   4659   4939   -472   1498    588       O  
ATOM   4123  N   VAL A 550      46.228  -4.388 -36.273  1.00 38.23           N  
ANISOU 4123  N   VAL A 550     6360   4135   4030   -494   1760    546       N  
ATOM   4124  CA  VAL A 550      47.326  -4.993 -37.015  1.00 40.23           C  
ANISOU 4124  CA  VAL A 550     6563   4449   4273   -539   1856    496       C  
ATOM   4125  C   VAL A 550      48.272  -3.904 -37.462  1.00 42.68           C  
ANISOU 4125  C   VAL A 550     6907   4696   4614   -628   1991    485       C  
ATOM   4126  O   VAL A 550      49.490  -4.080 -37.461  1.00 45.41           O  
ANISOU 4126  O   VAL A 550     7146   5083   5026   -722   2087    414       O  
ATOM   4127  CB  VAL A 550      46.832  -5.743 -38.257  1.00 40.00           C  
ANISOU 4127  CB  VAL A 550     6633   4458   4105   -429   1820    533       C  
ATOM   4128  CG1 VAL A 550      48.007  -6.211 -39.092  1.00 31.41           C  
ANISOU 4128  CG1 VAL A 550     5505   3424   3006   -477   1934    481       C  
ATOM   4129  CG2 VAL A 550      45.965  -6.919 -37.848  1.00 41.17           C  
ANISOU 4129  CG2 VAL A 550     6708   4684   4251   -333   1646    514       C  
ATOM   4130  N   VAL A 551      47.696  -2.770 -37.836  1.00 45.22           N  
ANISOU 4130  N   VAL A 551     7375   4917   4890   -595   1996    553       N  
ATOM   4131  CA  VAL A 551      48.477  -1.645 -38.331  1.00 50.67           C  
ANISOU 4131  CA  VAL A 551     8127   5530   5596   -672   2126    553       C  
ATOM   4132  C   VAL A 551      49.256  -0.972 -37.202  1.00 55.43           C  
ANISOU 4132  C   VAL A 551     8617   6106   6340   -800   2181    486       C  
ATOM   4133  O   VAL A 551      50.401  -0.565 -37.387  1.00 62.09           O  
ANISOU 4133  O   VAL A 551     9416   6939   7235   -903   2300    435       O  
ATOM   4134  CB  VAL A 551      47.584  -0.637 -39.085  1.00 48.04           C  
ANISOU 4134  CB  VAL A 551     7992   5095   5166   -587   2114    645       C  
ATOM   4135  CG1 VAL A 551      48.302   0.678 -39.286  1.00 54.68           C  
ANISOU 4135  CG1 VAL A 551     8896   5837   6043   -676   2246    644       C  
ATOM   4136  CG2 VAL A 551      47.159  -1.224 -40.422  1.00 44.82           C  
ANISOU 4136  CG2 VAL A 551     7692   4721   4618   -482   2091    695       C  
ATOM   4137  N   LYS A 552      48.645  -0.877 -36.027  1.00 54.95           N  
ANISOU 4137  N   LYS A 552     8503   6036   6339   -794   2091    479       N  
ATOM   4138  CA  LYS A 552      49.325  -0.305 -34.870  1.00 54.50           C  
ANISOU 4138  CA  LYS A 552     8331   5964   6412   -910   2125    407       C  
ATOM   4139  C   LYS A 552      49.402  -1.315 -33.739  1.00 52.20           C  
ANISOU 4139  C   LYS A 552     7865   5771   6200   -930   2044    343       C  
ATOM   4140  O   LYS A 552      48.498  -1.397 -32.921  1.00 64.37           O  
ANISOU 4140  O   LYS A 552     9402   7305   7751   -884   1942    365       O  
ATOM   4141  CB  LYS A 552      48.619   0.971 -34.410  1.00 60.92           C  
ANISOU 4141  CB  LYS A 552     9248   6664   7236   -898   2108    447       C  
ATOM   4142  CG  LYS A 552      48.867   2.164 -35.325  1.00 70.91           C  
ANISOU 4142  CG  LYS A 552    10662   7823   8456   -914   2217    486       C  
ATOM   4143  CD  LYS A 552      48.111   3.406 -34.877  1.00 75.04           C  
ANISOU 4143  CD  LYS A 552    11293   8233   8986   -890   2200    525       C  
ATOM   4144  CE  LYS A 552      46.644   3.344 -35.270  1.00 76.18           C  
ANISOU 4144  CE  LYS A 552    11564   8353   9027   -735   2090    619       C  
ATOM   4145  NZ  LYS A 552      45.949   4.632 -34.980  1.00 74.62           N1+
ANISOU 4145  NZ  LYS A 552    11481   8042   8830   -702   2087    658       N1+
ATOM   4146  N   THR A 553      50.487  -2.078 -33.696  1.00 47.97           N  
ANISOU 4146  N   THR A 553     7181   5326   5718   -996   2089    263       N  
ATOM   4147  CA  THR A 553      50.622  -3.169 -32.738  1.00 45.97           C  
ANISOU 4147  CA  THR A 553     6757   5176   5532  -1006   2015    200       C  
ATOM   4148  C   THR A 553      51.072  -2.684 -31.371  1.00 53.09           C  
ANISOU 4148  C   THR A 553     7531   6082   6560  -1099   1998    125       C  
ATOM   4149  O   THR A 553      52.241  -2.346 -31.188  1.00 64.38           O  
ANISOU 4149  O   THR A 553     8860   7533   8070  -1199   2071     43       O  
ATOM   4150  CB  THR A 553      51.648  -4.219 -33.211  1.00 52.40           C  
ANISOU 4150  CB  THR A 553     7448   6098   6362  -1029   2066    132       C  
ATOM   4151  CG2 THR A 553      51.309  -4.710 -34.601  1.00 58.53           C  
ANISOU 4151  CG2 THR A 553     8349   6878   7010   -942   2089    194       C  
ATOM   4152  OG1 THR A 553      52.967  -3.650 -33.214  1.00 47.96           O  
ANISOU 4152  OG1 THR A 553     6801   5541   5882  -1141   2169     55       O  
ATOM   4153  N   SER A 554      50.157  -2.655 -30.407  1.00 43.96           N  
ANISOU 4153  N   SER A 554     6375   4908   5418  -1066   1899    147       N  
ATOM   4154  CA  SER A 554      50.550  -2.407 -29.026  1.00 39.02           C  
ANISOU 4154  CA  SER A 554     5613   4306   4907  -1146   1864     66       C  
ATOM   4155  C   SER A 554      50.802  -3.739 -28.323  1.00 36.56           C  
ANISOU 4155  C   SER A 554     5114   4130   4644  -1106   1737     -4       C  
ATOM   4156  O   SER A 554      50.131  -4.724 -28.607  1.00 29.21           O  
ANISOU 4156  O   SER A 554     4193   3249   3659   -990   1629     33       O  
ATOM   4157  CB  SER A 554      49.479  -1.604 -28.281  1.00 42.40           C  
ANISOU 4157  CB  SER A 554     6131   4648   5331  -1117   1799    114       C  
ATOM   4158  OG  SER A 554      48.293  -2.357 -28.132  1.00 50.66           O  
ANISOU 4158  OG  SER A 554     7200   5727   6324   -984   1649    166       O  
ATOM   4159  N   PRO A 555      51.782  -3.774 -27.407  1.00 38.14           N  
ANISOU 4159  N   PRO A 555     5147   4396   4951  -1194   1739   -109       N  
ATOM   4160  CA  PRO A 555      52.124  -5.000 -26.676  1.00 37.07           C  
ANISOU 4160  CA  PRO A 555     4830   4389   4864  -1147   1610   -179       C  
ATOM   4161  C   PRO A 555      50.954  -5.572 -25.887  1.00 36.82           C  
ANISOU 4161  C   PRO A 555     4806   4374   4809  -1036   1434   -139       C  
ATOM   4162  O   PRO A 555      50.757  -6.793 -25.861  1.00 33.93           O  
ANISOU 4162  O   PRO A 555     4377   4085   4428   -946   1328   -141       O  
ATOM   4163  CB  PRO A 555      53.209  -4.530 -25.708  1.00 35.44           C  
ANISOU 4163  CB  PRO A 555     4475   4222   4770  -1268   1645   -290       C  
ATOM   4164  CG  PRO A 555      53.855  -3.374 -26.413  1.00 35.84           C  
ANISOU 4164  CG  PRO A 555     4598   4189   4829  -1384   1826   -295       C  
ATOM   4165  CD  PRO A 555      52.739  -2.685 -27.143  1.00 34.64           C  
ANISOU 4165  CD  PRO A 555     4671   3912   4581  -1331   1856   -173       C  
ATOM   4166  N   GLN A 556      50.197  -4.695 -25.238  1.00 37.40           N  
ANISOU 4166  N   GLN A 556     4955   4373   4882  -1046   1410   -107       N  
ATOM   4167  CA  GLN A 556      49.079  -5.112 -24.401  1.00 30.70           C  
ANISOU 4167  CA  GLN A 556     4110   3537   4017   -954   1257    -74       C  
ATOM   4168  C   GLN A 556      48.035  -5.844 -25.238  1.00 30.62           C  
ANISOU 4168  C   GLN A 556     4194   3522   3918   -831   1193     11       C  
ATOM   4169  O   GLN A 556      47.549  -6.908 -24.847  1.00 31.77           O  
ANISOU 4169  O   GLN A 556     4281   3732   4058   -750   1067     13       O  
ATOM   4170  CB  GLN A 556      48.443  -3.899 -23.706  1.00 34.57           C  
ANISOU 4170  CB  GLN A 556     4682   3936   4517   -988   1266    -54       C  
ATOM   4171  CG  GLN A 556      48.468  -3.942 -22.177  1.00 51.89           C  
ANISOU 4171  CG  GLN A 556     6764   6180   6773  -1007   1170   -119       C  
ATOM   4172  CD  GLN A 556      47.552  -5.000 -21.586  1.00 59.41           C  
ANISOU 4172  CD  GLN A 556     7682   7193   7699   -894   1012    -91       C  
ATOM   4173  NE2 GLN A 556      48.051  -5.723 -20.589  1.00 59.50           N  
ANISOU 4173  NE2 GLN A 556     7551   7299   7756   -895    927   -158       N  
ATOM   4174  OE1 GLN A 556      46.411  -5.164 -22.017  1.00 68.50           O  
ANISOU 4174  OE1 GLN A 556     8933   8306   8788   -806    969    -11       O  
ATOM   4175  N   THR A 557      47.693  -5.256 -26.383  1.00 23.36           N  
ANISOU 4175  N   THR A 557     3425   2522   2928   -820   1282     80       N  
ATOM   4176  CA  THR A 557      46.718  -5.838 -27.308  1.00 32.60           C  
ANISOU 4176  CA  THR A 557     4695   3686   4005   -706   1228    157       C  
ATOM   4177  C   THR A 557      47.136  -7.215 -27.823  1.00 22.61           C  
ANISOU 4177  C   THR A 557     3348   2515   2728   -659   1187    127       C  
ATOM   4178  O   THR A 557      46.345  -8.145 -27.820  1.00 21.93           O  
ANISOU 4178  O   THR A 557     3255   2466   2612   -565   1071    149       O  
ATOM   4179  CB  THR A 557      46.430  -4.892 -28.504  1.00 28.18           C  
ANISOU 4179  CB  THR A 557     4318   3025   3363   -705   1341    233       C  
ATOM   4180  CG2 THR A 557      45.691  -5.616 -29.606  1.00 23.60           C  
ANISOU 4180  CG2 THR A 557     3824   2461   2682   -593   1292    293       C  
ATOM   4181  OG1 THR A 557      45.612  -3.809 -28.056  1.00 33.07           O  
ANISOU 4181  OG1 THR A 557     5036   3552   3977   -700   1337    279       O  
ATOM   4182  N   LEU A 558      48.380  -7.350 -28.256  1.00 25.91           N  
ANISOU 4182  N   LEU A 558     3701   2968   3174   -726   1287     73       N  
ATOM   4183  CA  LEU A 558      48.846  -8.640 -28.740  1.00 28.46           C  
ANISOU 4183  CA  LEU A 558     3944   3378   3491   -679   1255     37       C  
ATOM   4184  C   LEU A 558      48.850  -9.662 -27.604  1.00 23.83           C  
ANISOU 4184  C   LEU A 558     3212   2873   2970   -641   1116    -14       C  
ATOM   4185  O   LEU A 558      48.468 -10.815 -27.795  1.00 24.13           O  
ANISOU 4185  O   LEU A 558     3229   2956   2984   -555   1026     -8       O  
ATOM   4186  CB  LEU A 558      50.238  -8.519 -29.359  1.00 30.96           C  
ANISOU 4186  CB  LEU A 558     4207   3722   3835   -763   1399    -21       C  
ATOM   4187  CG  LEU A 558      50.365  -7.712 -30.652  1.00 37.65           C  
ANISOU 4187  CG  LEU A 558     5203   4495   4605   -798   1553     31       C  
ATOM   4188  CD1 LEU A 558      51.718  -7.935 -31.257  1.00 35.53           C  
ANISOU 4188  CD1 LEU A 558     4856   4278   4365   -866   1681    -36       C  
ATOM   4189  CD2 LEU A 558      49.285  -8.087 -31.644  1.00 36.41           C  
ANISOU 4189  CD2 LEU A 558     5193   4312   4330   -686   1505    114       C  
ATOM   4190  N   SER A 559      49.277  -9.225 -26.421  1.00 25.46           N  
ANISOU 4190  N   SER A 559     3325   3093   3254   -704   1101    -64       N  
ATOM   4191  CA  SER A 559      49.304 -10.095 -25.240  1.00 27.46           C  
ANISOU 4191  CA  SER A 559     3451   3421   3563   -668    971   -108       C  
ATOM   4192  C   SER A 559      47.909 -10.631 -24.909  1.00 25.47           C  
ANISOU 4192  C   SER A 559     3257   3153   3268   -572    842    -45       C  
ATOM   4193  O   SER A 559      47.739 -11.822 -24.677  1.00 23.72           O  
ANISOU 4193  O   SER A 559     2978   2985   3051   -504    746    -54       O  
ATOM   4194  CB  SER A 559      49.889  -9.368 -24.030  1.00 27.32           C  
ANISOU 4194  CB  SER A 559     3344   3415   3620   -753    976   -169       C  
ATOM   4195  OG  SER A 559      49.796 -10.177 -22.863  1.00 33.82           O  
ANISOU 4195  OG  SER A 559     4065   4306   4480   -707    843   -200       O  
ATOM   4196  N   ASN A 560      46.917  -9.747 -24.909  1.00 20.17           N  
ANISOU 4196  N   ASN A 560     2701   2406   2559   -568    846     16       N  
ATOM   4197  CA  ASN A 560      45.517 -10.155 -24.754  1.00 19.24           C  
ANISOU 4197  CA  ASN A 560     2643   2270   2397   -480    739     76       C  
ATOM   4198  C   ASN A 560      45.021 -11.146 -25.810  1.00 20.92           C  
ANISOU 4198  C   ASN A 560     2901   2498   2549   -396    702    109       C  
ATOM   4199  O   ASN A 560      44.250 -12.056 -25.494  1.00 20.55           O  
ANISOU 4199  O   ASN A 560     2835   2477   2497   -329    593    122       O  
ATOM   4200  CB  ASN A 560      44.606  -8.918 -24.686  1.00 19.29           C  
ANISOU 4200  CB  ASN A 560     2765   2190   2373   -486    764    131       C  
ATOM   4201  CG  ASN A 560      44.649  -8.226 -23.299  1.00 25.63           C  
ANISOU 4201  CG  ASN A 560     3518   2985   3236   -540    745     99       C  
ATOM   4202  ND2 ASN A 560      44.123  -7.014 -23.220  1.00 23.67           N  
ANISOU 4202  ND2 ASN A 560     3365   2655   2975   -561    791    132       N  
ATOM   4203  OD1 ASN A 560      45.141  -8.791 -22.328  1.00 23.43           O  
ANISOU 4203  OD1 ASN A 560     3121   2771   3009   -555    688     45       O  
ATOM   4204  N   LEU A 561      45.462 -10.972 -27.061  1.00 25.56           N  
ANISOU 4204  N   LEU A 561     3553   3070   3090   -405    796    118       N  
ATOM   4205  CA  LEU A 561      45.103 -11.900 -28.142  1.00 25.66           C  
ANISOU 4205  CA  LEU A 561     3611   3101   3038   -330    768    138       C  
ATOM   4206  C   LEU A 561      45.612 -13.311 -27.826  1.00 23.15           C  
ANISOU 4206  C   LEU A 561     3173   2859   2765   -299    700     82       C  
ATOM   4207  O   LEU A 561      44.909 -14.300 -28.045  1.00 18.82           O  
ANISOU 4207  O   LEU A 561     2634   2327   2191   -226    612     94       O  
ATOM   4208  CB  LEU A 561      45.639 -11.424 -29.497  1.00 21.85           C  
ANISOU 4208  CB  LEU A 561     3217   2591   2492   -351    895    152       C  
ATOM   4209  CG  LEU A 561      44.791 -10.427 -30.290  1.00 28.28           C  
ANISOU 4209  CG  LEU A 561     4199   3328   3220   -328    936    231       C  
ATOM   4210  CD1 LEU A 561      45.640  -9.715 -31.330  1.00 29.55           C  
ANISOU 4210  CD1 LEU A 561     4437   3454   3336   -382   1093    239       C  
ATOM   4211  CD2 LEU A 561      43.622 -11.117 -30.979  1.00 26.50           C  
ANISOU 4211  CD2 LEU A 561     4045   3109   2915   -222    839    271       C  
ATOM   4212  N   CYS A 562      46.828 -13.385 -27.290  1.00 20.88           N  
ANISOU 4212  N   CYS A 562     2771   2616   2547   -355    739     18       N  
ATOM   4213  CA  CYS A 562      47.407 -14.659 -26.863  1.00 23.80           C  
ANISOU 4213  CA  CYS A 562     3022   3055   2966   -321    674    -37       C  
ATOM   4214  C   CYS A 562      46.562 -15.386 -25.831  1.00 23.61           C  
ANISOU 4214  C   CYS A 562     2966   3040   2962   -268    537    -22       C  
ATOM   4215  O   CYS A 562      46.471 -16.620 -25.881  1.00 21.44           O  
ANISOU 4215  O   CYS A 562     2659   2795   2693   -206    468    -35       O  
ATOM   4216  CB  CYS A 562      48.817 -14.461 -26.321  1.00 25.46           C  
ANISOU 4216  CB  CYS A 562     3108   3316   3252   -388    730   -112       C  
ATOM   4217  SG  CYS A 562      49.962 -14.009 -27.614  1.00 30.10           S  
ANISOU 4217  SG  CYS A 562     3706   3909   3824   -446    896   -146       S  
ATOM   4218  N   LEU A 563      45.943 -14.623 -24.921  1.00 21.04           N  
ANISOU 4218  N   LEU A 563     2658   2687   2650   -293    507      5       N  
ATOM   4219  CA  LEU A 563      45.100 -15.188 -23.862  1.00 20.84           C  
ANISOU 4219  CA  LEU A 563     2609   2668   2642   -252    391     23       C  
ATOM   4220  C   LEU A 563      43.944 -15.967 -24.460  1.00 22.34           C  
ANISOU 4220  C   LEU A 563     2867   2839   2784   -179    326     67       C  
ATOM   4221  O   LEU A 563      43.622 -17.080 -24.025  1.00 17.08           O  
ANISOU 4221  O   LEU A 563     2162   2193   2135   -133    241     63       O  
ATOM   4222  CB  LEU A 563      44.527 -14.091 -22.947  1.00 21.20           C  
ANISOU 4222  CB  LEU A 563     2680   2680   2696   -291    386     47       C  
ATOM   4223  CG  LEU A 563      45.451 -13.214 -22.102  1.00 25.88           C  
ANISOU 4223  CG  LEU A 563     3208   3286   3339   -369    433      0       C  
ATOM   4224  CD1 LEU A 563      44.629 -12.333 -21.173  1.00 26.84           C  
ANISOU 4224  CD1 LEU A 563     3367   3370   3461   -388    408     26       C  
ATOM   4225  CD2 LEU A 563      46.422 -14.043 -21.307  1.00 22.37           C  
ANISOU 4225  CD2 LEU A 563     2636   2916   2948   -368    386    -61       C  
ATOM   4226  N   LYS A 564      43.320 -15.365 -25.466  1.00 22.23           N  
ANISOU 4226  N   LYS A 564     2956   2782   2708   -169    367    107       N  
ATOM   4227  CA  LYS A 564      42.195 -15.987 -26.149  1.00 24.22           C  
ANISOU 4227  CA  LYS A 564     3273   3019   2909   -102    306    141       C  
ATOM   4228  C   LYS A 564      42.653 -17.186 -26.977  1.00 23.03           C  
ANISOU 4228  C   LYS A 564     3105   2900   2747    -64    298    108       C  
ATOM   4229  O   LYS A 564      42.033 -18.255 -26.936  1.00 20.54           O  
ANISOU 4229  O   LYS A 564     2780   2592   2434    -15    216    105       O  
ATOM   4230  CB  LYS A 564      41.478 -14.962 -27.031  1.00 24.06           C  
ANISOU 4230  CB  LYS A 564     3371   2951   2819    -93    348    190       C  
ATOM   4231  CG  LYS A 564      40.810 -13.837 -26.238  1.00 23.77           C  
ANISOU 4231  CG  LYS A 564     3363   2875   2793   -115    345    225       C  
ATOM   4232  CD  LYS A 564      40.716 -12.552 -27.057  1.00 25.26           C  
ANISOU 4232  CD  LYS A 564     3663   3008   2925   -126    430    264       C  
ATOM   4233  CE  LYS A 564      39.883 -12.726 -28.317  1.00 26.47           C  
ANISOU 4233  CE  LYS A 564     3916   3149   2993    -55    409    302       C  
ATOM   4234  NZ  LYS A 564      38.452 -12.995 -28.036  1.00 21.29           N1+
ANISOU 4234  NZ  LYS A 564     3270   2493   2327      7    302    327       N1+
ATOM   4235  N   ILE A 565      43.744 -17.006 -27.715  1.00 21.00           N  
ANISOU 4235  N   ILE A 565     2844   2657   2480    -89    389     78       N  
ATOM   4236  CA  ILE A 565      44.222 -18.034 -28.633  1.00 22.05           C  
ANISOU 4236  CA  ILE A 565     2969   2816   2592    -51    398     42       C  
ATOM   4237  C   ILE A 565      44.612 -19.299 -27.878  1.00 22.68           C  
ANISOU 4237  C   ILE A 565     2949   2931   2737    -22    327      0       C  
ATOM   4238  O   ILE A 565      44.220 -20.400 -28.258  1.00 23.18           O  
ANISOU 4238  O   ILE A 565     3023   2995   2789     32    269    -11       O  
ATOM   4239  CB  ILE A 565      45.430 -17.548 -29.448  1.00 23.08           C  
ANISOU 4239  CB  ILE A 565     3101   2960   2707    -91    525     13       C  
ATOM   4240  CG1 ILE A 565      44.999 -16.453 -30.424  1.00 19.38           C  
ANISOU 4240  CG1 ILE A 565     2761   2448   2155   -105    600     63       C  
ATOM   4241  CG2 ILE A 565      46.091 -18.725 -30.178  1.00 22.77           C  
ANISOU 4241  CG2 ILE A 565     3028   2959   2664    -49    533    -39       C  
ATOM   4242  CD1 ILE A 565      46.150 -15.676 -30.984  1.00 22.41           C  
ANISOU 4242  CD1 ILE A 565     3151   2832   2532   -168    742     44       C  
ATOM   4243  N   ASN A 566      45.362 -19.134 -26.795  1.00 19.19           N  
ANISOU 4243  N   ASN A 566     2415   2514   2362    -57    327    -25       N  
ATOM   4244  CA  ASN A 566      45.774 -20.279 -25.994  1.00 17.46           C  
ANISOU 4244  CA  ASN A 566     2106   2327   2201    -22    256    -59       C  
ATOM   4245  C   ASN A 566      44.614 -21.159 -25.536  1.00 20.40           C  
ANISOU 4245  C   ASN A 566     2506   2674   2573     26    150    -27       C  
ATOM   4246  O   ASN A 566      44.667 -22.384 -25.680  1.00 19.64           O  
ANISOU 4246  O   ASN A 566     2394   2579   2489     77    104    -48       O  
ATOM   4247  CB  ASN A 566      46.623 -19.832 -24.811  1.00 17.56           C  
ANISOU 4247  CB  ASN A 566     2023   2374   2275    -63    260    -86       C  
ATOM   4248  CG  ASN A 566      47.377 -20.970 -24.183  1.00 27.18           C  
ANISOU 4248  CG  ASN A 566     3146   3634   3546    -18    203   -130       C  
ATOM   4249  ND2 ASN A 566      47.138 -21.207 -22.881  1.00 17.32           N  
ANISOU 4249  ND2 ASN A 566     1860   2392   2328     -7    123   -117       N  
ATOM   4250  OD1 ASN A 566      48.177 -21.632 -24.848  1.00 24.72           O  
ANISOU 4250  OD1 ASN A 566     2798   3348   3245     12    233   -175       O  
ATOM   4251  N   VAL A 567      43.548 -20.562 -25.016  1.00 16.22           N  
ANISOU 4251  N   VAL A 567     2019   2116   2029     10    115     21       N  
ATOM   4252  CA  VAL A 567      42.448 -21.405 -24.539  1.00 20.39           C  
ANISOU 4252  CA  VAL A 567     2563   2621   2562     46     23     46       C  
ATOM   4253  C   VAL A 567      41.602 -21.973 -25.683  1.00 23.28           C  
ANISOU 4253  C   VAL A 567     3000   2964   2883     84      2     52       C  
ATOM   4254  O   VAL A 567      41.071 -23.077 -25.588  1.00 25.08           O  
ANISOU 4254  O   VAL A 567     3227   3177   3124    117    -62     48       O  
ATOM   4255  CB  VAL A 567      41.576 -20.711 -23.468  1.00 17.91           C  
ANISOU 4255  CB  VAL A 567     2256   2292   2257     20    -11     88       C  
ATOM   4256  CG1 VAL A 567      42.425 -20.402 -22.208  1.00 15.15           C  
ANISOU 4256  CG1 VAL A 567     1832   1973   1954    -10    -10     71       C  
ATOM   4257  CG2 VAL A 567      40.948 -19.444 -24.016  1.00 15.91           C  
ANISOU 4257  CG2 VAL A 567     2071   2015   1958     -3     33    119       C  
ATOM   4258  N   LYS A 568      41.485 -21.220 -26.767  1.00 16.04           N  
ANISOU 4258  N   LYS A 568     2148   2041   1908     78     57     61       N  
ATOM   4259  CA  LYS A 568      40.788 -21.717 -27.958  1.00 17.36           C  
ANISOU 4259  CA  LYS A 568     2383   2196   2018    118     37     58       C  
ATOM   4260  C   LYS A 568      41.453 -22.987 -28.482  1.00 19.16           C  
ANISOU 4260  C   LYS A 568     2587   2436   2258    153     32      6       C  
ATOM   4261  O   LYS A 568      40.799 -23.863 -29.037  1.00 21.82           O  
ANISOU 4261  O   LYS A 568     2956   2759   2576    188    -19     -9       O  
ATOM   4262  CB  LYS A 568      40.766 -20.657 -29.062  1.00 16.73           C  
ANISOU 4262  CB  LYS A 568     2385   2111   1862    112    107     77       C  
ATOM   4263  CG  LYS A 568      39.691 -19.602 -28.888  1.00 22.58           C  
ANISOU 4263  CG  LYS A 568     3179   2827   2573    106     90    130       C  
ATOM   4264  CD  LYS A 568      39.788 -18.539 -29.978  1.00 30.00           C  
ANISOU 4264  CD  LYS A 568     4213   3754   3433    107    166    155       C  
ATOM   4265  CE  LYS A 568      38.697 -17.494 -29.831  1.00 30.84           C  
ANISOU 4265  CE  LYS A 568     4378   3830   3508    116    145    208       C  
ATOM   4266  NZ  LYS A 568      38.795 -16.409 -30.860  1.00 26.00           N1+
ANISOU 4266  NZ  LYS A 568     3873   3194   2814    122    221    242       N1+
ATOM   4267  N   LEU A 569      42.759 -23.078 -28.289  1.00 19.52           N  
ANISOU 4267  N   LEU A 569     2571   2506   2338    143     84    -27       N  
ATOM   4268  CA  LEU A 569      43.512 -24.246 -28.729  1.00 19.23           C  
ANISOU 4268  CA  LEU A 569     2504   2482   2320    183     85    -80       C  
ATOM   4269  C   LEU A 569      43.671 -25.290 -27.628  1.00 24.17           C  
ANISOU 4269  C   LEU A 569     3064   3102   3018    207     15    -92       C  
ATOM   4270  O   LEU A 569      44.457 -26.213 -27.776  1.00 32.96           O  
ANISOU 4270  O   LEU A 569     4140   4223   4160    245     17   -137       O  
ATOM   4271  CB  LEU A 569      44.877 -23.818 -29.271  1.00 19.98           C  
ANISOU 4271  CB  LEU A 569     2566   2614   2411    167    187   -118       C  
ATOM   4272  CG  LEU A 569      44.881 -23.433 -30.765  1.00 19.62           C  
ANISOU 4272  CG  LEU A 569     2604   2570   2281    170    260   -125       C  
ATOM   4273  CD1 LEU A 569      43.798 -22.439 -31.118  1.00 18.49           C  
ANISOU 4273  CD1 LEU A 569     2553   2401   2071    152    257    -67       C  
ATOM   4274  CD2 LEU A 569      46.226 -22.894 -31.188  1.00 21.75           C  
ANISOU 4274  CD2 LEU A 569     2836   2875   2552    139    376   -159       C  
ATOM   4275  N   GLY A 570      42.936 -25.127 -26.523  1.00 22.34           N  
ANISOU 4275  N   GLY A 570     2823   2853   2813    190    -42    -50       N  
ATOM   4276  CA  GLY A 570      42.915 -26.103 -25.440  1.00 18.35           C  
ANISOU 4276  CA  GLY A 570     2276   2333   2364    214   -110    -48       C  
ATOM   4277  C   GLY A 570      43.953 -25.938 -24.332  1.00 25.89           C  
ANISOU 4277  C   GLY A 570     3149   3323   3367    210   -107    -56       C  
ATOM   4278  O   GLY A 570      44.197 -26.863 -23.537  1.00 19.88           O  
ANISOU 4278  O   GLY A 570     2355   2552   2645    246   -159    -59       O  
ATOM   4279  N   GLY A 571      44.581 -24.768 -24.277  1.00 25.41           N  
ANISOU 4279  N   GLY A 571     3058   3299   3300    166    -47    -61       N  
ATOM   4280  CA  GLY A 571      45.561 -24.493 -23.250  1.00 22.77           C  
ANISOU 4280  CA  GLY A 571     2638   3006   3008    156    -47    -79       C  
ATOM   4281  C   GLY A 571      44.903 -24.025 -21.962  1.00 20.97           C  
ANISOU 4281  C   GLY A 571     2410   2771   2788    129    -95    -36       C  
ATOM   4282  O   GLY A 571      43.697 -23.810 -21.905  1.00 18.86           O  
ANISOU 4282  O   GLY A 571     2204   2467   2496    114   -117      8       O  
ATOM   4283  N   ILE A 572      45.708 -23.868 -20.922  1.00 19.78           N  
ANISOU 4283  N   ILE A 572     2185   2660   2669    125   -112    -54       N  
ATOM   4284  CA  ILE A 572      45.255 -23.262 -19.676  1.00 20.67           C  
ANISOU 4284  CA  ILE A 572     2295   2777   2783     94   -146    -22       C  
ATOM   4285  C   ILE A 572      46.162 -22.074 -19.384  1.00 18.41           C  
ANISOU 4285  C   ILE A 572     1947   2538   2509     39    -95    -59       C  
ATOM   4286  O   ILE A 572      47.391 -22.191 -19.408  1.00 17.00           O  
ANISOU 4286  O   ILE A 572     1689   2409   2361     48    -78   -114       O  
ATOM   4287  CB  ILE A 572      45.314 -24.271 -18.511  1.00 25.92           C  
ANISOU 4287  CB  ILE A 572     2936   3445   3468    146   -229    -10       C  
ATOM   4288  CG1 ILE A 572      44.280 -25.386 -18.722  1.00 24.37           C  
ANISOU 4288  CG1 ILE A 572     2809   3188   3263    184   -271     30       C  
ATOM   4289  CG2 ILE A 572      45.108 -23.569 -17.169  1.00 22.87           C  
ANISOU 4289  CG2 ILE A 572     2535   3079   3075    114   -257     11       C  
ATOM   4290  CD1 ILE A 572      44.549 -26.637 -17.866  1.00 25.36           C  
ANISOU 4290  CD1 ILE A 572     2923   3303   3410    248   -339     39       C  
ATOM   4291  N   ASN A 573      45.564 -20.920 -19.135  1.00 16.02           N  
ANISOU 4291  N   ASN A 573     1680   2219   2187    -18    -68    -35       N  
ATOM   4292  CA  ASN A 573      46.350 -19.711 -18.942  1.00 16.41           C  
ANISOU 4292  CA  ASN A 573     1684   2300   2250    -82    -10    -72       C  
ATOM   4293  C   ASN A 573      46.966 -19.639 -17.544  1.00 19.29           C  
ANISOU 4293  C   ASN A 573     1971   2715   2641    -87    -60   -102       C  
ATOM   4294  O   ASN A 573      48.177 -19.411 -17.388  1.00 19.99           O  
ANISOU 4294  O   ASN A 573     1971   2859   2763   -106    -40   -164       O  
ATOM   4295  CB  ASN A 573      45.506 -18.473 -19.275  1.00 16.09           C  
ANISOU 4295  CB  ASN A 573     1720   2213   2179   -137     44    -37       C  
ATOM   4296  CG  ASN A 573      45.179 -18.372 -20.757  1.00 20.86           C  
ANISOU 4296  CG  ASN A 573     2394   2781   2750   -133    103    -20       C  
ATOM   4297  ND2 ASN A 573      44.343 -17.383 -21.123  1.00 15.92           N  
ANISOU 4297  ND2 ASN A 573     1849   2110   2090   -161    140     19       N  
ATOM   4298  OD1 ASN A 573      45.690 -19.157 -21.575  1.00 20.02           O  
ANISOU 4298  OD1 ASN A 573     2273   2688   2645    -99    116    -42       O  
ATOM   4299  N   ASN A 574      46.131 -19.846 -16.533  1.00 19.18           N  
ANISOU 4299  N   ASN A 574     1990   2687   2611    -69   -126    -60       N  
ATOM   4300  CA  ASN A 574      46.582 -19.933 -15.144  1.00 16.44           C  
ANISOU 4300  CA  ASN A 574     1586   2388   2271    -59   -189    -80       C  
ATOM   4301  C   ASN A 574      45.553 -20.720 -14.331  1.00 18.69           C  
ANISOU 4301  C   ASN A 574     1928   2645   2530    -13   -261    -19       C  
ATOM   4302  O   ASN A 574      44.457 -20.984 -14.823  1.00 16.86           O  
ANISOU 4302  O   ASN A 574     1768   2357   2281     -6   -254     30       O  
ATOM   4303  CB  ASN A 574      46.765 -18.531 -14.554  1.00 20.49           C  
ANISOU 4303  CB  ASN A 574     2081   2919   2786   -135   -154   -109       C  
ATOM   4304  CG  ASN A 574      45.461 -17.733 -14.519  1.00 25.89           C  
ANISOU 4304  CG  ASN A 574     2855   3542   3438   -170   -129    -57       C  
ATOM   4305  ND2 ASN A 574      45.505 -16.489 -14.998  1.00 23.55           N  
ANISOU 4305  ND2 ASN A 574     2578   3223   3146   -236    -51    -73       N  
ATOM   4306  OD1 ASN A 574      44.428 -18.235 -14.082  1.00 28.87           O  
ANISOU 4306  OD1 ASN A 574     3285   3893   3792   -136   -174     -5       O  
ATOM   4307  N   ILE A 575      45.889 -21.088 -13.099  1.00 16.26           N  
ANISOU 4307  N   ILE A 575     1586   2375   2215     17   -327    -24       N  
ATOM   4308  CA  ILE A 575      44.908 -21.687 -12.183  1.00 16.20           C  
ANISOU 4308  CA  ILE A 575     1639   2340   2176     48   -382     36       C  
ATOM   4309  C   ILE A 575      44.913 -20.938 -10.854  1.00 17.28           C  
ANISOU 4309  C   ILE A 575     1765   2514   2287     21   -407     27       C  
ATOM   4310  O   ILE A 575      45.903 -20.288 -10.502  1.00 18.13           O  
ANISOU 4310  O   ILE A 575     1802   2680   2406     -3   -408    -34       O  
ATOM   4311  CB  ILE A 575      45.198 -23.189 -11.885  1.00 18.00           C  
ANISOU 4311  CB  ILE A 575     1867   2565   2406    133   -448     56       C  
ATOM   4312  CG1 ILE A 575      46.547 -23.355 -11.177  1.00 17.11           C  
ANISOU 4312  CG1 ILE A 575     1670   2528   2302    174   -498      4       C  
ATOM   4313  CG2 ILE A 575      45.148 -24.020 -13.161  1.00 22.35           C  
ANISOU 4313  CG2 ILE A 575     2436   3074   2982    164   -427     60       C  
ATOM   4314  CD1 ILE A 575      46.893 -24.811 -10.796  1.00 17.61           C  
ANISOU 4314  CD1 ILE A 575     1740   2587   2365    273   -569     26       C  
ATOM   4315  N   LEU A 576      43.808 -21.016 -10.117  1.00 16.17           N  
ANISOU 4315  N   LEU A 576     1689   2343   2111     21   -425     81       N  
ATOM   4316  CA  LEU A 576      43.820 -20.557  -8.728  1.00 22.62           C  
ANISOU 4316  CA  LEU A 576     2503   3199   2891     11   -460     75       C  
ATOM   4317  C   LEU A 576      44.845 -21.400  -8.000  1.00 23.09           C  
ANISOU 4317  C   LEU A 576     2518   3314   2942     77   -534     56       C  
ATOM   4318  O   LEU A 576      44.820 -22.636  -8.100  1.00 18.85           O  
ANISOU 4318  O   LEU A 576     2004   2754   2405    143   -570     93       O  
ATOM   4319  CB  LEU A 576      42.459 -20.775  -8.056  1.00 20.42           C  
ANISOU 4319  CB  LEU A 576     2305   2879   2575     13   -465    141       C  
ATOM   4320  CG  LEU A 576      41.294 -19.922  -8.545  1.00 20.26           C  
ANISOU 4320  CG  LEU A 576     2330   2811   2558    -41   -403    162       C  
ATOM   4321  CD1 LEU A 576      40.024 -20.396  -7.880  1.00 21.46           C  
ANISOU 4321  CD1 LEU A 576     2544   2929   2679    -31   -411    223       C  
ATOM   4322  CD2 LEU A 576      41.549 -18.455  -8.237  1.00 21.58           C  
ANISOU 4322  CD2 LEU A 576     2476   3003   2722    -98   -369    113       C  
ATOM   4323  N   VAL A 577      45.760 -20.749  -7.296  1.00 22.36           N  
ANISOU 4323  N   VAL A 577     2361   3293   2842     63   -560     -6       N  
ATOM   4324  CA  VAL A 577      46.657 -21.480  -6.411  1.00 25.77           C  
ANISOU 4324  CA  VAL A 577     2751   3788   3252    136   -646    -24       C  
ATOM   4325  C   VAL A 577      45.788 -22.362  -5.501  1.00 37.69           C  
ANISOU 4325  C   VAL A 577     4353   5264   4703    189   -690     58       C  
ATOM   4326  O   VAL A 577      44.959 -21.853  -4.742  1.00 34.65           O  
ANISOU 4326  O   VAL A 577     4023   4869   4274    155   -679     85       O  
ATOM   4327  CB  VAL A 577      47.544 -20.534  -5.603  1.00 28.73           C  
ANISOU 4327  CB  VAL A 577     3051   4249   3617    104   -673   -105       C  
ATOM   4328  CG1 VAL A 577      48.184 -21.264  -4.417  1.00 30.00           C  
ANISOU 4328  CG1 VAL A 577     3193   4476   3729    189   -777   -109       C  
ATOM   4329  CG2 VAL A 577      48.602 -19.915  -6.522  1.00 27.02           C  
ANISOU 4329  CG2 VAL A 577     2731   4067   3467     59   -629   -189       C  
ATOM   4330  N   PRO A 578      45.962 -23.695  -5.612  1.00 40.46           N  
ANISOU 4330  N   PRO A 578     4726   5591   5056    271   -732     98       N  
ATOM   4331  CA  PRO A 578      44.993 -24.684  -5.121  1.00 35.79           C  
ANISOU 4331  CA  PRO A 578     4238   4936   4426    311   -748    188       C  
ATOM   4332  C   PRO A 578      44.676 -24.647  -3.624  1.00 34.68           C  
ANISOU 4332  C   PRO A 578     4151   4821   4205    329   -790    221       C  
ATOM   4333  O   PRO A 578      43.536 -24.948  -3.266  1.00 34.40           O  
ANISOU 4333  O   PRO A 578     4204   4729   4140    314   -764    290       O  
ATOM   4334  CB  PRO A 578      45.613 -26.031  -5.538  1.00 33.74           C  
ANISOU 4334  CB  PRO A 578     3975   4654   4191    402   -790    203       C  
ATOM   4335  CG  PRO A 578      47.047 -25.740  -5.794  1.00 37.67           C  
ANISOU 4335  CG  PRO A 578     4358   5233   4721    428   -821    117       C  
ATOM   4336  CD  PRO A 578      47.088 -24.339  -6.311  1.00 38.79           C  
ANISOU 4336  CD  PRO A 578     4443   5405   4892    328   -757     57       C  
ATOM   4337  N   HIS A 579      45.629 -24.268  -2.777  1.00 31.65           N  
ANISOU 4337  N   HIS A 579     3714   4525   3787    356   -852    170       N  
ATOM   4338  CA  HIS A 579      45.412 -24.326  -1.328  1.00 27.94           C  
ANISOU 4338  CA  HIS A 579     3303   4086   3227    386   -901    202       C  
ATOM   4339  C   HIS A 579      44.436 -23.274  -0.796  1.00 30.59           C  
ANISOU 4339  C   HIS A 579     3680   4418   3527    303   -847    206       C  
ATOM   4340  O   HIS A 579      43.992 -23.362   0.362  1.00 32.99           O  
ANISOU 4340  O   HIS A 579     4053   4734   3749    320   -869    244       O  
ATOM   4341  CB  HIS A 579      46.742 -24.261  -0.554  1.00 24.25           C  
ANISOU 4341  CB  HIS A 579     2764   3724   2726    449   -995    138       C  
ATOM   4342  CG  HIS A 579      47.478 -22.965  -0.706  1.00 37.94           C  
ANISOU 4342  CG  HIS A 579     4388   5535   4493    381   -986     30       C  
ATOM   4343  CD2 HIS A 579      48.653 -22.673  -1.314  1.00 47.28           C  
ANISOU 4343  CD2 HIS A 579     5449   6776   5738    379  -1001    -58       C  
ATOM   4344  ND1 HIS A 579      47.018 -21.775  -0.177  1.00 40.82           N  
ANISOU 4344  ND1 HIS A 579     4763   5920   4829    300   -952     -1       N  
ATOM   4345  CE1 HIS A 579      47.872 -20.808  -0.459  1.00 39.99           C  
ANISOU 4345  CE1 HIS A 579     4552   5874   4768    246   -947   -102       C  
ATOM   4346  NE2 HIS A 579      48.876 -21.326  -1.144  1.00 46.83           N  
ANISOU 4346  NE2 HIS A 579     5334   6768   5691    290   -974   -139       N  
ATOM   4347  N   GLN A 580      44.107 -22.281  -1.618  1.00 25.40           N  
ANISOU 4347  N   GLN A 580     2985   3741   2923    218   -776    167       N  
ATOM   4348  CA  GLN A 580      43.218 -21.214  -1.152  1.00 34.17           C  
ANISOU 4348  CA  GLN A 580     4131   4846   4006    146   -725    163       C  
ATOM   4349  C   GLN A 580      41.735 -21.484  -1.460  1.00 33.64           C  
ANISOU 4349  C   GLN A 580     4144   4694   3945    118   -658    239       C  
ATOM   4350  O   GLN A 580      40.860 -20.679  -1.131  1.00 35.12           O  
ANISOU 4350  O   GLN A 580     4361   4869   4113     66   -610    242       O  
ATOM   4351  CB  GLN A 580      43.654 -19.850  -1.694  1.00 33.51           C  
ANISOU 4351  CB  GLN A 580     3973   4788   3970     71   -685     78       C  
ATOM   4352  CG  GLN A 580      43.457 -19.672  -3.190  1.00 37.26           C  
ANISOU 4352  CG  GLN A 580     4427   5207   4525     33   -619     77       C  
ATOM   4353  CD  GLN A 580      44.474 -18.713  -3.801  1.00 39.58           C  
ANISOU 4353  CD  GLN A 580     4631   5538   4870    -16   -597    -12       C  
ATOM   4354  NE2 GLN A 580      44.803 -18.938  -5.057  1.00 34.17           N  
ANISOU 4354  NE2 GLN A 580     3912   4825   4244    -19   -565    -19       N  
ATOM   4355  OE1 GLN A 580      44.964 -17.788  -3.140  1.00 42.07           O  
ANISOU 4355  OE1 GLN A 580     4911   5905   5170    -53   -607    -78       O  
ATOM   4356  N   ARG A 581      41.457 -22.639  -2.052  1.00 27.44           N  
ANISOU 4356  N   ARG A 581     3389   3852   3185    156   -658    296       N  
ATOM   4357  CA  ARG A 581      40.104 -22.966  -2.478  1.00 20.78           C  
ANISOU 4357  CA  ARG A 581     2605   2931   2360    125   -599    356       C  
ATOM   4358  C   ARG A 581      39.143 -23.480  -1.382  1.00 22.90           C  
ANISOU 4358  C   ARG A 581     2961   3175   2565    133   -589    425       C  
ATOM   4359  O   ARG A 581      39.549 -23.932  -0.299  1.00 27.85           O  
ANISOU 4359  O   ARG A 581     3625   3834   3124    181   -637    447       O  
ATOM   4360  CB  ARG A 581      40.176 -23.951  -3.641  1.00 25.63           C  
ANISOU 4360  CB  ARG A 581     3214   3489   3034    151   -597    376       C  
ATOM   4361  CG  ARG A 581      40.855 -23.362  -4.859  1.00 26.33           C  
ANISOU 4361  CG  ARG A 581     3228   3592   3185    130   -581    314       C  
ATOM   4362  CD  ARG A 581      41.004 -24.412  -5.951  1.00 28.60           C  
ANISOU 4362  CD  ARG A 581     3515   3831   3521    165   -584    329       C  
ATOM   4363  NE  ARG A 581      41.656 -25.609  -5.432  1.00 29.35           N  
ANISOU 4363  NE  ARG A 581     3629   3926   3598    244   -644    354       N  
ATOM   4364  CZ  ARG A 581      41.576 -26.799  -6.006  1.00 30.17           C  
ANISOU 4364  CZ  ARG A 581     3764   3969   3730    285   -652    386       C  
ATOM   4365  NH1 ARG A 581      40.865 -26.945  -7.117  1.00 27.41           N1+
ANISOU 4365  NH1 ARG A 581     3425   3564   3426    250   -605    390       N1+
ATOM   4366  NH2 ARG A 581      42.186 -27.841  -5.460  1.00 36.80           N  
ANISOU 4366  NH2 ARG A 581     4630   4805   4550    366   -708    411       N  
ATOM   4367  N   SER A 582      37.855 -23.388  -1.680  1.00 29.72           N  
ANISOU 4367  N   SER A 582     3856   3986   3449     85   -525    457       N  
ATOM   4368  CA  SER A 582      36.811 -23.905  -0.800  1.00 32.88           C  
ANISOU 4368  CA  SER A 582     4335   4356   3803     78   -495    522       C  
ATOM   4369  C   SER A 582      36.945 -25.421  -0.620  1.00 29.88           C  
ANISOU 4369  C   SER A 582     4015   3929   3411    132   -523    586       C  
ATOM   4370  O   SER A 582      37.460 -26.130  -1.501  1.00 29.42           O  
ANISOU 4370  O   SER A 582     3936   3838   3403    163   -549    584       O  
ATOM   4371  CB  SER A 582      35.428 -23.526  -1.365  1.00 33.49           C  
ANISOU 4371  CB  SER A 582     4411   4388   3924     16   -420    531       C  
ATOM   4372  OG  SER A 582      34.527 -24.612  -1.406  1.00 30.61           O  
ANISOU 4372  OG  SER A 582     4097   3960   3572      9   -391    592       O  
ATOM   4373  N   ALA A 583      36.489 -25.902   0.532  1.00 24.11           N  
ANISOU 4373  N   ALA A 583     3363   3189   2609    144   -514    644       N  
ATOM   4374  CA  ALA A 583      36.413 -27.332   0.826  1.00 19.72           C  
ANISOU 4374  CA  ALA A 583     2888   2570   2034    188   -525    719       C  
ATOM   4375  C   ALA A 583      35.550 -28.092  -0.201  1.00 21.14           C  
ANISOU 4375  C   ALA A 583     3076   2659   2296    150   -475    744       C  
ATOM   4376  O   ALA A 583      35.592 -29.311  -0.265  1.00 26.32           O  
ANISOU 4376  O   ALA A 583     3790   3249   2962    183   -483    794       O  
ATOM   4377  CB  ALA A 583      35.876 -27.554   2.252  1.00 19.73           C  
ANISOU 4377  CB  ALA A 583     2984   2574   1939    192   -501    779       C  
ATOM   4378  N   VAL A 584      34.772 -27.372  -1.002  1.00 23.63           N  
ANISOU 4378  N   VAL A 584     3336   2972   2671     84   -427    707       N  
ATOM   4379  CA  VAL A 584      34.060 -27.995  -2.120  1.00 33.95           C  
ANISOU 4379  CA  VAL A 584     4633   4208   4059     51   -394    712       C  
ATOM   4380  C   VAL A 584      35.006 -28.745  -3.064  1.00 31.51           C  
ANISOU 4380  C   VAL A 584     4307   3871   3795    102   -445    697       C  
ATOM   4381  O   VAL A 584      34.572 -29.655  -3.773  1.00 28.34           O  
ANISOU 4381  O   VAL A 584     3925   3398   3445     92   -429    712       O  
ATOM   4382  CB  VAL A 584      33.194 -26.963  -2.928  1.00 46.91           C  
ANISOU 4382  CB  VAL A 584     6208   5866   5751    -12   -350    665       C  
ATOM   4383  CG1 VAL A 584      34.012 -26.244  -3.984  1.00 32.52           C  
ANISOU 4383  CG1 VAL A 584     4314   4076   3965      2   -382    603       C  
ATOM   4384  CG2 VAL A 584      32.042 -27.646  -3.591  1.00 54.68           C  
ANISOU 4384  CG2 VAL A 584     7199   6783   6795    -58   -306    682       C  
ATOM   4385  N   PHE A 585      36.290 -28.377  -3.076  1.00 22.76           N  
ANISOU 4385  N   PHE A 585     3158   2820   2670    155   -503    659       N  
ATOM   4386  CA  PHE A 585      37.226 -29.019  -4.006  1.00 28.14           C  
ANISOU 4386  CA  PHE A 585     3811   3483   3397    207   -544    635       C  
ATOM   4387  C   PHE A 585      37.834 -30.313  -3.475  1.00 28.92           C  
ANISOU 4387  C   PHE A 585     3977   3541   3470    285   -588    684       C  
ATOM   4388  O   PHE A 585      38.655 -30.922  -4.159  1.00 26.18           O  
ANISOU 4388  O   PHE A 585     3610   3178   3160    340   -625    663       O  
ATOM   4389  CB  PHE A 585      38.330 -28.055  -4.470  1.00 22.34           C  
ANISOU 4389  CB  PHE A 585     2988   2827   2672    222   -577    562       C  
ATOM   4390  CG  PHE A 585      37.818 -26.922  -5.312  1.00 25.80           C  
ANISOU 4390  CG  PHE A 585     3372   3284   3149    154   -531    517       C  
ATOM   4391  CD1 PHE A 585      37.706 -27.059  -6.694  1.00 19.13           C  
ANISOU 4391  CD1 PHE A 585     2497   2406   2364    141   -514    490       C  
ATOM   4392  CD2 PHE A 585      37.422 -25.731  -4.725  1.00 23.60           C  
ANISOU 4392  CD2 PHE A 585     3078   3049   2838    110   -506    501       C  
ATOM   4393  CE1 PHE A 585      37.225 -26.022  -7.463  1.00 23.39           C  
ANISOU 4393  CE1 PHE A 585     2999   2959   2928     89   -475    456       C  
ATOM   4394  CE2 PHE A 585      36.939 -24.692  -5.492  1.00 20.32           C  
ANISOU 4394  CE2 PHE A 585     2624   2642   2455     58   -465    464       C  
ATOM   4395  CZ  PHE A 585      36.844 -24.834  -6.866  1.00 18.98           C  
ANISOU 4395  CZ  PHE A 585     2429   2440   2341     49   -451    445       C  
ATOM   4396  N   GLN A 586      37.446 -30.719  -2.262  1.00 25.90           N  
ANISOU 4396  N   GLN A 586     3677   3141   3022    296   -582    748       N  
ATOM   4397  CA  GLN A 586      37.840 -32.025  -1.721  1.00 26.70           C  
ANISOU 4397  CA  GLN A 586     3867   3183   3095    371   -615    810       C  
ATOM   4398  C   GLN A 586      37.297 -33.162  -2.567  1.00 29.10           C  
ANISOU 4398  C   GLN A 586     4213   3375   3468    357   -582    835       C  
ATOM   4399  O   GLN A 586      37.809 -34.275  -2.520  1.00 35.17           O  
ANISOU 4399  O   GLN A 586     5041   4082   4238    428   -613    869       O  
ATOM   4400  CB  GLN A 586      37.341 -32.227  -0.286  1.00 28.68           C  
ANISOU 4400  CB  GLN A 586     4216   3425   3255    374   -597    884       C  
ATOM   4401  CG  GLN A 586      38.146 -31.516   0.783  1.00 45.15           C  
ANISOU 4401  CG  GLN A 586     6292   5613   5251    424   -655    870       C  
ATOM   4402  CD  GLN A 586      39.620 -31.884   0.774  1.00 45.25           C  
ANISOU 4402  CD  GLN A 586     6276   5664   5251    535   -752    847       C  
ATOM   4403  NE2 GLN A 586      39.917 -33.177   0.669  1.00 37.41           N  
ANISOU 4403  NE2 GLN A 586     5353   4593   4269    607   -776    897       N  
ATOM   4404  OE1 GLN A 586      40.482 -31.009   0.871  1.00 55.70           O  
ANISOU 4404  OE1 GLN A 586     7515   7088   6559    555   -803    780       O  
ATOM   4405  N   GLN A 587      36.241 -32.873  -3.320  1.00 27.86           N  
ANISOU 4405  N   GLN A 587     4027   3192   3368    268   -522    814       N  
ATOM   4406  CA  GLN A 587      35.570 -33.861  -4.155  1.00 27.74           C  
ANISOU 4406  CA  GLN A 587     4044   3076   3422    236   -487    823       C  
ATOM   4407  C   GLN A 587      35.331 -33.232  -5.518  1.00 25.33           C  
ANISOU 4407  C   GLN A 587     3646   2794   3184    189   -475    750       C  
ATOM   4408  O   GLN A 587      35.492 -32.017  -5.678  1.00 24.97           O  
ANISOU 4408  O   GLN A 587     3527   2832   3128    171   -480    705       O  
ATOM   4409  CB  GLN A 587      34.235 -34.277  -3.524  1.00 24.07           C  
ANISOU 4409  CB  GLN A 587     3649   2546   2949    163   -415    881       C  
ATOM   4410  CG  GLN A 587      34.359 -34.888  -2.130  1.00 33.91           C  
ANISOU 4410  CG  GLN A 587     5006   3762   4116    204   -412    965       C  
ATOM   4411  CD  GLN A 587      33.344 -34.300  -1.162  1.00 52.68           C  
ANISOU 4411  CD  GLN A 587     7406   6166   6443    134   -348    997       C  
ATOM   4412  NE2 GLN A 587      33.796 -33.953   0.049  1.00 52.21           N  
ANISOU 4412  NE2 GLN A 587     7390   6162   6287    180   -370   1032       N  
ATOM   4413  OE1 GLN A 587      32.169 -34.144  -1.503  1.00 57.98           O  
ANISOU 4413  OE1 GLN A 587     8052   6816   7163     43   -280    984       O  
ATOM   4414  N   PRO A 588      34.960 -34.054  -6.511  1.00 25.32           N  
ANISOU 4414  N   PRO A 588     3655   2718   3249    172   -461    735       N  
ATOM   4415  CA  PRO A 588      34.630 -33.449  -7.802  1.00 24.98           C  
ANISOU 4415  CA  PRO A 588     3534   2699   3256    129   -451    667       C  
ATOM   4416  C   PRO A 588      33.474 -32.460  -7.652  1.00 25.79           C  
ANISOU 4416  C   PRO A 588     3601   2842   3356     48   -406    660       C  
ATOM   4417  O   PRO A 588      32.513 -32.716  -6.916  1.00 17.59           O  
ANISOU 4417  O   PRO A 588     2603   1771   2309      0   -363    702       O  
ATOM   4418  CB  PRO A 588      34.197 -34.647  -8.652  1.00 26.11           C  
ANISOU 4418  CB  PRO A 588     3714   2745   3462    114   -439    660       C  
ATOM   4419  CG  PRO A 588      34.854 -35.817  -8.021  1.00 26.22           C  
ANISOU 4419  CG  PRO A 588     3812   2690   3462    182   -460    710       C  
ATOM   4420  CD  PRO A 588      34.885 -35.524  -6.549  1.00 19.42           C  
ANISOU 4420  CD  PRO A 588     2992   1857   2528    194   -456    773       C  
ATOM   4421  N   VAL A 589      33.587 -31.329  -8.339  1.00 16.48           N  
ANISOU 4421  N   VAL A 589     2348   1732   2183     36   -411    608       N  
ATOM   4422  CA  VAL A 589      32.540 -30.316  -8.335  1.00 21.89           C  
ANISOU 4422  CA  VAL A 589     2993   2455   2868    -26   -374    594       C  
ATOM   4423  C   VAL A 589      32.457 -29.678  -9.716  1.00 19.02           C  
ANISOU 4423  C   VAL A 589     2570   2117   2539    -37   -380    535       C  
ATOM   4424  O   VAL A 589      33.475 -29.467 -10.364  1.00 17.05           O  
ANISOU 4424  O   VAL A 589     2297   1891   2289      4   -408    504       O  
ATOM   4425  CB  VAL A 589      32.777 -29.229  -7.244  1.00 18.56           C  
ANISOU 4425  CB  VAL A 589     2561   2103   2387    -23   -369    607       C  
ATOM   4426  CG1 VAL A 589      34.165 -28.628  -7.377  1.00 17.34           C  
ANISOU 4426  CG1 VAL A 589     2373   2006   2210     29   -412    575       C  
ATOM   4427  CG2 VAL A 589      31.729 -28.134  -7.340  1.00 25.26           C  
ANISOU 4427  CG2 VAL A 589     3368   2988   3243    -78   -330    585       C  
ATOM   4428  N   ILE A 590      31.241 -29.401 -10.172  1.00 16.24           N  
ANISOU 4428  N   ILE A 590     2193   1760   2215    -89   -353    519       N  
ATOM   4429  CA  ILE A 590      31.059 -28.684 -11.425  1.00 19.03           C  
ANISOU 4429  CA  ILE A 590     2500   2144   2589    -93   -361    468       C  
ATOM   4430  C   ILE A 590      30.441 -27.292 -11.192  1.00 16.99           C  
ANISOU 4430  C   ILE A 590     2204   1941   2311   -115   -338    460       C  
ATOM   4431  O   ILE A 590      29.526 -27.128 -10.380  1.00 19.72           O  
ANISOU 4431  O   ILE A 590     2548   2290   2653   -150   -308    481       O  
ATOM   4432  CB  ILE A 590      30.222 -29.527 -12.443  1.00 20.12           C  
ANISOU 4432  CB  ILE A 590     2636   2234   2777   -119   -364    441       C  
ATOM   4433  CG1 ILE A 590      30.245 -28.899 -13.842  1.00 14.58           C  
ANISOU 4433  CG1 ILE A 590     1897   1562   2079   -105   -384    389       C  
ATOM   4434  CG2 ILE A 590      28.795 -29.755 -11.932  1.00 15.67           C  
ANISOU 4434  CG2 ILE A 590     2065   1650   2239   -180   -330    454       C  
ATOM   4435  CD1 ILE A 590      29.656 -29.817 -14.928  1.00 15.49           C  
ANISOU 4435  CD1 ILE A 590     2014   1636   2236   -120   -400    351       C  
ATOM   4436  N   PHE A 591      30.968 -26.293 -11.893  1.00 18.75           N  
ANISOU 4436  N   PHE A 591     2400   2204   2520    -94   -347    429       N  
ATOM   4437  CA  PHE A 591      30.419 -24.941 -11.870  1.00 13.57           C  
ANISOU 4437  CA  PHE A 591     1717   1589   1850   -107   -327    417       C  
ATOM   4438  C   PHE A 591      29.693 -24.660 -13.184  1.00 20.98           C  
ANISOU 4438  C   PHE A 591     2633   2527   2810   -108   -334    385       C  
ATOM   4439  O   PHE A 591      30.272 -24.831 -14.268  1.00 16.65           O  
ANISOU 4439  O   PHE A 591     2089   1974   2264    -84   -354    361       O  
ATOM   4440  CB  PHE A 591      31.529 -23.910 -11.629  1.00 13.96           C  
ANISOU 4440  CB  PHE A 591     1762   1677   1866    -87   -325    408       C  
ATOM   4441  CG  PHE A 591      32.206 -24.058 -10.276  1.00 20.57           C  
ANISOU 4441  CG  PHE A 591     2615   2528   2672    -82   -327    433       C  
ATOM   4442  CD1 PHE A 591      31.679 -23.441  -9.154  1.00 16.19           C  
ANISOU 4442  CD1 PHE A 591     2065   1995   2091   -102   -303    448       C  
ATOM   4443  CD2 PHE A 591      33.344 -24.843 -10.127  1.00 21.13           C  
ANISOU 4443  CD2 PHE A 591     2698   2593   2737    -49   -357    437       C  
ATOM   4444  CE1 PHE A 591      32.286 -23.584  -7.899  1.00 17.05           C  
ANISOU 4444  CE1 PHE A 591     2197   2123   2161    -93   -310    469       C  
ATOM   4445  CE2 PHE A 591      33.952 -24.999  -8.875  1.00 15.65           C  
ANISOU 4445  CE2 PHE A 591     2022   1918   2007    -34   -369    460       C  
ATOM   4446  CZ  PHE A 591      33.417 -24.376  -7.762  1.00 15.71           C  
ANISOU 4446  CZ  PHE A 591     2040   1949   1981    -57   -347    476       C  
ATOM   4447  N   LEU A 592      28.422 -24.261 -13.084  1.00 20.68           N  
ANISOU 4447  N   LEU A 592     2571   2499   2786   -130   -319    381       N  
ATOM   4448  CA  LEU A 592      27.632 -23.887 -14.254  1.00 22.91           C  
ANISOU 4448  CA  LEU A 592     2829   2792   3082   -121   -335    349       C  
ATOM   4449  C   LEU A 592      27.302 -22.408 -14.236  1.00 20.81           C  
ANISOU 4449  C   LEU A 592     2551   2561   2795   -105   -319    345       C  
ATOM   4450  O   LEU A 592      27.168 -21.801 -13.168  1.00 19.01           O  
ANISOU 4450  O   LEU A 592     2320   2347   2556   -116   -289    362       O  
ATOM   4451  CB  LEU A 592      26.308 -24.663 -14.345  1.00 13.97           C  
ANISOU 4451  CB  LEU A 592     1667   1648   1995   -154   -340    335       C  
ATOM   4452  CG  LEU A 592      26.291 -26.186 -14.345  1.00 23.71           C  
ANISOU 4452  CG  LEU A 592     2915   2833   3262   -183   -348    336       C  
ATOM   4453  CD1 LEU A 592      24.980 -26.679 -14.901  1.00 23.01           C  
ANISOU 4453  CD1 LEU A 592     2784   2740   3219   -215   -360    299       C  
ATOM   4454  CD2 LEU A 592      27.434 -26.744 -15.134  1.00 23.86           C  
ANISOU 4454  CD2 LEU A 592     2968   2828   3270   -152   -376    325       C  
ATOM   4455  N   GLY A 593      27.167 -21.845 -15.432  1.00 18.19           N  
ANISOU 4455  N   GLY A 593     2218   2238   2453    -74   -338    323       N  
ATOM   4456  CA  GLY A 593      26.667 -20.493 -15.617  1.00 15.14           C  
ANISOU 4456  CA  GLY A 593     1828   1874   2050    -48   -327    319       C  
ATOM   4457  C   GLY A 593      25.565 -20.534 -16.664  1.00 18.51           C  
ANISOU 4457  C   GLY A 593     2231   2314   2489    -24   -362    293       C  
ATOM   4458  O   GLY A 593      25.639 -21.309 -17.619  1.00 15.92           O  
ANISOU 4458  O   GLY A 593     1908   1979   2164    -18   -396    273       O  
ATOM   4459  N   ALA A 594      24.523 -19.735 -16.481  1.00 14.92           N  
ANISOU 4459  N   ALA A 594     1747   1881   2041     -7   -358    287       N  
ATOM   4460  CA  ALA A 594      23.404 -19.781 -17.414  1.00 20.78           C  
ANISOU 4460  CA  ALA A 594     2454   2645   2796     22   -401    255       C  
ATOM   4461  C   ALA A 594      22.889 -18.387 -17.702  1.00 26.78           C  
ANISOU 4461  C   ALA A 594     3220   3423   3533     80   -401    257       C  
ATOM   4462  O   ALA A 594      22.919 -17.510 -16.846  1.00 29.42           O  
ANISOU 4462  O   ALA A 594     3561   3753   3862     82   -360    274       O  
ATOM   4463  CB  ALA A 594      22.281 -20.672 -16.887  1.00 18.10           C  
ANISOU 4463  CB  ALA A 594     2045   2319   2511    -21   -406    233       C  
ATOM   4464  N   ASP A 595      22.419 -18.190 -18.920  1.00 26.50           N  
ANISOU 4464  N   ASP A 595     3187   3403   3477    132   -450    237       N  
ATOM   4465  CA  ASP A 595      21.935 -16.896 -19.330  1.00 26.84           C  
ANISOU 4465  CA  ASP A 595     3250   3456   3492    202   -457    242       C  
ATOM   4466  C   ASP A 595      20.939 -17.096 -20.455  1.00 23.30           C  
ANISOU 4466  C   ASP A 595     2769   3044   3038    254   -529    206       C  
ATOM   4467  O   ASP A 595      20.948 -18.129 -21.125  1.00 20.99           O  
ANISOU 4467  O   ASP A 595     2463   2761   2750    235   -569    179       O  
ATOM   4468  CB  ASP A 595      23.106 -16.028 -19.795  1.00 34.41           C  
ANISOU 4468  CB  ASP A 595     4302   4379   4395    228   -428    275       C  
ATOM   4469  CG  ASP A 595      22.728 -14.561 -19.930  1.00 43.26           C  
ANISOU 4469  CG  ASP A 595     5459   5488   5488    293   -415    292       C  
ATOM   4470  OD1 ASP A 595      23.431 -13.839 -20.666  1.00 48.55           O  
ANISOU 4470  OD1 ASP A 595     6210   6128   6108    326   -400    316       O  
ATOM   4471  OD2 ASP A 595      21.730 -14.130 -19.307  1.00 39.86           O1-
ANISOU 4471  OD2 ASP A 595     4980   5078   5088    313   -415    282       O1-
ATOM   4472  N   VAL A 596      20.051 -16.127 -20.640  1.00 23.20           N  
ANISOU 4472  N   VAL A 596     2742   3054   3018    323   -549    201       N  
ATOM   4473  CA  VAL A 596      19.182 -16.124 -21.793  1.00 24.62           C  
ANISOU 4473  CA  VAL A 596     2900   3274   3179    392   -627    168       C  
ATOM   4474  C   VAL A 596      19.129 -14.723 -22.372  1.00 31.59           C  
ANISOU 4474  C   VAL A 596     3854   4144   4003    490   -633    198       C  
ATOM   4475  O   VAL A 596      19.114 -13.744 -21.633  1.00 31.72           O  
ANISOU 4475  O   VAL A 596     3888   4137   4027    507   -585    224       O  
ATOM   4476  CB  VAL A 596      17.771 -16.751 -21.528  1.00 38.78           C  
ANISOU 4476  CB  VAL A 596     4569   5125   5039    379   -668    110       C  
ATOM   4477  CG1 VAL A 596      17.534 -16.999 -20.061  1.00 28.04           C  
ANISOU 4477  CG1 VAL A 596     3149   3761   3744    305   -603    112       C  
ATOM   4478  CG2 VAL A 596      16.650 -15.928 -22.158  1.00 40.96           C  
ANISOU 4478  CG2 VAL A 596     4812   5449   5302    481   -730     86       C  
ATOM   4479  N   THR A 597      19.172 -14.629 -23.697  1.00 23.25           N  
ANISOU 4479  N   THR A 597     2852   3098   2885    555   -689    197       N  
ATOM   4480  CA  THR A 597      19.084 -13.331 -24.344  1.00 25.18           C  
ANISOU 4480  CA  THR A 597     3178   3323   3065    657   -698    231       C  
ATOM   4481  C   THR A 597      17.865 -13.335 -25.212  1.00 30.08           C  
ANISOU 4481  C   THR A 597     3754   4006   3669    747   -796    192       C  
ATOM   4482  O   THR A 597      17.554 -14.317 -25.890  1.00 36.32           O  
ANISOU 4482  O   THR A 597     4501   4843   4457    736   -861    145       O  
ATOM   4483  CB  THR A 597      20.311 -13.005 -25.197  1.00 24.72           C  
ANISOU 4483  CB  THR A 597     3250   3216   2927    667   -667    276       C  
ATOM   4484  CG2 THR A 597      21.560 -13.129 -24.379  1.00 24.08           C  
ANISOU 4484  CG2 THR A 597     3196   3086   2869    574   -579    302       C  
ATOM   4485  OG1 THR A 597      20.393 -13.928 -26.285  1.00 34.37           O  
ANISOU 4485  OG1 THR A 597     4479   4470   4111    672   -726    247       O  
ATOM   4486  N   HIS A 598      17.161 -12.224 -25.174  1.00 32.52           N  
ANISOU 4486  N   HIS A 598     4072   4318   3968    840   -809    206       N  
ATOM   4487  CA  HIS A 598      15.918 -12.109 -25.884  1.00 32.67           C  
ANISOU 4487  CA  HIS A 598     4034   4403   3975    940   -908    165       C  
ATOM   4488  C   HIS A 598      16.162 -11.307 -27.144  1.00 32.69           C  
ANISOU 4488  C   HIS A 598     4167   4384   3868   1053   -946    207       C  
ATOM   4489  O   HIS A 598      17.148 -10.576 -27.232  1.00 34.29           O  
ANISOU 4489  O   HIS A 598     4497   4511   4020   1055   -877    272       O  
ATOM   4490  CB  HIS A 598      14.877 -11.464 -24.978  1.00 30.33           C  
ANISOU 4490  CB  HIS A 598     3650   4131   3744    979   -902    146       C  
ATOM   4491  CG  HIS A 598      14.505 -12.333 -23.822  1.00 33.02           C  
ANISOU 4491  CG  HIS A 598     3860   4501   4184    871   -866    101       C  
ATOM   4492  CD2 HIS A 598      14.850 -12.271 -22.513  1.00 29.06           C  
ANISOU 4492  CD2 HIS A 598     3342   3965   3736    790   -774    118       C  
ATOM   4493  ND1 HIS A 598      13.729 -13.461 -23.968  1.00 34.64           N  
ANISOU 4493  ND1 HIS A 598     3944   4778   4441    829   -925     30       N  
ATOM   4494  CE1 HIS A 598      13.592 -14.049 -22.790  1.00 34.86           C  
ANISOU 4494  CE1 HIS A 598     3888   4808   4550    727   -863     11       C  
ATOM   4495  NE2 HIS A 598      14.258 -13.348 -21.893  1.00 30.08           N  
ANISOU 4495  NE2 HIS A 598     3345   4142   3942    706   -775     64       N  
ATOM   4496  N   PRO A 599      15.302 -11.493 -28.147  1.00 31.20           N  
ANISOU 4496  N   PRO A 599     3950   4263   3640   1143  -1056    168       N  
ATOM   4497  CA  PRO A 599      15.437 -10.680 -29.356  1.00 36.62           C  
ANISOU 4497  CA  PRO A 599     4771   4932   4209   1266  -1097    213       C  
ATOM   4498  C   PRO A 599      15.066  -9.225 -29.092  1.00 40.85           C  
ANISOU 4498  C   PRO A 599     5366   5425   4731   1373  -1076    263       C  
ATOM   4499  O   PRO A 599      14.089  -8.975 -28.389  1.00 38.98           O  
ANISOU 4499  O   PRO A 599     5022   5224   4566   1405  -1097    229       O  
ATOM   4500  CB  PRO A 599      14.424 -11.313 -30.321  1.00 36.06           C  
ANISOU 4500  CB  PRO A 599     4627   4961   4115   1328  -1227    142       C  
ATOM   4501  CG  PRO A 599      13.446 -12.018 -29.459  1.00 37.73           C  
ANISOU 4501  CG  PRO A 599     4651   5241   4443   1278  -1261     63       C  
ATOM   4502  CD  PRO A 599      14.233 -12.500 -28.267  1.00 32.32           C  
ANISOU 4502  CD  PRO A 599     3943   4502   3837   1129  -1146     78       C  
ATOM   4503  N   PRO A 600      15.854  -8.285 -29.641  1.00 52.09           N  
ANISOU 4503  N   PRO A 600     6960   6766   6068   1420  -1024    341       N  
ATOM   4504  CA  PRO A 600      15.606  -6.842 -29.749  1.00 50.34           C  
ANISOU 4504  CA  PRO A 600     6830   6482   5815   1508   -987    392       C  
ATOM   4505  C   PRO A 600      14.132  -6.480 -29.891  1.00 46.82           C  
ANISOU 4505  C   PRO A 600     6292   6100   5395   1602  -1064    345       C  
ATOM   4506  O   PRO A 600      13.368  -7.249 -30.473  1.00 44.29           O  
ANISOU 4506  O   PRO A 600     5879   5872   5077   1613  -1154    281       O  
ATOM   4507  CB  PRO A 600      16.320  -6.483 -31.053  1.00 51.79           C  
ANISOU 4507  CB  PRO A 600     7174   6621   5884   1530   -964    441       C  
ATOM   4508  CG  PRO A 600      17.491  -7.431 -31.111  1.00 57.30           C  
ANISOU 4508  CG  PRO A 600     7898   7310   6565   1430   -929    448       C  
ATOM   4509  CD  PRO A 600      17.144  -8.649 -30.256  1.00 60.61           C  
ANISOU 4509  CD  PRO A 600     8151   7800   7077   1358   -974    379       C  
ATOM   4510  N   ALA A 601      13.748  -5.316 -29.371  1.00 53.22           N  
ANISOU 4510  N   ALA A 601     7131   6862   6228   1667  -1028    372       N  
ATOM   4511  CA  ALA A 601      12.386  -4.802 -29.520  1.00 60.39           C  
ANISOU 4511  CA  ALA A 601     7967   7822   7157   1770  -1094    334       C  
ATOM   4512  C   ALA A 601      11.973  -4.740 -30.989  1.00 69.29           C  
ANISOU 4512  C   ALA A 601     9149   8986   8192   1845  -1168    329       C  
ATOM   4513  O   ALA A 601      12.786  -4.424 -31.860  1.00 67.42           O  
ANISOU 4513  O   ALA A 601     9063   8692   7861   1851  -1136    385       O  
ATOM   4514  CB  ALA A 601      12.270  -3.428 -28.881  1.00 58.73           C  
ANISOU 4514  CB  ALA A 601     7822   7529   6965   1835  -1030    378       C  
ATOM   4515  N   GLY A 602      10.704  -5.036 -31.257  1.00 78.09           N  
ANISOU 4515  N   GLY A 602    10138  10198   9334   1900  -1264    259       N  
ATOM   4516  CA  GLY A 602      10.219  -5.128 -32.622  1.00 84.60           C  
ANISOU 4516  CA  GLY A 602    10996  11075  10076   1971  -1348    240       C  
ATOM   4517  C   GLY A 602      10.202  -6.583 -33.032  1.00 92.87           C  
ANISOU 4517  C   GLY A 602    11950  12207  11130   1893  -1409    172       C  
ATOM   4518  O   GLY A 602       9.142  -7.151 -33.294  1.00 96.39           O  
ANISOU 4518  O   GLY A 602    12266  12751  11608   1913  -1499     92       O  
ATOM   4519  N   ASP A 603      11.390  -7.184 -33.075  1.00 95.80           N  
ANISOU 4519  N   ASP A 603    12387  12538  11475   1801  -1358    201       N  
ATOM   4520  CA  ASP A 603      11.541  -8.617 -33.303  1.00 95.40           C  
ANISOU 4520  CA  ASP A 603    12254  12552  11440   1713  -1401    139       C  
ATOM   4521  C   ASP A 603      10.734  -9.435 -32.306  1.00 93.69           C  
ANISOU 4521  C   ASP A 603    11840  12409  11350   1650  -1433     57       C  
ATOM   4522  O   ASP A 603      10.929  -9.333 -31.097  1.00 96.72           O  
ANISOU 4522  O   ASP A 603    12175  12763  11812   1603  -1373     71       O  
ATOM   4523  CB  ASP A 603      13.011  -9.026 -33.188  1.00 95.72           C  
ANISOU 4523  CB  ASP A 603    12392  12527  11453   1622  -1323    188       C  
ATOM   4524  CG  ASP A 603      13.798  -8.735 -34.441  1.00 97.11           C  
ANISOU 4524  CG  ASP A 603    12736  12661  11502   1655  -1305    239       C  
ATOM   4525  OD1 ASP A 603      14.785  -7.976 -34.353  1.00 93.83           O  
ANISOU 4525  OD1 ASP A 603    12455  12150  11044   1649  -1212    320       O  
ATOM   4526  OD2 ASP A 603      13.435  -9.277 -35.506  1.00101.71           O1-
ANISOU 4526  OD2 ASP A 603    13315  13305  12027   1683  -1380    195       O1-
ATOM   4527  N   GLY A 604       9.822 -10.242 -32.825  1.00 90.47           N  
ANISOU 4527  N   GLY A 604    11318  12097  10961   1648  -1524    -30       N  
ATOM   4528  CA  GLY A 604       9.119 -11.217 -32.020  1.00 86.30           C  
ANISOU 4528  CA  GLY A 604    10601  11639  10551   1566  -1548   -116       C  
ATOM   4529  C   GLY A 604       9.246 -12.532 -32.751  1.00 84.59           C  
ANISOU 4529  C   GLY A 604    10351  11470  10318   1495  -1603   -180       C  
ATOM   4530  O   GLY A 604       9.024 -13.601 -32.190  1.00 85.61           O  
ANISOU 4530  O   GLY A 604    10352  11639  10535   1394  -1609   -246       O  
ATOM   4531  N   LYS A 605       9.604 -12.435 -34.029  1.00 81.47           N  
ANISOU 4531  N   LYS A 605    10077  11069   9808   1548  -1637   -160       N  
ATOM   4532  CA  LYS A 605       9.850 -13.601 -34.860  1.00 77.44           C  
ANISOU 4532  CA  LYS A 605     9564  10595   9264   1492  -1685   -216       C  
ATOM   4533  C   LYS A 605      11.070 -14.361 -34.347  1.00 65.25           C  
ANISOU 4533  C   LYS A 605     8054   8998   7739   1381  -1619   -193       C  
ATOM   4534  O   LYS A 605      11.029 -15.580 -34.149  1.00 66.58           O  
ANISOU 4534  O   LYS A 605     8130   9198   7968   1285  -1640   -263       O  
ATOM   4535  CB  LYS A 605      10.077 -13.169 -36.314  1.00 84.63           C  
ANISOU 4535  CB  LYS A 605    10618  11501  10035   1585  -1723   -188       C  
ATOM   4536  CG  LYS A 605      10.898 -11.885 -36.466  1.00 90.81           C  
ANISOU 4536  CG  LYS A 605    11577  12193  10732   1656  -1649    -73       C  
ATOM   4537  CD  LYS A 605      11.760 -11.886 -37.733  1.00 95.16           C  
ANISOU 4537  CD  LYS A 605    12291  12716  11148   1685  -1643    -35       C  
ATOM   4538  CE  LYS A 605      11.072 -11.205 -38.911  1.00 97.37           C  
ANISOU 4538  CE  LYS A 605    12636  13028  11333   1812  -1710    -35       C  
ATOM   4539  NZ  LYS A 605       9.997 -12.036 -39.523  1.00 98.94           N1+
ANISOU 4539  NZ  LYS A 605    12715  13333  11543   1826  -1827   -143       N1+
ATOM   4540  N   LYS A 606      12.150 -13.621 -34.123  1.00 49.30           N  
ANISOU 4540  N   LYS A 606     6170   6893   5670   1395  -1538    -96       N  
ATOM   4541  CA  LYS A 606      13.427 -14.208 -33.770  1.00 43.00           C  
ANISOU 4541  CA  LYS A 606     5428   6039   4870   1307  -1475    -65       C  
ATOM   4542  C   LYS A 606      13.364 -14.892 -32.409  1.00 36.78           C  
ANISOU 4542  C   LYS A 606     4510   5257   4210   1208  -1450    -98       C  
ATOM   4543  O   LYS A 606      12.620 -14.475 -31.529  1.00 39.27           O  
ANISOU 4543  O   LYS A 606     4731   5588   4603   1218  -1443   -107       O  
ATOM   4544  CB  LYS A 606      14.534 -13.147 -33.821  1.00 47.18           C  
ANISOU 4544  CB  LYS A 606     6128   6476   5322   1344  -1387     45       C  
ATOM   4545  CG  LYS A 606      14.787 -12.582 -35.221  1.00 57.28           C  
ANISOU 4545  CG  LYS A 606     7554   7742   6470   1426  -1396     81       C  
ATOM   4546  CD  LYS A 606      15.996 -13.238 -35.913  1.00 64.26           C  
ANISOU 4546  CD  LYS A 606     8539   8598   7277   1378  -1364     95       C  
ATOM   4547  CE  LYS A 606      15.796 -14.741 -36.203  1.00 63.01           C  
ANISOU 4547  CE  LYS A 606     8286   8508   7148   1311  -1434     -2       C  
ATOM   4548  NZ  LYS A 606      17.060 -15.471 -36.544  1.00 54.99           N1+
ANISOU 4548  NZ  LYS A 606     7352   7459   6083   1251  -1392      7       N1+
ATOM   4549  N   PRO A 607      14.131 -15.967 -32.241  1.00 32.04           N  
ANISOU 4549  N   PRO A 607     3903   4642   3629   1113  -1437   -120       N  
ATOM   4550  CA  PRO A 607      14.041 -16.703 -30.980  1.00 31.55           C  
ANISOU 4550  CA  PRO A 607     3722   4569   3697    988  -1382   -150       C  
ATOM   4551  C   PRO A 607      14.791 -16.042 -29.827  1.00 31.98           C  
ANISOU 4551  C   PRO A 607     3821   4541   3789    942  -1257    -68       C  
ATOM   4552  O   PRO A 607      15.675 -15.208 -30.018  1.00 31.69           O  
ANISOU 4552  O   PRO A 607     3917   4444   3681    979  -1201     10       O  
ATOM   4553  CB  PRO A 607      14.692 -18.042 -31.322  1.00 33.11           C  
ANISOU 4553  CB  PRO A 607     3926   4753   3900    888  -1377   -191       C  
ATOM   4554  CG  PRO A 607      15.686 -17.706 -32.379  1.00 31.99           C  
ANISOU 4554  CG  PRO A 607     3945   4579   3631    944  -1371   -141       C  
ATOM   4555  CD  PRO A 607      15.081 -16.585 -33.182  1.00 29.37           C  
ANISOU 4555  CD  PRO A 607     3668   4284   3206   1093  -1440   -118       C  
ATOM   4556  N   SER A 608      14.414 -16.418 -28.616  1.00 32.81           N  
ANISOU 4556  N   SER A 608     3815   4647   4005    856  -1210    -90       N  
ATOM   4557  CA  SER A 608      15.280 -16.178 -27.481  1.00 29.94           C  
ANISOU 4557  CA  SER A 608     3489   4209   3679    780  -1092    -28       C  
ATOM   4558  C   SER A 608      16.332 -17.282 -27.483  1.00 25.56           C  
ANISOU 4558  C   SER A 608     2969   3613   3130    675  -1049    -28       C  
ATOM   4559  O   SER A 608      16.097 -18.364 -28.018  1.00 21.19           O  
ANISOU 4559  O   SER A 608     2371   3091   2589    638  -1103    -90       O  
ATOM   4560  CB  SER A 608      14.486 -16.153 -26.175  1.00 30.23           C  
ANISOU 4560  CB  SER A 608     3404   4262   3820    734  -1054    -49       C  
ATOM   4561  OG  SER A 608      13.585 -15.063 -26.169  1.00 30.84           O  
ANISOU 4561  OG  SER A 608     3453   4372   3892    841  -1087    -49       O  
ATOM   4562  N   ILE A 609      17.490 -16.990 -26.896  1.00 27.11           N  
ANISOU 4562  N   ILE A 609     3244   3739   3317    630   -955     37       N  
ATOM   4563  CA  ILE A 609      18.630 -17.901 -26.887  1.00 27.74           C  
ANISOU 4563  CA  ILE A 609     3366   3776   3396    547   -911     45       C  
ATOM   4564  C   ILE A 609      18.987 -18.262 -25.446  1.00 29.21           C  
ANISOU 4564  C   ILE A 609     3509   3926   3663    449   -831     63       C  
ATOM   4565  O   ILE A 609      19.106 -17.378 -24.591  1.00 22.54           O  
ANISOU 4565  O   ILE A 609     2675   3058   2830    454   -774    106       O  
ATOM   4566  CB  ILE A 609      19.846 -17.250 -27.586  1.00 27.38           C  
ANISOU 4566  CB  ILE A 609     3459   3685   3258    584   -872    103       C  
ATOM   4567  CG1 ILE A 609      19.477 -16.865 -29.026  1.00 25.02           C  
ANISOU 4567  CG1 ILE A 609     3220   3421   2864    688   -949     92       C  
ATOM   4568  CG2 ILE A 609      21.056 -18.168 -27.578  1.00 18.23           C  
ANISOU 4568  CG2 ILE A 609     2336   2489   2103    506   -825    105       C  
ATOM   4569  CD1 ILE A 609      20.594 -16.184 -29.778  1.00 24.06           C  
ANISOU 4569  CD1 ILE A 609     3242   3255   2646    726   -902    151       C  
ATOM   4570  N   THR A 610      19.106 -19.560 -25.162  1.00 28.81           N  
ANISOU 4570  N   THR A 610     3412   3870   3666    365   -827     28       N  
ATOM   4571  CA  THR A 610      19.543 -20.001 -23.837  1.00 30.08           C  
ANISOU 4571  CA  THR A 610     3548   3993   3889    277   -753     52       C  
ATOM   4572  C   THR A 610      20.928 -20.629 -23.916  1.00 28.71           C  
ANISOU 4572  C   THR A 610     3445   3769   3695    234   -714     75       C  
ATOM   4573  O   THR A 610      21.249 -21.346 -24.872  1.00 25.02           O  
ANISOU 4573  O   THR A 610     3005   3301   3200    238   -750     46       O  
ATOM   4574  CB  THR A 610      18.533 -20.962 -23.142  1.00 23.74           C  
ANISOU 4574  CB  THR A 610     2634   3211   3175    208   -761      2       C  
ATOM   4575  CG2 THR A 610      17.160 -20.316 -23.017  1.00 18.49           C  
ANISOU 4575  CG2 THR A 610     1883   2604   2538    251   -795    -28       C  
ATOM   4576  OG1 THR A 610      18.417 -22.189 -23.877  1.00 22.79           O  
ANISOU 4576  OG1 THR A 610     2496   3095   3070    173   -810    -53       O  
ATOM   4577  N   ALA A 611      21.755 -20.334 -22.919  1.00 23.02           N  
ANISOU 4577  N   ALA A 611     2751   3010   2984    200   -643    124       N  
ATOM   4578  CA  ALA A 611      23.126 -20.827 -22.891  1.00 23.40           C  
ANISOU 4578  CA  ALA A 611     2857   3018   3017    167   -605    146       C  
ATOM   4579  C   ALA A 611      23.504 -21.336 -21.505  1.00 24.41           C  
ANISOU 4579  C   ALA A 611     2960   3118   3197     99   -554    168       C  
ATOM   4580  O   ALA A 611      23.259 -20.669 -20.504  1.00 21.78           O  
ANISOU 4580  O   ALA A 611     2607   2787   2880     90   -518    192       O  
ATOM   4581  CB  ALA A 611      24.095 -19.725 -23.322  1.00 18.82           C  
ANISOU 4581  CB  ALA A 611     2358   2421   2370    211   -572    186       C  
ATOM   4582  N   VAL A 612      24.113 -22.515 -21.457  1.00 20.49           N  
ANISOU 4582  N   VAL A 612     2471   2594   2721     57   -551    158       N  
ATOM   4583  CA  VAL A 612      24.618 -23.064 -20.214  1.00 14.63           C  
ANISOU 4583  CA  VAL A 612     1723   1821   2016      3   -506    185       C  
ATOM   4584  C   VAL A 612      26.044 -23.548 -20.438  1.00 21.59           C  
ANISOU 4584  C   VAL A 612     2656   2673   2876      3   -491    196       C  
ATOM   4585  O   VAL A 612      26.315 -24.332 -21.349  1.00 19.00           O  
ANISOU 4585  O   VAL A 612     2346   2333   2542     11   -519    166       O  
ATOM   4586  CB  VAL A 612      23.729 -24.220 -19.706  1.00 15.03           C  
ANISOU 4586  CB  VAL A 612     1720   1860   2128    -52   -515    161       C  
ATOM   4587  CG1 VAL A 612      24.205 -24.709 -18.349  1.00 14.77           C  
ANISOU 4587  CG1 VAL A 612     1696   1794   2122    -99   -466    199       C  
ATOM   4588  CG2 VAL A 612      22.282 -23.777 -19.614  1.00 17.12           C  
ANISOU 4588  CG2 VAL A 612     1918   2165   2420    -52   -532    136       C  
ATOM   4589  N   VAL A 613      26.966 -23.045 -19.631  1.00 18.34           N  
ANISOU 4589  N   VAL A 613     2265   2252   2452     -2   -449    233       N  
ATOM   4590  CA  VAL A 613      28.346 -23.519 -19.659  1.00 16.69           C  
ANISOU 4590  CA  VAL A 613     2088   2021   2232     -2   -433    240       C  
ATOM   4591  C   VAL A 613      28.671 -24.282 -18.376  1.00 18.77           C  
ANISOU 4591  C   VAL A 613     2342   2261   2528    -37   -416    263       C  
ATOM   4592  O   VAL A 613      27.986 -24.141 -17.358  1.00 18.67           O  
ANISOU 4592  O   VAL A 613     2307   2253   2535    -63   -401    282       O  
ATOM   4593  CB  VAL A 613      29.353 -22.356 -19.835  1.00 14.65           C  
ANISOU 4593  CB  VAL A 613     1861   1774   1930     22   -400    257       C  
ATOM   4594  CG1 VAL A 613      28.971 -21.493 -21.047  1.00 13.62           C  
ANISOU 4594  CG1 VAL A 613     1757   1660   1757     62   -410    247       C  
ATOM   4595  CG2 VAL A 613      29.392 -21.512 -18.584  1.00 14.04           C  
ANISOU 4595  CG2 VAL A 613     1772   1704   1857      4   -366    286       C  
ATOM   4596  N   GLY A 614      29.721 -25.087 -18.429  1.00 22.44           N  
ANISOU 4596  N   GLY A 614     2828   2704   2996    -32   -416    262       N  
ATOM   4597  CA  GLY A 614      30.088 -25.921 -17.306  1.00 16.20           C  
ANISOU 4597  CA  GLY A 614     2040   1886   2229    -51   -408    286       C  
ATOM   4598  C   GLY A 614      31.571 -26.205 -17.303  1.00 19.42           C  
ANISOU 4598  C   GLY A 614     2466   2289   2625    -24   -404    288       C  
ATOM   4599  O   GLY A 614      32.183 -26.399 -18.362  1.00 21.91           O  
ANISOU 4599  O   GLY A 614     2792   2603   2930      2   -412    259       O  
ATOM   4600  N   SER A 615      32.150 -26.207 -16.103  1.00 19.68           N  
ANISOU 4600  N   SER A 615     2499   2324   2654    -27   -393    317       N  
ATOM   4601  CA  SER A 615      33.575 -26.423 -15.919  1.00 18.00           C  
ANISOU 4601  CA  SER A 615     2290   2118   2433      4   -395    316       C  
ATOM   4602  C   SER A 615      33.904 -27.875 -16.225  1.00 18.50           C  
ANISOU 4602  C   SER A 615     2373   2134   2521     25   -417    307       C  
ATOM   4603  O   SER A 615      33.068 -28.771 -16.065  1.00 16.91           O  
ANISOU 4603  O   SER A 615     2191   1888   2346      5   -426    317       O  
ATOM   4604  CB  SER A 615      34.009 -26.051 -14.488  1.00 15.86           C  
ANISOU 4604  CB  SER A 615     2013   1868   2146     -1   -388    346       C  
ATOM   4605  OG  SER A 615      33.271 -26.799 -13.536  1.00 13.81           O  
ANISOU 4605  OG  SER A 615     1774   1578   1897    -18   -392    380       O  
ATOM   4606  N   MET A 616      35.130 -28.102 -16.668  1.00 19.69           N  
ANISOU 4606  N   MET A 616     2519   2293   2668     64   -422    285       N  
ATOM   4607  CA  MET A 616      35.514 -29.412 -17.175  1.00 20.87           C  
ANISOU 4607  CA  MET A 616     2690   2396   2842     95   -440    267       C  
ATOM   4608  C   MET A 616      36.806 -29.940 -16.534  1.00 18.88           C  
ANISOU 4608  C   MET A 616     2434   2145   2593    144   -453    274       C  
ATOM   4609  O   MET A 616      37.388 -30.924 -16.991  1.00 28.29           O  
ANISOU 4609  O   MET A 616     3640   3303   3804    185   -466    253       O  
ATOM   4610  CB  MET A 616      35.645 -29.336 -18.696  1.00 16.55           C  
ANISOU 4610  CB  MET A 616     2143   1856   2288    107   -435    218       C  
ATOM   4611  CG  MET A 616      34.339 -28.975 -19.410  1.00 16.58           C  
ANISOU 4611  CG  MET A 616     2154   1859   2286     73   -437    207       C  
ATOM   4612  SD  MET A 616      33.225 -30.399 -19.305  1.00 22.26           S  
ANISOU 4612  SD  MET A 616     2899   2508   3051     46   -462    203       S  
ATOM   4613  CE  MET A 616      34.373 -31.565 -19.950  1.00115.31           C  
ANISOU 4613  CE  MET A 616    14709  14254  14850     97   -471    169       C  
ATOM   4614  N   ASP A 617      37.258 -29.266 -15.486  1.00 17.97           N  
ANISOU 4614  N   ASP A 617     2298   2071   2458    144   -452    298       N  
ATOM   4615  CA  ASP A 617      38.433 -29.706 -14.742  1.00 17.42           C  
ANISOU 4615  CA  ASP A 617     2218   2014   2387    196   -476    303       C  
ATOM   4616  C   ASP A 617      38.278 -29.216 -13.304  1.00 22.93           C  
ANISOU 4616  C   ASP A 617     2918   2738   3057    181   -483    344       C  
ATOM   4617  O   ASP A 617      37.304 -28.536 -12.986  1.00 22.17           O  
ANISOU 4617  O   ASP A 617     2828   2647   2947    131   -463    363       O  
ATOM   4618  CB  ASP A 617      39.724 -29.174 -15.393  1.00 15.61           C  
ANISOU 4618  CB  ASP A 617     1934   1839   2156    224   -467    254       C  
ATOM   4619  CG  ASP A 617      39.762 -27.627 -15.480  1.00 23.79           C  
ANISOU 4619  CG  ASP A 617     2934   2935   3170    179   -434    239       C  
ATOM   4620  OD1 ASP A 617      39.369 -26.938 -14.510  1.00 27.55           O  
ANISOU 4620  OD1 ASP A 617     3409   3430   3627    149   -434    266       O  
ATOM   4621  OD2 ASP A 617      40.207 -27.092 -16.516  1.00 23.97           O1-
ANISOU 4621  OD2 ASP A 617     2934   2980   3193    173   -403    201       O1-
ATOM   4622  N   ALA A 618      39.248 -29.526 -12.452  1.00 16.90           N  
ANISOU 4622  N   ALA A 618     2146   1995   2280    230   -514    353       N  
ATOM   4623  CA  ALA A 618      39.113 -29.252 -11.020  1.00 19.84           C  
ANISOU 4623  CA  ALA A 618     2534   2389   2616    226   -529    394       C  
ATOM   4624  C   ALA A 618      39.762 -27.937 -10.597  1.00 18.24           C  
ANISOU 4624  C   ALA A 618     2274   2269   2387    211   -527    364       C  
ATOM   4625  O   ALA A 618      39.858 -27.664  -9.422  1.00 23.01           O  
ANISOU 4625  O   ALA A 618     2885   2903   2955    215   -545    385       O  
ATOM   4626  CB  ALA A 618      39.702 -30.412 -10.196  1.00 16.51           C  
ANISOU 4626  CB  ALA A 618     2150   1939   2184    296   -572    427       C  
ATOM   4627  N   HIS A 619      40.204 -27.129 -11.551  1.00 21.37           N  
ANISOU 4627  N   HIS A 619     2621   2699   2801    191   -501    315       N  
ATOM   4628  CA  HIS A 619      41.003 -25.954 -11.210  1.00 18.30           C  
ANISOU 4628  CA  HIS A 619     2175   2382   2397    174   -495    277       C  
ATOM   4629  C   HIS A 619      40.206 -24.806 -10.582  1.00 22.29           C  
ANISOU 4629  C   HIS A 619     2691   2902   2875    116   -469    290       C  
ATOM   4630  O   HIS A 619      40.657 -24.245  -9.582  1.00 21.28           O  
ANISOU 4630  O   HIS A 619     2543   2822   2720    113   -486    280       O  
ATOM   4631  CB  HIS A 619      41.846 -25.452 -12.401  1.00 17.18           C  
ANISOU 4631  CB  HIS A 619     1979   2266   2281    168   -465    219       C  
ATOM   4632  CG  HIS A 619      42.795 -26.468 -12.951  1.00 18.35           C  
ANISOU 4632  CG  HIS A 619     2103   2413   2457    230   -486    194       C  
ATOM   4633  CD2 HIS A 619      42.927 -26.985 -14.200  1.00 18.40           C  
ANISOU 4633  CD2 HIS A 619     2112   2391   2488    247   -465    172       C  
ATOM   4634  ND1 HIS A 619      43.775 -27.066 -12.184  1.00 17.71           N  
ANISOU 4634  ND1 HIS A 619     1991   2363   2375    292   -538    185       N  
ATOM   4635  CE1 HIS A 619      44.459 -27.914 -12.934  1.00 22.42           C  
ANISOU 4635  CE1 HIS A 619     2569   2948   3002    346   -544    158       C  
ATOM   4636  NE2 HIS A 619      43.962 -27.887 -14.158  1.00 21.22           N  
ANISOU 4636  NE2 HIS A 619     2438   2759   2864    317   -498    149       N  
ATOM   4637  N   PRO A 620      39.070 -24.393 -11.189  1.00 23.10           N  
ANISOU 4637  N   PRO A 620     2822   2971   2985     73   -431    304       N  
ATOM   4638  CA  PRO A 620      38.427 -24.662 -12.495  1.00 18.22           C  
ANISOU 4638  CA  PRO A 620     2220   2311   2391     65   -408    302       C  
ATOM   4639  C   PRO A 620      38.798 -23.635 -13.580  1.00 24.64           C  
ANISOU 4639  C   PRO A 620     3008   3144   3210     43   -369    262       C  
ATOM   4640  O   PRO A 620      38.693 -22.428 -13.331  1.00 18.36           O  
ANISOU 4640  O   PRO A 620     2205   2371   2401      7   -342    254       O  
ATOM   4641  CB  PRO A 620      36.928 -24.537 -12.173  1.00 16.92           C  
ANISOU 4641  CB  PRO A 620     2093   2116   2220     31   -395    338       C  
ATOM   4642  CG  PRO A 620      36.876 -23.496 -11.057  1.00 21.54           C  
ANISOU 4642  CG  PRO A 620     2670   2739   2775      6   -384    343       C  
ATOM   4643  CD  PRO A 620      38.209 -23.567 -10.313  1.00 20.19           C  
ANISOU 4643  CD  PRO A 620     2471   2611   2588     34   -414    324       C  
ATOM   4644  N   SER A 621      39.187 -24.096 -14.773  1.00 17.72           N  
ANISOU 4644  N   SER A 621     2128   2254   2350     63   -361    239       N  
ATOM   4645  CA  SER A 621      39.651 -23.173 -15.816  1.00 20.33           C  
ANISOU 4645  CA  SER A 621     2444   2603   2678     43   -315    205       C  
ATOM   4646  C   SER A 621      38.899 -23.340 -17.120  1.00 25.92           C  
ANISOU 4646  C   SER A 621     3190   3277   3381     45   -300    207       C  
ATOM   4647  O   SER A 621      38.380 -22.370 -17.692  1.00 21.42           O  
ANISOU 4647  O   SER A 621     2642   2704   2794     21   -268    210       O  
ATOM   4648  CB  SER A 621      41.146 -23.360 -16.095  1.00 23.99           C  
ANISOU 4648  CB  SER A 621     2856   3101   3156     66   -308    161       C  
ATOM   4649  OG  SER A 621      41.916 -23.092 -14.943  1.00 35.96           O  
ANISOU 4649  OG  SER A 621     4328   4661   4675     65   -329    148       O  
ATOM   4650  N   ARG A 622      38.864 -24.583 -17.586  1.00 20.75           N  
ANISOU 4650  N   ARG A 622     2547   2595   2741     79   -326    203       N  
ATOM   4651  CA  ARG A 622      38.280 -24.909 -18.866  1.00 20.62           C  
ANISOU 4651  CA  ARG A 622     2565   2553   2719     86   -320    192       C  
ATOM   4652  C   ARG A 622      36.783 -25.108 -18.735  1.00 20.83           C  
ANISOU 4652  C   ARG A 622     2622   2549   2746     70   -344    219       C  
ATOM   4653  O   ARG A 622      36.307 -25.715 -17.774  1.00 16.68           O  
ANISOU 4653  O   ARG A 622     2098   2004   2237     64   -369    245       O  
ATOM   4654  CB  ARG A 622      38.943 -26.167 -19.437  1.00 22.91           C  
ANISOU 4654  CB  ARG A 622     2853   2826   3027    129   -336    164       C  
ATOM   4655  CG  ARG A 622      38.033 -26.987 -20.349  1.00 28.92           C  
ANISOU 4655  CG  ARG A 622     3656   3545   3788    137   -355    156       C  
ATOM   4656  CD  ARG A 622      38.826 -27.675 -21.453  1.00 32.37           C  
ANISOU 4656  CD  ARG A 622     4097   3977   4226    174   -344    111       C  
ATOM   4657  NE  ARG A 622      38.474 -29.078 -21.637  1.00 40.02           N  
ANISOU 4657  NE  ARG A 622     5092   4893   5220    198   -379     99       N  
ATOM   4658  CZ  ARG A 622      37.493 -29.517 -22.419  1.00 51.74           C  
ANISOU 4658  CZ  ARG A 622     6613   6348   6699    189   -396     83       C  
ATOM   4659  NH1 ARG A 622      36.739 -28.660 -23.089  1.00 60.15           N1+
ANISOU 4659  NH1 ARG A 622     7691   7434   7728    165   -387     83       N1+
ATOM   4660  NH2 ARG A 622      37.261 -30.817 -22.527  1.00 57.10           N  
ANISOU 4660  NH2 ARG A 622     7316   6971   7408    204   -423     66       N  
ATOM   4661  N   TYR A 623      36.048 -24.589 -19.713  1.00 18.09           N  
ANISOU 4661  N   TYR A 623     2299   2200   2377     63   -333    213       N  
ATOM   4662  CA  TYR A 623      34.596 -24.686 -19.728  1.00 14.47           C  
ANISOU 4662  CA  TYR A 623     1855   1723   1922     49   -357    227       C  
ATOM   4663  C   TYR A 623      34.087 -25.185 -21.075  1.00 20.51           C  
ANISOU 4663  C   TYR A 623     2644   2474   2675     65   -374    198       C  
ATOM   4664  O   TYR A 623      34.659 -24.860 -22.112  1.00 22.23           O  
ANISOU 4664  O   TYR A 623     2880   2705   2861     85   -354    177       O  
ATOM   4665  CB  TYR A 623      33.989 -23.309 -19.427  1.00 13.23           C  
ANISOU 4665  CB  TYR A 623     1698   1585   1744     30   -336    247       C  
ATOM   4666  CG  TYR A 623      34.012 -22.948 -17.947  1.00 16.80           C  
ANISOU 4666  CG  TYR A 623     2129   2046   2209      7   -329    273       C  
ATOM   4667  CD1 TYR A 623      32.865 -23.068 -17.165  1.00 14.09           C  
ANISOU 4667  CD1 TYR A 623     1780   1694   1878    -11   -343    295       C  
ATOM   4668  CD2 TYR A 623      35.183 -22.516 -17.334  1.00 14.99           C  
ANISOU 4668  CD2 TYR A 623     1883   1838   1975      3   -309    270       C  
ATOM   4669  CE1 TYR A 623      32.878 -22.749 -15.797  1.00 15.23           C  
ANISOU 4669  CE1 TYR A 623     1913   1849   2024    -30   -333    318       C  
ATOM   4670  CE2 TYR A 623      35.209 -22.193 -15.971  1.00 20.66           C  
ANISOU 4670  CE2 TYR A 623     2585   2569   2694    -15   -309    289       C  
ATOM   4671  CZ  TYR A 623      34.059 -22.313 -15.215  1.00 18.84           C  
ANISOU 4671  CZ  TYR A 623     2361   2329   2469    -29   -319    314       C  
ATOM   4672  OH  TYR A 623      34.100 -22.005 -13.882  1.00 14.48           O  
ANISOU 4672  OH  TYR A 623     1801   1791   1908    -44   -315    330       O  
ATOM   4673  N   CYS A 624      33.016 -25.975 -21.053  1.00 23.12           N  
ANISOU 4673  N   CYS A 624     2976   2781   3029     55   -409    194       N  
ATOM   4674  CA  CYS A 624      32.303 -26.336 -22.280  1.00 24.30           C  
ANISOU 4674  CA  CYS A 624     3144   2926   3165     66   -436    159       C  
ATOM   4675  C   CYS A 624      30.943 -25.664 -22.288  1.00 25.28           C  
ANISOU 4675  C   CYS A 624     3256   3067   3283     53   -455    166       C  
ATOM   4676  O   CYS A 624      30.390 -25.318 -21.225  1.00 20.29           O  
ANISOU 4676  O   CYS A 624     2599   2437   2673     28   -448    195       O  
ATOM   4677  CB  CYS A 624      32.131 -27.848 -22.413  1.00 24.68           C  
ANISOU 4677  CB  CYS A 624     3196   2930   3250     61   -465    131       C  
ATOM   4678  SG  CYS A 624      33.625 -28.692 -22.948  1.00 40.65           S  
ANISOU 4678  SG  CYS A 624     5240   4934   5272     99   -452    102       S  
ATOM   4679  N   ALA A 625      30.410 -25.481 -23.489  1.00 22.14           N  
ANISOU 4679  N   ALA A 625     2877   2686   2852     76   -479    137       N  
ATOM   4680  CA  ALA A 625      29.197 -24.704 -23.666  1.00 20.83           C  
ANISOU 4680  CA  ALA A 625     2698   2546   2672     82   -502    139       C  
ATOM   4681  C   ALA A 625      28.094 -25.507 -24.322  1.00 15.05           C  
ANISOU 4681  C   ALA A 625     1948   1816   1954     79   -558     93       C  
ATOM   4682  O   ALA A 625      28.348 -26.334 -25.191  1.00 21.60           O  
ANISOU 4682  O   ALA A 625     2798   2634   2773     88   -579     52       O  
ATOM   4683  CB  ALA A 625      29.490 -23.469 -24.486  1.00 19.49           C  
ANISOU 4683  CB  ALA A 625     2569   2401   2436    122   -484    152       C  
ATOM   4684  N   THR A 626      26.867 -25.245 -23.899  1.00 15.17           N  
ANISOU 4684  N   THR A 626     1920   1849   1996     64   -580     92       N  
ATOM   4685  CA  THR A 626      25.681 -25.743 -24.583  1.00 21.42           C  
ANISOU 4685  CA  THR A 626     2680   2658   2799     62   -639     39       C  
ATOM   4686  C   THR A 626      24.793 -24.542 -24.885  1.00 18.91           C  
ANISOU 4686  C   THR A 626     2347   2389   2449    104   -662     45       C  
ATOM   4687  O   THR A 626      24.825 -23.540 -24.177  1.00 19.98           O  
ANISOU 4687  O   THR A 626     2480   2531   2580    112   -628     90       O  
ATOM   4688  CB  THR A 626      24.892 -26.767 -23.738  1.00 30.78           C  
ANISOU 4688  CB  THR A 626     3811   3819   4066     -2   -644     21       C  
ATOM   4689  CG2 THR A 626      25.717 -28.011 -23.493  1.00 33.68           C  
ANISOU 4689  CG2 THR A 626     4206   4128   4464    -33   -624     17       C  
ATOM   4690  OG1 THR A 626      24.533 -26.182 -22.475  1.00 30.73           O  
ANISOU 4690  OG1 THR A 626     3772   3818   4088    -26   -607     65       O  
ATOM   4691  N   VAL A 627      24.004 -24.629 -25.945  1.00 19.53           N  
ANISOU 4691  N   VAL A 627     2418   2502   2502    136   -725     -4       N  
ATOM   4692  CA  VAL A 627      23.220 -23.480 -26.360  1.00 21.78           C  
ANISOU 4692  CA  VAL A 627     2697   2833   2745    194   -756      2       C  
ATOM   4693  C   VAL A 627      21.929 -23.977 -27.014  1.00 21.26           C  
ANISOU 4693  C   VAL A 627     2572   2810   2694    203   -838    -69       C  
ATOM   4694  O   VAL A 627      21.909 -25.055 -27.614  1.00 26.73           O  
ANISOU 4694  O   VAL A 627     3261   3497   3396    179   -873   -124       O  
ATOM   4695  CB  VAL A 627      24.068 -22.531 -27.284  1.00 31.36           C  
ANISOU 4695  CB  VAL A 627     4002   4049   3863    261   -741     35       C  
ATOM   4696  CG1 VAL A 627      24.485 -23.238 -28.559  1.00 28.35           C  
ANISOU 4696  CG1 VAL A 627     3669   3672   3429    282   -773     -8       C  
ATOM   4697  CG2 VAL A 627      23.323 -21.247 -27.609  1.00 30.24           C  
ANISOU 4697  CG2 VAL A 627     3871   3942   3675    330   -766     55       C  
ATOM   4698  N   ARG A 628      20.842 -23.231 -26.852  1.00 18.11           N  
ANISOU 4698  N   ARG A 628     2121   2457   2305    234   -869    -73       N  
ATOM   4699  CA  ARG A 628      19.579 -23.602 -27.476  1.00 19.06           C  
ANISOU 4699  CA  ARG A 628     2170   2631   2440    248   -954   -148       C  
ATOM   4700  C   ARG A 628      18.824 -22.376 -27.919  1.00 33.12           C  
ANISOU 4700  C   ARG A 628     3946   4467   4173    341  -1000   -140       C  
ATOM   4701  O   ARG A 628      19.110 -21.264 -27.497  1.00 36.79           O  
ANISOU 4701  O   ARG A 628     4448   4919   4611    380   -956    -76       O  
ATOM   4702  CB  ARG A 628      18.668 -24.407 -26.537  1.00 25.27           C  
ANISOU 4702  CB  ARG A 628     2848   3418   3334    165   -948   -187       C  
ATOM   4703  CG  ARG A 628      19.208 -25.752 -26.060  1.00 25.18           C  
ANISOU 4703  CG  ARG A 628     2842   3345   3382     72   -907   -199       C  
ATOM   4704  CD  ARG A 628      19.186 -26.772 -27.192  1.00 25.60           C  
ANISOU 4704  CD  ARG A 628     2907   3400   3422     64   -968   -275       C  
ATOM   4705  NE  ARG A 628      19.489 -28.120 -26.720  1.00 23.97           N  
ANISOU 4705  NE  ARG A 628     2698   3128   3284    -24   -933   -295       N  
ATOM   4706  CZ  ARG A 628      20.710 -28.566 -26.432  1.00 25.47           C  
ANISOU 4706  CZ  ARG A 628     2960   3252   3466    -40   -879   -252       C  
ATOM   4707  NH1 ARG A 628      21.763 -27.776 -26.551  1.00 20.06           N1+
ANISOU 4707  NH1 ARG A 628     2346   2563   2712     15   -848   -192       N1+
ATOM   4708  NH2 ARG A 628      20.877 -29.812 -26.012  1.00 28.67           N  
ANISOU 4708  NH2 ARG A 628     3365   3593   3935   -113   -853   -272       N  
ATOM   4709  N   VAL A 629      17.847 -22.617 -28.776  1.00 20.53           N  
ANISOU 4709  N   VAL A 629     2303   2933   2566    377  -1092   -211       N  
ATOM   4710  CA  VAL A 629      16.910 -21.627 -29.226  1.00 27.49           C  
ANISOU 4710  CA  VAL A 629     3159   3877   3409    473  -1157   -219       C  
ATOM   4711  C   VAL A 629      15.565 -22.005 -28.612  1.00 29.90           C  
ANISOU 4711  C   VAL A 629     3316   4231   3813    433  -1191   -284       C  
ATOM   4712  O   VAL A 629      15.254 -23.193 -28.487  1.00 22.13           O  
ANISOU 4712  O   VAL A 629     2265   3247   2898    347  -1201   -348       O  
ATOM   4713  CB  VAL A 629      16.834 -21.693 -30.767  1.00 29.53           C  
ANISOU 4713  CB  VAL A 629     3472   4179   3569    551  -1248   -261       C  
ATOM   4714  CG1 VAL A 629      15.421 -21.599 -31.239  1.00 32.58           C  
ANISOU 4714  CG1 VAL A 629     3762   4653   3964    607  -1357   -335       C  
ATOM   4715  CG2 VAL A 629      17.727 -20.636 -31.386  1.00 27.00           C  
ANISOU 4715  CG2 VAL A 629     3292   3834   3135    636  -1220   -183       C  
ATOM   4716  N   GLN A 630      14.772 -21.014 -28.218  1.00 28.49           N  
ANISOU 4716  N   GLN A 630     3087   4090   3647    492  -1201   -270       N  
ATOM   4717  CA  GLN A 630      13.439 -21.298 -27.695  1.00 28.81           C  
ANISOU 4717  CA  GLN A 630     2976   4189   3782    461  -1231   -338       C  
ATOM   4718  C   GLN A 630      12.477 -20.165 -27.999  1.00 30.32           C  
ANISOU 4718  C   GLN A 630     3124   4450   3947    582  -1296   -348       C  
ATOM   4719  O   GLN A 630      12.889 -19.096 -28.448  1.00 32.28           O  
ANISOU 4719  O   GLN A 630     3473   4685   4106    684  -1303   -286       O  
ATOM   4720  CB  GLN A 630      13.479 -21.551 -26.177  1.00 22.22           C  
ANISOU 4720  CB  GLN A 630     2090   3311   3043    360  -1127   -309       C  
ATOM   4721  CG  GLN A 630      13.735 -20.311 -25.326  1.00 21.61           C  
ANISOU 4721  CG  GLN A 630     2050   3208   2951    404  -1058   -229       C  
ATOM   4722  CD  GLN A 630      13.878 -20.631 -23.813  1.00 31.37           C  
ANISOU 4722  CD  GLN A 630     3250   4402   4266    301   -953   -200       C  
ATOM   4723  NE2 GLN A 630      13.943 -19.588 -22.989  1.00 24.98           N  
ANISOU 4723  NE2 GLN A 630     2459   3580   3455    334   -896   -146       N  
ATOM   4724  OE1 GLN A 630      13.929 -21.796 -23.407  1.00 25.05           O  
ANISOU 4724  OE1 GLN A 630     2415   3578   3525    198   -925   -226       O  
ATOM   4725  N   ARG A 631      11.197 -20.422 -27.743  1.00 34.52           N  
ANISOU 4725  N   ARG A 631     3505   5052   4559    567  -1340   -427       N  
ATOM   4726  CA  ARG A 631      10.119 -19.438 -27.855  1.00 38.79           C  
ANISOU 4726  CA  ARG A 631     3972   5669   5099    679  -1402   -449       C  
ATOM   4727  C   ARG A 631      10.525 -18.038 -27.395  1.00 35.20           C  
ANISOU 4727  C   ARG A 631     3605   5172   4598    764  -1345   -352       C  
ATOM   4728  O   ARG A 631      11.052 -17.871 -26.301  1.00 34.74           O  
ANISOU 4728  O   ARG A 631     3571   5052   4578    700  -1237   -296       O  
ATOM   4729  CB  ARG A 631       8.922 -19.916 -27.033  1.00 50.34           C  
ANISOU 4729  CB  ARG A 631     5251   7186   6689    608  -1393   -528       C  
ATOM   4730  CG  ARG A 631       7.817 -18.893 -26.845  1.00 62.12           C  
ANISOU 4730  CG  ARG A 631     6647   8752   8203    713  -1432   -550       C  
ATOM   4731  CD  ARG A 631       6.639 -19.514 -26.100  1.00 71.43           C  
ANISOU 4731  CD  ARG A 631     7644   9986   9510    622  -1406   -635       C  
ATOM   4732  NE  ARG A 631       6.453 -18.937 -24.771  1.00 79.23           N  
ANISOU 4732  NE  ARG A 631     8583  10959  10562    604  -1310   -599       N  
ATOM   4733  CZ  ARG A 631       5.743 -19.507 -23.801  1.00 85.25           C  
ANISOU 4733  CZ  ARG A 631     9210  11744  11438    497  -1244   -649       C  
ATOM   4734  NH1 ARG A 631       5.156 -20.682 -24.006  1.00 88.05           N1+
ANISOU 4734  NH1 ARG A 631     9458  12134  11864    395  -1267   -740       N1+
ATOM   4735  NH2 ARG A 631       5.627 -18.908 -22.621  1.00 85.40           N  
ANISOU 4735  NH2 ARG A 631     9210  11742  11495    487  -1143   -607       N  
ATOM   4736  N   PRO A 632      10.290 -17.027 -28.248  1.00 34.38           N  
ANISOU 4736  N   PRO A 632     3557   5098   4408    912  -1419   -334       N  
ATOM   4737  CA  PRO A 632      10.667 -15.637 -27.965  1.00 35.12           C  
ANISOU 4737  CA  PRO A 632     3751   5143   4451   1003  -1370   -243       C  
ATOM   4738  C   PRO A 632      10.080 -15.124 -26.648  1.00 40.74           C  
ANISOU 4738  C   PRO A 632     4372   5854   5253    985  -1300   -240       C  
ATOM   4739  O   PRO A 632       8.901 -15.370 -26.368  1.00 41.45           O  
ANISOU 4739  O   PRO A 632     4306   6021   5421    985  -1340   -317       O  
ATOM   4740  CB  PRO A 632      10.064 -14.866 -29.141  1.00 36.36           C  
ANISOU 4740  CB  PRO A 632     3953   5340   4521   1143  -1455   -246       C  
ATOM   4741  CG  PRO A 632       9.971 -15.871 -30.234  1.00 37.91           C  
ANISOU 4741  CG  PRO A 632     4144   5577   4683   1110  -1524   -308       C  
ATOM   4742  CD  PRO A 632       9.641 -17.169 -29.563  1.00 27.07           C  
ANISOU 4742  CD  PRO A 632     2627   4237   3424    979  -1521   -389       C  
ATOM   4743  N   ARG A 633      10.914 -14.431 -25.871  1.00 40.03           N  
ANISOU 4743  N   ARG A 633     4376   5681   5152    967  -1196   -157       N  
ATOM   4744  CA  ARG A 633      10.546 -13.777 -24.600  1.00 46.36           C  
ANISOU 4744  CA  ARG A 633     5125   6468   6020    958  -1117   -141       C  
ATOM   4745  C   ARG A 633      10.421 -14.697 -23.368  1.00 42.72           C  
ANISOU 4745  C   ARG A 633     4562   6009   5662    811  -1037   -171       C  
ATOM   4746  O   ARG A 633      10.234 -14.209 -22.249  1.00 40.17           O  
ANISOU 4746  O   ARG A 633     4208   5670   5385    792   -959   -155       O  
ATOM   4747  CB  ARG A 633       9.286 -12.903 -24.739  1.00 55.61           C  
ANISOU 4747  CB  ARG A 633     6214   7707   7207   1091  -1181   -179       C  
ATOM   4748  CG  ARG A 633       9.275 -11.933 -25.923  1.00 60.56           C  
ANISOU 4748  CG  ARG A 633     6946   8333   7729   1254  -1265   -145       C  
ATOM   4749  CD  ARG A 633      10.454 -10.967 -25.909  1.00 59.83           C  
ANISOU 4749  CD  ARG A 633     7042   8131   7559   1283  -1190    -40       C  
ATOM   4750  NE  ARG A 633      10.305  -9.926 -26.926  1.00 62.88           N  
ANISOU 4750  NE  ARG A 633     7536   8505   7851   1435  -1247     -2       N  
ATOM   4751  CZ  ARG A 633      11.269  -9.083 -27.287  1.00 61.46           C  
ANISOU 4751  CZ  ARG A 633     7533   8232   7585   1477  -1201     86       C  
ATOM   4752  NH1 ARG A 633      12.467  -9.150 -26.718  1.00 56.94           N1+
ANISOU 4752  NH1 ARG A 633     7042   7581   7013   1379  -1102    137       N1+
ATOM   4753  NH2 ARG A 633      11.038  -8.173 -28.223  1.00 62.43           N  
ANISOU 4753  NH2 ARG A 633     7757   8333   7631   1577  -1223    119       N  
ATOM   4754  N   GLN A 634      10.517 -16.010 -23.561  1.00 40.23           N  
ANISOU 4754  N   GLN A 634     4202   5707   5377    709  -1052   -214       N  
ATOM   4755  CA  GLN A 634      10.458 -16.935 -22.431  1.00 34.80           C  
ANISOU 4755  CA  GLN A 634     3439   5008   4778    569   -972   -232       C  
ATOM   4756  C   GLN A 634      11.740 -16.822 -21.624  1.00 35.53           C  
ANISOU 4756  C   GLN A 634     3646   5009   4844    506   -869   -149       C  
ATOM   4757  O   GLN A 634      12.842 -16.880 -22.182  1.00 31.05           O  
ANISOU 4757  O   GLN A 634     3197   4390   4210    508   -871   -104       O  
ATOM   4758  CB  GLN A 634      10.253 -18.374 -22.898  1.00 37.33           C  
ANISOU 4758  CB  GLN A 634     3694   5352   5137    478  -1014   -299       C  
ATOM   4759  CG  GLN A 634      10.098 -19.361 -21.753  1.00 38.97           C  
ANISOU 4759  CG  GLN A 634     3828   5540   5436    335   -928   -317       C  
ATOM   4760  CD  GLN A 634       9.748 -20.766 -22.222  1.00 48.73           C  
ANISOU 4760  CD  GLN A 634     4995   6796   6723    244   -968   -392       C  
ATOM   4761  NE2 GLN A 634       8.630 -20.893 -22.922  1.00 52.40           N  
ANISOU 4761  NE2 GLN A 634     5342   7346   7220    280  -1058   -483       N  
ATOM   4762  OE1 GLN A 634      10.470 -21.728 -21.947  1.00 53.09           O  
ANISOU 4762  OE1 GLN A 634     5598   7285   7288    145   -920   -372       O  
ATOM   4763  N   GLU A 635      11.597 -16.645 -20.315  1.00 36.35           N  
ANISOU 4763  N   GLU A 635     3714   5099   5000    454   -780   -134       N  
ATOM   4764  CA  GLU A 635      12.753 -16.481 -19.444  1.00 37.84           C  
ANISOU 4764  CA  GLU A 635     4002   5212   5164    400   -689    -62       C  
ATOM   4765  C   GLU A 635      13.244 -17.807 -18.877  1.00 32.86           C  
ANISOU 4765  C   GLU A 635     3366   4551   4570    269   -642    -61       C  
ATOM   4766  O   GLU A 635      14.431 -17.995 -18.667  1.00 35.10           O  
ANISOU 4766  O   GLU A 635     3746   4774   4816    231   -604     -9       O  
ATOM   4767  CB  GLU A 635      12.448 -15.490 -18.318  1.00 40.07           C  
ANISOU 4767  CB  GLU A 635     4270   5490   5465    422   -617    -42       C  
ATOM   4768  CG  GLU A 635      13.013 -14.101 -18.577  1.00 46.09           C  
ANISOU 4768  CG  GLU A 635     5142   6211   6160    521   -614      9       C  
ATOM   4769  CD  GLU A 635      14.546 -14.064 -18.583  1.00 51.97           C  
ANISOU 4769  CD  GLU A 635     6021   6880   6846    483   -575     73       C  
ATOM   4770  OE1 GLU A 635      15.201 -14.958 -17.972  1.00 47.32           O  
ANISOU 4770  OE1 GLU A 635     5440   6266   6272    381   -530     86       O  
ATOM   4771  OE2 GLU A 635      15.095 -13.120 -19.197  1.00 52.02           O1-
ANISOU 4771  OE2 GLU A 635     6127   6849   6791    557   -586    111       O1-
ATOM   4772  N   ILE A 636      12.315 -18.716 -18.626  1.00 32.07           N  
ANISOU 4772  N   ILE A 636     3152   4491   4544    203   -644   -119       N  
ATOM   4773  CA  ILE A 636      12.640 -20.061 -18.186  1.00 33.29           C  
ANISOU 4773  CA  ILE A 636     3301   4610   4737     82   -604   -122       C  
ATOM   4774  C   ILE A 636      13.574 -20.698 -19.208  1.00 37.02           C  
ANISOU 4774  C   ILE A 636     3857   5045   5162     80   -656   -113       C  
ATOM   4775  O   ILE A 636      13.351 -20.590 -20.415  1.00 39.19           O  
ANISOU 4775  O   ILE A 636     4128   5353   5408    144   -742   -148       O  
ATOM   4776  CB  ILE A 636      11.357 -20.909 -18.125  1.00 39.71           C  
ANISOU 4776  CB  ILE A 636     3973   5477   5639     20   -615   -203       C  
ATOM   4777  CG1 ILE A 636      10.354 -20.303 -17.136  1.00 45.98           C  
ANISOU 4777  CG1 ILE A 636     4670   6317   6485     23   -558   -222       C  
ATOM   4778  CG2 ILE A 636      11.674 -22.355 -17.828  1.00 39.66           C  
ANISOU 4778  CG2 ILE A 636     3975   5422   5673   -103   -578   -207       C  
ATOM   4779  CD1 ILE A 636      10.272 -20.993 -15.822  1.00 48.64           C  
ANISOU 4779  CD1 ILE A 636     4984   6624   6871    -93   -450   -206       C  
ATOM   4780  N   ILE A 637      14.625 -21.357 -18.743  1.00 32.98           N  
ANISOU 4780  N   ILE A 637     3423   4469   4640     13   -605    -68       N  
ATOM   4781  CA  ILE A 637      15.457 -22.115 -19.672  1.00 27.43           C  
ANISOU 4781  CA  ILE A 637     2786   3732   3904      4   -648    -69       C  
ATOM   4782  C   ILE A 637      14.820 -23.473 -19.928  1.00 27.64           C  
ANISOU 4782  C   ILE A 637     2743   3763   3996    -74   -671   -134       C  
ATOM   4783  O   ILE A 637      14.995 -24.420 -19.169  1.00 23.04           O  
ANISOU 4783  O   ILE A 637     2163   3135   3458   -165   -615   -124       O  
ATOM   4784  CB  ILE A 637      16.876 -22.284 -19.164  1.00 24.85           C  
ANISOU 4784  CB  ILE A 637     2565   3337   3541    -24   -593     -1       C  
ATOM   4785  CG1 ILE A 637      17.570 -20.928 -19.095  1.00 20.30           C  
ANISOU 4785  CG1 ILE A 637     2060   2754   2900     49   -575     52       C  
ATOM   4786  CG2 ILE A 637      17.647 -23.190 -20.087  1.00 20.15           C  
ANISOU 4786  CG2 ILE A 637     2025   2709   2923    -36   -631    -13       C  
ATOM   4787  CD1 ILE A 637      18.893 -20.963 -18.341  1.00 23.71           C  
ANISOU 4787  CD1 ILE A 637     2574   3131   3305     17   -515    112       C  
ATOM   4788  N   GLU A 638      14.061 -23.552 -21.010  1.00 25.48           N  
ANISOU 4788  N   GLU A 638     2412   3544   3727    -37   -756   -204       N  
ATOM   4789  CA  GLU A 638      13.230 -24.721 -21.266  1.00 26.72           C  
ANISOU 4789  CA  GLU A 638     2479   3716   3956   -113   -784   -285       C  
ATOM   4790  C   GLU A 638      13.986 -26.064 -21.414  1.00 26.70           C  
ANISOU 4790  C   GLU A 638     2538   3640   3967   -193   -768   -287       C  
ATOM   4791  O   GLU A 638      13.536 -27.084 -20.894  1.00 24.35           O  
ANISOU 4791  O   GLU A 638     2191   3315   3746   -294   -730   -318       O  
ATOM   4792  CB  GLU A 638      12.311 -24.447 -22.469  1.00 33.01           C  
ANISOU 4792  CB  GLU A 638     3202   4595   4743    -43   -893   -367       C  
ATOM   4793  CG  GLU A 638      11.445 -25.611 -22.899  1.00 49.19           C  
ANISOU 4793  CG  GLU A 638     5154   6670   6867   -120   -936   -469       C  
ATOM   4794  CD  GLU A 638      10.315 -25.171 -23.813  1.00 71.83           C  
ANISOU 4794  CD  GLU A 638     7917   9641   9736    -47  -1042   -555       C  
ATOM   4795  OE1 GLU A 638       9.819 -26.005 -24.604  1.00 80.02           O  
ANISOU 4795  OE1 GLU A 638     8897  10707  10801    -82  -1112   -647       O  
ATOM   4796  OE2 GLU A 638       9.917 -23.987 -23.735  1.00 78.79           O1-
ANISOU 4796  OE2 GLU A 638     8772  10574  10589     48  -1060   -535       O1-
ATOM   4797  N   ASP A 639      15.117 -26.084 -22.117  1.00 24.72           N  
ANISOU 4797  N   ASP A 639     2394   3353   3645   -150   -793   -257       N  
ATOM   4798  CA  ASP A 639      15.836 -27.349 -22.280  1.00 20.31           C  
ANISOU 4798  CA  ASP A 639     1892   2724   3100   -214   -780   -263       C  
ATOM   4799  C   ASP A 639      16.892 -27.555 -21.204  1.00 22.65           C  
ANISOU 4799  C   ASP A 639     2268   2946   3393   -250   -693   -179       C  
ATOM   4800  O   ASP A 639      17.808 -28.344 -21.404  1.00 23.83           O  
ANISOU 4800  O   ASP A 639     2489   3034   3529   -269   -686   -166       O  
ATOM   4801  CB  ASP A 639      16.483 -27.471 -23.672  1.00 35.79           C  
ANISOU 4801  CB  ASP A 639     3920   4687   4991   -155   -851   -289       C  
ATOM   4802  CG  ASP A 639      15.474 -27.394 -24.798  1.00 45.96           C  
ANISOU 4802  CG  ASP A 639     5138   6051   6274   -116   -949   -379       C  
ATOM   4803  OD1 ASP A 639      14.688 -28.349 -24.936  1.00 52.30           O  
ANISOU 4803  OD1 ASP A 639     5866   6859   7145   -187   -973   -458       O  
ATOM   4804  OD2 ASP A 639      15.468 -26.387 -25.547  1.00 49.44           O1-
ANISOU 4804  OD2 ASP A 639     5601   6545   6639    -15  -1003   -371       O1-
ATOM   4805  N   LEU A 640      16.769 -26.846 -20.078  1.00 19.09           N  
ANISOU 4805  N   LEU A 640     1802   2502   2948   -253   -633   -126       N  
ATOM   4806  CA  LEU A 640      17.777 -26.898 -19.016  1.00 21.12           C  
ANISOU 4806  CA  LEU A 640     2134   2702   3188   -274   -559    -47       C  
ATOM   4807  C   LEU A 640      18.190 -28.316 -18.577  1.00 22.90           C  
ANISOU 4807  C   LEU A 640     2397   2849   3454   -354   -522    -38       C  
ATOM   4808  O   LEU A 640      19.375 -28.600 -18.441  1.00 22.21           O  
ANISOU 4808  O   LEU A 640     2396   2712   3333   -341   -506      8       O  
ATOM   4809  CB  LEU A 640      17.357 -26.061 -17.790  1.00 18.17           C  
ANISOU 4809  CB  LEU A 640     1729   2353   2824   -279   -498     -7       C  
ATOM   4810  CG  LEU A 640      18.453 -26.014 -16.718  1.00 18.68           C  
ANISOU 4810  CG  LEU A 640     1874   2368   2856   -290   -433     72       C  
ATOM   4811  CD1 LEU A 640      19.759 -25.432 -17.267  1.00 16.65           C  
ANISOU 4811  CD1 LEU A 640     1700   2100   2528   -222   -458    106       C  
ATOM   4812  CD2 LEU A 640      17.996 -25.245 -15.472  1.00 22.50           C  
ANISOU 4812  CD2 LEU A 640     2329   2875   3343   -299   -370    103       C  
ATOM   4813  N   SER A 641      17.221 -29.196 -18.365  1.00 19.34           N  
ANISOU 4813  N   SER A 641     1884   2386   3078   -435   -507    -84       N  
ATOM   4814  CA  SER A 641      17.539 -30.557 -17.964  1.00 26.24           C  
ANISOU 4814  CA  SER A 641     2803   3173   3994   -511   -466    -75       C  
ATOM   4815  C   SER A 641      18.432 -31.282 -18.978  1.00 27.78           C  
ANISOU 4815  C   SER A 641     3068   3321   4166   -487   -515    -96       C  
ATOM   4816  O   SER A 641      19.431 -31.890 -18.593  1.00 31.69           O  
ANISOU 4816  O   SER A 641     3647   3745   4648   -491   -485    -48       O  
ATOM   4817  CB  SER A 641      16.277 -31.376 -17.689  1.00 23.55           C  
ANISOU 4817  CB  SER A 641     2380   2823   3744   -612   -438   -131       C  
ATOM   4818  OG  SER A 641      16.640 -32.714 -17.387  1.00 26.54           O  
ANISOU 4818  OG  SER A 641     2822   3102   4160   -683   -398   -120       O  
ATOM   4819  N   TYR A 642      18.070 -31.206 -20.259  1.00 26.09           N  
ANISOU 4819  N   TYR A 642     2819   3152   3943   -456   -592   -170       N  
ATOM   4820  CA  TYR A 642      18.879 -31.765 -21.341  1.00 29.11           C  
ANISOU 4820  CA  TYR A 642     3265   3503   4292   -423   -640   -198       C  
ATOM   4821  C   TYR A 642      20.286 -31.178 -21.347  1.00 24.91           C  
ANISOU 4821  C   TYR A 642     2821   2961   3684   -347   -630   -130       C  
ATOM   4822  O   TYR A 642      21.269 -31.887 -21.525  1.00 25.57           O  
ANISOU 4822  O   TYR A 642     2976   2985   3755   -340   -623   -117       O  
ATOM   4823  CB  TYR A 642      18.249 -31.441 -22.703  1.00 42.04           C  
ANISOU 4823  CB  TYR A 642     4853   5212   5907   -381   -728   -282       C  
ATOM   4824  CG  TYR A 642      17.156 -32.368 -23.177  1.00 65.37           C  
ANISOU 4824  CG  TYR A 642     7735   8169   8934   -453   -764   -382       C  
ATOM   4825  CD1 TYR A 642      17.028 -33.656 -22.670  1.00 75.42           C  
ANISOU 4825  CD1 TYR A 642     9016   9355  10284   -552   -717   -398       C  
ATOM   4826  CD2 TYR A 642      16.253 -31.954 -24.162  1.00 73.58           C  
ANISOU 4826  CD2 TYR A 642     8699   9295   9962   -420   -847   -463       C  
ATOM   4827  CE1 TYR A 642      16.020 -34.504 -23.122  1.00 81.98           C  
ANISOU 4827  CE1 TYR A 642     9777  10185  11189   -629   -745   -499       C  
ATOM   4828  CE2 TYR A 642      15.249 -32.791 -24.620  1.00 75.82           C  
ANISOU 4828  CE2 TYR A 642     8904   9589  10314   -489   -886   -568       C  
ATOM   4829  CZ  TYR A 642      15.137 -34.065 -24.096  1.00 82.26           C  
ANISOU 4829  CZ  TYR A 642     9725  10315  11215   -600   -832   -588       C  
ATOM   4830  OH  TYR A 642      14.145 -34.906 -24.547  1.00 86.18           O  
ANISOU 4830  OH  TYR A 642    10141  10817  11786   -680   -866   -699       O  
ATOM   4831  N   MET A 643      20.361 -29.864 -21.183  1.00 18.26           N  
ANISOU 4831  N   MET A 643     1969   2177   2792   -290   -629    -91       N  
ATOM   4832  CA  MET A 643      21.610 -29.138 -21.291  1.00 17.43           C  
ANISOU 4832  CA  MET A 643     1933   2073   2615   -222   -620    -37       C  
ATOM   4833  C   MET A 643      22.583 -29.478 -20.162  1.00 20.49           C  
ANISOU 4833  C   MET A 643     2374   2403   3007   -242   -559     31       C  
ATOM   4834  O   MET A 643      23.768 -29.706 -20.402  1.00 21.09           O  
ANISOU 4834  O   MET A 643     2512   2450   3051   -210   -557     50       O  
ATOM   4835  CB  MET A 643      21.327 -27.640 -21.335  1.00 17.09           C  
ANISOU 4835  CB  MET A 643     1868   2099   2528   -164   -629    -16       C  
ATOM   4836  CG  MET A 643      20.449 -27.203 -22.538  1.00 17.65           C  
ANISOU 4836  CG  MET A 643     1898   2232   2578   -121   -701    -78       C  
ATOM   4837  SD  MET A 643      20.339 -25.402 -22.626  1.00 21.03           S  
ANISOU 4837  SD  MET A 643     2328   2718   2942    -35   -706    -39       S  
ATOM   4838  CE  MET A 643      18.634 -25.178 -22.487  1.00 31.36           C  
ANISOU 4838  CE  MET A 643     3523   4087   4303    -44   -739    -91       C  
ATOM   4839  N   VAL A 644      22.069 -29.526 -18.937  1.00 17.02           N  
ANISOU 4839  N   VAL A 644     1909   1953   2605   -291   -511     63       N  
ATOM   4840  CA  VAL A 644      22.877 -29.889 -17.784  1.00 22.14           C  
ANISOU 4840  CA  VAL A 644     2609   2551   3252   -307   -458    128       C  
ATOM   4841  C   VAL A 644      23.376 -31.317 -17.945  1.00 22.33           C  
ANISOU 4841  C   VAL A 644     2683   2495   3305   -333   -458    119       C  
ATOM   4842  O   VAL A 644      24.540 -31.605 -17.703  1.00 26.32           O  
ANISOU 4842  O   VAL A 644     3250   2965   3786   -302   -449    156       O  
ATOM   4843  CB  VAL A 644      22.088 -29.725 -16.460  1.00 18.14           C  
ANISOU 4843  CB  VAL A 644     2070   2050   2774   -358   -402    161       C  
ATOM   4844  CG1 VAL A 644      22.840 -30.350 -15.295  1.00 16.87           C  
ANISOU 4844  CG1 VAL A 644     1974   1829   2607   -378   -354    226       C  
ATOM   4845  CG2 VAL A 644      21.836 -28.247 -16.182  1.00 19.10           C  
ANISOU 4845  CG2 VAL A 644     2157   2241   2859   -319   -396    177       C  
ATOM   4846  N   ARG A 645      22.493 -32.201 -18.389  1.00 26.54           N  
ANISOU 4846  N   ARG A 645     3187   3001   3894   -388   -471     63       N  
ATOM   4847  CA  ARG A 645      22.862 -33.593 -18.633  1.00 32.88           C  
ANISOU 4847  CA  ARG A 645     4042   3718   4733   -416   -471     44       C  
ATOM   4848  C   ARG A 645      24.075 -33.716 -19.588  1.00 25.29           C  
ANISOU 4848  C   ARG A 645     3135   2747   3727   -345   -509     31       C  
ATOM   4849  O   ARG A 645      25.025 -34.451 -19.282  1.00 18.62           O  
ANISOU 4849  O   ARG A 645     2355   1837   2882   -329   -492     61       O  
ATOM   4850  CB  ARG A 645      21.648 -34.379 -19.152  1.00 41.10           C  
ANISOU 4850  CB  ARG A 645     5032   4742   5843   -489   -485    -33       C  
ATOM   4851  CG  ARG A 645      21.843 -35.878 -19.276  1.00 52.20           C  
ANISOU 4851  CG  ARG A 645     6493   6042   7299   -535   -473    -56       C  
ATOM   4852  CD  ARG A 645      21.223 -36.417 -20.578  1.00 63.83           C  
ANISOU 4852  CD  ARG A 645     7930   7519   8803   -559   -529   -163       C  
ATOM   4853  NE  ARG A 645      19.760 -36.361 -20.594  1.00 72.52           N  
ANISOU 4853  NE  ARG A 645     8934   8660   9961   -633   -533   -222       N  
ATOM   4854  CZ  ARG A 645      18.961 -37.416 -20.436  1.00 77.34           C  
ANISOU 4854  CZ  ARG A 645     9524   9207  10655   -733   -506   -269       C  
ATOM   4855  NH1 ARG A 645      19.475 -38.627 -20.251  1.00 77.06           N1+
ANISOU 4855  NH1 ARG A 645     9572   9053  10653   -767   -473   -259       N1+
ATOM   4856  NH2 ARG A 645      17.642 -37.261 -20.463  1.00 78.23           N  
ANISOU 4856  NH2 ARG A 645     9531   9372  10821   -798   -510   -330       N  
ATOM   4857  N   GLU A 646      24.050 -32.977 -20.707  1.00 21.24           N  
ANISOU 4857  N   GLU A 646     2598   2301   3173   -298   -557    -12       N  
ATOM   4858  CA  GLU A 646      25.165 -32.954 -21.664  1.00 21.59           C  
ANISOU 4858  CA  GLU A 646     2690   2348   3166   -232   -583    -27       C  
ATOM   4859  C   GLU A 646      26.460 -32.542 -21.000  1.00 19.60           C  
ANISOU 4859  C   GLU A 646     2479   2090   2877   -186   -550     40       C  
ATOM   4860  O   GLU A 646      27.503 -33.148 -21.228  1.00 24.27           O  
ANISOU 4860  O   GLU A 646     3119   2642   3461   -154   -548     41       O  
ATOM   4861  CB  GLU A 646      24.935 -31.951 -22.807  1.00 21.76           C  
ANISOU 4861  CB  GLU A 646     2687   2448   3131   -184   -628    -65       C  
ATOM   4862  CG  GLU A 646      24.143 -32.429 -23.993  1.00 40.09           C  
ANISOU 4862  CG  GLU A 646     4988   4785   5461   -195   -684   -152       C  
ATOM   4863  CD  GLU A 646      23.973 -31.325 -25.052  1.00 49.66           C  
ANISOU 4863  CD  GLU A 646     6189   6079   6600   -132   -729   -174       C  
ATOM   4864  OE1 GLU A 646      24.984 -30.894 -25.661  1.00 47.26           O  
ANISOU 4864  OE1 GLU A 646     5938   5788   6231    -73   -725   -159       O  
ATOM   4865  OE2 GLU A 646      22.826 -30.876 -25.264  1.00 51.74           O1-
ANISOU 4865  OE2 GLU A 646     6393   6395   6870   -139   -766   -205       O1-
ATOM   4866  N   LEU A 647      26.391 -31.464 -20.224  1.00 18.24           N  
ANISOU 4866  N   LEU A 647     2285   1964   2682   -180   -528     90       N  
ATOM   4867  CA  LEU A 647      27.549 -30.960 -19.497  1.00 18.92           C  
ANISOU 4867  CA  LEU A 647     2398   2056   2734   -144   -500    147       C  
ATOM   4868  C   LEU A 647      28.096 -31.979 -18.502  1.00 19.40           C  
ANISOU 4868  C   LEU A 647     2499   2049   2823   -157   -475    186       C  
ATOM   4869  O   LEU A 647      29.305 -32.160 -18.410  1.00 22.42           O  
ANISOU 4869  O   LEU A 647     2915   2418   3186   -113   -473    204       O  
ATOM   4870  CB  LEU A 647      27.202 -29.654 -18.783  1.00 16.54           C  
ANISOU 4870  CB  LEU A 647     2065   1810   2409   -144   -479    184       C  
ATOM   4871  CG  LEU A 647      26.992 -28.494 -19.764  1.00 19.22           C  
ANISOU 4871  CG  LEU A 647     2385   2211   2706   -108   -502    159       C  
ATOM   4872  CD1 LEU A 647      26.515 -27.239 -19.059  1.00 14.78           C  
ANISOU 4872  CD1 LEU A 647     1795   1694   2129   -108   -480    190       C  
ATOM   4873  CD2 LEU A 647      28.280 -28.213 -20.519  1.00 14.84           C  
ANISOU 4873  CD2 LEU A 647     1869   1665   2106    -57   -503    156       C  
ATOM   4874  N   LEU A 648      27.206 -32.640 -17.764  1.00 20.01           N  
ANISOU 4874  N   LEU A 648     2573   2083   2945   -216   -454    199       N  
ATOM   4875  CA  LEU A 648      27.620 -33.606 -16.746  1.00 23.05           C  
ANISOU 4875  CA  LEU A 648     3012   2397   3351   -227   -426    246       C  
ATOM   4876  C   LEU A 648      28.283 -34.792 -17.406  1.00 25.08           C  
ANISOU 4876  C   LEU A 648     3317   2583   3629   -204   -444    218       C  
ATOM   4877  O   LEU A 648      29.217 -35.367 -16.852  1.00 17.48           O  
ANISOU 4877  O   LEU A 648     2407   1575   2661   -167   -436    256       O  
ATOM   4878  CB  LEU A 648      26.422 -34.107 -15.936  1.00 21.69           C  
ANISOU 4878  CB  LEU A 648     2832   2187   3224   -305   -388    262       C  
ATOM   4879  CG  LEU A 648      25.795 -33.134 -14.947  1.00 24.36           C  
ANISOU 4879  CG  LEU A 648     3132   2580   3544   -330   -355    300       C  
ATOM   4880  CD1 LEU A 648      24.522 -33.739 -14.396  1.00 19.52           C  
ANISOU 4880  CD1 LEU A 648     2502   1930   2986   -415   -312    298       C  
ATOM   4881  CD2 LEU A 648      26.774 -32.854 -13.822  1.00 16.86           C  
ANISOU 4881  CD2 LEU A 648     2228   1633   2547   -290   -336    369       C  
ATOM   4882  N   ILE A 649      27.780 -35.156 -18.588  1.00 21.35           N  
ANISOU 4882  N   ILE A 649     2829   2104   3180   -220   -471    148       N  
ATOM   4883  CA  ILE A 649      28.304 -36.297 -19.324  1.00 24.19           C  
ANISOU 4883  CA  ILE A 649     3235   2394   3562   -201   -487    107       C  
ATOM   4884  C   ILE A 649      29.682 -35.927 -19.848  1.00 23.11           C  
ANISOU 4884  C   ILE A 649     3115   2291   3377   -117   -503    105       C  
ATOM   4885  O   ILE A 649      30.615 -36.722 -19.785  1.00 23.53           O  
ANISOU 4885  O   ILE A 649     3215   2288   3438    -74   -502    111       O  
ATOM   4886  CB  ILE A 649      27.368 -36.703 -20.479  1.00 25.70           C  
ANISOU 4886  CB  ILE A 649     3402   2581   3784   -242   -517     21       C  
ATOM   4887  CG1 ILE A 649      26.074 -37.294 -19.922  1.00 23.14           C  
ANISOU 4887  CG1 ILE A 649     3059   2211   3524   -335   -493     14       C  
ATOM   4888  CG2 ILE A 649      28.026 -37.715 -21.406  1.00 19.23           C  
ANISOU 4888  CG2 ILE A 649     2632   1701   2975   -211   -536    -33       C  
ATOM   4889  CD1 ILE A 649      25.074 -37.693 -21.011  1.00 26.10           C  
ANISOU 4889  CD1 ILE A 649     3394   2588   3934   -384   -528    -83       C  
ATOM   4890  N   GLN A 650      29.816 -34.689 -20.308  1.00 19.02           N  
ANISOU 4890  N   GLN A 650     2556   1862   2810    -92   -514     98       N  
ATOM   4891  CA  GLN A 650      31.095 -34.204 -20.820  1.00 23.28           C  
ANISOU 4891  CA  GLN A 650     3102   2440   3304    -23   -517     94       C  
ATOM   4892  C   GLN A 650      32.142 -34.052 -19.701  1.00 20.30           C  
ANISOU 4892  C   GLN A 650     2736   2063   2916     12   -497    155       C  
ATOM   4893  O   GLN A 650      33.319 -34.399 -19.870  1.00 22.19           O  
ANISOU 4893  O   GLN A 650     2992   2293   3148     68   -499    148       O  
ATOM   4894  CB  GLN A 650      30.891 -32.899 -21.603  1.00 25.00           C  
ANISOU 4894  CB  GLN A 650     3285   2743   3472    -13   -525     75       C  
ATOM   4895  CG  GLN A 650      32.118 -32.408 -22.328  1.00 30.09           C  
ANISOU 4895  CG  GLN A 650     3938   3425   4071     46   -518     61       C  
ATOM   4896  CD  GLN A 650      32.705 -33.450 -23.269  1.00 36.70           C  
ANISOU 4896  CD  GLN A 650     4808   4222   4915     78   -528      7       C  
ATOM   4897  NE2 GLN A 650      34.012 -33.671 -23.163  1.00 37.16           N  
ANISOU 4897  NE2 GLN A 650     4876   4274   4968    127   -510     13       N  
ATOM   4898  OE1 GLN A 650      31.992 -34.047 -24.079  1.00 34.03           O  
ANISOU 4898  OE1 GLN A 650     4482   3860   4587     60   -552    -45       O  
ATOM   4899  N   PHE A 651      31.707 -33.556 -18.550  1.00 24.27           N  
ANISOU 4899  N   PHE A 651     3224   2580   3416    -18   -481    208       N  
ATOM   4900  CA  PHE A 651      32.564 -33.496 -17.372  1.00 24.09           C  
ANISOU 4900  CA  PHE A 651     3215   2557   3379     12   -470    263       C  
ATOM   4901  C   PHE A 651      33.115 -34.895 -17.050  1.00 22.87           C  
ANISOU 4901  C   PHE A 651     3117   2319   3255     42   -475    276       C  
ATOM   4902  O   PHE A 651      34.316 -35.082 -16.851  1.00 24.96           O  
ANISOU 4902  O   PHE A 651     3392   2587   3506    106   -485    285       O  
ATOM   4903  CB  PHE A 651      31.772 -32.920 -16.186  1.00 15.96           C  
ANISOU 4903  CB  PHE A 651     2174   1547   2343    -33   -449    313       C  
ATOM   4904  CG  PHE A 651      32.573 -32.782 -14.910  1.00 15.94           C  
ANISOU 4904  CG  PHE A 651     2189   1555   2313     -2   -443    369       C  
ATOM   4905  CD1 PHE A 651      33.088 -31.549 -14.527  1.00 15.41           C  
ANISOU 4905  CD1 PHE A 651     2087   1563   2206     13   -440    378       C  
ATOM   4906  CD2 PHE A 651      32.779 -33.882 -14.071  1.00 25.58           C  
ANISOU 4906  CD2 PHE A 651     3466   2707   3547     11   -441    410       C  
ATOM   4907  CE1 PHE A 651      33.813 -31.406 -13.337  1.00 15.49           C  
ANISOU 4907  CE1 PHE A 651     2108   1590   2186     41   -442    420       C  
ATOM   4908  CE2 PHE A 651      33.491 -33.758 -12.882  1.00 22.11           C  
ANISOU 4908  CE2 PHE A 651     3047   2283   3072     47   -444    460       C  
ATOM   4909  CZ  PHE A 651      34.012 -32.509 -12.512  1.00 18.71           C  
ANISOU 4909  CZ  PHE A 651     2571   1939   2599     61   -448    461       C  
ATOM   4910  N   TYR A 652      32.229 -35.880 -17.008  1.00 17.41           N  
ANISOU 4910  N   TYR A 652     2460   1550   2606     -3   -468    273       N  
ATOM   4911  CA  TYR A 652      32.649 -37.252 -16.749  1.00 18.20           C  
ANISOU 4911  CA  TYR A 652     2627   1551   2737     24   -469    286       C  
ATOM   4912  C   TYR A 652      33.632 -37.792 -17.784  1.00 28.58           C  
ANISOU 4912  C   TYR A 652     3953   2848   4057     89   -490    233       C  
ATOM   4913  O   TYR A 652      34.586 -38.467 -17.431  1.00 35.19           O  
ANISOU 4913  O   TYR A 652     4828   3643   4898    155   -498    252       O  
ATOM   4914  CB  TYR A 652      31.448 -38.180 -16.678  1.00 25.74           C  
ANISOU 4914  CB  TYR A 652     3616   2419   3744    -51   -448    281       C  
ATOM   4915  CG  TYR A 652      31.841 -39.608 -16.397  1.00 36.07           C  
ANISOU 4915  CG  TYR A 652     5009   3609   5087    -26   -442    298       C  
ATOM   4916  CD1 TYR A 652      32.317 -39.982 -15.148  1.00 35.13           C  
ANISOU 4916  CD1 TYR A 652     4947   3447   4952      8   -429    377       C  
ATOM   4917  CD2 TYR A 652      31.745 -40.582 -17.381  1.00 43.09           C  
ANISOU 4917  CD2 TYR A 652     5927   4424   6020    -31   -450    235       C  
ATOM   4918  CE1 TYR A 652      32.676 -41.292 -14.883  1.00 43.19           C  
ANISOU 4918  CE1 TYR A 652     6057   4350   6002     40   -423    400       C  
ATOM   4919  CE2 TYR A 652      32.100 -41.890 -17.130  1.00 45.99           C  
ANISOU 4919  CE2 TYR A 652     6380   4670   6423     -5   -441    251       C  
ATOM   4920  CZ  TYR A 652      32.565 -42.242 -15.880  1.00 52.28           C  
ANISOU 4920  CZ  TYR A 652     7238   5421   7205     33   -427    337       C  
ATOM   4921  OH  TYR A 652      32.924 -43.549 -15.629  1.00 59.85           O  
ANISOU 4921  OH  TYR A 652     8293   6250   8196     69   -418    359       O  
ATOM   4922  N   LYS A 653      33.391 -37.504 -19.060  1.00 31.88           N  
ANISOU 4922  N   LYS A 653     4340   3300   4473     78   -501    165       N  
ATOM   4923  CA  LYS A 653      34.302 -37.929 -20.122  1.00 36.32           C  
ANISOU 4923  CA  LYS A 653     4912   3855   5033    138   -513    108       C  
ATOM   4924  C   LYS A 653      35.701 -37.351 -19.928  1.00 34.31           C  
ANISOU 4924  C   LYS A 653     4630   3662   4744    214   -514    123       C  
ATOM   4925  O   LYS A 653      36.689 -38.016 -20.211  1.00 39.98           O  
ANISOU 4925  O   LYS A 653     5366   4353   5472    281   -519    101       O  
ATOM   4926  CB  LYS A 653      33.785 -37.506 -21.504  1.00 39.94           C  
ANISOU 4926  CB  LYS A 653     5343   4357   5474    114   -523     37       C  
ATOM   4927  CG  LYS A 653      32.807 -38.462 -22.156  1.00 49.65           C  
ANISOU 4927  CG  LYS A 653     6602   5518   6745     65   -535    -18       C  
ATOM   4928  CD  LYS A 653      32.744 -38.213 -23.660  1.00 59.41           C  
ANISOU 4928  CD  LYS A 653     7825   6800   7950     76   -554    -99       C  
ATOM   4929  CE  LYS A 653      34.146 -38.240 -24.279  1.00 68.48           C  
ANISOU 4929  CE  LYS A 653     8983   7968   9068    159   -546   -123       C  
ATOM   4930  NZ  LYS A 653      34.167 -37.913 -25.741  1.00 69.67           N1+
ANISOU 4930  NZ  LYS A 653     9130   8170   9172    174   -555   -196       N1+
ATOM   4931  N   SER A 654      35.774 -36.113 -19.448  1.00 26.43           N  
ANISOU 4931  N   SER A 654     3585   2748   3709    201   -507    155       N  
ATOM   4932  CA  SER A 654      37.039 -35.393 -19.371  1.00 28.57           C  
ANISOU 4932  CA  SER A 654     3816   3089   3950    256   -504    155       C  
ATOM   4933  C   SER A 654      37.823 -35.629 -18.099  1.00 25.74           C  
ANISOU 4933  C   SER A 654     3462   2726   3593    302   -515    206       C  
ATOM   4934  O   SER A 654      39.047 -35.562 -18.113  1.00 26.72           O  
ANISOU 4934  O   SER A 654     3558   2885   3710    365   -522    190       O  
ATOM   4935  CB  SER A 654      36.800 -33.903 -19.515  1.00 31.80           C  
ANISOU 4935  CB  SER A 654     4176   3586   4320    220   -489    158       C  
ATOM   4936  OG  SER A 654      36.278 -33.628 -20.801  1.00 42.83           O  
ANISOU 4936  OG  SER A 654     5571   4998   5704    199   -483    109       O  
ATOM   4937  N   THR A 655      37.134 -35.875 -16.993  1.00 23.94           N  
ANISOU 4937  N   THR A 655     3268   2459   3369    271   -517    264       N  
ATOM   4938  CA  THR A 655      37.836 -36.018 -15.714  1.00 25.08           C  
ANISOU 4938  CA  THR A 655     3425   2606   3499    318   -533    317       C  
ATOM   4939  C   THR A 655      37.726 -37.427 -15.166  1.00 25.53           C  
ANISOU 4939  C   THR A 655     3563   2556   3583    347   -542    354       C  
ATOM   4940  O   THR A 655      38.464 -37.806 -14.251  1.00 29.97           O  
ANISOU 4940  O   THR A 655     4150   3107   4131    411   -565    394       O  
ATOM   4941  CB  THR A 655      37.283 -35.058 -14.655  1.00 21.87           C  
ANISOU 4941  CB  THR A 655     3002   2250   3059    270   -524    366       C  
ATOM   4942  CG2 THR A 655      37.253 -33.625 -15.192  1.00 16.58           C  
ANISOU 4942  CG2 THR A 655     2264   1670   2364    236   -509    333       C  
ATOM   4943  OG1 THR A 655      35.962 -35.472 -14.279  1.00 20.95           O  
ANISOU 4943  OG1 THR A 655     2931   2072   2958    204   -504    399       O  
ATOM   4944  N   ARG A 656      36.788 -38.189 -15.725  1.00 20.34           N  
ANISOU 4944  N   ARG A 656     2949   1817   2963    299   -526    337       N  
ATOM   4945  CA  ARG A 656      36.476 -39.528 -15.245  1.00 27.70           C  
ANISOU 4945  CA  ARG A 656     3969   2627   3927    305   -521    372       C  
ATOM   4946  C   ARG A 656      35.855 -39.547 -13.840  1.00 24.41           C  
ANISOU 4946  C   ARG A 656     3599   2186   3491    269   -504    455       C  
ATOM   4947  O   ARG A 656      35.868 -40.578 -13.187  1.00 28.53           O  
ANISOU 4947  O   ARG A 656     4205   2612   4025    293   -500    503       O  
ATOM   4948  CB  ARG A 656      37.708 -40.446 -15.308  1.00 36.71           C  
ANISOU 4948  CB  ARG A 656     5146   3722   5080    414   -548    365       C  
ATOM   4949  CG  ARG A 656      38.533 -40.328 -16.598  1.00 40.78           C  
ANISOU 4949  CG  ARG A 656     5609   4280   5605    461   -558    283       C  
ATOM   4950  CD  ARG A 656      37.796 -40.870 -17.814  1.00 45.26           C  
ANISOU 4950  CD  ARG A 656     6197   4790   6210    412   -542    219       C  
ATOM   4951  NE  ARG A 656      37.524 -42.302 -17.697  1.00 58.05           N  
ANISOU 4951  NE  ARG A 656     7910   6271   7877    422   -537    227       N  
ATOM   4952  CZ  ARG A 656      36.313 -42.847 -17.786  1.00 60.43           C  
ANISOU 4952  CZ  ARG A 656     8257   6491   8212    335   -515    225       C  
ATOM   4953  NH1 ARG A 656      35.252 -42.078 -18.001  1.00 60.48           N1+
ANISOU 4953  NH1 ARG A 656     8217   6551   8212    240   -502    212       N1+
ATOM   4954  NH2 ARG A 656      36.162 -44.161 -17.661  1.00 60.41           N  
ANISOU 4954  NH2 ARG A 656     8346   6352   8255    343   -505    232       N  
ATOM   4955  N   PHE A 657      35.295 -38.427 -13.383  1.00 27.97           N  
ANISOU 4955  N   PHE A 657     4001   2716   3910    213   -491    473       N  
ATOM   4956  CA  PHE A 657      34.523 -38.422 -12.125  1.00 31.47           C  
ANISOU 4956  CA  PHE A 657     4486   3136   4333    166   -462    545       C  
ATOM   4957  C   PHE A 657      33.139 -37.830 -12.333  1.00 25.35           C  
ANISOU 4957  C   PHE A 657     3673   2384   3575     61   -426    528       C  
ATOM   4958  O   PHE A 657      32.943 -36.993 -13.206  1.00 29.13           O  
ANISOU 4958  O   PHE A 657     4080   2932   4056     39   -433    473       O  
ATOM   4959  CB  PHE A 657      35.172 -37.568 -11.024  1.00 34.11           C  
ANISOU 4959  CB  PHE A 657     4802   3554   4603    207   -480    590       C  
ATOM   4960  CG  PHE A 657      36.659 -37.695 -10.914  1.00 40.26           C  
ANISOU 4960  CG  PHE A 657     5574   4362   5359    316   -528    586       C  
ATOM   4961  CD1 PHE A 657      37.476 -36.656 -11.332  1.00 46.65           C  
ANISOU 4961  CD1 PHE A 657     6296   5278   6150    344   -552    538       C  
ATOM   4962  CD2 PHE A 657      37.241 -38.816 -10.357  1.00 45.12           C  
ANISOU 4962  CD2 PHE A 657     6270   4900   5972    391   -549    629       C  
ATOM   4963  CE1 PHE A 657      38.850 -36.741 -11.222  1.00 48.74           C  
ANISOU 4963  CE1 PHE A 657     6537   5580   6401    439   -595    525       C  
ATOM   4964  CE2 PHE A 657      38.623 -38.910 -10.242  1.00 53.47           C  
ANISOU 4964  CE2 PHE A 657     7309   5996   7012    501   -601    619       C  
ATOM   4965  CZ  PHE A 657      39.428 -37.868 -10.678  1.00 50.19           C  
ANISOU 4965  CZ  PHE A 657     6790   5696   6584    522   -624    562       C  
ATOM   4966  N   LYS A 658      32.186 -38.250 -11.512  1.00 26.46           N  
ANISOU 4966  N   LYS A 658     3861   2469   3725     -1   -384    576       N  
ATOM   4967  CA  LYS A 658      30.904 -37.563 -11.419  1.00 26.32           C  
ANISOU 4967  CA  LYS A 658     3795   2489   3715    -94   -347    567       C  
ATOM   4968  C   LYS A 658      31.011 -36.470 -10.343  1.00 23.81           C  
ANISOU 4968  C   LYS A 658     3455   2257   3335    -86   -339    612       C  
ATOM   4969  O   LYS A 658      31.545 -36.703  -9.264  1.00 24.74           O  
ANISOU 4969  O   LYS A 658     3631   2361   3409    -45   -339    674       O  
ATOM   4970  CB  LYS A 658      29.777 -38.555 -11.103  1.00 25.30           C  
ANISOU 4970  CB  LYS A 658     3719   2261   3635   -176   -295    586       C  
ATOM   4971  CG  LYS A 658      29.450 -39.497 -12.262  1.00 32.37           C  
ANISOU 4971  CG  LYS A 658     4621   3078   4599   -205   -300    523       C  
ATOM   4972  CD  LYS A 658      29.350 -40.983 -11.873  1.00 38.85           C  
ANISOU 4972  CD  LYS A 658     5549   3754   5459   -221   -267    558       C  
ATOM   4973  CE  LYS A 658      29.600 -41.871 -13.119  1.00 57.24           C  
ANISOU 4973  CE  LYS A 658     7893   6013   7843   -207   -294    486       C  
ATOM   4974  NZ  LYS A 658      29.276 -43.324 -12.961  1.00 56.55           N1+
ANISOU 4974  NZ  LYS A 658     7905   5769   7811   -243   -256    501       N1+
ATOM   4975  N   PRO A 659      30.546 -35.255 -10.654  1.00 23.62           N  
ANISOU 4975  N   PRO A 659     3351   2321   3301   -117   -337    577       N  
ATOM   4976  CA  PRO A 659      30.579 -34.237  -9.600  1.00 23.23           C  
ANISOU 4976  CA  PRO A 659     3287   2345   3196   -115   -325    614       C  
ATOM   4977  C   PRO A 659      29.681 -34.622  -8.424  1.00 25.65           C  
ANISOU 4977  C   PRO A 659     3643   2611   3493   -170   -268    672       C  
ATOM   4978  O   PRO A 659      28.640 -35.230  -8.629  1.00 29.11           O  
ANISOU 4978  O   PRO A 659     4087   2993   3981   -239   -229    664       O  
ATOM   4979  CB  PRO A 659      30.072 -32.963 -10.304  1.00 26.84           C  
ANISOU 4979  CB  PRO A 659     3656   2884   3657   -143   -326    561       C  
ATOM   4980  CG  PRO A 659      29.553 -33.393 -11.627  1.00 28.75           C  
ANISOU 4980  CG  PRO A 659     3873   3097   3956   -169   -337    504       C  
ATOM   4981  CD  PRO A 659      30.190 -34.701 -11.973  1.00 17.49           C  
ANISOU 4981  CD  PRO A 659     2504   1588   2555   -137   -354    505       C  
ATOM   4982  N   THR A 660      30.101 -34.306  -7.204  1.00 22.56           N  
ANISOU 4982  N   THR A 660     3288   2248   3035   -140   -263    726       N  
ATOM   4983  CA  THR A 660      29.279 -34.578  -6.030  1.00 19.90           C  
ANISOU 4983  CA  THR A 660     3005   1881   2675   -190   -201    784       C  
ATOM   4984  C   THR A 660      28.480 -33.320  -5.672  1.00 22.58           C  
ANISOU 4984  C   THR A 660     3279   2306   2996   -237   -168    767       C  
ATOM   4985  O   THR A 660      27.599 -33.354  -4.813  1.00 24.08           O  
ANISOU 4985  O   THR A 660     3491   2486   3172   -291   -104    800       O  
ATOM   4986  CB  THR A 660      30.124 -35.020  -4.801  1.00 29.61           C  
ANISOU 4986  CB  THR A 660     4329   3091   3829   -126   -212    859       C  
ATOM   4987  CG2 THR A 660      30.920 -36.267  -5.104  1.00 20.43           C  
ANISOU 4987  CG2 THR A 660     3237   1840   2685    -66   -246    880       C  
ATOM   4988  OG1 THR A 660      31.040 -33.985  -4.450  1.00 28.99           O  
ANISOU 4988  OG1 THR A 660     4215   3109   3689    -66   -260    847       O  
ATOM   4989  N   ARG A 661      28.809 -32.215  -6.337  1.00 17.77           N  
ANISOU 4989  N   ARG A 661     2592   1775   2385   -214   -205    713       N  
ATOM   4990  CA  ARG A 661      28.155 -30.932  -6.114  1.00 21.92           C  
ANISOU 4990  CA  ARG A 661     3055   2377   2896   -244   -180    690       C  
ATOM   4991  C   ARG A 661      28.049 -30.134  -7.416  1.00 22.37           C  
ANISOU 4991  C   ARG A 661     3031   2478   2992   -241   -210    622       C  
ATOM   4992  O   ARG A 661      28.913 -30.213  -8.301  1.00 16.20           O  
ANISOU 4992  O   ARG A 661     2240   1695   2220   -198   -258    595       O  
ATOM   4993  CB  ARG A 661      28.905 -30.104  -5.058  1.00 21.53           C  
ANISOU 4993  CB  ARG A 661     3024   2389   2766   -202   -192    714       C  
ATOM   4994  CG  ARG A 661      28.923 -30.733  -3.659  1.00 22.91           C  
ANISOU 4994  CG  ARG A 661     3286   2535   2882   -199   -161    785       C  
ATOM   4995  CD  ARG A 661      29.607 -29.829  -2.662  1.00 21.88           C  
ANISOU 4995  CD  ARG A 661     3167   2479   2669   -158   -179    795       C  
ATOM   4996  NE  ARG A 661      29.551 -30.371  -1.319  1.00 27.25           N  
ANISOU 4996  NE  ARG A 661     3938   3139   3279   -153   -149    863       N  
ATOM   4997  CZ  ARG A 661      30.422 -31.246  -0.832  1.00 27.01           C  
ANISOU 4997  CZ  ARG A 661     3986   3072   3205    -93   -186    912       C  
ATOM   4998  NH1 ARG A 661      31.427 -31.679  -1.580  1.00 29.36           N1+
ANISOU 4998  NH1 ARG A 661     4274   3352   3530    -35   -252    894       N1+
ATOM   4999  NH2 ARG A 661      30.279 -31.691   0.406  1.00 24.89           N  
ANISOU 4999  NH2 ARG A 661     3810   2784   2862    -87   -154    979       N  
ATOM   5000  N   ILE A 662      26.976 -29.361  -7.512  1.00 18.44           N  
ANISOU 5000  N   ILE A 662     2476   2017   2512   -284   -179    596       N  
ATOM   5001  CA  ILE A 662      26.712 -28.542  -8.668  1.00 17.36           C  
ANISOU 5001  CA  ILE A 662     2271   1921   2404   -278   -204    539       C  
ATOM   5002  C   ILE A 662      26.467 -27.117  -8.204  1.00 18.99           C  
ANISOU 5002  C   ILE A 662     2442   2195   2576   -272   -187    529       C  
ATOM   5003  O   ILE A 662      25.497 -26.853  -7.491  1.00 19.17           O  
ANISOU 5003  O   ILE A 662     2450   2234   2601   -309   -139    537       O  
ATOM   5004  CB  ILE A 662      25.465 -29.052  -9.424  1.00 20.48           C  
ANISOU 5004  CB  ILE A 662     2624   2291   2865   -330   -191    504       C  
ATOM   5005  CG1 ILE A 662      25.734 -30.432 -10.024  1.00 21.72           C  
ANISOU 5005  CG1 ILE A 662     2818   2374   3060   -337   -211    500       C  
ATOM   5006  CG2 ILE A 662      25.060 -28.075 -10.498  1.00 15.66           C  
ANISOU 5006  CG2 ILE A 662     1946   1733   2270   -314   -219    449       C  
ATOM   5007  CD1 ILE A 662      24.473 -31.155 -10.489  1.00 20.61           C  
ANISOU 5007  CD1 ILE A 662     2644   2198   2988   -405   -189    467       C  
ATOM   5008  N   ILE A 663      27.352 -26.203  -8.599  1.00 16.39           N  
ANISOU 5008  N   ILE A 663     2102   1904   2220   -228   -219    510       N  
ATOM   5009  CA  ILE A 663      27.198 -24.799  -8.248  1.00 15.39           C  
ANISOU 5009  CA  ILE A 663     1949   1831   2065   -220   -203    496       C  
ATOM   5010  C   ILE A 663      26.731 -24.002  -9.474  1.00 19.01           C  
ANISOU 5010  C   ILE A 663     2360   2310   2553   -209   -218    452       C  
ATOM   5011  O   ILE A 663      27.487 -23.832 -10.438  1.00 14.92           O  
ANISOU 5011  O   ILE A 663     1843   1791   2034   -179   -252    433       O  
ATOM   5012  CB  ILE A 663      28.522 -24.198  -7.716  1.00 17.62           C  
ANISOU 5012  CB  ILE A 663     2257   2142   2296   -185   -222    502       C  
ATOM   5013  CG1 ILE A 663      29.190 -25.149  -6.719  1.00 22.42           C  
ANISOU 5013  CG1 ILE A 663     2919   2730   2870   -176   -228    545       C  
ATOM   5014  CG2 ILE A 663      28.275 -22.820  -7.083  1.00 16.22           C  
ANISOU 5014  CG2 ILE A 663     2066   2010   2089   -187   -194    488       C  
ATOM   5015  CD1 ILE A 663      28.335 -25.471  -5.523  1.00 22.57           C  
ANISOU 5015  CD1 ILE A 663     2967   2741   2868   -209   -180    582       C  
ATOM   5016  N   PHE A 664      25.495 -23.508  -9.413  1.00 21.59           N  
ANISOU 5016  N   PHE A 664     2646   2656   2900   -229   -191    437       N  
ATOM   5017  CA  PHE A 664      24.797 -22.934 -10.562  1.00 17.68           C  
ANISOU 5017  CA  PHE A 664     2106   2178   2434   -213   -211    398       C  
ATOM   5018  C   PHE A 664      24.579 -21.418 -10.421  1.00 20.42           C  
ANISOU 5018  C   PHE A 664     2438   2561   2759   -185   -195    384       C  
ATOM   5019  O   PHE A 664      23.809 -20.965  -9.558  1.00 20.36           O  
ANISOU 5019  O   PHE A 664     2410   2574   2751   -199   -155    386       O  
ATOM   5020  CB  PHE A 664      23.445 -23.638 -10.686  1.00 19.31           C  
ANISOU 5020  CB  PHE A 664     2267   2379   2693   -252   -198    381       C  
ATOM   5021  CG  PHE A 664      22.678 -23.295 -11.933  1.00 21.86           C  
ANISOU 5021  CG  PHE A 664     2538   2722   3045   -231   -234    336       C  
ATOM   5022  CD1 PHE A 664      22.796 -24.080 -13.071  1.00 21.46           C  
ANISOU 5022  CD1 PHE A 664     2487   2651   3017   -228   -279    312       C  
ATOM   5023  CD2 PHE A 664      21.793 -22.220 -11.947  1.00 30.18           C  
ANISOU 5023  CD2 PHE A 664     3545   3817   4104   -209   -224    314       C  
ATOM   5024  CE1 PHE A 664      22.070 -23.769 -14.222  1.00 29.09           C  
ANISOU 5024  CE1 PHE A 664     3410   3644   4001   -203   -320    267       C  
ATOM   5025  CE2 PHE A 664      21.069 -21.900 -13.097  1.00 32.30           C  
ANISOU 5025  CE2 PHE A 664     3769   4110   4395   -177   -266    273       C  
ATOM   5026  CZ  PHE A 664      21.208 -22.675 -14.233  1.00 28.64           C  
ANISOU 5026  CZ  PHE A 664     3307   3631   3944   -175   -316    250       C  
ATOM   5027  N   TYR A 665      25.250 -20.646 -11.274  1.00 16.26           N  
ANISOU 5027  N   TYR A 665     1925   2038   2214   -146   -220    371       N  
ATOM   5028  CA  TYR A 665      25.111 -19.181 -11.314  1.00 17.03           C  
ANISOU 5028  CA  TYR A 665     2022   2155   2294   -116   -205    359       C  
ATOM   5029  C   TYR A 665      24.213 -18.786 -12.465  1.00 17.30           C  
ANISOU 5029  C   TYR A 665     2027   2197   2348    -83   -230    334       C  
ATOM   5030  O   TYR A 665      24.552 -18.998 -13.628  1.00 19.63           O  
ANISOU 5030  O   TYR A 665     2335   2484   2642    -61   -266    325       O  
ATOM   5031  CB  TYR A 665      26.468 -18.489 -11.498  1.00 15.28           C  
ANISOU 5031  CB  TYR A 665     1843   1926   2037    -99   -208    361       C  
ATOM   5032  CG  TYR A 665      27.321 -18.501 -10.265  1.00 16.90           C  
ANISOU 5032  CG  TYR A 665     2071   2138   2214   -121   -189    375       C  
ATOM   5033  CD1 TYR A 665      27.138 -17.561  -9.252  1.00 13.28           C  
ANISOU 5033  CD1 TYR A 665     1617   1694   1734   -126   -154    371       C  
ATOM   5034  CD2 TYR A 665      28.298 -19.465 -10.093  1.00 18.10           C  
ANISOU 5034  CD2 TYR A 665     2239   2281   2358   -130   -209    389       C  
ATOM   5035  CE1 TYR A 665      27.926 -17.582  -8.097  1.00 15.06           C  
ANISOU 5035  CE1 TYR A 665     1864   1933   1924   -143   -144    378       C  
ATOM   5036  CE2 TYR A 665      29.083 -19.496  -8.958  1.00 22.36           C  
ANISOU 5036  CE2 TYR A 665     2797   2833   2865   -140   -202    399       C  
ATOM   5037  CZ  TYR A 665      28.896 -18.555  -7.955  1.00 19.99           C  
ANISOU 5037  CZ  TYR A 665     2503   2554   2538   -149   -172    393       C  
ATOM   5038  OH  TYR A 665      29.693 -18.610  -6.818  1.00 17.13           O  
ANISOU 5038  OH  TYR A 665     2161   2213   2135   -156   -173    398       O  
ATOM   5039  N   ARG A 666      23.072 -18.211 -12.121  1.00 16.62           N  
ANISOU 5039  N   ARG A 666     1902   2134   2280    -73   -211    321       N  
ATOM   5040  CA  ARG A 666      22.033 -17.859 -13.067  1.00 18.56           C  
ANISOU 5040  CA  ARG A 666     2108   2398   2548    -33   -240    293       C  
ATOM   5041  C   ARG A 666      22.015 -16.351 -13.222  1.00 30.44           C  
ANISOU 5041  C   ARG A 666     3637   3903   4027     22   -229    292       C  
ATOM   5042  O   ARG A 666      21.965 -15.617 -12.236  1.00 31.76           O  
ANISOU 5042  O   ARG A 666     3811   4071   4186     19   -186    295       O  
ATOM   5043  CB  ARG A 666      20.681 -18.309 -12.522  1.00 20.15           C  
ANISOU 5043  CB  ARG A 666     2235   2627   2794    -59   -224    273       C  
ATOM   5044  CG  ARG A 666      19.478 -17.856 -13.342  1.00 15.48           C  
ANISOU 5044  CG  ARG A 666     1583   2068   2230    -11   -258    236       C  
ATOM   5045  CD  ARG A 666      19.488 -18.533 -14.693  1.00 25.81           C  
ANISOU 5045  CD  ARG A 666     2887   3377   3545      3   -323    216       C  
ATOM   5046  NE  ARG A 666      18.149 -18.734 -15.237  1.00 29.81           N  
ANISOU 5046  NE  ARG A 666     3308   3925   4094     18   -360    169       N  
ATOM   5047  CZ  ARG A 666      17.534 -17.868 -16.040  1.00 25.50           C  
ANISOU 5047  CZ  ARG A 666     2742   3408   3538     96   -403    146       C  
ATOM   5048  NH1 ARG A 666      18.129 -16.733 -16.372  1.00 23.31           N1+
ANISOU 5048  NH1 ARG A 666     2536   3112   3210    160   -404    173       N1+
ATOM   5049  NH2 ARG A 666      16.329 -18.138 -16.518  1.00 19.29           N  
ANISOU 5049  NH2 ARG A 666     1867   2669   2793    111   -445     96       N  
ATOM   5050  N   ASP A 667      22.059 -15.869 -14.452  1.00 33.65           N  
ANISOU 5050  N   ASP A 667     4066   4303   4418     74   -266    286       N  
ATOM   5051  CA  ASP A 667      21.857 -14.445 -14.644  1.00 36.25           C  
ANISOU 5051  CA  ASP A 667     4424   4623   4727    134   -254    287       C  
ATOM   5052  C   ASP A 667      20.491 -13.971 -14.146  1.00 38.58           C  
ANISOU 5052  C   ASP A 667     4658   4949   5053    163   -244    265       C  
ATOM   5053  O   ASP A 667      19.490 -14.682 -14.262  1.00 35.78           O  
ANISOU 5053  O   ASP A 667     4229   4630   4736    157   -269    240       O  
ATOM   5054  CB  ASP A 667      21.958 -14.058 -16.096  1.00 27.86           C  
ANISOU 5054  CB  ASP A 667     3400   3549   3636    194   -297    289       C  
ATOM   5055  CG  ASP A 667      21.733 -12.585 -16.286  1.00 38.08           C  
ANISOU 5055  CG  ASP A 667     4739   4822   4908    260   -281    297       C  
ATOM   5056  OD1 ASP A 667      22.593 -11.810 -15.798  1.00 40.85           O  
ANISOU 5056  OD1 ASP A 667     5147   5135   5240    244   -232    313       O  
ATOM   5057  OD2 ASP A 667      20.695 -12.205 -16.876  1.00 39.26           O1-
ANISOU 5057  OD2 ASP A 667     4864   4991   5062    328   -317    284       O1-
ATOM   5058  N   GLY A 668      20.461 -12.747 -13.628  1.00 41.74           N  
ANISOU 5058  N   GLY A 668     5087   5332   5440    195   -206    267       N  
ATOM   5059  CA  GLY A 668      19.243 -12.135 -13.133  1.00 41.40           C  
ANISOU 5059  CA  GLY A 668     4991   5314   5424    234   -190    243       C  
ATOM   5060  C   GLY A 668      18.038 -12.271 -14.037  1.00 42.51           C  
ANISOU 5060  C   GLY A 668     5066   5494   5593    294   -246    216       C  
ATOM   5061  O   GLY A 668      18.139 -12.286 -15.271  1.00 42.23           O  
ANISOU 5061  O   GLY A 668     5055   5453   5536    339   -302    221       O  
ATOM   5062  N   VAL A 669      16.883 -12.386 -13.401  1.00 42.25           N  
ANISOU 5062  N   VAL A 669     4944   5505   5604    294   -230    184       N  
ATOM   5063  CA  VAL A 669      15.625 -12.487 -14.109  1.00 49.50           C  
ANISOU 5063  CA  VAL A 669     5777   6474   6558    351   -283    145       C  
ATOM   5064  C   VAL A 669      14.704 -11.421 -13.524  1.00 54.23           C  
ANISOU 5064  C   VAL A 669     6337   7090   7177    415   -252    122       C  
ATOM   5065  O   VAL A 669      15.062 -10.775 -12.545  1.00 58.45           O  
ANISOU 5065  O   VAL A 669     6912   7596   7699    401   -186    134       O  
ATOM   5066  CB  VAL A 669      15.022 -13.899 -13.929  1.00 48.28           C  
ANISOU 5066  CB  VAL A 669     5527   6364   6455    274   -291    116       C  
ATOM   5067  CG1 VAL A 669      15.970 -14.960 -14.486  1.00 40.78           C  
ANISOU 5067  CG1 VAL A 669     4622   5387   5484    216   -320    137       C  
ATOM   5068  CG2 VAL A 669      14.717 -14.165 -12.460  1.00 46.75           C  
ANISOU 5068  CG2 VAL A 669     5290   6181   6289    204   -209    111       C  
ATOM   5069  N   PRO A 670      13.524 -11.212 -14.124  1.00 57.43           N  
ANISOU 5069  N   PRO A 670     6662   7544   7614    491   -302     82       N  
ATOM   5070  CA  PRO A 670      12.587 -10.300 -13.455  1.00 59.38           C  
ANISOU 5070  CA  PRO A 670     6856   7814   7890    552   -266     52       C  
ATOM   5071  C   PRO A 670      12.087 -10.852 -12.112  1.00 56.51           C  
ANISOU 5071  C   PRO A 670     6412   7487   7573    467   -188     26       C  
ATOM   5072  O   PRO A 670      11.585 -11.979 -12.050  1.00 48.55           O  
ANISOU 5072  O   PRO A 670     5315   6524   6607    399   -193      0       O  
ATOM   5073  CB  PRO A 670      11.426 -10.200 -14.449  1.00 61.51           C  
ANISOU 5073  CB  PRO A 670     7039   8143   8189    647   -349      9       C  
ATOM   5074  CG  PRO A 670      12.021 -10.567 -15.767  1.00 60.35           C  
ANISOU 5074  CG  PRO A 670     6954   7979   7998    665   -428     33       C  
ATOM   5075  CD  PRO A 670      13.058 -11.599 -15.467  1.00 56.28           C  
ANISOU 5075  CD  PRO A 670     6481   7434   7470    542   -396     61       C  
ATOM   5076  N   GLU A 671      12.221 -10.047 -11.060  1.00 62.69           N  
ANISOU 5076  N   GLU A 671     7230   8246   8343    471   -113     31       N  
ATOM   5077  CA  GLU A 671      11.835 -10.424  -9.696  1.00 66.30           C  
ANISOU 5077  CA  GLU A 671     7633   8733   8827    397    -27     12       C  
ATOM   5078  C   GLU A 671      10.499 -11.173  -9.599  1.00 56.68           C  
ANISOU 5078  C   GLU A 671     6262   7593   7679    374    -23    -42       C  
ATOM   5079  O   GLU A 671      10.404 -12.215  -8.945  1.00 50.94           O  
ANISOU 5079  O   GLU A 671     5496   6886   6974    271     24    -44       O  
ATOM   5080  CB  GLU A 671      11.797  -9.169  -8.814  1.00 77.03           C  
ANISOU 5080  CB  GLU A 671     9033  10068  10168    445     38      4       C  
ATOM   5081  CG  GLU A 671      11.426  -9.418  -7.360  1.00 87.21           C  
ANISOU 5081  CG  GLU A 671    10280  11387  11468    378    135    -16       C  
ATOM   5082  CD  GLU A 671      11.522  -8.161  -6.498  1.00 93.80           C  
ANISOU 5082  CD  GLU A 671    11170  12193  12275    424    198    -29       C  
ATOM   5083  OE1 GLU A 671      11.982  -7.111  -7.006  1.00 92.88           O  
ANISOU 5083  OE1 GLU A 671    11136  12021  12134    500    169    -17       O  
ATOM   5084  OE2 GLU A 671      11.135  -8.230  -5.310  1.00 96.37           O1-
ANISOU 5084  OE2 GLU A 671    11465  12548  12603    383    280    -51       O1-
ATOM   5085  N   GLY A 672       9.481 -10.649 -10.273  1.00 51.91           N  
ANISOU 5085  N   GLY A 672     5577   7033   7114    472    -72    -87       N  
ATOM   5086  CA  GLY A 672       8.144 -11.206 -10.192  1.00 52.87           C  
ANISOU 5086  CA  GLY A 672     5538   7239   7312    460    -69   -152       C  
ATOM   5087  C   GLY A 672       7.958 -12.574 -10.827  1.00 60.14           C  
ANISOU 5087  C   GLY A 672     6392   8191   8269    381   -117   -169       C  
ATOM   5088  O   GLY A 672       6.922 -13.218 -10.627  1.00 59.80           O  
ANISOU 5088  O   GLY A 672     6212   8213   8296    337    -98   -226       O  
ATOM   5089  N   GLN A 673       8.945 -13.029 -11.594  1.00 58.41           N  
ANISOU 5089  N   GLN A 673     6265   7924   8005    359   -174   -125       N  
ATOM   5090  CA  GLN A 673       8.817 -14.320 -12.267  1.00 56.42           C  
ANISOU 5090  CA  GLN A 673     5960   7693   7784    289   -223   -145       C  
ATOM   5091  C   GLN A 673       9.698 -15.424 -11.667  1.00 43.59           C  
ANISOU 5091  C   GLN A 673     4399   6019   6144    160   -169   -101       C  
ATOM   5092  O   GLN A 673       9.455 -16.606 -11.903  1.00 39.45           O  
ANISOU 5092  O   GLN A 673     3822   5507   5660     80   -181   -123       O  
ATOM   5093  CB  GLN A 673       9.059 -14.178 -13.779  1.00 64.04           C  
ANISOU 5093  CB  GLN A 673     6960   8655   8717    370   -341   -145       C  
ATOM   5094  CG  GLN A 673       8.025 -14.918 -14.632  1.00 74.57           C  
ANISOU 5094  CG  GLN A 673     8161  10063  10110    370   -418   -219       C  
ATOM   5095  CD  GLN A 673       8.160 -14.640 -16.123  1.00 80.60           C  
ANISOU 5095  CD  GLN A 673     8961  10834  10829    470   -539   -223       C  
ATOM   5096  NE2 GLN A 673       7.103 -14.934 -16.875  1.00 81.28           N  
ANISOU 5096  NE2 GLN A 673     8923  10999  10960    507   -619   -298       N  
ATOM   5097  OE1 GLN A 673       9.196 -14.163 -16.591  1.00 80.89           O  
ANISOU 5097  OE1 GLN A 673     9135  10809  10790    511   -558   -162       O  
ATOM   5098  N   LEU A 674      10.694 -15.046 -10.871  1.00 41.54           N  
ANISOU 5098  N   LEU A 674     4252   5704   5829    141   -112    -43       N  
ATOM   5099  CA  LEU A 674      11.649 -16.023 -10.340  1.00 48.45           C  
ANISOU 5099  CA  LEU A 674     5200   6531   6678     39    -73      4       C  
ATOM   5100  C   LEU A 674      11.116 -17.159  -9.432  1.00 53.03           C  
ANISOU 5100  C   LEU A 674     5720   7126   7305    -74      2     -7       C  
ATOM   5101  O   LEU A 674      11.812 -18.149  -9.234  1.00 55.88           O  
ANISOU 5101  O   LEU A 674     6137   7444   7651   -151     15     30       O  
ATOM   5102  CB  LEU A 674      12.859 -15.332  -9.701  1.00 46.66           C  
ANISOU 5102  CB  LEU A 674     5101   6250   6379     49    -38     61       C  
ATOM   5103  CG  LEU A 674      12.760 -14.691  -8.329  1.00 47.96           C  
ANISOU 5103  CG  LEU A 674     5280   6418   6526     40     53     66       C  
ATOM   5104  CD1 LEU A 674      13.013 -15.707  -7.254  1.00 49.01           C  
ANISOU 5104  CD1 LEU A 674     5430   6540   6650    -65    123     93       C  
ATOM   5105  CD2 LEU A 674      13.774 -13.579  -8.233  1.00 50.50           C  
ANISOU 5105  CD2 LEU A 674     5710   6694   6783     93     50     97       C  
ATOM   5106  N   PRO A 675       9.916 -17.015  -8.844  1.00 52.10           N  
ANISOU 5106  N   PRO A 675     5492   7063   7240    -84     57    -55       N  
ATOM   5107  CA  PRO A 675       9.431 -18.243  -8.214  1.00 47.45           C  
ANISOU 5107  CA  PRO A 675     4849   6480   6698   -202    125    -64       C  
ATOM   5108  C   PRO A 675       9.156 -19.303  -9.258  1.00 48.69           C  
ANISOU 5108  C   PRO A 675     4951   6641   6908   -244     58    -98       C  
ATOM   5109  O   PRO A 675       9.474 -20.473  -9.055  1.00 50.55           O  
ANISOU 5109  O   PRO A 675     5217   6835   7153   -340     85    -75       O  
ATOM   5110  CB  PRO A 675       8.123 -17.802  -7.564  1.00 46.40           C  
ANISOU 5110  CB  PRO A 675     4593   6416   6620   -197    193   -122       C  
ATOM   5111  CG  PRO A 675       8.372 -16.382  -7.205  1.00 52.32           C  
ANISOU 5111  CG  PRO A 675     5393   7167   7319    -97    202   -109       C  
ATOM   5112  CD  PRO A 675       9.195 -15.828  -8.343  1.00 56.03           C  
ANISOU 5112  CD  PRO A 675     5941   7603   7745    -11     95    -86       C  
ATOM   5113  N   GLN A 676       8.569 -18.890 -10.373  1.00 49.13           N  
ANISOU 5113  N   GLN A 676     4930   6744   6993   -167    -32   -153       N  
ATOM   5114  CA  GLN A 676       8.275 -19.812 -11.456  1.00 55.19           C  
ANISOU 5114  CA  GLN A 676     5642   7523   7805   -198   -109   -197       C  
ATOM   5115  C   GLN A 676       9.584 -20.305 -12.081  1.00 45.38           C  
ANISOU 5115  C   GLN A 676     4530   6210   6504   -204   -162   -143       C  
ATOM   5116  O   GLN A 676       9.729 -21.491 -12.380  1.00 38.88           O  
ANISOU 5116  O   GLN A 676     3709   5356   5706   -284   -172   -150       O  
ATOM   5117  CB  GLN A 676       7.384 -19.134 -12.498  1.00 64.75           C  
ANISOU 5117  CB  GLN A 676     6748   8809   9044    -95   -204   -268       C  
ATOM   5118  CG  GLN A 676       6.212 -19.982 -12.957  1.00 74.76           C  
ANISOU 5118  CG  GLN A 676     7860  10139  10405   -151   -231   -360       C  
ATOM   5119  CD  GLN A 676       4.965 -19.158 -13.220  1.00 85.21           C  
ANISOU 5119  CD  GLN A 676     9039  11561  11778    -61   -267   -438       C  
ATOM   5120  NE2 GLN A 676       4.638 -18.954 -14.497  1.00 88.24           N  
ANISOU 5120  NE2 GLN A 676     9377  11991  12160     26   -394   -487       N  
ATOM   5121  OE1 GLN A 676       4.300 -18.709 -12.285  1.00 90.12           O  
ANISOU 5121  OE1 GLN A 676     9590  12218  12434    -65   -184   -455       O  
ATOM   5122  N   ILE A 677      10.530 -19.383 -12.256  1.00 38.50           N  
ANISOU 5122  N   ILE A 677     3764   5307   5555   -123   -189    -92       N  
ATOM   5123  CA  ILE A 677      11.835 -19.702 -12.810  1.00 40.94           C  
ANISOU 5123  CA  ILE A 677     4194   5555   5807   -121   -230    -41       C  
ATOM   5124  C   ILE A 677      12.522 -20.744 -11.948  1.00 39.66           C  
ANISOU 5124  C   ILE A 677     4095   5336   5640   -224   -163      5       C  
ATOM   5125  O   ILE A 677      12.983 -21.772 -12.448  1.00 29.28           O  
ANISOU 5125  O   ILE A 677     2812   3984   4331   -271   -192      9       O  
ATOM   5126  CB  ILE A 677      12.744 -18.456 -12.876  1.00 43.58           C  
ANISOU 5126  CB  ILE A 677     4629   5864   6064    -33   -243      7       C  
ATOM   5127  CG1 ILE A 677      12.095 -17.346 -13.710  1.00 45.82           C  
ANISOU 5127  CG1 ILE A 677     4873   6193   6345     82   -306    -27       C  
ATOM   5128  CG2 ILE A 677      14.141 -18.824 -13.389  1.00 33.41           C  
ANISOU 5128  CG2 ILE A 677     3457   4517   4722    -40   -274     55       C  
ATOM   5129  CD1 ILE A 677      11.662 -17.785 -15.065  1.00 51.49           C  
ANISOU 5129  CD1 ILE A 677     5542   6942   7079    113   -403    -74       C  
ATOM   5130  N   LEU A 678      12.573 -20.472 -10.645  1.00 40.70           N  
ANISOU 5130  N   LEU A 678     4248   5460   5757   -253    -74     38       N  
ATOM   5131  CA  LEU A 678      13.242 -21.351  -9.701  1.00 34.85           C  
ANISOU 5131  CA  LEU A 678     3580   4665   4996   -337     -9     90       C  
ATOM   5132  C   LEU A 678      12.597 -22.719  -9.674  1.00 31.38           C  
ANISOU 5132  C   LEU A 678     3086   4213   4623   -436     18     65       C  
ATOM   5133  O   LEU A 678      13.286 -23.738  -9.683  1.00 34.90           O  
ANISOU 5133  O   LEU A 678     3600   4599   5061   -488     19     98       O  
ATOM   5134  CB  LEU A 678      13.203 -20.773  -8.287  1.00 37.65           C  
ANISOU 5134  CB  LEU A 678     3958   5027   5320   -347     83    120       C  
ATOM   5135  CG  LEU A 678      13.850 -21.737  -7.288  1.00 38.03           C  
ANISOU 5135  CG  LEU A 678     4087   5023   5338   -427    146    177       C  
ATOM   5136  CD1 LEU A 678      15.369 -21.735  -7.496  1.00 32.92           C  
ANISOU 5136  CD1 LEU A 678     3558   4326   4624   -395     98    230       C  
ATOM   5137  CD2 LEU A 678      13.459 -21.430  -5.846  1.00 39.64           C  
ANISOU 5137  CD2 LEU A 678     4295   5245   5520   -457    250    194       C  
ATOM   5138  N   HIS A 679      11.272 -22.742  -9.612  1.00 23.12           N  
ANISOU 5138  N   HIS A 679     1916   3221   3647   -463     45      4       N  
ATOM   5139  CA  HIS A 679      10.568 -24.009  -9.541  1.00 28.29           C  
ANISOU 5139  CA  HIS A 679     2510   3864   4376   -570     83    -28       C  
ATOM   5140  C   HIS A 679      10.924 -24.884 -10.750  1.00 35.99           C  
ANISOU 5140  C   HIS A 679     3500   4804   5370   -584     -3    -51       C  
ATOM   5141  O   HIS A 679      11.237 -26.067 -10.593  1.00 37.69           O  
ANISOU 5141  O   HIS A 679     3763   4954   5603   -666     26    -31       O  
ATOM   5142  CB  HIS A 679       9.053 -23.801  -9.453  1.00 28.94           C  
ANISOU 5142  CB  HIS A 679     2433   4023   4539   -591    115   -108       C  
ATOM   5143  CG  HIS A 679       8.273 -25.081  -9.513  1.00 39.16           C  
ANISOU 5143  CG  HIS A 679     3651   5307   5921   -710    152   -156       C  
ATOM   5144  CD2 HIS A 679       7.813 -25.794 -10.571  1.00 45.51           C  
ANISOU 5144  CD2 HIS A 679     4381   6120   6789   -742     83   -226       C  
ATOM   5145  ND1 HIS A 679       7.923 -25.790  -8.387  1.00 41.44           N  
ANISOU 5145  ND1 HIS A 679     3943   5566   6237   -820    276   -133       N  
ATOM   5146  CE1 HIS A 679       7.264 -26.882  -8.745  1.00 44.17           C  
ANISOU 5146  CE1 HIS A 679     4218   5897   6668   -919    288   -187       C  
ATOM   5147  NE2 HIS A 679       7.181 -26.905 -10.062  1.00 47.77           N  
ANISOU 5147  NE2 HIS A 679     4622   6379   7150   -875    169   -249       N  
ATOM   5148  N   TYR A 680      10.895 -24.293 -11.946  1.00 27.55           N  
ANISOU 5148  N   TYR A 680     2400   3775   4293   -498   -106    -92       N  
ATOM   5149  CA  TYR A 680      11.209 -25.026 -13.169  1.00 31.57           C  
ANISOU 5149  CA  TYR A 680     2924   4262   4811   -499   -193   -122       C  
ATOM   5150  C   TYR A 680      12.676 -25.448 -13.227  1.00 26.10           C  
ANISOU 5150  C   TYR A 680     2375   3488   4054   -495   -203    -51       C  
ATOM   5151  O   TYR A 680      12.987 -26.603 -13.537  1.00 22.53           O  
ANISOU 5151  O   TYR A 680     1956   2980   3623   -555   -211    -55       O  
ATOM   5152  CB  TYR A 680      10.883 -24.173 -14.405  1.00 40.21           C  
ANISOU 5152  CB  TYR A 680     3966   5421   5890   -394   -300   -173       C  
ATOM   5153  CG  TYR A 680      11.086 -24.875 -15.742  1.00 49.32           C  
ANISOU 5153  CG  TYR A 680     5128   6565   7046   -389   -395   -217       C  
ATOM   5154  CD1 TYR A 680      10.010 -25.142 -16.570  1.00 49.18           C  
ANISOU 5154  CD1 TYR A 680     4990   6609   7087   -393   -459   -312       C  
ATOM   5155  CD2 TYR A 680      12.361 -25.261 -16.183  1.00 50.61           C  
ANISOU 5155  CD2 TYR A 680     5415   6663   7153   -378   -421   -169       C  
ATOM   5156  CE1 TYR A 680      10.192 -25.769 -17.779  1.00 51.37           C  
ANISOU 5156  CE1 TYR A 680     5279   6880   7358   -388   -547   -357       C  
ATOM   5157  CE2 TYR A 680      12.545 -25.906 -17.379  1.00 43.45           C  
ANISOU 5157  CE2 TYR A 680     4519   5746   6243   -373   -500   -213       C  
ATOM   5158  CZ  TYR A 680      11.455 -26.159 -18.174  1.00 53.55           C  
ANISOU 5158  CZ  TYR A 680     5686   7086   7575   -379   -564   -307       C  
ATOM   5159  OH  TYR A 680      11.627 -26.789 -19.384  1.00 62.16           O  
ANISOU 5159  OH  TYR A 680     6790   8171   8655   -372   -647   -358       O  
ATOM   5160  N   GLU A 681      13.575 -24.502 -12.977  1.00 19.94           N  
ANISOU 5160  N   GLU A 681     1676   2702   3199   -422   -204      7       N  
ATOM   5161  CA  GLU A 681      14.981 -24.734 -13.271  1.00 22.74           C  
ANISOU 5161  CA  GLU A 681     2149   2998   3493   -399   -232     58       C  
ATOM   5162  C   GLU A 681      15.662 -25.623 -12.229  1.00 24.33           C  
ANISOU 5162  C   GLU A 681     2428   3131   3685   -468   -163    118       C  
ATOM   5163  O   GLU A 681      16.472 -26.483 -12.574  1.00 26.71           O  
ANISOU 5163  O   GLU A 681     2796   3375   3977   -485   -184    136       O  
ATOM   5164  CB  GLU A 681      15.719 -23.410 -13.502  1.00 18.24           C  
ANISOU 5164  CB  GLU A 681     1633   2447   2853   -302   -262     89       C  
ATOM   5165  CG  GLU A 681      15.183 -22.662 -14.734  1.00 23.49           C  
ANISOU 5165  CG  GLU A 681     2247   3165   3515   -222   -342     39       C  
ATOM   5166  CD  GLU A 681      16.035 -21.473 -15.161  1.00 26.16           C  
ANISOU 5166  CD  GLU A 681     2659   3501   3781   -131   -371     73       C  
ATOM   5167  OE1 GLU A 681      16.979 -21.095 -14.421  1.00 23.17           O  
ANISOU 5167  OE1 GLU A 681     2355   3088   3359   -131   -327    128       O  
ATOM   5168  OE2 GLU A 681      15.752 -20.915 -16.253  1.00 24.16           O1-
ANISOU 5168  OE2 GLU A 681     2390   3279   3511    -59   -439     44       O1-
ATOM   5169  N   LEU A 682      15.309 -25.437 -10.963  1.00 24.62           N  
ANISOU 5169  N   LEU A 682     2458   3174   3722   -504    -80    146       N  
ATOM   5170  CA  LEU A 682      15.829 -26.298  -9.914  1.00 25.89           C  
ANISOU 5170  CA  LEU A 682     2697   3273   3868   -566    -12    206       C  
ATOM   5171  C   LEU A 682      15.369 -27.718 -10.191  1.00 27.60           C  
ANISOU 5171  C   LEU A 682     2897   3440   4151   -652      1    181       C  
ATOM   5172  O   LEU A 682      16.164 -28.655 -10.107  1.00 20.53           O  
ANISOU 5172  O   LEU A 682     2087   2471   3243   -676      3    220       O  
ATOM   5173  CB  LEU A 682      15.344 -25.853  -8.539  1.00 27.05           C  
ANISOU 5173  CB  LEU A 682     2834   3442   4000   -592     80    232       C  
ATOM   5174  CG  LEU A 682      15.863 -26.675  -7.356  1.00 32.00           C  
ANISOU 5174  CG  LEU A 682     3556   4010   4595   -648    153    302       C  
ATOM   5175  CD1 LEU A 682      17.373 -26.518  -7.198  1.00 28.78           C  
ANISOU 5175  CD1 LEU A 682     3259   3569   4107   -590    115    360       C  
ATOM   5176  CD2 LEU A 682      15.150 -26.278  -6.067  1.00 30.93           C  
ANISOU 5176  CD2 LEU A 682     3399   3905   4447   -681    252    316       C  
ATOM   5177  N   LEU A 683      14.096 -27.878 -10.543  1.00 20.87           N  
ANISOU 5177  N   LEU A 683     1930   2625   3373   -697      7    111       N  
ATOM   5178  CA  LEU A 683      13.601 -29.208 -10.876  1.00 21.74           C  
ANISOU 5178  CA  LEU A 683     2016   2686   3556   -788     19     74       C  
ATOM   5179  C   LEU A 683      14.332 -29.816 -12.084  1.00 24.15           C  
ANISOU 5179  C   LEU A 683     2368   2951   3858   -762    -70     54       C  
ATOM   5180  O   LEU A 683      14.652 -31.005 -12.087  1.00 26.13           O  
ANISOU 5180  O   LEU A 683     2677   3120   4133   -821    -52     66       O  
ATOM   5181  CB  LEU A 683      12.092 -29.199 -11.106  1.00 22.82           C  
ANISOU 5181  CB  LEU A 683     2006   2886   3780   -841     33    -13       C  
ATOM   5182  CG  LEU A 683      11.222 -29.114  -9.856  1.00 43.87           C  
ANISOU 5182  CG  LEU A 683     4622   5572   6475   -908    149     -2       C  
ATOM   5183  CD1 LEU A 683       9.744 -28.976 -10.224  1.00 24.72           C  
ANISOU 5183  CD1 LEU A 683     2027   3225   4140   -945    151   -103       C  
ATOM   5184  CD2 LEU A 683      11.463 -30.330  -8.967  1.00 43.12           C  
ANISOU 5184  CD2 LEU A 683     4615   5379   6389  -1009    244     55       C  
ATOM   5185  N   ALA A 684      14.610 -28.992 -13.095  1.00 21.36           N  
ANISOU 5185  N   ALA A 684     1996   2648   3470   -672   -159     26       N  
ATOM   5186  CA  ALA A 684      15.278 -29.474 -14.297  1.00 22.78           C  
ANISOU 5186  CA  ALA A 684     2218   2799   3638   -641   -240      1       C  
ATOM   5187  C   ALA A 684      16.686 -29.974 -13.982  1.00 19.81           C  
ANISOU 5187  C   ALA A 684     1972   2345   3211   -626   -228     74       C  
ATOM   5188  O   ALA A 684      17.092 -31.036 -14.446  1.00 30.16           O  
ANISOU 5188  O   ALA A 684     3329   3591   4541   -654   -245     63       O  
ATOM   5189  CB  ALA A 684      15.314 -28.393 -15.374  1.00 20.04           C  
ANISOU 5189  CB  ALA A 684     1839   2524   3250   -542   -328    -33       C  
ATOM   5190  N   ILE A 685      17.422 -29.205 -13.190  1.00 22.98           N  
ANISOU 5190  N   ILE A 685     2428   2754   3548   -580   -200    142       N  
ATOM   5191  CA  ILE A 685      18.769 -29.597 -12.783  1.00 18.53           C  
ANISOU 5191  CA  ILE A 685     1976   2129   2935   -558   -192    208       C  
ATOM   5192  C   ILE A 685      18.743 -30.916 -12.019  1.00 22.01           C  
ANISOU 5192  C   ILE A 685     2468   2486   3409   -636   -131    240       C  
ATOM   5193  O   ILE A 685      19.549 -31.812 -12.297  1.00 20.06           O  
ANISOU 5193  O   ILE A 685     2294   2170   3159   -632   -150    256       O  
ATOM   5194  CB  ILE A 685      19.422 -28.519 -11.912  1.00 27.47           C  
ANISOU 5194  CB  ILE A 685     3146   3293   3999   -506   -168    266       C  
ATOM   5195  CG1 ILE A 685      19.539 -27.215 -12.697  1.00 17.23           C  
ANISOU 5195  CG1 ILE A 685     1816   2061   2668   -429   -222    239       C  
ATOM   5196  CG2 ILE A 685      20.788 -28.973 -11.421  1.00 17.42           C  
ANISOU 5196  CG2 ILE A 685     1976   1966   2678   -484   -164    327       C  
ATOM   5197  CD1 ILE A 685      19.913 -26.036 -11.838  1.00 18.34           C  
ANISOU 5197  CD1 ILE A 685     1976   2236   2755   -390   -192    279       C  
ATOM   5198  N   ARG A 686      17.802 -31.033 -11.077  1.00 19.89           N  
ANISOU 5198  N   ARG A 686     2164   2221   3172   -704    -55    249       N  
ATOM   5199  CA  ARG A 686      17.585 -32.267 -10.334  1.00 27.74           C  
ANISOU 5199  CA  ARG A 686     3208   3131   4202   -789     17    280       C  
ATOM   5200  C   ARG A 686      17.259 -33.409 -11.287  1.00 26.10           C  
ANISOU 5200  C   ARG A 686     2986   2866   4066   -843    -10    221       C  
ATOM   5201  O   ARG A 686      17.801 -34.516 -11.171  1.00 29.63           O  
ANISOU 5201  O   ARG A 686     3520   3215   4521   -868      6    251       O  
ATOM   5202  CB  ARG A 686      16.408 -32.096  -9.364  1.00 33.71           C  
ANISOU 5202  CB  ARG A 686     3904   3915   4988   -861    108    280       C  
ATOM   5203  CG  ARG A 686      16.753 -32.105  -7.892  1.00 41.18           C  
ANISOU 5203  CG  ARG A 686     4935   4835   5877   -872    191    367       C  
ATOM   5204  CD  ARG A 686      17.186 -33.472  -7.359  1.00 40.02           C  
ANISOU 5204  CD  ARG A 686     4901   4573   5732   -922    239    426       C  
ATOM   5205  NE  ARG A 686      18.606 -33.503  -6.994  1.00 40.10           N  
ANISOU 5205  NE  ARG A 686     5028   4549   5659   -842    204    499       N  
ATOM   5206  CZ  ARG A 686      19.197 -32.718  -6.089  1.00 38.04           C  
ANISOU 5206  CZ  ARG A 686     4810   4330   5314   -787    214    554       C  
ATOM   5207  NH1 ARG A 686      18.518 -31.790  -5.411  1.00 43.47           N1+
ANISOU 5207  NH1 ARG A 686     5444   5090   5982   -798    263    549       N1+
ATOM   5208  NH2 ARG A 686      20.493 -32.857  -5.869  1.00 34.45           N  
ANISOU 5208  NH2 ARG A 686     4449   3846   4793   -716    173    606       N  
ATOM   5209  N   ASP A 687      16.332 -33.137 -12.202  1.00 25.14           N  
ANISOU 5209  N   ASP A 687     2754   2803   3997   -858    -51    133       N  
ATOM   5210  CA  ASP A 687      15.896 -34.125 -13.189  1.00 27.79           C  
ANISOU 5210  CA  ASP A 687     3059   3099   4403   -912    -85     57       C  
ATOM   5211  C   ASP A 687      17.076 -34.630 -14.028  1.00 25.77           C  
ANISOU 5211  C   ASP A 687     2890   2788   4113   -855   -152     61       C  
ATOM   5212  O   ASP A 687      17.184 -35.820 -14.311  1.00 28.61           O  
ANISOU 5212  O   ASP A 687     3295   3059   4515   -905   -146     43       O  
ATOM   5213  CB  ASP A 687      14.795 -33.534 -14.084  1.00 26.41           C  
ANISOU 5213  CB  ASP A 687     2743   3020   4270   -913   -140    -43       C  
ATOM   5214  CG  ASP A 687      14.349 -34.492 -15.181  1.00 32.54           C  
ANISOU 5214  CG  ASP A 687     3483   3769   5114   -965   -189   -136       C  
ATOM   5215  OD1 ASP A 687      13.639 -35.484 -14.876  1.00 36.08           O  
ANISOU 5215  OD1 ASP A 687     3907   4160   5642  -1077   -130   -167       O  
ATOM   5216  OD2 ASP A 687      14.700 -34.254 -16.355  1.00 38.10           O1-
ANISOU 5216  OD2 ASP A 687     4182   4505   5789   -897   -284   -181       O1-
ATOM   5217  N   ALA A 688      17.971 -33.723 -14.404  1.00 20.88           N  
ANISOU 5217  N   ALA A 688     2296   2217   3420   -752   -209     85       N  
ATOM   5218  CA  ALA A 688      19.150 -34.093 -15.192  1.00 20.39           C  
ANISOU 5218  CA  ALA A 688     2311   2115   3322   -691   -265     88       C  
ATOM   5219  C   ALA A 688      20.004 -35.138 -14.469  1.00 26.77           C  
ANISOU 5219  C   ALA A 688     3231   2815   4126   -705   -221    154       C  
ATOM   5220  O   ALA A 688      20.508 -36.060 -15.107  1.00 22.35           O  
ANISOU 5220  O   ALA A 688     2722   2187   3583   -702   -247    131       O  
ATOM   5221  CB  ALA A 688      19.977 -32.867 -15.516  1.00 19.30           C  
ANISOU 5221  CB  ALA A 688     2182   2047   3106   -588   -312    111       C  
ATOM   5222  N   CYS A 689      20.153 -34.979 -13.147  1.00 20.53           N  
ANISOU 5222  N   CYS A 689     2481   2011   3309   -715   -156    233       N  
ATOM   5223  CA  CYS A 689      20.890 -35.924 -12.303  1.00 23.13           C  
ANISOU 5223  CA  CYS A 689     2922   2241   3624   -721   -112    306       C  
ATOM   5224  C   CYS A 689      20.149 -37.241 -12.190  1.00 26.11           C  
ANISOU 5224  C   CYS A 689     3322   2520   4080   -822    -59    288       C  
ATOM   5225  O   CYS A 689      20.716 -38.313 -12.391  1.00 25.20           O  
ANISOU 5225  O   CYS A 689     3288   2305   3981   -821    -62    297       O  
ATOM   5226  CB  CYS A 689      21.091 -35.343 -10.887  1.00 20.94           C  
ANISOU 5226  CB  CYS A 689     2680   1987   3289   -707    -57    390       C  
ATOM   5227  SG  CYS A 689      22.004 -33.786 -10.897  1.00 27.28           S  
ANISOU 5227  SG  CYS A 689     3464   2895   4006   -600   -110    408       S  
ATOM   5228  N   ILE A 690      18.867 -37.142 -11.868  1.00 29.89           N  
ANISOU 5228  N   ILE A 690     3723   3025   4610   -909     -6    258       N  
ATOM   5229  CA  ILE A 690      18.011 -38.309 -11.702  1.00 29.68           C  
ANISOU 5229  CA  ILE A 690     3701   2909   4666  -1025     60    234       C  
ATOM   5230  C   ILE A 690      17.931 -39.158 -12.970  1.00 31.47           C  
ANISOU 5230  C   ILE A 690     3917   3086   4955  -1050      5    146       C  
ATOM   5231  O   ILE A 690      17.947 -40.378 -12.908  1.00 34.93           O  
ANISOU 5231  O   ILE A 690     4425   3404   5441  -1109     43    148       O  
ATOM   5232  CB  ILE A 690      16.612 -37.855 -11.236  1.00 34.53           C  
ANISOU 5232  CB  ILE A 690     4205   3588   5327  -1111    122    201       C  
ATOM   5233  CG1 ILE A 690      16.669 -37.467  -9.751  1.00 32.12           C  
ANISOU 5233  CG1 ILE A 690     3949   3287   4967  -1113    208    297       C  
ATOM   5234  CG2 ILE A 690      15.553 -38.912 -11.495  1.00 29.55           C  
ANISOU 5234  CG2 ILE A 690     3531   2892   4803  -1241    170    132       C  
ATOM   5235  CD1 ILE A 690      15.355 -36.938  -9.214  1.00 32.93           C  
ANISOU 5235  CD1 ILE A 690     3943   3461   5109  -1188    279    267       C  
ATOM   5236  N   LYS A 691      17.882 -38.502 -14.124  1.00 34.27           N  
ANISOU 5236  N   LYS A 691     4191   3528   5303  -1000    -84     70       N  
ATOM   5237  CA  LYS A 691      17.762 -39.205 -15.395  1.00 37.89           C  
ANISOU 5237  CA  LYS A 691     4632   3956   5809  -1018   -144    -25       C  
ATOM   5238  C   LYS A 691      19.108 -39.721 -15.917  1.00 36.42           C  
ANISOU 5238  C   LYS A 691     4554   3703   5582   -938   -189     -4       C  
ATOM   5239  O   LYS A 691      19.161 -40.436 -16.918  1.00 35.12           O  
ANISOU 5239  O   LYS A 691     4397   3496   5450   -948   -232    -77       O  
ATOM   5240  CB  LYS A 691      17.102 -38.300 -16.443  1.00 44.30           C  
ANISOU 5240  CB  LYS A 691     5317   4893   6621   -992   -223   -117       C  
ATOM   5241  CG  LYS A 691      15.680 -37.842 -16.098  1.00 46.72           C  
ANISOU 5241  CG  LYS A 691     5496   5273   6981  -1067   -190   -160       C  
ATOM   5242  CD  LYS A 691      14.640 -38.888 -16.466  1.00 53.64           C  
ANISOU 5242  CD  LYS A 691     6314   6102   7963  -1190   -170   -255       C  
ATOM   5243  CE  LYS A 691      13.222 -38.310 -16.410  1.00 52.47           C  
ANISOU 5243  CE  LYS A 691     6008   6057   7871  -1248   -161   -325       C  
ATOM   5244  NZ  LYS A 691      12.709 -38.251 -15.019  1.00 38.26           N1+
ANISOU 5244  NZ  LYS A 691     4201   4242   6095  -1318    -43   -260       N1+
ATOM   5245  N   LEU A 692      20.189 -39.362 -15.237  1.00 34.13           N  
ANISOU 5245  N   LEU A 692     4341   3408   5220   -857   -180     90       N  
ATOM   5246  CA  LEU A 692      21.523 -39.804 -15.627  1.00 29.36           C  
ANISOU 5246  CA  LEU A 692     3830   2750   4577   -773   -219    113       C  
ATOM   5247  C   LEU A 692      21.834 -41.206 -15.104  1.00 30.05           C  
ANISOU 5247  C   LEU A 692     4030   2687   4702   -808   -167    152       C  
ATOM   5248  O   LEU A 692      22.349 -42.042 -15.837  1.00 34.26           O  
ANISOU 5248  O   LEU A 692     4615   3146   5256   -787   -196    114       O  
ATOM   5249  CB  LEU A 692      22.565 -38.817 -15.119  1.00 32.66           C  
ANISOU 5249  CB  LEU A 692     4272   3232   4907   -672   -235    188       C  
ATOM   5250  CG  LEU A 692      23.992 -38.935 -15.646  1.00 33.82           C  
ANISOU 5250  CG  LEU A 692     4481   3363   5007   -570   -285    198       C  
ATOM   5251  CD1 LEU A 692      24.048 -38.470 -17.078  1.00 31.33           C  
ANISOU 5251  CD1 LEU A 692     4109   3115   4681   -533   -354    114       C  
ATOM   5252  CD2 LEU A 692      24.928 -38.101 -14.789  1.00 35.66           C  
ANISOU 5252  CD2 LEU A 692     4738   3645   5165   -494   -282    280       C  
ATOM   5253  N   GLU A 693      21.472 -41.476 -13.854  1.00 35.10           N  
ANISOU 5253  N   GLU A 693     4710   3275   5349   -862    -86    225       N  
ATOM   5254  CA  GLU A 693      21.884 -42.700 -13.178  1.00 34.54           C  
ANISOU 5254  CA  GLU A 693     4769   3058   5296   -878    -31    288       C  
ATOM   5255  C   GLU A 693      21.079 -42.865 -11.901  1.00 29.72           C  
ANISOU 5255  C   GLU A 693     4181   2412   4701   -966     70    353       C  
ATOM   5256  O   GLU A 693      20.799 -41.881 -11.216  1.00 33.87           O  
ANISOU 5256  O   GLU A 693     4655   3031   5181   -961     90    389       O  
ATOM   5257  CB  GLU A 693      23.339 -42.548 -12.757  1.00 46.15           C  
ANISOU 5257  CB  GLU A 693     6327   4524   6686   -751    -62    369       C  
ATOM   5258  CG  GLU A 693      24.310 -43.551 -13.308  1.00 56.59           C  
ANISOU 5258  CG  GLU A 693     7740   5744   8018   -689    -95    360       C  
ATOM   5259  CD  GLU A 693      25.703 -43.320 -12.747  1.00 63.33           C  
ANISOU 5259  CD  GLU A 693     8662   6609   8792   -562   -125    440       C  
ATOM   5260  OE1 GLU A 693      26.699 -43.586 -13.453  1.00 63.97           O  
ANISOU 5260  OE1 GLU A 693     8768   6675   8862   -476   -180    415       O  
ATOM   5261  OE2 GLU A 693      25.795 -42.858 -11.591  1.00 68.74           O1-
ANISOU 5261  OE2 GLU A 693     9371   7324   9424   -548    -93    524       O1-
ATOM   5262  N   LYS A 694      20.731 -44.097 -11.553  1.00 27.35           N  
ANISOU 5262  N   LYS A 694     3963   1969   4458  -1046    140    369       N  
ATOM   5263  CA  LYS A 694      20.151 -44.348 -10.236  1.00 35.70           C  
ANISOU 5263  CA  LYS A 694     5073   2976   5515  -1121    250    450       C  
ATOM   5264  C   LYS A 694      21.082 -43.861  -9.117  1.00 34.40           C  
ANISOU 5264  C   LYS A 694     4992   2835   5241  -1020    254    570       C  
ATOM   5265  O   LYS A 694      22.312 -43.972  -9.225  1.00 29.07           O  
ANISOU 5265  O   LYS A 694     4390   2141   4513   -905    193    607       O  
ATOM   5266  CB  LYS A 694      19.883 -45.832 -10.032  1.00 36.91           C  
ANISOU 5266  CB  LYS A 694     5338   2950   5737  -1207    326    465       C  
ATOM   5267  CG  LYS A 694      18.682 -46.364 -10.773  1.00 45.88           C  
ANISOU 5267  CG  LYS A 694     6389   4054   6989  -1347    355    352       C  
ATOM   5268  CD  LYS A 694      18.508 -47.861 -10.528  1.00 47.12           C  
ANISOU 5268  CD  LYS A 694     6674   4015   7216  -1434    439    371       C  
ATOM   5269  CE  LYS A 694      17.416 -48.143  -9.522  1.00 54.17           C  
ANISOU 5269  CE  LYS A 694     7559   4890   8132  -1553    554    409       C  
ATOM   5270  NZ  LYS A 694      17.051 -49.590  -9.543  1.00 61.55           N1+
ANISOU 5270  NZ  LYS A 694     8566   5696   9124  -1620    592    398       N1+
ATOM   5271  N   ASP A 695      20.489 -43.308  -8.063  1.00 36.04           N  
ANISOU 5271  N   ASP A 695     5184   3093   5416  -1063    325    623       N  
ATOM   5272  CA  ASP A 695      21.221 -42.989  -6.840  1.00 42.57           C  
ANISOU 5272  CA  ASP A 695     6105   3930   6140   -987    344    737       C  
ATOM   5273  C   ASP A 695      22.341 -41.975  -7.050  1.00 38.47           C  
ANISOU 5273  C   ASP A 695     5556   3522   5540   -850    242    743       C  
ATOM   5274  O   ASP A 695      23.379 -42.031  -6.397  1.00 43.44           O  
ANISOU 5274  O   ASP A 695     6280   4134   6090   -756    220    821       O  
ATOM   5275  CB  ASP A 695      21.782 -44.270  -6.225  1.00 47.00           C  
ANISOU 5275  CB  ASP A 695     6841   4329   6688   -971    388    825       C  
ATOM   5276  CG  ASP A 695      20.701 -45.291  -5.937  1.00 48.67           C  
ANISOU 5276  CG  ASP A 695     7097   4416   6979  -1116    504    827       C  
ATOM   5277  OD1 ASP A 695      19.622 -44.882  -5.453  1.00 47.54           O  
ANISOU 5277  OD1 ASP A 695     6885   4324   6856  -1216    584    817       O  
ATOM   5278  OD2 ASP A 695      20.931 -46.494  -6.204  1.00 45.67           O1-
ANISOU 5278  OD2 ASP A 695     6820   3887   6646  -1130    520    834       O1-
ATOM   5279  N   TYR A 696      22.135 -41.070  -7.993  1.00 28.49           N  
ANISOU 5279  N   TYR A 696     4162   2369   4296   -840    180    657       N  
ATOM   5280  CA  TYR A 696      23.066 -39.981  -8.206  1.00 27.40           C  
ANISOU 5280  CA  TYR A 696     3984   2341   4087   -729     98    655       C  
ATOM   5281  C   TYR A 696      22.385 -38.689  -7.770  1.00 30.01           C  
ANISOU 5281  C   TYR A 696     4219   2794   4389   -751    118    646       C  
ATOM   5282  O   TYR A 696      21.540 -38.144  -8.484  1.00 29.59           O  
ANISOU 5282  O   TYR A 696     4051   2807   4384   -796    107    569       O  
ATOM   5283  CB  TYR A 696      23.521 -39.911  -9.667  1.00 23.10           C  
ANISOU 5283  CB  TYR A 696     3384   1820   3573   -684     10    571       C  
ATOM   5284  CG  TYR A 696      24.427 -38.735  -9.944  1.00 27.57           C  
ANISOU 5284  CG  TYR A 696     3904   2498   4072   -583    -63    565       C  
ATOM   5285  CD1 TYR A 696      24.063 -37.746 -10.849  1.00 21.04           C  
ANISOU 5285  CD1 TYR A 696     2966   1772   3255   -581   -105    493       C  
ATOM   5286  CD2 TYR A 696      25.639 -38.599  -9.278  1.00 30.05           C  
ANISOU 5286  CD2 TYR A 696     4287   2816   4313   -490    -87    632       C  
ATOM   5287  CE1 TYR A 696      24.888 -36.669 -11.094  1.00 23.53           C  
ANISOU 5287  CE1 TYR A 696     3250   2179   3513   -497   -160    490       C  
ATOM   5288  CE2 TYR A 696      26.477 -37.518  -9.517  1.00 20.48           C  
ANISOU 5288  CE2 TYR A 696     3028   1705   3047   -410   -145    620       C  
ATOM   5289  CZ  TYR A 696      26.097 -36.557 -10.412  1.00 24.15           C  
ANISOU 5289  CZ  TYR A 696     3392   2258   3526   -418   -176    552       C  
ATOM   5290  OH  TYR A 696      26.929 -35.488 -10.638  1.00 21.82           O  
ANISOU 5290  OH  TYR A 696     3060   2051   3180   -346   -223    543       O  
ATOM   5291  N   GLN A 697      22.746 -38.217  -6.580  1.00 35.42           N  
ANISOU 5291  N   GLN A 697     4954   3510   4994   -715    146    723       N  
ATOM   5292  CA  GLN A 697      22.109 -37.043  -6.003  1.00 35.73           C  
ANISOU 5292  CA  GLN A 697     4919   3655   5002   -735    178    720       C  
ATOM   5293  C   GLN A 697      23.112 -35.996  -5.550  1.00 26.46           C  
ANISOU 5293  C   GLN A 697     3753   2565   3735   -636    127    751       C  
ATOM   5294  O   GLN A 697      23.299 -35.782  -4.361  1.00 27.24           O  
ANISOU 5294  O   GLN A 697     3911   2676   3762   -621    165    817       O  
ATOM   5295  CB  GLN A 697      21.217 -37.458  -4.828  1.00 41.10           C  
ANISOU 5295  CB  GLN A 697     5644   4293   5680   -822    292    773       C  
ATOM   5296  CG  GLN A 697      20.064 -38.390  -5.199  1.00 52.73           C  
ANISOU 5296  CG  GLN A 697     7090   5690   7256   -943    359    732       C  
ATOM   5297  CD  GLN A 697      18.950 -37.699  -5.991  1.00 61.12           C  
ANISOU 5297  CD  GLN A 697     7992   6840   8390  -1000    352    630       C  
ATOM   5298  NE2 GLN A 697      17.714 -38.119  -5.744  1.00 55.69           N  
ANISOU 5298  NE2 GLN A 697     7259   6128   7771  -1118    442    605       N  
ATOM   5299  OE1 GLN A 697      19.197 -36.806  -6.817  1.00 68.75           O  
ANISOU 5299  OE1 GLN A 697     8877   7895   9352   -938    268    575       O  
ATOM   5300  N   PRO A 698      23.766 -35.329  -6.498  1.00 25.77           N  
ANISOU 5300  N   PRO A 698     3609   2537   3645   -571     44    701       N  
ATOM   5301  CA  PRO A 698      24.727 -34.318  -6.040  1.00 23.57           C  
ANISOU 5301  CA  PRO A 698     3335   2336   3284   -487      2    725       C  
ATOM   5302  C   PRO A 698      24.015 -33.147  -5.378  1.00 29.98           C  
ANISOU 5302  C   PRO A 698     4090   3235   4067   -512     42    720       C  
ATOM   5303  O   PRO A 698      22.877 -32.862  -5.736  1.00 33.45           O  
ANISOU 5303  O   PRO A 698     4450   3699   4560   -574     74    674       O  
ATOM   5304  CB  PRO A 698      25.399 -33.862  -7.332  1.00 19.06           C  
ANISOU 5304  CB  PRO A 698     2708   1804   2731   -432    -80    663       C  
ATOM   5305  CG  PRO A 698      24.409 -34.204  -8.431  1.00 19.24           C  
ANISOU 5305  CG  PRO A 698     2665   1808   2837   -494    -77    596       C  
ATOM   5306  CD  PRO A 698      23.662 -35.412  -7.967  1.00 20.83           C  
ANISOU 5306  CD  PRO A 698     2916   1914   3083   -572    -11    621       C  
ATOM   5307  N   GLY A 699      24.669 -32.484  -4.426  1.00 24.67           N  
ANISOU 5307  N   GLY A 699     3453   2609   3311   -463     38    761       N  
ATOM   5308  CA  GLY A 699      24.110 -31.283  -3.828  1.00 19.20           C  
ANISOU 5308  CA  GLY A 699     2710   2001   2586   -476     72    749       C  
ATOM   5309  C   GLY A 699      24.110 -30.080  -4.769  1.00 21.47           C  
ANISOU 5309  C   GLY A 699     2900   2363   2894   -448     23    680       C  
ATOM   5310  O   GLY A 699      25.119 -29.767  -5.386  1.00 17.61           O  
ANISOU 5310  O   GLY A 699     2409   1891   2390   -389    -44    663       O  
ATOM   5311  N   ILE A 700      22.975 -29.393  -4.856  1.00 18.25           N  
ANISOU 5311  N   ILE A 700     2416   2001   2519   -490     61    642       N  
ATOM   5312  CA  ILE A 700      22.841 -28.250  -5.743  1.00 17.51           C  
ANISOU 5312  CA  ILE A 700     2240   1970   2443   -460     19    582       C  
ATOM   5313  C   ILE A 700      22.839 -26.926  -4.981  1.00 23.00           C  
ANISOU 5313  C   ILE A 700     2920   2734   3084   -435     39    581       C  
ATOM   5314  O   ILE A 700      22.095 -26.751  -4.014  1.00 19.33           O  
ANISOU 5314  O   ILE A 700     2454   2287   2604   -470    106    596       O  
ATOM   5315  CB  ILE A 700      21.531 -28.315  -6.585  1.00 17.78           C  
ANISOU 5315  CB  ILE A 700     2184   2013   2559   -509     32    525       C  
ATOM   5316  CG1 ILE A 700      21.488 -29.584  -7.437  1.00 27.01           C  
ANISOU 5316  CG1 ILE A 700     3362   3113   3785   -539      9    510       C  
ATOM   5317  CG2 ILE A 700      21.402 -27.077  -7.482  1.00 17.12           C  
ANISOU 5317  CG2 ILE A 700     2028   1994   2482   -463    -15    471       C  
ATOM   5318  CD1 ILE A 700      20.106 -29.900  -8.002  1.00 18.74           C  
ANISOU 5318  CD1 ILE A 700     2230   2069   2820   -606     31    454       C  
ATOM   5319  N   THR A 701      23.665 -25.993  -5.439  1.00 17.75           N  
ANISOU 5319  N   THR A 701     2245   2105   2392   -378    -14    560       N  
ATOM   5320  CA  THR A 701      23.568 -24.607  -5.004  1.00 23.58           C  
ANISOU 5320  CA  THR A 701     2959   2904   3096   -355      0    541       C  
ATOM   5321  C   THR A 701      23.166 -23.754  -6.218  1.00 15.73           C  
ANISOU 5321  C   THR A 701     1895   1936   2145   -332    -33    487       C  
ATOM   5322  O   THR A 701      23.816 -23.783  -7.246  1.00 20.58           O  
ANISOU 5322  O   THR A 701     2509   2540   2771   -303    -87    472       O  
ATOM   5323  CB  THR A 701      24.898 -24.101  -4.413  1.00 24.88           C  
ANISOU 5323  CB  THR A 701     3177   3087   3190   -311    -29    559       C  
ATOM   5324  CG2 THR A 701      24.745 -22.677  -3.856  1.00 22.28           C  
ANISOU 5324  CG2 THR A 701     2830   2811   2825   -296     -6    535       C  
ATOM   5325  OG1 THR A 701      25.326 -24.982  -3.369  1.00 24.58           O  
ANISOU 5325  OG1 THR A 701     3211   3024   3105   -318    -13    613       O  
ATOM   5326  N   TYR A 702      22.080 -23.012  -6.076  1.00 15.94           N  
ANISOU 5326  N   TYR A 702     1867   1998   2192   -342      3    460       N  
ATOM   5327  CA  TYR A 702      21.540 -22.200  -7.140  1.00 18.98           C  
ANISOU 5327  CA  TYR A 702     2189   2409   2612   -312    -26    412       C  
ATOM   5328  C   TYR A 702      21.628 -20.728  -6.748  1.00 17.05           C  
ANISOU 5328  C   TYR A 702     1944   2201   2332   -272    -12    399       C  
ATOM   5329  O   TYR A 702      20.948 -20.291  -5.831  1.00 15.86           O  
ANISOU 5329  O   TYR A 702     1778   2076   2173   -285     43    395       O  
ATOM   5330  CB  TYR A 702      20.077 -22.591  -7.355  1.00 24.42           C  
ANISOU 5330  CB  TYR A 702     2803   3110   3365   -350      1    382       C  
ATOM   5331  CG  TYR A 702      19.412 -21.998  -8.579  1.00 29.25           C  
ANISOU 5331  CG  TYR A 702     3345   3749   4018   -313    -44    331       C  
ATOM   5332  CD1 TYR A 702      18.975 -22.813  -9.613  1.00 29.19           C  
ANISOU 5332  CD1 TYR A 702     3298   3731   4061   -330    -84    302       C  
ATOM   5333  CD2 TYR A 702      19.195 -20.633  -8.688  1.00 27.29           C  
ANISOU 5333  CD2 TYR A 702     3076   3538   3754   -258    -47    310       C  
ATOM   5334  CE1 TYR A 702      18.345 -22.287 -10.713  1.00 32.77           C  
ANISOU 5334  CE1 TYR A 702     3692   4218   4543   -289   -132    254       C  
ATOM   5335  CE2 TYR A 702      18.580 -20.100  -9.779  1.00 30.20           C  
ANISOU 5335  CE2 TYR A 702     3392   3931   4152   -214    -92    270       C  
ATOM   5336  CZ  TYR A 702      18.149 -20.926 -10.794  1.00 34.90           C  
ANISOU 5336  CZ  TYR A 702     3946   4523   4790   -227   -137    242       C  
ATOM   5337  OH  TYR A 702      17.528 -20.383 -11.895  1.00 32.85           O  
ANISOU 5337  OH  TYR A 702     3636   4294   4550   -173   -191    200       O  
ATOM   5338  N   ILE A 703      22.419 -19.958  -7.484  1.00 24.16           N  
ANISOU 5338  N   ILE A 703     2862   3101   3215   -226    -55    387       N  
ATOM   5339  CA  ILE A 703      22.655 -18.560  -7.153  1.00 22.81           C  
ANISOU 5339  CA  ILE A 703     2704   2950   3013   -193    -41    374       C  
ATOM   5340  C   ILE A 703      22.303 -17.660  -8.327  1.00 21.36           C  
ANISOU 5340  C   ILE A 703     2494   2771   2853   -145    -70    344       C  
ATOM   5341  O   ILE A 703      22.835 -17.831  -9.422  1.00 16.57           O  
ANISOU 5341  O   ILE A 703     1899   2147   2251   -125   -116    342       O  
ATOM   5342  CB  ILE A 703      24.139 -18.334  -6.839  1.00 21.00           C  
ANISOU 5342  CB  ILE A 703     2536   2711   2734   -185    -58    389       C  
ATOM   5343  CG1 ILE A 703      24.617 -19.346  -5.797  1.00 22.83           C  
ANISOU 5343  CG1 ILE A 703     2803   2937   2933   -217    -46    424       C  
ATOM   5344  CG2 ILE A 703      24.390 -16.888  -6.399  1.00 20.00           C  
ANISOU 5344  CG2 ILE A 703     2426   2598   2577   -162    -37    368       C  
ATOM   5345  CD1 ILE A 703      26.105 -19.502  -5.743  1.00 24.34           C  
ANISOU 5345  CD1 ILE A 703     3039   3122   3089   -204    -84    436       C  
ATOM   5346  N   VAL A 704      21.412 -16.695  -8.115  1.00 19.42           N  
ANISOU 5346  N   VAL A 704     2217   2545   2616   -119    -43    320       N  
ATOM   5347  CA  VAL A 704      21.158 -15.725  -9.171  1.00 20.03           C  
ANISOU 5347  CA  VAL A 704     2286   2621   2705    -60    -72    298       C  
ATOM   5348  C   VAL A 704      22.039 -14.492  -9.018  1.00 18.44           C  
ANISOU 5348  C   VAL A 704     2144   2399   2464    -33    -59    299       C  
ATOM   5349  O   VAL A 704      22.166 -13.929  -7.929  1.00 19.89           O  
ANISOU 5349  O   VAL A 704     2347   2587   2624    -44    -16    295       O  
ATOM   5350  CB  VAL A 704      19.659 -15.347  -9.339  1.00 29.52           C  
ANISOU 5350  CB  VAL A 704     3415   3853   3948    -29    -63    267       C  
ATOM   5351  CG1 VAL A 704      18.917 -15.589  -8.098  1.00 32.65           C  
ANISOU 5351  CG1 VAL A 704     3774   4276   4355    -67     -3    261       C  
ATOM   5352  CG2 VAL A 704      19.513 -13.885  -9.780  1.00 27.61           C  
ANISOU 5352  CG2 VAL A 704     3191   3603   3695     44    -68    251       C  
ATOM   5353  N   VAL A 705      22.667 -14.094 -10.120  1.00 14.36           N  
ANISOU 5353  N   VAL A 705     1661   1858   1938     -1    -94    302       N  
ATOM   5354  CA  VAL A 705      23.525 -12.926 -10.114  1.00 19.89           C  
ANISOU 5354  CA  VAL A 705     2419   2529   2608     16    -77    300       C  
ATOM   5355  C   VAL A 705      22.860 -11.795 -10.884  1.00 21.29           C  
ANISOU 5355  C   VAL A 705     2607   2690   2794     82    -79    289       C  
ATOM   5356  O   VAL A 705      22.404 -11.983 -12.005  1.00 25.02           O  
ANISOU 5356  O   VAL A 705     3066   3164   3277    121   -119    291       O  
ATOM   5357  CB  VAL A 705      24.932 -13.254 -10.661  1.00 26.76           C  
ANISOU 5357  CB  VAL A 705     3332   3379   3458     -5    -98    314       C  
ATOM   5358  CG1 VAL A 705      24.831 -13.987 -11.975  1.00 35.38           C  
ANISOU 5358  CG1 VAL A 705     4412   4468   4563     13   -144    321       C  
ATOM   5359  CG2 VAL A 705      25.766 -11.976 -10.813  1.00 26.77           C  
ANISOU 5359  CG2 VAL A 705     3389   3346   3437      6    -73    306       C  
ATOM   5360  N   GLN A 706      22.784 -10.622 -10.261  1.00 24.87           N  
ANISOU 5360  N   GLN A 706     3088   3126   3237    100    -38    275       N  
ATOM   5361  CA  GLN A 706      22.145  -9.457 -10.861  1.00 16.91           C  
ANISOU 5361  CA  GLN A 706     2099   2091   2234    173    -35    267       C  
ATOM   5362  C   GLN A 706      23.093  -8.270 -10.901  1.00 20.96           C  
ANISOU 5362  C   GLN A 706     2696   2546   2722    176     -3    268       C  
ATOM   5363  O   GLN A 706      23.622  -7.855  -9.854  1.00 15.22           O  
ANISOU 5363  O   GLN A 706     1990   1811   1983    136     38    251       O  
ATOM   5364  CB  GLN A 706      20.910  -9.029 -10.055  1.00 22.72           C  
ANISOU 5364  CB  GLN A 706     2787   2851   2992    203     -6    241       C  
ATOM   5365  CG  GLN A 706      19.585  -9.514 -10.573  1.00 39.36           C  
ANISOU 5365  CG  GLN A 706     4815   5002   5137    246    -40    230       C  
ATOM   5366  CD  GLN A 706      19.120  -8.809 -11.850  1.00 43.36           C  
ANISOU 5366  CD  GLN A 706     5341   5490   5645    337    -83    233       C  
ATOM   5367  NE2 GLN A 706      17.869  -9.052 -12.223  1.00 40.15           N  
ANISOU 5367  NE2 GLN A 706     4855   5127   5271    386   -117    211       N  
ATOM   5368  OE1 GLN A 706      19.872  -8.072 -12.492  1.00 44.38           O  
ANISOU 5368  OE1 GLN A 706     5553   5565   5744    363    -85    253       O  
ATOM   5369  N   LYS A 707      23.270  -7.704 -12.098  1.00 17.99           N  
ANISOU 5369  N   LYS A 707     2371   2129   2335    222    -18    285       N  
ATOM   5370  CA  LYS A 707      23.971  -6.441 -12.272  1.00 24.64           C  
ANISOU 5370  CA  LYS A 707     3299   2902   3160    231     22    287       C  
ATOM   5371  C   LYS A 707      22.939  -5.372 -12.584  1.00 27.41           C  
ANISOU 5371  C   LYS A 707     3677   3221   3518    321     29    285       C  
ATOM   5372  O   LYS A 707      23.242  -4.176 -12.576  1.00 25.02           O  
ANISOU 5372  O   LYS A 707     3450   2850   3207    340     71    284       O  
ATOM   5373  CB  LYS A 707      24.945  -6.505 -13.453  1.00 38.05           C  
ANISOU 5373  CB  LYS A 707     5054   4568   4836    222     12    313       C  
ATOM   5374  CG  LYS A 707      26.203  -7.333 -13.252  1.00 45.08           C  
ANISOU 5374  CG  LYS A 707     5931   5478   5719    141     12    311       C  
ATOM   5375  CD  LYS A 707      27.299  -6.911 -14.250  1.00 45.59           C  
ANISOU 5375  CD  LYS A 707     6065   5495   5763    127     33    326       C  
ATOM   5376  CE  LYS A 707      27.547  -5.400 -14.167  1.00 46.23           C  
ANISOU 5376  CE  LYS A 707     6226   5501   5839    134     93    321       C  
ATOM   5377  NZ  LYS A 707      28.920  -4.985 -14.566  1.00 33.76           N1+
ANISOU 5377  NZ  LYS A 707     4700   3878   4250     77    139    319       N1+
ATOM   5378  N   ARG A 708      21.718  -5.803 -12.884  1.00 26.31           N  
ANISOU 5378  N   ARG A 708     3472   3127   3396    380    -14    283       N  
ATOM   5379  CA  ARG A 708      20.706  -4.873 -13.390  1.00 33.12           C  
ANISOU 5379  CA  ARG A 708     4353   3966   4264    485    -24    283       C  
ATOM   5380  C   ARG A 708      19.844  -4.332 -12.256  1.00 35.65           C  
ANISOU 5380  C   ARG A 708     4633   4300   4613    508     12    247       C  
ATOM   5381  O   ARG A 708      18.663  -4.679 -12.134  1.00 40.48           O  
ANISOU 5381  O   ARG A 708     5158   4969   5254    551    -13    226       O  
ATOM   5382  CB  ARG A 708      19.808  -5.538 -14.435  1.00 39.11           C  
ANISOU 5382  CB  ARG A 708     5058   4774   5027    548    -99    290       C  
ATOM   5383  CG  ARG A 708      20.429  -5.779 -15.799  1.00 51.18           C  
ANISOU 5383  CG  ARG A 708     6646   6282   6517    562   -137    325       C  
ATOM   5384  CD  ARG A 708      19.333  -6.222 -16.785  1.00 69.27           C  
ANISOU 5384  CD  ARG A 708     8885   8626   8809    644   -217    321       C  
ATOM   5385  NE  ARG A 708      19.737  -6.114 -18.188  1.00 81.15           N  
ANISOU 5385  NE  ARG A 708    10469  10103  10261    690   -254    355       N  
ATOM   5386  CZ  ARG A 708      18.914  -6.277 -19.222  1.00 88.33           C  
ANISOU 5386  CZ  ARG A 708    11361  11048  11152    778   -329    354       C  
ATOM   5387  NH1 ARG A 708      17.632  -6.552 -19.018  1.00 91.79           N1+
ANISOU 5387  NH1 ARG A 708    11694  11553  11630    825   -377    316       N1+
ATOM   5388  NH2 ARG A 708      19.371  -6.162 -20.464  1.00 88.69           N  
ANISOU 5388  NH2 ARG A 708    11494  11068  11138    817   -356    388       N  
ATOM   5389  N   HIS A 709      20.436  -3.481 -11.429  1.00 22.50           N  
ANISOU 5389  N   HIS A 709     3025   2583   2941    477     74    232       N  
ATOM   5390  CA  HIS A 709      19.733  -2.913 -10.298  1.00 18.29           C  
ANISOU 5390  CA  HIS A 709     2464   2058   2427    495    118    193       C  
ATOM   5391  C   HIS A 709      20.309  -1.524 -10.093  1.00 27.99           C  
ANISOU 5391  C   HIS A 709     3799   3192   3644    507    172    184       C  
ATOM   5392  O   HIS A 709      21.240  -1.117 -10.801  1.00 26.70           O  
ANISOU 5392  O   HIS A 709     3720   2963   3460    491    178    211       O  
ATOM   5393  CB  HIS A 709      19.944  -3.790  -9.058  1.00 17.82           C  
ANISOU 5393  CB  HIS A 709     2343   2059   2368    403    141    170       C  
ATOM   5394  CG  HIS A 709      21.386  -3.981  -8.705  1.00 26.64           C  
ANISOU 5394  CG  HIS A 709     3510   3156   3457    311    158    176       C  
ATOM   5395  CD2 HIS A 709      22.216  -5.040  -8.880  1.00 20.69           C  
ANISOU 5395  CD2 HIS A 709     2741   2432   2690    243    129    196       C  
ATOM   5396  ND1 HIS A 709      22.154  -2.981  -8.146  1.00 17.42           N  
ANISOU 5396  ND1 HIS A 709     2415   1930   2273    283    206    153       N  
ATOM   5397  CE1 HIS A 709      23.389  -3.422  -7.974  1.00 16.90           C  
ANISOU 5397  CE1 HIS A 709     2367   1867   2187    201    204    156       C  
ATOM   5398  NE2 HIS A 709      23.450  -4.670  -8.410  1.00 16.37           N  
ANISOU 5398  NE2 HIS A 709     2247   1852   2120    180    158    185       N  
ATOM   5399  N   HIS A 710      19.767  -0.792  -9.130  1.00 27.35           N  
ANISOU 5399  N   HIS A 710     3716   3100   3577    532    219    144       N  
ATOM   5400  CA  HIS A 710      20.215   0.574  -8.898  1.00 28.02           C  
ANISOU 5400  CA  HIS A 710     3903   3086   3656    546    274    127       C  
ATOM   5401  C   HIS A 710      20.876   0.829  -7.572  1.00 20.84           C  
ANISOU 5401  C   HIS A 710     3009   2172   2736    460    330     80       C  
ATOM   5402  O   HIS A 710      20.950   1.972  -7.134  1.00 24.74           O  
ANISOU 5402  O   HIS A 710     3572   2594   3234    478    381     47       O  
ATOM   5403  CB  HIS A 710      19.062   1.544  -9.064  1.00 27.77           C  
ANISOU 5403  CB  HIS A 710     3887   3017   3646    671    283    115       C  
ATOM   5404  CG  HIS A 710      18.698   1.755 -10.490  1.00 35.27           C  
ANISOU 5404  CG  HIS A 710     4873   3935   4592    767    233    164       C  
ATOM   5405  CD2 HIS A 710      19.154   2.650 -11.395  1.00 30.44           C  
ANISOU 5405  CD2 HIS A 710     4383   3220   3962    811    242    200       C  
ATOM   5406  ND1 HIS A 710      17.825   0.928 -11.158  1.00 36.20           N  
ANISOU 5406  ND1 HIS A 710     4903   4133   4720    822    163    179       N  
ATOM   5407  CE1 HIS A 710      17.717   1.338 -12.408  1.00 26.49           C  
ANISOU 5407  CE1 HIS A 710     3737   2855   3471    908    124    222       C  
ATOM   5408  NE2 HIS A 710      18.512   2.375 -12.577  1.00 30.81           N  
ANISOU 5408  NE2 HIS A 710     4417   3290   3999    903    174    240       N  
ATOM   5409  N   THR A 711      21.379  -0.208  -6.929  1.00 19.00           N  
ANISOU 5409  N   THR A 711     2720   2012   2488    372    319     73       N  
ATOM   5410  CA  THR A 711      22.058   0.073  -5.675  1.00 24.46           C  
ANISOU 5410  CA  THR A 711     3433   2702   3159    297    364     26       C  
ATOM   5411  C   THR A 711      23.525   0.451  -5.929  1.00 20.19           C  
ANISOU 5411  C   THR A 711     2965   2102   2603    223    375     24       C  
ATOM   5412  O   THR A 711      24.232  -0.216  -6.685  1.00 20.89           O  
ANISOU 5412  O   THR A 711     3048   2203   2687    188    340     61       O  
ATOM   5413  CB  THR A 711      21.843  -1.034  -4.595  1.00 35.26           C  
ANISOU 5413  CB  THR A 711     4718   4172   4509    245    358     12       C  
ATOM   5414  CG2 THR A 711      20.749  -1.966  -4.999  1.00 18.55           C  
ANISOU 5414  CG2 THR A 711     2514   2120   2413    289    324     41       C  
ATOM   5415  OG1 THR A 711      23.041  -1.771  -4.390  1.00 38.39           O  
ANISOU 5415  OG1 THR A 711     5116   4595   4877    155    337     21       O  
ATOM   5416  N   ARG A 712      23.942   1.568  -5.343  1.00 19.40           N  
ANISOU 5416  N   ARG A 712     2934   1936   2503    203    427    -24       N  
ATOM   5417  CA  ARG A 712      25.308   2.058  -5.482  1.00 24.41           C  
ANISOU 5417  CA  ARG A 712     3632   2511   3131    124    448    -41       C  
ATOM   5418  C   ARG A 712      25.970   2.188  -4.114  1.00 22.52           C  
ANISOU 5418  C   ARG A 712     3387   2301   2869     44    471   -110       C  
ATOM   5419  O   ARG A 712      25.331   2.541  -3.133  1.00 20.01           O  
ANISOU 5419  O   ARG A 712     3064   1998   2541     66    498   -154       O  
ATOM   5420  CB  ARG A 712      25.334   3.417  -6.189  1.00 25.80           C  
ANISOU 5420  CB  ARG A 712     3913   2560   3330    165    495    -38       C  
ATOM   5421  CG  ARG A 712      24.560   3.473  -7.491  1.00 25.92           C  
ANISOU 5421  CG  ARG A 712     3950   2541   3357    266    471     28       C  
ATOM   5422  CD  ARG A 712      25.359   2.911  -8.658  1.00 23.04           C  
ANISOU 5422  CD  ARG A 712     3597   2174   2984    233    443     82       C  
ATOM   5423  NE  ARG A 712      24.842   3.408  -9.922  1.00 24.34           N  
ANISOU 5423  NE  ARG A 712     3828   2270   3149    326    438    137       N  
ATOM   5424  CZ  ARG A 712      25.476   3.310 -11.090  1.00 28.94           C  
ANISOU 5424  CZ  ARG A 712     4461   2818   3718    315    433    186       C  
ATOM   5425  NH1 ARG A 712      26.662   2.716 -11.173  1.00 22.11           N1+
ANISOU 5425  NH1 ARG A 712     3574   1980   2845    213    435    183       N1+
ATOM   5426  NH2 ARG A 712      24.912   3.808 -12.182  1.00 24.21           N  
ANISOU 5426  NH2 ARG A 712     3933   2158   3109    412    427    238       N  
ATOM   5427  N   LEU A 713      27.259   1.891  -4.066  1.00 20.80           N  
ANISOU 5427  N   LEU A 713     3166   2097   2639    -45    458   -124       N  
ATOM   5428  CA  LEU A 713      28.024   1.960  -2.833  1.00 20.46           C  
ANISOU 5428  CA  LEU A 713     3114   2091   2569   -123    466   -194       C  
ATOM   5429  C   LEU A 713      29.180   2.938  -3.019  1.00 20.54           C  
ANISOU 5429  C   LEU A 713     3187   2020   2599   -193    503   -241       C  
ATOM   5430  O   LEU A 713      29.841   2.929  -4.049  1.00 21.17           O  
ANISOU 5430  O   LEU A 713     3284   2061   2701   -217    503   -209       O  
ATOM   5431  CB  LEU A 713      28.552   0.570  -2.466  1.00 18.78           C  
ANISOU 5431  CB  LEU A 713     2825   1988   2324   -166    407   -177       C  
ATOM   5432  CG  LEU A 713      27.459  -0.462  -2.174  1.00 18.38           C  
ANISOU 5432  CG  LEU A 713     2714   2014   2255   -114    379   -134       C  
ATOM   5433  CD1 LEU A 713      28.025  -1.889  -2.167  1.00 17.69           C  
ANISOU 5433  CD1 LEU A 713     2567   2010   2145   -149    321    -98       C  
ATOM   5434  CD2 LEU A 713      26.808  -0.122  -0.830  1.00 18.92           C  
ANISOU 5434  CD2 LEU A 713     2785   2112   2291   -103    411   -185       C  
ATOM   5435  N   PHE A 714      29.413   3.778  -2.021  1.00 20.72           N  
ANISOU 5435  N   PHE A 714     3242   2017   2612   -231    538   -323       N  
ATOM   5436  CA  PHE A 714      30.484   4.760  -2.079  1.00 25.72           C  
ANISOU 5436  CA  PHE A 714     3932   2571   3270   -310    580   -383       C  
ATOM   5437  C   PHE A 714      31.313   4.656  -0.804  1.00 29.16           C  
ANISOU 5437  C   PHE A 714     4332   3077   3671   -392    560   -472       C  
ATOM   5438  O   PHE A 714      30.766   4.378   0.269  1.00 26.93           O  
ANISOU 5438  O   PHE A 714     4026   2863   3344   -368    544   -499       O  
ATOM   5439  CB  PHE A 714      29.895   6.172  -2.174  1.00 22.30           C  
ANISOU 5439  CB  PHE A 714     3597   2010   2866   -270    651   -409       C  
ATOM   5440  CG  PHE A 714      28.841   6.334  -3.245  1.00 26.02           C  
ANISOU 5440  CG  PHE A 714     4105   2420   3360   -162    662   -326       C  
ATOM   5441  CD1 PHE A 714      29.202   6.614  -4.564  1.00 22.25           C  
ANISOU 5441  CD1 PHE A 714     3683   1861   2911   -159    681   -269       C  
ATOM   5442  CD2 PHE A 714      27.496   6.219  -2.936  1.00 22.21           C  
ANISOU 5442  CD2 PHE A 714     3604   1966   2868    -62    655   -308       C  
ATOM   5443  CE1 PHE A 714      28.233   6.772  -5.558  1.00 23.64           C  
ANISOU 5443  CE1 PHE A 714     3898   1986   3096    -50    681   -194       C  
ATOM   5444  CE2 PHE A 714      26.518   6.376  -3.917  1.00 29.22           C  
ANISOU 5444  CE2 PHE A 714     4517   2808   3776     45    654   -240       C  
ATOM   5445  CZ  PHE A 714      26.890   6.653  -5.239  1.00 22.30           C  
ANISOU 5445  CZ  PHE A 714     3701   1851   2920     55    662   -181       C  
ATOM   5446  N   CYS A 715      32.620   4.895  -0.913  1.00 21.96           N  
ANISOU 5446  N   CYS A 715     3415   2151   2776   -487    563   -520       N  
ATOM   5447  CA  CYS A 715      33.476   5.013   0.271  1.00 22.49           C  
ANISOU 5447  CA  CYS A 715     3454   2277   2814   -566    544   -622       C  
ATOM   5448  C   CYS A 715      33.032   6.174   1.150  1.00 27.03           C  
ANISOU 5448  C   CYS A 715     4096   2790   3383   -566    595   -705       C  
ATOM   5449  O   CYS A 715      32.910   7.297   0.668  1.00 27.35           O  
ANISOU 5449  O   CYS A 715     4217   2703   3472   -569    664   -721       O  
ATOM   5450  CB  CYS A 715      34.932   5.264  -0.126  1.00 22.86           C  
ANISOU 5450  CB  CYS A 715     3482   2304   2897   -671    549   -671       C  
ATOM   5451  SG  CYS A 715      35.657   4.068  -1.274  1.00 29.10           S  
ANISOU 5451  SG  CYS A 715     4200   3153   3706   -681    504   -589       S  
ATOM   5452  N   ALA A 716      32.814   5.923   2.442  1.00 26.95           N  
ANISOU 5452  N   ALA A 716     4062   2865   3311   -561    566   -758       N  
ATOM   5453  CA  ALA A 716      32.563   7.019   3.377  1.00 32.95           C  
ANISOU 5453  CA  ALA A 716     4885   3576   4060   -573    613   -856       C  
ATOM   5454  C   ALA A 716      33.820   7.882   3.564  1.00 32.84           C  
ANISOU 5454  C   ALA A 716     4890   3513   4076   -687    632   -965       C  
ATOM   5455  O   ALA A 716      33.734   9.100   3.674  1.00 26.58           O  
ANISOU 5455  O   ALA A 716     4174   2609   3316   -708    699  -1031       O  
ATOM   5456  CB  ALA A 716      32.065   6.486   4.716  1.00 34.36           C  
ANISOU 5456  CB  ALA A 716     5035   3867   4154   -542    579   -888       C  
ATOM   5457  N   ASP A 717      34.986   7.245   3.579  1.00 29.80           N  
ANISOU 5457  N   ASP A 717     4431   3209   3683   -760    575   -986       N  
ATOM   5458  CA  ASP A 717      36.239   7.961   3.780  1.00 35.84           C  
ANISOU 5458  CA  ASP A 717     5190   3946   4479   -877    586  -1099       C  
ATOM   5459  C   ASP A 717      36.849   8.293   2.434  1.00 39.69           C  
ANISOU 5459  C   ASP A 717     5692   4339   5051   -927    634  -1061       C  
ATOM   5460  O   ASP A 717      37.281   7.402   1.708  1.00 40.15           O  
ANISOU 5460  O   ASP A 717     5687   4451   5119   -926    597   -992       O  
ATOM   5461  CB  ASP A 717      37.236   7.130   4.609  1.00 54.14           C  
ANISOU 5461  CB  ASP A 717     7412   6416   6743   -928    493  -1158       C  
ATOM   5462  CG  ASP A 717      36.822   6.985   6.074  1.00 77.08           C  
ANISOU 5462  CG  ASP A 717    10320   9411   9554   -897    452  -1219       C  
ATOM   5463  OD1 ASP A 717      36.354   7.983   6.669  1.00 87.20           O  
ANISOU 5463  OD1 ASP A 717    11675  10628  10831   -899    504  -1292       O  
ATOM   5464  OD2 ASP A 717      36.974   5.874   6.637  1.00 82.01           O1-
ANISOU 5464  OD2 ASP A 717    10882  10169  10107   -868    370  -1194       O1-
ATOM   5465  N   LYS A 718      36.877   9.583   2.121  1.00 42.67           N  
ANISOU 5465  N   LYS A 718     6157   4569   5486   -968    722  -1106       N  
ATOM   5466  CA  LYS A 718      37.449  10.106   0.892  1.00 38.38           C  
ANISOU 5466  CA  LYS A 718     5652   3912   5020  -1024    789  -1077       C  
ATOM   5467  C   LYS A 718      38.759   9.415   0.528  1.00 36.59           C  
ANISOU 5467  C   LYS A 718     5322   3768   4811  -1112    749  -1093       C  
ATOM   5468  O   LYS A 718      38.998   9.103  -0.635  1.00 29.93           O  
ANISOU 5468  O   LYS A 718     4474   2896   4003  -1111    771  -1012       O  
ATOM   5469  CB  LYS A 718      37.677  11.613   1.044  1.00 48.05           C  
ANISOU 5469  CB  LYS A 718     6973   4986   6297  -1099    882  -1173       C  
ATOM   5470  CG  LYS A 718      38.007  12.342  -0.242  1.00 58.56           C  
ANISOU 5470  CG  LYS A 718     8382   6163   7704  -1142    976  -1128       C  
ATOM   5471  CD  LYS A 718      38.222  13.829   0.012  1.00 65.85           C  
ANISOU 5471  CD  LYS A 718     9411   6929   8680  -1219   1072  -1228       C  
ATOM   5472  CE  LYS A 718      37.016  14.478   0.699  1.00 71.38           C  
ANISOU 5472  CE  LYS A 718    10201   7566   9354  -1124   1091  -1244       C  
ATOM   5473  NZ  LYS A 718      35.803  14.577  -0.170  1.00 71.28           N1+
ANISOU 5473  NZ  LYS A 718    10275   7466   9342   -985   1124  -1111       N1+
ATOM   5474  N   ASN A 719      39.590   9.143   1.532  1.00 31.49           N  
ANISOU 5474  N   ASN A 719     4593   3235   4139  -1178    686  -1198       N  
ATOM   5475  CA  ASN A 719      40.901   8.542   1.299  1.00 31.48           C  
ANISOU 5475  CA  ASN A 719     4481   3322   4159  -1260    643  -1233       C  
ATOM   5476  C   ASN A 719      40.897   7.067   0.873  1.00 34.02           C  
ANISOU 5476  C   ASN A 719     4719   3762   4446  -1190    564  -1130       C  
ATOM   5477  O   ASN A 719      41.945   6.515   0.524  1.00 34.24           O  
ANISOU 5477  O   ASN A 719     4656   3858   4497  -1243    533  -1146       O  
ATOM   5478  CB  ASN A 719      41.814   8.765   2.509  1.00 37.17           C  
ANISOU 5478  CB  ASN A 719     5134   4127   4861  -1349    592  -1388       C  
ATOM   5479  CG  ASN A 719      42.258  10.216   2.636  1.00 49.90           C  
ANISOU 5479  CG  ASN A 719     6808   5613   6537  -1462    680  -1507       C  
ATOM   5480  ND2 ASN A 719      41.934  10.838   3.763  1.00 56.58           N  
ANISOU 5480  ND2 ASN A 719     7696   6455   7346  -1467    673  -1603       N  
ATOM   5481  OD1 ASN A 719      42.858  10.779   1.716  1.00 54.94           O  
ANISOU 5481  OD1 ASN A 719     7465   6153   7257  -1544    761  -1511       O  
ATOM   5482  N   GLU A 720      39.731   6.429   0.885  1.00 34.89           N  
ANISOU 5482  N   GLU A 720     4857   3895   4505  -1072    536  -1029       N  
ATOM   5483  CA  GLU A 720      39.654   5.018   0.512  1.00 31.72           C  
ANISOU 5483  CA  GLU A 720     4385   3595   4071  -1006    465   -934       C  
ATOM   5484  C   GLU A 720      39.227   4.846  -0.952  1.00 30.52           C  
ANISOU 5484  C   GLU A 720     4271   3366   3959   -962    512   -816       C  
ATOM   5485  O   GLU A 720      39.227   3.738  -1.486  1.00 34.98           O  
ANISOU 5485  O   GLU A 720     4783   3996   4510   -916    465   -738       O  
ATOM   5486  CB  GLU A 720      38.680   4.273   1.420  1.00 31.35           C  
ANISOU 5486  CB  GLU A 720     4335   3633   3944   -912    403   -895       C  
ATOM   5487  CG  GLU A 720      38.924   4.459   2.907  1.00 49.28           C  
ANISOU 5487  CG  GLU A 720     6589   5979   6155   -939    358  -1002       C  
ATOM   5488  CD  GLU A 720      39.577   3.257   3.562  1.00 61.65           C  
ANISOU 5488  CD  GLU A 720     8063   7700   7661   -929    252  -1010       C  
ATOM   5489  OE1 GLU A 720      40.732   2.939   3.204  1.00 71.41           O  
ANISOU 5489  OE1 GLU A 720     9223   8981   8930   -984    220  -1041       O  
ATOM   5490  OE2 GLU A 720      38.934   2.632   4.434  1.00 61.97           O1-
ANISOU 5490  OE2 GLU A 720     8108   7815   7622   -863    205   -985       O1-
ATOM   5491  N   ARG A 721      38.855   5.953  -1.581  1.00 30.47           N  
ANISOU 5491  N   ARG A 721     4362   3216   3997   -972    604   -806       N  
ATOM   5492  CA  ARG A 721      38.385   5.967  -2.967  1.00 27.01           C  
ANISOU 5492  CA  ARG A 721     3981   2692   3587   -924    653   -698       C  
ATOM   5493  C   ARG A 721      39.508   5.566  -3.919  1.00 27.31           C  
ANISOU 5493  C   ARG A 721     3967   2747   3663   -989    665   -685       C  
ATOM   5494  O   ARG A 721      40.658   5.950  -3.732  1.00 30.05           O  
ANISOU 5494  O   ARG A 721     4272   3098   4046  -1098    686   -775       O  
ATOM   5495  CB  ARG A 721      37.787   7.347  -3.304  1.00 24.48           C  
ANISOU 5495  CB  ARG A 721     3792   2210   3301   -917    750   -698       C  
ATOM   5496  CG  ARG A 721      36.785   7.781  -2.238  1.00 34.02           C  
ANISOU 5496  CG  ARG A 721     5040   3410   4475   -859    741   -732       C  
ATOM   5497  CD  ARG A 721      35.648   8.658  -2.714  1.00 37.19           C  
ANISOU 5497  CD  ARG A 721     5560   3678   4891   -777    806   -680       C  
ATOM   5498  NE  ARG A 721      36.060  10.028  -2.916  1.00 26.21           N  
ANISOU 5498  NE  ARG A 721     4267   2139   3553   -846    900   -736       N  
ATOM   5499  CZ  ARG A 721      35.358  11.090  -2.531  1.00 27.32           C  
ANISOU 5499  CZ  ARG A 721     4504   2172   3703   -811    954   -769       C  
ATOM   5500  NH1 ARG A 721      34.194  10.949  -1.911  1.00 26.71           N1+
ANISOU 5500  NH1 ARG A 721     4431   2128   3587   -706    923   -754       N1+
ATOM   5501  NH2 ARG A 721      35.827  12.305  -2.777  1.00 28.21           N  
ANISOU 5501  NH2 ARG A 721     4712   2137   3868   -883   1045   -818       N  
ATOM   5502  N   ILE A 722      39.183   4.767  -4.927  1.00 25.78           N  
ANISOU 5502  N   ILE A 722     3767   2567   3460   -924    649   -581       N  
ATOM   5503  CA  ILE A 722      40.218   4.254  -5.815  1.00 28.04           C  
ANISOU 5503  CA  ILE A 722     3996   2882   3774   -976    657   -568       C  
ATOM   5504  C   ILE A 722      40.121   4.743  -7.255  1.00 31.06           C  
ANISOU 5504  C   ILE A 722     4467   3149   4185   -972    744   -494       C  
ATOM   5505  O   ILE A 722      39.048   4.754  -7.850  1.00 34.03           O  
ANISOU 5505  O   ILE A 722     4918   3472   4539   -877    750   -404       O  
ATOM   5506  CB  ILE A 722      40.308   2.719  -5.719  1.00 32.26           C  
ANISOU 5506  CB  ILE A 722     4429   3556   4273   -923    558   -528       C  
ATOM   5507  CG1 ILE A 722      41.011   2.379  -4.402  1.00 34.24           C  
ANISOU 5507  CG1 ILE A 722     4586   3918   4505   -967    488   -624       C  
ATOM   5508  CG2 ILE A 722      41.075   2.111  -6.933  1.00 21.50           C  
ANISOU 5508  CG2 ILE A 722     3027   2208   2935   -943    574   -486       C  
ATOM   5509  CD1 ILE A 722      40.587   1.122  -3.820  1.00 40.33           C  
ANISOU 5509  CD1 ILE A 722     5300   4802   5220   -889    390   -584       C  
ATOM   5510  N   GLY A 723      41.260   5.174  -7.789  1.00 37.39           N  
ANISOU 5510  N   GLY A 723     5259   3914   5034  -1076    811   -537       N  
ATOM   5511  CA  GLY A 723      41.369   5.575  -9.181  1.00 36.92           C  
ANISOU 5511  CA  GLY A 723     5281   3751   4994  -1084    901   -469       C  
ATOM   5512  C   GLY A 723      40.782   6.942  -9.476  1.00 37.37           C  
ANISOU 5512  C   GLY A 723     5489   3642   5066  -1082    996   -451       C  
ATOM   5513  O   GLY A 723      40.317   7.644  -8.564  1.00 37.73           O  
ANISOU 5513  O   GLY A 723     5573   3647   5115  -1080    997   -502       O  
ATOM   5514  N   LYS A 724      40.806   7.306 -10.758  1.00 33.09           N  
ANISOU 5514  N   LYS A 724     5040   3002   4530  -1077   1077   -377       N  
ATOM   5515  CA  LYS A 724      40.253   8.561 -11.255  1.00 37.36           C  
ANISOU 5515  CA  LYS A 724     5744   3371   5079  -1060   1172   -338       C  
ATOM   5516  C   LYS A 724      38.762   8.607 -10.984  1.00 25.49           C  
ANISOU 5516  C   LYS A 724     4301   1849   3534   -917   1117   -279       C  
ATOM   5517  O   LYS A 724      38.204   9.651 -10.697  1.00 29.21           O  
ANISOU 5517  O   LYS A 724     4875   2206   4016   -897   1163   -290       O  
ATOM   5518  CB  LYS A 724      40.482   8.673 -12.770  1.00 42.18           C  
ANISOU 5518  CB  LYS A 724     6442   3904   5680  -1056   1252   -248       C  
ATOM   5519  CG  LYS A 724      41.499   9.713 -13.217  1.00 53.26           C  
ANISOU 5519  CG  LYS A 724     7906   5200   7131  -1180   1382   -288       C  
ATOM   5520  CD  LYS A 724      41.642   9.689 -14.742  1.00 61.30           C  
ANISOU 5520  CD  LYS A 724     8994   6186   8111  -1140   1437   -188       C  
ATOM   5521  CE  LYS A 724      42.825  10.526 -15.238  1.00 71.09           C  
ANISOU 5521  CE  LYS A 724    10242   7390   9380  -1241   1539   -230       C  
ATOM   5522  NZ  LYS A 724      42.614  12.005 -15.145  1.00 76.18           N1+
ANISOU 5522  NZ  LYS A 724    11007   7905  10035  -1243   1612   -239       N1+
ATOM   5523  N   SER A 725      38.123   7.454 -11.097  1.00 26.57           N  
ANISOU 5523  N   SER A 725     4372   2098   3627   -819   1020   -220       N  
ATOM   5524  CA  SER A 725      36.691   7.345 -10.890  1.00 23.76           C  
ANISOU 5524  CA  SER A 725     4049   1744   3234   -684    963   -167       C  
ATOM   5525  C   SER A 725      36.310   7.350  -9.397  1.00 29.89           C  
ANISOU 5525  C   SER A 725     4766   2580   4011   -682    911   -244       C  
ATOM   5526  O   SER A 725      35.142   7.549  -9.053  1.00 24.68           O  
ANISOU 5526  O   SER A 725     4142   1903   3332   -585    886   -221       O  
ATOM   5527  CB  SER A 725      36.187   6.073 -11.563  1.00 31.70           C  
ANISOU 5527  CB  SER A 725     4998   2848   4198   -595    883    -84       C  
ATOM   5528  OG  SER A 725      36.840   4.932 -11.014  1.00 35.41           O  
ANISOU 5528  OG  SER A 725     5329   3459   4666   -641    814   -126       O  
ATOM   5529  N   GLY A 726      37.293   7.129  -8.524  1.00 23.68           N  
ANISOU 5529  N   GLY A 726     3887   1868   3243   -785    894   -338       N  
ATOM   5530  CA  GLY A 726      37.073   7.174  -7.087  1.00 23.70           C  
ANISOU 5530  CA  GLY A 726     3840   1928   3235   -793    849   -419       C  
ATOM   5531  C   GLY A 726      36.105   6.128  -6.558  1.00 31.72           C  
ANISOU 5531  C   GLY A 726     4791   3057   4202   -692    754   -379       C  
ATOM   5532  O   GLY A 726      35.303   6.418  -5.683  1.00 22.74           O  
ANISOU 5532  O   GLY A 726     3670   1922   3048   -646    740   -405       O  
ATOM   5533  N   ASN A 727      36.174   4.909  -7.088  1.00 26.17           N  
ANISOU 5533  N   ASN A 727     4018   2447   3480   -660    695   -319       N  
ATOM   5534  CA  ASN A 727      35.245   3.863  -6.680  1.00 22.59           C  
ANISOU 5534  CA  ASN A 727     3507   2092   2985   -571    613   -276       C  
ATOM   5535  C   ASN A 727      35.731   3.033  -5.490  1.00 22.91           C  
ANISOU 5535  C   ASN A 727     3445   2259   3000   -609    544   -334       C  
ATOM   5536  O   ASN A 727      36.893   3.126  -5.082  1.00 22.31           O  
ANISOU 5536  O   ASN A 727     3325   2213   2938   -700    545   -408       O  
ATOM   5537  CB  ASN A 727      34.920   2.937  -7.867  1.00 21.83           C  
ANISOU 5537  CB  ASN A 727     3397   2022   2877   -508    582   -179       C  
ATOM   5538  CG  ASN A 727      33.896   3.538  -8.805  1.00 22.34           C  
ANISOU 5538  CG  ASN A 727     3558   1990   2941   -420    617   -108       C  
ATOM   5539  ND2 ASN A 727      34.344   3.961  -9.986  1.00 24.24           N  
ANISOU 5539  ND2 ASN A 727     3866   2152   3194   -435    671    -70       N  
ATOM   5540  OD1 ASN A 727      32.720   3.632  -8.469  1.00 20.12           O  
ANISOU 5540  OD1 ASN A 727     3292   1707   2646   -336    597    -89       O  
ATOM   5541  N   ILE A 728      34.830   2.212  -4.950  1.00 22.87           N  
ANISOU 5541  N   ILE A 728     3402   2330   2956   -536    485   -301       N  
ATOM   5542  CA  ILE A 728      35.167   1.283  -3.865  1.00 24.71           C  
ANISOU 5542  CA  ILE A 728     3551   2684   3152   -554    415   -336       C  
ATOM   5543  C   ILE A 728      36.154   0.230  -4.400  1.00 29.47           C  
ANISOU 5543  C   ILE A 728     4081   3357   3760   -584    370   -316       C  
ATOM   5544  O   ILE A 728      36.174  -0.050  -5.597  1.00 23.23           O  
ANISOU 5544  O   ILE A 728     3300   2537   2990   -564    383   -255       O  
ATOM   5545  CB  ILE A 728      33.901   0.602  -3.307  1.00 23.72           C  
ANISOU 5545  CB  ILE A 728     3413   2613   2987   -469    377   -291       C  
ATOM   5546  CG1 ILE A 728      33.198  -0.188  -4.419  1.00 20.57           C  
ANISOU 5546  CG1 ILE A 728     3005   2214   2595   -400    358   -195       C  
ATOM   5547  CG2 ILE A 728      32.948   1.652  -2.697  1.00 19.58           C  
ANISOU 5547  CG2 ILE A 728     2953   2029   2459   -436    424   -322       C  
ATOM   5548  CD1 ILE A 728      31.896  -0.837  -3.993  1.00 17.87           C  
ANISOU 5548  CD1 ILE A 728     2644   1919   2226   -325    329   -153       C  
ATOM   5549  N   PRO A 729      37.002  -0.329  -3.520  1.00 28.66           N  
ANISOU 5549  N   PRO A 729     3907   3348   3636   -626    317   -371       N  
ATOM   5550  CA  PRO A 729      38.014  -1.302  -3.968  1.00 20.89           C  
ANISOU 5550  CA  PRO A 729     2848   2431   2659   -649    273   -362       C  
ATOM   5551  C   PRO A 729      37.418  -2.591  -4.541  1.00 21.74           C  
ANISOU 5551  C   PRO A 729     2932   2578   2749   -574    228   -269       C  
ATOM   5552  O   PRO A 729      36.309  -2.968  -4.189  1.00 17.57           O  
ANISOU 5552  O   PRO A 729     2422   2062   2192   -512    209   -225       O  
ATOM   5553  CB  PRO A 729      38.818  -1.610  -2.686  1.00 19.31           C  
ANISOU 5553  CB  PRO A 729     2582   2327   2427   -687    214   -441       C  
ATOM   5554  CG  PRO A 729      38.048  -0.994  -1.557  1.00 21.01           C  
ANISOU 5554  CG  PRO A 729     2843   2535   2604   -673    221   -477       C  
ATOM   5555  CD  PRO A 729      37.217   0.109  -2.129  1.00 20.96           C  
ANISOU 5555  CD  PRO A 729     2924   2410   2630   -661    302   -458       C  
ATOM   5556  N   ALA A 730      38.136  -3.257  -5.436  1.00 17.70           N  
ANISOU 5556  N   ALA A 730     2380   2086   2259   -583    215   -244       N  
ATOM   5557  CA  ALA A 730      37.654  -4.547  -5.921  1.00 19.14           C  
ANISOU 5557  CA  ALA A 730     2539   2309   2425   -518    167   -167       C  
ATOM   5558  C   ALA A 730      37.670  -5.490  -4.735  1.00 16.79           C  
ANISOU 5558  C   ALA A 730     2193   2102   2084   -497     94   -176       C  
ATOM   5559  O   ALA A 730      38.656  -5.562  -4.015  1.00 19.80           O  
ANISOU 5559  O   ALA A 730     2527   2541   2455   -536     62   -237       O  
ATOM   5560  CB  ALA A 730      38.542  -5.084  -7.025  1.00 16.78           C  
ANISOU 5560  CB  ALA A 730     2204   2017   2155   -533    168   -152       C  
ATOM   5561  N   GLY A 731      36.573  -6.195  -4.513  1.00 25.31           N  
ANISOU 5561  N   GLY A 731     3286   3196   3135   -437     69   -117       N  
ATOM   5562  CA  GLY A 731      36.505  -7.116  -3.394  1.00 23.81           C  
ANISOU 5562  CA  GLY A 731     3067   3083   2897   -415     10   -113       C  
ATOM   5563  C   GLY A 731      35.583  -6.690  -2.270  1.00 23.81           C  
ANISOU 5563  C   GLY A 731     3102   3087   2855   -401     23   -125       C  
ATOM   5564  O   GLY A 731      35.383  -7.465  -1.333  1.00 20.91           O  
ANISOU 5564  O   GLY A 731     2726   2780   2439   -379    -17   -112       O  
ATOM   5565  N   THR A 732      35.002  -5.486  -2.336  1.00 16.75           N  
ANISOU 5565  N   THR A 732     2256   2131   1979   -409     82   -148       N  
ATOM   5566  CA  THR A 732      34.156  -5.074  -1.219  1.00 22.43           C  
ANISOU 5566  CA  THR A 732     3006   2858   2658   -394     99   -168       C  
ATOM   5567  C   THR A 732      32.835  -5.813  -1.220  1.00 20.43           C  
ANISOU 5567  C   THR A 732     2757   2614   2392   -335     99    -99       C  
ATOM   5568  O   THR A 732      32.169  -5.908  -2.240  1.00 20.03           O  
ANISOU 5568  O   THR A 732     2711   2522   2379   -304    116    -50       O  
ATOM   5569  CB  THR A 732      33.944  -3.523  -1.032  1.00 28.43           C  
ANISOU 5569  CB  THR A 732     3817   3549   3435   -418    162   -229       C  
ATOM   5570  CG2 THR A 732      35.013  -2.722  -1.675  1.00 18.01           C  
ANISOU 5570  CG2 THR A 732     2502   2181   2160   -476    187   -276       C  
ATOM   5571  OG1 THR A 732      32.666  -3.119  -1.521  1.00 35.83           O  
ANISOU 5571  OG1 THR A 732     4793   4427   4394   -366    206   -187       O  
ATOM   5572  N   THR A 733      32.477  -6.321  -0.043  1.00 16.84           N  
ANISOU 5572  N   THR A 733     2301   2217   1880   -324     82    -99       N  
ATOM   5573  CA  THR A 733      31.327  -7.192   0.143  1.00 16.57           C  
ANISOU 5573  CA  THR A 733     2263   2203   1829   -282     84    -38       C  
ATOM   5574  C   THR A 733      30.415  -6.630   1.230  1.00 19.09           C  
ANISOU 5574  C   THR A 733     2611   2532   2109   -270    128    -65       C  
ATOM   5575  O   THR A 733      30.882  -6.163   2.276  1.00 18.78           O  
ANISOU 5575  O   THR A 733     2592   2522   2020   -293    127   -122       O  
ATOM   5576  CB  THR A 733      31.805  -8.591   0.559  1.00 19.43           C  
ANISOU 5576  CB  THR A 733     2602   2628   2152   -279     28      0       C  
ATOM   5577  CG2 THR A 733      30.683  -9.608   0.504  1.00 18.34           C  
ANISOU 5577  CG2 THR A 733     2458   2497   2013   -247     36     69       C  
ATOM   5578  OG1 THR A 733      32.846  -9.000  -0.327  1.00 26.04           O  
ANISOU 5578  OG1 THR A 733     3410   3463   3023   -291    -12      7       O  
ATOM   5579  N   VAL A 734      29.114  -6.668   0.973  1.00 16.95           N  
ANISOU 5579  N   VAL A 734     2339   2241   1862   -233    166    -30       N  
ATOM   5580  CA  VAL A 734      28.105  -6.216   1.927  1.00 17.47           C  
ANISOU 5580  CA  VAL A 734     2423   2319   1897   -215    217    -53       C  
ATOM   5581  C   VAL A 734      27.040  -7.289   2.069  1.00 20.91           C  
ANISOU 5581  C   VAL A 734     2831   2787   2326   -192    227      6       C  
ATOM   5582  O   VAL A 734      26.445  -7.715   1.063  1.00 16.91           O  
ANISOU 5582  O   VAL A 734     2292   2258   1874   -170    223     50       O  
ATOM   5583  CB  VAL A 734      27.402  -4.935   1.443  1.00 23.09           C  
ANISOU 5583  CB  VAL A 734     3153   2963   2656   -187    269    -84       C  
ATOM   5584  CG1 VAL A 734      26.266  -4.564   2.381  1.00 26.29           C  
ANISOU 5584  CG1 VAL A 734     3568   3386   3036   -160    325   -107       C  
ATOM   5585  CG2 VAL A 734      28.402  -3.787   1.320  1.00 17.98           C  
ANISOU 5585  CG2 VAL A 734     2543   2267   2020   -219    273   -145       C  
ATOM   5586  N   ASP A 735      26.794  -7.722   3.307  1.00 20.61           N  
ANISOU 5586  N   ASP A 735     2808   2802   2220   -200    243      5       N  
ATOM   5587  CA  ASP A 735      25.763  -8.728   3.570  1.00 21.62           C  
ANISOU 5587  CA  ASP A 735     2916   2959   2341   -190    269     58       C  
ATOM   5588  C   ASP A 735      24.890  -8.400   4.775  1.00 26.83           C  
ANISOU 5588  C   ASP A 735     3595   3651   2949   -184    337     32       C  
ATOM   5589  O   ASP A 735      24.210  -9.274   5.323  1.00 27.50           O  
ANISOU 5589  O   ASP A 735     3674   3768   3005   -189    368     71       O  
ATOM   5590  CB  ASP A 735      26.353 -10.149   3.673  1.00 20.25           C  
ANISOU 5590  CB  ASP A 735     2742   2816   2136   -207    221    116       C  
ATOM   5591  CG  ASP A 735      27.318 -10.320   4.833  1.00 25.28           C  
ANISOU 5591  CG  ASP A 735     3425   3499   2680   -223    191     98       C  
ATOM   5592  OD1 ASP A 735      27.716 -11.485   5.066  1.00 27.52           O  
ANISOU 5592  OD1 ASP A 735     3719   3808   2929   -225    155    149       O  
ATOM   5593  OD2 ASP A 735      27.671  -9.323   5.518  1.00 20.50           O1-
ANISOU 5593  OD2 ASP A 735     2847   2906   2035   -229    201     33       O1-
ATOM   5594  N   THR A 736      24.905  -7.129   5.164  1.00 19.03           N  
ANISOU 5594  N   THR A 736     2632   2646   1951   -176    367    -37       N  
ATOM   5595  CA  THR A 736      24.054  -6.629   6.227  1.00 23.13           C  
ANISOU 5595  CA  THR A 736     3171   3191   2426   -164    438    -75       C  
ATOM   5596  C   THR A 736      23.410  -5.324   5.816  1.00 23.26           C  
ANISOU 5596  C   THR A 736     3181   3156   2502   -128    483   -127       C  
ATOM   5597  O   THR A 736      23.847  -4.673   4.856  1.00 19.65           O  
ANISOU 5597  O   THR A 736     2724   2641   2102   -118    455   -139       O  
ATOM   5598  CB  THR A 736      24.856  -6.352   7.521  1.00 26.79           C  
ANISOU 5598  CB  THR A 736     3694   3696   2787   -187    431   -123       C  
ATOM   5599  CG2 THR A 736      25.462  -7.638   8.062  1.00 20.43           C  
ANISOU 5599  CG2 THR A 736     2907   2944   1911   -209    386    -69       C  
ATOM   5600  OG1 THR A 736      25.899  -5.404   7.240  1.00 20.37           O  
ANISOU 5600  OG1 THR A 736     2902   2848   1989   -201    392   -182       O  
ATOM   5601  N   ASN A 737      22.364  -4.948   6.555  1.00 21.36           N  
ANISOU 5601  N   ASN A 737     2938   2935   2243   -104    556   -156       N  
ATOM   5602  CA  ASN A 737      21.835  -3.584   6.507  1.00 27.68           C  
ANISOU 5602  CA  ASN A 737     3750   3689   3079    -63    604   -221       C  
ATOM   5603  C   ASN A 737      21.010  -3.269   5.260  1.00 24.16           C  
ANISOU 5603  C   ASN A 737     3253   3193   2733    -10    608   -202       C  
ATOM   5604  O   ASN A 737      19.828  -2.949   5.368  1.00 22.99           O  
ANISOU 5604  O   ASN A 737     3069   3050   2614     36    664   -219       O  
ATOM   5605  CB  ASN A 737      22.968  -2.563   6.701  1.00 35.70           C  
ANISOU 5605  CB  ASN A 737     4829   4665   4072    -85    580   -285       C  
ATOM   5606  CG  ASN A 737      22.469  -1.205   7.124  1.00 52.35           C  
ANISOU 5606  CG  ASN A 737     6972   6732   6188    -51    642   -365       C  
ATOM   5607  ND2 ASN A 737      23.253  -0.524   7.960  1.00 57.74           N  
ANISOU 5607  ND2 ASN A 737     7715   7413   6812    -83    643   -437       N  
ATOM   5608  OD1 ASN A 737      21.397  -0.763   6.709  1.00 55.77           O  
ANISOU 5608  OD1 ASN A 737     7377   7136   6678      7    686   -367       O  
ATOM   5609  N   ILE A 738      21.615  -3.349   4.080  1.00 21.84           N  
ANISOU 5609  N   ILE A 738     2955   2856   2489    -12    548   -168       N  
ATOM   5610  CA  ILE A 738      20.854  -3.074   2.864  1.00 20.05           C  
ANISOU 5610  CA  ILE A 738     2687   2586   2344     46    542   -146       C  
ATOM   5611  C   ILE A 738      20.361  -4.362   2.192  1.00 21.20           C  
ANISOU 5611  C   ILE A 738     2762   2769   2522     43    511    -80       C  
ATOM   5612  O   ILE A 738      19.598  -4.315   1.227  1.00 26.65           O  
ANISOU 5612  O   ILE A 738     3407   3443   3276     92    500    -63       O  
ATOM   5613  CB  ILE A 738      21.633  -2.192   1.870  1.00 19.78           C  
ANISOU 5613  CB  ILE A 738     2699   2469   2347     58    509   -154       C  
ATOM   5614  CG1 ILE A 738      22.940  -2.878   1.461  1.00 21.86           C  
ANISOU 5614  CG1 ILE A 738     2976   2736   2594     -2    447   -120       C  
ATOM   5615  CG2 ILE A 738      21.887  -0.826   2.480  1.00 20.47           C  
ANISOU 5615  CG2 ILE A 738     2853   2505   2419     66    552   -227       C  
ATOM   5616  CD1 ILE A 738      23.679  -2.179   0.329  1.00 24.47           C  
ANISOU 5616  CD1 ILE A 738     3344   2989   2965      3    422   -116       C  
ATOM   5617  N   THR A 739      20.778  -5.508   2.727  1.00 22.53           N  
ANISOU 5617  N   THR A 739     2927   2989   2645    -12    495    -46       N  
ATOM   5618  CA  THR A 739      20.388  -6.800   2.171  1.00 21.79           C  
ANISOU 5618  CA  THR A 739     2776   2924   2580    -27    469     13       C  
ATOM   5619  C   THR A 739      19.075  -7.333   2.763  1.00 23.79           C  
ANISOU 5619  C   THR A 739     2972   3227   2840    -24    531     15       C  
ATOM   5620  O   THR A 739      18.410  -6.651   3.561  1.00 20.21           O  
ANISOU 5620  O   THR A 739     2518   2790   2371     -2    597    -30       O  
ATOM   5621  CB  THR A 739      21.523  -7.817   2.319  1.00 22.31           C  
ANISOU 5621  CB  THR A 739     2870   3005   2600    -82    419     54       C  
ATOM   5622  CG2 THR A 739      22.690  -7.412   1.405  1.00 17.80           C  
ANISOU 5622  CG2 THR A 739     2328   2387   2047    -83    358     54       C  
ATOM   5623  OG1 THR A 739      21.983  -7.831   3.680  1.00 25.52           O  
ANISOU 5623  OG1 THR A 739     3326   3448   2923   -113    443     34       O  
ATOM   5624  N   HIS A 740      18.688  -8.531   2.345  1.00 19.84           N  
ANISOU 5624  N   HIS A 740     2420   2749   2368    -48    516     62       N  
ATOM   5625  CA  HIS A 740      17.410  -9.113   2.760  1.00 19.89           C  
ANISOU 5625  CA  HIS A 740     2360   2801   2397    -57    579     63       C  
ATOM   5626  C   HIS A 740      17.380  -9.318   4.278  1.00 22.09           C  
ANISOU 5626  C   HIS A 740     2680   3120   2594    -95    650     57       C  
ATOM   5627  O   HIS A 740      18.403  -9.652   4.876  1.00 20.34           O  
ANISOU 5627  O   HIS A 740     2531   2900   2298   -129    628     79       O  
ATOM   5628  CB  HIS A 740      17.176 -10.449   2.054  1.00 24.30           C  
ANISOU 5628  CB  HIS A 740     2867   3367   2998    -91    546    113       C  
ATOM   5629  CG  HIS A 740      15.744 -10.882   2.044  1.00 26.24           C  
ANISOU 5629  CG  HIS A 740     3019   3651   3302    -94    601    101       C  
ATOM   5630  CD2 HIS A 740      14.792 -10.791   1.085  1.00 21.93           C  
ANISOU 5630  CD2 HIS A 740     2380   3112   2840    -56    584     80       C  
ATOM   5631  ND1 HIS A 740      15.141 -11.487   3.127  1.00 27.11           N  
ANISOU 5631  ND1 HIS A 740     3117   3800   3382   -142    685    106       N  
ATOM   5632  CE1 HIS A 740      13.880 -11.750   2.836  1.00 25.04           C  
ANISOU 5632  CE1 HIS A 740     2753   3569   3193   -141    724     85       C  
ATOM   5633  NE2 HIS A 740      13.646 -11.344   1.599  1.00 25.68           N  
ANISOU 5633  NE2 HIS A 740     2779   3634   3344    -87    657     66       N  
ATOM   5634  N   PRO A 741      16.215  -9.088   4.898  1.00 21.39           N  
ANISOU 5634  N   PRO A 741     2546   3067   2514    -84    735     24       N  
ATOM   5635  CA  PRO A 741      15.994  -9.275   6.340  1.00 23.73           C  
ANISOU 5635  CA  PRO A 741     2880   3406   2730   -117    819     17       C  
ATOM   5636  C   PRO A 741      16.175 -10.720   6.843  1.00 26.86           C  
ANISOU 5636  C   PRO A 741     3301   3824   3080   -187    834     83       C  
ATOM   5637  O   PRO A 741      16.545 -10.886   7.995  1.00 24.69           O  
ANISOU 5637  O   PRO A 741     3100   3573   2707   -212    872     92       O  
ATOM   5638  CB  PRO A 741      14.537  -8.827   6.538  1.00 23.08           C  
ANISOU 5638  CB  PRO A 741     2714   3357   2699    -86    906    -31       C  
ATOM   5639  CG  PRO A 741      13.917  -8.899   5.176  1.00 25.11           C  
ANISOU 5639  CG  PRO A 741     2874   3598   3067    -52    859    -31       C  
ATOM   5640  CD  PRO A 741      15.026  -8.529   4.234  1.00 21.76           C  
ANISOU 5640  CD  PRO A 741     2501   3118   2650    -28    756    -14       C  
ATOM   5641  N   PHE A 742      15.933 -11.743   6.028  1.00 21.92           N  
ANISOU 5641  N   PHE A 742     2624   3188   2517   -214    805    128       N  
ATOM   5642  CA  PHE A 742      16.168 -13.097   6.529  1.00 31.24           C  
ANISOU 5642  CA  PHE A 742     3846   4374   3652   -278    821    194       C  
ATOM   5643  C   PHE A 742      16.749 -14.108   5.541  1.00 30.76           C  
ANISOU 5643  C   PHE A 742     3780   4274   3632   -300    739    247       C  
ATOM   5644  O   PHE A 742      17.227 -15.159   5.960  1.00 28.12           O  
ANISOU 5644  O   PHE A 742     3504   3931   3250   -342    737    305       O  
ATOM   5645  CB  PHE A 742      14.925 -13.663   7.242  1.00 26.96           C  
ANISOU 5645  CB  PHE A 742     3260   3868   3116   -321    938    197       C  
ATOM   5646  CG  PHE A 742      13.663 -13.571   6.439  1.00 33.08           C  
ANISOU 5646  CG  PHE A 742     3904   4656   4008   -311    964    159       C  
ATOM   5647  CD1 PHE A 742      13.348 -14.541   5.495  1.00 42.14           C  
ANISOU 5647  CD1 PHE A 742     4987   5786   5237   -345    931    186       C  
ATOM   5648  CD2 PHE A 742      12.785 -12.511   6.624  1.00 29.37           C  
ANISOU 5648  CD2 PHE A 742     3371   4219   3568   -264   1019     89       C  
ATOM   5649  CE1 PHE A 742      12.178 -14.455   4.746  1.00 40.55           C  
ANISOU 5649  CE1 PHE A 742     4656   5606   5143   -334    945    142       C  
ATOM   5650  CE2 PHE A 742      11.610 -12.421   5.879  1.00 33.46           C  
ANISOU 5650  CE2 PHE A 742     3759   4758   4196   -245   1035     49       C  
ATOM   5651  CZ  PHE A 742      11.308 -13.397   4.942  1.00 37.56           C  
ANISOU 5651  CZ  PHE A 742     4211   5268   4794   -281    995     74       C  
ATOM   5652  N   GLU A 743      16.734 -13.790   4.248  1.00 27.39           N  
ANISOU 5652  N   GLU A 743     3295   3823   3289   -266    672    229       N  
ATOM   5653  CA  GLU A 743      17.280 -14.708   3.243  1.00 19.96           C  
ANISOU 5653  CA  GLU A 743     2350   2848   2387   -283    595    271       C  
ATOM   5654  C   GLU A 743      18.749 -14.462   2.916  1.00 19.15           C  
ANISOU 5654  C   GLU A 743     2316   2716   2244   -261    508    285       C  
ATOM   5655  O   GLU A 743      19.344 -13.470   3.335  1.00 19.07           O  
ANISOU 5655  O   GLU A 743     2350   2710   2187   -233    500    255       O  
ATOM   5656  CB  GLU A 743      16.398 -14.753   1.977  1.00 19.84           C  
ANISOU 5656  CB  GLU A 743     2232   2828   2480   -267    570    248       C  
ATOM   5657  CG  GLU A 743      15.041 -15.402   2.257  1.00 30.78           C  
ANISOU 5657  CG  GLU A 743     3537   4243   3913   -310    651    240       C  
ATOM   5658  CD  GLU A 743      14.080 -15.404   1.077  1.00 42.86           C  
ANISOU 5658  CD  GLU A 743     4952   5784   5550   -290    623    203       C  
ATOM   5659  OE1 GLU A 743      14.212 -14.558   0.171  1.00 41.55           O  
ANISOU 5659  OE1 GLU A 743     4765   5609   5413   -223    557    175       O  
ATOM   5660  OE2 GLU A 743      13.173 -16.265   1.069  1.00 53.42           O1-
ANISOU 5660  OE2 GLU A 743     6220   7138   6939   -343    668    200       O1-
ATOM   5661  N   PHE A 744      19.332 -15.390   2.170  1.00 18.63           N  
ANISOU 5661  N   PHE A 744     2257   2621   2200   -277    446    325       N  
ATOM   5662  CA  PHE A 744      20.773 -15.437   1.946  1.00 17.99           C  
ANISOU 5662  CA  PHE A 744     2237   2518   2080   -266    371    343       C  
ATOM   5663  C   PHE A 744      21.164 -14.674   0.658  1.00 20.77           C  
ANISOU 5663  C   PHE A 744     2561   2846   2486   -226    307    315       C  
ATOM   5664  O   PHE A 744      21.146 -15.231  -0.447  1.00 20.00           O  
ANISOU 5664  O   PHE A 744     2430   2726   2444   -224    264    329       O  
ATOM   5665  CB  PHE A 744      21.195 -16.913   1.904  1.00 17.95           C  
ANISOU 5665  CB  PHE A 744     2261   2493   2067   -300    347    403       C  
ATOM   5666  CG  PHE A 744      22.680 -17.154   1.967  1.00 23.28           C  
ANISOU 5666  CG  PHE A 744     2999   3157   2689   -287    277    425       C  
ATOM   5667  CD1 PHE A 744      23.583 -16.111   2.135  1.00 19.76           C  
ANISOU 5667  CD1 PHE A 744     2579   2724   2205   -259    244    389       C  
ATOM   5668  CD2 PHE A 744      23.172 -18.451   1.848  1.00 17.53           C  
ANISOU 5668  CD2 PHE A 744     2302   2402   1955   -303    246    478       C  
ATOM   5669  CE1 PHE A 744      24.941 -16.358   2.189  1.00 17.03           C  
ANISOU 5669  CE1 PHE A 744     2275   2377   1819   -249    179    401       C  
ATOM   5670  CE2 PHE A 744      24.524 -18.702   1.899  1.00 17.26           C  
ANISOU 5670  CE2 PHE A 744     2316   2364   1878   -283    180    494       C  
ATOM   5671  CZ  PHE A 744      25.413 -17.649   2.065  1.00 20.43           C  
ANISOU 5671  CZ  PHE A 744     2729   2789   2243   -256    145    453       C  
ATOM   5672  N   ASP A 745      21.514 -13.396   0.816  1.00 20.28           N  
ANISOU 5672  N   ASP A 745     2518   2784   2403   -195    307    273       N  
ATOM   5673  CA  ASP A 745      21.919 -12.544  -0.304  1.00 19.51           C  
ANISOU 5673  CA  ASP A 745     2412   2655   2347   -158    261    249       C  
ATOM   5674  C   ASP A 745      23.072 -11.603   0.076  1.00 21.26           C  
ANISOU 5674  C   ASP A 745     2691   2867   2520   -153    244    221       C  
ATOM   5675  O   ASP A 745      23.220 -11.225   1.245  1.00 24.91           O  
ANISOU 5675  O   ASP A 745     3189   3352   2924   -164    277    199       O  
ATOM   5676  CB  ASP A 745      20.720 -11.760  -0.863  1.00 19.36           C  
ANISOU 5676  CB  ASP A 745     2338   2633   2385   -117    288    217       C  
ATOM   5677  CG  ASP A 745      20.315 -10.558   0.012  1.00 25.96           C  
ANISOU 5677  CG  ASP A 745     3189   3478   3196    -93    345    170       C  
ATOM   5678  OD1 ASP A 745      20.380 -10.646   1.257  1.00 29.57           O  
ANISOU 5678  OD1 ASP A 745     3677   3963   3594   -120    389    165       O  
ATOM   5679  OD2 ASP A 745      19.919  -9.515  -0.560  1.00 24.99           O1-
ANISOU 5679  OD2 ASP A 745     3053   3332   3110    -42    347    139       O1-
ATOM   5680  N   PHE A 746      23.910 -11.260  -0.896  1.00 18.33           N  
ANISOU 5680  N   PHE A 746     2330   2463   2172   -142    195    217       N  
ATOM   5681  CA  PHE A 746      24.996 -10.304  -0.662  1.00 16.05           C  
ANISOU 5681  CA  PHE A 746     2086   2160   1853   -146    184    181       C  
ATOM   5682  C   PHE A 746      25.388  -9.493  -1.902  1.00 19.43           C  
ANISOU 5682  C   PHE A 746     2518   2539   2325   -124    163    167       C  
ATOM   5683  O   PHE A 746      25.154  -9.899  -3.048  1.00 16.08           O  
ANISOU 5683  O   PHE A 746     2068   2096   1944   -106    136    195       O  
ATOM   5684  CB  PHE A 746      26.240 -10.988  -0.066  1.00 15.97           C  
ANISOU 5684  CB  PHE A 746     2104   2176   1789   -178    145    192       C  
ATOM   5685  CG  PHE A 746      26.827 -12.076  -0.941  1.00 15.47           C  
ANISOU 5685  CG  PHE A 746     2024   2104   1750   -183     91    234       C  
ATOM   5686  CD1 PHE A 746      27.803 -11.781  -1.886  1.00 15.08           C  
ANISOU 5686  CD1 PHE A 746     1975   2030   1726   -182     54    224       C  
ATOM   5687  CD2 PHE A 746      26.396 -13.396  -0.821  1.00 17.53           C  
ANISOU 5687  CD2 PHE A 746     2272   2378   2010   -191     85    282       C  
ATOM   5688  CE1 PHE A 746      28.337 -12.788  -2.703  1.00 14.69           C  
ANISOU 5688  CE1 PHE A 746     1909   1973   1697   -183      9    257       C  
ATOM   5689  CE2 PHE A 746      26.935 -14.411  -1.622  1.00 16.00           C  
ANISOU 5689  CE2 PHE A 746     2069   2171   1841   -193     38    316       C  
ATOM   5690  CZ  PHE A 746      27.899 -14.107  -2.563  1.00 16.06           C  
ANISOU 5690  CZ  PHE A 746     2073   2159   1871   -186     -2    302       C  
ATOM   5691  N   TYR A 747      25.998  -8.342  -1.655  1.00 21.90           N  
ANISOU 5691  N   TYR A 747     2869   2828   2625   -128    177    124       N  
ATOM   5692  CA  TYR A 747      26.595  -7.576  -2.718  1.00 15.73           C  
ANISOU 5692  CA  TYR A 747     2107   1993   1875   -120    166    113       C  
ATOM   5693  C   TYR A 747      28.072  -7.821  -2.699  1.00 24.01           C  
ANISOU 5693  C   TYR A 747     3169   3050   2904   -163    132    104       C  
ATOM   5694  O   TYR A 747      28.689  -7.834  -1.633  1.00 15.79           O  
ANISOU 5694  O   TYR A 747     2139   2043   1818   -194    128     76       O  
ATOM   5695  CB  TYR A 747      26.344  -6.094  -2.530  1.00 16.21           C  
ANISOU 5695  CB  TYR A 747     2207   2009   1943   -101    212     67       C  
ATOM   5696  CG  TYR A 747      24.915  -5.696  -2.757  1.00 16.50           C  
ANISOU 5696  CG  TYR A 747     2227   2031   2010    -42    243     71       C  
ATOM   5697  CD1 TYR A 747      24.453  -5.400  -4.028  1.00 18.10           C  
ANISOU 5697  CD1 TYR A 747     2429   2192   2256      7    231     94       C  
ATOM   5698  CD2 TYR A 747      24.035  -5.593  -1.700  1.00 16.96           C  
ANISOU 5698  CD2 TYR A 747     2272   2123   2051    -30    283     49       C  
ATOM   5699  CE1 TYR A 747      23.143  -5.024  -4.241  1.00 16.79           C  
ANISOU 5699  CE1 TYR A 747     2240   2021   2118     72    250     93       C  
ATOM   5700  CE2 TYR A 747      22.736  -5.213  -1.895  1.00 20.03           C  
ANISOU 5700  CE2 TYR A 747     2633   2505   2472     28    311     44       C  
ATOM   5701  CZ  TYR A 747      22.286  -4.936  -3.167  1.00 22.87           C  
ANISOU 5701  CZ  TYR A 747     2984   2827   2879     81    291     65       C  
ATOM   5702  OH  TYR A 747      20.978  -4.559  -3.355  1.00 24.44           O  
ANISOU 5702  OH  TYR A 747     3146   3027   3111    149    311     56       O  
ATOM   5703  N   LEU A 748      28.635  -8.021  -3.886  1.00 15.15           N  
ANISOU 5703  N   LEU A 748     2042   1901   1812   -163    106    125       N  
ATOM   5704  CA  LEU A 748      30.068  -8.154  -4.021  1.00 16.46           C  
ANISOU 5704  CA  LEU A 748     2209   2073   1970   -202     79    109       C  
ATOM   5705  C   LEU A 748      30.505  -7.385  -5.249  1.00 20.93           C  
ANISOU 5705  C   LEU A 748     2799   2581   2573   -201     95    105       C  
ATOM   5706  O   LEU A 748      30.152  -7.736  -6.377  1.00 17.42           O  
ANISOU 5706  O   LEU A 748     2350   2116   2153   -172     84    144       O  
ATOM   5707  CB  LEU A 748      30.486  -9.619  -4.138  1.00 14.68           C  
ANISOU 5707  CB  LEU A 748     1951   1890   1737   -206     29    147       C  
ATOM   5708  CG  LEU A 748      31.896  -9.827  -4.706  1.00 18.85           C  
ANISOU 5708  CG  LEU A 748     2468   2421   2274   -231      0    135       C  
ATOM   5709  CD1 LEU A 748      32.955  -9.163  -3.838  1.00 22.99           C  
ANISOU 5709  CD1 LEU A 748     2996   2966   2774   -272      0     75       C  
ATOM   5710  CD2 LEU A 748      32.180 -11.319  -4.854  1.00 22.00           C  
ANISOU 5710  CD2 LEU A 748     2837   2853   2668   -222    -48    174       C  
ATOM   5711  N   CYS A 749      31.254  -6.318  -5.025  1.00 19.70           N  
ANISOU 5711  N   CYS A 749     2672   2395   2418   -236    124     56       N  
ATOM   5712  CA  CYS A 749      31.817  -5.578  -6.134  1.00 21.58           C  
ANISOU 5712  CA  CYS A 749     2941   2571   2686   -248    150     53       C  
ATOM   5713  C   CYS A 749      33.182  -6.208  -6.421  1.00 23.48           C  
ANISOU 5713  C   CYS A 749     3148   2844   2930   -292    122     43       C  
ATOM   5714  O   CYS A 749      34.168  -5.927  -5.742  1.00 25.65           O  
ANISOU 5714  O   CYS A 749     3408   3141   3196   -342    121    -11       O  
ATOM   5715  CB  CYS A 749      31.954  -4.103  -5.791  1.00 16.09           C  
ANISOU 5715  CB  CYS A 749     2298   1817   1999   -271    205      1       C  
ATOM   5716  SG  CYS A 749      32.537  -3.121  -7.178  1.00 23.43           S  
ANISOU 5716  SG  CYS A 749     3286   2653   2964   -286    255      7       S  
ATOM   5717  N   SER A 750      33.222  -7.090  -7.408  1.00 19.84           N  
ANISOU 5717  N   SER A 750     2667   2390   2479   -270     96     88       N  
ATOM   5718  CA  SER A 750      34.391  -7.941  -7.606  1.00 21.84           C  
ANISOU 5718  CA  SER A 750     2878   2687   2735   -297     62     81       C  
ATOM   5719  C   SER A 750      35.489  -7.262  -8.415  1.00 16.53           C  
ANISOU 5719  C   SER A 750     2215   1979   2087   -340    100     53       C  
ATOM   5720  O   SER A 750      36.636  -7.697  -8.399  1.00 17.66           O  
ANISOU 5720  O   SER A 750     2314   2161   2237   -373     82     25       O  
ATOM   5721  CB  SER A 750      33.977  -9.260  -8.263  1.00 17.58           C  
ANISOU 5721  CB  SER A 750     2314   2169   2196   -256     21    135       C  
ATOM   5722  OG  SER A 750      33.079  -9.003  -9.331  1.00 28.22           O  
ANISOU 5722  OG  SER A 750     3694   3470   3557   -218     39    172       O  
ATOM   5723  N   HIS A 751      35.147  -6.169  -9.076  1.00 15.30           N  
ANISOU 5723  N   HIS A 751     2118   1749   1945   -339    155     58       N  
ATOM   5724  CA  HIS A 751      36.034  -5.554 -10.061  1.00 24.33           C  
ANISOU 5724  CA  HIS A 751     3288   2846   3111   -377    205     46       C  
ATOM   5725  C   HIS A 751      36.482  -4.161  -9.672  1.00 23.44           C  
ANISOU 5725  C   HIS A 751     3214   2678   3014   -434    268     -8       C  
ATOM   5726  O   HIS A 751      35.801  -3.465  -8.912  1.00 21.81           O  
ANISOU 5726  O   HIS A 751     3039   2446   2801   -424    280    -24       O  
ATOM   5727  CB  HIS A 751      35.306  -5.431 -11.406  1.00 18.85           C  
ANISOU 5727  CB  HIS A 751     2651   2097   2415   -325    226    106       C  
ATOM   5728  CG  HIS A 751      34.069  -4.587 -11.328  1.00 23.25           C  
ANISOU 5728  CG  HIS A 751     3270   2599   2966   -276    246    127       C  
ATOM   5729  CD2 HIS A 751      33.830  -3.320 -11.731  1.00 25.41           C  
ANISOU 5729  CD2 HIS A 751     3624   2786   3245   -270    306    130       C  
ATOM   5730  ND1 HIS A 751      32.900  -5.034 -10.748  1.00 23.44           N  
ANISOU 5730  ND1 HIS A 751     3273   2655   2979   -223    205    146       N  
ATOM   5731  CE1 HIS A 751      31.983  -4.087 -10.831  1.00 21.58           C  
ANISOU 5731  CE1 HIS A 751     3094   2362   2744   -181    234    156       C  
ATOM   5732  NE2 HIS A 751      32.520  -3.035 -11.418  1.00 21.93           N  
ANISOU 5732  NE2 HIS A 751     3206   2331   2797   -204    293    149       N  
ATOM   5733  N   ALA A 752      37.618  -3.758 -10.243  1.00 26.24           N  
ANISOU 5733  N   ALA A 752     3567   3009   3393   -496    313    -38       N  
ATOM   5734  CA  ALA A 752      38.125  -2.397 -10.132  1.00 24.47           C  
ANISOU 5734  CA  ALA A 752     3390   2715   3194   -563    388    -88       C  
ATOM   5735  C   ALA A 752      37.290  -1.472 -11.002  1.00 25.16           C  
ANISOU 5735  C   ALA A 752     3585   2695   3279   -524    448    -37       C  
ATOM   5736  O   ALA A 752      37.018  -1.782 -12.151  1.00 24.27           O  
ANISOU 5736  O   ALA A 752     3505   2561   3155   -480    454     24       O  
ATOM   5737  CB  ALA A 752      39.597  -2.334 -10.543  1.00 20.08           C  
ANISOU 5737  CB  ALA A 752     2791   2171   2670   -646    425   -136       C  
ATOM   5738  N   GLY A 753      36.868  -0.342 -10.442  1.00 32.25           N  
ANISOU 5738  N   GLY A 753     4543   3526   4185   -532    488    -64       N  
ATOM   5739  CA  GLY A 753      36.098   0.632 -11.196  1.00 28.01           C  
ANISOU 5739  CA  GLY A 753     4117   2879   3646   -487    545    -18       C  
ATOM   5740  C   GLY A 753      37.024   1.442 -12.085  1.00 33.06           C  
ANISOU 5740  C   GLY A 753     4819   3433   4309   -555    635    -24       C  
ATOM   5741  O   GLY A 753      37.937   2.096 -11.593  1.00 40.67           O  
ANISOU 5741  O   GLY A 753     5775   4374   5305   -649    683    -95       O  
ATOM   5742  N   ILE A 754      36.797   1.394 -13.392  1.00 34.49           N  
ANISOU 5742  N   ILE A 754     5063   3571   4471   -509    659     48       N  
ATOM   5743  CA  ILE A 754      37.639   2.109 -14.344  1.00 37.37           C  
ANISOU 5743  CA  ILE A 754     5499   3852   4849   -571    756     55       C  
ATOM   5744  C   ILE A 754      37.031   3.446 -14.692  1.00 36.56           C  
ANISOU 5744  C   ILE A 754     5538   3610   4743   -541    828     87       C  
ATOM   5745  O   ILE A 754      37.730   4.456 -14.753  1.00 45.88           O  
ANISOU 5745  O   ILE A 754     6780   4698   5953   -624    921     54       O  
ATOM   5746  CB  ILE A 754      37.801   1.338 -15.670  1.00 43.10           C  
ANISOU 5746  CB  ILE A 754     6231   4601   5543   -536    752    119       C  
ATOM   5747  CG1 ILE A 754      38.493  -0.004 -15.449  1.00 45.28           C  
ANISOU 5747  CG1 ILE A 754     6375   5004   5825   -562    688     90       C  
ATOM   5748  CG2 ILE A 754      38.583   2.170 -16.671  1.00 42.76           C  
ANISOU 5748  CG2 ILE A 754     6280   4461   5505   -597    866    134       C  
ATOM   5749  CD1 ILE A 754      38.663  -0.798 -16.726  1.00 48.61           C  
ANISOU 5749  CD1 ILE A 754     6801   5451   6216   -528    685    143       C  
ATOM   5750  N   GLN A 755      35.726   3.447 -14.946  1.00 28.91           N  
ANISOU 5750  N   GLN A 755     4620   2622   3740   -422    785    149       N  
ATOM   5751  CA  GLN A 755      35.040   4.669 -15.336  1.00 39.71           C  
ANISOU 5751  CA  GLN A 755     6129   3859   5101   -367    843    187       C  
ATOM   5752  C   GLN A 755      33.699   4.765 -14.651  1.00 38.49           C  
ANISOU 5752  C   GLN A 755     5970   3714   4938   -266    782    193       C  
ATOM   5753  O   GLN A 755      33.074   3.749 -14.365  1.00 37.21           O  
ANISOU 5753  O   GLN A 755     5718   3658   4761   -211    693    201       O  
ATOM   5754  CB  GLN A 755      34.795   4.695 -16.837  1.00 51.48           C  
ANISOU 5754  CB  GLN A 755     7717   5298   6545   -300    865    278       C  
ATOM   5755  CG  GLN A 755      36.034   4.692 -17.675  1.00 65.76           C  
ANISOU 5755  CG  GLN A 755     9549   7083   8354   -391    943    282       C  
ATOM   5756  CD  GLN A 755      35.749   4.196 -19.068  1.00 75.96           C  
ANISOU 5756  CD  GLN A 755    10896   8382   9584   -314    930    367       C  
ATOM   5757  NE2 GLN A 755      36.806   3.908 -19.824  1.00 76.26           N  
ANISOU 5757  NE2 GLN A 755    10931   8429   9614   -387    987    370       N  
ATOM   5758  OE1 GLN A 755      34.586   4.058 -19.461  1.00 81.33           O  
ANISOU 5758  OE1 GLN A 755    11615   9065  10222   -189    867    424       O  
ATOM   5759  N   GLY A 756      33.252   5.995 -14.420  1.00 32.08           N  
ANISOU 5759  N   GLY A 756     5260   2789   4140   -241    836    187       N  
ATOM   5760  CA  GLY A 756      31.945   6.232 -13.846  1.00 28.88           C  
ANISOU 5760  CA  GLY A 756     4860   2383   3730   -136    791    191       C  
ATOM   5761  C   GLY A 756      31.824   5.606 -12.473  1.00 25.31           C  
ANISOU 5761  C   GLY A 756     4283   2039   3294   -166    734    122       C  
ATOM   5762  O   GLY A 756      32.799   5.498 -11.732  1.00 27.99           O  
ANISOU 5762  O   GLY A 756     4566   2414   3656   -275    749     53       O  
ATOM   5763  N   THR A 757      30.616   5.173 -12.145  1.00 22.09           N  
ANISOU 5763  N   THR A 757     3831   1690   2872    -67    668    139       N  
ATOM   5764  CA  THR A 757      30.351   4.586 -10.861  1.00 20.69           C  
ANISOU 5764  CA  THR A 757     3549   1611   2700    -84    620     84       C  
ATOM   5765  C   THR A 757      30.143   3.095 -11.042  1.00 20.13           C  
ANISOU 5765  C   THR A 757     3373   1668   2610    -64    538    115       C  
ATOM   5766  O   THR A 757      29.324   2.660 -11.856  1.00 19.44           O  
ANISOU 5766  O   THR A 757     3285   1597   2504     24    497    174       O  
ATOM   5767  CB  THR A 757      29.150   5.265 -10.205  1.00 21.14           C  
ANISOU 5767  CB  THR A 757     3633   1635   2763      1    623     68       C  
ATOM   5768  CG2 THR A 757      28.962   4.785  -8.750  1.00 20.74           C  
ANISOU 5768  CG2 THR A 757     3488   1679   2712    -29    593      2       C  
ATOM   5769  OG1 THR A 757      29.370   6.683 -10.206  1.00 24.28           O  
ANISOU 5769  OG1 THR A 757     4148   1895   3182    -12    705     44       O  
ATOM   5770  N   SER A 758      30.925   2.316 -10.302  1.00 19.12           N  
ANISOU 5770  N   SER A 758     3157   1626   2483   -146    512     72       N  
ATOM   5771  CA  SER A 758      30.795   0.870 -10.293  1.00 27.63           C  
ANISOU 5771  CA  SER A 758     4136   2817   3544   -135    438     95       C  
ATOM   5772  C   SER A 758      29.380   0.418  -9.939  1.00 26.22           C  
ANISOU 5772  C   SER A 758     3918   2688   3357    -46    391    115       C  
ATOM   5773  O   SER A 758      28.641   1.120  -9.259  1.00 24.19           O  
ANISOU 5773  O   SER A 758     3681   2403   3105    -10    412     90       O  
ATOM   5774  CB  SER A 758      31.790   0.242  -9.310  1.00 25.16           C  
ANISOU 5774  CB  SER A 758     3746   2582   3232   -225    418     39       C  
ATOM   5775  OG  SER A 758      33.123   0.366  -9.766  1.00 27.92           O  
ANISOU 5775  OG  SER A 758     4102   2912   3595   -306    450     20       O  
ATOM   5776  N   ARG A 759      29.016  -0.751 -10.452  1.00 27.11           N  
ANISOU 5776  N   ARG A 759     3972   2870   3458    -14    332    157       N  
ATOM   5777  CA  ARG A 759      27.788  -1.445 -10.103  1.00 32.74           C  
ANISOU 5777  CA  ARG A 759     4623   3648   4169     49    285    170       C  
ATOM   5778  C   ARG A 759      28.208  -2.675  -9.313  1.00 28.02           C  
ANISOU 5778  C   ARG A 759     3940   3144   3563     -8    247    154       C  
ATOM   5779  O   ARG A 759      28.915  -3.527  -9.830  1.00 28.45           O  
ANISOU 5779  O   ARG A 759     3968   3230   3613    -40    219    173       O  
ATOM   5780  CB  ARG A 759      27.066  -1.918 -11.365  1.00 37.56           C  
ANISOU 5780  CB  ARG A 759     5232   4266   4775    125    244    226       C  
ATOM   5781  CG  ARG A 759      26.583  -0.826 -12.289  1.00 47.67           C  
ANISOU 5781  CG  ARG A 759     6603   5458   6051    201    269    254       C  
ATOM   5782  CD  ARG A 759      26.007  -1.410 -13.578  1.00 54.55           C  
ANISOU 5782  CD  ARG A 759     7471   6350   6906    273    215    305       C  
ATOM   5783  NE  ARG A 759      25.024  -0.516 -14.182  1.00 60.81           N  
ANISOU 5783  NE  ARG A 759     8324   7087   7693    382    215    330       N  
ATOM   5784  CZ  ARG A 759      23.752  -0.457 -13.802  1.00 66.99           C  
ANISOU 5784  CZ  ARG A 759     9059   7901   8491    459    187    318       C  
ATOM   5785  NH1 ARG A 759      23.319  -1.240 -12.823  1.00 69.03           N1+
ANISOU 5785  NH1 ARG A 759     9215   8242   8771    429    166    285       N1+
ATOM   5786  NH2 ARG A 759      22.914   0.383 -14.393  1.00 67.78           N  
ANISOU 5786  NH2 ARG A 759     9216   7951   8586    568    181    339       N  
ATOM   5787  N   PRO A 760      27.811  -2.764  -8.042  1.00 26.79           N  
ANISOU 5787  N   PRO A 760     3748   3029   3401    -19    249    120       N  
ATOM   5788  CA  PRO A 760      28.159  -4.015  -7.366  1.00 29.87           C  
ANISOU 5788  CA  PRO A 760     4070   3504   3776    -62    210    118       C  
ATOM   5789  C   PRO A 760      27.217  -5.135  -7.800  1.00 27.32           C  
ANISOU 5789  C   PRO A 760     3692   3230   3458    -18    166    161       C  
ATOM   5790  O   PRO A 760      26.007  -4.932  -7.822  1.00 28.29           O  
ANISOU 5790  O   PRO A 760     3804   3353   3593     40    170    168       O  
ATOM   5791  CB  PRO A 760      27.979  -3.676  -5.876  1.00 30.31           C  
ANISOU 5791  CB  PRO A 760     4118   3585   3813    -84    233     70       C  
ATOM   5792  CG  PRO A 760      27.027  -2.519  -5.851  1.00 29.40           C  
ANISOU 5792  CG  PRO A 760     4046   3413   3713    -28    276     55       C  
ATOM   5793  CD  PRO A 760      27.156  -1.786  -7.159  1.00 24.20           C  
ANISOU 5793  CD  PRO A 760     3446   2673   3076      4    290     82       C  
ATOM   5794  N   SER A 761      27.752  -6.296  -8.161  1.00 15.05           N  
ANISOU 5794  N   SER A 761     2102   1716   1900    -44    126    185       N  
ATOM   5795  CA  SER A 761      26.875  -7.414  -8.468  1.00 22.74           C  
ANISOU 5795  CA  SER A 761     3024   2733   2882    -14     87    217       C  
ATOM   5796  C   SER A 761      26.137  -7.874  -7.217  1.00 21.85           C  
ANISOU 5796  C   SER A 761     2870   2670   2763    -22     94    206       C  
ATOM   5797  O   SER A 761      26.694  -7.897  -6.119  1.00 17.12           O  
ANISOU 5797  O   SER A 761     2275   2093   2138    -64    107    183       O  
ATOM   5798  CB  SER A 761      27.664  -8.578  -9.036  1.00 22.76           C  
ANISOU 5798  CB  SER A 761     3005   2761   2883    -43     46    239       C  
ATOM   5799  OG  SER A 761      28.047  -8.293 -10.354  1.00 17.93           O  
ANISOU 5799  OG  SER A 761     2426   2111   2276    -24     42    255       O  
ATOM   5800  N   HIS A 762      24.879  -8.251  -7.392  1.00 20.54           N  
ANISOU 5800  N   HIS A 762     2663   2525   2617     18     86    219       N  
ATOM   5801  CA  HIS A 762      24.095  -8.787  -6.291  1.00 16.95           C  
ANISOU 5801  CA  HIS A 762     2165   2117   2157      5    103    212       C  
ATOM   5802  C   HIS A 762      23.872 -10.303  -6.425  1.00 20.24           C  
ANISOU 5802  C   HIS A 762     2534   2574   2584    -18     70    241       C  
ATOM   5803  O   HIS A 762      23.473 -10.794  -7.487  1.00 18.12           O  
ANISOU 5803  O   HIS A 762     2240   2303   2343      5     36    258       O  
ATOM   5804  CB  HIS A 762      22.754  -8.062  -6.208  1.00 18.20           C  
ANISOU 5804  CB  HIS A 762     2301   2274   2339     61    131    193       C  
ATOM   5805  CG  HIS A 762      21.884  -8.546  -5.088  1.00 25.58           C  
ANISOU 5805  CG  HIS A 762     3189   3258   3271     46    163    182       C  
ATOM   5806  CD2 HIS A 762      21.966  -8.350  -3.752  1.00 21.83           C  
ANISOU 5806  CD2 HIS A 762     2728   2803   2761     17    207    160       C  
ATOM   5807  ND1 HIS A 762      20.772  -9.331  -5.298  1.00 27.26           N  
ANISOU 5807  ND1 HIS A 762     3331   3508   3517     58    157    191       N  
ATOM   5808  CE1 HIS A 762      20.200  -9.595  -4.136  1.00 28.09           C  
ANISOU 5808  CE1 HIS A 762     3410   3650   3611     33    203    178       C  
ATOM   5809  NE2 HIS A 762      20.906  -9.018  -3.183  1.00 25.46           N  
ANISOU 5809  NE2 HIS A 762     3132   3310   3232     12    234    162       N  
ATOM   5810  N   TYR A 763      24.114 -11.032  -5.340  1.00 20.12           N  
ANISOU 5810  N   TYR A 763     2513   2591   2542    -62     80    247       N  
ATOM   5811  CA  TYR A 763      23.972 -12.482  -5.337  1.00 14.76           C  
ANISOU 5811  CA  TYR A 763     1803   1935   1869    -89     58    277       C  
ATOM   5812  C   TYR A 763      22.861 -12.953  -4.414  1.00 22.95           C  
ANISOU 5812  C   TYR A 763     2805   3006   2909   -103     98    279       C  
ATOM   5813  O   TYR A 763      22.856 -12.660  -3.214  1.00 20.07           O  
ANISOU 5813  O   TYR A 763     2461   2660   2506   -119    139    268       O  
ATOM   5814  CB  TYR A 763      25.299 -13.152  -4.967  1.00 14.48           C  
ANISOU 5814  CB  TYR A 763     1799   1904   1798   -125     32    293       C  
ATOM   5815  CG  TYR A 763      26.379 -12.803  -5.952  1.00 17.09           C  
ANISOU 5815  CG  TYR A 763     2152   2208   2135   -117      0    289       C  
ATOM   5816  CD1 TYR A 763      26.585 -13.581  -7.090  1.00 16.53           C  
ANISOU 5816  CD1 TYR A 763     2068   2125   2089   -110    -39    309       C  
ATOM   5817  CD2 TYR A 763      27.151 -11.659  -5.788  1.00 15.49           C  
ANISOU 5817  CD2 TYR A 763     1983   1988   1914   -120     15    259       C  
ATOM   5818  CE1 TYR A 763      27.556 -13.245  -8.027  1.00 17.04           C  
ANISOU 5818  CE1 TYR A 763     2153   2166   2155   -104    -58    304       C  
ATOM   5819  CE2 TYR A 763      28.132 -11.310  -6.719  1.00 18.81           C  
ANISOU 5819  CE2 TYR A 763     2422   2381   2344   -121     -2    253       C  
ATOM   5820  CZ  TYR A 763      28.327 -12.112  -7.839  1.00 22.36           C  
ANISOU 5820  CZ  TYR A 763     2860   2824   2814   -112    -36    278       C  
ATOM   5821  OH  TYR A 763      29.290 -11.785  -8.769  1.00 14.09           O  
ANISOU 5821  OH  TYR A 763     1831   1751   1770   -114    -43    272       O  
ATOM   5822  N   TYR A 764      21.917 -13.688  -4.989  1.00 15.33           N  
ANISOU 5822  N   TYR A 764     1787   2050   1988   -101     90    288       N  
ATOM   5823  CA  TYR A 764      20.801 -14.225  -4.237  1.00 16.96           C  
ANISOU 5823  CA  TYR A 764     1948   2286   2208   -124    136    287       C  
ATOM   5824  C   TYR A 764      20.855 -15.751  -4.262  1.00 21.60           C  
ANISOU 5824  C   TYR A 764     2528   2873   2806   -172    123    321       C  
ATOM   5825  O   TYR A 764      20.773 -16.370  -5.340  1.00 21.61           O  
ANISOU 5825  O   TYR A 764     2503   2860   2847   -169     79    326       O  
ATOM   5826  CB  TYR A 764      19.498 -13.730  -4.853  1.00 20.94           C  
ANISOU 5826  CB  TYR A 764     2384   2805   2767    -83    143    257       C  
ATOM   5827  CG  TYR A 764      18.386 -13.526  -3.869  1.00 27.63           C  
ANISOU 5827  CG  TYR A 764     3188   3688   3622    -90    212    234       C  
ATOM   5828  CD1 TYR A 764      18.092 -14.489  -2.905  1.00 29.60           C  
ANISOU 5828  CD1 TYR A 764     3430   3958   3859   -150    261    252       C  
ATOM   5829  CD2 TYR A 764      17.637 -12.358  -3.882  1.00 38.15           C  
ANISOU 5829  CD2 TYR A 764     4492   5030   4973    -33    235    195       C  
ATOM   5830  CE1 TYR A 764      17.058 -14.302  -1.990  1.00 29.55           C  
ANISOU 5830  CE1 TYR A 764     3383   3987   3858   -161    337    229       C  
ATOM   5831  CE2 TYR A 764      16.607 -12.149  -2.963  1.00 45.29           C  
ANISOU 5831  CE2 TYR A 764     5350   5971   5886    -36    306    167       C  
ATOM   5832  CZ  TYR A 764      16.317 -13.126  -2.022  1.00 42.09           C  
ANISOU 5832  CZ  TYR A 764     4932   5592   5467   -103    360    183       C  
ATOM   5833  OH  TYR A 764      15.293 -12.920  -1.117  1.00 48.56           O  
ANISOU 5833  OH  TYR A 764     5706   6451   6294   -109    440    155       O  
ATOM   5834  N   VAL A 765      21.000 -16.365  -3.086  1.00 16.82           N  
ANISOU 5834  N   VAL A 765     1952   2278   2161   -213    162    345       N  
ATOM   5835  CA  VAL A 765      21.029 -17.826  -3.008  1.00 16.67           C  
ANISOU 5835  CA  VAL A 765     1939   2244   2149   -258    159    383       C  
ATOM   5836  C   VAL A 765      19.608 -18.393  -2.907  1.00 23.61           C  
ANISOU 5836  C   VAL A 765     2753   3137   3080   -292    209    375       C  
ATOM   5837  O   VAL A 765      18.944 -18.247  -1.893  1.00 25.05           O  
ANISOU 5837  O   VAL A 765     2928   3344   3245   -313    279    371       O  
ATOM   5838  CB  VAL A 765      21.890 -18.322  -1.826  1.00 21.84           C  
ANISOU 5838  CB  VAL A 765     2669   2898   2732   -281    173    421       C  
ATOM   5839  CG1 VAL A 765      21.891 -19.834  -1.771  1.00 24.10           C  
ANISOU 5839  CG1 VAL A 765     2974   3156   3028   -320    174    465       C  
ATOM   5840  CG2 VAL A 765      23.307 -17.801  -1.951  1.00 17.21           C  
ANISOU 5840  CG2 VAL A 765     2129   2306   2103   -251    119    418       C  
ATOM   5841  N   LEU A 766      19.132 -19.042  -3.961  1.00 19.16           N  
ANISOU 5841  N   LEU A 766     2138   2561   2580   -301    176    365       N  
ATOM   5842  CA  LEU A 766      17.756 -19.511  -3.955  1.00 20.77           C  
ANISOU 5842  CA  LEU A 766     2263   2784   2843   -337    221    343       C  
ATOM   5843  C   LEU A 766      17.646 -20.960  -3.492  1.00 19.63           C  
ANISOU 5843  C   LEU A 766     2139   2610   2707   -410    257    379       C  
ATOM   5844  O   LEU A 766      16.562 -21.437  -3.150  1.00 20.29           O  
ANISOU 5844  O   LEU A 766     2170   2707   2834   -461    318    367       O  
ATOM   5845  CB  LEU A 766      17.120 -19.320  -5.337  1.00 23.31           C  
ANISOU 5845  CB  LEU A 766     2506   3118   3232   -305    165    299       C  
ATOM   5846  CG  LEU A 766      17.067 -17.856  -5.782  1.00 27.06           C  
ANISOU 5846  CG  LEU A 766     2968   3615   3700   -227    139    268       C  
ATOM   5847  CD1 LEU A 766      16.300 -17.727  -7.099  1.00 23.99           C  
ANISOU 5847  CD1 LEU A 766     2502   3244   3370   -188     82    226       C  
ATOM   5848  CD2 LEU A 766      16.434 -16.975  -4.709  1.00 26.00           C  
ANISOU 5848  CD2 LEU A 766     2815   3513   3550   -216    211    249       C  
ATOM   5849  N   TRP A 767      18.777 -21.655  -3.474  1.00 18.83           N  
ANISOU 5849  N   TRP A 767     2118   2468   2569   -415    222    423       N  
ATOM   5850  CA  TRP A 767      18.788 -23.055  -3.080  1.00 19.20           C  
ANISOU 5850  CA  TRP A 767     2205   2472   2621   -475    251    465       C  
ATOM   5851  C   TRP A 767      20.198 -23.462  -2.717  1.00 20.05           C  
ANISOU 5851  C   TRP A 767     2413   2545   2660   -454    215    516       C  
ATOM   5852  O   TRP A 767      21.159 -23.094  -3.413  1.00 21.82           O  
ANISOU 5852  O   TRP A 767     2652   2766   2872   -406    144    508       O  
ATOM   5853  CB  TRP A 767      18.250 -23.956  -4.210  1.00 22.82           C  
ANISOU 5853  CB  TRP A 767     2608   2902   3162   -507    221    440       C  
ATOM   5854  CG  TRP A 767      17.987 -25.356  -3.736  1.00 23.26           C  
ANISOU 5854  CG  TRP A 767     2696   2904   3235   -582    273    476       C  
ATOM   5855  CD1 TRP A 767      18.853 -26.412  -3.771  1.00 22.93           C  
ANISOU 5855  CD1 TRP A 767     2737   2798   3176   -591    249    522       C  
ATOM   5856  CD2 TRP A 767      16.784 -25.844  -3.110  1.00 20.11           C  
ANISOU 5856  CD2 TRP A 767     2256   2507   2876   -658    365    470       C  
ATOM   5857  CE2 TRP A 767      16.992 -27.206  -2.812  1.00 20.64           C  
ANISOU 5857  CE2 TRP A 767     2394   2502   2948   -715    396    518       C  
ATOM   5858  CE3 TRP A 767      15.557 -25.263  -2.790  1.00 20.70           C  
ANISOU 5858  CE3 TRP A 767     2240   2638   2987   -682    429    427       C  
ATOM   5859  NE1 TRP A 767      18.260 -27.528  -3.210  1.00 22.23           N  
ANISOU 5859  NE1 TRP A 767     2672   2662   3112   -667    321    550       N  
ATOM   5860  CZ2 TRP A 767      16.011 -27.993  -2.198  1.00 30.80           C  
ANISOU 5860  CZ2 TRP A 767     3668   3764   4271   -806    495    526       C  
ATOM   5861  CZ3 TRP A 767      14.581 -26.053  -2.182  1.00 21.82           C  
ANISOU 5861  CZ3 TRP A 767     2356   2766   3167   -771    526    429       C  
ATOM   5862  CH2 TRP A 767      14.817 -27.395  -1.889  1.00 24.00           C  
ANISOU 5862  CH2 TRP A 767     2709   2964   3446   -837    562    480       C  
ATOM   5863  N   ASP A 768      20.324 -24.223  -1.629  1.00 18.38           N  
ANISOU 5863  N   ASP A 768     2271   2309   2403   -488    266    568       N  
ATOM   5864  CA  ASP A 768      21.633 -24.667  -1.165  1.00 23.73           C  
ANISOU 5864  CA  ASP A 768     3044   2960   3011   -459    229    618       C  
ATOM   5865  C   ASP A 768      21.619 -25.995  -0.406  1.00 29.23           C  
ANISOU 5865  C   ASP A 768     3819   3601   3684   -500    274    682       C  
ATOM   5866  O   ASP A 768      21.548 -26.016   0.827  1.00 30.92           O  
ANISOU 5866  O   ASP A 768     4093   3826   3829   -511    331    720       O  
ATOM   5867  CB  ASP A 768      22.293 -23.587  -0.302  1.00 26.44           C  
ANISOU 5867  CB  ASP A 768     3422   3352   3271   -416    224    616       C  
ATOM   5868  CG  ASP A 768      23.755 -23.886  -0.018  1.00 29.78           C  
ANISOU 5868  CG  ASP A 768     3923   3763   3630   -373    162    650       C  
ATOM   5869  OD1 ASP A 768      24.328 -23.247   0.896  1.00 31.75           O  
ANISOU 5869  OD1 ASP A 768     4213   4051   3801   -347    160    653       O  
ATOM   5870  OD2 ASP A 768      24.330 -24.768  -0.705  1.00 29.80           O1-
ANISOU 5870  OD2 ASP A 768     3942   3721   3661   -364    114    668       O1-
ATOM   5871  N   ASP A 769      21.719 -27.104  -1.134  1.00 27.68           N  
ANISOU 5871  N   ASP A 769     3633   3343   3540   -519    249    695       N  
ATOM   5872  CA  ASP A 769      21.874 -28.410  -0.491  1.00 24.63           C  
ANISOU 5872  CA  ASP A 769     3341   2887   3132   -548    285    761       C  
ATOM   5873  C   ASP A 769      23.229 -28.484   0.217  1.00 21.40           C  
ANISOU 5873  C   ASP A 769     3029   2475   2626   -482    238    812       C  
ATOM   5874  O   ASP A 769      23.465 -29.385   1.006  1.00 20.62           O  
ANISOU 5874  O   ASP A 769     3027   2327   2480   -486    266    878       O  
ATOM   5875  CB  ASP A 769      21.864 -29.549  -1.522  1.00 20.02           C  
ANISOU 5875  CB  ASP A 769     2752   2228   2625   -573    257    757       C  
ATOM   5876  CG  ASP A 769      20.572 -29.649  -2.302  1.00 29.98           C  
ANISOU 5876  CG  ASP A 769     3915   3491   3987   -640    290    699       C  
ATOM   5877  OD1 ASP A 769      19.489 -29.570  -1.696  1.00 31.75           O  
ANISOU 5877  OD1 ASP A 769     4106   3731   4226   -700    376    695       O  
ATOM   5878  OD2 ASP A 769      20.648 -29.836  -3.537  1.00 35.98           O1-
ANISOU 5878  OD2 ASP A 769     4627   4237   4809   -631    229    655       O1-
ATOM   5879  N   ASN A 770      24.140 -27.580  -0.128  1.00 20.76           N  
ANISOU 5879  N   ASN A 770     2924   2444   2520   -419    164    780       N  
ATOM   5880  CA  ASN A 770      25.541 -27.738   0.253  1.00 24.12           C  
ANISOU 5880  CA  ASN A 770     3419   2871   2876   -352     99    811       C  
ATOM   5881  C   ASN A 770      25.936 -27.009   1.537  1.00 21.98           C  
ANISOU 5881  C   ASN A 770     3193   2657   2500   -324    108    827       C  
ATOM   5882  O   ASN A 770      27.076 -27.098   1.960  1.00 22.65           O  
ANISOU 5882  O   ASN A 770     3331   2755   2521   -266     50    847       O  
ATOM   5883  CB  ASN A 770      26.454 -27.323  -0.901  1.00 18.01           C  
ANISOU 5883  CB  ASN A 770     2594   2113   2138   -305     12    764       C  
ATOM   5884  CG  ASN A 770      26.361 -28.281  -2.080  1.00 24.14           C  
ANISOU 5884  CG  ASN A 770     3353   2825   2995   -318    -10    756       C  
ATOM   5885  ND2 ASN A 770      26.065 -27.754  -3.276  1.00 17.26           N  
ANISOU 5885  ND2 ASN A 770     2401   1971   2187   -324    -33    698       N  
ATOM   5886  OD1 ASN A 770      26.540 -29.482  -1.910  1.00 20.30           O  
ANISOU 5886  OD1 ASN A 770     2932   2272   2509   -319     -6    802       O  
ATOM   5887  N   ARG A 771      24.981 -26.289   2.118  1.00 23.38           N  
ANISOU 5887  N   ARG A 771     3346   2874   2665   -361    179    810       N  
ATOM   5888  CA  ARG A 771      25.155 -25.588   3.392  1.00 30.74           C  
ANISOU 5888  CA  ARG A 771     4324   3862   3495   -344    202    818       C  
ATOM   5889  C   ARG A 771      26.436 -24.753   3.479  1.00 24.68           C  
ANISOU 5889  C   ARG A 771     3556   3147   2675   -280    117    785       C  
ATOM   5890  O   ARG A 771      27.217 -24.883   4.415  1.00 25.72           O  
ANISOU 5890  O   ARG A 771     3759   3299   2712   -241     89    814       O  
ATOM   5891  CB  ARG A 771      25.080 -26.578   4.547  1.00 35.07           C  
ANISOU 5891  CB  ARG A 771     4984   4377   3965   -353    251    897       C  
ATOM   5892  CG  ARG A 771      23.708 -27.221   4.707  1.00 38.27           C  
ANISOU 5892  CG  ARG A 771     5389   4739   4414   -432    361    922       C  
ATOM   5893  CD  ARG A 771      23.815 -28.488   5.529  1.00 43.27           C  
ANISOU 5893  CD  ARG A 771     6148   5307   4986   -440    400   1013       C  
ATOM   5894  NE  ARG A 771      22.547 -28.857   6.151  1.00 52.19           N  
ANISOU 5894  NE  ARG A 771     7296   6414   6119   -520    529   1040       N  
ATOM   5895  CZ  ARG A 771      22.433 -29.280   7.410  1.00 52.94           C  
ANISOU 5895  CZ  ARG A 771     7506   6497   6112   -528    598   1109       C  
ATOM   5896  NH1 ARG A 771      23.515 -29.382   8.176  1.00 43.39           N1+
ANISOU 5896  NH1 ARG A 771     6401   5300   4784   -451    539   1156       N1+
ATOM   5897  NH2 ARG A 771      21.241 -29.598   7.906  1.00 57.49           N  
ANISOU 5897  NH2 ARG A 771     8090   7053   6701   -610    727   1129       N  
ATOM   5898  N   PHE A 772      26.643 -23.913   2.479  1.00 21.54           N  
ANISOU 5898  N   PHE A 772     3077   2770   2338   -270     76    724       N  
ATOM   5899  CA  PHE A 772      27.741 -22.980   2.492  1.00 19.65           C  
ANISOU 5899  CA  PHE A 772     2824   2580   2064   -226     12    681       C  
ATOM   5900  C   PHE A 772      27.560 -22.049   3.658  1.00 23.69           C  
ANISOU 5900  C   PHE A 772     3359   3146   2497   -228     47    661       C  
ATOM   5901  O   PHE A 772      26.434 -21.674   3.998  1.00 22.80           O  
ANISOU 5901  O   PHE A 772     3232   3041   2389   -263    124    653       O  
ATOM   5902  CB  PHE A 772      27.732 -22.133   1.228  1.00 18.65           C  
ANISOU 5902  CB  PHE A 772     2612   2456   2017   -228    -11    621       C  
ATOM   5903  CG  PHE A 772      28.417 -22.770   0.053  1.00 26.16           C  
ANISOU 5903  CG  PHE A 772     3542   3372   3025   -208    -71    622       C  
ATOM   5904  CD1 PHE A 772      29.784 -22.620  -0.133  1.00 31.15           C  
ANISOU 5904  CD1 PHE A 772     4174   4023   3637   -167   -140    604       C  
ATOM   5905  CD2 PHE A 772      27.692 -23.482  -0.891  1.00 29.67           C  
ANISOU 5905  CD2 PHE A 772     3960   3769   3545   -233    -56    632       C  
ATOM   5906  CE1 PHE A 772      30.427 -23.190  -1.239  1.00 32.73           C  
ANISOU 5906  CE1 PHE A 772     4352   4194   3890   -147   -187    600       C  
ATOM   5907  CE2 PHE A 772      28.326 -24.056  -2.001  1.00 29.35           C  
ANISOU 5907  CE2 PHE A 772     3902   3696   3552   -213   -108    626       C  
ATOM   5908  CZ  PHE A 772      29.694 -23.911  -2.169  1.00 28.11           C  
ANISOU 5908  CZ  PHE A 772     3750   3558   3373   -168   -170    612       C  
ATOM   5909  N   THR A 773      28.675 -21.675   4.270  1.00 19.37           N  
ANISOU 5909  N   THR A 773     2841   2641   1876   -188    -10    646       N  
ATOM   5910  CA  THR A 773      28.662 -20.555   5.189  1.00 25.67           C  
ANISOU 5910  CA  THR A 773     3649   3497   2606   -188     10    603       C  
ATOM   5911  C   THR A 773      28.780 -19.284   4.355  1.00 25.16           C  
ANISOU 5911  C   THR A 773     3508   3445   2605   -195     -3    527       C  
ATOM   5912  O   THR A 773      29.078 -19.347   3.153  1.00 21.79           O  
ANISOU 5912  O   THR A 773     3032   2990   2256   -192    -38    516       O  
ATOM   5913  CB  THR A 773      29.834 -20.612   6.136  1.00 34.83           C  
ANISOU 5913  CB  THR A 773     4865   4703   3664   -144    -55    604       C  
ATOM   5914  CG2 THR A 773      31.092 -20.340   5.381  1.00 18.87           C  
ANISOU 5914  CG2 THR A 773     2794   2695   1679   -116   -143    561       C  
ATOM   5915  OG1 THR A 773      29.669 -19.594   7.122  1.00 53.79           O  
ANISOU 5915  OG1 THR A 773     7286   7159   5993   -150    -26    560       O  
ATOM   5916  N   ALA A 774      28.551 -18.134   4.981  1.00 20.63           N  
ANISOU 5916  N   ALA A 774     2934   2909   1996   -202     28    477       N  
ATOM   5917  CA  ALA A 774      28.615 -16.870   4.259  1.00 20.72           C  
ANISOU 5917  CA  ALA A 774     2888   2921   2064   -208     25    409       C  
ATOM   5918  C   ALA A 774      29.999 -16.643   3.640  1.00 24.00           C  
ANISOU 5918  C   ALA A 774     3280   3342   2498   -191    -55    377       C  
ATOM   5919  O   ALA A 774      30.114 -16.364   2.448  1.00 23.15           O  
ANISOU 5919  O   ALA A 774     3124   3204   2467   -194    -67    360       O  
ATOM   5920  CB  ALA A 774      28.239 -15.697   5.186  1.00 19.98           C  
ANISOU 5920  CB  ALA A 774     2810   2862   1919   -215     71    357       C  
ATOM   5921  N   ASP A 775      31.039 -16.758   4.464  1.00 25.56           N  
ANISOU 5921  N   ASP A 775     3509   3583   2620   -171   -107    366       N  
ATOM   5922  CA  ASP A 775      32.417 -16.571   4.020  1.00 24.27           C  
ANISOU 5922  CA  ASP A 775     3314   3438   2471   -156   -182    327       C  
ATOM   5923  C   ASP A 775      32.802 -17.513   2.876  1.00 25.33           C  
ANISOU 5923  C   ASP A 775     3419   3535   2672   -141   -217    364       C  
ATOM   5924  O   ASP A 775      33.396 -17.085   1.892  1.00 27.30           O  
ANISOU 5924  O   ASP A 775     3617   3772   2982   -147   -238    328       O  
ATOM   5925  CB  ASP A 775      33.389 -16.777   5.185  1.00 21.60           C  
ANISOU 5925  CB  ASP A 775     3012   3161   2034   -128   -242    315       C  
ATOM   5926  CG  ASP A 775      33.468 -15.566   6.119  1.00 28.69           C  
ANISOU 5926  CG  ASP A 775     3923   4106   2873   -144   -229    244       C  
ATOM   5927  OD1 ASP A 775      33.373 -14.423   5.640  1.00 38.00           O  
ANISOU 5927  OD1 ASP A 775     5065   5270   4104   -176   -200    183       O  
ATOM   5928  OD2 ASP A 775      33.646 -15.757   7.338  1.00 31.55           O1-
ANISOU 5928  OD2 ASP A 775     4339   4518   3132   -124   -248    247       O1-
ATOM   5929  N   GLU A 776      32.468 -18.790   3.011  1.00 23.85           N  
ANISOU 5929  N   GLU A 776     3266   3323   2471   -124   -218    434       N  
ATOM   5930  CA  GLU A 776      32.858 -19.777   2.019  1.00 28.54           C  
ANISOU 5930  CA  GLU A 776     3842   3879   3123   -106   -253    466       C  
ATOM   5931  C   GLU A 776      32.279 -19.393   0.661  1.00 22.25           C  
ANISOU 5931  C   GLU A 776     2993   3041   2420   -132   -222    449       C  
ATOM   5932  O   GLU A 776      32.975 -19.400  -0.339  1.00 20.47           O  
ANISOU 5932  O   GLU A 776     2729   2805   2245   -124   -255    428       O  
ATOM   5933  CB  GLU A 776      32.374 -21.168   2.417  1.00 41.56           C  
ANISOU 5933  CB  GLU A 776     5550   5493   4747    -92   -242    545       C  
ATOM   5934  CG  GLU A 776      33.260 -22.304   1.944  1.00 50.37           C  
ANISOU 5934  CG  GLU A 776     6673   6586   5880    -49   -304    576       C  
ATOM   5935  CD  GLU A 776      32.720 -23.666   2.346  1.00 57.99           C  
ANISOU 5935  CD  GLU A 776     7709   7500   6823    -39   -284    657       C  
ATOM   5936  OE1 GLU A 776      31.913 -23.738   3.312  1.00 61.67           O  
ANISOU 5936  OE1 GLU A 776     8231   7967   7234    -59   -230    692       O  
ATOM   5937  OE2 GLU A 776      33.103 -24.658   1.684  1.00 53.10           O1-
ANISOU 5937  OE2 GLU A 776     7094   6836   6244    -13   -315    683       O1-
ATOM   5938  N   LEU A 777      31.009 -19.018   0.653  1.00 16.06           N  
ANISOU 5938  N   LEU A 777     2208   2239   1656   -161   -157    454       N  
ATOM   5939  CA  LEU A 777      30.326 -18.697  -0.573  1.00 15.47           C  
ANISOU 5939  CA  LEU A 777     2089   2130   1661   -177   -133    441       C  
ATOM   5940  C   LEU A 777      30.709 -17.318  -1.134  1.00 26.70           C  
ANISOU 5940  C   LEU A 777     3477   3560   3108   -181   -133    381       C  
ATOM   5941  O   LEU A 777      30.750 -17.134  -2.337  1.00 21.86           O  
ANISOU 5941  O   LEU A 777     2834   2921   2552   -179   -139    370       O  
ATOM   5942  CB  LEU A 777      28.819 -18.780  -0.363  1.00 18.57           C  
ANISOU 5942  CB  LEU A 777     2481   2506   2068   -200    -68    462       C  
ATOM   5943  CG  LEU A 777      28.021 -18.710  -1.667  1.00 19.94           C  
ANISOU 5943  CG  LEU A 777     2606   2647   2325   -208    -55    454       C  
ATOM   5944  CD1 LEU A 777      28.567 -19.708  -2.703  1.00 17.26           C  
ANISOU 5944  CD1 LEU A 777     2258   2276   2025   -197   -102    473       C  
ATOM   5945  CD2 LEU A 777      26.591 -19.014  -1.364  1.00 19.44           C  
ANISOU 5945  CD2 LEU A 777     2532   2577   2279   -232      4    472       C  
ATOM   5946  N   GLN A 778      30.989 -16.349  -0.272  1.00 21.12           N  
ANISOU 5946  N   GLN A 778     2783   2886   2356   -187   -123    342       N  
ATOM   5947  CA  GLN A 778      31.410 -15.050  -0.777  1.00 19.67           C  
ANISOU 5947  CA  GLN A 778     2577   2698   2198   -198   -117    284       C  
ATOM   5948  C   GLN A 778      32.827 -15.163  -1.339  1.00 15.94           C  
ANISOU 5948  C   GLN A 778     2082   2235   1740   -194   -169    262       C  
ATOM   5949  O   GLN A 778      33.130 -14.611  -2.391  1.00 15.72           O  
ANISOU 5949  O   GLN A 778     2031   2181   1761   -201   -164    239       O  
ATOM   5950  CB  GLN A 778      31.321 -13.985   0.322  1.00 20.91           C  
ANISOU 5950  CB  GLN A 778     2756   2883   2305   -210    -89    239       C  
ATOM   5951  CG  GLN A 778      29.880 -13.604   0.678  1.00 19.22           C  
ANISOU 5951  CG  GLN A 778     2554   2658   2092   -212    -25    247       C  
ATOM   5952  CD  GLN A 778      29.750 -12.971   2.062  1.00 20.30           C  
ANISOU 5952  CD  GLN A 778     2725   2830   2157   -219      3    213       C  
ATOM   5953  NE2 GLN A 778      28.533 -12.937   2.574  1.00 16.71           N  
ANISOU 5953  NE2 GLN A 778     2280   2377   1691   -219     61    227       N  
ATOM   5954  OE1 GLN A 778      30.731 -12.526   2.656  1.00 20.68           O  
ANISOU 5954  OE1 GLN A 778     2786   2909   2162   -226    -28    170       O  
ATOM   5955  N   ILE A 779      33.692 -15.887  -0.633  1.00 15.44           N  
ANISOU 5955  N   ILE A 779     2027   2209   1631   -178   -218    269       N  
ATOM   5956  CA  ILE A 779      35.052 -16.104  -1.116  1.00 16.88           C  
ANISOU 5956  CA  ILE A 779     2175   2409   1829   -168   -270    243       C  
ATOM   5957  C   ILE A 779      35.059 -16.886  -2.444  1.00 21.90           C  
ANISOU 5957  C   ILE A 779     2790   3005   2527   -155   -277    275       C  
ATOM   5958  O   ILE A 779      35.777 -16.525  -3.380  1.00 20.66           O  
ANISOU 5958  O   ILE A 779     2598   2841   2411   -162   -282    244       O  
ATOM   5959  CB  ILE A 779      35.923 -16.843  -0.089  1.00 18.33           C  
ANISOU 5959  CB  ILE A 779     2370   2645   1950   -138   -331    248       C  
ATOM   5960  CG1 ILE A 779      36.097 -15.995   1.180  1.00 31.40           C  
ANISOU 5960  CG1 ILE A 779     4043   4350   3538   -151   -334    202       C  
ATOM   5961  CG2 ILE A 779      37.300 -17.187  -0.682  1.00 16.14           C  
ANISOU 5961  CG2 ILE A 779     2042   2389   1701   -119   -387    220       C  
ATOM   5962  CD1 ILE A 779      36.670 -14.628   0.911  1.00 38.88           C  
ANISOU 5962  CD1 ILE A 779     4952   5305   4513   -191   -320    120       C  
ATOM   5963  N   LEU A 780      34.261 -17.948  -2.521  1.00 19.46           N  
ANISOU 5963  N   LEU A 780     2504   2668   2221   -139   -273    333       N  
ATOM   5964  CA  LEU A 780      34.246 -18.772  -3.720  1.00 18.80           C  
ANISOU 5964  CA  LEU A 780     2406   2547   2190   -126   -284    357       C  
ATOM   5965  C   LEU A 780      33.802 -17.941  -4.925  1.00 21.42           C  
ANISOU 5965  C   LEU A 780     2716   2849   2573   -144   -249    335       C  
ATOM   5966  O   LEU A 780      34.367 -18.055  -5.998  1.00 19.42           O  
ANISOU 5966  O   LEU A 780     2442   2583   2355   -138   -261    324       O  
ATOM   5967  CB  LEU A 780      33.340 -19.987  -3.552  1.00 19.81           C  
ANISOU 5967  CB  LEU A 780     2565   2643   2318   -117   -277    417       C  
ATOM   5968  CG  LEU A 780      33.127 -20.838  -4.821  1.00 19.74           C  
ANISOU 5968  CG  LEU A 780     2544   2589   2366   -110   -284    434       C  
ATOM   5969  CD1 LEU A 780      34.450 -21.355  -5.342  1.00 14.31           C  
ANISOU 5969  CD1 LEU A 780     1840   1908   1691    -78   -332    420       C  
ATOM   5970  CD2 LEU A 780      32.200 -22.015  -4.543  1.00 15.64           C  
ANISOU 5970  CD2 LEU A 780     2058   2033   1851   -114   -271    486       C  
ATOM   5971  N   THR A 781      32.799 -17.091  -4.727  1.00 20.14           N  
ANISOU 5971  N   THR A 781     2563   2678   2410   -162   -206    330       N  
ATOM   5972  CA  THR A 781      32.245 -16.287  -5.801  1.00 19.93           C  
ANISOU 5972  CA  THR A 781     2527   2621   2424   -167   -176    316       C  
ATOM   5973  C   THR A 781      33.268 -15.266  -6.288  1.00 23.61           C  
ANISOU 5973  C   THR A 781     2983   3087   2899   -179   -170    272       C  
ATOM   5974  O   THR A 781      33.396 -15.006  -7.482  1.00 18.92           O  
ANISOU 5974  O   THR A 781     2385   2467   2337   -176   -161    267       O  
ATOM   5975  CB  THR A 781      30.974 -15.573  -5.330  1.00 21.00           C  
ANISOU 5975  CB  THR A 781     2672   2750   2555   -173   -132    316       C  
ATOM   5976  CG2 THR A 781      30.407 -14.656  -6.424  1.00 13.50           C  
ANISOU 5976  CG2 THR A 781     1719   1769   1643   -164   -108    303       C  
ATOM   5977  OG1 THR A 781      29.998 -16.558  -4.961  1.00 15.23           O  
ANISOU 5977  OG1 THR A 781     1943   2019   1825   -171   -127    355       O  
ATOM   5978  N   TYR A 782      34.004 -14.702  -5.346  1.00 13.93           N  
ANISOU 5978  N   TYR A 782     1757   1893   1643   -196   -174    237       N  
ATOM   5979  CA  TYR A 782      35.047 -13.750  -5.655  1.00 14.07           C  
ANISOU 5979  CA  TYR A 782     1761   1913   1672   -220   -164    185       C  
ATOM   5980  C   TYR A 782      36.210 -14.402  -6.434  1.00 18.43           C  
ANISOU 5980  C   TYR A 782     2279   2476   2246   -215   -194    178       C  
ATOM   5981  O   TYR A 782      36.712 -13.844  -7.427  1.00 15.70           O  
ANISOU 5981  O   TYR A 782     1925   2109   1932   -231   -168    156       O  
ATOM   5982  CB  TYR A 782      35.544 -13.149  -4.345  1.00 14.56           C  
ANISOU 5982  CB  TYR A 782     1824   2015   1694   -242   -170    141       C  
ATOM   5983  CG  TYR A 782      36.452 -11.979  -4.526  1.00 16.76           C  
ANISOU 5983  CG  TYR A 782     2088   2289   1989   -282   -148     77       C  
ATOM   5984  CD1 TYR A 782      36.201 -11.024  -5.508  1.00 16.84           C  
ANISOU 5984  CD1 TYR A 782     2117   2243   2037   -299    -96     70       C  
ATOM   5985  CD2 TYR A 782      37.558 -11.809  -3.705  1.00 15.38           C  
ANISOU 5985  CD2 TYR A 782     1885   2167   1792   -303   -180     22       C  
ATOM   5986  CE1 TYR A 782      37.032  -9.940  -5.668  1.00 19.44           C  
ANISOU 5986  CE1 TYR A 782     2442   2558   2386   -345    -64     12       C  
ATOM   5987  CE2 TYR A 782      38.395 -10.733  -3.860  1.00 15.76           C  
ANISOU 5987  CE2 TYR A 782     1914   2209   1864   -352   -154    -45       C  
ATOM   5988  CZ  TYR A 782      38.134  -9.800  -4.834  1.00 15.61           C  
ANISOU 5988  CZ  TYR A 782     1920   2125   1887   -377    -91    -49       C  
ATOM   5989  OH  TYR A 782      38.974  -8.724  -4.968  1.00 16.87           O  
ANISOU 5989  OH  TYR A 782     2068   2269   2072   -434    -55   -115       O  
ATOM   5990  N   GLN A 783      36.633 -15.577  -5.978  1.00 14.16           N  
ANISOU 5990  N   GLN A 783     1724   1967   1689   -189   -243    196       N  
ATOM   5991  CA  GLN A 783      37.689 -16.329  -6.643  1.00 14.75           C  
ANISOU 5991  CA  GLN A 783     1764   2055   1785   -172   -274    189       C  
ATOM   5992  C   GLN A 783      37.324 -16.628  -8.118  1.00 23.61           C  
ANISOU 5992  C   GLN A 783     2891   3132   2946   -162   -253    211       C  
ATOM   5993  O   GLN A 783      38.179 -16.556  -9.011  1.00 20.94           O  
ANISOU 5993  O   GLN A 783     2528   2795   2634   -167   -245    186       O  
ATOM   5994  CB  GLN A 783      37.997 -17.627  -5.879  1.00 14.48           C  
ANISOU 5994  CB  GLN A 783     1728   2050   1724   -131   -332    216       C  
ATOM   5995  CG  GLN A 783      38.815 -17.404  -4.597  1.00 15.81           C  
ANISOU 5995  CG  GLN A 783     1881   2278   1848   -129   -370    181       C  
ATOM   5996  CD  GLN A 783      39.114 -18.691  -3.837  1.00 18.11           C  
ANISOU 5996  CD  GLN A 783     2184   2594   2102    -75   -431    216       C  
ATOM   5997  NE2 GLN A 783      39.957 -18.599  -2.806  1.00 24.43           N  
ANISOU 5997  NE2 GLN A 783     2968   3457   2859    -59   -479    183       N  
ATOM   5998  OE1 GLN A 783      38.590 -19.744  -4.165  1.00 28.31           O  
ANISOU 5998  OE1 GLN A 783     3506   3848   3403    -47   -436    270       O  
ATOM   5999  N   LEU A 784      36.052 -16.939  -8.364  1.00 18.38           N  
ANISOU 5999  N   LEU A 784     2260   2436   2287   -151   -242    253       N  
ATOM   6000  CA  LEU A 784      35.590 -17.266  -9.710  1.00 14.92           C  
ANISOU 6000  CA  LEU A 784     1830   1961   1877   -138   -231    271       C  
ATOM   6001  C   LEU A 784      35.651 -16.072 -10.651  1.00 17.06           C  
ANISOU 6001  C   LEU A 784     2112   2210   2161   -155   -187    250       C  
ATOM   6002  O   LEU A 784      35.697 -16.243 -11.879  1.00 21.55           O  
ANISOU 6002  O   LEU A 784     2686   2757   2743   -143   -179    254       O  
ATOM   6003  CB  LEU A 784      34.165 -17.818  -9.672  1.00 14.95           C  
ANISOU 6003  CB  LEU A 784     1855   1942   1884   -127   -233    311       C  
ATOM   6004  CG  LEU A 784      34.078 -19.207  -9.049  1.00 19.94           C  
ANISOU 6004  CG  LEU A 784     2490   2576   2509   -111   -267    341       C  
ATOM   6005  CD1 LEU A 784      32.628 -19.657  -8.961  1.00 19.16           C  
ANISOU 6005  CD1 LEU A 784     2406   2455   2421   -116   -257    373       C  
ATOM   6006  CD2 LEU A 784      34.911 -20.185  -9.876  1.00 20.36           C  
ANISOU 6006  CD2 LEU A 784     2531   2621   2582    -87   -296    339       C  
ATOM   6007  N   CYS A 785      35.632 -14.866 -10.084  1.00 14.35           N  
ANISOU 6007  N   CYS A 785     1778   1866   1807   -182   -156    227       N  
ATOM   6008  CA  CYS A 785      35.776 -13.655 -10.892  1.00 16.33           C  
ANISOU 6008  CA  CYS A 785     2051   2084   2068   -200   -107    209       C  
ATOM   6009  C   CYS A 785      37.215 -13.458 -11.341  1.00 16.91           C  
ANISOU 6009  C   CYS A 785     2100   2171   2156   -228    -91    171       C  
ATOM   6010  O   CYS A 785      37.476 -12.618 -12.192  1.00 18.15           O  
ANISOU 6010  O   CYS A 785     2279   2295   2321   -246    -43    160       O  
ATOM   6011  CB  CYS A 785      35.286 -12.412 -10.150  1.00 14.71           C  
ANISOU 6011  CB  CYS A 785     1872   1863   1854   -220    -73    193       C  
ATOM   6012  SG  CYS A 785      33.551 -12.472  -9.643  1.00 17.37           S  
ANISOU 6012  SG  CYS A 785     2230   2190   2181   -189    -77    228       S  
ATOM   6013  N   HIS A 786      38.140 -14.228 -10.763  1.00 14.96           N  
ANISOU 6013  N   HIS A 786     1805   1971   1909   -227   -130    150       N  
ATOM   6014  CA  HIS A 786      39.552 -14.169 -11.152  1.00 17.38           C  
ANISOU 6014  CA  HIS A 786     2067   2302   2235   -250   -119    106       C  
ATOM   6015  C   HIS A 786      39.970 -15.294 -12.107  1.00 19.33           C  
ANISOU 6015  C   HIS A 786     2294   2555   2496   -216   -137    118       C  
ATOM   6016  O   HIS A 786      41.160 -15.452 -12.386  1.00 19.91           O  
ANISOU 6016  O   HIS A 786     2319   2659   2588   -225   -132     79       O  
ATOM   6017  CB  HIS A 786      40.481 -14.225  -9.927  1.00 14.58           C  
ANISOU 6017  CB  HIS A 786     1659   2006   1874   -264   -155     60       C  
ATOM   6018  CG  HIS A 786      40.340 -13.061  -8.999  1.00 18.37           C  
ANISOU 6018  CG  HIS A 786     2152   2486   2341   -306   -135     28       C  
ATOM   6019  CD2 HIS A 786      41.169 -12.018  -8.739  1.00 17.00           C  
ANISOU 6019  CD2 HIS A 786     1954   2324   2182   -362   -104    -36       C  
ATOM   6020  ND1 HIS A 786      39.241 -12.887  -8.183  1.00 14.63           N  
ANISOU 6020  ND1 HIS A 786     1720   2001   1838   -294   -143     55       N  
ATOM   6021  CE1 HIS A 786      39.394 -11.785  -7.469  1.00 24.43           C  
ANISOU 6021  CE1 HIS A 786     2966   3243   3072   -335   -119     10       C  
ATOM   6022  NE2 HIS A 786      40.556 -11.240  -7.788  1.00 22.16           N  
ANISOU 6022  NE2 HIS A 786     2641   2968   2812   -380    -97    -47       N  
ATOM   6023  N   THR A 787      39.016 -16.092 -12.579  1.00 17.14           N  
ANISOU 6023  N   THR A 787     2049   2253   2212   -177   -158    165       N  
ATOM   6024  CA  THR A 787      39.354 -17.197 -13.460  1.00 18.44           C  
ANISOU 6024  CA  THR A 787     2200   2417   2387   -143   -176    172       C  
ATOM   6025  C   THR A 787      38.979 -16.914 -14.922  1.00 26.35           C  
ANISOU 6025  C   THR A 787     3242   3381   3388   -140   -136    183       C  
ATOM   6026  O   THR A 787      39.097 -17.790 -15.788  1.00 23.19           O  
ANISOU 6026  O   THR A 787     2842   2976   2991   -111   -148    187       O  
ATOM   6027  CB  THR A 787      38.689 -18.517 -13.008  1.00 19.95           C  
ANISOU 6027  CB  THR A 787     2400   2606   2575   -103   -232    208       C  
ATOM   6028  CG2 THR A 787      39.092 -18.889 -11.567  1.00 13.68           C  
ANISOU 6028  CG2 THR A 787     1581   1848   1769    -96   -274    205       C  
ATOM   6029  OG1 THR A 787      37.264 -18.397 -13.114  1.00 13.12           O  
ANISOU 6029  OG1 THR A 787     1577   1707   1701   -101   -228    244       O  
ATOM   6030  N   TYR A 788      38.520 -15.695 -15.190  1.00 21.60           N  
ANISOU 6030  N   TYR A 788     2680   2751   2776   -164    -90    188       N  
ATOM   6031  CA  TYR A 788      38.060 -15.328 -16.531  1.00 23.37           C  
ANISOU 6031  CA  TYR A 788     2956   2939   2985   -151    -56    207       C  
ATOM   6032  C   TYR A 788      39.246 -15.224 -17.503  1.00 18.93           C  
ANISOU 6032  C   TYR A 788     2385   2381   2426   -167     -9    179       C  
ATOM   6033  O   TYR A 788      40.170 -14.446 -17.294  1.00 20.30           O  
ANISOU 6033  O   TYR A 788     2538   2562   2613   -212     38    146       O  
ATOM   6034  CB  TYR A 788      37.299 -14.018 -16.440  1.00 19.97           C  
ANISOU 6034  CB  TYR A 788     2576   2472   2542   -164    -21    222       C  
ATOM   6035  CG  TYR A 788      36.617 -13.514 -17.685  1.00 19.18           C  
ANISOU 6035  CG  TYR A 788     2542   2330   2416   -138      5    250       C  
ATOM   6036  CD1 TYR A 788      37.049 -12.345 -18.307  1.00 21.98           C  
ANISOU 6036  CD1 TYR A 788     2946   2648   2758   -161     75    248       C  
ATOM   6037  CD2 TYR A 788      35.507 -14.157 -18.205  1.00 22.19           C  
ANISOU 6037  CD2 TYR A 788     2940   2708   2783    -90    -39    277       C  
ATOM   6038  CE1 TYR A 788      36.396 -11.838 -19.430  1.00 19.29           C  
ANISOU 6038  CE1 TYR A 788     2681   2268   2382   -126     96    281       C  
ATOM   6039  CE2 TYR A 788      34.856 -13.668 -19.336  1.00 20.88           C  
ANISOU 6039  CE2 TYR A 788     2836   2512   2585    -55    -26    300       C  
ATOM   6040  CZ  TYR A 788      35.302 -12.511 -19.936  1.00 20.30           C  
ANISOU 6040  CZ  TYR A 788     2821   2402   2490    -68     40    306       C  
ATOM   6041  OH  TYR A 788      34.646 -12.023 -21.043  1.00 20.01           O  
ANISOU 6041  OH  TYR A 788     2857   2334   2411    -24     49    335       O  
ATOM   6042  N   VAL A 789      39.218 -16.018 -18.563  1.00 21.17           N  
ANISOU 6042  N   VAL A 789     2683   2662   2699   -134    -17    187       N  
ATOM   6043  CA  VAL A 789      40.408 -16.174 -19.406  1.00 27.78           C  
ANISOU 6043  CA  VAL A 789     3501   3514   3540   -144     27    155       C  
ATOM   6044  C   VAL A 789      40.813 -14.966 -20.256  1.00 22.10           C  
ANISOU 6044  C   VAL A 789     2828   2767   2803   -180    115    152       C  
ATOM   6045  O   VAL A 789      41.977 -14.836 -20.607  1.00 26.02           O  
ANISOU 6045  O   VAL A 789     3292   3282   3314   -211    168    115       O  
ATOM   6046  CB  VAL A 789      40.316 -17.444 -20.295  1.00 27.95           C  
ANISOU 6046  CB  VAL A 789     3526   3540   3552    -95     -4    157       C  
ATOM   6047  CG1 VAL A 789      40.199 -18.671 -19.414  1.00 24.14           C  
ANISOU 6047  CG1 VAL A 789     2998   3078   3096    -67    -78    156       C  
ATOM   6048  CG2 VAL A 789      39.138 -17.350 -21.275  1.00 14.20           C  
ANISOU 6048  CG2 VAL A 789     1859   1765   1770    -65    -11    191       C  
ATOM   6049  N   ARG A 790      39.871 -14.077 -20.560  1.00 17.90           N  
ANISOU 6049  N   ARG A 790     2370   2190   2241   -175    134    189       N  
ATOM   6050  CA  ARG A 790      40.115 -13.015 -21.554  1.00 20.61           C  
ANISOU 6050  CA  ARG A 790     2784   2492   2554   -196    219    200       C  
ATOM   6051  C   ARG A 790      40.901 -11.797 -21.043  1.00 23.68           C  
ANISOU 6051  C   ARG A 790     3167   2861   2968   -268    293    175       C  
ATOM   6052  O   ARG A 790      41.270 -10.931 -21.827  1.00 24.64           O  
ANISOU 6052  O   ARG A 790     3348   2943   3072   -298    377    182       O  
ATOM   6053  CB  ARG A 790      38.800 -12.564 -22.207  1.00 16.85           C  
ANISOU 6053  CB  ARG A 790     2400   1972   2030   -148    206    252       C  
ATOM   6054  CG  ARG A 790      38.250 -13.540 -23.235  1.00 18.24           C  
ANISOU 6054  CG  ARG A 790     2600   2161   2169    -88    161    267       C  
ATOM   6055  CD  ARG A 790      36.714 -13.534 -23.341  1.00 21.97           C  
ANISOU 6055  CD  ARG A 790     3114   2619   2616    -31     98    302       C  
ATOM   6056  NE  ARG A 790      36.095 -12.217 -23.511  1.00 20.58           N  
ANISOU 6056  NE  ARG A 790     3014   2394   2411    -19    131    337       N  
ATOM   6057  CZ  ARG A 790      35.462 -11.808 -24.615  1.00 23.85           C  
ANISOU 6057  CZ  ARG A 790     3514   2782   2765     33    134    370       C  
ATOM   6058  NH1 ARG A 790      35.379 -12.589 -25.689  1.00 20.31           N1+
ANISOU 6058  NH1 ARG A 790     3088   2356   2275     72    109    369       N1+
ATOM   6059  NH2 ARG A 790      34.919 -10.604 -24.654  1.00 19.39           N  
ANISOU 6059  NH2 ARG A 790     3021   2168   2178     51    162    403       N  
ATOM   6060  N   CYS A 791      41.155 -11.717 -19.740  1.00 19.81           N  
ANISOU 6060  N   CYS A 791     2612   2397   2518   -299    264    144       N  
ATOM   6061  CA  CYS A 791      41.980 -10.624 -19.221  1.00 19.93           C  
ANISOU 6061  CA  CYS A 791     2611   2399   2563   -375    330    105       C  
ATOM   6062  C   CYS A 791      42.610 -10.978 -17.876  1.00 22.88           C  
ANISOU 6062  C   CYS A 791     2884   2832   2978   -402    281     52       C  
ATOM   6063  O   CYS A 791      42.139 -11.864 -17.166  1.00 24.32           O  
ANISOU 6063  O   CYS A 791     3032   3049   3158   -358    198     62       O  
ATOM   6064  CB  CYS A 791      41.164  -9.332 -19.093  1.00 16.24           C  
ANISOU 6064  CB  CYS A 791     2230   1860   2079   -386    366    135       C  
ATOM   6065  SG  CYS A 791      39.631  -9.517 -18.111  1.00 21.02           S  
ANISOU 6065  SG  CYS A 791     2848   2465   2674   -327    276    169       S  
ATOM   6066  N   THR A 792      43.691 -10.292 -17.539  1.00 19.95           N  
ANISOU 6066  N   THR A 792     2467   2473   2641   -475    334     -5       N  
ATOM   6067  CA  THR A 792      44.339 -10.492 -16.249  1.00 26.49           C  
ANISOU 6067  CA  THR A 792     3200   3362   3502   -499    284    -63       C  
ATOM   6068  C   THR A 792      43.756  -9.455 -15.284  1.00 23.23           C  
ANISOU 6068  C   THR A 792     2825   2916   3087   -530    286    -67       C  
ATOM   6069  O   THR A 792      44.439  -8.540 -14.838  1.00 21.26           O  
ANISOU 6069  O   THR A 792     2551   2660   2865   -603    331   -123       O  
ATOM   6070  CB  THR A 792      45.877 -10.378 -16.367  1.00 29.14           C  
ANISOU 6070  CB  THR A 792     3446   3744   3882   -562    332   -139       C  
ATOM   6071  CG2 THR A 792      46.434 -11.519 -17.227  1.00 30.63           C  
ANISOU 6071  CG2 THR A 792     3592   3974   4073   -519    324   -140       C  
ATOM   6072  OG1 THR A 792      46.220  -9.131 -16.982  1.00 23.36           O  
ANISOU 6072  OG1 THR A 792     2762   2953   3162   -638    444   -153       O  
ATOM   6073  N   ARG A 793      42.458  -9.596 -15.026  1.00 19.86           N  
ANISOU 6073  N   ARG A 793     2456   2463   2629   -475    241    -12       N  
ATOM   6074  CA  ARG A 793      41.698  -8.689 -14.185  1.00 22.41           C  
ANISOU 6074  CA  ARG A 793     2822   2749   2944   -488    243     -9       C  
ATOM   6075  C   ARG A 793      40.566  -9.486 -13.552  1.00 25.58           C  
ANISOU 6075  C   ARG A 793     3229   3171   3319   -420    162     33       C  
ATOM   6076  O   ARG A 793      40.009 -10.400 -14.175  1.00 20.91           O  
ANISOU 6076  O   ARG A 793     2648   2584   2711   -364    129     79       O  
ATOM   6077  CB  ARG A 793      41.042  -7.570 -15.000  1.00 17.39           C  
ANISOU 6077  CB  ARG A 793     2292   2022   2295   -493    316     28       C  
ATOM   6078  CG  ARG A 793      41.942  -6.737 -15.877  1.00 20.96           C  
ANISOU 6078  CG  ARG A 793     2772   2428   2764   -557    416      8       C  
ATOM   6079  CD  ARG A 793      41.158  -5.556 -16.439  1.00 23.58           C  
ANISOU 6079  CD  ARG A 793     3224   2658   3075   -551    481     51       C  
ATOM   6080  NE  ARG A 793      41.778  -4.274 -16.098  1.00 33.33           N  
ANISOU 6080  NE  ARG A 793     4482   3839   4342   -637    562      4       N  
ATOM   6081  CZ  ARG A 793      41.233  -3.373 -15.294  1.00 37.12           C  
ANISOU 6081  CZ  ARG A 793     5003   4273   4828   -648    568     -9       C  
ATOM   6082  NH1 ARG A 793      40.052  -3.597 -14.749  1.00 42.99           N1+
ANISOU 6082  NH1 ARG A 793     5764   5022   5547   -577    502     25       N1+
ATOM   6083  NH2 ARG A 793      41.860  -2.238 -15.046  1.00 49.24           N  
ANISOU 6083  NH2 ARG A 793     6561   5752   6396   -734    647    -59       N  
ATOM   6084  N   SER A 794      40.211  -9.118 -12.327  1.00 19.11           N  
ANISOU 6084  N   SER A 794     2403   2362   2494   -429    137     14       N  
ATOM   6085  CA  SER A 794      39.005  -9.631 -11.702  1.00 16.96           C  
ANISOU 6085  CA  SER A 794     2149   2099   2197   -375     83     55       C  
ATOM   6086  C   SER A 794      37.799  -9.000 -12.390  1.00 20.95           C  
ANISOU 6086  C   SER A 794     2732   2536   2690   -344    116    103       C  
ATOM   6087  O   SER A 794      37.709  -7.776 -12.457  1.00 23.93           O  
ANISOU 6087  O   SER A 794     3159   2859   3072   -370    172     91       O  
ATOM   6088  CB  SER A 794      39.007  -9.240 -10.217  1.00 20.51           C  
ANISOU 6088  CB  SER A 794     2579   2576   2637   -399     61     16       C  
ATOM   6089  OG  SER A 794      37.847  -9.727  -9.579  1.00 34.29           O  
ANISOU 6089  OG  SER A 794     4341   4331   4357   -352     22     55       O  
ATOM   6090  N   VAL A 795      36.869  -9.813 -12.889  1.00 20.43           N  
ANISOU 6090  N   VAL A 795     2679   2472   2611   -285     79    153       N  
ATOM   6091  CA  VAL A 795      35.706  -9.274 -13.611  1.00 21.78           C  
ANISOU 6091  CA  VAL A 795     2915   2590   2769   -243     98    195       C  
ATOM   6092  C   VAL A 795      34.483  -9.156 -12.707  1.00 17.49           C  
ANISOU 6092  C   VAL A 795     2377   2050   2220   -214     73    207       C  
ATOM   6093  O   VAL A 795      34.502  -9.644 -11.589  1.00 22.13           O  
ANISOU 6093  O   VAL A 795     2922   2681   2806   -225     42    191       O  
ATOM   6094  CB  VAL A 795      35.369 -10.067 -14.900  1.00 19.12           C  
ANISOU 6094  CB  VAL A 795     2592   2252   2420   -197     77    233       C  
ATOM   6095  CG1 VAL A 795      36.487  -9.899 -15.928  1.00 19.34           C  
ANISOU 6095  CG1 VAL A 795     2635   2265   2448   -225    124    223       C  
ATOM   6096  CG2 VAL A 795      35.125 -11.540 -14.600  1.00 13.59           C  
ANISOU 6096  CG2 VAL A 795     1837   1603   1722   -173     10    243       C  
ATOM   6097  N   SER A 796      33.429  -8.507 -13.197  1.00 15.46           N  
ANISOU 6097  N   SER A 796     2170   1748   1955   -171     89    234       N  
ATOM   6098  CA  SER A 796      32.316  -8.105 -12.346  1.00 21.56           C  
ANISOU 6098  CA  SER A 796     2947   2518   2727   -146     83    235       C  
ATOM   6099  C   SER A 796      31.360  -9.227 -11.969  1.00 24.50           C  
ANISOU 6099  C   SER A 796     3272   2937   3098   -113     30    255       C  
ATOM   6100  O   SER A 796      30.553  -9.068 -11.050  1.00 18.56           O  
ANISOU 6100  O   SER A 796     2508   2198   2346   -103     29    249       O  
ATOM   6101  CB  SER A 796      31.531  -6.966 -12.977  1.00 14.59           C  
ANISOU 6101  CB  SER A 796     2132   1570   1840   -103    118    253       C  
ATOM   6102  OG  SER A 796      30.977  -7.384 -14.214  1.00 14.78           O  
ANISOU 6102  OG  SER A 796     2174   1589   1854    -49     93    292       O  
ATOM   6103  N   ILE A 797      31.427 -10.347 -12.684  1.00 13.55           N  
ANISOU 6103  N   ILE A 797     1860   1574   1712    -99     -8    276       N  
ATOM   6104  CA  ILE A 797      30.583 -11.499 -12.356  1.00 13.93           C  
ANISOU 6104  CA  ILE A 797     1866   1661   1766    -80    -53    292       C  
ATOM   6105  C   ILE A 797      31.459 -12.740 -12.479  1.00 17.15           C  
ANISOU 6105  C   ILE A 797     2243   2098   2177   -100    -84    294       C  
ATOM   6106  O   ILE A 797      32.529 -12.673 -13.078  1.00 13.90           O  
ANISOU 6106  O   ILE A 797     1839   1678   1762   -116    -73    283       O  
ATOM   6107  CB  ILE A 797      29.361 -11.603 -13.286  1.00 20.20           C  
ANISOU 6107  CB  ILE A 797     2665   2444   2565    -27    -73    314       C  
ATOM   6108  CG1 ILE A 797      29.809 -11.633 -14.756  1.00 20.76           C  
ANISOU 6108  CG1 ILE A 797     2769   2494   2623     -7    -78    326       C  
ATOM   6109  CG2 ILE A 797      28.411 -10.438 -13.056  1.00 13.68           C  
ANISOU 6109  CG2 ILE A 797     1863   1595   1740      7    -48    312       C  
ATOM   6110  CD1 ILE A 797      28.668 -11.770 -15.758  1.00 13.55           C  
ANISOU 6110  CD1 ILE A 797     1864   1580   1706     52   -111    342       C  
ATOM   6111  N   PRO A 798      31.035 -13.869 -11.887  1.00 17.16           N  
ANISOU 6111  N   PRO A 798     2209   2128   2183   -100   -118    305       N  
ATOM   6112  CA  PRO A 798      31.889 -15.061 -11.977  1.00 17.93           C  
ANISOU 6112  CA  PRO A 798     2286   2244   2283   -110   -148    307       C  
ATOM   6113  C   PRO A 798      32.102 -15.507 -13.426  1.00 17.86           C  
ANISOU 6113  C   PRO A 798     2285   2220   2281    -90   -161    312       C  
ATOM   6114  O   PRO A 798      31.195 -15.375 -14.246  1.00 12.72           O  
ANISOU 6114  O   PRO A 798     1648   1555   1631    -62   -167    322       O  
ATOM   6115  CB  PRO A 798      31.079 -16.117 -11.213  1.00 14.97           C  
ANISOU 6115  CB  PRO A 798     1890   1886   1914   -109   -173    327       C  
ATOM   6116  CG  PRO A 798      30.284 -15.307 -10.217  1.00 12.89           C  
ANISOU 6116  CG  PRO A 798     1629   1628   1641   -115   -146    324       C  
ATOM   6117  CD  PRO A 798      29.883 -14.089 -10.988  1.00 16.17           C  
ANISOU 6117  CD  PRO A 798     2065   2017   2060    -96   -121    314       C  
ATOM   6118  N   ALA A 799      33.287 -16.024 -13.730  1.00 16.81           N  
ANISOU 6118  N   ALA A 799     2142   2096   2148    -98   -168    300       N  
ATOM   6119  CA  ALA A 799      33.600 -16.483 -15.088  1.00 20.16           C  
ANISOU 6119  CA  ALA A 799     2577   2510   2573    -79   -174    299       C  
ATOM   6120  C   ALA A 799      32.488 -17.329 -15.759  1.00 19.38           C  
ANISOU 6120  C   ALA A 799     2480   2403   2481    -51   -209    314       C  
ATOM   6121  O   ALA A 799      32.113 -17.031 -16.891  1.00 21.53           O  
ANISOU 6121  O   ALA A 799     2779   2662   2740    -27   -208    315       O  
ATOM   6122  CB  ALA A 799      34.963 -17.207 -15.127  1.00 12.78           C  
ANISOU 6122  CB  ALA A 799     1616   1593   1645    -88   -182    280       C  
ATOM   6123  N   PRO A 800      31.935 -18.352 -15.057  1.00 21.67           N  
ANISOU 6123  N   PRO A 800     2745   2700   2788    -55   -240    324       N  
ATOM   6124  CA  PRO A 800      30.884 -19.166 -15.704  1.00 18.14           C  
ANISOU 6124  CA  PRO A 800     2293   2245   2355    -39   -271    328       C  
ATOM   6125  C   PRO A 800      29.707 -18.330 -16.216  1.00 17.87           C  
ANISOU 6125  C   PRO A 800     2266   2209   2315    -18   -269    328       C  
ATOM   6126  O   PRO A 800      29.250 -18.540 -17.325  1.00 21.92           O  
ANISOU 6126  O   PRO A 800     2787   2720   2823      7   -293    320       O  
ATOM   6127  CB  PRO A 800      30.372 -20.084 -14.584  1.00 23.14           C  
ANISOU 6127  CB  PRO A 800     2904   2879   3009    -60   -284    342       C  
ATOM   6128  CG  PRO A 800      31.332 -19.964 -13.452  1.00 23.94           C  
ANISOU 6128  CG  PRO A 800     3006   2993   3098    -76   -271    348       C  
ATOM   6129  CD  PRO A 800      32.210 -18.774 -13.666  1.00 17.55           C  
ANISOU 6129  CD  PRO A 800     2205   2192   2269    -75   -244    332       C  
ATOM   6130  N   ALA A 801      29.222 -17.393 -15.411  1.00 21.80           N  
ANISOU 6130  N   ALA A 801     2761   2712   2811    -23   -245    335       N  
ATOM   6131  CA  ALA A 801      28.107 -16.556 -15.839  1.00 20.03           C  
ANISOU 6131  CA  ALA A 801     2541   2487   2584      9   -245    334       C  
ATOM   6132  C   ALA A 801      28.506 -15.681 -17.017  1.00 13.11           C  
ANISOU 6132  C   ALA A 801     1714   1592   1677     43   -235    335       C  
ATOM   6133  O   ALA A 801      27.711 -15.416 -17.904  1.00 19.08           O  
ANISOU 6133  O   ALA A 801     2481   2347   2420     85   -258    335       O  
ATOM   6134  CB  ALA A 801      27.612 -15.692 -14.693  1.00 16.88           C  
ANISOU 6134  CB  ALA A 801     2133   2091   2189      2   -214    337       C  
ATOM   6135  N   TYR A 802      29.741 -15.216 -17.009  1.00 13.80           N  
ANISOU 6135  N   TYR A 802     1830   1664   1748     23   -200    335       N  
ATOM   6136  CA  TYR A 802      30.195 -14.348 -18.070  1.00 14.06           C  
ANISOU 6136  CA  TYR A 802     1919   1673   1749     45   -174    341       C  
ATOM   6137  C   TYR A 802      30.298 -15.138 -19.398  1.00 19.82           C  
ANISOU 6137  C   TYR A 802     2663   2408   2459     70   -204    337       C  
ATOM   6138  O   TYR A 802      29.913 -14.645 -20.463  1.00 19.83           O  
ANISOU 6138  O   TYR A 802     2710   2398   2426    113   -208    346       O  
ATOM   6139  CB  TYR A 802      31.540 -13.747 -17.670  1.00 13.23           C  
ANISOU 6139  CB  TYR A 802     1830   1555   1642      3   -122    332       C  
ATOM   6140  CG  TYR A 802      31.786 -12.347 -18.197  1.00 17.98           C  
ANISOU 6140  CG  TYR A 802     2496   2116   2220     10    -69    341       C  
ATOM   6141  CD1 TYR A 802      32.377 -11.372 -17.392  1.00 18.73           C  
ANISOU 6141  CD1 TYR A 802     2602   2190   2325    -30    -20    329       C  
ATOM   6142  CD2 TYR A 802      31.449 -12.001 -19.510  1.00 19.37           C  
ANISOU 6142  CD2 TYR A 802     2730   2269   2359     56    -68    360       C  
ATOM   6143  CE1 TYR A 802      32.616 -10.065 -17.883  1.00 20.83           C  
ANISOU 6143  CE1 TYR A 802     2938   2404   2573    -29     38    338       C  
ATOM   6144  CE2 TYR A 802      31.678 -10.707 -20.006  1.00 17.47           C  
ANISOU 6144  CE2 TYR A 802     2566   1979   2093     65    -12    376       C  
ATOM   6145  CZ  TYR A 802      32.266  -9.751 -19.193  1.00 22.34           C  
ANISOU 6145  CZ  TYR A 802     3194   2566   2728     19     44    366       C  
ATOM   6146  OH  TYR A 802      32.487  -8.486 -19.687  1.00 22.45           O  
ANISOU 6146  OH  TYR A 802     3292   2519   2720     22    106    382       O  
ATOM   6147  N   TYR A 803      30.836 -16.354 -19.323  1.00 20.56           N  
ANISOU 6147  N   TYR A 803     2724   2517   2569     48   -224    324       N  
ATOM   6148  CA  TYR A 803      30.961 -17.220 -20.495  1.00 14.37           C  
ANISOU 6148  CA  TYR A 803     1952   1739   1770     69   -252    312       C  
ATOM   6149  C   TYR A 803      29.584 -17.522 -21.080  1.00 15.36           C  
ANISOU 6149  C   TYR A 803     2071   1875   1891    106   -304    307       C  
ATOM   6150  O   TYR A 803      29.423 -17.612 -22.300  1.00 17.28           O  
ANISOU 6150  O   TYR A 803     2347   2121   2098    142   -325    299       O  
ATOM   6151  CB  TYR A 803      31.664 -18.528 -20.139  1.00 13.14           C  
ANISOU 6151  CB  TYR A 803     1759   1591   1642     44   -267    296       C  
ATOM   6152  CG  TYR A 803      33.115 -18.374 -19.742  1.00 13.69           C  
ANISOU 6152  CG  TYR A 803     1824   1663   1716     17   -227    290       C  
ATOM   6153  CD1 TYR A 803      33.894 -17.339 -20.244  1.00 13.71           C  
ANISOU 6153  CD1 TYR A 803     1861   1657   1693     12   -174    289       C  
ATOM   6154  CD2 TYR A 803      33.707 -19.267 -18.860  1.00 13.59           C  
ANISOU 6154  CD2 TYR A 803     1772   1659   1733     -2   -241    283       C  
ATOM   6155  CE1 TYR A 803      35.236 -17.203 -19.879  1.00 16.12           C  
ANISOU 6155  CE1 TYR A 803     2146   1971   2009    -19   -137    272       C  
ATOM   6156  CE2 TYR A 803      35.035 -19.138 -18.490  1.00 15.07           C  
ANISOU 6156  CE2 TYR A 803     1942   1859   1925    -20   -213    269       C  
ATOM   6157  CZ  TYR A 803      35.797 -18.113 -19.001  1.00 17.96           C  
ANISOU 6157  CZ  TYR A 803     2327   2224   2273    -32   -162    259       C  
ATOM   6158  OH  TYR A 803      37.121 -18.008 -18.624  1.00 17.98           O  
ANISOU 6158  OH  TYR A 803     2297   2246   2289    -55   -135    235       O  
ATOM   6159  N   ALA A 804      28.589 -17.682 -20.210  1.00 17.20           N  
ANISOU 6159  N   ALA A 804     2258   2118   2159     97   -325    307       N  
ATOM   6160  CA  ALA A 804      27.241 -17.963 -20.703  1.00 21.83           C  
ANISOU 6160  CA  ALA A 804     2821   2724   2751    128   -376    292       C  
ATOM   6161  C   ALA A 804      26.719 -16.828 -21.582  1.00 20.65           C  
ANISOU 6161  C   ALA A 804     2714   2574   2557    189   -383    301       C  
ATOM   6162  O   ALA A 804      26.070 -17.074 -22.608  1.00 24.88           O  
ANISOU 6162  O   ALA A 804     3256   3128   3069    231   -433    284       O  
ATOM   6163  CB  ALA A 804      26.279 -18.274 -19.572  1.00 13.78           C  
ANISOU 6163  CB  ALA A 804     1739   1717   1780    102   -384    288       C  
ATOM   6164  N   ARG A 805      27.015 -15.597 -21.176  1.00 16.53           N  
ANISOU 6164  N   ARG A 805     2229   2031   2022    196   -336    326       N  
ATOM   6165  CA  ARG A 805      26.653 -14.415 -21.943  1.00 24.77           C  
ANISOU 6165  CA  ARG A 805     3332   3059   3020    257   -332    344       C  
ATOM   6166  C   ARG A 805      27.357 -14.454 -23.297  1.00 21.83           C  
ANISOU 6166  C   ARG A 805     3029   2676   2588    282   -329    350       C  
ATOM   6167  O   ARG A 805      26.732 -14.240 -24.333  1.00 24.96           O  
ANISOU 6167  O   ARG A 805     3462   3082   2940    345   -368    352       O  
ATOM   6168  CB  ARG A 805      27.057 -13.135 -21.200  1.00 34.64           C  
ANISOU 6168  CB  ARG A 805     4618   4273   4271    247   -269    367       C  
ATOM   6169  CG  ARG A 805      26.250 -12.830 -19.946  1.00 57.14           C  
ANISOU 6169  CG  ARG A 805     7414   7131   7164    238   -265    361       C  
ATOM   6170  CD  ARG A 805      26.685 -11.514 -19.300  1.00 69.79           C  
ANISOU 6170  CD  ARG A 805     9063   8691   8763    230   -202    376       C  
ATOM   6171  NE  ARG A 805      27.135 -10.533 -20.291  1.00 81.57           N  
ANISOU 6171  NE  ARG A 805    10648  10137  10207    266   -172    400       N  
ATOM   6172  CZ  ARG A 805      26.362  -9.594 -20.832  1.00 87.62           C  
ANISOU 6172  CZ  ARG A 805    11465  10880  10948    340   -179    419       C  
ATOM   6173  NH1 ARG A 805      25.085  -9.501 -20.481  1.00 91.29           N1+
ANISOU 6173  NH1 ARG A 805    11883  11370  11435    389   -220    408       N1+
ATOM   6174  NH2 ARG A 805      26.866  -8.744 -21.723  1.00 84.73           N  
ANISOU 6174  NH2 ARG A 805    11199  10464  10533    368   -143    448       N  
ATOM   6175  N   LEU A 806      28.661 -14.723 -23.280  1.00 17.66           N  
ANISOU 6175  N   LEU A 806     2518   2134   2058    235   -283    351       N  
ATOM   6176  CA  LEU A 806      29.430 -14.784 -24.514  1.00 20.19           C  
ANISOU 6176  CA  LEU A 806     2902   2445   2323    250   -265    354       C  
ATOM   6177  C   LEU A 806      28.857 -15.833 -25.471  1.00 18.66           C  
ANISOU 6177  C   LEU A 806     2698   2285   2108    284   -334    326       C  
ATOM   6178  O   LEU A 806      28.729 -15.587 -26.673  1.00 21.02           O  
ANISOU 6178  O   LEU A 806     3061   2586   2340    335   -348    332       O  
ATOM   6179  CB  LEU A 806      30.899 -15.078 -24.213  1.00 17.04           C  
ANISOU 6179  CB  LEU A 806     2496   2037   1941    190   -208    346       C  
ATOM   6180  CG  LEU A 806      31.582 -13.986 -23.388  1.00 21.26           C  
ANISOU 6180  CG  LEU A 806     3044   2541   2493    151   -138    362       C  
ATOM   6181  CD1 LEU A 806      33.016 -14.351 -23.016  1.00 16.66           C  
ANISOU 6181  CD1 LEU A 806     2433   1963   1935     92    -92    343       C  
ATOM   6182  CD2 LEU A 806      31.524 -12.641 -24.109  1.00 15.47           C  
ANISOU 6182  CD2 LEU A 806     2403   1766   1707    184    -93    394       C  
ATOM   6183  N   VAL A 807      28.520 -16.995 -24.921  1.00 21.46           N  
ANISOU 6183  N   VAL A 807     2977   2662   2515    254   -376    296       N  
ATOM   6184  CA  VAL A 807      27.992 -18.109 -25.691  1.00 23.63           C  
ANISOU 6184  CA  VAL A 807     3231   2963   2784    271   -440    259       C  
ATOM   6185  C   VAL A 807      26.658 -17.724 -26.310  1.00 25.16           C  
ANISOU 6185  C   VAL A 807     3427   3182   2949    333   -503    251       C  
ATOM   6186  O   VAL A 807      26.407 -17.993 -27.486  1.00 26.94           O  
ANISOU 6186  O   VAL A 807     3686   3428   3121    377   -547    230       O  
ATOM   6187  CB  VAL A 807      27.807 -19.374 -24.814  1.00 21.01           C  
ANISOU 6187  CB  VAL A 807     2821   2636   2524    218   -464    231       C  
ATOM   6188  CG1 VAL A 807      26.924 -20.400 -25.518  1.00 15.25           C  
ANISOU 6188  CG1 VAL A 807     2063   1929   1800    231   -535    185       C  
ATOM   6189  CG2 VAL A 807      29.154 -19.984 -24.464  1.00 14.45           C  
ANISOU 6189  CG2 VAL A 807     1992   1785   1712    176   -421    231       C  
ATOM   6190  N   ALA A 808      25.797 -17.084 -25.526  1.00 20.75           N  
ANISOU 6190  N   ALA A 808     2831   2628   2423    342   -510    263       N  
ATOM   6191  CA  ALA A 808      24.519 -16.650 -26.077  1.00 18.17           C  
ANISOU 6191  CA  ALA A 808     2498   2333   2074    412   -573    252       C  
ATOM   6192  C   ALA A 808      24.732 -15.607 -27.172  1.00 18.52           C  
ANISOU 6192  C   ALA A 808     2646   2363   2027    487   -566    285       C  
ATOM   6193  O   ALA A 808      24.049 -15.634 -28.190  1.00 20.01           O  
ANISOU 6193  O   ALA A 808     2855   2584   2165    553   -632    268       O  
ATOM   6194  CB  ALA A 808      23.609 -16.110 -24.999  1.00 16.29           C  
ANISOU 6194  CB  ALA A 808     2198   2103   1890    412   -572    257       C  
ATOM   6195  N   PHE A 809      25.679 -14.694 -26.969  1.00 24.49           N  
ANISOU 6195  N   PHE A 809     3471   3072   2762    474   -486    330       N  
ATOM   6196  CA  PHE A 809      25.958 -13.677 -27.985  1.00 24.89           C  
ANISOU 6196  CA  PHE A 809     3636   3095   2725    537   -462    369       C  
ATOM   6197  C   PHE A 809      26.545 -14.267 -29.254  1.00 26.06           C  
ANISOU 6197  C   PHE A 809     3843   3256   2803    551   -471    358       C  
ATOM   6198  O   PHE A 809      26.249 -13.785 -30.346  1.00 27.29           O  
ANISOU 6198  O   PHE A 809     4081   3415   2873    627   -495    375       O  
ATOM   6199  CB  PHE A 809      26.869 -12.567 -27.461  1.00 34.22           C  
ANISOU 6199  CB  PHE A 809     4878   4215   3908    507   -364    414       C  
ATOM   6200  CG  PHE A 809      26.196 -11.647 -26.502  1.00 41.61           C  
ANISOU 6200  CG  PHE A 809     5794   5131   4885    522   -355    430       C  
ATOM   6201  CD1 PHE A 809      24.815 -11.539 -26.483  1.00 41.92           C  
ANISOU 6201  CD1 PHE A 809     5790   5204   4933    590   -429    418       C  
ATOM   6202  CD2 PHE A 809      26.939 -10.901 -25.602  1.00 50.06           C  
ANISOU 6202  CD2 PHE A 809     6879   6153   5987    468   -273    450       C  
ATOM   6203  CE1 PHE A 809      24.186 -10.693 -25.583  1.00 47.04           C  
ANISOU 6203  CE1 PHE A 809     6416   5834   5622    608   -416    428       C  
ATOM   6204  CE2 PHE A 809      26.316 -10.056 -24.696  1.00 49.80           C  
ANISOU 6204  CE2 PHE A 809     6831   6100   5991    483   -262    458       C  
ATOM   6205  CZ  PHE A 809      24.939  -9.952 -24.688  1.00 47.69           C  
ANISOU 6205  CZ  PHE A 809     6525   5864   5732    556   -331    449       C  
ATOM   6206  N   ARG A 810      27.374 -15.300 -29.118  1.00 19.27           N  
ANISOU 6206  N   ARG A 810     2946   2401   1973    485   -450    329       N  
ATOM   6207  CA  ARG A 810      27.945 -15.937 -30.296  1.00 21.38           C  
ANISOU 6207  CA  ARG A 810     3265   2683   2177    497   -453    310       C  
ATOM   6208  C   ARG A 810      26.849 -16.605 -31.140  1.00 24.90           C  
ANISOU 6208  C   ARG A 810     3694   3179   2587    554   -559    266       C  
ATOM   6209  O   ARG A 810      26.880 -16.546 -32.367  1.00 31.51           O  
ANISOU 6209  O   ARG A 810     4610   4031   3333    610   -578    265       O  
ATOM   6210  CB  ARG A 810      29.045 -16.952 -29.943  1.00 17.00           C  
ANISOU 6210  CB  ARG A 810     2668   2123   1669    422   -413    281       C  
ATOM   6211  CG  ARG A 810      29.538 -17.744 -31.174  1.00 22.61           C  
ANISOU 6211  CG  ARG A 810     3423   2852   2317    439   -421    249       C  
ATOM   6212  CD  ARG A 810      30.225 -16.828 -32.203  1.00 20.14           C  
ANISOU 6212  CD  ARG A 810     3228   2520   1905    474   -355    287       C  
ATOM   6213  NE  ARG A 810      31.266 -16.041 -31.543  1.00 20.49           N  
ANISOU 6213  NE  ARG A 810     3285   2522   1979    421   -253    324       N  
ATOM   6214  CZ  ARG A 810      32.455 -16.525 -31.195  1.00 22.06           C  
ANISOU 6214  CZ  ARG A 810     3448   2714   2219    359   -191    306       C  
ATOM   6215  NH1 ARG A 810      32.763 -17.775 -31.485  1.00 17.31           N1+
ANISOU 6215  NH1 ARG A 810     2808   2138   1630    349   -217    257       N1+
ATOM   6216  NH2 ARG A 810      33.335 -15.759 -30.561  1.00 23.90           N  
ANISOU 6216  NH2 ARG A 810     3682   2916   2483    310   -105    331       N  
ATOM   6217  N   ALA A 811      25.878 -17.220 -30.472  1.00 17.97           N  
ANISOU 6217  N   ALA A 811     2715   2330   1783    539   -623    229       N  
ATOM   6218  CA  ALA A 811      24.801 -17.902 -31.167  1.00 18.61           C  
ANISOU 6218  CA  ALA A 811     2760   2463   1847    580   -726    174       C  
ATOM   6219  C   ALA A 811      23.948 -16.922 -31.942  1.00 22.33           C  
ANISOU 6219  C   ALA A 811     3285   2959   2239    683   -779    194       C  
ATOM   6220  O   ALA A 811      23.381 -17.287 -32.963  1.00 21.84           O  
ANISOU 6220  O   ALA A 811     3238   2942   2118    738   -858    155       O  
ATOM   6221  CB  ALA A 811      23.952 -18.688 -30.214  1.00 20.65           C  
ANISOU 6221  CB  ALA A 811     2896   2743   2208    531   -769    131       C  
ATOM   6222  N   ARG A 812      23.845 -15.685 -31.462  1.00 26.21           N  
ANISOU 6222  N   ARG A 812     3809   3420   2730    713   -739    251       N  
ATOM   6223  CA  ARG A 812      23.138 -14.657 -32.235  1.00 29.23           C  
ANISOU 6223  CA  ARG A 812     4265   3814   3029    825   -783    280       C  
ATOM   6224  C   ARG A 812      23.851 -14.406 -33.581  1.00 25.63           C  
ANISOU 6224  C   ARG A 812     3947   3345   2447    873   -763    308       C  
ATOM   6225  O   ARG A 812      23.207 -14.253 -34.613  1.00 28.29           O  
ANISOU 6225  O   ARG A 812     4334   3720   2696    966   -839    300       O  
ATOM   6226  CB  ARG A 812      22.961 -13.362 -31.430  1.00 20.28           C  
ANISOU 6226  CB  ARG A 812     3150   2635   1921    847   -734    336       C  
ATOM   6227  CG  ARG A 812      21.983 -12.365 -32.050  1.00 38.91           C  
ANISOU 6227  CG  ARG A 812     5564   5007   4214    975   -796    361       C  
ATOM   6228  CD  ARG A 812      20.541 -12.886 -32.100  1.00 42.33           C  
ANISOU 6228  CD  ARG A 812     5882   5522   4679   1025   -919    296       C  
ATOM   6229  NE  ARG A 812      19.888 -12.881 -30.789  1.00 43.05           N  
ANISOU 6229  NE  ARG A 812     5850   5621   4885    984   -913    275       N  
ATOM   6230  CZ  ARG A 812      18.685 -13.399 -30.545  1.00 42.04           C  
ANISOU 6230  CZ  ARG A 812     5595   5562   4815    998   -997    211       C  
ATOM   6231  NH1 ARG A 812      17.997 -13.974 -31.519  1.00 42.95           N1+
ANISOU 6231  NH1 ARG A 812     5683   5746   4889   1051  -1102    157       N1+
ATOM   6232  NH2 ARG A 812      18.171 -13.358 -29.323  1.00 42.45           N  
ANISOU 6232  NH2 ARG A 812     5544   5617   4967    955   -974    197       N  
ATOM   6233  N   TYR A 813      25.183 -14.399 -33.565  1.00 27.09           N  
ANISOU 6233  N   TYR A 813     4189   3482   2621    810   -661    336       N  
ATOM   6234  CA  TYR A 813      25.968 -14.320 -34.799  1.00 23.30           C  
ANISOU 6234  CA  TYR A 813     3832   2993   2029    838   -624    355       C  
ATOM   6235  C   TYR A 813      25.768 -15.536 -35.712  1.00 23.69           C  
ANISOU 6235  C   TYR A 813     3863   3103   2036    851   -700    286       C  
ATOM   6236  O   TYR A 813      25.696 -15.385 -36.923  1.00 22.57           O  
ANISOU 6236  O   TYR A 813     3819   2981   1776    924   -728    291       O  
ATOM   6237  CB  TYR A 813      27.460 -14.104 -34.504  1.00 20.67           C  
ANISOU 6237  CB  TYR A 813     3541   2602   1710    757   -491    388       C  
ATOM   6238  CG  TYR A 813      27.788 -12.690 -34.060  1.00 26.63           C  
ANISOU 6238  CG  TYR A 813     4366   3290   2464    759   -406    460       C  
ATOM   6239  CD1 TYR A 813      27.743 -11.634 -34.959  1.00 28.83           C  
ANISOU 6239  CD1 TYR A 813     4786   3534   2633    836   -380    519       C  
ATOM   6240  CD2 TYR A 813      28.138 -12.409 -32.744  1.00 21.27           C  
ANISOU 6240  CD2 TYR A 813     3619   2577   1888    685   -350    467       C  
ATOM   6241  CE1 TYR A 813      28.032 -10.332 -34.569  1.00 28.16           C  
ANISOU 6241  CE1 TYR A 813     4775   3375   2551    835   -296    583       C  
ATOM   6242  CE2 TYR A 813      28.433 -11.096 -32.342  1.00 27.31           C  
ANISOU 6242  CE2 TYR A 813     4450   3274   2653    682   -271    524       C  
ATOM   6243  CZ  TYR A 813      28.375 -10.068 -33.269  1.00 33.09           C  
ANISOU 6243  CZ  TYR A 813     5324   3965   3283    756   -242    582       C  
ATOM   6244  OH  TYR A 813      28.664  -8.776 -32.908  1.00 43.04           O  
ANISOU 6244  OH  TYR A 813     6661   5147   4546    751   -159    637       O  
ATOM   6245  N   HIS A 814      25.662 -16.731 -35.136  1.00 25.29           N  
ANISOU 6245  N   HIS A 814     3949   3329   2331    783   -733    221       N  
ATOM   6246  CA  HIS A 814      25.425 -17.934 -35.940  1.00 24.35           C  
ANISOU 6246  CA  HIS A 814     3808   3259   2183    788   -806    145       C  
ATOM   6247  C   HIS A 814      24.072 -17.897 -36.648  1.00 29.23           C  
ANISOU 6247  C   HIS A 814     4416   3941   2748    877   -934    108       C  
ATOM   6248  O   HIS A 814      23.886 -18.530 -37.692  1.00 36.02           O  
ANISOU 6248  O   HIS A 814     5306   4846   3536    913   -998     55       O  
ATOM   6249  CB  HIS A 814      25.490 -19.190 -35.062  1.00 24.82           C  
ANISOU 6249  CB  HIS A 814     3747   3319   2366    695   -813     88       C  
ATOM   6250  CG  HIS A 814      26.838 -19.459 -34.481  1.00 19.83           C  
ANISOU 6250  CG  HIS A 814     3116   2637   1780    618   -708    108       C  
ATOM   6251  CD2 HIS A 814      28.077 -19.029 -34.834  1.00 19.79           C  
ANISOU 6251  CD2 HIS A 814     3194   2600   1724    609   -612    147       C  
ATOM   6252  ND1 HIS A 814      27.030 -20.292 -33.392  1.00 25.58           N  
ANISOU 6252  ND1 HIS A 814     3748   3348   2622    538   -694     84       N  
ATOM   6253  CE1 HIS A 814      28.314 -20.358 -33.101  1.00 22.86           C  
ANISOU 6253  CE1 HIS A 814     3424   2968   2294    493   -604    105       C  
ATOM   6254  NE2 HIS A 814      28.975 -19.600 -33.974  1.00 25.64           N  
ANISOU 6254  NE2 HIS A 814     3878   3312   2551    530   -551    139       N  
ATOM   6255  N   LEU A 815      23.117 -17.173 -36.077  1.00 28.46           N  
ANISOU 6255  N   LEU A 815     4272   3853   2687    917   -974    129       N  
ATOM   6256  CA  LEU A 815      21.781 -17.113 -36.661  1.00 29.74           C  
ANISOU 6256  CA  LEU A 815     4405   4085   2811   1006  -1103     88       C  
ATOM   6257  C   LEU A 815      21.684 -16.085 -37.771  1.00 31.35           C  
ANISOU 6257  C   LEU A 815     4749   4296   2867   1129  -1125    140       C  
ATOM   6258  O   LEU A 815      20.697 -16.053 -38.501  1.00 35.54           O  
ANISOU 6258  O   LEU A 815     5265   4885   3355   1203  -1220    101       O  
ATOM   6259  CB  LEU A 815      20.725 -16.817 -35.597  1.00 29.26           C  
ANISOU 6259  CB  LEU A 815     4224   4040   2855   1004  -1141     79       C  
ATOM   6260  CG  LEU A 815      20.416 -17.959 -34.633  1.00 26.63           C  
ANISOU 6260  CG  LEU A 815     3743   3720   2658    898  -1150     13       C  
ATOM   6261  CD1 LEU A 815      19.757 -17.437 -33.353  1.00 29.51           C  
ANISOU 6261  CD1 LEU A 815     4013   4075   3124    879  -1133     32       C  
ATOM   6262  CD2 LEU A 815      19.560 -19.033 -35.299  1.00 26.92           C  
ANISOU 6262  CD2 LEU A 815     3705   3828   2695    903  -1265    -89       C  
ATOM   6263  N   VAL A 816      22.690 -15.228 -37.891  1.00 29.79           N  
ANISOU 6263  N   VAL A 816     4675   4030   2612   1132  -1015    224       N  
ATOM   6264  CA  VAL A 816      22.662 -14.221 -38.942  1.00 36.06           C  
ANISOU 6264  CA  VAL A 816     5608   4811   3281   1227  -1003    279       C  
ATOM   6265  C   VAL A 816      22.657 -14.949 -40.283  1.00 46.31           C  
ANISOU 6265  C   VAL A 816     6949   6162   4484   1256  -1053    224       C  
ATOM   6266  O   VAL A 816      23.570 -15.723 -40.578  1.00 45.37           O  
ANISOU 6266  O   VAL A 816     6868   6042   4328   1210  -1019    203       O  
ATOM   6267  CB  VAL A 816      23.858 -13.264 -38.857  1.00 34.62           C  
ANISOU 6267  CB  VAL A 816     5558   4541   3057   1208   -862    374       C  
ATOM   6268  CG1 VAL A 816      23.973 -12.461 -40.137  1.00 33.96           C  
ANISOU 6268  CG1 VAL A 816     5612   4437   2853   1276   -827    416       C  
ATOM   6269  CG2 VAL A 816      23.697 -12.334 -37.668  1.00 35.99           C  
ANISOU 6269  CG2 VAL A 816     5701   4659   3314   1196   -818    427       C  
ATOM   6270  N   ASP A 817      21.610 -14.736 -41.076  1.00 55.01           N  
ANISOU 6270  N   ASP A 817     8043   7313   5546   1333  -1137    194       N  
ATOM   6271  CA  ASP A 817      21.447 -15.524 -42.292  1.00 73.36           C  
ANISOU 6271  CA  ASP A 817    10389   9697   7788   1359  -1201    127       C  
ATOM   6272  C   ASP A 817      21.769 -14.734 -43.557  1.00 80.21           C  
ANISOU 6272  C   ASP A 817    11414  10545   8518   1434  -1159    181       C  
ATOM   6273  O   ASP A 817      21.897 -15.313 -44.634  1.00 89.18           O  
ANISOU 6273  O   ASP A 817    12599  11719   9567   1454  -1188    138       O  
ATOM   6274  CB  ASP A 817      20.039 -16.116 -42.374  1.00 83.34           C  
ANISOU 6274  CB  ASP A 817    11518  11042   9104   1384  -1337     34       C  
ATOM   6275  CG  ASP A 817      19.002 -15.095 -42.791  1.00 91.91           C  
ANISOU 6275  CG  ASP A 817    12615  12146  10159   1484  -1385     58       C  
ATOM   6276  OD1 ASP A 817      19.115 -13.921 -42.378  1.00 97.09           O  
ANISOU 6276  OD1 ASP A 817    13327  12745  10819   1515  -1322    142       O  
ATOM   6277  OD2 ASP A 817      18.073 -15.467 -43.536  1.00 94.14           O1-
ANISOU 6277  OD2 ASP A 817    12853  12500  10415   1532  -1487    -11       O1-
ATOM   6278  N   LYS A 818      21.881 -13.416 -43.416  1.00 78.18           N  
ANISOU 6278  N   LYS A 818    11237  10225   8243   1473  -1090    271       N  
ATOM   6279  CA  LYS A 818      22.325 -12.538 -44.500  1.00 80.53           C  
ANISOU 6279  CA  LYS A 818    11698  10484   8416   1533  -1027    336       C  
ATOM   6280  C   LYS A 818      21.427 -12.592 -45.751  1.00 79.71           C  
ANISOU 6280  C   LYS A 818    11621  10444   8221   1630  -1128    296       C  
ATOM   6281  O   LYS A 818      21.664 -13.359 -46.693  1.00 68.17           O  
ANISOU 6281  O   LYS A 818    10194   9026   6682   1634  -1154    249       O  
ATOM   6282  CB  LYS A 818      23.799 -12.816 -44.842  1.00 78.08           C  
ANISOU 6282  CB  LYS A 818    11489  10131   8045   1470   -908    365       C  
ATOM   6283  CG  LYS A 818      24.468 -11.759 -45.716  1.00 77.48           C  
ANISOU 6283  CG  LYS A 818    11585   9991   7861   1508   -803    449       C  
ATOM   6284  CD  LYS A 818      24.392 -12.143 -47.186  1.00 74.45           C  
ANISOU 6284  CD  LYS A 818    11282   9658   7350   1567   -842    418       C  
ATOM   6285  CE  LYS A 818      25.307 -11.309 -48.061  1.00 67.15           C  
ANISOU 6285  CE  LYS A 818    10530   8668   6315   1581   -717    497       C  
ATOM   6286  NZ  LYS A 818      25.453 -11.952 -49.391  1.00 57.89           N1+
ANISOU 6286  NZ  LYS A 818     9425   7549   5021   1617   -744    456       N1+
ATOM   6287  N   ARG A 835      12.329 -26.682 -42.536  1.00100.29           N  
ANISOU 6287  N   ARG A 835    12465  13678  11961    850  -2089  -1071       N  
ATOM   6288  CA  ARG A 835      11.348 -26.017 -41.685  1.00 96.22           C  
ANISOU 6288  CA  ARG A 835    11834  13192  11534    858  -2096  -1050       C  
ATOM   6289  C   ARG A 835      12.106 -25.158 -40.677  1.00 85.11           C  
ANISOU 6289  C   ARG A 835    10474  11724  10140    870  -2009   -929       C  
ATOM   6290  O   ARG A 835      13.207 -25.519 -40.267  1.00 82.03           O  
ANISOU 6290  O   ARG A 835    10146  11265   9754    818  -1946   -895       O  
ATOM   6291  CB  ARG A 835      10.454 -27.038 -40.969  1.00 99.13           C  
ANISOU 6291  CB  ARG A 835    12034  13574  12059    736  -2111  -1151       C  
ATOM   6292  CG  ARG A 835      10.313 -28.399 -41.674  1.00 99.84           C  
ANISOU 6292  CG  ARG A 835    12100  13670  12163    660  -2155  -1274       C  
ATOM   6293  CD  ARG A 835       9.784 -28.284 -43.105  1.00100.64           C  
ANISOU 6293  CD  ARG A 835    12236  13850  12152    750  -2248  -1329       C  
ATOM   6294  NE  ARG A 835       8.471 -27.651 -43.176  1.00103.06           N  
ANISOU 6294  NE  ARG A 835    12440  14239  12480    809  -2313  -1351       N  
ATOM   6295  CZ  ARG A 835       7.333 -28.310 -43.378  1.00106.46           C  
ANISOU 6295  CZ  ARG A 835    12741  14730  12980    762  -2378  -1466       C  
ATOM   6296  NH1 ARG A 835       7.345 -29.629 -43.530  1.00107.08           N1+
ANISOU 6296  NH1 ARG A 835    12782  14788  13115    650  -2384  -1567       N1+
ATOM   6297  NH2 ARG A 835       6.183 -27.652 -43.430  1.00107.75           N  
ANISOU 6297  NH2 ARG A 835    12812  14970  13157    826  -2437  -1483       N  
ATOM   6298  N   ASP A 836      11.523 -24.029 -40.280  1.00 78.27           N  
ANISOU 6298  N   ASP A 836     9579  10881   9280    940  -2008   -868       N  
ATOM   6299  CA  ASP A 836      12.263 -23.025 -39.509  1.00 70.53           C  
ANISOU 6299  CA  ASP A 836     8668   9843   8288    972  -1928   -747       C  
ATOM   6300  C   ASP A 836      12.715 -23.418 -38.089  1.00 65.48           C  
ANISOU 6300  C   ASP A 836     7967   9145   7767    867  -1857   -727       C  
ATOM   6301  O   ASP A 836      13.903 -23.311 -37.791  1.00 63.08           O  
ANISOU 6301  O   ASP A 836     7759   8777   7433    855  -1793   -659       O  
ATOM   6302  CB  ASP A 836      11.561 -21.660 -39.524  1.00 68.75           C  
ANISOU 6302  CB  ASP A 836     8445   9649   8030   1083  -1943   -687       C  
ATOM   6303  CG  ASP A 836      12.474 -20.542 -40.007  1.00 71.90           C  
ANISOU 6303  CG  ASP A 836     9018  10002   8300   1180  -1895   -573       C  
ATOM   6304  OD1 ASP A 836      13.471 -20.843 -40.694  1.00 68.10           O  
ANISOU 6304  OD1 ASP A 836     8656   9490   7730   1179  -1871   -556       O  
ATOM   6305  OD2 ASP A 836      12.197 -19.361 -39.703  1.00 78.53           O1-
ANISOU 6305  OD2 ASP A 836     9877  10832   9128   1254  -1875   -501       O1-
ATOM   6306  N   PRO A 837      11.789 -23.870 -37.214  1.00 60.98           N  
ANISOU 6306  N   PRO A 837     7239   8597   7332    791  -1866   -785       N  
ATOM   6307  CA  PRO A 837      12.214 -24.190 -35.840  1.00 54.54           C  
ANISOU 6307  CA  PRO A 837     6372   7725   6627    694  -1795   -759       C  
ATOM   6308  C   PRO A 837      13.323 -25.238 -35.787  1.00 49.99           C  
ANISOU 6308  C   PRO A 837     5853   7083   6058    610  -1763   -776       C  
ATOM   6309  O   PRO A 837      14.205 -25.173 -34.925  1.00 44.22           O  
ANISOU 6309  O   PRO A 837     5161   6282   5359    568  -1683   -708       O  
ATOM   6310  CB  PRO A 837      10.939 -24.743 -35.196  1.00 55.68           C  
ANISOU 6310  CB  PRO A 837     6339   7911   6906    615  -1813   -843       C  
ATOM   6311  CG  PRO A 837       9.825 -24.147 -35.991  1.00 54.25           C  
ANISOU 6311  CG  PRO A 837     6120   7813   6681    708  -1885   -875       C  
ATOM   6312  CD  PRO A 837      10.344 -24.101 -37.402  1.00 58.40           C  
ANISOU 6312  CD  PRO A 837     6777   8348   7064    786  -1933   -874       C  
ATOM   6313  N   GLN A 838      13.284 -26.191 -36.712  1.00 54.06           N  
ANISOU 6313  N   GLN A 838     6381   7611   6547    583  -1809   -862       N  
ATOM   6314  CA  GLN A 838      14.358 -27.168 -36.819  1.00 55.33           C  
ANISOU 6314  CA  GLN A 838     6612   7708   6702    518  -1784   -884       C  
ATOM   6315  C   GLN A 838      15.597 -26.551 -37.474  1.00 46.29           C  
ANISOU 6315  C   GLN A 838     5635   6537   5417    604  -1757   -804       C  
ATOM   6316  O   GLN A 838      16.727 -26.972 -37.205  1.00 43.78           O  
ANISOU 6316  O   GLN A 838     5391   6136   5108    550  -1660   -760       O  
ATOM   6317  CB  GLN A 838      13.888 -28.417 -37.567  1.00 67.14           C  
ANISOU 6317  CB  GLN A 838     8068   9221   8223    457  -1835  -1009       C  
ATOM   6318  CG  GLN A 838      12.859 -29.241 -36.797  1.00 81.26           C  
ANISOU 6318  CG  GLN A 838     9698  11011  10166    340  -1836  -1088       C  
ATOM   6319  CD  GLN A 838      13.348 -29.662 -35.413  1.00 93.66           C  
ANISOU 6319  CD  GLN A 838    11234  12499  11855    237  -1760  -1057       C  
ATOM   6320  NE2 GLN A 838      13.934 -30.856 -35.328  1.00 96.77           N  
ANISOU 6320  NE2 GLN A 838    11661  12810  12298    141  -1712  -1092       N  
ATOM   6321  OE1 GLN A 838      13.198 -28.924 -34.433  1.00 97.80           O  
ANISOU 6321  OE1 GLN A 838    11719  13016  12424    240  -1703   -979       O  
ATOM   6322  N   ALA A 839      15.382 -25.538 -38.313  1.00 39.22           N  
ANISOU 6322  N   ALA A 839     4806   5688   4408    718  -1781   -760       N  
ATOM   6323  CA  ALA A 839      16.486 -24.838 -38.974  1.00 37.69           C  
ANISOU 6323  CA  ALA A 839     4776   5469   4076    798  -1741   -677       C  
ATOM   6324  C   ALA A 839      17.221 -23.888 -38.017  1.00 35.14           C  
ANISOU 6324  C   ALA A 839     4499   5088   3763    809  -1650   -557       C  
ATOM   6325  O   ALA A 839      18.443 -23.737 -38.105  1.00 36.85           O  
ANISOU 6325  O   ALA A 839     4826   5243   3930    802  -1558   -489       O  
ATOM   6326  CB  ALA A 839      15.996 -24.086 -40.225  1.00 31.03           C  
ANISOU 6326  CB  ALA A 839     3997   4682   3110    910  -1787   -667       C  
ATOM   6327  N   LEU A 840      16.480 -23.255 -37.106  1.00 33.97           N  
ANISOU 6327  N   LEU A 840     4262   4953   3694    812  -1649   -528       N  
ATOM   6328  CA  LEU A 840      17.094 -22.366 -36.120  1.00 32.95           C  
ANISOU 6328  CA  LEU A 840     4167   4759   3594    803  -1538   -414       C  
ATOM   6329  C   LEU A 840      17.918 -23.147 -35.099  1.00 24.18           C  
ANISOU 6329  C   LEU A 840     3034   3567   2586    676  -1431   -396       C  
ATOM   6330  O   LEU A 840      19.014 -22.727 -34.748  1.00 26.06           O  
ANISOU 6330  O   LEU A 840     3354   3743   2805    665  -1333   -314       O  
ATOM   6331  CB  LEU A 840      16.054 -21.469 -35.440  1.00 37.72           C  
ANISOU 6331  CB  LEU A 840     4685   5399   4248    849  -1567   -395       C  
ATOM   6332  CG  LEU A 840      15.354 -20.456 -36.358  1.00 36.86           C  
ANISOU 6332  CG  LEU A 840     4619   5343   4045    975  -1624   -379       C  
ATOM   6333  CD1 LEU A 840      14.188 -19.797 -35.660  1.00 32.16           C  
ANISOU 6333  CD1 LEU A 840     3912   4782   3526   1001  -1640   -380       C  
ATOM   6334  CD2 LEU A 840      16.320 -19.391 -36.862  1.00 39.95           C  
ANISOU 6334  CD2 LEU A 840     5180   5686   4315   1053  -1563   -273       C  
ATOM   6335  N   ALA A 841      17.411 -24.303 -34.666  1.00 24.29           N  
ANISOU 6335  N   ALA A 841     2942   3583   2706    583  -1452   -476       N  
ATOM   6336  CA  ALA A 841      18.152 -25.163 -33.735  1.00 28.44           C  
ANISOU 6336  CA  ALA A 841     3454   4028   3323    470  -1359   -461       C  
ATOM   6337  C   ALA A 841      19.471 -25.645 -34.347  1.00 31.20           C  
ANISOU 6337  C   ALA A 841     3916   4328   3609    464  -1311   -447       C  
ATOM   6338  O   ALA A 841      20.505 -25.654 -33.682  1.00 30.83           O  
ANISOU 6338  O   ALA A 841     3910   4215   3587    423  -1215   -384       O  
ATOM   6339  CB  ALA A 841      17.294 -26.355 -33.281  1.00 26.85           C  
ANISOU 6339  CB  ALA A 841     3130   3832   3241    373  -1390   -553       C  
ATOM   6340  N   LYS A 842      19.433 -26.026 -35.622  1.00 31.23           N  
ANISOU 6340  N   LYS A 842     3968   4370   3528    508  -1381   -512       N  
ATOM   6341  CA  LYS A 842      20.637 -26.458 -36.331  1.00 35.37           C  
ANISOU 6341  CA  LYS A 842     4600   4856   3981    512  -1337   -509       C  
ATOM   6342  C   LYS A 842      21.673 -25.344 -36.487  1.00 32.71           C  
ANISOU 6342  C   LYS A 842     4376   4498   3555    571  -1259   -405       C  
ATOM   6343  O   LYS A 842      22.872 -25.591 -36.357  1.00 28.34           O  
ANISOU 6343  O   LYS A 842     3879   3889   2999    541  -1173   -372       O  
ATOM   6344  CB  LYS A 842      20.282 -27.020 -37.714  1.00 47.75           C  
ANISOU 6344  CB  LYS A 842     6200   6479   5464    555  -1432   -606       C  
ATOM   6345  CG  LYS A 842      21.443 -27.736 -38.401  1.00 57.21           C  
ANISOU 6345  CG  LYS A 842     7493   7636   6607    544  -1386   -626       C  
ATOM   6346  CD  LYS A 842      22.234 -26.818 -39.336  1.00 64.28           C  
ANISOU 6346  CD  LYS A 842     8523   8549   7351    637  -1355   -565       C  
ATOM   6347  CE  LYS A 842      23.744 -27.086 -39.264  1.00 67.21           C  
ANISOU 6347  CE  LYS A 842     8970   8853   7714    607  -1238   -523       C  
ATOM   6348  NZ  LYS A 842      24.391 -26.577 -38.003  1.00 62.36           N1+
ANISOU 6348  NZ  LYS A 842     8332   8181   7182    563  -1137   -429       N1+
ATOM   6349  N   ALA A 843      21.214 -24.127 -36.771  1.00 23.51           N  
ANISOU 6349  N   ALA A 843     3241   3374   2319    657  -1288   -358       N  
ATOM   6350  CA  ALA A 843      22.117 -23.002 -37.006  1.00 39.60           C  
ANISOU 6350  CA  ALA A 843     5394   5386   4266    712  -1213   -262       C  
ATOM   6351  C   ALA A 843      22.975 -22.727 -35.777  1.00 34.35           C  
ANISOU 6351  C   ALA A 843     4717   4652   3683    646  -1098   -188       C  
ATOM   6352  O   ALA A 843      24.067 -22.156 -35.855  1.00 29.51           O  
ANISOU 6352  O   ALA A 843     4189   4001   3022    653  -1011   -124       O  
ATOM   6353  CB  ALA A 843      21.323 -21.754 -37.372  1.00 23.85           C  
ANISOU 6353  CB  ALA A 843     3429   3436   2197    816  -1267   -222       C  
ATOM   6354  N   VAL A 844      22.466 -23.160 -34.638  1.00 30.02           N  
ANISOU 6354  N   VAL A 844     4059   4090   3257    577  -1099   -203       N  
ATOM   6355  CA  VAL A 844      23.036 -22.812 -33.361  1.00 29.13           C  
ANISOU 6355  CA  VAL A 844     3924   3925   3221    523  -1008   -137       C  
ATOM   6356  C   VAL A 844      23.920 -23.961 -32.845  1.00 30.53           C  
ANISOU 6356  C   VAL A 844     4083   4051   3467    438   -954   -156       C  
ATOM   6357  O   VAL A 844      24.684 -23.807 -31.896  1.00 25.58           O  
ANISOU 6357  O   VAL A 844     3452   3379   2887    395   -875   -104       O  
ATOM   6358  CB  VAL A 844      21.879 -22.398 -32.420  1.00 30.52           C  
ANISOU 6358  CB  VAL A 844     4002   4122   3473    515  -1039   -133       C  
ATOM   6359  CG1 VAL A 844      21.705 -23.341 -31.254  1.00 19.79           C  
ANISOU 6359  CG1 VAL A 844     2547   2734   2237    417  -1015   -157       C  
ATOM   6360  CG2 VAL A 844      22.012 -20.956 -32.018  1.00 35.00           C  
ANISOU 6360  CG2 VAL A 844     4611   4677   4012    563   -992    -50       C  
ATOM   6361  N   GLN A 845      23.848 -25.103 -33.516  1.00 31.55           N  
ANISOU 6361  N   GLN A 845     4208   4187   3594    421   -998   -232       N  
ATOM   6362  CA  GLN A 845      24.642 -26.264 -33.119  1.00 30.68           C  
ANISOU 6362  CA  GLN A 845     4088   4022   3546    353   -953   -255       C  
ATOM   6363  C   GLN A 845      26.059 -26.215 -33.699  1.00 26.25           C  
ANISOU 6363  C   GLN A 845     3618   3437   2919    375   -886   -231       C  
ATOM   6364  O   GLN A 845      26.257 -26.201 -34.911  1.00 30.21           O  
ANISOU 6364  O   GLN A 845     4188   3965   3326    425   -907   -260       O  
ATOM   6365  CB  GLN A 845      23.921 -27.575 -33.491  1.00 32.35           C  
ANISOU 6365  CB  GLN A 845     4251   4238   3801    317  -1023   -353       C  
ATOM   6366  CG  GLN A 845      24.704 -28.852 -33.192  1.00 39.74           C  
ANISOU 6366  CG  GLN A 845     5192   5108   4799    257   -982   -382       C  
ATOM   6367  CD  GLN A 845      25.327 -28.895 -31.786  1.00 53.69           C  
ANISOU 6367  CD  GLN A 845     6934   6818   6649    205   -903   -314       C  
ATOM   6368  NE2 GLN A 845      26.495 -29.524 -31.681  1.00 55.35           N  
ANISOU 6368  NE2 GLN A 845     7183   6978   6871    193   -849   -307       N  
ATOM   6369  OE1 GLN A 845      24.767 -28.376 -30.815  1.00 58.89           O  
ANISOU 6369  OE1 GLN A 845     7538   7481   7357    182   -894   -272       O  
ATOM   6370  N   VAL A 846      27.050 -26.166 -32.823  1.00 20.04           N  
ANISOU 6370  N   VAL A 846     2831   2606   2180    339   -804   -180       N  
ATOM   6371  CA  VAL A 846      28.427 -26.030 -33.277  1.00 29.74           C  
ANISOU 6371  CA  VAL A 846     4128   3816   3354    356   -732   -159       C  
ATOM   6372  C   VAL A 846      29.085 -27.374 -33.635  1.00 26.84           C  
ANISOU 6372  C   VAL A 846     3768   3420   3008    337   -725   -220       C  
ATOM   6373  O   VAL A 846      28.734 -28.415 -33.090  1.00 22.72           O  
ANISOU 6373  O   VAL A 846     3195   2868   2570    292   -752   -258       O  
ATOM   6374  CB  VAL A 846      29.283 -25.173 -32.296  1.00 29.12           C  
ANISOU 6374  CB  VAL A 846     4046   3714   3304    336   -647    -81       C  
ATOM   6375  CG1 VAL A 846      28.451 -24.687 -31.140  1.00 26.56           C  
ANISOU 6375  CG1 VAL A 846     3658   3388   3044    310   -663    -45       C  
ATOM   6376  CG2 VAL A 846      30.501 -25.917 -31.836  1.00 32.19           C  
ANISOU 6376  CG2 VAL A 846     4424   4064   3741    303   -589    -85       C  
ATOM   6377  N   HIS A 847      30.002 -27.332 -34.598  1.00 26.89           N  
ANISOU 6377  N   HIS A 847     3845   3434   2937    372   -685   -232       N  
ATOM   6378  CA  HIS A 847      30.654 -28.522 -35.133  1.00 27.44           C  
ANISOU 6378  CA  HIS A 847     3933   3481   3010    369   -676   -297       C  
ATOM   6379  C   HIS A 847      31.287 -29.363 -34.028  1.00 30.17           C  
ANISOU 6379  C   HIS A 847     4228   3771   3466    322   -641   -292       C  
ATOM   6380  O   HIS A 847      31.761 -28.835 -33.022  1.00 28.75           O  
ANISOU 6380  O   HIS A 847     4017   3577   3330    302   -593   -229       O  
ATOM   6381  CB  HIS A 847      31.721 -28.113 -36.152  1.00 20.69           C  
ANISOU 6381  CB  HIS A 847     3160   2646   2057    413   -611   -294       C  
ATOM   6382  CG  HIS A 847      32.237 -29.245 -36.985  1.00 27.35           C  
ANISOU 6382  CG  HIS A 847     4034   3478   2879    426   -610   -373       C  
ATOM   6383  CD2 HIS A 847      31.875 -29.679 -38.218  1.00 28.14           C  
ANISOU 6383  CD2 HIS A 847     4189   3606   2897    462   -656   -443       C  
ATOM   6384  ND1 HIS A 847      33.267 -30.062 -36.576  1.00 30.43           N  
ANISOU 6384  ND1 HIS A 847     4402   3825   3333    409   -557   -391       N  
ATOM   6385  CE1 HIS A 847      33.512 -30.964 -37.515  1.00 26.72           C  
ANISOU 6385  CE1 HIS A 847     3972   3352   2827    432   -566   -469       C  
ATOM   6386  NE2 HIS A 847      32.677 -30.750 -38.518  1.00 29.59           N  
ANISOU 6386  NE2 HIS A 847     4383   3759   3101    461   -625   -504       N  
ATOM   6387  N   GLN A 848      31.297 -30.674 -34.232  1.00 28.57           N  
ANISOU 6387  N   GLN A 848     4020   3532   3302    309   -666   -360       N  
ATOM   6388  CA  GLN A 848      31.829 -31.594 -33.239  1.00 33.59           C  
ANISOU 6388  CA  GLN A 848     4619   4105   4037    275   -640   -356       C  
ATOM   6389  C   GLN A 848      33.292 -31.283 -32.898  1.00 32.18           C  
ANISOU 6389  C   GLN A 848     4446   3921   3860    293   -558   -315       C  
ATOM   6390  O   GLN A 848      33.720 -31.498 -31.767  1.00 30.18           O  
ANISOU 6390  O   GLN A 848     4153   3634   3680    272   -534   -278       O  
ATOM   6391  CB  GLN A 848      31.674 -33.040 -33.719  1.00 39.11           C  
ANISOU 6391  CB  GLN A 848     5332   4760   4768    267   -675   -443       C  
ATOM   6392  CG  GLN A 848      32.653 -33.436 -34.805  1.00 49.88           C  
ANISOU 6392  CG  GLN A 848     6754   6129   6071    314   -642   -495       C  
ATOM   6393  CD  GLN A 848      32.296 -34.756 -35.468  1.00 64.55           C  
ANISOU 6393  CD  GLN A 848     8635   7947   7945    309   -687   -593       C  
ATOM   6394  NE2 GLN A 848      32.680 -35.863 -34.830  1.00 66.35           N  
ANISOU 6394  NE2 GLN A 848     8850   8096   8263    291   -673   -610       N  
ATOM   6395  OE1 GLN A 848      31.684 -34.782 -36.545  1.00 66.57           O  
ANISOU 6395  OE1 GLN A 848     8923   8239   8129    325   -736   -655       O  
ATOM   6396  N   ASP A 849      34.043 -30.753 -33.865  1.00 26.19           N  
ANISOU 6396  N   ASP A 849     3736   3200   3017    333   -513   -322       N  
ATOM   6397  CA  ASP A 849      35.457 -30.440 -33.657  1.00 26.67           C  
ANISOU 6397  CA  ASP A 849     3792   3263   3079    346   -429   -296       C  
ATOM   6398  C   ASP A 849      35.734 -29.186 -32.815  1.00 31.50           C  
ANISOU 6398  C   ASP A 849     4375   3895   3699    327   -387   -217       C  
ATOM   6399  O   ASP A 849      36.872 -28.951 -32.410  1.00 36.60           O  
ANISOU 6399  O   ASP A 849     4998   4544   4366    326   -323   -198       O  
ATOM   6400  CB  ASP A 849      36.202 -30.326 -34.993  1.00 24.30           C  
ANISOU 6400  CB  ASP A 849     3551   2993   2686    388   -381   -335       C  
ATOM   6401  CG  ASP A 849      36.344 -31.665 -35.703  1.00 31.16           C  
ANISOU 6401  CG  ASP A 849     4444   3837   3559    411   -402   -421       C  
ATOM   6402  OD1 ASP A 849      36.202 -32.698 -35.026  1.00 28.38           O  
ANISOU 6402  OD1 ASP A 849     4059   3432   3295    395   -435   -443       O  
ATOM   6403  OD2 ASP A 849      36.597 -31.678 -36.932  1.00 37.49           O1-
ANISOU 6403  OD2 ASP A 849     5306   4666   4272    445   -381   -466       O1-
ATOM   6404  N   THR A 850      34.713 -28.380 -32.552  1.00 30.92           N  
ANISOU 6404  N   THR A 850     4299   3837   3611    312   -422   -177       N  
ATOM   6405  CA  THR A 850      34.904 -27.188 -31.724  1.00 33.09           C  
ANISOU 6405  CA  THR A 850     4552   4124   3897    292   -383   -108       C  
ATOM   6406  C   THR A 850      33.957 -27.210 -30.533  1.00 24.74           C  
ANISOU 6406  C   THR A 850     3443   3049   2908    258   -431    -78       C  
ATOM   6407  O   THR A 850      34.102 -26.434 -29.581  1.00 26.43           O  
ANISOU 6407  O   THR A 850     3629   3265   3149    236   -405    -27       O  
ATOM   6408  CB  THR A 850      34.718 -25.893 -32.542  1.00 37.44           C  
ANISOU 6408  CB  THR A 850     5162   4709   4354    314   -357    -78       C  
ATOM   6409  CG2 THR A 850      35.861 -25.725 -33.530  1.00 37.60           C  
ANISOU 6409  CG2 THR A 850     5232   4744   4308    337   -282    -95       C  
ATOM   6410  OG1 THR A 850      33.494 -25.964 -33.280  1.00 38.31           O  
ANISOU 6410  OG1 THR A 850     5305   4836   4416    339   -431   -100       O  
ATOM   6411  N   LEU A 851      33.002 -28.129 -30.592  1.00 24.22           N  
ANISOU 6411  N   LEU A 851     3365   2966   2871    250   -497   -116       N  
ATOM   6412  CA  LEU A 851      31.984 -28.271 -29.562  1.00 25.30           C  
ANISOU 6412  CA  LEU A 851     3453   3087   3073    212   -539    -96       C  
ATOM   6413  C   LEU A 851      32.558 -28.377 -28.147  1.00 25.33           C  
ANISOU 6413  C   LEU A 851     3416   3063   3147    183   -506    -52       C  
ATOM   6414  O   LEU A 851      31.976 -27.861 -27.203  1.00 30.72           O  
ANISOU 6414  O   LEU A 851     4066   3748   3857    157   -510    -12       O  
ATOM   6415  CB  LEU A 851      31.110 -29.487 -29.877  1.00 26.93           C  
ANISOU 6415  CB  LEU A 851     3651   3269   3313    197   -600   -157       C  
ATOM   6416  CG  LEU A 851      29.911 -29.778 -28.970  1.00 32.40           C  
ANISOU 6416  CG  LEU A 851     4291   3945   4074    150   -640   -151       C  
ATOM   6417  CD1 LEU A 851      29.120 -28.517 -28.690  1.00 33.39           C  
ANISOU 6417  CD1 LEU A 851     4394   4115   4177    153   -650   -109       C  
ATOM   6418  CD2 LEU A 851      29.009 -30.833 -29.599  1.00 34.92           C  
ANISOU 6418  CD2 LEU A 851     4606   4249   4414    132   -700   -226       C  
ATOM   6419  N   ARG A 852      33.701 -29.041 -28.017  1.00 25.59           N  
ANISOU 6419  N   ARG A 852     3450   3073   3201    193   -474    -64       N  
ATOM   6420  CA  ARG A 852      34.339 -29.268 -26.720  1.00 28.84           C  
ANISOU 6420  CA  ARG A 852     3827   3461   3672    178   -453    -28       C  
ATOM   6421  C   ARG A 852      35.435 -28.256 -26.408  1.00 29.02           C  
ANISOU 6421  C   ARG A 852     3836   3516   3673    186   -397      4       C  
ATOM   6422  O   ARG A 852      36.192 -28.432 -25.462  1.00 30.91           O  
ANISOU 6422  O   ARG A 852     4045   3748   3952    184   -382     23       O  
ATOM   6423  CB  ARG A 852      34.956 -30.672 -26.664  1.00 25.26           C  
ANISOU 6423  CB  ARG A 852     3377   2959   3261    194   -459    -62       C  
ATOM   6424  CG  ARG A 852      34.083 -31.733 -26.008  1.00 39.14           C  
ANISOU 6424  CG  ARG A 852     5131   4659   5080    164   -499    -64       C  
ATOM   6425  CD  ARG A 852      32.862 -32.078 -26.851  1.00 54.61           C  
ANISOU 6425  CD  ARG A 852     7105   6613   7030    144   -542   -111       C  
ATOM   6426  NE  ARG A 852      31.599 -31.575 -26.297  1.00 62.28           N  
ANISOU 6426  NE  ARG A 852     8048   7600   8017    102   -566    -85       N  
ATOM   6427  CZ  ARG A 852      30.427 -32.194 -26.440  1.00 63.00           C  
ANISOU 6427  CZ  ARG A 852     8128   7669   8139     66   -607   -120       C  
ATOM   6428  NH1 ARG A 852      30.366 -33.342 -27.108  1.00 69.74           N1+
ANISOU 6428  NH1 ARG A 852     9006   8479   9011     64   -629   -183       N1+
ATOM   6429  NH2 ARG A 852      29.316 -31.678 -25.923  1.00 54.20           N  
ANISOU 6429  NH2 ARG A 852     6976   6577   7042     30   -623   -101       N  
ATOM   6430  N   THR A 853      35.532 -27.209 -27.212  1.00 21.60           N  
ANISOU 6430  N   THR A 853     2923   2613   2673    196   -368      8       N  
ATOM   6431  CA  THR A 853      36.576 -26.210 -27.034  1.00 21.54           C  
ANISOU 6431  CA  THR A 853     2905   2631   2647    193   -305     30       C  
ATOM   6432  C   THR A 853      35.959 -24.926 -26.492  1.00 17.53           C  
ANISOU 6432  C   THR A 853     2396   2137   2126    168   -298     78       C  
ATOM   6433  O   THR A 853      34.738 -24.790 -26.427  1.00 20.64           O  
ANISOU 6433  O   THR A 853     2798   2527   2517    164   -340     90       O  
ATOM   6434  CB  THR A 853      37.240 -25.839 -28.396  1.00 22.06           C  
ANISOU 6434  CB  THR A 853     3015   2721   2647    217   -256      4       C  
ATOM   6435  CG2 THR A 853      37.676 -27.074 -29.169  1.00 16.50           C  
ANISOU 6435  CG2 THR A 853     2323   2005   1943    248   -264    -53       C  
ATOM   6436  OG1 THR A 853      36.286 -25.129 -29.175  1.00 17.19           O  
ANISOU 6436  OG1 THR A 853     2450   2115   1968    225   -271     16       O  
ATOM   6437  N   MET A 854      36.803 -23.974 -26.120  1.00 17.50           N  
ANISOU 6437  N   MET A 854     2381   2150   2119    153   -242     98       N  
ATOM   6438  CA  MET A 854      36.315 -22.668 -25.689  1.00 20.49           C  
ANISOU 6438  CA  MET A 854     2769   2534   2482    132   -225    138       C  
ATOM   6439  C   MET A 854      36.285 -21.707 -26.888  1.00 22.53           C  
ANISOU 6439  C   MET A 854     3092   2799   2668    148   -185    145       C  
ATOM   6440  O   MET A 854      37.002 -20.709 -26.912  1.00 22.76           O  
ANISOU 6440  O   MET A 854     3135   2831   2681    129   -119    160       O  
ATOM   6441  CB  MET A 854      37.177 -22.128 -24.534  1.00 20.76           C  
ANISOU 6441  CB  MET A 854     2757   2576   2553    100   -190    153       C  
ATOM   6442  CG  MET A 854      37.161 -23.030 -23.276  1.00 21.11           C  
ANISOU 6442  CG  MET A 854     2751   2615   2656     93   -233    155       C  
ATOM   6443  SD  MET A 854      38.007 -22.401 -21.788  1.00 25.55           S  
ANISOU 6443  SD  MET A 854     3260   3196   3252     61   -211    168       S  
ATOM   6444  CE  MET A 854      36.938 -21.042 -21.308  1.00 16.10           C  
ANISOU 6444  CE  MET A 854     2087   1993   2037     34   -202    205       C  
ATOM   6445  N   TYR A 855      35.451 -22.027 -27.880  1.00 22.78           N  
ANISOU 6445  N   TYR A 855     3168   2832   2656    181   -225    133       N  
ATOM   6446  CA  TYR A 855      35.351 -21.244 -29.114  1.00 25.63           C  
ANISOU 6446  CA  TYR A 855     3607   3200   2933    210   -196    142       C  
ATOM   6447  C   TYR A 855      34.799 -19.843 -28.836  1.00 27.41           C  
ANISOU 6447  C   TYR A 855     3863   3416   3137    208   -179    191       C  
ATOM   6448  O   TYR A 855      34.923 -18.943 -29.662  1.00 21.70           O  
ANISOU 6448  O   TYR A 855     3212   2686   2345    227   -135    213       O  
ATOM   6449  CB  TYR A 855      34.437 -21.951 -30.127  1.00 16.76           C  
ANISOU 6449  CB  TYR A 855     2517   2086   1765    252   -262    112       C  
ATOM   6450  CG  TYR A 855      33.003 -22.076 -29.643  1.00 27.23           C  
ANISOU 6450  CG  TYR A 855     3814   3414   3119    257   -343    117       C  
ATOM   6451  CD1 TYR A 855      32.056 -21.094 -29.939  1.00 26.44           C  
ANISOU 6451  CD1 TYR A 855     3751   3323   2973    287   -365    146       C  
ATOM   6452  CD2 TYR A 855      32.602 -23.166 -28.872  1.00 15.79           C  
ANISOU 6452  CD2 TYR A 855     2302   1955   1743    233   -391     93       C  
ATOM   6453  CE1 TYR A 855      30.747 -21.200 -29.481  1.00 28.04           C  
ANISOU 6453  CE1 TYR A 855     3912   3534   3208    293   -436    143       C  
ATOM   6454  CE2 TYR A 855      31.301 -23.289 -28.421  1.00 22.47           C  
ANISOU 6454  CE2 TYR A