CNRS Nantes University US2B US2B
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***  Solo receptor  ***

elNémo ID: 230504123411133847

Job options:

ID        	=	 230504123411133847
JOBID     	=	 Solo receptor
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER Solo receptor

CRYST1   96.727   52.811   89.055  90.00  90.00  90.00 P 21 21 2     4
ATOM      1  N   ILE B 426       0.985 -22.627 -32.826  1.00 78.19      B    N  
ANISOU    1  N   ILE B 426    10935   8933   9842   3865   3713  -1195  B    N  
ATOM      2  CA  ILE B 426      -0.042 -22.306 -31.839  1.00 79.14      B    C  
ANISOU    2  CA  ILE B 426    11012   9051  10009   3552   3241  -1105  B    C  
ATOM      3  C   ILE B 426       0.482 -21.302 -30.787  1.00 79.45      B    C  
ANISOU    3  C   ILE B 426    10547   9250  10390   3340   3223   -868  B    C  
ATOM      4  O   ILE B 426       1.481 -21.554 -30.112  1.00 79.82      B    O  
ANISOU    4  O   ILE B 426    10199   9307  10823   3425   3272   -819  B    O  
ATOM      5  CB  ILE B 426      -0.697 -23.578 -31.225  1.00 79.83      B    C  
ANISOU    5  CB  ILE B 426    11235   8901  10196   3564   2840  -1236  B    C  
ATOM      6  CG1 ILE B 426      -1.661 -23.245 -30.069  1.00 80.54      B    C  
ANISOU    6  CG1 ILE B 426    11227   8990  10384   3249   2422  -1104  B    C  
ATOM      7  CG2 ILE B 426       0.338 -24.601 -30.815  1.00 80.45      B    C  
ANISOU    7  CG2 ILE B 426    11095   8856  10616   3810   2926  -1274  B    C  
ATOM      8  CD1 ILE B 426      -2.628 -24.322 -29.771  1.00 81.66      B    C  
ANISOU    8  CD1 ILE B 426    11612   8879  10535   3213   2088  -1230  B    C  
ATOM      9  N   ASP B 427      -0.198 -20.150 -30.683  1.00 79.07      B    N  
ANISOU    9  N   ASP B 427    10521   9322  10201   3082   3136   -744  B    N  
ATOM     10  CA  ASP B 427       0.168 -19.055 -29.792  1.00 79.13      B    C  
ANISOU   10  CA  ASP B 427    10109   9468  10487   2861   3108   -555  B    C  
ATOM     11  C   ASP B 427      -0.999 -18.756 -28.846  1.00 78.39      B    C  
ANISOU   11  C   ASP B 427    10065   9373  10345   2597   2657   -500  B    C  
ATOM     12  O   ASP B 427      -2.068 -18.355 -29.309  1.00 78.60      B    O  
ANISOU   12  O   ASP B 427    10399   9402  10064   2482   2558   -512  B    O  
ATOM     13  CB  ASP B 427       0.496 -17.821 -30.648  1.00 81.62      B    C  
ANISOU   13  CB  ASP B 427    10421   9905  10687   2810   3513   -444  B    C  
ATOM     14  CG  ASP B 427       1.056 -16.628 -29.898  1.00 88.06      B    C  
ANISOU   14  CG  ASP B 427    10780  10831  11849   2588   3558   -276  B    C  
ATOM     15  OD1 ASP B 427       1.046 -16.653 -28.645  1.00 88.75      B    O  
ANISOU   15  OD1 ASP B 427    10580  10934  12208   2464   3210   -259  B    O  
ATOM     16  OD2 ASP B 427       1.503 -15.664 -30.565  1.00 91.21      B    O1-
ANISOU   16  OD2 ASP B 427    11127  11286  12242   2547   3945   -165  B    O1-
ATOM     17  N   VAL B 428      -0.789 -18.905 -27.527  1.00 77.24      B    N  
ANISOU   17  N   VAL B 428     9620   9233  10496   2522   2392   -436  B    N  
ATOM     18  CA  VAL B 428      -1.853 -18.682 -26.544  1.00 76.63      B    C  
ANISOU   18  CA  VAL B 428     9591   9151  10375   2299   2010   -374  B    C  
ATOM     19  C   VAL B 428      -1.938 -17.210 -26.045  1.00 75.06      B    C  
ANISOU   19  C   VAL B 428     9176   9108  10234   2058   1983   -248  B    C  
ATOM     20  O   VAL B 428      -2.728 -16.917 -25.146  1.00 75.31      B    O  
ANISOU   20  O   VAL B 428     9215   9154  10243   1886   1696   -195  B    O  
ATOM     21  CB  VAL B 428      -1.759 -19.709 -25.377  1.00 77.91      B    C  
ANISOU   21  CB  VAL B 428     9654   9211  10736   2376   1731   -361  B    C  
ATOM     22  CG1 VAL B 428      -0.530 -19.470 -24.511  1.00 78.50      B    C  
ANISOU   22  CG1 VAL B 428     9287   9392  11147   2448   1720   -293  B    C  
ATOM     23  CG2 VAL B 428      -3.032 -19.729 -24.533  1.00 78.69      B    C  
ANISOU   23  CG2 VAL B 428     9909   9257  10733   2182   1405   -303  B    C  
ATOM     24  N   ASN B 429      -1.208 -16.269 -26.678  1.00 73.09      B    N  
ANISOU   24  N   ASN B 429     8764   8953  10055   2043   2306   -201  B    N  
ATOM     25  CA  ASN B 429      -1.284 -14.852 -26.283  1.00 71.35      B    C  
ANISOU   25  CA  ASN B 429     8352   8834   9925   1810   2299    -95  B    C  
ATOM     26  C   ASN B 429      -2.500 -14.139 -26.888  1.00 68.40      B    C  
ANISOU   26  C   ASN B 429     8321   8458   9209   1672   2280    -55  B    C  
ATOM     27  O   ASN B 429      -2.357 -13.224 -27.704  1.00 68.85      B    O  
ANISOU   27  O   ASN B 429     8430   8545   9186   1638   2564     19  B    O  
ATOM     28  CB  ASN B 429       0.005 -14.120 -26.619  1.00 73.20      B    C  
ANISOU   28  CB  ASN B 429     8230   9124  10459   1824   2663    -46  B    C  
ATOM     29  CG  ASN B 429       0.951 -14.119 -25.461  1.00 77.46      B    C  
ANISOU   29  CG  ASN B 429     8287   9711  11432   1819   2495    -69  B    C  
ATOM     30  ND2 ASN B 429       2.052 -14.854 -25.590  1.00 78.34      B    N  
ANISOU   30  ND2 ASN B 429     8165   9809  11792   2032   2654   -127  B    N  
ATOM     31  OD1 ASN B 429       0.691 -13.480 -24.434  1.00 79.23      B    O  
ANISOU   31  OD1 ASN B 429     8354   9988  11763   1648   2201    -52  B    O  
ATOM     32  N   ILE B 430      -3.693 -14.534 -26.444  1.00 65.08      B    N  
ANISOU   32  N   ILE B 430     8117   7993   8617   1598   1948    -91  B    N  
ATOM     33  CA  ILE B 430      -4.967 -14.029 -26.946  1.00 62.22      B    C  
ANISOU   33  CA  ILE B 430     8061   7621   7959   1494   1850    -86  B    C  
ATOM     34  C   ILE B 430      -5.342 -12.627 -26.422  1.00 59.21      B    C  
ANISOU   34  C   ILE B 430     7549   7313   7636   1275   1787     25  B    C  
ATOM     35  O   ILE B 430      -5.204 -12.352 -25.235  1.00 60.12      B    O  
ANISOU   35  O   ILE B 430     7409   7466   7967   1160   1617     54  B    O  
ATOM     36  CB  ILE B 430      -6.090 -15.065 -26.650  1.00 62.51      B    C  
ANISOU   36  CB  ILE B 430     8318   7552   7879   1492   1534   -186  B    C  
ATOM     37  CG1 ILE B 430      -5.678 -16.517 -27.002  1.00 63.78      B    C  
ANISOU   37  CG1 ILE B 430     8590   7594   8050   1702   1569   -310  B    C  
ATOM     38  CG2 ILE B 430      -7.413 -14.686 -27.309  1.00 62.78      B    C  
ANISOU   38  CG2 ILE B 430     8649   7568   7638   1420   1405   -226  B    C  
ATOM     39  CD1 ILE B 430      -5.427 -16.780 -28.446  1.00 65.44      B    C  
ANISOU   39  CD1 ILE B 430     9060   7779   8024   1894   1813   -412  B    C  
ATOM     40  N   ASN B 431      -5.857 -11.758 -27.308  1.00 55.31      B    N  
ANISOU   40  N   ASN B 431     7264   6828   6924   1242   1906     79  B    N  
ATOM     41  CA  ASN B 431      -6.348 -10.429 -26.961  1.00 52.50      B    C  
ANISOU   41  CA  ASN B 431     6847   6504   6597   1057   1853    179  B    C  
ATOM     42  C   ASN B 431      -7.876 -10.540 -26.776  1.00 47.27      B    C  
ANISOU   42  C   ASN B 431     6402   5819   5741    990   1525    129  B    C  
ATOM     43  O   ASN B 431      -8.565 -11.024 -27.671  1.00 47.60      B    O  
ANISOU   43  O   ASN B 431     6746   5823   5518   1096   1472     57  B    O  
ATOM     44  CB  ASN B 431      -6.010  -9.417 -28.082  1.00 55.41      B    C  
ANISOU   44  CB  ASN B 431     7338   6867   6850   1092   2203    299  B    C  
ATOM     45  CG  ASN B 431      -6.905  -8.177 -28.171  1.00 63.38      B    C  
ANISOU   45  CG  ASN B 431     8466   7863   7752    968   2133    398  B    C  
ATOM     46  ND2 ASN B 431      -6.891  -7.328 -27.139  1.00 64.90      B    N  
ANISOU   46  ND2 ASN B 431     8389   8059   8212    775   2026    434  B    N  
ATOM     47  OD1 ASN B 431      -7.632  -7.967 -29.162  1.00 66.04      B    O  
ANISOU   47  OD1 ASN B 431     9153   8182   7757   1066   2152    429  B    O  
ATOM     48  N   ILE B 432      -8.392 -10.114 -25.626  1.00 42.32      B    N  
ANISOU   48  N   ILE B 432     5613   5212   5254    827   1307    147  B    N  
ATOM     49  CA  ILE B 432      -9.823 -10.097 -25.393  1.00 38.24      B    C  
ANISOU   49  CA  ILE B 432     5237   4671   4620    750   1045    111  B    C  
ATOM     50  C   ILE B 432     -10.250  -8.632 -25.355  1.00 37.98      B    C  
ANISOU   50  C   ILE B 432     5182   4663   4586    636   1060    200  B    C  
ATOM     51  O   ILE B 432      -9.674  -7.869 -24.573  1.00 37.60      B    O  
ANISOU   51  O   ILE B 432     4902   4644   4741    532   1109    251  B    O  
ATOM     52  CB  ILE B 432     -10.209 -10.844 -24.101  1.00 35.24      B    C  
ANISOU   52  CB  ILE B 432     4734   4275   4380    681    823     73  B    C  
ATOM     53  CG1 ILE B 432      -9.771 -12.334 -24.165  1.00 34.62      B    C  
ANISOU   53  CG1 ILE B 432     4699   4129   4327    811    819      2  B    C  
ATOM     54  CG2 ILE B 432     -11.700 -10.729 -23.844  1.00 33.96      B    C  
ANISOU   54  CG2 ILE B 432     4666   4079   4158    585    612     47  B    C  
ATOM     55  CD1 ILE B 432      -9.829 -13.055 -22.764  1.00 34.55      B    C  
ANISOU   55  CD1 ILE B 432     4563   4093   4472    777    662     23  B    C  
ATOM     56  N   SER B 433     -11.192  -8.215 -26.230  1.00 37.30      B    N  
ANISOU   56  N   SER B 433     5338   4553   4281    674   1008    207  B    N  
ATOM     57  CA  SER B 433     -11.652  -6.819 -26.179  1.00 37.57      B    C  
ANISOU   57  CA  SER B 433     5365   4584   4327    587   1013    302  B    C  
ATOM     58  C   SER B 433     -13.131  -6.757 -25.830  1.00 35.48      B    C  
ANISOU   58  C   SER B 433     5149   4308   4023    533    723    243  B    C  
ATOM     59  O   SER B 433     -13.920  -7.594 -26.275  1.00 35.79      B    O  
ANISOU   59  O   SER B 433     5332   4326   3940    601    548    139  B    O  
ATOM     60  CB  SER B 433     -11.321  -6.051 -27.448  1.00 41.67      B    C  
ANISOU   60  CB  SER B 433     6094   5076   4663    695   1257    418  B    C  
ATOM     61  OG  SER B 433     -11.950  -6.662 -28.556  1.00 48.72      B    O  
ANISOU   61  OG  SER B 433     7310   5966   5236    871   1174    355  B    O  
ATOM     62  N   CYS B 434     -13.497  -5.799 -25.000  1.00 32.86      B    N  
ANISOU   62  N   CYS B 434     4673   3978   3833    411    670    285  B    N  
ATOM     63  CA  CYS B 434     -14.835  -5.703 -24.467  1.00 32.74      B    C  
ANISOU   63  CA  CYS B 434     4636   3955   3848    352    439    231  B    C  
ATOM     64  C   CYS B 434     -15.498  -4.367 -24.786  1.00 31.91      B    C  
ANISOU   64  C   CYS B 434     4595   3818   3712    353    418    300  B    C  
ATOM     65  O   CYS B 434     -14.832  -3.339 -24.834  1.00 31.59      B    O  
ANISOU   65  O   CYS B 434     4531   3748   3725    326    592    400  B    O  
ATOM     66  CB  CYS B 434     -14.813  -5.951 -22.958  1.00 34.20      B    C  
ANISOU   66  CB  CYS B 434     4601   4169   4223    234    382    200  B    C  
ATOM     67  SG  CYS B 434     -14.181  -7.584 -22.461  1.00 39.28      B    S  
ANISOU   67  SG  CYS B 434     5194   4821   4908    263    374    147  B    S  
ATOM     68  N   GLU B 435     -16.830  -4.394 -24.927  1.00 30.46      B    N  
ANISOU   68  N   GLU B 435     4461   3620   3492    379    200    239  B    N  
ATOM     69  CA  GLU B 435     -17.614  -3.215 -25.198  1.00 29.45      B    C  
ANISOU   69  CA  GLU B 435     4388   3454   3347    414    133    293  B    C  
ATOM     70  C   GLU B 435     -18.950  -3.351 -24.497  1.00 28.85      B    C  
ANISOU   70  C   GLU B 435     4168   3378   3414    360    -83    195  B    C  
ATOM     71  O   GLU B 435     -19.656  -4.358 -24.672  1.00 29.74      B    O  
ANISOU   71  O   GLU B 435     4272   3493   3535    376   -254     82  B    O  
ATOM     72  CB  GLU B 435     -17.826  -3.075 -26.706  1.00 30.49      B    C  
ANISOU   72  CB  GLU B 435     4813   3565   3206    604     91    333  B    C  
ATOM     73  CG  GLU B 435     -18.475  -1.766 -27.105  1.00 35.12      B    C  
ANISOU   73  CG  GLU B 435     5502   4093   3749    685     45    433  B    C  
ATOM     74  CD  GLU B 435     -18.658  -1.613 -28.605  1.00 44.49      B    C  
ANISOU   74  CD  GLU B 435     7039   5265   4599    922     -7    495  B    C  
ATOM     75  OE1 GLU B 435     -17.634  -1.513 -29.319  1.00 48.47      B    O  
ANISOU   75  OE1 GLU B 435     7737   5755   4925    998    257    619  B    O  
ATOM     76  OE2 GLU B 435     -19.822  -1.562 -29.067  1.00 45.47      B    O1-
ANISOU   76  OE2 GLU B 435     7246   5392   4638   1048   -308    420  B    O1-
ATOM     77  N   THR B 436     -19.296  -2.341 -23.705  1.00 26.89      B    N  
ANISOU   77  N   THR B 436     3796   3111   3310    296    -59    227  B    N  
ATOM     78  CA  THR B 436     -20.586  -2.232 -23.044  1.00 27.38      B    C  
ANISOU   78  CA  THR B 436     3709   3166   3527    264   -204    153  B    C  
ATOM     79  C   THR B 436     -21.519  -1.449 -23.965  1.00 27.87      B    C  
ANISOU   79  C   THR B 436     3871   3182   3537    401   -364    167  B    C  
ATOM     80  O   THR B 436     -21.099  -0.477 -24.598  1.00 27.61      B    O  
ANISOU   80  O   THR B 436     3998   3101   3392    485   -289    281  B    O  
ATOM     81  CB  THR B 436     -20.426  -1.541 -21.672  1.00 28.05      B    C  
ANISOU   81  CB  THR B 436     3636   3257   3766    158    -84    160  B    C  
ATOM     82  CG2 THR B 436     -21.764  -1.383 -20.921  1.00 27.15      B    C  
ANISOU   82  CG2 THR B 436     3363   3136   3816    141   -166     91  B    C  
ATOM     83  OG1 THR B 436     -19.549  -2.345 -20.899  1.00 28.93      B    O  
ANISOU   83  OG1 THR B 436     3687   3422   3883     77     13    147  B    O  
ATOM     84  N   ASP B 437     -22.762  -1.919 -24.127  1.00 29.42      B    N  
ANISOU   84  N   ASP B 437     3979   3378   3823    439   -592     55  B    N  
ATOM     85  CA  ASP B 437     -23.723  -1.249 -25.031  1.00 30.65      B    C  
ANISOU   85  CA  ASP B 437     4213   3498   3934    609   -817     45  B    C  
ATOM     86  C   ASP B 437     -24.098   0.158 -24.521  1.00 31.88      B    C  
ANISOU   86  C   ASP B 437     4299   3599   4213    632   -755    121  B    C  
ATOM     87  O   ASP B 437     -23.883   0.470 -23.343  1.00 32.57      B    O  
ANISOU   87  O   ASP B 437     4234   3685   4457    502   -576    127  B    O  
ATOM     88  CB  ASP B 437     -24.983  -2.119 -25.200  1.00 32.06      B    C  
ANISOU   88  CB  ASP B 437     4229   3680   4274    623  -1102   -134  B    C  
ATOM     89  CG  ASP B 437     -25.819  -2.216 -23.923  1.00 35.63      B    C  
ANISOU   89  CG  ASP B 437     4345   4119   5072    481  -1046   -197  B    C  
ATOM     90  OD1 ASP B 437     -25.234  -2.337 -22.840  1.00 32.87      B    O  
ANISOU   90  OD1 ASP B 437     3923   3788   4779    342   -797   -144  B    O  
ATOM     91  OD2 ASP B 437     -27.064  -2.140 -24.014  1.00 40.11      B    O1-
ANISOU   91  OD2 ASP B 437     4725   4660   5854    529  -1248   -299  B    O1-
ATOM     92  N   GLY B 438     -24.696   0.976 -25.394  1.00 31.70      B    N  
ANISOU   92  N   GLY B 438     4407   3527   4112    823   -921    167  B    N  
ATOM     93  CA  GLY B 438     -25.087   2.338 -25.078  1.00 32.78      B    C  
ANISOU   93  CA  GLY B 438     4514   3576   4367    885   -880    244  B    C  
ATOM     94  C   GLY B 438     -26.206   2.466 -24.062  1.00 34.25      B    C  
ANISOU   94  C   GLY B 438     4380   3763   4871    834   -937    123  B    C  
ATOM     95  O   GLY B 438     -26.457   3.562 -23.553  1.00 34.63      B    O  
ANISOU   95  O   GLY B 438     4377   3733   5048    865   -855    160  B    O  
ATOM     96  N   TYR B 439     -26.910   1.365 -23.773  1.00 34.85      B    N  
ANISOU   96  N   TYR B 439     4238   3905   5099    760  -1055    -24  B    N  
ATOM     97  CA  TYR B 439     -27.942   1.350 -22.739  1.00 36.49      B    C  
ANISOU   97  CA  TYR B 439     4117   4111   5634    694  -1029   -127  B    C  
ATOM     98  C   TYR B 439     -27.418   0.816 -21.388  1.00 34.82      B    C  
ANISOU   98  C   TYR B 439     3794   3943   5492    489   -739   -133  B    C  
ATOM     99  O   TYR B 439     -28.198   0.748 -20.448  1.00 34.73      B    O  
ANISOU   99  O   TYR B 439     3544   3933   5718    437   -645   -196  B    O  
ATOM    100  CB  TYR B 439     -29.166   0.545 -23.172  1.00 39.15      B    C  
ANISOU  100  CB  TYR B 439     4233   4460   6183    733  -1309   -280  B    C  
ATOM    101  CG  TYR B 439     -29.828   1.082 -24.418  1.00 43.40      B    C  
ANISOU  101  CG  TYR B 439     4865   4971   6656    978  -1663   -305  B    C  
ATOM    102  CD1 TYR B 439     -30.677   2.176 -24.362  1.00 46.12      B    C  
ANISOU  102  CD1 TYR B 439     5095   5261   7167   1134  -1754   -297  B    C  
ATOM    103  CD2 TYR B 439     -29.619   0.484 -25.653  1.00 46.05      B    C  
ANISOU  103  CD2 TYR B 439     5422   5333   6744   1084  -1922   -344  B    C  
ATOM    104  CE1 TYR B 439     -31.305   2.665 -25.506  1.00 48.24      B    C  
ANISOU  104  CE1 TYR B 439     5467   5505   7359   1400  -2117   -310  B    C  
ATOM    105  CE2 TYR B 439     -30.235   0.966 -26.803  1.00 47.93      B    C  
ANISOU  105  CE2 TYR B 439     5791   5557   6863   1354  -2284   -369  B    C  
ATOM    106  CZ  TYR B 439     -31.092   2.044 -26.721  1.00 49.96      B    C  
ANISOU  106  CZ  TYR B 439     5925   5763   7295   1514  -2394   -346  B    C  
ATOM    107  OH  TYR B 439     -31.685   2.536 -27.856  1.00 53.85      B    O  
ANISOU  107  OH  TYR B 439     6572   6241   7646   1819  -2780   -357  B    O  
ATOM    108  N   LEU B 440     -26.134   0.428 -21.302  1.00 33.48      B    N  
ANISOU  108  N   LEU B 440     3797   3808   5117    399   -597    -66  B    N  
ATOM    109  CA  LEU B 440     -25.504  -0.068 -20.077  1.00 34.55      B    C  
ANISOU  109  CA  LEU B 440     3877   3991   5261    250   -368    -64  B    C  
ATOM    110  C   LEU B 440     -26.241  -1.301 -19.525  1.00 35.42      B    C  
ANISOU  110  C   LEU B 440     3792   4120   5546    161   -351   -132  B    C  
ATOM    111  O   LEU B 440     -26.512  -1.377 -18.333  1.00 36.55      B    O  
ANISOU  111  O   LEU B 440     3816   4280   5794     98   -165   -137  B    O  
ATOM    112  CB  LEU B 440     -25.427   1.053 -19.019  1.00 34.34      B    C  
ANISOU  112  CB  LEU B 440     3816   3945   5289    246   -201    -60  B    C  
ATOM    113  CG  LEU B 440     -24.332   2.122 -19.175  1.00 36.43      B    C  
ANISOU  113  CG  LEU B 440     4255   4158   5429    259   -133      4  B    C  
ATOM    114  CD1 LEU B 440     -24.339   2.772 -20.563  1.00 37.31      B    C  
ANISOU  114  CD1 LEU B 440     4521   4187   5467    382   -260     89  B    C  
ATOM    115  CD2 LEU B 440     -24.556   3.250 -18.168  1.00 37.13      B    C  
ANISOU  115  CD2 LEU B 440     4289   4194   5625    273    -24    -51  B    C  
ATOM    116  N   THR B 441     -26.637  -2.213 -20.407  1.00 34.72      B    N  
ANISOU  116  N   THR B 441     3679   4011   5501    167   -539   -191  B    N  
ATOM    117  CA  THR B 441     -27.365  -3.426 -20.056  1.00 35.22      B    C  
ANISOU  117  CA  THR B 441     3544   4038   5798     64   -534   -263  B    C  
ATOM    118  C   THR B 441     -26.519  -4.722 -20.238  1.00 34.08      B    C  
ANISOU  118  C   THR B 441     3526   3886   5539    -15   -511   -253  B    C  
ATOM    119  O   THR B 441     -26.905  -5.772 -19.738  1.00 34.49      B    O  
ANISOU  119  O   THR B 441     3445   3876   5782   -122   -434   -276  B    O  
ATOM    120  CB  THR B 441     -28.649  -3.538 -20.898  1.00 37.32      B    C  
ANISOU  120  CB  THR B 441     3624   4249   6307    125   -817   -397  B    C  
ATOM    121  CG2 THR B 441     -29.550  -2.337 -20.751  1.00 38.22      B    C  
ANISOU  121  CG2 THR B 441     3586   4360   6577    231   -857   -413  B    C  
ATOM    122  OG1 THR B 441     -28.338  -3.762 -22.279  1.00 38.58      B    O  
ANISOU  122  OG1 THR B 441     3980   4409   6269    228  -1099   -453  B    O  
ATOM    123  N   LYS B 442     -25.405  -4.650 -20.975  1.00 32.73      B    N  
ANISOU  123  N   LYS B 442     3599   3751   5085     45   -557   -214  B    N  
ATOM    124  CA  LYS B 442     -24.602  -5.833 -21.270  1.00 31.99      B    C  
ANISOU  124  CA  LYS B 442     3626   3642   4887      7   -546   -221  B    C  
ATOM    125  C   LYS B 442     -23.204  -5.455 -21.723  1.00 30.88      B    C  
ANISOU  125  C   LYS B 442     3717   3561   4453     72   -475   -139  B    C  
ATOM    126  O   LYS B 442     -22.985  -4.363 -22.241  1.00 30.93      B    O  
ANISOU  126  O   LYS B 442     3824   3593   4333    159   -495    -91  B    O  
ATOM    127  CB  LYS B 442     -25.279  -6.666 -22.393  1.00 33.84      B    C  
ANISOU  127  CB  LYS B 442     3855   3802   5200     42   -817   -374  B    C  
ATOM    128  CG  LYS B 442     -25.345  -5.911 -23.710  1.00 38.09      B    C  
ANISOU  128  CG  LYS B 442     4567   4375   5530    216  -1048   -415  B    C  
ATOM    129  CD  LYS B 442     -25.794  -6.770 -24.845  1.00 44.00      B    C  
ANISOU  129  CD  LYS B 442     5379   5069   6269    287  -1347   -595  B    C  
ATOM    130  CE  LYS B 442     -25.846  -5.973 -26.103  1.00 49.78      B    C  
ANISOU  130  CE  LYS B 442     6345   5850   6719    507  -1567   -609  B    C  
ATOM    131  NZ  LYS B 442     -26.388  -6.804 -27.211  1.00 55.58      B    N1+
ANISOU  131  NZ  LYS B 442     7165   6541   7412    609  -1922   -832  B    N1+
ATOM    132  N   MET B 443     -22.265  -6.379 -21.558  1.00 29.15      B    N  
ANISOU  132  N   MET B 443     3573   3344   4159     37   -378   -115  B    N  
ATOM    133  CA  MET B 443     -20.905  -6.177 -22.023  1.00 28.55      B    C  
ANISOU  133  CA  MET B 443     3668   3317   3865     97   -289    -51  B    C  
ATOM    134  C   MET B 443     -20.573  -7.377 -22.885  1.00 28.67      B    C  
ANISOU  134  C   MET B 443     3805   3289   3799    145   -359   -123  B    C  
ATOM    135  O   MET B 443     -20.746  -8.511 -22.463  1.00 28.51      B    O  
ANISOU  135  O   MET B 443     3723   3205   3904     84   -362   -169  B    O  
ATOM    136  CB  MET B 443     -19.910  -6.076 -20.861  1.00 28.06      B    C  
ANISOU  136  CB  MET B 443     3555   3306   3802     37   -101     32  B    C  
ATOM    137  CG  MET B 443     -18.522  -5.780 -21.338  1.00 30.14      B    C  
ANISOU  137  CG  MET B 443     3919   3607   3926     85     -2     85  B    C  
ATOM    138  SD  MET B 443     -17.325  -5.572 -20.015  1.00 30.54      B    S  
ANISOU  138  SD  MET B 443     3866   3721   4015     32    134    132  B    S  
ATOM    139  CE  MET B 443     -17.448  -7.169 -19.195  1.00 32.16      B    C  
ANISOU  139  CE  MET B 443     4047   3911   4262     20    125    126  B    C  
ATOM    140  N   THR B 444     -20.138  -7.133 -24.097  1.00 29.22      B    N  
ANISOU  140  N   THR B 444     4067   3374   3659    268   -400   -132  B    N  
ATOM    141  CA  THR B 444     -19.780  -8.188 -25.040  1.00 30.37      B    C  
ANISOU  141  CA  THR B 444     4379   3484   3677    355   -462   -227  B    C  
ATOM    142  C   THR B 444     -18.248  -8.217 -25.151  1.00 31.28      B    C  
ANISOU  142  C   THR B 444     4590   3645   3648    403   -226   -132  B    C  
ATOM    143  O   THR B 444     -17.624  -7.189 -25.385  1.00 30.67      B    O  
ANISOU  143  O   THR B 444     4567   3618   3470    441    -86    -19  B    O  
ATOM    144  CB  THR B 444     -20.393  -7.862 -26.398  1.00 32.30      B    C  
ANISOU  144  CB  THR B 444     4816   3726   3731    510   -673   -312  B    C  
ATOM    145  CG2 THR B 444     -20.122  -8.958 -27.450  1.00 33.60      B    C  
ANISOU  145  CG2 THR B 444     5194   3849   3723    631   -772   -460  B    C  
ATOM    146  OG1 THR B 444     -21.801  -7.694 -26.219  1.00 33.65      B    O  
ANISOU  146  OG1 THR B 444     4829   3860   4096    468   -908   -404  B    O  
ATOM    147  N   CYS B 445     -17.654  -9.382 -24.980  1.00 32.40      B    N  
ANISOU  147  N   CYS B 445     4735   3749   3826    401   -172   -176  B    N  
ATOM    148  CA  CYS B 445     -16.223  -9.564 -25.094  1.00 34.31      B    C  
ANISOU  148  CA  CYS B 445     5022   4028   3985    463     41   -111  B    C  
ATOM    149  C   CYS B 445     -15.930 -10.466 -26.296  1.00 36.26      B    C  
ANISOU  149  C   CYS B 445     5491   4230   4056    614     23   -224  B    C  
ATOM    150  O   CYS B 445     -16.714 -11.352 -26.618  1.00 37.47      B    O  
ANISOU  150  O   CYS B 445     5708   4295   4235    627   -172   -377  B    O  
ATOM    151  CB  CYS B 445     -15.620 -10.075 -23.787  1.00 35.33      B    C  
ANISOU  151  CB  CYS B 445     4970   4160   4294    379    128    -57  B    C  
ATOM    152  SG  CYS B 445     -15.807  -8.903 -22.403  1.00 40.21      B    S  
ANISOU  152  SG  CYS B 445     5386   4850   5040    247    156     46  B    S  
ATOM    153  N   ARG B 446     -14.877 -10.162 -27.019  1.00 36.09      B    N  
ANISOU  153  N   ARG B 446     5593   4257   3864    733    230   -164  B    N  
ATOM    154  CA  ARG B 446     -14.567 -10.809 -28.278  1.00 37.25      B    C  
ANISOU  154  CA  ARG B 446     6005   4379   3770    920    258   -266  B    C  
ATOM    155  C   ARG B 446     -13.127 -11.265 -28.303  1.00 36.63      B    C  
ANISOU  155  C   ARG B 446     5898   4314   3706    995    541   -220  B    C  
ATOM    156  O   ARG B 446     -12.246 -10.549 -27.827  1.00 36.13      B    O  
ANISOU  156  O   ARG B 446     5665   4310   3753    940    758    -73  B    O  
ATOM    157  CB  ARG B 446     -14.797  -9.763 -29.378  1.00 40.08      B    C  
ANISOU  157  CB  ARG B 446     6602   4788   3840   1048    282   -206  B    C  
ATOM    158  CG  ARG B 446     -15.007 -10.312 -30.752  1.00 46.88      B    C  
ANISOU  158  CG  ARG B 446     7816   5631   4366   1274    193   -351  B    C  
ATOM    159  CD  ARG B 446     -15.502  -9.198 -31.677  1.00 51.48      B    C  
ANISOU  159  CD  ARG B 446     8652   6261   4649   1413    147   -268  B    C  
ATOM    160  NE  ARG B 446     -15.364  -9.565 -33.087  1.00 56.38      B    N  
ANISOU  160  NE  ARG B 446     9686   6893   4845   1692    151   -364  B    N  
ATOM    161  CZ  ARG B 446     -14.320  -9.237 -33.841  1.00 60.72      B    C  
ANISOU  161  CZ  ARG B 446    10457   7478   5134   1857    529   -222  B    C  
ATOM    162  NH1 ARG B 446     -13.309  -8.543 -33.327  1.00 61.94      B    N1+
ANISOU  162  NH1 ARG B 446    10411   7647   5477   1745    918     10  B    N1+
ATOM    163  NH2 ARG B 446     -14.268  -9.614 -35.109  1.00 61.43      B    N  
ANISOU  163  NH2 ARG B 446    10968   7584   4787   2141    531   -323  B    N  
ATOM    164  N   TRP B 447     -12.881 -12.445 -28.863  1.00 36.68      B    N  
ANISOU  164  N   TRP B 447     6050   4253   3633   1124    532   -364  B    N  
ATOM    165  CA  TRP B 447     -11.540 -12.989 -28.942  1.00 37.33      B    C  
ANISOU  165  CA  TRP B 447     6096   4338   3749   1229    800   -343  B    C  
ATOM    166  C   TRP B 447     -11.423 -13.982 -30.093  1.00 40.00      B    C  
ANISOU  166  C   TRP B 447     6733   4608   3858   1446    810   -525  B    C  
ATOM    167  O   TRP B 447     -12.400 -14.633 -30.462  1.00 39.10      B    O  
ANISOU  167  O   TRP B 447     6782   4404   3670   1467    531   -713  B    O  
ATOM    168  CB  TRP B 447     -11.106 -13.627 -27.598  1.00 36.29      B    C  
ANISOU  168  CB  TRP B 447     5678   4170   3941   1121    779   -309  B    C  
ATOM    169  CG  TRP B 447     -11.990 -14.741 -27.103  1.00 35.62      B    C  
ANISOU  169  CG  TRP B 447     5604   3948   3981   1061    527   -430  B    C  
ATOM    170  CD1 TRP B 447     -13.134 -14.616 -26.372  1.00 35.97      B    C  
ANISOU  170  CD1 TRP B 447     5559   3953   4153    893    316   -424  B    C  
ATOM    171  CD2 TRP B 447     -11.721 -16.143 -27.185  1.00 35.26      B    C  
ANISOU  171  CD2 TRP B 447     5629   3759   4008   1159    509   -553  B    C  
ATOM    172  CE2 TRP B 447     -12.773 -16.812 -26.530  1.00 35.60      B    C  
ANISOU  172  CE2 TRP B 447     5634   3661   4233   1028    285   -608  B    C  
ATOM    173  CE3 TRP B 447     -10.692 -16.904 -27.761  1.00 36.61      B    C  
ANISOU  173  CE3 TRP B 447     5890   3888   4130   1354    683   -622  B    C  
ATOM    174  NE1 TRP B 447     -13.650 -15.862 -26.093  1.00 35.66      B    N  
ANISOU  174  NE1 TRP B 447     5542   3743   4264    870    179   -532  B    N  
ATOM    175  CZ2 TRP B 447     -12.839 -18.199 -26.453  1.00 36.76      B    C  
ANISOU  175  CZ2 TRP B 447     5845   3602   4522   1071    222   -722  B    C  
ATOM    176  CZ3 TRP B 447     -10.769 -18.281 -27.699  1.00 37.90      B    C  
ANISOU  176  CZ3 TRP B 447     6129   3862   4411   1419    597   -756  B    C  
ATOM    177  CH2 TRP B 447     -11.826 -18.914 -27.035  1.00 37.85      B    C  
ANISOU  177  CH2 TRP B 447     6092   3694   4596   1270    365   -799  B    C  
ATOM    178  N   SER B 448     -10.234 -14.089 -30.664  1.00 43.33      B    N  
ANISOU  178  N   SER B 448     7213   5062   4187   1609   1134   -490  B    N  
ATOM    179  CA  SER B 448     -10.028 -14.996 -31.790  1.00 48.08      B    C  
ANISOU  179  CA  SER B 448     8131   5605   4532   1853   1189   -675  B    C  
ATOM    180  C   SER B 448      -9.237 -16.209 -31.398  1.00 53.05      B    C  
ANISOU  180  C   SER B 448     8643   6138   5375   1920   1274   -762  B    C  
ATOM    181  O   SER B 448      -8.138 -16.083 -30.864  1.00 53.00      B    O  
ANISOU  181  O   SER B 448     8378   6178   5580   1915   1526   -628  B    O  
ATOM    182  CB  SER B 448      -9.341 -14.277 -32.948  1.00 49.79      B    C  
ANISOU  182  CB  SER B 448     8586   5914   4417   2052   1543   -581  B    C  
ATOM    183  OG  SER B 448      -9.036 -15.177 -34.002  1.00 54.29      B    O  
ANISOU  183  OG  SER B 448     9481   6436   4709   2322   1637   -769  B    O  
ATOM    184  N   PRO B 449      -9.749 -17.402 -31.739  1.00 57.22      B    N  
ANISOU  184  N   PRO B 449     9365   6517   5858   2007   1063  -1004  B    N  
ATOM    185  CA  PRO B 449      -8.974 -18.616 -31.508  1.00 60.70      B    C  
ANISOU  185  CA  PRO B 449     9749   6831   6483   2118   1160  -1096  B    C  
ATOM    186  C   PRO B 449      -8.187 -18.993 -32.762  1.00 65.13      B    C  
ANISOU  186  C   PRO B 449    10594   7396   6756   2423   1434  -1224  B    C  
ATOM    187  O   PRO B 449      -7.840 -20.157 -32.863  1.00 66.22      B    O  
ANISOU  187  O   PRO B 449    10796   7385   6978   2559   1442  -1390  B    O  
ATOM    188  CB  PRO B 449     -10.064 -19.667 -31.321  1.00 60.92      B    C  
ANISOU  188  CB  PRO B 449     9870   6649   6627   2043    789  -1310  B    C  
ATOM    189  CG  PRO B 449     -11.102 -19.247 -32.357  1.00 60.66      B    C  
ANISOU  189  CG  PRO B 449    10136   6648   6262   2080    568  -1471  B    C  
ATOM    190  CD  PRO B 449     -11.035 -17.712 -32.393  1.00 57.92      B    C  
ANISOU  190  CD  PRO B 449     9728   6524   5757   2021    710  -1228  B    C  
ATOM    191  N   SER B 450      -7.949 -18.083 -33.734  1.00 68.21      B    N  
ANISOU  191  N   SER B 450    11191   7931   6796   2551   1669  -1153  B    N  
ATOM    192  CA  SER B 450      -7.235 -18.435 -34.975  1.00 71.90      B    C  
ANISOU  192  CA  SER B 450    11981   8406   6930   2874   1979  -1268  B    C  
ATOM    193  C   SER B 450      -5.827 -18.968 -34.737  1.00 75.12      B    C  
ANISOU  193  C   SER B 450    12161   8794   7586   2998   2362  -1219  B    C  
ATOM    194  O   SER B 450      -5.299 -19.700 -35.568  1.00 75.60      B    O  
ANISOU  194  O   SER B 450    12462   8802   7463   3275   2569  -1383  B    O  
ATOM    195  CB  SER B 450      -7.192 -17.255 -35.941  1.00 74.11      B    C  
ANISOU  195  CB  SER B 450    12519   8841   6798   2986   2224  -1125  B    C  
ATOM    196  OG  SER B 450      -6.723 -16.088 -35.285  1.00 77.34      B    O  
ANISOU  196  OG  SER B 450    12590   9358   7438   2794   2445   -813  B    O  
ATOM    197  N   THR B 451      -5.222 -18.609 -33.607  1.00 77.29      B    N  
ANISOU  197  N   THR B 451    11975   9114   8279   2816   2440  -1013  B    N  
ATOM    198  CA  THR B 451      -3.899 -19.096 -33.240  1.00 79.90      B    C  
ANISOU  198  CA  THR B 451    12011   9429   8920   2929   2735   -970  B    C  
ATOM    199  C   THR B 451      -3.959 -20.385 -32.363  1.00 82.43      B    C  
ANISOU  199  C   THR B 451    12196   9573   9552   2921   2457  -1091  B    C  
ATOM    200  O   THR B 451      -2.915 -20.913 -32.013  1.00 82.48      B    O  
ANISOU  200  O   THR B 451    11965   9547   9827   3048   2638  -1073  B    O  
ATOM    201  CB  THR B 451      -3.123 -17.962 -32.547  1.00 81.10      B    C  
ANISOU  201  CB  THR B 451    11729   9723   9362   2768   2958   -702  B    C  
ATOM    202  CG2 THR B 451      -3.076 -16.683 -33.388  1.00 81.11      B    C  
ANISOU  202  CG2 THR B 451    11872   9846   9101   2760   3261   -548  B    C  
ATOM    203  OG1 THR B 451      -3.728 -17.690 -31.280  1.00 81.98      B    O  
ANISOU  203  OG1 THR B 451    11586   9837   9725   2497   2594   -617  B    O  
ATOM    204  N   ILE B 452      -5.168 -20.869 -31.997  1.00 84.32      B    N  
ANISOU  204  N   ILE B 452    12569   9685   9784   2778   2035  -1198  B    N  
ATOM    205  CA  ILE B 452      -5.391 -22.049 -31.148  1.00 86.66      B    C  
ANISOU  205  CA  ILE B 452    12781   9773  10375   2745   1785  -1275  B    C  
ATOM    206  C   ILE B 452      -6.236 -23.120 -31.875  1.00 88.79      B    C  
ANISOU  206  C   ILE B 452    13429   9815  10493   2834   1563  -1577  B    C  
ATOM    207  O   ILE B 452      -7.148 -23.710 -31.282  1.00 89.09      B    O  
ANISOU  207  O   ILE B 452    13469   9673  10708   2672   1244  -1636  B    O  
ATOM    208  CB  ILE B 452      -6.059 -21.649 -29.800  1.00 87.53      B    C  
ANISOU  208  CB  ILE B 452    12634   9899  10722   2449   1512  -1094  B    C  
ATOM    209  CG1 ILE B 452      -5.364 -20.445 -29.141  1.00 88.72      B    C  
ANISOU  209  CG1 ILE B 452    12442  10274  10993   2344   1668   -847  B    C  
ATOM    210  CG2 ILE B 452      -6.144 -22.843 -28.836  1.00 88.15      B    C  
ANISOU  210  CG2 ILE B 452    12632   9753  11107   2440   1328  -1104  B    C  
ATOM    211  CD1 ILE B 452      -3.997 -20.741 -28.681  1.00 90.08      B    C  
ANISOU  211  CD1 ILE B 452    12328  10470  11428   2493   1870   -775  B    C  
ATOM    212  N   GLN B 453      -5.961 -23.349 -33.160  1.00 90.03      B    N  
ANISOU  212  N   GLN B 453    13910   9970  10329   3089   1735  -1777  B    N  
ATOM    213  CA  GLN B 453      -6.704 -24.360 -33.912  1.00 91.95      B    C  
ANISOU  213  CA  GLN B 453    14525   9990  10420   3197   1496  -2122  B    C  
ATOM    214  C   GLN B 453      -5.852 -25.604 -34.146  1.00 92.84      B    C  
ANISOU  214  C   GLN B 453    14718   9905  10652   3469   1667  -2297  B    C  
ATOM    215  O   GLN B 453      -5.799 -26.098 -35.277  1.00 93.42      B    O  
ANISOU  215  O   GLN B 453    15161   9908  10424   3721   1728  -2578  B    O  
ATOM    216  CB  GLN B 453      -7.280 -23.787 -35.225  1.00 94.17      B    C  
ANISOU  216  CB  GLN B 453    15208  10389  10184   3310   1451  -2286  B    C  
ATOM    217  CG  GLN B 453      -6.299 -22.961 -36.050  1.00 97.67      B    C  
ANISOU  217  CG  GLN B 453    15758  11065  10287   3533   1919  -2157  B    C  
ATOM    218  CD  GLN B 453      -6.994 -22.340 -37.235  1.00101.93      B    C  
ANISOU  218  CD  GLN B 453    16737  11714  10276   3652   1833  -2276  B    C  
ATOM    219  NE2 GLN B 453      -6.295 -22.252 -38.361  1.00102.72      B    N  
ANISOU  219  NE2 GLN B 453    17162  11903   9966   3979   2206  -2331  B    N  
ATOM    220  OE1 GLN B 453      -8.159 -21.932 -37.158  1.00103.13      B    O  
ANISOU  220  OE1 GLN B 453    16950  11875  10359   3476   1440  -2316  B    O  
ATOM    221  N   SER B 454      -5.181 -26.125 -33.079  1.00 92.71      B    N  
ANISOU  221  N   SER B 454    14376   9793  11057   3449   1732  -2141  B    N  
ATOM    222  CA  SER B 454      -4.320 -27.293 -33.267  1.00 92.94      B    C  
ANISOU  222  CA  SER B 454    14458   9622  11232   3736   1902  -2290  B    C  
ATOM    223  C   SER B 454      -4.032 -28.179 -32.025  1.00 92.31      B    C  
ANISOU  223  C   SER B 454    14118   9321  11633   3701   1794  -2170  B    C  
ATOM    224  O   SER B 454      -3.693 -29.347 -32.239  1.00 92.64      B    O  
ANISOU  224  O   SER B 454    14296   9100  11805   3919   1826  -2356  B    O  
ATOM    225  CB  SER B 454      -2.994 -26.878 -33.898  1.00 94.82      B    C  
ANISOU  225  CB  SER B 454    14630  10063  11336   4007   2385  -2231  B    C  
ATOM    226  OG  SER B 454      -3.149 -26.589 -35.279  1.00 97.45      B    O  
ANISOU  226  OG  SER B 454    15361  10487  11178   4181   2538  -2424  B    O  
ATOM    227  N   LEU B 455      -4.097 -27.664 -30.768  1.00 91.10      B    N  
ANISOU  227  N   LEU B 455    13629   9263  11721   3474   1684  -1867  B    N  
ATOM    228  CA  LEU B 455      -3.797 -28.522 -29.599  1.00 90.28      B    C  
ANISOU  228  CA  LEU B 455    13340   8952  12011   3494   1585  -1730  B    C  
ATOM    229  C   LEU B 455      -4.892 -29.577 -29.353  1.00 88.37      B    C  
ANISOU  229  C   LEU B 455    13319   8333  11926   3375   1298  -1859  B    C  
ATOM    230  O   LEU B 455      -5.879 -29.308 -28.668  1.00 88.88      B    O  
ANISOU  230  O   LEU B 455    13337   8368  12065   3089   1079  -1740  B    O  
ATOM    231  CB  LEU B 455      -3.485 -27.713 -28.321  1.00 90.87      B    C  
ANISOU  231  CB  LEU B 455    13035   9238  12252   3338   1544  -1390  B    C  
ATOM    232  CG  LEU B 455      -2.941 -28.537 -27.129  1.00 92.82      B    C  
ANISOU  232  CG  LEU B 455    13108   9315  12843   3445   1461  -1221  B    C  
ATOM    233  CD1 LEU B 455      -1.580 -29.113 -27.425  1.00 93.51      B    C  
ANISOU  233  CD1 LEU B 455    13084   9372  13074   3805   1689  -1280  B    C  
ATOM    234  CD2 LEU B 455      -2.854 -27.703 -25.873  1.00 93.68      B    C  
ANISOU  234  CD2 LEU B 455    12919   9636  13040   3282   1347   -927  B    C  
ATOM    235  N   VAL B 456      -4.717 -30.766 -29.933  1.00 85.99      B    N  
ANISOU  235  N   VAL B 456    13249   7725  11699   3594   1325  -2114  B    N  
ATOM    236  CA  VAL B 456      -5.699 -31.844 -29.870  1.00 84.15      B    C  
ANISOU  236  CA  VAL B 456    13235   7073  11665   3491   1081  -2291  B    C  
ATOM    237  C   VAL B 456      -5.871 -32.436 -28.463  1.00 81.03      B    C  
ANISOU  237  C   VAL B 456    12682   6443  11661   3374    977  -2012  B    C  
ATOM    238  O   VAL B 456      -4.903 -32.636 -27.728  1.00 81.19      B    O  
ANISOU  238  O   VAL B 456    12521   6490  11837   3550   1097  -1787  B    O  
ATOM    239  CB  VAL B 456      -5.412 -32.938 -30.926  1.00 85.20      B    C  
ANISOU  239  CB  VAL B 456    13679   6918  11774   3778   1143  -2673  B    C  
ATOM    240  CG1 VAL B 456      -5.508 -32.356 -32.335  1.00 86.15      B    C  
ANISOU  240  CG1 VAL B 456    14048   7254  11432   3881   1205  -2963  B    C  
ATOM    241  CG2 VAL B 456      -4.053 -33.590 -30.701  1.00 85.30      B    C  
ANISOU  241  CG2 VAL B 456    13586   6858  11967   4123   1398  -2597  B    C  
ATOM    242  N   GLY B 457      -7.119 -32.717 -28.114  1.00 77.64      B    N  
ANISOU  242  N   GLY B 457    12328   5780  11391   3091    755  -2028  B    N  
ATOM    243  CA  GLY B 457      -7.450 -33.250 -26.800  1.00 74.66      B    C  
ANISOU  243  CA  GLY B 457    11854   5159  11354   2960    694  -1739  B    C  
ATOM    244  C   GLY B 457      -7.679 -32.169 -25.758  1.00 70.79      B    C  
ANISOU  244  C   GLY B 457    11119   4986  10793   2752    673  -1387  B    C  
ATOM    245  O   GLY B 457      -7.755 -32.462 -24.563  1.00 70.38      B    O  
ANISOU  245  O   GLY B 457    10990   4812  10938   2703    667  -1089  B    O  
ATOM    246  N   SER B 458      -7.795 -30.914 -26.195  1.00 68.13      B    N  
ANISOU  246  N   SER B 458    10687   5042  10158   2646    669  -1414  B    N  
ATOM    247  CA  SER B 458      -7.968 -29.817 -25.267  1.00 66.17      B    C  
ANISOU  247  CA  SER B 458    10213   5096   9832   2464    649  -1119  B    C  
ATOM    248  C   SER B 458      -9.263 -29.047 -25.456  1.00 63.58      B    C  
ANISOU  248  C   SER B 458     9886   4862   9410   2150    504  -1176  B    C  
ATOM    249  O   SER B 458      -9.851 -29.056 -26.536  1.00 64.06      B    O  
ANISOU  249  O   SER B 458    10100   4876   9364   2107    410  -1469  B    O  
ATOM    250  CB  SER B 458      -6.760 -28.887 -25.316  1.00 67.55      B    C  
ANISOU  250  CB  SER B 458    10192   5663   9813   2629    798  -1019  B    C  
ATOM    251  OG  SER B 458      -6.640 -28.260 -26.581  1.00 69.80      B    O  
ANISOU  251  OG  SER B 458    10552   6137   9830   2674    880  -1242  B    O  
ATOM    252  N   THR B 459      -9.729 -28.420 -24.378  1.00 60.63      B    N  
ANISOU  252  N   THR B 459     9351   4608   9077   1955    470   -907  B    N  
ATOM    253  CA  THR B 459     -10.894 -27.562 -24.416  1.00 58.91      B    C  
ANISOU  253  CA  THR B 459     9078   4514   8790   1675    353   -924  B    C  
ATOM    254  C   THR B 459     -10.352 -26.134 -24.340  1.00 55.67      B    C  
ANISOU  254  C   THR B 459     8505   4541   8106   1682    414   -799  B    C  
ATOM    255  O   THR B 459      -9.366 -25.899 -23.646  1.00 55.39      B    O  
ANISOU  255  O   THR B 459     8337   4656   8055   1810    512   -605  B    O  
ATOM    256  CB  THR B 459     -11.804 -27.822 -23.214  1.00 61.43      B    C  
ANISOU  256  CB  THR B 459     9330   4655   9356   1461    325   -700  B    C  
ATOM    257  CG2 THR B 459     -12.359 -29.240 -23.191  1.00 61.42      B    C  
ANISOU  257  CG2 THR B 459     9467   4165   9704   1419    303   -787  B    C  
ATOM    258  OG1 THR B 459     -11.075 -27.561 -22.010  1.00 63.41      B    O  
ANISOU  258  OG1 THR B 459     9473   5050   9569   1555    423   -377  B    O  
ATOM    259  N   VAL B 460     -10.973 -25.189 -25.052  1.00 52.70      B    N  
ANISOU  259  N   VAL B 460     8135   4350   7537   1557    341   -918  B    N  
ATOM    260  CA  VAL B 460     -10.532 -23.802 -25.032  1.00 50.57      B    C  
ANISOU  260  CA  VAL B 460     7725   4446   7044   1545    414   -801  B    C  
ATOM    261  C   VAL B 460     -11.703 -22.965 -24.543  1.00 48.93      B    C  
ANISOU  261  C   VAL B 460     7427   4323   6841   1286    291   -718  B    C  
ATOM    262  O   VAL B 460     -12.765 -23.009 -25.157  1.00 49.23      B    O  
ANISOU  262  O   VAL B 460     7554   4266   6886   1169    144   -891  B    O  
ATOM    263  CB  VAL B 460     -10.080 -23.366 -26.432  1.00 51.14      B    C  
ANISOU  263  CB  VAL B 460     7926   4660   6846   1690    492   -992  B    C  
ATOM    264  CG1 VAL B 460      -9.633 -21.911 -26.435  1.00 51.58      B    C  
ANISOU  264  CG1 VAL B 460     7835   5046   6718   1659    606   -850  B    C  
ATOM    265  CG2 VAL B 460      -8.977 -24.280 -26.952  1.00 51.63      B    C  
ANISOU  265  CG2 VAL B 460     8083   4613   6922   1965    646  -1101  B    C  
ATOM    266  N   GLN B 461     -11.536 -22.247 -23.427  1.00 46.73      B    N  
ANISOU  266  N   GLN B 461     6968   4210   6575   1210    333   -479  B    N  
ATOM    267  CA  GLN B 461     -12.628 -21.476 -22.872  1.00 45.36      B    C  
ANISOU  267  CA  GLN B 461     6707   4109   6419    986    249   -396  B    C  
ATOM    268  C   GLN B 461     -12.190 -20.162 -22.232  1.00 41.70      B    C  
ANISOU  268  C   GLN B 461     6079   3939   5826    955    302   -231  B    C  
ATOM    269  O   GLN B 461     -11.074 -20.055 -21.715  1.00 41.61      B    O  
ANISOU  269  O   GLN B 461     5977   4036   5798   1080    380   -122  B    O  
ATOM    270  CB  GLN B 461     -13.392 -22.338 -21.841  1.00 49.40      B    C  
ANISOU  270  CB  GLN B 461     7214   4372   7183    874    234   -279  B    C  
ATOM    271  CG  GLN B 461     -12.696 -22.449 -20.472  1.00 54.62      B    C  
ANISOU  271  CG  GLN B 461     7813   5076   7863    958    326    -12  B    C  
ATOM    272  CD  GLN B 461     -12.976 -23.706 -19.669  1.00 60.49      B    C  
ANISOU  272  CD  GLN B 461     8649   5506   8827    971    378    122  B    C  
ATOM    273  NE2 GLN B 461     -14.027 -24.459 -20.031  1.00 60.84      B    N  
ANISOU  273  NE2 GLN B 461     8758   5255   9102    826    355     13  B    N  
ATOM    274  OE1 GLN B 461     -12.240 -24.016 -18.712  1.00 61.43      B    O  
ANISOU  274  OE1 GLN B 461     8783   5632   8926   1119    432    325  B    O  
ATOM    275  N   LEU B 462     -13.083 -19.174 -22.256  1.00 37.89      B    N  
ANISOU  275  N   LEU B 462     5545   3568   5285    794    237   -231  B    N  
ATOM    276  CA  LEU B 462     -12.824 -17.931 -21.587  1.00 35.94      B    C  
ANISOU  276  CA  LEU B 462     5152   3552   4950    743    271    -96  B    C  
ATOM    277  C   LEU B 462     -13.216 -18.166 -20.118  1.00 34.96      B    C  
ANISOU  277  C   LEU B 462     4967   3379   4935    673    269     75  B    C  
ATOM    278  O   LEU B 462     -14.282 -18.709 -19.845  1.00 35.96      B    O  
ANISOU  278  O   LEU B 462     5132   3335   5196    561    246     84  B    O  
ATOM    279  CB  LEU B 462     -13.663 -16.792 -22.217  1.00 35.58      B    C  
ANISOU  279  CB  LEU B 462     5100   3618   4800    626    209   -163  B    C  
ATOM    280  CG  LEU B 462     -13.433 -15.403 -21.576  1.00 36.37      B    C  
ANISOU  280  CG  LEU B 462     5058   3929   4833    565    247    -45  B    C  
ATOM    281  CD1 LEU B 462     -13.496 -14.305 -22.607  1.00 36.74      B    C  
ANISOU  281  CD1 LEU B 462     5139   4089   4731    561    258   -103  B    C  
ATOM    282  CD2 LEU B 462     -14.441 -15.134 -20.508  1.00 36.62      B    C  
ANISOU  282  CD2 LEU B 462     5016   3948   4948    426    198     39  B    C  
ATOM    283  N   ARG B 463     -12.348 -17.802 -19.189  1.00 33.38      B    N  
ANISOU  283  N   ARG B 463     4680   3316   4685    752    299    205  B    N  
ATOM    284  CA  ARG B 463     -12.612 -17.916 -17.756  1.00 32.82      B    C  
ANISOU  284  CA  ARG B 463     4605   3238   4628    738    300    378  B    C  
ATOM    285  C   ARG B 463     -12.656 -16.509 -17.200  1.00 31.60      B    C  
ANISOU  285  C   ARG B 463     4337   3311   4358    667    272    406  B    C  
ATOM    286  O   ARG B 463     -11.944 -15.628 -17.694  1.00 31.51      B    O  
ANISOU  286  O   ARG B 463     4222   3455   4294    683    257    332  B    O  
ATOM    287  CB  ARG B 463     -11.452 -18.611 -17.014  1.00 34.61      B    C  
ANISOU  287  CB  ARG B 463     4844   3456   4849    946    292    484  B    C  
ATOM    288  CG  ARG B 463     -10.874 -19.832 -17.665  1.00 39.70      B    C  
ANISOU  288  CG  ARG B 463     5567   3916   5599   1089    319    432  B    C  
ATOM    289  CD  ARG B 463     -11.539 -21.083 -17.210  1.00 43.95      B    C  
ANISOU  289  CD  ARG B 463     6266   4166   6266   1090    362    533  B    C  
ATOM    290  NE  ARG B 463     -11.723 -21.191 -15.756  1.00 46.59      B    N  
ANISOU  290  NE  ARG B 463     6662   4495   6544   1128    382    764  B    N  
ATOM    291  CZ  ARG B 463     -12.363 -22.198 -15.169  1.00 48.30      B    C  
ANISOU  291  CZ  ARG B 463     7033   4445   6872   1121    477    918  B    C  
ATOM    292  NH1 ARG B 463     -12.840 -23.204 -15.892  1.00 46.87      B    N1+
ANISOU  292  NH1 ARG B 463     6927   3967   6916   1060    531    838  B    N1+
ATOM    293  NH2 ARG B 463     -12.525 -22.212 -13.855  1.00 48.53      B    N  
ANISOU  293  NH2 ARG B 463     7159   4490   6791   1182    530   1149  B    N  
ATOM    294  N   TYR B 464     -13.399 -16.322 -16.121  1.00 30.71      B    N  
ANISOU  294  N   TYR B 464     4248   3202   4217    605    289    518  B    N  
ATOM    295  CA  TYR B 464     -13.457 -15.030 -15.482  1.00 32.79      B    C  
ANISOU  295  CA  TYR B 464     4430   3662   4369    558    258    525  B    C  
ATOM    296  C   TYR B 464     -13.801 -15.109 -13.991  1.00 32.48      B    C  
ANISOU  296  C   TYR B 464     4473   3639   4229    602    289    675  B    C  
ATOM    297  O   TYR B 464     -14.348 -16.096 -13.498  1.00 32.38      B    O  
ANISOU  297  O   TYR B 464     4585   3462   4259    619    386    806  B    O  
ATOM    298  CB  TYR B 464     -14.445 -14.093 -16.228  1.00 33.93      B    C  
ANISOU  298  CB  TYR B 464     4514   3834   4545    390    265    427  B    C  
ATOM    299  CG  TYR B 464     -15.874 -14.398 -15.848  1.00 36.96      B    C  
ANISOU  299  CG  TYR B 464     4931   4094   5020    275    334    478  B    C  
ATOM    300  CD1 TYR B 464     -16.506 -15.544 -16.311  1.00 38.44      B    C  
ANISOU  300  CD1 TYR B 464     5168   4061   5377    228    366    467  B    C  
ATOM    301  CD2 TYR B 464     -16.573 -13.576 -14.968  1.00 38.81      B    C  
ANISOU  301  CD2 TYR B 464     5130   4410   5204    217    382    529  B    C  
ATOM    302  CE1 TYR B 464     -17.790 -15.877 -15.893  1.00 40.55      B    C  
ANISOU  302  CE1 TYR B 464     5414   4186   5807    106    457    519  B    C  
ATOM    303  CE2 TYR B 464     -17.859 -13.895 -14.552  1.00 40.58      B    C  
ANISOU  303  CE2 TYR B 464     5351   4513   5554    119    498    590  B    C  
ATOM    304  CZ  TYR B 464     -18.460 -15.047 -15.018  1.00 43.13      B    C  
ANISOU  304  CZ  TYR B 464     5686   4611   6090     53    541    592  B    C  
ATOM    305  OH  TYR B 464     -19.750 -15.331 -14.660  1.00 48.90      B    O  
ANISOU  305  OH  TYR B 464     6355   5200   7025    -70    673    640  B    O  
ATOM    306  N   HIS B 465     -13.513 -14.036 -13.308  1.00 32.21      B    N  
ANISOU  306  N   HIS B 465     4385   3790   4063    621    224    652  B    N  
ATOM    307  CA  HIS B 465     -13.930 -13.827 -11.943  1.00 33.45      B    C  
ANISOU  307  CA  HIS B 465     4649   4003   4059    673    256    758  B    C  
ATOM    308  C   HIS B 465     -14.239 -12.359 -11.796  1.00 33.50      B    C  
ANISOU  308  C   HIS B 465     4562   4160   4009    582    220    645  B    C  
ATOM    309  O   HIS B 465     -13.706 -11.509 -12.535  1.00 33.20      B    O  
ANISOU  309  O   HIS B 465     4377   4200   4037    525    133    508  B    O  
ATOM    310  CB  HIS B 465     -12.962 -14.379 -10.886  1.00 34.61      B    C  
ANISOU  310  CB  HIS B 465     4911   4200   4038    907    159    858  B    C  
ATOM    311  CG  HIS B 465     -11.619 -13.734 -10.876  1.00 38.13      B    C  
ANISOU  311  CG  HIS B 465     5213   4818   4456   1008    -59    723  B    C  
ATOM    312  CD2 HIS B 465     -10.430 -14.213 -11.308  1.00 39.93      B    C  
ANISOU  312  CD2 HIS B 465     5338   5049   4783   1125   -168    682  B    C  
ATOM    313  ND1 HIS B 465     -11.414 -12.520 -10.255  1.00 41.06      B    N  
ANISOU  313  ND1 HIS B 465     5522   5363   4717   1006   -181    611  B    N  
ATOM    314  CE1 HIS B 465     -10.117 -12.274 -10.370  1.00 41.96      B    C  
ANISOU  314  CE1 HIS B 465     5468   5573   4902   1095   -372    496  B    C  
ATOM    315  NE2 HIS B 465      -9.485 -13.267 -10.990  1.00 41.72      B    N  
ANISOU  315  NE2 HIS B 465     5398   5454   4999   1175   -359    542  B    N  
ATOM    316  N   ARG B 466     -15.189 -12.070 -10.931  1.00 33.31      B    N  
ANISOU  316  N   ARG B 466     4625   4143   3889    561    328    711  B    N  
ATOM    317  CA  ARG B 466     -15.647 -10.710 -10.752  1.00 33.11      B    C  
ANISOU  317  CA  ARG B 466     4528   4227   3825    483    318    600  B    C  
ATOM    318  C   ARG B 466     -15.282 -10.232  -9.345  1.00 33.12      B    C  
ANISOU  318  C   ARG B 466     4653   4366   3563    636    254    599  B    C  
ATOM    319  O   ARG B 466     -15.412 -10.983  -8.394  1.00 32.68      B    O  
ANISOU  319  O   ARG B 466     4791   4291   3336    771    334    749  B    O  
ATOM    320  CB  ARG B 466     -17.166 -10.667 -11.035  1.00 34.60      B    C  
ANISOU  320  CB  ARG B 466     4685   4308   4152    338    502    633  B    C  
ATOM    321  CG  ARG B 466     -17.804  -9.331 -10.729  1.00 38.91      B    C  
ANISOU  321  CG  ARG B 466     5174   4943   4667    287    525    539  B    C  
ATOM    322  CD  ARG B 466     -19.223  -9.225 -11.261  1.00 42.70      B    C  
ANISOU  322  CD  ARG B 466     5549   5319   5358    149    659    538  B    C  
ATOM    323  NE  ARG B 466     -20.220  -9.902 -10.421  1.00 44.82      B    N  
ANISOU  323  NE  ARG B 466     5879   5498   5652    151    901    681  B    N  
ATOM    324  CZ  ARG B 466     -20.735  -9.398  -9.303  1.00 46.28      B    C  
ANISOU  324  CZ  ARG B 466     6141   5746   5697    218   1061    720  B    C  
ATOM    325  NH1 ARG B 466     -20.349  -8.209  -8.864  1.00 44.07      B    N1+
ANISOU  325  NH1 ARG B 466     5890   5615   5238    288    962    597  B    N1+
ATOM    326  NH2 ARG B 466     -21.680 -10.056  -8.647  1.00 47.37      B    N  
ANISOU  326  NH2 ARG B 466     6322   5779   5898    210   1344    874  B    N  
ATOM    327  N   ARG B 467     -14.765  -9.012  -9.223  1.00 33.25      B    N  
ANISOU  327  N   ARG B 467     4580   4509   3544    631    102    426  B    N  
ATOM    328  CA  ARG B 467     -14.451  -8.422  -7.925  1.00 33.84      B    C  
ANISOU  328  CA  ARG B 467     4776   4717   3363    780     -9    357  B    C  
ATOM    329  C   ARG B 467     -15.576  -7.414  -7.655  1.00 33.28      B    C  
ANISOU  329  C   ARG B 467     4721   4654   3270    696    129    294  B    C  
ATOM    330  O   ARG B 467     -15.974  -6.700  -8.570  1.00 33.69      B    O  
ANISOU  330  O   ARG B 467     4608   4656   3537    533    161    214  B    O  
ATOM    331  CB  ARG B 467     -13.104  -7.697  -7.960  1.00 36.85      B    C  
ANISOU  331  CB  ARG B 467     5009   5202   3790    816   -295    160  B    C  
ATOM    332  CG  ARG B 467     -12.640  -7.327  -6.559  1.00 43.17      B    C  
ANISOU  332  CG  ARG B 467     5959   6140   4303   1016   -491     60  B    C  
ATOM    333  CD  ARG B 467     -11.250  -6.719  -6.542  1.00 49.05      B    C  
ANISOU  333  CD  ARG B 467     6506   6968   5162   1050   -815   -164  B    C  
ATOM    334  NE  ARG B 467     -11.318  -5.259  -6.619  1.00 53.89      B    N  
ANISOU  334  NE  ARG B 467     6990   7586   5900    915   -876   -389  B    N  
ATOM    335  CZ  ARG B 467     -10.325  -4.444  -6.284  1.00 56.85      B    C  
ANISOU  335  CZ  ARG B 467     7213   8017   6369    934  -1161   -638  B    C  
ATOM    336  NH1 ARG B 467      -9.170  -4.936  -5.846  1.00 58.20      B    N1+
ANISOU  336  NH1 ARG B 467     7318   8272   6522   1094  -1438   -705  B    N1+
ATOM    337  NH2 ARG B 467     -10.478  -3.133  -6.377  1.00 55.84      B    N  
ANISOU  337  NH2 ARG B 467     6984   7845   6388    798  -1183   -832  B    N  
ATOM    338  N   SER B 468     -16.092  -7.343  -6.432  1.00 32.34      B    N  
ANISOU  338  N   SER B 468     4812   4592   2884    831    224    335  B    N  
ATOM    339  CA  SER B 468     -17.253  -6.501  -6.118  1.00 32.29      B    C  
ANISOU  339  CA  SER B 468     4824   4580   2864    779    410    289  B    C  
ATOM    340  C   SER B 468     -17.157  -5.071  -6.656  1.00 32.14      B    C  
ANISOU  340  C   SER B 468     4625   4576   3011    662    280     59  B    C  
ATOM    341  O   SER B 468     -18.101  -4.588  -7.291  1.00 31.75      B    O  
ANISOU  341  O   SER B 468     4455   4448   3160    531    418     52  B    O  
ATOM    342  CB  SER B 468     -17.542  -6.515  -4.631  1.00 32.93      B    C  
ANISOU  342  CB  SER B 468     5195   4749   2568    993    512    332  B    C  
ATOM    343  OG  SER B 468     -16.415  -6.051  -3.905  1.00 35.78      B    O  
ANISOU  343  OG  SER B 468     5660   5250   2684   1162    201    160  B    O  
ATOM    344  N   LEU B 469     -16.002  -4.423  -6.457  1.00 31.65      B    N  
ANISOU  344  N   LEU B 469     4526   4592   2908    709      5   -127  B    N  
ATOM    345  CA  LEU B 469     -15.799  -3.084  -6.989  1.00 32.02      B    C  
ANISOU  345  CA  LEU B 469     4401   4606   3160    585   -103   -330  B    C  
ATOM    346  C   LEU B 469     -14.389  -2.989  -7.547  1.00 33.28      B    C  
ANISOU  346  C   LEU B 469     4386   4772   3488    538   -340   -427  B    C  
ATOM    347  O   LEU B 469     -13.438  -3.391  -6.868  1.00 33.04      B    O  
ANISOU  347  O   LEU B 469     4399   4832   3321    674   -540   -480  B    O  
ATOM    348  CB  LEU B 469     -15.904  -2.030  -5.894  1.00 31.70      B    C  
ANISOU  348  CB  LEU B 469     4480   4625   2938    688   -180   -537  B    C  
ATOM    349  CG  LEU B 469     -17.279  -1.712  -5.330  1.00 33.16      B    C  
ANISOU  349  CG  LEU B 469     4804   4800   2998    738     79   -504  B    C  
ATOM    350  CD1 LEU B 469     -17.140  -0.708  -4.163  1.00 33.29      B    C  
ANISOU  350  CD1 LEU B 469     4982   4887   2779    886    -39   -754  B    C  
ATOM    351  CD2 LEU B 469     -18.236  -1.195  -6.445  1.00 33.32      B    C  
ANISOU  351  CD2 LEU B 469     4632   4688   3340    558    247   -463  B    C  
ATOM    352  N   TYR B 470     -14.264  -2.410  -8.756  1.00 33.57      B    N  
ANISOU  352  N   TYR B 470     4226   4709   3821    365   -310   -450  B    N  
ATOM    353  CA  TYR B 470     -13.021  -2.051  -9.421  1.00 34.85      B    C  
ANISOU  353  CA  TYR B 470     4182   4841   4219    286   -450   -543  B    C  
ATOM    354  C   TYR B 470     -12.103  -3.227  -9.761  1.00 36.44      B    C  
ANISOU  354  C   TYR B 470     4320   5081   4443    340   -504   -444  B    C  
ATOM    355  O   TYR B 470     -12.369  -4.376  -9.395  1.00 35.13      B    O  
ANISOU  355  O   TYR B 470     4297   4958   4091    454   -465   -304  B    O  
ATOM    356  CB  TYR B 470     -12.291  -0.990  -8.571  1.00 34.87      B    C  
ANISOU  356  CB  TYR B 470     4129   4869   4250    312   -677   -805  B    C  
ATOM    357  CG  TYR B 470     -13.121   0.272  -8.437  1.00 36.20      B    C  
ANISOU  357  CG  TYR B 470     4340   4952   4461    246   -607   -919  B    C  
ATOM    358  CD1 TYR B 470     -13.480   1.010  -9.554  1.00 37.04      B    C  
ANISOU  358  CD1 TYR B 470     4339   4910   4825     88   -459   -872  B    C  
ATOM    359  CD2 TYR B 470     -13.582   0.697  -7.198  1.00 37.70      B    C  
ANISOU  359  CD2 TYR B 470     4711   5206   4408    375   -674  -1064  B    C  
ATOM    360  CE1 TYR B 470     -14.286   2.135  -9.449  1.00 38.83      B    C  
ANISOU  360  CE1 TYR B 470     4612   5039   5104     54   -392   -961  B    C  
ATOM    361  CE2 TYR B 470     -14.359   1.845  -7.075  1.00 39.16      B    C  
ANISOU  361  CE2 TYR B 470     4936   5299   4646    336   -595  -1181  B    C  
ATOM    362  CZ  TYR B 470     -14.725   2.553  -8.209  1.00 40.55      B    C  
ANISOU  362  CZ  TYR B 470     4978   5312   5117    173   -457  -1123  B    C  
ATOM    363  OH  TYR B 470     -15.476   3.705  -8.117  1.00 42.76      B    O  
ANISOU  363  OH  TYR B 470     5294   5477   5478    153   -386  -1232  B    O  
ATOM    364  N   CYS B 471     -11.016  -2.922 -10.460  1.00 38.58      B    N  
ANISOU  364  N   CYS B 471     4372   5316   4971    264   -568   -513  B    N  
ATOM    365  CA  CYS B 471     -10.016  -3.891 -10.864  1.00 41.53      B    C  
ANISOU  365  CA  CYS B 471     4635   5717   5428    321   -610   -451  B    C  
ATOM    366  C   CYS B 471      -8.846  -3.834  -9.932  1.00 45.18      B    C  
ANISOU  366  C   CYS B 471     4981   6272   5914    436   -896   -621  B    C  
ATOM    367  O   CYS B 471      -8.402  -2.735  -9.600  1.00 45.44      B    O  
ANISOU  367  O   CYS B 471     4877   6289   6099    370  -1036   -826  B    O  
ATOM    368  CB  CYS B 471      -9.566  -3.575 -12.283  1.00 41.80      B    C  
ANISOU  368  CB  CYS B 471     4487   5649   5746    179   -451   -415  B    C  
ATOM    369  SG  CYS B 471     -10.697  -4.164 -13.551  1.00 44.13      B    S  
ANISOU  369  SG  CYS B 471     4936   5862   5969    124   -191   -210  B    S  
ATOM    370  N   PRO B 472      -8.248  -4.985  -9.577  1.00 47.92      B    N  
ANISOU  370  N   PRO B 472     5352   6694   6161    609  -1008   -554  B    N  
ATOM    371  CA  PRO B 472      -6.993  -4.931  -8.796  1.00 50.55      B    C  
ANISOU  371  CA  PRO B 472     5522   7120   6566    741  -1337   -738  B    C  
ATOM    372  C   PRO B 472      -5.865  -4.346  -9.658  1.00 54.06      B    C  
ANISOU  372  C   PRO B 472     5573   7497   7470    596  -1338   -860  B    C  
ATOM    373  O   PRO B 472      -5.934  -4.390 -10.891  1.00 53.97      B    O  
ANISOU  373  O   PRO B 472     5478   7388   7642    461  -1059   -737  B    O  
ATOM    374  CB  PRO B 472      -6.713  -6.399  -8.459  1.00 50.46      B    C  
ANISOU  374  CB  PRO B 472     5637   7169   6364    970  -1400   -581  B    C  
ATOM    375  CG  PRO B 472      -7.387  -7.168  -9.556  1.00 50.29      B    C  
ANISOU  375  CG  PRO B 472     5699   7042   6367    882  -1072   -352  B    C  
ATOM    376  CD  PRO B 472      -8.611  -6.368  -9.946  1.00 47.80      B    C  
ANISOU  376  CD  PRO B 472     5484   6657   6019    693   -859   -328  B    C  
ATOM    377  N   ASP B 473      -4.826  -3.782  -9.021  1.00 57.06      B    N  
ANISOU  377  N   ASP B 473     5711   7920   8048    629  -1645  -1109  B    N  
ATOM    378  CA  ASP B 473      -3.701  -3.184  -9.751  1.00 59.78      B    C  
ANISOU  378  CA  ASP B 473     5629   8178   8907    474  -1621  -1234  B    C  
ATOM    379  C   ASP B 473      -3.075  -4.122 -10.789  1.00 60.49      B    C  
ANISOU  379  C   ASP B 473     5556   8244   9183    500  -1409  -1067  B    C  
ATOM    380  O   ASP B 473      -2.778  -3.691 -11.901  1.00 60.79      B    O  
ANISOU  380  O   ASP B 473     5395   8165   9537    326  -1128  -1020  B    O  
ATOM    381  CB  ASP B 473      -2.632  -2.663  -8.789  1.00 64.02      B    C  
ANISOU  381  CB  ASP B 473     5895   8770   9659    536  -2049  -1555  B    C  
ATOM    382  CG  ASP B 473      -2.024  -1.366  -9.270  1.00 72.10      B    C  
ANISOU  382  CG  ASP B 473     6552   9632  11209    274  -1995  -1746  B    C  
ATOM    383  OD1 ASP B 473      -2.784  -0.514  -9.788  1.00 73.34      B    O  
ANISOU  383  OD1 ASP B 473     6822   9656  11388     82  -1739  -1689  B    O  
ATOM    384  OD2 ASP B 473      -0.785  -1.200  -9.130  1.00 75.77      B    O1-
ANISOU  384  OD2 ASP B 473     6604  10088  12099    263  -2206  -1950  B    O1-
ATOM    385  N   SER B 474      -2.894  -5.398 -10.436  1.00 60.72      B    N  
ANISOU  385  N   SER B 474     5699   8370   9002    734  -1519   -966  B    N  
ATOM    386  CA  SER B 474      -2.357  -6.378 -11.375  1.00 61.58      B    C  
ANISOU  386  CA  SER B 474     5692   8448   9257    795  -1319   -821  B    C  
ATOM    387  C   SER B 474      -3.275  -7.579 -11.398  1.00 61.10      B    C  
ANISOU  387  C   SER B 474     6016   8392   8807    928  -1203   -590  B    C  
ATOM    388  O   SER B 474      -3.435  -8.247 -10.379  1.00 61.42      B    O  
ANISOU  388  O   SER B 474     6258   8512   8568   1134  -1425   -558  B    O  
ATOM    389  CB  SER B 474      -0.928  -6.777 -11.015  1.00 64.59      B    C  
ANISOU  389  CB  SER B 474     5724   8898   9921    961  -1587   -962  B    C  
ATOM    390  OG  SER B 474      -0.778  -7.048  -9.631  1.00 68.65      B    O  
ANISOU  390  OG  SER B 474     6351   9540  10191   1189  -2022  -1070  B    O  
ATOM    391  N   PRO B 475      -3.938  -7.825 -12.544  1.00 60.41      B    N  
ANISOU  391  N   PRO B 475     6054   8205   8693    813   -857   -429  B    N  
ATOM    392  CA  PRO B 475      -4.894  -8.946 -12.630  1.00 59.65      B    C  
ANISOU  392  CA  PRO B 475     6297   8073   8294    902   -743   -237  B    C  
ATOM    393  C   PRO B 475      -4.264 -10.306 -12.391  1.00 58.82      B    C  
ANISOU  393  C   PRO B 475     6210   7976   8162   1143   -836   -164  B    C  
ATOM    394  O   PRO B 475      -3.086 -10.501 -12.684  1.00 58.55      B    O  
ANISOU  394  O   PRO B 475     5896   7959   8391   1226   -880   -236  B    O  
ATOM    395  CB  PRO B 475      -5.435  -8.843 -14.059  1.00 60.52      B    C  
ANISOU  395  CB  PRO B 475     6455   8075   8465    743   -412   -150  B    C  
ATOM    396  CG  PRO B 475      -5.162  -7.440 -14.477  1.00 61.32      B    C  
ANISOU  396  CG  PRO B 475     6354   8159   8787    556   -338   -254  B    C  
ATOM    397  CD  PRO B 475      -3.861  -7.090 -13.819  1.00 59.94      B    C  
ANISOU  397  CD  PRO B 475     5850   8048   8875    610   -558   -420  B    C  
ATOM    398  N   SER B 476      -5.057 -11.249 -11.870  1.00 58.24      B    N  
ANISOU  398  N   SER B 476     6456   7870   7802   1259   -842    -12  B    N  
ATOM    399  CA  SER B 476      -4.562 -12.585 -11.531  1.00 58.18      B    C  
ANISOU  399  CA  SER B 476     6526   7834   7746   1512   -931     89  B    C  
ATOM    400  C   SER B 476      -5.549 -13.701 -11.873  1.00 57.86      B    C  
ANISOU  400  C   SER B 476     6790   7639   7555   1522   -721    282  B    C  
ATOM    401  O   SER B 476      -6.765 -13.523 -11.763  1.00 56.89      B    O  
ANISOU  401  O   SER B 476     6877   7470   7270   1390   -601    355  B    O  
ATOM    402  CB  SER B 476      -4.207 -12.645 -10.044  1.00 59.29      B    C  
ANISOU  402  CB  SER B 476     6747   8091   7691   1735  -1266     68  B    C  
ATOM    403  OG  SER B 476      -3.939 -13.957  -9.575  1.00 61.56      B    O  
ANISOU  403  OG  SER B 476     7202   8328   7858   2008  -1348    219  B    O  
ATOM    404  N   ILE B 477      -5.011 -14.862 -12.263  1.00 58.47      B    N  
ANISOU  404  N   ILE B 477     6872   7619   7726   1684   -682    348  B    N  
ATOM    405  CA  ILE B 477      -5.815 -16.050 -12.562  1.00 60.05      B    C  
ANISOU  405  CA  ILE B 477     7345   7627   7845   1708   -510    507  B    C  
ATOM    406  C   ILE B 477      -6.021 -16.938 -11.310  1.00 62.42      B    C  
ANISOU  406  C   ILE B 477     7909   7873   7933   1924   -624    688  B    C  
ATOM    407  O   ILE B 477      -6.588 -18.024 -11.434  1.00 62.99      B    O  
ANISOU  407  O   ILE B 477     8201   7745   7986   1960   -481    838  B    O  
ATOM    408  CB  ILE B 477      -5.141 -16.895 -13.681  1.00 60.20      B    C  
ANISOU  408  CB  ILE B 477     7268   7528   8075   1788   -384    476  B    C  
ATOM    409  CG1 ILE B 477      -3.792 -17.470 -13.213  1.00 61.14      B    C  
ANISOU  409  CG1 ILE B 477     7231   7688   8313   2078   -569    465  B    C  
ATOM    410  CG2 ILE B 477      -4.977 -16.107 -14.969  1.00 60.41      B    C  
ANISOU  410  CG2 ILE B 477     7107   7592   8256   1608   -211    337  B    C  
ATOM    411  CD1 ILE B 477      -3.186 -18.521 -14.156  1.00 62.36      B    C  
ANISOU  411  CD1 ILE B 477     7342   7694   8658   2217   -428    454  B    C  
ATOM    412  N   HIS B 478      -5.499 -16.530 -10.135  1.00 63.28      B    N  
ANISOU  412  N   HIS B 478     8008   8142   7893   2089   -885    673  B    N  
ATOM    413  CA  HIS B 478      -5.522 -17.350  -8.927  1.00 64.35      B    C  
ANISOU  413  CA  HIS B 478     8428   8245   7778   2361  -1009    860  B    C  
ATOM    414  C   HIS B 478      -6.826 -17.296  -8.129  1.00 63.35      B    C  
ANISOU  414  C   HIS B 478     8638   8075   7358   2293   -865   1027  B    C  
ATOM    415  O   HIS B 478      -7.215 -18.357  -7.635  1.00 64.16      B    O  
ANISOU  415  O   HIS B 478     9030   8014   7335   2438   -760   1263  B    O  
ATOM    416  CB  HIS B 478      -4.307 -17.056  -8.053  1.00 66.85      B    C  
ANISOU  416  CB  HIS B 478     8608   8752   8041   2628  -1394    756  B    C  
ATOM    417  CG  HIS B 478      -3.051 -17.445  -8.762  1.00 71.86      B    C  
ANISOU  417  CG  HIS B 478     8919   9379   9007   2746  -1488    646  B    C  
ATOM    418  CD2 HIS B 478      -2.583 -18.679  -9.069  1.00 73.78      B    C  
ANISOU  418  CD2 HIS B 478     9197   9463   9372   2942  -1436    758  B    C  
ATOM    419  ND1 HIS B 478      -2.236 -16.499  -9.354  1.00 74.63      B    N  
ANISOU  419  ND1 HIS B 478     8849   9863   9645   2631  -1579    399  B    N  
ATOM    420  CE1 HIS B 478      -1.262 -17.179  -9.942  1.00 75.56      B    C  
ANISOU  420  CE1 HIS B 478     8745   9925  10039   2779  -1580    369  B    C  
ATOM    421  NE2 HIS B 478      -1.430 -18.496  -9.800  1.00 75.38      B    N  
ANISOU  421  NE2 HIS B 478     8992   9730   9920   2978  -1507    571  B    N  
ATOM    422  N   PRO B 479      -7.576 -16.170  -8.030  1.00 61.69      B    N  
ANISOU  422  N   PRO B 479     8407   7969   7063   2079   -805    934  B    N  
ATOM    423  CA  PRO B 479      -8.887 -16.237  -7.359  1.00 60.22      B    C  
ANISOU  423  CA  PRO B 479     8521   7715   6647   2018   -595   1106  B    C  
ATOM    424  C   PRO B 479      -9.805 -17.165  -8.171  1.00 58.56      B    C  
ANISOU  424  C   PRO B 479     8388   7240   6623   1857   -282   1250  B    C  
ATOM    425  O   PRO B 479      -9.728 -17.191  -9.411  1.00 59.13      B    O  
ANISOU  425  O   PRO B 479     8262   7242   6962   1695   -222   1131  B    O  
ATOM    426  CB  PRO B 479      -9.386 -14.787  -7.401  1.00 60.70      B    C  
ANISOU  426  CB  PRO B 479     8455   7924   6686   1804   -594    922  B    C  
ATOM    427  CG  PRO B 479      -8.196 -13.973  -7.691  1.00 61.36      B    C  
ANISOU  427  CG  PRO B 479     8236   8166   6911   1817   -866    678  B    C  
ATOM    428  CD  PRO B 479      -7.338 -14.818  -8.565  1.00 60.62      B    C  
ANISOU  428  CD  PRO B 479     7979   7982   7072   1878   -878    685  B    C  
ATOM    429  N   THR B 480     -10.624 -17.975  -7.484  1.00 56.03      B    N  
ANISOU  429  N   THR B 480     8362   6756   6172   1918    -82   1500  B    N  
ATOM    430  CA  THR B 480     -11.513 -18.950  -8.125  1.00 54.10      B    C  
ANISOU  430  CA  THR B 480     8185   6216   6154   1765    200   1629  B    C  
ATOM    431  C   THR B 480     -12.314 -18.368  -9.289  1.00 50.13      B    C  
ANISOU  431  C   THR B 480     7465   5685   5897   1438    312   1452  B    C  
ATOM    432  O   THR B 480     -12.884 -17.291  -9.171  1.00 50.28      B    O  
ANISOU  432  O   THR B 480     7409   5847   5849   1300    331   1361  B    O  
ATOM    433  CB  THR B 480     -12.419 -19.646  -7.127  1.00 57.34      B    C  
ANISOU  433  CB  THR B 480     8910   6455   6421   1827    455   1925  B    C  
ATOM    434  CG2 THR B 480     -12.916 -20.943  -7.668  1.00 58.16      B    C  
ANISOU  434  CG2 THR B 480     9088   6202   6808   1754    675   2069  B    C  
ATOM    435  OG1 THR B 480     -11.695 -19.924  -5.923  1.00 60.14      B    O  
ANISOU  435  OG1 THR B 480     9516   6900   6432   2171    318   2086  B    O  
ATOM    436  N   SER B 481     -12.281 -19.051 -10.421  1.00 46.37      B    N  
ANISOU  436  N   SER B 481     6901   5031   5686   1350    354   1385  B    N  
ATOM    437  CA  SER B 481     -12.895 -18.585 -11.643  1.00 43.71      B    C  
ANISOU  437  CA  SER B 481     6387   4673   5549   1098    400   1199  B    C  
ATOM    438  C   SER B 481     -13.989 -19.508 -12.157  1.00 41.72      B    C  
ANISOU  438  C   SER B 481     6194   4122   5538    940    584   1245  B    C  
ATOM    439  O   SER B 481     -14.177 -20.608 -11.650  1.00 40.91      B    O  
ANISOU  439  O   SER B 481     6260   3788   5496   1014    708   1431  B    O  
ATOM    440  CB  SER B 481     -11.821 -18.405 -12.711  1.00 43.53      B    C  
ANISOU  440  CB  SER B 481     6193   4735   5612   1138    257   1009  B    C  
ATOM    441  OG  SER B 481     -11.252 -19.662 -13.028  1.00 45.41      B    O  
ANISOU  441  OG  SER B 481     6506   4783   5966   1283    265   1054  B    O  
ATOM    442  N   GLU B 482     -14.737 -19.035 -13.150  1.00 40.88      B    N  
ANISOU  442  N   GLU B 482     5941   4438   5155    594    294   1010  B    N  
ATOM    443  CA  GLU B 482     -15.803 -19.788 -13.795  1.00 41.33      B    C  
ANISOU  443  CA  GLU B 482     5997   4352   5356    469    393    995  B    C  
ATOM    444  C   GLU B 482     -15.634 -19.704 -15.313  1.00 40.39      B    C  
ANISOU  444  C   GLU B 482     5773   4220   5353    464    323    854  B    C  
ATOM    445  O   GLU B 482     -15.190 -18.679 -15.826  1.00 38.78      B    O  
ANISOU  445  O   GLU B 482     5469   4148   5116    495    261    767  B    O  
ATOM    446  CB  GLU B 482     -17.169 -19.209 -13.403  1.00 44.54      B    C  
ANISOU  446  CB  GLU B 482     6337   4802   5785    323    523    983  B    C  
ATOM    447  CG  GLU B 482     -17.721 -19.886 -12.159  1.00 54.44      B    C  
ANISOU  447  CG  GLU B 482     7747   5968   6969    272    682   1132  B    C  
ATOM    448  CD  GLU B 482     -18.981 -19.255 -11.604  1.00 64.81      B    C  
ANISOU  448  CD  GLU B 482     8979   7340   8306    144    860   1114  B    C  
ATOM    449  OE1 GLU B 482     -18.929 -18.062 -11.226  1.00 67.71      B    O  
ANISOU  449  OE1 GLU B 482     9288   7870   8569    182    847   1057  B    O  
ATOM    450  OE2 GLU B 482     -20.019 -19.953 -11.541  1.00 67.67      B    O1-
ANISOU  450  OE2 GLU B 482     9327   7574   8813      2   1023   1146  B    O1-
ATOM    451  N   PRO B 483     -15.989 -20.769 -16.052  1.00 41.23      B    N  
ANISOU  451  N   PRO B 483     5928   4155   5582    417    338    828  B    N  
ATOM    452  CA  PRO B 483     -15.949 -20.662 -17.519  1.00 41.32      B    C  
ANISOU  452  CA  PRO B 483     5889   4152   5659    405    274    681  B    C  
ATOM    453  C   PRO B 483     -17.163 -19.862 -17.976  1.00 41.04      B    C  
ANISOU  453  C   PRO B 483     5741   4178   5676    273    259    598  B    C  
ATOM    454  O   PRO B 483     -18.221 -19.871 -17.336  1.00 40.98      B    O  
ANISOU  454  O   PRO B 483     5682   4152   5737    166    328    636  B    O  
ATOM    455  CB  PRO B 483     -16.000 -22.119 -18.001  1.00 42.42      B    C  
ANISOU  455  CB  PRO B 483     6148   4066   5905    397    285    672  B    C  
ATOM    456  CG  PRO B 483     -16.348 -22.956 -16.794  1.00 42.67      B    C  
ANISOU  456  CG  PRO B 483     6278   3975   5959    362    371    828  B    C  
ATOM    457  CD  PRO B 483     -16.555 -22.064 -15.610  1.00 41.07      B    C  
ANISOU  457  CD  PRO B 483     6034   3931   5641    352    422    923  B    C  
ATOM    458  N   LYS B 484     -16.999 -19.127 -19.054  1.00 40.73      B    N  
ANISOU  458  N   LYS B 484     5663   4207   5605    289    177    487  B    N  
ATOM    459  CA  LYS B 484     -18.059 -18.308 -19.620  1.00 41.34      B    C  
ANISOU  459  CA  LYS B 484     5647   4334   5728    202    110    403  B    C  
ATOM    460  C   LYS B 484     -18.531 -18.920 -20.944  1.00 43.12      B    C  
ANISOU  460  C   LYS B 484     5932   4434   6016    152      7    285  B    C  
ATOM    461  O   LYS B 484     -17.710 -19.402 -21.725  1.00 43.36      B    O  
ANISOU  461  O   LYS B 484     6090   4407   5979    218     -7    238  B    O  
ATOM    462  CB  LYS B 484     -17.521 -16.888 -19.867  1.00 41.40      B    C  
ANISOU  462  CB  LYS B 484     5616   4495   5618    265     71    376  B    C  
ATOM    463  CG  LYS B 484     -18.515 -15.935 -20.499  1.00 42.65      B    C  
ANISOU  463  CG  LYS B 484     5703   4693   5811    214    -27    300  B    C  
ATOM    464  CD  LYS B 484     -19.658 -15.639 -19.553  1.00 44.25      B    C  
ANISOU  464  CD  LYS B 484     5759   4922   6131    146     18    325  B    C  
ATOM    465  CE  LYS B 484     -20.569 -14.631 -20.185  1.00 46.79      B    C  
ANISOU  465  CE  LYS B 484     5987   5277   6514    131   -105    243  B    C  
ATOM    466  NZ  LYS B 484     -21.949 -14.736 -19.662  1.00 48.60      B    N1+
ANISOU  466  NZ  LYS B 484     6036   5479   6949     47    -78    219  B    N1+
ATOM    467  N   ASN B 485     -19.843 -18.932 -21.185  1.00 44.42      B    N  
ANISOU  467  N   ASN B 485     6005   4553   6321     38    -67    224  B    N  
ATOM    468  CA  ASN B 485     -20.375 -19.452 -22.438  1.00 46.02      B    C  
ANISOU  468  CA  ASN B 485     6270   4638   6579    -16   -220     91  B    C  
ATOM    469  C   ASN B 485     -20.069 -18.454 -23.575  1.00 45.04      B    C  
ANISOU  469  C   ASN B 485     6228   4597   6289     57   -354     12  B    C  
ATOM    470  O   ASN B 485     -20.585 -17.337 -23.553  1.00 45.70      B    O  
ANISOU  470  O   ASN B 485     6211   4781   6372     60   -425     10  B    O  
ATOM    471  CB  ASN B 485     -21.895 -19.695 -22.326  1.00 49.88      B    C  
ANISOU  471  CB  ASN B 485     6587   5057   7308   -163   -291     36  B    C  
ATOM    472  CG  ASN B 485     -22.590 -19.931 -23.657  1.00 57.39      B    C  
ANISOU  472  CG  ASN B 485     7572   5915   8317   -217   -531   -129  B    C  
ATOM    473  ND2 ASN B 485     -22.590 -21.167 -24.130  1.00 58.21      B    N  
ANISOU  473  ND2 ASN B 485     7793   5842   8482   -277   -565   -199  B    N  
ATOM    474  OD1 ASN B 485     -23.107 -18.992 -24.288  1.00 61.10      B    O  
ANISOU  474  OD1 ASN B 485     7989   6461   8767   -193   -707   -199  B    O  
ATOM    475  N   CYS B 486     -19.235 -18.845 -24.545  1.00 43.31      B    N  
ANISOU  475  N   CYS B 486     6207   4323   5926    121   -368    -49  B    N  
ATOM    476  CA  CYS B 486     -18.961 -17.997 -25.711  1.00 43.13      B    C  
ANISOU  476  CA  CYS B 486     6324   4351   5714    176   -465   -116  B    C  
ATOM    477  C   CYS B 486     -19.620 -18.592 -26.967  1.00 42.27      B    C  
ANISOU  477  C   CYS B 486     6373   4111   5577    133   -661   -265  B    C  
ATOM    478  O   CYS B 486     -19.729 -19.815 -27.079  1.00 42.09      B    O  
ANISOU  478  O   CYS B 486     6405   3946   5641     88   -663   -328  B    O  
ATOM    479  CB  CYS B 486     -17.463 -17.780 -25.915  1.00 43.85      B    C  
ANISOU  479  CB  CYS B 486     6533   4495   5632    281   -299    -81  B    C  
ATOM    480  SG  CYS B 486     -16.644 -16.941 -24.538  1.00 48.14      B    S  
ANISOU  480  SG  CYS B 486     6895   5195   6199    330   -140     62  B    S  
ATOM    481  N   VAL B 487     -20.057 -17.734 -27.900  1.00 41.79      B    N  
ANISOU  481  N   VAL B 487     6407   4081   5389    149   -845   -322  B    N  
ATOM    482  CA  VAL B 487     -20.696 -18.184 -29.136  1.00 43.13      B    C  
ANISOU  482  CA  VAL B 487     6763   4134   5490    120  -1087   -473  B    C  
ATOM    483  C   VAL B 487     -19.755 -17.877 -30.299  1.00 42.12      B    C  
ANISOU  483  C   VAL B 487     6974   4004   5027    211  -1046   -510  B    C  
ATOM    484  O   VAL B 487     -19.323 -16.732 -30.438  1.00 41.56      B    O  
ANISOU  484  O   VAL B 487     6955   4032   4802    270   -992   -430  B    O  
ATOM    485  CB  VAL B 487     -22.057 -17.477 -29.385  1.00 46.07      B    C  
ANISOU  485  CB  VAL B 487     7008   4523   5972     82  -1387   -520  B    C  
ATOM    486  CG1 VAL B 487     -22.830 -18.162 -30.508  1.00 46.92      B    C  
ANISOU  486  CG1 VAL B 487     7269   4493   6067     35  -1691   -697  B    C  
ATOM    487  CG2 VAL B 487     -22.901 -17.371 -28.114  1.00 47.51      B    C  
ANISOU  487  CG2 VAL B 487     6818   4752   6480      8  -1345   -459  B    C  
ATOM    488  N   LEU B 488     -19.446 -18.866 -31.133  1.00 41.75      B    N  
ANISOU  488  N   LEU B 488     7168   3831   4864    218  -1049   -634  B    N  
ATOM    489  CA  LEU B 488     -18.611 -18.645 -32.314  1.00 42.40      B    C  
ANISOU  489  CA  LEU B 488     7608   3897   4606    299   -976   -687  B    C  
ATOM    490  C   LEU B 488     -19.427 -17.806 -33.301  1.00 44.27      B    C  
ANISOU  490  C   LEU B 488     8038   4134   4651    304  -1280   -732  B    C  
ATOM    491  O   LEU B 488     -20.607 -18.074 -33.497  1.00 44.25      B    O  
ANISOU  491  O   LEU B 488     7978   4065   4768    245  -1598   -825  B    O  
ATOM    492  CB  LEU B 488     -18.232 -19.988 -32.958  1.00 42.03      B    C  
ANISOU  492  CB  LEU B 488     7784   3693   4492    308   -921   -840  B    C  
ATOM    493  CG  LEU B 488     -17.288 -19.945 -34.155  1.00 43.10      B    C  
ANISOU  493  CG  LEU B 488     8307   3797   4272    396   -767   -916  B    C  
ATOM    494  CD1 LEU B 488     -15.982 -19.214 -33.815  1.00 43.58      B    C  
ANISOU  494  CD1 LEU B 488     8305   3984   4268    471   -413   -782  B    C  
ATOM    495  CD2 LEU B 488     -17.004 -21.364 -34.669  1.00 44.36      B    C  
ANISOU  495  CD2 LEU B 488     8663   3780   4411    413   -710  -1090  B    C  
ATOM    496  N   GLN B 489     -18.825 -16.763 -33.863  1.00 45.41      B    N  
ANISOU  496  N   GLN B 489     8388   4342   4523    371  -1191   -659  B    N  
ATOM    497  CA  GLN B 489     -19.495 -15.858 -34.802  1.00 46.90      B    C  
ANISOU  497  CA  GLN B 489     8815   4517   4487    402  -1476   -667  B    C  
ATOM    498  C   GLN B 489     -19.101 -16.160 -36.240  1.00 48.98      B    C  
ANISOU  498  C   GLN B 489     9580   4683   4347    447  -1492   -776  B    C  
ATOM    499  O   GLN B 489     -18.113 -16.849 -36.481  1.00 48.20      B    O  
ANISOU  499  O   GLN B 489     9626   4550   4139    465  -1198   -827  B    O  
ATOM    500  CB  GLN B 489     -19.136 -14.379 -34.480  1.00 48.11      B    C  
ANISOU  500  CB  GLN B 489     8919   4778   4584    442  -1363   -491  B    C  
ATOM    501  CG  GLN B 489     -19.398 -13.977 -33.044  1.00 50.14      B    C  
ANISOU  501  CG  GLN B 489     8726   5135   5189    411  -1305   -389  B    C  
ATOM    502  CD  GLN B 489     -20.859 -14.068 -32.701  1.00 51.87      B    C  
ANISOU  502  CD  GLN B 489     8706   5336   5667    377  -1641   -445  B    C  
ATOM    503  NE2 GLN B 489     -21.185 -14.786 -31.640  1.00 49.61      B    N  
ANISOU  503  NE2 GLN B 489     8085   5067   5696    308  -1575   -457  B    N  
ATOM    504  OE1 GLN B 489     -21.706 -13.487 -33.375  1.00 53.38      B    O  
ANISOU  504  OE1 GLN B 489     9007   5489   5785    415  -1959   -475  B    O  
ATOM    505  N   ARG B 490     -19.831 -15.559 -37.201  1.00 51.26      B    N  
ANISOU  505  N   ARG B 490    10154   4926   4396    483  -1825   -805  B    N  
ATOM    506  CA  ARG B 490     -19.578 -15.687 -38.640  1.00 53.79      B    C  
ANISOU  506  CA  ARG B 490    11033   5149   4256    535  -1883   -900  B    C  
ATOM    507  C   ARG B 490     -18.117 -15.347 -39.034  1.00 54.29      B    C  
ANISOU  507  C   ARG B 490    11368   5238   4023    574  -1400   -817  B    C  
ATOM    508  O   ARG B 490     -17.593 -15.936 -39.974  1.00 54.90      B    O  
ANISOU  508  O   ARG B 490    11835   5233   3790    601  -1269   -933  B    O  
ATOM    509  CB  ARG B 490     -20.566 -14.783 -39.420  1.00 56.48      B    C  
ANISOU  509  CB  ARG B 490    11613   5453   4392    589  -2333   -882  B    C  
ATOM    510  CG  ARG B 490     -20.561 -13.347 -38.891  1.00 61.72      B    C  
ANISOU  510  CG  ARG B 490    12124   6204   5121    625  -2285   -668  B    C  
ATOM    511  CD  ARG B 490     -21.560 -12.450 -39.575  1.00 67.70      B    C  
ANISOU  511  CD  ARG B 490    13087   6908   5728    705  -2753   -639  B    C  
ATOM    512  NE  ARG B 490     -22.929 -12.663 -39.108  1.00 72.43      B    N  
ANISOU  512  NE  ARG B 490    13301   7508   6713    693  -3190   -731  B    N  
ATOM    513  CZ  ARG B 490     -23.880 -13.269 -39.812  1.00 75.68      B    C  
ANISOU  513  CZ  ARG B 490    13827   7830   7097    700  -3649   -909  B    C  
ATOM    514  NH1 ARG B 490     -23.618 -13.752 -41.022  1.00 75.59      B    N1+
ANISOU  514  NH1 ARG B 490    14353   7721   6649    728  -3747  -1019  B    N1+
ATOM    515  NH2 ARG B 490     -25.101 -13.399 -39.313  1.00 76.55      B    N  
ANISOU  515  NH2 ARG B 490    13515   7945   7625    675  -4010   -991  B    N  
ATOM    516  N   ASP B 491     -17.471 -14.389 -38.338  1.00 53.67      B    N  
ANISOU  516  N   ASP B 491    11082   5264   4045    570  -1129   -633  B    N  
ATOM    517  CA  ASP B 491     -16.090 -14.009 -38.661  1.00 53.45      B    C  
ANISOU  517  CA  ASP B 491    11245   5259   3804    584   -657   -558  B    C  
ATOM    518  C   ASP B 491     -15.003 -14.933 -38.048  1.00 52.69      B    C  
ANISOU  518  C   ASP B 491    10902   5197   3920    575   -258   -611  B    C  
ATOM    519  O   ASP B 491     -13.814 -14.699 -38.261  1.00 53.60      B    O  
ANISOU  519  O   ASP B 491    11100   5336   3930    585    152   -569  B    O  
ATOM    520  CB  ASP B 491     -15.837 -12.548 -38.245  1.00 54.66      B    C  
ANISOU  520  CB  ASP B 491    11299   5484   3986    571   -555   -352  B    C  
ATOM    521  CG  ASP B 491     -16.120 -12.259 -36.777  1.00 57.73      B    C  
ANISOU  521  CG  ASP B 491    11138   5977   4818    537   -600   -272  B    C  
ATOM    522  OD1 ASP B 491     -16.403 -13.219 -36.019  1.00 56.43      B    O  
ANISOU  522  OD1 ASP B 491    10662   5838   4941    518   -658   -353  B    O  
ATOM    523  OD2 ASP B 491     -16.088 -11.070 -36.391  1.00 60.48      B    O1-
ANISOU  523  OD2 ASP B 491    11398   6367   5215    528   -577   -128  B    O1-
ATOM    524  N   GLY B 492     -15.405 -15.941 -37.278  1.00 50.62      B    N  
ANISOU  524  N   GLY B 492    10332   4928   3973    558   -376   -694  B    N  
ATOM    525  CA  GLY B 492     -14.444 -16.847 -36.656  1.00 48.81      B    C  
ANISOU  525  CA  GLY B 492     9878   4710   3959    575    -55   -734  B    C  
ATOM    526  C   GLY B 492     -14.004 -16.431 -35.265  1.00 46.27      B    C  
ANISOU  526  C   GLY B 492     9091   4512   3977    556     89   -590  B    C  
ATOM    527  O   GLY B 492     -13.209 -17.128 -34.642  1.00 45.98      B    O  
ANISOU  527  O   GLY B 492     8845   4488   4139    587    314   -605  B    O  
ATOM    528  N   PHE B 493     -14.512 -15.297 -34.763  1.00 43.88      B    N  
ANISOU  528  N   PHE B 493     8640   4293   3741    519    -54   -457  B    N  
ATOM    529  CA  PHE B 493     -14.218 -14.841 -33.415  1.00 42.95      B    C  
ANISOU  529  CA  PHE B 493     8113   4289   3918    498     39   -336  B    C  
ATOM    530  C   PHE B 493     -15.284 -15.398 -32.477  1.00 41.19      B    C  
ANISOU  530  C   PHE B 493     7615   4066   3969    465   -216   -348  B    C  
ATOM    531  O   PHE B 493     -16.423 -15.597 -32.892  1.00 41.22      B    O  
ANISOU  531  O   PHE B 493     7708   4005   3948    441   -514   -415  B    O  
ATOM    532  CB  PHE B 493     -14.254 -13.288 -33.324  1.00 43.52      B    C  
ANISOU  532  CB  PHE B 493     8179   4428   3927    473     28   -199  B    C  
ATOM    533  CG  PHE B 493     -13.027 -12.539 -33.809  1.00 45.21      B    C  
ANISOU  533  CG  PHE B 493     8537   4661   3980    467    365   -138  B    C  
ATOM    534  CD1 PHE B 493     -12.643 -12.588 -35.137  1.00 47.19      B    C  
ANISOU  534  CD1 PHE B 493     9202   4829   3898    484    501   -187  B    C  
ATOM    535  CD2 PHE B 493     -12.268 -11.775 -32.935  1.00 46.20      B    C  
ANISOU  535  CD2 PHE B 493     8391   4876   4288    434    552    -40  B    C  
ATOM    536  CE1 PHE B 493     -11.533 -11.871 -35.589  1.00 48.12      B    C  
ANISOU  536  CE1 PHE B 493     9447   4952   3883    457    859   -124  B    C  
ATOM    537  CE2 PHE B 493     -11.154 -11.074 -33.386  1.00 46.87      B    C  
ANISOU  537  CE2 PHE B 493     8575   4963   4270    402    873      9  B    C  
ATOM    538  CZ  PHE B 493     -10.779 -11.150 -34.699  1.00 47.54      B    C  
ANISOU  538  CZ  PHE B 493     9052   4965   4046    409   1049    -29  B    C  
ATOM    539  N   TYR B 494     -14.941 -15.590 -31.202  1.00 39.26      B    N  
ANISOU  539  N   TYR B 494     7038   3892   3988    460   -106   -280  B    N  
ATOM    540  CA  TYR B 494     -15.920 -15.947 -30.189  1.00 39.16      B    C  
ANISOU  540  CA  TYR B 494     6767   3886   4224    415   -285   -261  B    C  
ATOM    541  C   TYR B 494     -16.462 -14.646 -29.563  1.00 38.97      B    C  
ANISOU  541  C   TYR B 494     6579   3961   4265    391   -381   -157  B    C  
ATOM    542  O   TYR B 494     -15.697 -13.706 -29.348  1.00 38.23      B    O  
ANISOU  542  O   TYR B 494     6459   3945   4121    408   -232    -77  B    O  
ATOM    543  CB  TYR B 494     -15.274 -16.783 -29.068  1.00 39.43      B    C  
ANISOU  543  CB  TYR B 494     6577   3934   4468    434   -117   -223  B    C  
ATOM    544  CG  TYR B 494     -15.179 -18.232 -29.451  1.00 41.15      B    C  
ANISOU  544  CG  TYR B 494     6909   4014   4713    453    -98   -330  B    C  
ATOM    545  CD1 TYR B 494     -16.300 -19.049 -29.431  1.00 42.49      B    C  
ANISOU  545  CD1 TYR B 494     7074   4074   4997    384   -297   -398  B    C  
ATOM    546  CD2 TYR B 494     -14.008 -18.753 -29.977  1.00 43.27      B    C  
ANISOU  546  CD2 TYR B 494     7305   4239   4896    535    120   -387  B    C  
ATOM    547  CE1 TYR B 494     -16.238 -20.374 -29.855  1.00 44.06      B    C  
ANISOU  547  CE1 TYR B 494     7408   4112   5220    391   -290   -512  B    C  
ATOM    548  CE2 TYR B 494     -13.929 -20.075 -30.392  1.00 44.98      B    C  
ANISOU  548  CE2 TYR B 494     7655   4302   5133    567    139   -504  B    C  
ATOM    549  CZ  TYR B 494     -15.048 -20.882 -30.335  1.00 46.38      B    C  
ANISOU  549  CZ  TYR B 494     7849   4358   5414    492    -75   -566  B    C  
ATOM    550  OH  TYR B 494     -14.955 -22.187 -30.766  1.00 50.44      B    O  
ANISOU  550  OH  TYR B 494     8516   4693   5956    515    -58   -693  B    O  
ATOM    551  N   GLU B 495     -17.763 -14.599 -29.254  1.00 38.83      B    N  
ANISOU  551  N   GLU B 495     6435   3931   4388    350   -618   -172  B    N  
ATOM    552  CA  GLU B 495     -18.333 -13.459 -28.526  1.00 38.98      B    C  
ANISOU  552  CA  GLU B 495     6266   4033   4513    344   -690    -92  B    C  
ATOM    553  C   GLU B 495     -19.044 -13.992 -27.306  1.00 37.87      B    C  
ANISOU  553  C   GLU B 495     5834   3912   4642    295   -701    -81  B    C  
ATOM    554  O   GLU B 495     -19.836 -14.924 -27.395  1.00 37.45      B    O  
ANISOU  554  O   GLU B 495     5736   3780   4712    244   -818   -154  B    O  
ATOM    555  CB  GLU B 495     -19.240 -12.567 -29.368  1.00 42.58      B    C  
ANISOU  555  CB  GLU B 495     6850   4456   4875    367   -949   -113  B    C  
ATOM    556  CG  GLU B 495     -18.446 -11.544 -30.161  1.00 52.07      B    C  
ANISOU  556  CG  GLU B 495     8316   5658   5811    411   -865    -53  B    C  
ATOM    557  CD  GLU B 495     -19.284 -10.626 -31.020  1.00 61.86      B    C  
ANISOU  557  CD  GLU B 495     9741   6841   6924    456  -1139    -49  B    C  
ATOM    558  OE1 GLU B 495     -20.454 -10.382 -30.646  1.00 63.53      B    O  
ANISOU  558  OE1 GLU B 495     9758   7052   7330    468  -1377    -72  B    O  
ATOM    559  OE2 GLU B 495     -18.780 -10.160 -32.070  1.00 65.51      B    O1-
ANISOU  559  OE2 GLU B 495    10544   7249   7096    486  -1112    -22  B    O1-
ATOM    560  N   CYS B 496     -18.710 -13.421 -26.162  1.00 37.26      B    N  
ANISOU  560  N   CYS B 496     5577   3931   4648    302   -563      8  B    N  
ATOM    561  CA  CYS B 496     -19.176 -13.780 -24.835  1.00 37.76      B    C  
ANISOU  561  CA  CYS B 496     5404   4028   4914    263   -501     47  B    C  
ATOM    562  C   CYS B 496     -19.973 -12.546 -24.298  1.00 38.00      B    C  
ANISOU  562  C   CYS B 496     5284   4126   5029    270   -569     71  B    C  
ATOM    563  O   CYS B 496     -19.452 -11.436 -24.310  1.00 39.18      B    O  
ANISOU  563  O   CYS B 496     5480   4328   5078    315   -537    111  B    O  
ATOM    564  CB  CYS B 496     -17.936 -14.091 -23.993  1.00 40.07      B    C  
ANISOU  564  CB  CYS B 496     5673   4373   5178    293   -290    121  B    C  
ATOM    565  SG  CYS B 496     -16.604 -14.938 -24.955  1.00 51.85      B    S  
ANISOU  565  SG  CYS B 496     7368   5802   6529    344   -186     82  B    S  
ATOM    566  N   VAL B 497     -21.237 -12.721 -23.912  1.00 36.14      B    N  
ANISOU  566  N   VAL B 497     4868   3868   4994    226   -656     34  B    N  
ATOM    567  CA  VAL B 497     -22.073 -11.617 -23.444  1.00 35.67      B    C  
ANISOU  567  CA  VAL B 497     4647   3858   5050    252   -712     32  B    C  
ATOM    568  C   VAL B 497     -22.332 -11.736 -21.936  1.00 34.47      B    C  
ANISOU  568  C   VAL B 497     4296   3764   5037    216   -517     75  B    C  
ATOM    569  O   VAL B 497     -22.773 -12.777 -21.464  1.00 33.50      B    O  
ANISOU  569  O   VAL B 497     4080   3602   5045    139   -443     72  B    O  
ATOM    570  CB  VAL B 497     -23.399 -11.568 -24.240  1.00 37.45      B    C  
ANISOU  570  CB  VAL B 497     4793   4014   5424    248   -975    -65  B    C  
ATOM    571  CG1 VAL B 497     -24.314 -10.445 -23.749  1.00 37.99      B    C  
ANISOU  571  CG1 VAL B 497     4658   4118   5659    301  -1031    -80  B    C  
ATOM    572  CG2 VAL B 497     -23.146 -11.442 -25.743  1.00 38.24      B    C  
ANISOU  572  CG2 VAL B 497     5160   4048   5322    294  -1187   -103  B    C  
ATOM    573  N   PHE B 498     -22.032 -10.686 -21.181  1.00 33.62      B    N  
ANISOU  573  N   PHE B 498     4154   3736   4883    266   -423    114  B    N  
ATOM    574  CA  PHE B 498     -22.316 -10.651 -19.749  1.00 34.02      B    C  
ANISOU  574  CA  PHE B 498     4064   3844   5017    245   -238    144  B    C  
ATOM    575  C   PHE B 498     -23.577  -9.794 -19.640  1.00 34.65      B    C  
ANISOU  575  C   PHE B 498     3957   3923   5285    273   -299     74  B    C  
ATOM    576  O   PHE B 498     -23.533  -8.628 -20.000  1.00 34.27      B    O  
ANISOU  576  O   PHE B 498     3944   3881   5196    353   -398     55  B    O  
ATOM    577  CB  PHE B 498     -21.162  -9.980 -18.960  1.00 33.00      B    C  
ANISOU  577  CB  PHE B 498     4029   3798   4714    290   -118    202  B    C  
ATOM    578  CG  PHE B 498     -19.905 -10.812 -18.956  1.00 33.24      B    C  
ANISOU  578  CG  PHE B 498     4191   3833   4607    284    -62    262  B    C  
ATOM    579  CD1 PHE B 498     -18.949 -10.654 -19.939  1.00 34.24      B    C  
ANISOU  579  CD1 PHE B 498     4446   3945   4618    312   -126    261  B    C  
ATOM    580  CD2 PHE B 498     -19.697 -11.777 -17.982  1.00 33.39      B    C  
ANISOU  580  CD2 PHE B 498     4212   3857   4620    257     65    322  B    C  
ATOM    581  CE1 PHE B 498     -17.801 -11.442 -19.945  1.00 35.00      B    C  
ANISOU  581  CE1 PHE B 498     4623   4041   4633    322    -62    298  B    C  
ATOM    582  CE2 PHE B 498     -18.538 -12.540 -17.973  1.00 34.04      B    C  
ANISOU  582  CE2 PHE B 498     4399   3930   4604    281     90    374  B    C  
ATOM    583  CZ  PHE B 498     -17.595 -12.366 -18.952  1.00 33.99      B    C  
ANISOU  583  CZ  PHE B 498     4473   3919   4522    318     27    352  B    C  
ATOM    584  N   GLN B 499     -24.685 -10.367 -19.208  1.00 35.29      B    N  
ANISOU  584  N   GLN B 499     3837   3980   5592    210   -240     35  B    N  
ATOM    585  CA  GLN B 499     -25.942  -9.647 -19.094  1.00 36.49      B    C  
ANISOU  585  CA  GLN B 499     3753   4127   5986    245   -285    -50  B    C  
ATOM    586  C   GLN B 499     -26.799 -10.320 -18.030  1.00 37.18      B    C  
ANISOU  586  C   GLN B 499     3628   4217   6282    150    -45    -61  B    C  
ATOM    587  O   GLN B 499     -27.052 -11.496 -18.155  1.00 37.32      B    O  
ANISOU  587  O   GLN B 499     3609   4175   6396     37    -20    -54  B    O  
ATOM    588  CB  GLN B 499     -26.711  -9.692 -20.425  1.00 39.31      B    C  
ANISOU  588  CB  GLN B 499     4039   4405   6490    262   -596   -135  B    C  
ATOM    589  CG  GLN B 499     -27.986  -8.864 -20.367  1.00 44.89      B    C  
ANISOU  589  CG  GLN B 499     4472   5102   7484    333   -687   -232  B    C  
ATOM    590  CD  GLN B 499     -28.769  -8.930 -21.642  1.00 53.51      B    C  
ANISOU  590  CD  GLN B 499     5492   6113   8727    364  -1049   -321  B    C  
ATOM    591  NE2 GLN B 499     -30.074  -8.788 -21.520  1.00 56.05      B    N  
ANISOU  591  NE2 GLN B 499     5474   6411   9410    377  -1121   -428  B    N  
ATOM    592  OE1 GLN B 499     -28.224  -9.120 -22.737  1.00 56.34      B    O  
ANISOU  592  OE1 GLN B 499     6096   6426   8882    380  -1267   -304  B    O  
ATOM    593  N   PRO B 500     -27.324  -9.597 -17.028  1.00 37.10      B    N  
ANISOU  593  N   PRO B 500     3479   4257   6359    187    145    -89  B    N  
ATOM    594  CA  PRO B 500     -27.056  -8.183 -16.725  1.00 36.38      B    C  
ANISOU  594  CA  PRO B 500     3438   4215   6167    318    143   -112  B    C  
ATOM    595  C   PRO B 500     -25.611  -7.941 -16.276  1.00 35.70      B    C  
ANISOU  595  C   PRO B 500     3636   4185   5742    340    209    -23  B    C  
ATOM    596  O   PRO B 500     -24.839  -8.892 -16.051  1.00 36.57      B    O  
ANISOU  596  O   PRO B 500     3887   4307   5701    271    279     61  B    O  
ATOM    597  CB  PRO B 500     -28.117  -7.850 -15.665  1.00 37.60      B    C  
ANISOU  597  CB  PRO B 500     3356   4393   6536    323    390   -183  B    C  
ATOM    598  CG  PRO B 500     -28.368  -9.137 -14.960  1.00 38.70      B    C  
ANISOU  598  CG  PRO B 500     3454   4525   6723    172    638   -128  B    C  
ATOM    599  CD  PRO B 500     -28.176 -10.231 -15.996  1.00 37.04      B    C  
ANISOU  599  CD  PRO B 500     3284   4246   6544     84    434    -96  B    C  
ATOM    600  N   ILE B 501     -25.199  -6.683 -16.242  1.00 34.61      B    N  
ANISOU  600  N   ILE B 501     3579   4066   5506    440    155    -48  B    N  
ATOM    601  CA  ILE B 501     -23.822  -6.340 -15.892  1.00 34.14      B    C  
ANISOU  601  CA  ILE B 501     3748   4051   5172    452    182     12  B    C  
ATOM    602  C   ILE B 501     -23.725  -5.713 -14.523  1.00 33.03      B    C  
ANISOU  602  C   ILE B 501     3638   3966   4944    481    379    -17  B    C  
ATOM    603  O   ILE B 501     -24.719  -5.199 -14.001  1.00 33.60      B    O  
ANISOU  603  O   ILE B 501     3568   4033   5164    524    489    -97  B    O  
ATOM    604  CB  ILE B 501     -23.218  -5.363 -16.955  1.00 36.48      B    C  
ANISOU  604  CB  ILE B 501     4165   4302   5394    516    -29      8  B    C  
ATOM    605  CG1 ILE B 501     -24.121  -4.162 -17.198  1.00 37.99      B    C  
ANISOU  605  CG1 ILE B 501     4257   4433   5744    618   -120    -73  B    C  
ATOM    606  CG2 ILE B 501     -22.919  -6.098 -18.194  1.00 39.14      B    C  
ANISOU  606  CG2 ILE B 501     4575   4597   5702    480   -187     50  B    C  
ATOM    607  CD1 ILE B 501     -23.525  -3.125 -18.051  1.00 40.58      B    C  
ANISOU  607  CD1 ILE B 501     4750   4692   5978    676   -286    -55  B    C  
ATOM    608  N   PHE B 502     -22.507  -5.698 -13.964  1.00 31.49      B    N  
ANISOU  608  N   PHE B 502     3628   3822   4513    469    409     33  B    N  
ATOM    609  CA  PHE B 502     -22.197  -4.976 -12.751  1.00 31.10      B    C  
ANISOU  609  CA  PHE B 502     3669   3820   4326    504    532     -9  B    C  
ATOM    610  C   PHE B 502     -21.239  -3.875 -13.252  1.00 29.66      B    C  
ANISOU  610  C   PHE B 502     3590   3614   4065    539    368    -36  B    C  
ATOM    611  O   PHE B 502     -20.046  -4.119 -13.412  1.00 29.48      B    O  
ANISOU  611  O   PHE B 502     3674   3616   3911    505    292     18  B    O  
ATOM    612  CB  PHE B 502     -21.541  -5.915 -11.718  1.00 31.28      B    C  
ANISOU  612  CB  PHE B 502     3830   3906   4147    457    651     69  B    C  
ATOM    613  CG  PHE B 502     -22.517  -6.874 -11.070  1.00 32.80      B    C  
ANISOU  613  CG  PHE B 502     3960   4097   4403    406    869    105  B    C  
ATOM    614  CD1 PHE B 502     -23.281  -6.482  -9.980  1.00 32.85      B    C  
ANISOU  614  CD1 PHE B 502     3961   4126   4395    424   1100     44  B    C  
ATOM    615  CD2 PHE B 502     -22.703  -8.156 -11.580  1.00 33.70      B    C  
ANISOU  615  CD2 PHE B 502     4027   4172   4606    332    865    190  B    C  
ATOM    616  CE1 PHE B 502     -24.175  -7.361  -9.385  1.00 34.11      B    C  
ANISOU  616  CE1 PHE B 502     4065   4273   4623    356   1351     85  B    C  
ATOM    617  CE2 PHE B 502     -23.620  -9.031 -10.993  1.00 34.70      B    C  
ANISOU  617  CE2 PHE B 502     4093   4271   4820    258   1088    227  B    C  
ATOM    618  CZ  PHE B 502     -24.332  -8.634  -9.882  1.00 34.33      B    C  
ANISOU  618  CZ  PHE B 502     4040   4252   4753    264   1343    183  B    C  
ATOM    619  N   LEU B 503     -21.759  -2.672 -13.524  1.00 29.01      B    N  
ANISOU  619  N   LEU B 503     3465   3467   4091    608    319   -119  B    N  
ATOM    620  CA  LEU B 503     -20.956  -1.581 -14.099  1.00 29.28      B    C  
ANISOU  620  CA  LEU B 503     3606   3437   4080    625    179   -135  B    C  
ATOM    621  C   LEU B 503     -19.642  -1.286 -13.423  1.00 29.38      B    C  
ANISOU  621  C   LEU B 503     3759   3493   3912    580    182   -141  B    C  
ATOM    622  O   LEU B 503     -18.682  -0.975 -14.109  1.00 29.88      B    O  
ANISOU  622  O   LEU B 503     3889   3522   3942    539     80   -108  B    O  
ATOM    623  CB  LEU B 503     -21.754  -0.270 -14.174  1.00 29.66      B    C  
ANISOU  623  CB  LEU B 503     3618   3387   4266    723    152   -230  B    C  
ATOM    624  CG  LEU B 503     -22.873  -0.221 -15.188  1.00 31.63      B    C  
ANISOU  624  CG  LEU B 503     3734   3559   4726    792     41   -230  B    C  
ATOM    625  CD1 LEU B 503     -23.874   0.881 -14.824  1.00 31.93      B    C  
ANISOU  625  CD1 LEU B 503     3680   3516   4936    920     69   -347  B    C  
ATOM    626  CD2 LEU B 503     -22.309   0.017 -16.575  1.00 32.71      B    C  
ANISOU  626  CD2 LEU B 503     3991   3614   4824    780   -161   -151  B    C  
ATOM    627  N   LEU B 504     -19.612  -1.293 -12.094  1.00 28.65      B    N  
ANISOU  627  N   LEU B 504     3715   3464   3707    588    298   -194  B    N  
ATOM    628  CA  LEU B 504     -18.425  -0.907 -11.352  1.00 29.26      B    C  
ANISOU  628  CA  LEU B 504     3921   3577   3618    556    253   -231  B    C  
ATOM    629  C   LEU B 504     -17.651  -2.070 -10.734  1.00 29.32      B    C  
ANISOU  629  C   LEU B 504     3986   3687   3468    518    255   -155  B    C  
ATOM    630  O   LEU B 504     -16.782  -1.837  -9.891  1.00 29.55      B    O  
ANISOU  630  O   LEU B 504     4118   3758   3350    508    199   -199  B    O  
ATOM    631  CB  LEU B 504     -18.790   0.130 -10.282  1.00 29.75      B    C  
ANISOU  631  CB  LEU B 504     4063   3617   3626    607    330   -371  B    C  
ATOM    632  CG  LEU B 504     -19.201   1.504 -10.834  1.00 32.52      B    C  
ANISOU  632  CG  LEU B 504     4397   3830   4127    655    283   -458  B    C  
ATOM    633  CD1 LEU B 504     -19.615   2.419  -9.711  1.00 33.89      B    C  
ANISOU  633  CD1 LEU B 504     4657   3973   4247    719    384   -616  B    C  
ATOM    634  CD2 LEU B 504     -18.054   2.151 -11.647  1.00 32.83      B    C  
ANISOU  634  CD2 LEU B 504     4491   3793   4189    583    121   -435  B    C  
ATOM    635  N   SER B 505     -17.930  -3.294 -11.175  1.00 28.74      B    N  
ANISOU  635  N   SER B 505     3850   3636   3431    502    289    -49  B    N  
ATOM    636  CA  SER B 505     -17.227  -4.478 -10.714  1.00 29.53      B    C  
ANISOU  636  CA  SER B 505     4012   3801   3406    485    279     41  B    C  
ATOM    637  C   SER B 505     -16.090  -4.754 -11.706  1.00 29.35      B    C  
ANISOU  637  C   SER B 505     3948   3769   3435    455    140     90  B    C  
ATOM    638  O   SER B 505     -16.284  -4.580 -12.894  1.00 29.84      B    O  
ANISOU  638  O   SER B 505     3942   3775   3622    437    113    100  B    O  
ATOM    639  CB  SER B 505     -18.166  -5.683 -10.708  1.00 29.45      B    C  
ANISOU  639  CB  SER B 505     3964   3787   3440    474    411    126  B    C  
ATOM    640  OG  SER B 505     -19.055  -5.649  -9.604  1.00 29.68      B    O  
ANISOU  640  OG  SER B 505     4045   3835   3399    489    594     97  B    O  
ATOM    641  N   GLY B 506     -14.944  -5.220 -11.226  1.00 29.04      B    N  
ANISOU  641  N   GLY B 506     3954   3781   3299    459     56    118  B    N  
ATOM    642  CA  GLY B 506     -13.841  -5.556 -12.125  1.00 28.66      B    C  
ANISOU  642  CA  GLY B 506     3834   3726   3329    439    -36    152  B    C  
ATOM    643  C   GLY B 506     -14.021  -6.979 -12.631  1.00 28.94      B    C  
ANISOU  643  C   GLY B 506     3855   3746   3394    455      6    255  B    C  
ATOM    644  O   GLY B 506     -14.134  -7.907 -11.838  1.00 28.86      B    O  
ANISOU  644  O   GLY B 506     3914   3756   3296    489     29    319  B    O  
ATOM    645  N   TYR B 507     -14.080  -7.161 -13.934  1.00 28.86      B    N  
ANISOU  645  N   TYR B 507     3788   3683   3492    431     18    271  B    N  
ATOM    646  CA  TYR B 507     -14.170  -8.497 -14.527  1.00 29.41      B    C  
ANISOU  646  CA  TYR B 507     3857   3717   3599    443     45    343  B    C  
ATOM    647  C   TYR B 507     -12.786  -8.922 -15.000  1.00 30.02      B    C  
ANISOU  647  C   TYR B 507     3898   3802   3708    465     -3    353  B    C  
ATOM    648  O   TYR B 507     -12.272  -8.345 -15.958  1.00 30.31      B    O  
ANISOU  648  O   TYR B 507     3895   3819   3801    433      2    315  B    O  
ATOM    649  CB  TYR B 507     -15.123  -8.496 -15.713  1.00 29.31      B    C  
ANISOU  649  CB  TYR B 507     3828   3636   3672    410     70    334  B    C  
ATOM    650  CG  TYR B 507     -16.593  -8.398 -15.351  1.00 29.43      B    C  
ANISOU  650  CG  TYR B 507     3821   3634   3729    397    122    321  B    C  
ATOM    651  CD1 TYR B 507     -17.114  -7.244 -14.779  1.00 29.48      B    C  
ANISOU  651  CD1 TYR B 507     3809   3660   3731    406    140    262  B    C  
ATOM    652  CD2 TYR B 507     -17.477  -9.420 -15.673  1.00 29.81      B    C  
ANISOU  652  CD2 TYR B 507     3844   3629   3854    373    156    351  B    C  
ATOM    653  CE1 TYR B 507     -18.459  -7.145 -14.454  1.00 29.94      B    C  
ANISOU  653  CE1 TYR B 507     3807   3702   3868    406    214    235  B    C  
ATOM    654  CE2 TYR B 507     -18.842  -9.296 -15.429  1.00 30.18      B    C  
ANISOU  654  CE2 TYR B 507     3813   3656   3998    350    213    323  B    C  
ATOM    655  CZ  TYR B 507     -19.325  -8.164 -14.806  1.00 31.01      B    C  
ANISOU  655  CZ  TYR B 507     3881   3795   4107    374    251    266  B    C  
ATOM    656  OH  TYR B 507     -20.666  -8.035 -14.549  1.00 32.73      B    O  
ANISOU  656  OH  TYR B 507     3985   3993   4458    364    330    224  B    O  
ATOM    657  N   THR B 508     -12.159  -9.916 -14.332  1.00 30.10      B    N  
ANISOU  657  N   THR B 508     3922   3828   3685    526    -40    405  B    N  
ATOM    658  CA  THR B 508     -10.848 -10.392 -14.771  1.00 30.58      B    C  
ANISOU  658  CA  THR B 508     3908   3891   3822    572    -82    401  B    C  
ATOM    659  C   THR B 508     -11.083 -11.586 -15.677  1.00 30.94      B    C  
ANISOU  659  C   THR B 508     3983   3852   3919    594    -15    442  B    C  
ATOM    660  O   THR B 508     -11.793 -12.498 -15.280  1.00 31.03      B    O  
ANISOU  660  O   THR B 508     4078   3815   3896    610      4    506  B    O  
ATOM    661  CB  THR B 508      -9.965 -10.762 -13.578  1.00 31.77      B    C  
ANISOU  661  CB  THR B 508     4052   4091   3929    655   -207    424  B    C  
ATOM    662  CG2 THR B 508      -8.617 -11.376 -14.009  1.00 31.07      B    C  
ANISOU  662  CG2 THR B 508     3837   3996   3973    730   -258    412  B    C  
ATOM    663  OG1 THR B 508      -9.764  -9.583 -12.792  1.00 32.93      B    O  
ANISOU  663  OG1 THR B 508     4187   4307   4018    623   -288    357  B    O  
ATOM    664  N   MET B 509     -10.541 -11.567 -16.898  1.00 30.40      B    N  
ANISOU  664  N   MET B 509     3871   3753   3927    583     40    398  B    N  
ATOM    665  CA  MET B 509     -10.777 -12.653 -17.835  1.00 30.71      B    C  
ANISOU  665  CA  MET B 509     3971   3702   3996    603    102    409  B    C  
ATOM    666  C   MET B 509      -9.534 -13.055 -18.593  1.00 30.87      B    C  
ANISOU  666  C   MET B 509     3926   3703   4101    659    160    368  B    C  
ATOM    667  O   MET B 509      -8.603 -12.265 -18.740  1.00 30.68      B    O  
ANISOU  667  O   MET B 509     3792   3734   4132    644    186    321  B    O  
ATOM    668  CB  MET B 509     -11.958 -12.361 -18.781  1.00 31.37      B    C  
ANISOU  668  CB  MET B 509     4140   3733   4045    526    133    385  B    C  
ATOM    669  CG  MET B 509     -11.782 -11.161 -19.646  1.00 36.06      B    C  
ANISOU  669  CG  MET B 509     4740   4343   4617    473    162    337  B    C  
ATOM    670  SD  MET B 509     -13.404 -10.604 -20.302  1.00 44.52      B    S  
ANISOU  670  SD  MET B 509     5906   5364   5644    413    108    324  B    S  
ATOM    671  CE  MET B 509     -14.299 -10.354 -18.847  1.00 41.17      B    C  
ANISOU  671  CE  MET B 509     5411   4990   5243    407     67    351  B    C  
ATOM    672  N   TRP B 510      -9.507 -14.317 -19.020  1.00 30.93      B    N  
ANISOU  672  N   TRP B 510     3992   3620   4140    722    195    376  B    N  
ATOM    673  CA  TRP B 510      -8.397 -14.910 -19.767  1.00 31.99      B    C  
ANISOU  673  CA  TRP B 510     4071   3714   4368    801    282    324  B    C  
ATOM    674  C   TRP B 510      -8.893 -16.169 -20.467  1.00 32.01      B    C  
ANISOU  674  C   TRP B 510     4217   3583   4363    835    327    314  B    C  
ATOM    675  O   TRP B 510     -10.008 -16.616 -20.214  1.00 32.17      B    O  
ANISOU  675  O   TRP B 510     4345   3544   4334    791    272    357  B    O  
ATOM    676  CB  TRP B 510      -7.202 -15.238 -18.826  1.00 32.50      B    C  
ANISOU  676  CB  TRP B 510     3975   3820   4552    921    205    339  B    C  
ATOM    677  CG  TRP B 510      -7.454 -16.351 -17.855  1.00 33.89      B    C  
ANISOU  677  CG  TRP B 510     4226   3932   4719   1019     91    428  B    C  
ATOM    678  CD1 TRP B 510      -7.047 -17.650 -17.968  1.00 35.90      B    C  
ANISOU  678  CD1 TRP B 510     4512   4071   5058   1147     95    443  B    C  
ATOM    679  CD2 TRP B 510      -8.071 -16.232 -16.566  1.00 34.47      B    C  
ANISOU  679  CD2 TRP B 510     4373   4040   4686   1005    -31    520  B    C  
ATOM    680  CE2 TRP B 510      -8.051 -17.511 -15.969  1.00 35.87      B    C  
ANISOU  680  CE2 TRP B 510     4649   4110   4871   1115    -91    608  B    C  
ATOM    681  CE3 TRP B 510      -8.662 -15.167 -15.865  1.00 34.79      B    C  
ANISOU  681  CE3 TRP B 510     4428   4175   4616    913    -77    533  B    C  
ATOM    682  NE1 TRP B 510      -7.421 -18.362 -16.843  1.00 36.52      B    N  
ANISOU  682  NE1 TRP B 510     4698   4095   5084   1205    -25    559  B    N  
ATOM    683  CZ2 TRP B 510      -8.582 -17.748 -14.702  1.00 36.50      B    C  
ANISOU  683  CZ2 TRP B 510     4860   4182   4828   1125   -179    723  B    C  
ATOM    684  CZ3 TRP B 510      -9.195 -15.409 -14.620  1.00 35.72      B    C  
ANISOU  684  CZ3 TRP B 510     4660   4294   4618    929   -154    625  B    C  
ATOM    685  CH2 TRP B 510      -9.138 -16.681 -14.043  1.00 36.20      B    C  
ANISOU  685  CH2 TRP B 510     4835   4255   4665   1030   -199    726  B    C  
ATOM    686  N   ILE B 511      -8.101 -16.704 -21.381  1.00 32.28      B    N  
ANISOU  686  N   ILE B 511     4249   3558   4456    902    444    241  B    N  
ATOM    687  CA  ILE B 511      -8.439 -17.916 -22.093  1.00 33.30      B    C  
ANISOU  687  CA  ILE B 511     4530   3541   4580    943    488    203  B    C  
ATOM    688  C   ILE B 511      -7.650 -19.068 -21.458  1.00 35.19      B    C  
ANISOU  688  C   ILE B 511     4705   3704   4961   1102    463    229  B    C  
ATOM    689  O   ILE B 511      -6.442 -18.948 -21.271  1.00 36.25      B    O  
ANISOU  689  O   ILE B 511     4665   3890   5216   1203    496    203  B    O  
ATOM    690  CB  ILE B 511      -8.091 -17.807 -23.596  1.00 33.58      B    C  
ANISOU  690  CB  ILE B 511     4660   3539   4558    930    656     89  B    C  
ATOM    691  CG1 ILE B 511      -8.703 -16.543 -24.242  1.00 33.73      B    C  
ANISOU  691  CG1 ILE B 511     4764   3626   4426    795    666     82  B    C  
ATOM    692  CG2 ILE B 511      -8.519 -19.094 -24.345  1.00 33.43      B    C  
ANISOU  692  CG2 ILE B 511     4835   3352   4516    971    680     22  B    C  
ATOM    693  CD1 ILE B 511     -10.288 -16.451 -24.103  1.00 34.29      B    C  
ANISOU  693  CD1 ILE B 511     4954   3668   4406    700    498    120  B    C  
ATOM    694  N   ARG B 512      -8.327 -20.160 -21.096  1.00 35.64      B    N  
ANISOU  694  N   ARG B 512     4892   3625   5024   1125    396    281  B    N  
ATOM    695  CA  ARG B 512      -7.656 -21.334 -20.574  1.00 37.42      B    C  
ANISOU  695  CA  ARG B 512     5110   3733   5375   1290    362    318  B    C  
ATOM    696  C   ARG B 512      -7.738 -22.443 -21.637  1.00 40.93      B    C  
ANISOU  696  C   ARG B 512     5706   3988   5857   1334    462    220  B    C  
ATOM    697  O   ARG B 512      -8.810 -22.682 -22.200  1.00 41.12      B    O  
ANISOU  697  O   ARG B 512     5895   3930   5797   1212    465    188  B    O  
ATOM    698  CB  ARG B 512      -8.290 -21.836 -19.255  1.00 37.59      B    C  
ANISOU  698  CB  ARG B 512     5212   3700   5371   1288    226    472  B    C  
ATOM    699  CG  ARG B 512      -7.722 -23.198 -18.782  1.00 40.57      B    C  
ANISOU  699  CG  ARG B 512     5653   3899   5863   1468    176    532  B    C  
ATOM    700  CD  ARG B 512      -8.089 -23.553 -17.360  1.00 43.30      B    C  
ANISOU  700  CD  ARG B 512     6098   4203   6150   1487     48    710  B    C  
ATOM    701  NE  ARG B 512      -7.592 -22.549 -16.426  1.00 46.04      B    N  
ANISOU  701  NE  ARG B 512     6315   4744   6433   1512    -65    759  B    N  
ATOM    702  CZ  ARG B 512      -7.996 -22.423 -15.166  1.00 48.84      B    C  
ANISOU  702  CZ  ARG B 512     6770   5128   6660   1493   -165    898  B    C  
ATOM    703  NH1 ARG B 512      -8.899 -23.259 -14.664  1.00 47.26      B    N1+
ANISOU  703  NH1 ARG B 512     6791   4771   6395   1442   -135   1022  B    N1+
ATOM    704  NH2 ARG B 512      -7.501 -21.459 -14.398  1.00 49.98      B    N  
ANISOU  704  NH2 ARG B 512     6809   5448   6735   1516   -282    909  B    N  
ATOM    705  N   ILE B 513      -6.604 -23.089 -21.930  1.00 43.01      B    N  
ANISOU  705  N   ILE B 513     5901   4182   6259   1510    537    153  B    N  
ATOM    706  CA  ILE B 513      -6.588 -24.244 -22.807  1.00 46.59      B    C  
ANISOU  706  CA  ILE B 513     6513   4430   6758   1584    633     49  B    C  
ATOM    707  C   ILE B 513      -6.357 -25.390 -21.842  1.00 48.75      B    C  
ANISOU  707  C   ILE B 513     6815   4540   7168   1736    520    152  B    C  
ATOM    708  O   ILE B 513      -5.297 -25.451 -21.219  1.00 48.49      B    O  
ANISOU  708  O   ILE B 513     6607   4543   7272   1910    470    188  B    O  
ATOM    709  CB  ILE B 513      -5.451 -24.220 -23.846  1.00 48.53      B    C  
ANISOU  709  CB  ILE B 513     6676   4685   7077   1698    840   -111  B    C  
ATOM    710  CG1 ILE B 513      -5.503 -22.950 -24.711  1.00 51.06      B    C  
ANISOU  710  CG1 ILE B 513     6983   5171   7247   1553    970   -181  B    C  
ATOM    711  CG2 ILE B 513      -5.517 -25.494 -24.681  1.00 48.79      B    C  
ANISOU  711  CG2 ILE B 513     6916   4481   7141   1785    933   -231  B    C  
ATOM    712  CD1 ILE B 513      -4.318 -22.894 -25.687  1.00 53.67      B    C  
ANISOU  712  CD1 ILE B 513     7228   5512   7652   1655   1234   -329  B    C  
ATOM    713  N   GLN B 514      -7.352 -26.256 -21.666  1.00 50.84      B    N  
ANISOU  713  N   GLN B 514     7292   4620   7405   1666    463    207  B    N  
ATOM    714  CA  GLN B 514      -7.248 -27.365 -20.733  1.00 53.64      B    C  
ANISOU  714  CA  GLN B 514     7734   4781   7863   1791    364    334  B    C  
ATOM    715  C   GLN B 514      -7.095 -28.688 -21.460  1.00 57.02      B    C  
ANISOU  715  C   GLN B 514     8327   4929   8408   1898    436    232  B    C  
ATOM    716  O   GLN B 514      -8.011 -29.146 -22.127  1.00 57.35      B    O  
ANISOU  716  O   GLN B 514     8554   4831   8404   1758    477    157  B    O  
ATOM    717  CB  GLN B 514      -8.473 -27.402 -19.804  1.00 55.32      B    C  
ANISOU  717  CB  GLN B 514     8075   4963   7980   1620    273    500  B    C  
ATOM    718  CG  GLN B 514      -8.412 -28.504 -18.758  1.00 60.19      B    C  
ANISOU  718  CG  GLN B 514     8838   5367   8666   1732    186    670  B    C  
ATOM    719  CD  GLN B 514      -7.352 -28.215 -17.722  1.00 66.44      B    C  
ANISOU  719  CD  GLN B 514     9504   6268   9472   1929     54    782  B    C  
ATOM    720  NE2 GLN B 514      -6.322 -29.068 -17.659  1.00 67.37      B    N  
ANISOU  720  NE2 GLN B 514     9611   6236   9749   2185      0    777  B    N  
ATOM    721  OE1 GLN B 514      -7.441 -27.232 -16.969  1.00 68.17      B    O  
ANISOU  721  OE1 GLN B 514     9634   6697   9569   1864    -18    862  B    O  
ATOM    722  N   HIS B 515      -5.934 -29.304 -21.316  1.00 59.21      B    N  
ANISOU  722  N   HIS B 515     8530   5115   8855   2154    437    216  B    N  
ATOM    723  CA  HIS B 515      -5.608 -30.595 -21.887  1.00 62.19      B    C  
ANISOU  723  CA  HIS B 515     9050   5203   9375   2311    505    115  B    C  
ATOM    724  C   HIS B 515      -5.509 -31.580 -20.704  1.00 64.93      B    C  
ANISOU  724  C   HIS B 515     9507   5335   9831   2457    345    310  B    C  
ATOM    725  O   HIS B 515      -5.348 -31.157 -19.548  1.00 65.54      B    O  
ANISOU  725  O   HIS B 515     9502   5530   9869   2488    194    492  B    O  
ATOM    726  CB  HIS B 515      -4.262 -30.483 -22.625  1.00 63.57      B    C  
ANISOU  726  CB  HIS B 515     9024   5439   9691   2525    649    -59  B    C  
ATOM    727  CG  HIS B 515      -3.898 -31.652 -23.489  1.00 66.89      B    C  
ANISOU  727  CG  HIS B 515     9587   5585  10242   2686    784   -228  B    C  
ATOM    728  CD2 HIS B 515      -3.931 -31.773 -24.836  1.00 68.42      B    C  
ANISOU  728  CD2 HIS B 515     9894   5729  10374   2650    993   -455  B    C  
ATOM    729  ND1 HIS B 515      -3.362 -32.820 -22.948  1.00 69.15      B    N  
ANISOU  729  ND1 HIS B 515     9924   5611  10739   2933    701   -173  B    N  
ATOM    730  CE1 HIS B 515      -3.116 -33.621 -23.977  1.00 69.87      B    C  
ANISOU  730  CE1 HIS B 515    10142   5494  10910   3037    873   -379  B    C  
ATOM    731  NE2 HIS B 515      -3.445 -33.043 -25.134  1.00 70.10      B    N  
ANISOU  731  NE2 HIS B 515    10224   5643  10767   2870   1056   -559  B    N  
ATOM    732  N   SER B 516      -5.633 -32.881 -20.971  1.00 66.63      B    N  
ANISOU  732  N   SER B 516     9941   5217  10158   2542    370    278  B    N  
ATOM    733  CA  SER B 516      -5.518 -33.881 -19.906  1.00 68.60      B    C  
ANISOU  733  CA  SER B 516    10345   5214  10507   2693    226    476  B    C  
ATOM    734  C   SER B 516      -4.114 -33.837 -19.263  1.00 69.22      B    C  
ANISOU  734  C   SER B 516    10208   5359  10734   3020     99    532  B    C  
ATOM    735  O   SER B 516      -3.965 -34.073 -18.058  1.00 70.04      B    O  
ANISOU  735  O   SER B 516    10376   5407  10828   3126    -94    752  B    O  
ATOM    736  CB  SER B 516      -5.772 -35.274 -20.467  1.00 71.11      B    C  
ANISOU  736  CB  SER B 516    10929   5135  10955   2744    292    396  B    C  
ATOM    737  OG  SER B 516      -4.817 -35.555 -21.478  1.00 75.06      B    O  
ANISOU  737  OG  SER B 516    11330   5587  11601   2957    415    161  B    O  
ATOM    738  N   LEU B 517      -3.091 -33.508 -20.072  1.00 68.05      B    N  
ANISOU  738  N   LEU B 517     9802   5330  10721   3175    210    327  B    N  
ATOM    739  CA  LEU B 517      -1.707 -33.475 -19.619  1.00 66.78      B    C  
ANISOU  739  CA  LEU B 517     9367   5231  10775   3489     99    328  B    C  
ATOM    740  C   LEU B 517      -1.224 -32.089 -19.127  1.00 63.90      B    C  
ANISOU  740  C   LEU B 517     8678   5242  10357   3438     12    358  B    C  
ATOM    741  O   LEU B 517      -0.036 -31.905 -18.878  1.00 63.67      B    O  
ANISOU  741  O   LEU B 517     8351   5302  10537   3670    -74    316  B    O  
ATOM    742  CB  LEU B 517      -0.817 -34.034 -20.724  1.00 67.43      B    C  
ANISOU  742  CB  LEU B 517     9336   5189  11095   3704    299     80  B    C  
ATOM    743  CG  LEU B 517      -1.156 -35.480 -21.108  1.00 69.08      B    C  
ANISOU  743  CG  LEU B 517     9873   4984  11388   3798    351     41  B    C  
ATOM    744  CD1 LEU B 517      -0.442 -35.907 -22.358  1.00 70.10      B    C  
ANISOU  744  CD1 LEU B 517     9933   5010  11692   3961    608   -248  B    C  
ATOM    745  CD2 LEU B 517      -0.889 -36.455 -19.954  1.00 69.65      B    C  
ANISOU  745  CD2 LEU B 517    10079   4791  11595   4040     93    260  B    C  
ATOM    746  N   GLY B 518      -2.150 -31.160 -18.919  1.00 61.47      B    N  
ANISOU  746  N   GLY B 518     8428   5133   9797   3145     14    430  B    N  
ATOM    747  CA  GLY B 518      -1.803 -29.839 -18.408  1.00 59.64      B    C  
ANISOU  747  CA  GLY B 518     7935   5226   9500   3075    -75    459  B    C  
ATOM    748  C   GLY B 518      -2.702 -28.733 -18.904  1.00 57.68      B    C  
ANISOU  748  C   GLY B 518     7700   5186   9029   2756     61    413  B    C  
ATOM    749  O   GLY B 518      -3.623 -28.974 -19.685  1.00 57.13      B    O  
ANISOU  749  O   GLY B 518     7831   5024   8852   2586    209    354  B    O  
ATOM    750  N   SER B 519      -2.440 -27.509 -18.449  1.00 56.28      B    N  
ANISOU  750  N   SER B 519     7311   5280   8794   2679    -12    433  B    N  
ATOM    751  CA  SER B 519      -3.228 -26.369 -18.861  1.00 55.83      B    C  
ANISOU  751  CA  SER B 519     7256   5415   8542   2402     96    397  B    C  
ATOM    752  C   SER B 519      -2.358 -25.149 -19.105  1.00 53.75      B    C  
ANISOU  752  C   SER B 519     6673   5399   8352   2383    145    293  B    C  
ATOM    753  O   SER B 519      -1.265 -25.022 -18.550  1.00 54.41      B    O  
ANISOU  753  O   SER B 519     6509   5549   8616   2553     19    287  B    O  
ATOM    754  CB  SER B 519      -4.295 -26.045 -17.819  1.00 58.76      B    C  
ANISOU  754  CB  SER B 519     7800   5830   8696   2243    -44    578  B    C  
ATOM    755  OG  SER B 519      -3.704 -25.561 -16.625  1.00 62.62      B    O  
ANISOU  755  OG  SER B 519     8169   6446   9179   2337   -260    680  B    O  
ATOM    756  N   LEU B 520      -2.825 -24.280 -19.978  1.00 50.78      B    N  
ANISOU  756  N   LEU B 520     6301   5139   7854   2179    323    204  B    N  
ATOM    757  CA  LEU B 520      -2.158 -23.021 -20.276  1.00 48.99      B    C  
ANISOU  757  CA  LEU B 520     5816   5126   7673   2106    406    118  B    C  
ATOM    758  C   LEU B 520      -3.207 -21.931 -20.082  1.00 45.82      B    C  
ANISOU  758  C   LEU B 520     5519   4857   7033   1862    373    184  B    C  
ATOM    759  O   LEU B 520      -4.373 -22.132 -20.413  1.00 44.19      B    O  
ANISOU  759  O   LEU B 520     5554   4579   6657   1736    407    213  B    O  
ATOM    760  CB  LEU B 520      -1.608 -22.998 -21.713  1.00 49.99      B    C  
ANISOU  760  CB  LEU B 520     5879   5234   7881   2112    710    -62  B    C  
ATOM    761  CG  LEU B 520      -0.675 -24.170 -22.067  1.00 53.40      B    C  
ANISOU  761  CG  LEU B 520     6230   5505   8556   2365    799   -159  B    C  
ATOM    762  CD1 LEU B 520      -1.023 -24.764 -23.418  1.00 54.72      B    C  
ANISOU  762  CD1 LEU B 520     6630   5528   8635   2343   1059   -292  B    C  
ATOM    763  CD2 LEU B 520       0.782 -23.753 -22.019  1.00 54.48      B    C  
ANISOU  763  CD2 LEU B 520     5960   5751   8987   2494    863   -255  B    C  
ATOM    764  N   ASP B 521      -2.799 -20.785 -19.523  1.00 44.69      B    N  
ANISOU  764  N   ASP B 521     5181   4896   6903   1800    293    196  B    N  
ATOM    765  CA  ASP B 521      -3.708 -19.675 -19.281  1.00 43.94      B    C  
ANISOU  765  CA  ASP B 521     5167   4920   6609   1593    259    246  B    C  
ATOM    766  C   ASP B 521      -3.109 -18.448 -19.923  1.00 43.56      B    C  
ANISOU  766  C   ASP B 521     4933   5006   6612   1489    399    146  B    C  
ATOM    767  O   ASP B 521      -1.972 -18.116 -19.621  1.00 43.28      B    O  
ANISOU  767  O   ASP B 521     4629   5044   6771   1559    369     95  B    O  
ATOM    768  CB  ASP B 521      -3.852 -19.420 -17.767  1.00 45.25      B    C  
ANISOU  768  CB  ASP B 521     5328   5154   6711   1612      5    366  B    C  
ATOM    769  CG  ASP B 521      -4.618 -20.490 -17.021  1.00 50.42      B    C  
ANISOU  769  CG  ASP B 521     6221   5671   7266   1673   -107    501  B    C  
ATOM    770  OD1 ASP B 521      -5.827 -20.622 -17.256  1.00 48.96      B    O  
ANISOU  770  OD1 ASP B 521     6236   5428   6938   1541    -35    542  B    O  
ATOM    771  OD2 ASP B 521      -4.001 -21.195 -16.198  1.00 56.39      B    O1-
ANISOU  771  OD2 ASP B 521     6960   6365   8099   1852   -270    568  B    O1-
ATOM    772  N   SER B 522      -3.868 -17.742 -20.775  1.00 43.00      B    N  
ANISOU  772  N   SER B 522     5001   4957   6381   1318    539    120  B    N  
ATOM    773  CA  SER B 522      -3.358 -16.515 -21.394  1.00 42.93      B    C  
ANISOU  773  CA  SER B 522     4867   5047   6398   1200    689     50  B    C  
ATOM    774  C   SER B 522      -3.207 -15.415 -20.321  1.00 42.60      B    C  
ANISOU  774  C   SER B 522     4674   5134   6377   1128    517     90  B    C  
ATOM    775  O   SER B 522      -3.745 -15.574 -19.223  1.00 42.02      B    O  
ANISOU  775  O   SER B 522     4664   5076   6227   1155    304    175  B    O  
ATOM    776  CB  SER B 522      -4.310 -16.069 -22.494  1.00 44.40      B    C  
ANISOU  776  CB  SER B 522     5298   5200   6372   1056    827     37  B    C  
ATOM    777  OG  SER B 522      -5.542 -15.667 -21.924  1.00 46.27      B    O  
ANISOU  777  OG  SER B 522     5673   5460   6449    963    662    122  B    O  
ATOM    778  N   PRO B 523      -2.440 -14.319 -20.574  1.00 42.98      B    N  
ANISOU  778  N   PRO B 523     4535   5263   6534   1034    615     25  B    N  
ATOM    779  CA  PRO B 523      -2.318 -13.270 -19.550  1.00 42.91      B    C  
ANISOU  779  CA  PRO B 523     4404   5356   6546    957    433     41  B    C  
ATOM    780  C   PRO B 523      -3.677 -12.642 -19.244  1.00 42.37      B    C  
ANISOU  780  C   PRO B 523     4574   5296   6228    843    351    115  B    C  
ATOM    781  O   PRO B 523      -4.419 -12.286 -20.156  1.00 42.22      B    O  
ANISOU  781  O   PRO B 523     4729   5236   6076    746    489    123  B    O  
ATOM    782  CB  PRO B 523      -1.373 -12.249 -20.194  1.00 43.99      B    C  
ANISOU  782  CB  PRO B 523     4333   5531   6849    840    621    -50  B    C  
ATOM    783  CG  PRO B 523      -0.631 -13.038 -21.277  1.00 44.58      B    C  
ANISOU  783  CG  PRO B 523     4334   5545   7061    921    885   -121  B    C  
ATOM    784  CD  PRO B 523      -1.692 -13.958 -21.796  1.00 42.75      B    C  
ANISOU  784  CD  PRO B 523     4422   5221   6601    976    913    -67  B    C  
ATOM    785  N   PRO B 524      -4.039 -12.562 -17.957  1.00 41.49      B    N  
ANISOU  785  N   PRO B 524     4486   5231   6048    871    121    169  B    N  
ATOM    786  CA  PRO B 524      -5.356 -12.011 -17.612  1.00 40.63      B    C  
ANISOU  786  CA  PRO B 524     4579   5127   5729    779     72    226  B    C  
ATOM    787  C   PRO B 524      -5.492 -10.513 -17.841  1.00 39.77      B    C  
ANISOU  787  C   PRO B 524     4457   5056   5597    628    120    184  B    C  
ATOM    788  O   PRO B 524      -4.538  -9.760 -17.698  1.00 39.58      B    O  
ANISOU  788  O   PRO B 524     4253   5075   5710    580    110    118  B    O  
ATOM    789  CB  PRO B 524      -5.507 -12.351 -16.124  1.00 41.91      B    C  
ANISOU  789  CB  PRO B 524     4775   5326   5822    860   -149    285  B    C  
ATOM    790  CG  PRO B 524      -4.100 -12.446 -15.613  1.00 43.07      B    C  
ANISOU  790  CG  PRO B 524     4693   5521   6151    954   -279    233  B    C  
ATOM    791  CD  PRO B 524      -3.274 -12.989 -16.765  1.00 41.07      B    C  
ANISOU  791  CD  PRO B 524     4293   5219   6091   1002   -104    176  B    C  
ATOM    792  N   THR B 525      -6.701 -10.079 -18.153  1.00 38.80      B    N  
ANISOU  792  N   THR B 525     4516   4902   5323    554    156    218  B    N  
ATOM    793  CA  THR B 525      -6.999  -8.659 -18.323  1.00 38.57      B    C  
ANISOU  793  CA  THR B 525     4518   4877   5260    431    181    191  B    C  
ATOM    794  C   THR B 525      -8.203  -8.332 -17.432  1.00 36.63      B    C  
ANISOU  794  C   THR B 525     4390   4647   4880    427     67    224  B    C  
ATOM    795  O   THR B 525      -9.085  -9.178 -17.272  1.00 35.70      B    O  
ANISOU  795  O   THR B 525     4372   4509   4684    478     50    278  B    O  
ATOM    796  CB  THR B 525      -7.208  -8.297 -19.812  1.00 41.29      B    C  
ANISOU  796  CB  THR B 525     4972   5147   5570    359    360    191  B    C  
ATOM    797  CG2 THR B 525      -8.297  -9.113 -20.476  1.00 41.87      B    C  
ANISOU  797  CG2 THR B 525     5228   5161   5518    399    375    232  B    C  
ATOM    798  OG1 THR B 525      -7.568  -6.920 -19.899  1.00 44.75      B    O  
ANISOU  798  OG1 THR B 525     5471   5562   5971    255    362    184  B    O  
ATOM    799  N   CYS B 526      -8.224  -7.143 -16.809  1.00 35.42      B    N  
ANISOU  799  N   CYS B 526     4220   4519   4718    364      5    182  B    N  
ATOM    800  CA  CYS B 526      -9.365  -6.788 -15.973  1.00 34.78      B    C  
ANISOU  800  CA  CYS B 526     4249   4449   4518    370    -63    194  B    C  
ATOM    801  C   CYS B 526     -10.071  -5.616 -16.592  1.00 33.56      B    C  
ANISOU  801  C   CYS B 526     4170   4233   4349    295     -9    173  B    C  
ATOM    802  O   CYS B 526      -9.429  -4.645 -16.979  1.00 33.61      B    O  
ANISOU  802  O   CYS B 526     4140   4207   4424    218     20    131  B    O  
ATOM    803  CB  CYS B 526      -8.981  -6.536 -14.517  1.00 36.13      B    C  
ANISOU  803  CB  CYS B 526     4392   4690   4647    398   -203    156  B    C  
ATOM    804  SG  CYS B 526     -10.405  -6.205 -13.434  1.00 41.80      B    S  
ANISOU  804  SG  CYS B 526     5269   5419   5194    416   -219    161  B    S  
ATOM    805  N   VAL B 527     -11.389  -5.720 -16.742  1.00 32.54      B    N  
ANISOU  805  N   VAL B 527     4139   4071   4154    316      4    205  B    N  
ATOM    806  CA  VAL B 527     -12.167  -4.670 -17.381  1.00 31.92      B    C  
ANISOU  806  CA  VAL B 527     4138   3918   4074    279     20    192  B    C  
ATOM    807  C   VAL B 527     -13.272  -4.197 -16.448  1.00 30.11      B    C  
ANISOU  807  C   VAL B 527     3932   3697   3812    311    -17    162  B    C  
ATOM    808  O   VAL B 527     -13.920  -4.998 -15.758  1.00 28.84      B    O  
ANISOU  808  O   VAL B 527     3763   3579   3614    355    -11    182  B    O  
ATOM    809  CB  VAL B 527     -12.719  -5.171 -18.751  1.00 34.83      B    C  
ANISOU  809  CB  VAL B 527     4588   4220   4426    286     56    238  B    C  
ATOM    810  CG1 VAL B 527     -13.554  -6.415 -18.574  1.00 37.24      B    C  
ANISOU  810  CG1 VAL B 527     4888   4544   4717    337     37    267  B    C  
ATOM    811  CG2 VAL B 527     -13.533  -4.103 -19.469  1.00 35.92      B    C  
ANISOU  811  CG2 VAL B 527     4829   4265   4553    274     27    237  B    C  
ATOM    812  N   LEU B 528     -13.452  -2.881 -16.386  1.00 29.20      B    N  
ANISOU  812  N   LEU B 528     3851   3526   3717    286    -34    110  B    N  
ATOM    813  CA  LEU B 528     -14.557  -2.316 -15.656  1.00 29.52      B    C  
ANISOU  813  CA  LEU B 528     3914   3555   3750    331    -41     63  B    C  
ATOM    814  C   LEU B 528     -15.614  -2.065 -16.739  1.00 29.41      B    C  
ANISOU  814  C   LEU B 528     3935   3450   3792    361    -55     91  B    C  
ATOM    815  O   LEU B 528     -15.348  -1.267 -17.625  1.00 29.69      B    O  
ANISOU  815  O   LEU B 528     4043   3392   3847    334    -78    104  B    O  
ATOM    816  CB  LEU B 528     -14.104  -0.979 -15.054  1.00 30.49      B    C  
ANISOU  816  CB  LEU B 528     4068   3638   3881    299    -70    -25  B    C  
ATOM    817  CG  LEU B 528     -15.006  -0.415 -13.984  1.00 32.56      B    C  
ANISOU  817  CG  LEU B 528     4359   3900   4112    356    -55   -107  B    C  
ATOM    818  CD1 LEU B 528     -14.962  -1.296 -12.774  1.00 32.63      B    C  
ANISOU  818  CD1 LEU B 528     4366   4026   4005    385    -33   -112  B    C  
ATOM    819  CD2 LEU B 528     -14.534   0.966 -13.578  1.00 33.10      B    C  
ANISOU  819  CD2 LEU B 528     4485   3892   4200    318    -95   -210  B    C  
ATOM    820  N   PRO B 529     -16.814  -2.694 -16.713  1.00 29.05      B    N  
ANISOU  820  N   PRO B 529     3842   3415   3780    413    -51    102  B    N  
ATOM    821  CA  PRO B 529     -17.807  -2.435 -17.772  1.00 28.63      B    C  
ANISOU  821  CA  PRO B 529     3805   3274   3801    454   -124    113  B    C  
ATOM    822  C   PRO B 529     -18.123  -0.970 -18.007  1.00 29.01      B    C  
ANISOU  822  C   PRO B 529     3914   3213   3897    492   -180     76  B    C  
ATOM    823  O   PRO B 529     -18.318  -0.573 -19.150  1.00 28.47      B    O  
ANISOU  823  O   PRO B 529     3939   3044   3833    511   -269    116  B    O  
ATOM    824  CB  PRO B 529     -19.030  -3.215 -17.295  1.00 28.67      B    C  
ANISOU  824  CB  PRO B 529     3688   3317   3888    490    -98     95  B    C  
ATOM    825  CG  PRO B 529     -18.404  -4.387 -16.591  1.00 29.11      B    C  
ANISOU  825  CG  PRO B 529     3729   3465   3866    446    -11    133  B    C  
ATOM    826  CD  PRO B 529     -17.319  -3.705 -15.771  1.00 27.96      B    C  
ANISOU  826  CD  PRO B 529     3638   3359   3627    431     14    107  B    C  
ATOM    827  N   ASP B 530     -18.149  -0.162 -16.924  1.00 28.42      B    N  
ANISOU  827  N   ASP B 530     3820   3140   3838    510   -132      0  B    N  
ATOM    828  CA  ASP B 530     -18.429   1.269 -16.992  1.00 28.81      B    C  
ANISOU  828  CA  ASP B 530     3937   3061   3949    556   -175    -51  B    C  
ATOM    829  C   ASP B 530     -17.428   2.025 -17.862  1.00 29.26      B    C  
ANISOU  829  C   ASP B 530     4142   3009   3966    485   -210      0  B    C  
ATOM    830  O   ASP B 530     -17.774   3.090 -18.402  1.00 29.99      B    O  
ANISOU  830  O   ASP B 530     4339   2947   4109    528   -274      5  B    O  
ATOM    831  CB  ASP B 530     -18.350   1.865 -15.577  1.00 30.32      B    C  
ANISOU  831  CB  ASP B 530     4111   3281   4126    566    -98   -162  B    C  
ATOM    832  CG  ASP B 530     -18.903   3.262 -15.503  1.00 37.26      B    C  
ANISOU  832  CG  ASP B 530     5045   4013   5099    642   -128   -241  B    C  
ATOM    833  OD1 ASP B 530     -20.131   3.423 -15.694  1.00 37.65      B    O  
ANISOU  833  OD1 ASP B 530     5021   4012   5271    757   -152   -264  B    O  
ATOM    834  OD2 ASP B 530     -18.104   4.210 -15.252  1.00 40.46      B    O1-
ANISOU  834  OD2 ASP B 530     5555   4339   5481    588   -135   -288  B    O1-
ATOM    835  N   SER B 531     -16.185   1.513 -17.969  1.00 28.75      B    N  
ANISOU  835  N   SER B 531     4086   3010   3828    379   -156     38  B    N  
ATOM    836  CA  SER B 531     -15.108   2.173 -18.715  1.00 30.26      B    C  
ANISOU  836  CA  SER B 531     4388   3105   4003    280   -128     81  B    C  
ATOM    837  C   SER B 531     -14.973   1.763 -20.163  1.00 30.50      B    C  
ANISOU  837  C   SER B 531     4531   3085   3970    262   -122    188  B    C  
ATOM    838  O   SER B 531     -14.139   2.337 -20.861  1.00 31.70      B    O  
ANISOU  838  O   SER B 531     4801   3142   4101    173    -56    235  B    O  
ATOM    839  CB  SER B 531     -13.764   1.970 -18.022  1.00 32.52      B    C  
ANISOU  839  CB  SER B 531     4588   3478   4289    174    -65     38  B    C  
ATOM    840  OG  SER B 531     -13.816   2.603 -16.757  1.00 35.87      B    O  
ANISOU  840  OG  SER B 531     4977   3915   4738    183    -94    -73  B    O  
ATOM    841  N   VAL B 532     -15.775   0.808 -20.631  1.00 29.25      B    N  
ANISOU  841  N   VAL B 532     3997   3244   3872    472   -186    437  B    N  
ATOM    842  CA  VAL B 532     -15.714   0.377 -22.027  1.00 28.71      B    C  
ANISOU  842  CA  VAL B 532     3886   3157   3865    525    -65    412  B    C  
ATOM    843  C   VAL B 532     -17.057   0.570 -22.732  1.00 28.48      B    C  
ANISOU  843  C   VAL B 532     3944   3069   3809    459    -36    286  B    C  
ATOM    844  O   VAL B 532     -17.403  -0.210 -23.623  1.00 28.18      B    O  
ANISOU  844  O   VAL B 532     4008   2931   3769    478     10    250  B    O  
ATOM    845  CB  VAL B 532     -15.217  -1.091 -22.146  1.00 28.92      B    C  
ANISOU  845  CB  VAL B 532     3957   3115   3916    663     43    481  B    C  
ATOM    846  CG1 VAL B 532     -13.732  -1.212 -21.758  1.00 29.69      B    C  
ANISOU  846  CG1 VAL B 532     3875   3295   4110    765     25    678  B    C  
ATOM    847  CG2 VAL B 532     -16.079  -2.048 -21.318  1.00 28.13      B    C  
ANISOU  847  CG2 VAL B 532     3991   2925   3773    636     46    452  B    C  
ATOM    848  N   VAL B 533     -17.844   1.563 -22.312  1.00 28.76      B    N  
ANISOU  848  N   VAL B 533     3976   3136   3816    391    -83    243  B    N  
ATOM    849  CA  VAL B 533     -19.153   1.814 -22.927  1.00 28.68      B    C  
ANISOU  849  CA  VAL B 533     3967   3092   3840    337    -74    192  B    C  
ATOM    850  C   VAL B 533     -18.963   2.506 -24.280  1.00 29.01      B    C  
ANISOU  850  C   VAL B 533     4021   3129   3874    316   -117    130  B    C  
ATOM    851  O   VAL B 533     -18.139   3.412 -24.395  1.00 28.82      B    O  
ANISOU  851  O   VAL B 533     3970   3162   3818    324   -135    133  B    O  
ATOM    852  CB  VAL B 533     -20.027   2.686 -21.983  1.00 29.08      B    C  
ANISOU  852  CB  VAL B 533     4014   3175   3860    357    -36    215  B    C  
ATOM    853  CG1 VAL B 533     -21.281   3.246 -22.694  1.00 29.80      B    C  
ANISOU  853  CG1 VAL B 533     4020   3264   4038    330    -32    222  B    C  
ATOM    854  CG2 VAL B 533     -20.395   1.942 -20.698  1.00 28.91      B    C  
ANISOU  854  CG2 VAL B 533     4033   3132   3819    408     65    301  B    C  
ATOM    855  N   LYS B 534     -19.735   2.098 -25.301  1.00 28.74      B    N  
ANISOU  855  N   LYS B 534     4054   3002   3865    266   -166     97  B    N  
ATOM    856  CA  LYS B 534     -19.748   2.839 -26.559  1.00 28.82      B    C  
ANISOU  856  CA  LYS B 534     4140   2982   3828    252   -219     39  B    C  
ATOM    857  C   LYS B 534     -21.092   3.571 -26.504  1.00 29.14      B    C  
ANISOU  857  C   LYS B 534     4079   3042   3951    181   -311     55  B    C  
ATOM    858  O   LYS B 534     -22.130   2.916 -26.595  1.00 29.04      B    O  
ANISOU  858  O   LYS B 534     4029   2963   4044     96   -404    116  B    O  
ATOM    859  CB  LYS B 534     -19.732   1.899 -27.781  1.00 29.91      B    C  
ANISOU  859  CB  LYS B 534     4533   2946   3887    259   -262      4  B    C  
ATOM    860  CG  LYS B 534     -19.647   2.735 -29.063  1.00 32.15      B    C  
ANISOU  860  CG  LYS B 534     4963   3182   4069    273   -295    -49  B    C  
ATOM    861  CD  LYS B 534     -19.463   1.881 -30.273  1.00 36.20      B    C  
ANISOU  861  CD  LYS B 534     5873   3471   4409    336   -308    -89  B    C  
ATOM    862  CE  LYS B 534     -19.329   2.717 -31.514  1.00 41.07      B    C  
ANISOU  862  CE  LYS B 534     6696   4025   4884    378   -311   -129  B    C  
ATOM    863  NZ  LYS B 534     -19.419   1.830 -32.709  1.00 45.50      B    N1+
ANISOU  863  NZ  LYS B 534     7797   4288   5205    437   -377   -182  B    N1+
ATOM    864  N   PRO B 535     -21.124   4.894 -26.258  1.00 29.51      B    N  
ANISOU  864  N   PRO B 535     4069   3168   3974    217   -288     42  B    N  
ATOM    865  CA  PRO B 535     -22.426   5.572 -26.176  1.00 30.15      B    C  
ANISOU  865  CA  PRO B 535     4044   3266   4147    222   -319    101  B    C  
ATOM    866  C   PRO B 535     -23.157   5.543 -27.506  1.00 31.74      B    C  
ANISOU  866  C   PRO B 535     4266   3388   4407    133   -500    107  B    C  
ATOM    867  O   PRO B 535     -22.530   5.419 -28.564  1.00 32.03      B    O  
ANISOU  867  O   PRO B 535     4497   3343   4328    103   -572     20  B    O  
ATOM    868  CB  PRO B 535     -22.066   7.040 -25.845  1.00 30.07      B    C  
ANISOU  868  CB  PRO B 535     4100   3296   4028    303   -270     58  B    C  
ATOM    869  CG  PRO B 535     -20.627   7.071 -25.561  1.00 30.60      B    C  
ANISOU  869  CG  PRO B 535     4258   3377   3993    282   -262     11  B    C  
ATOM    870  CD  PRO B 535     -20.000   5.843 -26.159  1.00 28.65      B    C  
ANISOU  870  CD  PRO B 535     4003   3110   3773    248   -257     10  B    C  
ATOM    871  N   LEU B 536     -24.488   5.726 -27.468  1.00 32.26      B    N  
ANISOU  871  N   LEU B 536     4142   3465   4652    111   -571    245  B    N  
ATOM    872  CA  LEU B 536     -25.250   5.929 -28.685  1.00 33.95      B    C  
ANISOU  872  CA  LEU B 536     4365   3597   4938     13   -821    286  B    C  
ATOM    873  C   LEU B 536     -24.822   7.320 -29.229  1.00 34.31      B    C  
ANISOU  873  C   LEU B 536     4539   3664   4834    109   -792    180  B    C  
ATOM    874  O   LEU B 536     -24.262   8.151 -28.496  1.00 34.00      B    O  
ANISOU  874  O   LEU B 536     4519   3700   4701    231   -604    129  B    O  
ATOM    875  CB  LEU B 536     -26.779   5.926 -28.404  1.00 35.33      B    C  
ANISOU  875  CB  LEU B 536     4191   3814   5420    -20   -900    550  B    C  
ATOM    876  CG  LEU B 536     -27.362   4.612 -27.824  1.00 38.48      B    C  
ANISOU  876  CG  LEU B 536     4401   4189   6032   -153   -937    733  B    C  
ATOM    877  CD1 LEU B 536     -28.907   4.694 -27.707  1.00 39.38      B    C  
ANISOU  877  CD1 LEU B 536     4074   4356   6533   -203  -1028   1093  B    C  
ATOM    878  CD2 LEU B 536     -26.958   3.404 -28.647  1.00 39.33      B    C  
ANISOU  878  CD2 LEU B 536     4800   4100   6044   -365  -1209    633  B    C  
ATOM    879  N   PRO B 537     -24.966   7.541 -30.532  1.00 34.98      B    N  
ANISOU  879  N   PRO B 537     4789   3643   4857     37  -1005    142  B    N  
ATOM    880  CA  PRO B 537     -24.573   8.846 -31.081  1.00 35.71      B    C  
ANISOU  880  CA  PRO B 537     5018   3741   4810    119   -973     62  B    C  
ATOM    881  C   PRO B 537     -25.443   9.970 -30.522  1.00 36.90      B    C  
ANISOU  881  C   PRO B 537     4966   3973   5081    243   -915    170  B    C  
ATOM    882  O   PRO B 537     -26.618   9.746 -30.177  1.00 36.94      B    O  
ANISOU  882  O   PRO B 537     4697   4018   5321    260   -961    358  B    O  
ATOM    883  CB  PRO B 537     -24.865   8.706 -32.588  1.00 36.32      B    C  
ANISOU  883  CB  PRO B 537     5340   3655   4803     21  -1249     41  B    C  
ATOM    884  CG  PRO B 537     -25.120   7.253 -32.826  1.00 37.44      B    C  
ANISOU  884  CG  PRO B 537     5577   3671   4977   -118  -1426     68  B    C  
ATOM    885  CD  PRO B 537     -25.588   6.661 -31.543  1.00 34.80      B    C  
ANISOU  885  CD  PRO B 537     4892   3455   4877   -134  -1328    190  B    C  
ATOM    886  N   PRO B 538     -24.961  11.224 -30.586  1.00 37.58      B    N  
ANISOU  886  N   PRO B 538     5198   4059   5023    338   -829     93  B    N  
ATOM    887  CA  PRO B 538     -25.855  12.363 -30.294  1.00 38.86      B    C  
ANISOU  887  CA  PRO B 538     5273   4240   5253    504   -784    194  B    C  
ATOM    888  C   PRO B 538     -27.034  12.363 -31.278  1.00 41.17      B    C  
ANISOU  888  C   PRO B 538     5420   4499   5724    470  -1035    342  B    C  
ATOM    889  O   PRO B 538     -26.891  11.901 -32.418  1.00 41.51      B    O  
ANISOU  889  O   PRO B 538     5613   4448   5710    307  -1284    289  B    O  
ATOM    890  CB  PRO B 538     -24.955  13.583 -30.538  1.00 39.01      B    C  
ANISOU  890  CB  PRO B 538     5581   4196   5045    535   -742     62  B    C  
ATOM    891  CG  PRO B 538     -23.533  13.035 -30.390  1.00 38.67      B    C  
ANISOU  891  CG  PRO B 538     5652   4161   4881    406   -684    -52  B    C  
ATOM    892  CD  PRO B 538     -23.630  11.685 -31.020  1.00 36.74      B    C  
ANISOU  892  CD  PRO B 538     5340   3915   4706    301   -776    -44  B    C  
ATOM    893  N   SER B 539     -28.210  12.804 -30.831  1.00 42.18      B    N  
ANISOU  893  N   SER B 539     5272   4686   6068    634   -979    564  B    N  
ATOM    894  CA  SER B 539     -29.407  12.786 -31.662  1.00 43.68      B    C  
ANISOU  894  CA  SER B 539     5222   4861   6513    588  -1265    791  B    C  
ATOM    895  C   SER B 539     -29.930  14.213 -31.933  1.00 44.75      B    C  
ANISOU  895  C   SER B 539     5378   4982   6644    818  -1231    873  B    C  
ATOM    896  O   SER B 539     -29.321  15.190 -31.484  1.00 44.34      B    O  
ANISOU  896  O   SER B 539     5589   4900   6356    993   -990    726  B    O  
ATOM    897  CB  SER B 539     -30.482  11.922 -31.003  1.00 46.44      B    C  
ANISOU  897  CB  SER B 539     5097   5307   7239    577  -1248   1107  B    C  
ATOM    898  OG  SER B 539     -31.033  12.604 -29.884  1.00 50.65      B    O  
ANISOU  898  OG  SER B 539     5424   5944   7875    913   -853   1291  B    O  
ATOM    899  N   ASN B 540     -31.009  14.335 -32.734  1.00 46.01      B    N  
ANISOU  899  N   ASN B 540     5304   5127   7051    791  -1529   1114  B    N  
ATOM    900  CA  ASN B 540     -31.634  15.610 -33.112  1.00 48.39      B    C  
ANISOU  900  CA  ASN B 540     5589   5406   7390   1022  -1542   1243  B    C  
ATOM    901  C   ASN B 540     -30.568  16.618 -33.605  1.00 48.71      B    C  
ANISOU  901  C   ASN B 540     6167   5324   7018   1050  -1495    924  B    C  
ATOM    902  O   ASN B 540     -30.551  17.764 -33.163  1.00 49.14      B    O  
ANISOU  902  O   ASN B 540     6362   5351   6958   1317  -1254    912  B    O  
ATOM    903  CB  ASN B 540     -32.451  16.178 -31.936  1.00 51.52      B    C  
ANISOU  903  CB  ASN B 540     5672   5914   7989   1413  -1131   1515  B    C  
ATOM    904  CG  ASN B 540     -33.408  17.279 -32.326  1.00 59.17      B    C  
ANISOU  904  CG  ASN B 540     6486   6874   9122   1691  -1158   1776  B    C  
ATOM    905  ND2 ASN B 540     -33.831  18.078 -31.353  1.00 60.99      B    N  
ANISOU  905  ND2 ASN B 540     6670   7135   9367   2134   -701   1935  B    N  
ATOM    906  OD1 ASN B 540     -33.772  17.438 -33.501  1.00 61.82      B    O  
ANISOU  906  OD1 ASN B 540     6797   7150   9542   1540  -1582   1846  B    O  
ATOM    907  N   VAL B 541     -29.604  16.138 -34.422  1.00 47.86      B    N  
ANISOU  907  N   VAL B 541     6388   5124   6674    788  -1679    684  B    N  
ATOM    908  CA  VAL B 541     -28.557  17.013 -34.927  1.00 47.62      B    C  
ANISOU  908  CA  VAL B 541     6802   4988   6304    786  -1614    453  B    C  
ATOM    909  C   VAL B 541     -29.149  17.914 -35.996  1.00 48.33      B    C  
ANISOU  909  C   VAL B 541     7016   4974   6373    846  -1857    536  B    C  
ATOM    910  O   VAL B 541     -29.826  17.423 -36.900  1.00 47.79      B    O  
ANISOU  910  O   VAL B 541     6887   4853   6417    719  -2223    653  B    O  
ATOM    911  CB  VAL B 541     -27.329  16.239 -35.442  1.00 47.68      B    C  
ANISOU  911  CB  VAL B 541     7092   4940   6086    563  -1632    243  B    C  
ATOM    912  CG1 VAL B 541     -26.291  17.196 -36.030  1.00 48.04      B    C  
ANISOU  912  CG1 VAL B 541     7522   4888   5845    559  -1543     98  B    C  
ATOM    913  CG2 VAL B 541     -26.723  15.393 -34.322  1.00 47.50      B    C  
ANISOU  913  CG2 VAL B 541     6931   5021   6097    526  -1400    183  B    C  
ATOM    914  N   LYS B 542     -28.944  19.242 -35.849  1.00 48.44      B    N  
ANISOU  914  N   LYS B 542     7235   4930   6240   1035  -1691    493  B    N  
ATOM    915  CA  LYS B 542     -29.434  20.242 -36.783  1.00 48.88      B    C  
ANISOU  915  CA  LYS B 542     7452   4872   6246   1131  -1882    567  B    C  
ATOM    916  C   LYS B 542     -28.280  21.147 -37.237  1.00 48.60      B    C  
ANISOU  916  C   LYS B 542     7904   4699   5863   1079  -1787    360  B    C  
ATOM    917  O   LYS B 542     -27.353  21.411 -36.470  1.00 48.53      B    O  
ANISOU  917  O   LYS B 542     8030   4688   5720   1063  -1535    231  B    O  
ATOM    918  CB  LYS B 542     -30.523  21.110 -36.120  1.00 51.81      B    C  
ANISOU  918  CB  LYS B 542     7585   5280   6819   1483  -1745    799  B    C  
ATOM    919  CG  LYS B 542     -31.748  20.330 -35.641  1.00 57.22      B    C  
ANISOU  919  CG  LYS B 542     7689   6122   7928   1568  -1785   1116  B    C  
ATOM    920  CD  LYS B 542     -32.864  21.264 -35.203  1.00 63.05      B    C  
ANISOU  920  CD  LYS B 542     8183   6890   8882   1988  -1609   1422  B    C  
ATOM    921  CE  LYS B 542     -34.051  20.510 -34.648  1.00 67.72      B    C  
ANISOU  921  CE  LYS B 542     8111   7661   9958   2089  -1580   1826  B    C  
ATOM    922  NZ  LYS B 542     -35.138  21.431 -34.198  1.00 69.72      B    N1+
ANISOU  922  NZ  LYS B 542     8091   7954  10446   2584  -1307   2194  B    N1+
ATOM    923  N   ALA B 543     -28.357  21.658 -38.469  1.00 47.72      B    N  
ANISOU  923  N   ALA B 543     8061   4455   5616   1042  -2013    364  B    N  
ATOM    924  CA  ALA B 543     -27.355  22.578 -38.987  1.00 47.77      B    C  
ANISOU  924  CA  ALA B 543     8505   4321   5324    992  -1918    233  B    C  
ATOM    925  C   ALA B 543     -28.080  23.695 -39.726  1.00 49.05      B    C  
ANISOU  925  C   ALA B 543     8847   4348   5441   1152  -2095    336  B    C  
ATOM    926  O   ALA B 543     -29.032  23.425 -40.459  1.00 48.31      B    O  
ANISOU  926  O   ALA B 543     8651   4241   5465   1175  -2408    472  B    O  
ATOM    927  CB  ALA B 543     -26.404  21.855 -39.917  1.00 47.95      B    C  
ANISOU  927  CB  ALA B 543     8777   4293   5150    767  -1950    127  B    C  
ATOM    928  N   GLU B 544     -27.662  24.956 -39.514  1.00 50.53      B    N  
ANISOU  928  N   GLU B 544     9316   4414   5467   1251  -1939    295  B    N  
ATOM    929  CA  GLU B 544     -28.342  26.091 -40.142  1.00 53.13      B    C  
ANISOU  929  CA  GLU B 544     9849   4596   5741   1441  -2081    398  B    C  
ATOM    930  C   GLU B 544     -27.383  27.238 -40.409  1.00 55.04      B    C  
ANISOU  930  C   GLU B 544    10572   4644   5698   1378  -1969    302  B    C  
ATOM    931  O   GLU B 544     -26.560  27.548 -39.551  1.00 54.02      B    O  
ANISOU  931  O   GLU B 544    10545   4484   5496   1308  -1758    216  B    O  
ATOM    932  CB  GLU B 544     -29.429  26.581 -39.175  1.00 56.88      B    C  
ANISOU  932  CB  GLU B 544    10071   5114   6429   1795  -1974    558  B    C  
ATOM    933  CG  GLU B 544     -30.437  27.564 -39.727  1.00 66.09      B    C  
ANISOU  933  CG  GLU B 544    11295   6171   7644   2078  -2127    747  B    C  
ATOM    934  CD  GLU B 544     -31.346  28.137 -38.652  1.00 77.27      B    C  
ANISOU  934  CD  GLU B 544    12518   7607   9233   2512  -1880    930  B    C  
ATOM    935  OE1 GLU B 544     -31.529  27.480 -37.600  1.00 78.89      B    O  
ANISOU  935  OE1 GLU B 544    12407   7963   9607   2590  -1661    972  B    O  
ATOM    936  OE2 GLU B 544     -31.875  29.253 -38.861  1.00 81.47      B    O1-
ANISOU  936  OE2 GLU B 544    13253   7988   9712   2812  -1871   1046  B    O1-
ATOM    937  N   ILE B 545     -27.509  27.887 -41.582  1.00 57.49      B    N  
ANISOU  937  N   ILE B 545    11194   4798   5851   1386  -2145    345  B    N  
ATOM    938  CA  ILE B 545     -26.745  29.081 -41.958  1.00 60.70      B    C  
ANISOU  938  CA  ILE B 545    12066   4990   6006   1331  -2067    310  B    C  
ATOM    939  C   ILE B 545     -27.731  30.174 -42.309  1.00 63.97      B    C  
ANISOU  939  C   ILE B 545    12659   5249   6397   1616  -2215    425  B    C  
ATOM    940  O   ILE B 545     -28.606  29.966 -43.150  1.00 64.31      B    O  
ANISOU  940  O   ILE B 545    12631   5302   6503   1711  -2481    534  B    O  
ATOM    941  CB  ILE B 545     -25.754  28.912 -43.149  1.00 61.46      B    C  
ANISOU  941  CB  ILE B 545    12465   5009   5878   1081  -2062    281  B    C  
ATOM    942  CG1 ILE B 545     -24.588  28.020 -42.766  1.00 62.98      B    C  
ANISOU  942  CG1 ILE B 545    12506   5331   6091    841  -1837    215  B    C  
ATOM    943  CG2 ILE B 545     -25.226  30.303 -43.636  1.00 62.09      B    C  
ANISOU  943  CG2 ILE B 545    13011   4843   5737   1053  -2019    321  B    C  
ATOM    944  CD1 ILE B 545     -23.717  27.718 -43.884  1.00 64.69      B    C  
ANISOU  944  CD1 ILE B 545    12976   5491   6113    690  -1744    243  B    C  
ATOM    945  N   THR B 546     -27.535  31.352 -41.731  1.00 65.89      B    N  
ANISOU  945  N   THR B 546    13196   5312   6528   1734  -2082    412  B    N  
ATOM    946  CA  THR B 546     -28.315  32.553 -42.029  1.00 68.26      B    C  
ANISOU  946  CA  THR B 546    13770   5410   6755   2036  -2170    520  B    C  
ATOM    947  C   THR B 546     -27.349  33.730 -42.199  1.00 69.38      B    C  
ANISOU  947  C   THR B 546    14485   5266   6611   1886  -2108    457  B    C  
ATOM    948  O   THR B 546     -26.247  33.706 -41.645  1.00 68.79      B    O  
ANISOU  948  O   THR B 546    14511   5158   6466   1609  -1976    365  B    O  
ATOM    949  CB  THR B 546     -29.246  32.875 -40.848  1.00 71.09      B    C  
ANISOU  949  CB  THR B 546    13969   5780   7263   2444  -2015    605  B    C  
ATOM    950  CG2 THR B 546     -30.227  31.730 -40.547  1.00 72.34      B    C  
ANISOU  950  CG2 THR B 546    13483   6230   7774   2585  -2047    741  B    C  
ATOM    951  OG1 THR B 546     -28.441  33.132 -39.687  1.00 72.28      B    O  
ANISOU  951  OG1 THR B 546    14341   5836   7286   2363  -1789    467  B    O  
ATOM    952  N   VAL B 547     -27.782  34.785 -42.896  1.00 70.93      B    N  
ANISOU  952  N   VAL B 547    15043   5240   6667   2061  -2226    541  B    N  
ATOM    953  CA  VAL B 547     -26.965  35.999 -42.988  1.00 72.85      B    C  
ANISOU  953  CA  VAL B 547    15862   5168   6651   1924  -2185    515  B    C  
ATOM    954  C   VAL B 547     -27.065  36.811 -41.653  1.00 74.38      B    C  
ANISOU  954  C   VAL B 547    16328   5155   6777   2129  -2054    473  B    C  
ATOM    955  O   VAL B 547     -26.156  37.586 -41.351  1.00 75.18      B    O  
ANISOU  955  O   VAL B 547    16879   4995   6692   1895  -2047    426  B    O  
ATOM    956  CB  VAL B 547     -27.243  36.814 -44.270  1.00 74.31      B    C  
ANISOU  956  CB  VAL B 547    16417   5154   6664   1998  -2355    613  B    C  
ATOM    957  CG1 VAL B 547     -28.738  36.971 -44.511  1.00 75.42      B    C  
ANISOU  957  CG1 VAL B 547    16402   5325   6930   2454  -2514    747  B    C  
ATOM    958  CG2 VAL B 547     -26.533  38.168 -44.251  1.00 74.86      B    C  
ANISOU  958  CG2 VAL B 547    17103   4858   6484   1887  -2322    617  B    C  
ATOM    959  N   ASN B 548     -28.086  36.522 -40.784  1.00 74.68      B    N  
ANISOU  959  N   ASN B 548    16097   5307   6971   2534  -1943    509  B    N  
ATOM    960  CA  ASN B 548     -28.268  37.148 -39.456  1.00 74.86      B    C  
ANISOU  960  CA  ASN B 548    16444   5121   6879   2820  -1757    474  B    C  
ATOM    961  C   ASN B 548     -27.118  36.826 -38.506  1.00 73.20      B    C  
ANISOU  961  C   ASN B 548    16350   4876   6586   2449  -1707    321  B    C  
ATOM    962  O   ASN B 548     -26.812  37.616 -37.609  1.00 74.46      B    O  
ANISOU  962  O   ASN B 548    17067   4712   6513   2504  -1670    258  B    O  
ATOM    963  CB  ASN B 548     -29.592  36.723 -38.831  1.00 77.80      B    C  
ANISOU  963  CB  ASN B 548    16404   5678   7477   3349  -1575    612  B    C  
ATOM    964  CG  ASN B 548     -30.778  37.042 -39.701  1.00 84.58      B    C  
ANISOU  964  CG  ASN B 548    17072   6577   8487   3721  -1672    837  B    C  
ATOM    965  ND2 ASN B 548     -31.231  36.040 -40.459  1.00 86.76      B    N  
ANISOU  965  ND2 ASN B 548    16742   7171   9052   3597  -1861    940  B    N  
ATOM    966  OD1 ASN B 548     -31.272  38.183 -39.745  1.00 86.33      B    O  
ANISOU  966  OD1 ASN B 548    17721   6521   8559   4103  -1622    931  B    O  
ATOM    967  N   THR B 549     -26.488  35.673 -38.698  1.00 70.23      B    N  
ANISOU  967  N   THR B 549    15498   4802   6386   2081  -1733    276  B    N  
ATOM    968  CA  THR B 549     -25.314  35.266 -37.950  1.00 68.10      B    C  
ANISOU  968  CA  THR B 549    15238   4540   6096   1684  -1730    180  B    C  
ATOM    969  C   THR B 549     -24.066  35.332 -38.850  1.00 64.85      B    C  
ANISOU  969  C   THR B 549    14863   4109   5668   1172  -1851    214  B    C  
ATOM    970  O   THR B 549     -22.980  35.627 -38.375  1.00 65.04      B    O  
ANISOU  970  O   THR B 549    15093   3985   5636    811  -1925    216  B    O  
ATOM    971  CB  THR B 549     -25.488  33.825 -37.398  1.00 69.81      B    C  
ANISOU  971  CB  THR B 549    14848   5124   6552   1689  -1612    145  B    C  
ATOM    972  CG2 THR B 549     -26.734  33.672 -36.546  1.00 70.63      B    C  
ANISOU  972  CG2 THR B 549    14824   5286   6727   2202  -1431    186  B    C  
ATOM    973  OG1 THR B 549     -25.512  32.880 -38.477  1.00 70.31      B    O  
ANISOU  973  OG1 THR B 549    14445   5475   6796   1541  -1661    184  B    O  
ATOM    974  N   GLY B 550     -24.228  35.010 -40.128  1.00 61.95      B    N  
ANISOU  974  N   GLY B 550    14291   3888   5360   1147  -1872    277  B    N  
ATOM    975  CA  GLY B 550     -23.127  34.914 -41.070  1.00 59.78      B    C  
ANISOU  975  CA  GLY B 550    14011   3631   5071    751  -1879    355  B    C  
ATOM    976  C   GLY B 550     -22.256  33.706 -40.749  1.00 56.80      B    C  
ANISOU  976  C   GLY B 550    13184   3525   4871    472  -1772    348  B    C  
ATOM    977  O   GLY B 550     -21.063  33.733 -41.033  1.00 56.25      B    O  
ANISOU  977  O   GLY B 550    13104   3439   4829    115  -1727    462  B    O  
ATOM    978  N   LEU B 551     -22.833  32.651 -40.107  1.00 55.02      B    N  
ANISOU  978  N   LEU B 551    12566   3546   4793    640  -1717    256  B    N  
ATOM    979  CA  LEU B 551     -22.115  31.476 -39.605  1.00 53.45      B    C  
ANISOU  979  CA  LEU B 551    11961   3589   4759    432  -1619    236  B    C  
ATOM    980  C   LEU B 551     -22.927  30.206 -39.728  1.00 50.28      B    C  
ANISOU  980  C   LEU B 551    11147   3462   4493    624  -1576    176  B    C  
ATOM    981  O   LEU B 551     -24.154  30.241 -39.775  1.00 49.81      B    O  
ANISOU  981  O   LEU B 551    11043   3420   4461    931  -1642    163  B    O  
ATOM    982  CB  LEU B 551     -21.878  31.643 -38.072  1.00 55.24      B    C  
ANISOU  982  CB  LEU B 551    12256   3735   5000    391  -1647    174  B    C  
ATOM    983  CG  LEU B 551     -20.925  32.692 -37.592  1.00 59.15      B    C  
ANISOU  983  CG  LEU B 551    13159   3929   5385    102  -1785    237  B    C  
ATOM    984  CD1 LEU B 551     -21.351  33.170 -36.237  1.00 61.04      B    C  
ANISOU  984  CD1 LEU B 551    13747   3958   5489    277  -1860    133  B    C  
ATOM    985  CD2 LEU B 551     -19.537  32.132 -37.479  1.00 60.30      B    C  
ANISOU  985  CD2 LEU B 551    13018   4191   5700   -334  -1790    364  B    C  
ATOM    986  N   LEU B 552     -22.239  29.073 -39.621  1.00 48.26      B    N  
ANISOU  986  N   LEU B 552    10568   3413   4357    442  -1475    172  B    N  
ATOM    987  CA  LEU B 552     -22.872  27.767 -39.579  1.00 47.60      B    C  
ANISOU  987  CA  LEU B 552    10119   3561   4406    561  -1458    117  B    C  
ATOM    988  C   LEU B 552     -23.138  27.399 -38.089  1.00 48.61      B    C  
ANISOU  988  C   LEU B 552    10034   3776   4659    642  -1413     54  B    C  
ATOM    989  O   LEU B 552     -22.201  27.281 -37.290  1.00 48.86      B    O  
ANISOU  989  O   LEU B 552    10032   3817   4716    448  -1355     45  B    O  
ATOM    990  CB  LEU B 552     -21.931  26.743 -40.215  1.00 46.39      B    C  
ANISOU  990  CB  LEU B 552     9816   3539   4271    363  -1332    150  B    C  
ATOM    991  CG  LEU B 552     -22.331  25.283 -40.099  1.00 46.37      B    C  
ANISOU  991  CG  LEU B 552     9499   3735   4385    422  -1322     90  B    C  
ATOM    992  CD1 LEU B 552     -23.674  25.026 -40.754  1.00 46.36      B    C  
ANISOU  992  CD1 LEU B 552     9511   3723   4380    611  -1535     77  B    C  
ATOM    993  CD2 LEU B 552     -21.273  24.397 -40.719  1.00 46.44      B    C  
ANISOU  993  CD2 LEU B 552     9472   3815   4357    282  -1139    138  B    C  
ATOM    994  N   LYS B 553     -24.407  27.233 -37.722  1.00 48.59      B    N  
ANISOU  994  N   LYS B 553     9887   3830   4745    932  -1441     51  B    N  
ATOM    995  CA  LYS B 553     -24.766  26.854 -36.362  1.00 49.10      B    C  
ANISOU  995  CA  LYS B 553     9778   3971   4906   1070  -1335     24  B    C  
ATOM    996  C   LYS B 553     -25.143  25.387 -36.347  1.00 48.06      B    C  
ANISOU  996  C   LYS B 553     9193   4090   4979   1055  -1319     33  B    C  
ATOM    997  O   LYS B 553     -26.010  24.968 -37.115  1.00 48.13      B    O  
ANISOU  997  O   LYS B 553     9022   4170   5095   1143  -1440    104  B    O  
ATOM    998  CB  LYS B 553     -25.918  27.721 -35.815  1.00 53.49      B    C  
ANISOU  998  CB  LYS B 553    10480   4406   5439   1464  -1285     85  B    C  
ATOM    999  CG  LYS B 553     -26.357  27.253 -34.409  1.00 61.42      B    C  
ANISOU  999  CG  LYS B 553    11334   5483   6518   1671  -1097     92  B    C  
ATOM   1000  CD  LYS B 553     -27.470  28.101 -33.794  1.00 68.70      B    C  
ANISOU 1000  CD  LYS B 553    12432   6272   7400   2151   -936    201  B    C  
ATOM   1001  CE  LYS B 553     -27.987  27.464 -32.521  1.00 73.61      B    C  
ANISOU 1001  CE  LYS B 553    12861   6997   8112   2394   -683    258  B    C  
ATOM   1002  NZ  LYS B 553     -28.575  26.125 -32.794  1.00 76.29      B    N1+
ANISOU 1002  NZ  LYS B 553    12539   7653   8795   2336   -698    372  B    N1+
ATOM   1003  N   VAL B 554     -24.458  24.597 -35.512  1.00 46.42      B    N  
ANISOU 1003  N   VAL B 554     8828   3988   4822    914  -1219    -22  B    N  
ATOM   1004  CA  VAL B 554     -24.710  23.166 -35.362  1.00 46.15      B    C  
ANISOU 1004  CA  VAL B 554     8408   4163   4966    882  -1195    -18  B    C  
ATOM   1005  C   VAL B 554     -25.240  22.937 -33.957  1.00 46.39      B    C  
ANISOU 1005  C   VAL B 554     8295   4249   5082   1066  -1055      1  B    C  
ATOM   1006  O   VAL B 554     -24.754  23.562 -33.015  1.00 47.40      B    O  
ANISOU 1006  O   VAL B 554     8678   4257   5073   1086   -974    -47  B    O  
ATOM   1007  CB  VAL B 554     -23.436  22.318 -35.607  1.00 46.30      B    C  
ANISOU 1007  CB  VAL B 554     8364   4259   4968    603  -1154    -68  B    C  
ATOM   1008  CG1 VAL B 554     -23.708  20.825 -35.386  1.00 46.62      B    C  
ANISOU 1008  CG1 VAL B 554     8078   4471   5163    587  -1134    -74  B    C  
ATOM   1009  CG2 VAL B 554     -22.881  22.549 -37.003  1.00 46.81      B    C  
ANISOU 1009  CG2 VAL B 554     8623   4250   4913    484  -1200    -47  B    C  
ATOM   1010  N   SER B 555     -26.252  22.086 -33.802  1.00 44.95      B    N  
ANISOU 1010  N   SER B 555     7753   4214   5113   1197  -1039     97  B    N  
ATOM   1011  CA  SER B 555     -26.793  21.791 -32.476  1.00 44.02      B    C  
ANISOU 1011  CA  SER B 555     7484   4158   5084   1405   -836    161  B    C  
ATOM   1012  C   SER B 555     -27.137  20.311 -32.365  1.00 42.46      B    C  
ANISOU 1012  C   SER B 555     6854   4155   5122   1311   -849    226  B    C  
ATOM   1013  O   SER B 555     -27.335  19.645 -33.386  1.00 42.02      B    O  
ANISOU 1013  O   SER B 555     6632   4156   5179   1153  -1057    255  B    O  
ATOM   1014  CB  SER B 555     -27.988  22.683 -32.142  1.00 46.20      B    C  
ANISOU 1014  CB  SER B 555     7787   4364   5402   1805   -707    325  B    C  
ATOM   1015  OG  SER B 555     -29.110  22.363 -32.949  1.00 49.65      B    O  
ANISOU 1015  OG  SER B 555     7839   4911   6115   1886   -842    526  B    O  
ATOM   1016  N   TRP B 556     -27.156  19.785 -31.134  1.00 41.35      B    N  
ANISOU 1016  N   TRP B 556     6612   4078   5019   1394   -648    245  B    N  
ATOM   1017  CA  TRP B 556     -27.384  18.356 -30.939  1.00 41.05      B    C  
ANISOU 1017  CA  TRP B 556     6202   4203   5194   1279   -656    307  B    C  
ATOM   1018  C   TRP B 556     -27.960  18.071 -29.542  1.00 41.45      B    C  
ANISOU 1018  C   TRP B 556     6117   4308   5322   1517   -369    433  B    C  
ATOM   1019  O   TRP B 556     -28.077  18.975 -28.705  1.00 41.47      B    O  
ANISOU 1019  O   TRP B 556     6398   4200   5158   1788   -151    443  B    O  
ATOM   1020  CB  TRP B 556     -26.043  17.583 -31.154  1.00 39.81      B    C  
ANISOU 1020  CB  TRP B 556     6138   4063   4925    967   -739    125  B    C  
ATOM   1021  CG  TRP B 556     -24.980  17.989 -30.176  1.00 39.41      B    C  
ANISOU 1021  CG  TRP B 556     6356   3944   4673    938   -621     10  B    C  
ATOM   1022  CD1 TRP B 556     -24.796  17.498 -28.919  1.00 39.97      B    C  
ANISOU 1022  CD1 TRP B 556     6419   4044   4725    986   -478      8  B    C  
ATOM   1023  CD2 TRP B 556     -24.025  19.049 -30.337  1.00 39.53      B    C  
ANISOU 1023  CD2 TRP B 556     6722   3816   4482    841   -686    -81  B    C  
ATOM   1024  CE2 TRP B 556     -23.294  19.140 -29.134  1.00 40.50      B    C  
ANISOU 1024  CE2 TRP B 556     7036   3873   4479    805   -637   -128  B    C  
ATOM   1025  CE3 TRP B 556     -23.726  19.941 -31.378  1.00 40.09      B    C  
ANISOU 1025  CE3 TRP B 556     6980   3787   4464    765   -804   -102  B    C  
ATOM   1026  NE1 TRP B 556     -23.782  18.176 -28.290  1.00 40.66      B    N  
ANISOU 1026  NE1 TRP B 556     6854   4000   4594    912   -501    -87  B    N  
ATOM   1027  CZ2 TRP B 556     -22.279  20.081 -28.943  1.00 41.31      B    C  
ANISOU 1027  CZ2 TRP B 556     7486   3807   4403    653   -759   -176  B    C  
ATOM   1028  CZ3 TRP B 556     -22.719  20.868 -31.191  1.00 41.01      B    C  
ANISOU 1028  CZ3 TRP B 556     7414   3755   4414    632   -861   -146  B    C  
ATOM   1029  CH2 TRP B 556     -22.025  20.954 -29.979  1.00 41.22      B    C  
ANISOU 1029  CH2 TRP B 556     7606   3708   4347    561   -865   -173  B    C  
ATOM   1030  N   GLU B 557     -28.317  16.812 -29.300  1.00 41.11      B    N  
ANISOU 1030  N   GLU B 557     5715   4403   5503   1428   -361    537  B    N  
ATOM   1031  CA  GLU B 557     -28.781  16.350 -28.013  1.00 41.93      B    C  
ANISOU 1031  CA  GLU B 557     5677   4569   5686   1624    -65    677  B    C  
ATOM   1032  C   GLU B 557     -27.864  15.191 -27.659  1.00 41.69      B    C  
ANISOU 1032  C   GLU B 557     5646   4587   5608   1360   -116    532  B    C  
ATOM   1033  O   GLU B 557     -27.759  14.247 -28.439  1.00 42.55      B    O  
ANISOU 1033  O   GLU B 557     5558   4754   5855   1104   -339    517  B    O  
ATOM   1034  CB  GLU B 557     -30.211  15.822 -28.132  1.00 46.28      B    C  
ANISOU 1034  CB  GLU B 557     5689   5250   6645   1736    -33   1032  B    C  
ATOM   1035  CG  GLU B 557     -31.264  16.869 -27.836  1.00 56.44      B    C  
ANISOU 1035  CG  GLU B 557     6906   6519   8021   2167    223   1294  B    C  
ATOM   1036  CD  GLU B 557     -31.463  17.135 -26.356  1.00 67.29      B    C  
ANISOU 1036  CD  GLU B 557     8463   7852   9253   2563    720   1390  B    C  
ATOM   1037  OE1 GLU B 557     -31.012  16.309 -25.522  1.00 69.17      B    O  
ANISOU 1037  OE1 GLU B 557     8742   8119   9421   2477    841   1326  B    O  
ATOM   1038  OE2 GLU B 557     -32.084  18.172 -26.032  1.00 69.85      B    O1-
ANISOU 1038  OE2 GLU B 557     8941   8090   9508   2992   1001   1540  B    O1-
ATOM   1039  N   LYS B 558     -27.217  15.237 -26.498  1.00 40.32      B    N  
ANISOU 1039  N   LYS B 558     5740   4360   5221   1435     68    437  B    N  
ATOM   1040  CA  LYS B 558     -26.336  14.160 -26.088  1.00 39.96      B    C  
ANISOU 1040  CA  LYS B 558     5682   4360   5141   1217     21    330  B    C  
ATOM   1041  C   LYS B 558     -27.167  12.899 -25.827  1.00 38.95      B    C  
ANISOU 1041  C   LYS B 558     5148   4358   5294   1208    101    523  B    C  
ATOM   1042  O   LYS B 558     -28.382  12.975 -25.561  1.00 38.56      B    O  
ANISOU 1042  O   LYS B 558     4842   4360   5450   1421    274    780  B    O  
ATOM   1043  CB  LYS B 558     -25.543  14.568 -24.842  1.00 42.78      B    C  
ANISOU 1043  CB  LYS B 558     6449   4600   5204   1300    140    223  B    C  
ATOM   1044  CG  LYS B 558     -26.423  14.883 -23.660  1.00 48.37      B    C  
ANISOU 1044  CG  LYS B 558     7293   5250   5837   1669    475    373  B    C  
ATOM   1045  CD  LYS B 558     -25.599  15.134 -22.410  1.00 55.39      B    C  
ANISOU 1045  CD  LYS B 558     8701   5970   6376   1720    521    255  B    C  
ATOM   1046  CE  LYS B 558     -26.507  15.360 -21.236  1.00 61.12      B    C  
ANISOU 1046  CE  LYS B 558     9657   6603   6964   2153    924    416  B    C  
ATOM   1047  NZ  LYS B 558     -27.321  14.142 -20.967  1.00 66.24      B    N1+
ANISOU 1047  NZ  LYS B 558     9812   7445   7912   2222   1163    644  B    N1+
ATOM   1048  N   PRO B 559     -26.543  11.716 -25.963  1.00 38.05      B    N  
ANISOU 1048  N   PRO B 559     4947   4287   5223    962    -26    446  B    N  
ATOM   1049  CA  PRO B 559     -27.273  10.489 -25.634  1.00 38.17      B    C  
ANISOU 1049  CA  PRO B 559     4632   4382   5490    917     24    634  B    C  
ATOM   1050  C   PRO B 559     -27.601  10.456 -24.143  1.00 39.65      B    C  
ANISOU 1050  C   PRO B 559     4851   4584   5631   1165    376    764  B    C  
ATOM   1051  O   PRO B 559     -26.930  11.093 -23.336  1.00 39.29      B    O  
ANISOU 1051  O   PRO B 559     5184   4455   5290   1301    504    631  B    O  
ATOM   1052  CB  PRO B 559     -26.291   9.374 -26.018  1.00 38.11      B    C  
ANISOU 1052  CB  PRO B 559     4687   4361   5432    650   -160    475  B    C  
ATOM   1053  CG  PRO B 559     -24.942   9.994 -25.846  1.00 38.10      B    C  
ANISOU 1053  CG  PRO B 559     5014   4312   5150    643   -156    257  B    C  
ATOM   1054  CD  PRO B 559     -25.117  11.446 -26.251  1.00 37.00      B    C  
ANISOU 1054  CD  PRO B 559     5022   4120   4914    754   -171    227  B    C  
ATOM   1055  N   VAL B 560     -28.665   9.737 -23.790  1.00 41.08      B    N  
ANISOU 1055  N   VAL B 560     4664   4844   6102   1221    518   1056  B    N  
ATOM   1056  CA  VAL B 560     -29.147   9.580 -22.426  1.00 42.73      B    C  
ANISOU 1056  CA  VAL B 560     4871   5069   6297   1493    922   1253  B    C  
ATOM   1057  C   VAL B 560     -28.056   8.959 -21.530  1.00 41.99      B    C  
ANISOU 1057  C   VAL B 560     5111   4917   5928   1423    955   1051  B    C  
ATOM   1058  O   VAL B 560     -27.814   9.455 -20.430  1.00 42.86      B    O  
ANISOU 1058  O   VAL B 560     5596   4938   5750   1671   1204   1017  B    O  
ATOM   1059  CB  VAL B 560     -30.441   8.743 -22.479  1.00 44.84      B    C  
ANISOU 1059  CB  VAL B 560     4562   5449   7026   1464    998   1666  B    C  
ATOM   1060  CG1 VAL B 560     -30.886   8.316 -21.100  1.00 45.62      B    C  
ANISOU 1060  CG1 VAL B 560     4627   5571   7137   1715   1452   1910  B    C  
ATOM   1061  CG2 VAL B 560     -31.540   9.519 -23.198  1.00 45.73      B    C  
ANISOU 1061  CG2 VAL B 560     4335   5617   7424   1595    980   1933  B    C  
ATOM   1062  N   PHE B 561     -27.334   7.962 -22.042  1.00 39.76      B    N  
ANISOU 1062  N   PHE B 561     4768   4648   5690   1104    677    910  B    N  
ATOM   1063  CA  PHE B 561     -26.224   7.362 -21.317  1.00 38.71      B    C  
ANISOU 1063  CA  PHE B 561     4904   4469   5334   1032    661    742  B    C  
ATOM   1064  C   PHE B 561     -24.911   7.607 -22.068  1.00 37.68      B    C  
ANISOU 1064  C   PHE B 561     4967   4303   5046    840    371    472  B    C  
ATOM   1065  O   PHE B 561     -24.904   7.712 -23.293  1.00 37.38      B    O  
ANISOU 1065  O   PHE B 561     4815   4279   5109    701    176    418  B    O  
ATOM   1066  CB  PHE B 561     -26.439   5.853 -21.102  1.00 38.66      B    C  
ANISOU 1066  CB  PHE B 561     4671   4499   5520    883    660    867  B    C  
ATOM   1067  CG  PHE B 561     -27.425   5.516 -20.011  1.00 40.36      B    C  
ANISOU 1067  CG  PHE B 561     4749   4741   5845   1081   1013   1161  B    C  
ATOM   1068  CD1 PHE B 561     -27.408   6.193 -18.804  1.00 41.64      B    C  
ANISOU 1068  CD1 PHE B 561     5242   4845   5735   1401   1339   1187  B    C  
ATOM   1069  CD2 PHE B 561     -28.390   4.549 -20.204  1.00 41.88      B    C  
ANISOU 1069  CD2 PHE B 561     4521   4988   6403    952   1020   1446  B    C  
ATOM   1070  CE1 PHE B 561     -28.318   5.884 -17.802  1.00 43.14      B    C  
ANISOU 1070  CE1 PHE B 561     5342   5048   5999   1644   1749   1495  B    C  
ATOM   1071  CE2 PHE B 561     -29.275   4.212 -19.184  1.00 43.45      B    C  
ANISOU 1071  CE2 PHE B 561     4546   5222   6740   1140   1397   1783  B    C  
ATOM   1072  CZ  PHE B 561     -29.238   4.887 -17.990  1.00 43.40      B    C  
ANISOU 1072  CZ  PHE B 561     4870   5176   6445   1515   1803   1809  B    C  
ATOM   1073  N   PRO B 562     -23.771   7.649 -21.370  1.00 37.05      B    N  
ANISOU 1073  N   PRO B 562     5174   4169   4735    824    329    340  B    N  
ATOM   1074  CA  PRO B 562     -23.630   7.575 -19.914  1.00 36.90      B    C  
ANISOU 1074  CA  PRO B 562     5422   4082   4516    977    493    377  B    C  
ATOM   1075  C   PRO B 562     -23.946   8.917 -19.239  1.00 38.41      B    C  
ANISOU 1075  C   PRO B 562     5991   4149   4455   1227    636    377  B    C  
ATOM   1076  O   PRO B 562     -24.117   9.951 -19.910  1.00 39.48      B    O  
ANISOU 1076  O   PRO B 562     6168   4257   4575   1257    578    330  B    O  
ATOM   1077  CB  PRO B 562     -22.164   7.151 -19.747  1.00 36.48      B    C  
ANISOU 1077  CB  PRO B 562     5503   4004   4352    799    260    250  B    C  
ATOM   1078  CG  PRO B 562     -21.458   7.849 -20.891  1.00 36.66      B    C  
ANISOU 1078  CG  PRO B 562     5482   4042   4404    649     41    140  B    C  
ATOM   1079  CD  PRO B 562     -22.462   7.857 -22.037  1.00 35.92      B    C  
ANISOU 1079  CD  PRO B 562     5123   4013   4512    647     88    178  B    C  
ATOM   1080  N   GLU B 563     -24.045   8.905 -17.917  1.00 39.05      B    N  
ANISOU 1080  N   GLU B 563     6416   4120   4300   1431    833    434  B    N  
ATOM   1081  CA  GLU B 563     -24.302  10.117 -17.143  1.00 40.56      B    C  
ANISOU 1081  CA  GLU B 563     7142   4116   4155   1722    990    429  B    C  
ATOM   1082  C   GLU B 563     -23.040  10.972 -16.935  1.00 41.17      B    C  
ANISOU 1082  C   GLU B 563     7725   4001   3917   1567    617    225  B    C  
ATOM   1083  O   GLU B 563     -23.151  12.113 -16.515  1.00 43.30      B    O  
ANISOU 1083  O   GLU B 563     8519   4053   3881   1753    647    184  B    O  
ATOM   1084  CB  GLU B 563     -24.895   9.753 -15.791  1.00 44.12      B    C  
ANISOU 1084  CB  GLU B 563     7880   4473   4411   2036   1368    585  B    C  
ATOM   1085  CG  GLU B 563     -26.268   9.126 -15.898  1.00 51.61      B    C  
ANISOU 1085  CG  GLU B 563     8321   5590   5698   2221   1781    883  B    C  
ATOM   1086  CD  GLU B 563     -27.345  10.121 -16.275  1.00 63.68      B    C  
ANISOU 1086  CD  GLU B 563     9760   7123   7312   2525   2061   1044  B    C  
ATOM   1087  OE1 GLU B 563     -27.206  11.316 -15.922  1.00 66.64      B    O  
ANISOU 1087  OE1 GLU B 563    10705   7290   7324   2763   2116    944  B    O  
ATOM   1088  OE2 GLU B 563     -28.333   9.705 -16.922  1.00 67.67      B    O1-
ANISOU 1088  OE2 GLU B 563     9643   7818   8252   2521   2195   1293  B    O1-
ATOM   1089  N   ASN B 564     -21.857  10.445 -17.241  1.00 39.61      B    N  
ANISOU 1089  N   ASN B 564     7379   3863   3807   1234    263    137  B    N  
ATOM   1090  CA  ASN B 564     -20.591  11.149 -17.091  1.00 38.53      B    C  
ANISOU 1090  CA  ASN B 564     7586   3571   3483   1014   -150     33  B    C  
ATOM   1091  C   ASN B 564     -20.509  12.278 -18.098  1.00 38.24      B    C  
ANISOU 1091  C   ASN B 564     7528   3509   3493    925   -283    -30  B    C  
ATOM   1092  O   ASN B 564     -21.153  12.201 -19.145  1.00 38.31      B    O  
ANISOU 1092  O   ASN B 564     7126   3682   3747    953   -131    -12  B    O  
ATOM   1093  CB  ASN B 564     -19.412  10.176 -17.361  1.00 37.97      B    C  
ANISOU 1093  CB  ASN B 564     7167   3636   3622    713   -423     47  B    C  
ATOM   1094  CG  ASN B 564     -19.500   8.889 -16.594  1.00 40.24      B    C  
ANISOU 1094  CG  ASN B 564     7379   3981   3929    779   -292    114  B    C  
ATOM   1095  ND2 ASN B 564     -20.466   8.075 -16.944  1.00 38.72      B    N  
ANISOU 1095  ND2 ASN B 564     6835   3938   3938    896     23    174  B    N  
ATOM   1096  OD1 ASN B 564     -18.714   8.619 -15.671  1.00 42.37      B    O  
ANISOU 1096  OD1 ASN B 564     7917   4143   4039    708   -508    135  B    O  
ATOM   1097  N   ASN B 565     -19.639  13.264 -17.844  1.00 38.12      B    N  
ANISOU 1097  N   ASN B 565     7944   3277   3261    767   -629    -85  B    N  
ATOM   1098  CA  ASN B 565     -19.415  14.374 -18.775  1.00 38.91      B    C  
ANISOU 1098  CA  ASN B 565     8062   3323   3397    637   -796   -127  B    C  
ATOM   1099  C   ASN B 565     -18.893  13.862 -20.104  1.00 37.75      B    C  
ANISOU 1099  C   ASN B 565     7276   3437   3629    401   -861    -94  B    C  
ATOM   1100  O   ASN B 565     -18.059  12.967 -20.127  1.00 36.91      B    O  
ANISOU 1100  O   ASN B 565     6874   3457   3692    224   -979    -33  B    O  
ATOM   1101  CB  ASN B 565     -18.401  15.348 -18.198  1.00 42.56      B    C  
ANISOU 1101  CB  ASN B 565     9080   3487   3603    413  -1248   -143  B    C  
ATOM   1102  CG  ASN B 565     -18.920  16.089 -17.001  1.00 51.28      B    C  
ANISOU 1102  CG  ASN B 565    11026   4233   4226    677  -1208   -202  B    C  
ATOM   1103  ND2 ASN B 565     -18.027  16.362 -16.038  1.00 54.09      B    N  
ANISOU 1103  ND2 ASN B 565    11941   4303   4307    483  -1642   -197  B    N  
ATOM   1104  OD1 ASN B 565     -20.111  16.435 -16.925  1.00 53.34      B    O  
ANISOU 1104  OD1 ASN B 565    11476   4445   4346   1070   -797   -225  B    O  
ATOM   1105  N   LEU B 566     -19.378  14.426 -21.213  1.00 37.14      B    N  
ANISOU 1105  N   LEU B 566     7033   3419   3661    432   -769   -119  B    N  
ATOM   1106  CA  LEU B 566     -18.941  14.016 -22.539  1.00 37.09      B    C  
ANISOU 1106  CA  LEU B 566     6548   3609   3937    257   -795    -89  B    C  
ATOM   1107  C   LEU B 566     -18.193  15.145 -23.263  1.00 37.09      B    C  
ANISOU 1107  C   LEU B 566     6644   3516   3933     54  -1019    -71  B    C  
ATOM   1108  O   LEU B 566     -18.349  16.320 -22.948  1.00 37.37      B    O  
ANISOU 1108  O   LEU B 566     7106   3336   3759     76  -1131   -109  B    O  
ATOM   1109  CB  LEU B 566     -20.185  13.651 -23.388  1.00 37.31      B    C  
ANISOU 1109  CB  LEU B 566     6301   3771   4106    440   -532   -105  B    C  
ATOM   1110  CG  LEU B 566     -21.019  12.484 -22.871  1.00 39.19      B    C  
ANISOU 1110  CG  LEU B 566     6348   4113   4432    594   -315    -62  B    C  
ATOM   1111  CD1 LEU B 566     -22.311  12.332 -23.655  1.00 39.58      B    C  
ANISOU 1111  CD1 LEU B 566     6139   4251   4650    725   -156    -12  B    C  
ATOM   1112  CD2 LEU B 566     -20.222  11.191 -22.892  1.00 39.50      B    C  
ANISOU 1112  CD2 LEU B 566     6139   4266   4604    443   -368    -39  B    C  
ATOM   1113  N   GLN B 567     -17.392  14.773 -24.246  1.00 35.87      B    N  
ANISOU 1113  N   GLN B 567     6125   3505   3999   -122  -1055      9  B    N  
ATOM   1114  CA  GLN B 567     -16.776  15.683 -25.198  1.00 35.22      B    C  
ANISOU 1114  CA  GLN B 567     6023   3384   3976   -295  -1172     76  B    C  
ATOM   1115  C   GLN B 567     -17.463  15.332 -26.534  1.00 34.31      B    C  
ANISOU 1115  C   GLN B 567     5678   3402   3956   -163   -934     28  B    C  
ATOM   1116  O   GLN B 567     -17.968  14.214 -26.731  1.00 33.09      B    O  
ANISOU 1116  O   GLN B 567     5318   3376   3881    -42   -766     -7  B    O  
ATOM   1117  CB  GLN B 567     -15.239  15.489 -25.295  1.00 36.52      B    C  
ANISOU 1117  CB  GLN B 567     5934   3606   4337   -569  -1352    287  B    C  
ATOM   1118  CG  GLN B 567     -14.809  14.078 -25.748  1.00 39.02      B    C  
ANISOU 1118  CG  GLN B 567     5814   4146   4864   -507  -1144    373  B    C  
ATOM   1119  CD  GLN B 567     -13.314  13.898 -25.760  1.00 41.71      B    C  
ANISOU 1119  CD  GLN B 567     5851   4557   5440   -713  -1272    656  B    C  
ATOM   1120  NE2 GLN B 567     -12.818  12.965 -24.971  1.00 43.60      B    N  
ANISOU 1120  NE2 GLN B 567     5935   4865   5768   -712  -1324    741  B    N  
ATOM   1121  OE1 GLN B 567     -12.592  14.565 -26.480  1.00 42.01      B    O  
ANISOU 1121  OE1 GLN B 567     5759   4593   5609   -865  -1312    839  B    O  
ATOM   1122  N   PHE B 568     -17.526  16.302 -27.431  1.00 34.09      B    N  
ANISOU 1122  N   PHE B 568     5749   3306   3898   -201   -960     31  B    N  
ATOM   1123  CA  PHE B 568     -18.146  16.107 -28.727  1.00 34.60      B    C  
ANISOU 1123  CA  PHE B 568     5698   3443   4004    -95   -809     -8  B    C  
ATOM   1124  C   PHE B 568     -17.158  16.446 -29.809  1.00 36.12      B    C  
ANISOU 1124  C   PHE B 568     5813   3647   4264   -241   -801    115  B    C  
ATOM   1125  O   PHE B 568     -16.259  17.264 -29.620  1.00 36.22      B    O  
ANISOU 1125  O   PHE B 568     5883   3580   4299   -434   -942    238  B    O  
ATOM   1126  CB  PHE B 568     -19.419  16.980 -28.890  1.00 34.17      B    C  
ANISOU 1126  CB  PHE B 568     5863   3287   3831     77   -801   -100  B    C  
ATOM   1127  CG  PHE B 568     -20.444  16.708 -27.820  1.00 34.42      B    C  
ANISOU 1127  CG  PHE B 568     5948   3312   3818    282   -720   -148  B    C  
ATOM   1128  CD1 PHE B 568     -21.368  15.688 -27.970  1.00 34.66      B    C  
ANISOU 1128  CD1 PHE B 568     5728   3468   3974    408   -597   -142  B    C  
ATOM   1129  CD2 PHE B 568     -20.440  17.429 -26.634  1.00 35.49      B    C  
ANISOU 1129  CD2 PHE B 568     6420   3288   3778    343   -767   -167  B    C  
ATOM   1130  CE1 PHE B 568     -22.260  15.379 -26.951  1.00 35.32      B    C  
ANISOU 1130  CE1 PHE B 568     5798   3561   4059    599   -468   -116  B    C  
ATOM   1131  CE2 PHE B 568     -21.343  17.133 -25.619  1.00 36.71      B    C  
ANISOU 1131  CE2 PHE B 568     6654   3427   3866    587   -607   -173  B    C  
ATOM   1132  CZ  PHE B 568     -22.250  16.107 -25.786  1.00 36.08      B    C  
ANISOU 1132  CZ  PHE B 568     6225   3518   3966    718   -431   -128  B    C  
ATOM   1133  N   GLN B 569     -17.343  15.828 -30.950  1.00 37.16      B    N  
ANISOU 1133  N   GLN B 569     5852   3848   4420   -153   -645    110  B    N  
ATOM   1134  CA  GLN B 569     -16.548  16.127 -32.122  1.00 38.32      B    C  
ANISOU 1134  CA  GLN B 569     5987   3989   4585   -212   -544    241  B    C  
ATOM   1135  C   GLN B 569     -17.525  16.344 -33.263  1.00 37.84      B    C  
ANISOU 1135  C   GLN B 569     6126   3861   4389    -83   -515    133  B    C  
ATOM   1136  O   GLN B 569     -18.433  15.540 -33.457  1.00 37.65      B    O  
ANISOU 1136  O   GLN B 569     6114   3854   4336     38   -515     23  B    O  
ATOM   1137  CB  GLN B 569     -15.596  14.978 -32.401  1.00 40.95      B    C  
ANISOU 1137  CB  GLN B 569     6092   4437   5032   -180   -344    382  B    C  
ATOM   1138  CG  GLN B 569     -14.449  15.319 -33.306  1.00 46.61      B    C  
ANISOU 1138  CG  GLN B 569     6727   5165   5819   -224   -165    628  B    C  
ATOM   1139  CD  GLN B 569     -13.510  14.141 -33.262  1.00 53.94      B    C  
ANISOU 1139  CD  GLN B 569     7395   6213   6888   -134     59    806  B    C  
ATOM   1140  NE2 GLN B 569     -12.605  14.139 -32.289  1.00 55.52      B    N  
ANISOU 1140  NE2 GLN B 569     7294   6493   7309   -290    -48   1004  B    N  
ATOM   1141  OE1 GLN B 569     -13.613  13.208 -34.065  1.00 54.96      B    O  
ANISOU 1141  OE1 GLN B 569     7631   6336   6915     83    301    773  B    O  
ATOM   1142  N   ILE B 570     -17.392  17.465 -33.975  1.00 37.53      B    N  
ANISOU 1142  N   ILE B 570     6258   3724   4278   -134   -542    182  B    N  
ATOM   1143  CA  ILE B 570     -18.262  17.769 -35.105  1.00 38.48      B    C  
ANISOU 1143  CA  ILE B 570     6606   3759   4258    -21   -559    103  B    C  
ATOM   1144  C   ILE B 570     -17.441  17.712 -36.351  1.00 40.08      B    C  
ANISOU 1144  C   ILE B 570     6906   3932   4391    -15   -366    234  B    C  
ATOM   1145  O   ILE B 570     -16.385  18.338 -36.392  1.00 41.75      B    O  
ANISOU 1145  O   ILE B 570     7048   4143   4674   -140   -276    419  B    O  
ATOM   1146  CB  ILE B 570     -18.863  19.187 -34.991  1.00 38.89      B    C  
ANISOU 1146  CB  ILE B 570     6857   3684   4235    -31   -720     63  B    C  
ATOM   1147  CG1 ILE B 570     -19.559  19.405 -33.645  1.00 40.12      B    C  
ANISOU 1147  CG1 ILE B 570     6992   3833   4420     24   -830    -23  B    C  
ATOM   1148  CG2 ILE B 570     -19.801  19.495 -36.183  1.00 39.62      B    C  
ANISOU 1148  CG2 ILE B 570     7166   3688   4200     93   -779      9  B    C  
ATOM   1149  CD1 ILE B 570     -19.874  20.812 -33.400  1.00 42.22      B    C  
ANISOU 1149  CD1 ILE B 570     7528   3932   4580     42   -941    -37  B    C  
ATOM   1150  N   ARG B 571     -17.897  16.990 -37.369  1.00 39.32      B    N  
ANISOU 1150  N   ARG B 571     7004   3784   4151    126   -306    173  B    N  
ATOM   1151  CA  ARG B 571     -17.259  17.053 -38.664  1.00 40.27      B    C  
ANISOU 1151  CA  ARG B 571     7367   3819   4115    200    -87    292  B    C  
ATOM   1152  C   ARG B 571     -18.246  17.706 -39.640  1.00 42.06      B    C  
ANISOU 1152  C   ARG B 571     7962   3884   4135    254   -270    192  B    C  
ATOM   1153  O   ARG B 571     -19.461  17.499 -39.557  1.00 41.11      B    O  
ANISOU 1153  O   ARG B 571     7895   3728   3997    283   -541     46  B    O  
ATOM   1154  CB  ARG B 571     -16.687  15.722 -39.138  1.00 41.42      B    C  
ANISOU 1154  CB  ARG B 571     7581   3969   4186    355    177    346  B    C  
ATOM   1155  CG  ARG B 571     -17.689  14.675 -39.575  1.00 41.87      B    C  
ANISOU 1155  CG  ARG B 571     7929   3912   4067    464     17    160  B    C  
ATOM   1156  CD  ARG B 571     -16.900  13.523 -40.102  1.00 41.63      B    C  
ANISOU 1156  CD  ARG B 571     8087   3826   3904    651    337    241  B    C  
ATOM   1157  NE  ARG B 571     -17.742  12.429 -40.558  1.00 43.04      B    N  
ANISOU 1157  NE  ARG B 571     8646   3829   3879    727    148     76  B    N  
ATOM   1158  CZ  ARG B 571     -17.278  11.233 -40.915  1.00 46.34      B    C  
ANISOU 1158  CZ  ARG B 571     9338   4136   4132    911    365     95  B    C  
ATOM   1159  NH1 ARG B 571     -15.978  10.964 -40.834  1.00 47.06      B    N1+
ANISOU 1159  NH1 ARG B 571     9281   4320   4280   1081    832    299  B    N1+
ATOM   1160  NH2 ARG B 571     -18.110  10.294 -41.350  1.00 44.95      B    N  
ANISOU 1160  NH2 ARG B 571     9593   3738   3747    928    101    -57  B    N  
ATOM   1161  N   TYR B 572     -17.732  18.600 -40.475  1.00 44.36      B    N  
ANISOU 1161  N   TYR B 572     8458   4084   4313    249   -144    316  B    N  
ATOM   1162  CA  TYR B 572     -18.552  19.368 -41.384  1.00 47.33      B    C  
ANISOU 1162  CA  TYR B 572     9197   4295   4490    295   -325    251  B    C  
ATOM   1163  C   TYR B 572     -17.815  19.664 -42.672  1.00 50.09      B    C  
ANISOU 1163  C   TYR B 572     9903   4516   4614    377    -54    405  B    C  
ATOM   1164  O   TYR B 572     -16.592  19.843 -42.686  1.00 50.60      B    O  
ANISOU 1164  O   TYR B 572     9817   4641   4767    344    280    632  B    O  
ATOM   1165  CB  TYR B 572     -19.054  20.674 -40.725  1.00 47.98      B    C  
ANISOU 1165  CB  TYR B 572     9183   4368   4680    192   -548    220  B    C  
ATOM   1166  CG  TYR B 572     -17.961  21.655 -40.348  1.00 49.76      B    C  
ANISOU 1166  CG  TYR B 572     9294   4600   5013     26   -415    394  B    C  
ATOM   1167  CD1 TYR B 572     -17.186  21.461 -39.214  1.00 51.21      B    C  
ANISOU 1167  CD1 TYR B 572     9131   4908   5419   -118   -372    472  B    C  
ATOM   1168  CD2 TYR B 572     -17.720  22.787 -41.115  1.00 51.49      B    C  
ANISOU 1168  CD2 TYR B 572     9769   4676   5118    -19   -387    506  B    C  
ATOM   1169  CE1 TYR B 572     -16.167  22.340 -38.875  1.00 52.72      B    C  
ANISOU 1169  CE1 TYR B 572     9219   5073   5740   -336   -348    679  B    C  
ATOM   1170  CE2 TYR B 572     -16.714  23.686 -40.776  1.00 52.96      B    C  
ANISOU 1170  CE2 TYR B 572     9847   4840   5436   -232   -323    711  B    C  
ATOM   1171  CZ  TYR B 572     -15.944  23.463 -39.648  1.00 54.32      B    C  
ANISOU 1171  CZ  TYR B 572     9659   5126   5852   -409   -333    805  B    C  
ATOM   1172  OH  TYR B 572     -14.963  24.360 -39.282  1.00 56.53      B    O  
ANISOU 1172  OH  TYR B 572     9835   5351   6293   -684   -375   1046  B    O  
ATOM   1173  N   GLY B 573     -18.577  19.736 -43.744  1.00 51.27      B    N  
ANISOU 1173  N   GLY B 573    10516   4478   4485    485   -209    320  B    N  
ATOM   1174  CA  GLY B 573     -18.040  20.070 -45.049  1.00 53.46      B    C  
ANISOU 1174  CA  GLY B 573    11259   4583   4470    603     41    454  B    C  
ATOM   1175  C   GLY B 573     -19.115  20.413 -46.055  1.00 55.25      B    C  
ANISOU 1175  C   GLY B 573    12010   4581   4401    672   -291    337  B    C  
ATOM   1176  O   GLY B 573     -20.312  20.307 -45.772  1.00 53.90      B    O  
ANISOU 1176  O   GLY B 573    11786   4399   4295    627   -732    181  B    O  
ATOM   1177  N   LEU B 574     -18.685  20.834 -47.246  1.00 57.83      B    N  
ANISOU 1177  N   LEU B 574    12836   4721   4416    790    -74    456  B    N  
ATOM   1178  CA  LEU B 574     -19.593  21.138 -48.341  1.00 60.97      B    C  
ANISOU 1178  CA  LEU B 574    13837   4857   4471    867   -395    372  B    C  
ATOM   1179  C   LEU B 574     -20.194  19.810 -48.800  1.00 63.85      B    C  
ANISOU 1179  C   LEU B 574    14604   5061   4596    963   -629    227  B    C  
ATOM   1180  O   LEU B 574     -19.463  18.834 -48.922  1.00 63.83      B    O  
ANISOU 1180  O   LEU B 574    14752   5035   4467   1095   -285    262  B    O  
ATOM   1181  CB  LEU B 574     -18.814  21.778 -49.503  1.00 61.48      B    C  
ANISOU 1181  CB  LEU B 574    14407   4740   4212   1001    -16    562  B    C  
ATOM   1182  CG  LEU B 574     -18.347  23.225 -49.297  1.00 62.87      B    C  
ANISOU 1182  CG  LEU B 574    14334   4984   4571    866    116    731  B    C  
ATOM   1183  CD1 LEU B 574     -17.481  23.690 -50.474  1.00 63.20      B    C  
ANISOU 1183  CD1 LEU B 574    14858   4850   4305   1009    574    980  B    C  
ATOM   1184  CD2 LEU B 574     -19.524  24.148 -49.113  1.00 63.05      B    C  
ANISOU 1184  CD2 LEU B 574    14349   4952   4655    767   -412    591  B    C  
ATOM   1185  N   SER B 575     -21.517  19.745 -48.958  1.00 66.57      B    N  
ANISOU 1185  N   SER B 575    15075   5296   4922    885  -1230     96  B    N  
ATOM   1186  CA  SER B 575     -22.180  18.515 -49.377  1.00 70.04      B    C  
ANISOU 1186  CA  SER B 575    15913   5538   5163    894  -1589    -16  B    C  
ATOM   1187  C   SER B 575     -21.869  18.231 -50.837  1.00 73.40      B    C  
ANISOU 1187  C   SER B 575    17317   5582   4990   1086  -1497     -2  B    C  
ATOM   1188  O   SER B 575     -22.011  19.113 -51.679  1.00 73.89      B    O  
ANISOU 1188  O   SER B 575    17791   5476   4807   1140  -1566     52  B    O  
ATOM   1189  CB  SER B 575     -23.687  18.618 -49.166  1.00 71.97      B    C  
ANISOU 1189  CB  SER B 575    15954   5769   5621    724  -2297    -66  B    C  
ATOM   1190  OG  SER B 575     -24.260  17.349 -48.885  1.00 74.93      B    O  
ANISOU 1190  OG  SER B 575    16284   6104   6080    621  -2624   -133  B    O  
ATOM   1191  N   GLY B 576     -21.410  17.021 -51.124  1.00 75.83      B    N  
ANISOU 1191  N   GLY B 576    18052   5730   5028   1221  -1305    -42  B    N  
ATOM   1192  CA  GLY B 576     -21.057  16.635 -52.485  1.00 78.68      B    C  
ANISOU 1192  CA  GLY B 576    19483   5673   4738   1474  -1148    -29  B    C  
ATOM   1193  C   GLY B 576     -20.529  15.219 -52.586  1.00 81.70      B    C  
ANISOU 1193  C   GLY B 576    20302   5885   4857   1664   -885    -75  B    C  
ATOM   1194  O   GLY B 576     -20.615  14.446 -51.625  1.00 81.79      B    O  
ANISOU 1194  O   GLY B 576    19788   6086   5203   1546   -954   -139  B    O  
ATOM   1195  N   LYS B 577     -19.953  14.874 -53.748  1.00 84.16      B    N  
ANISOU 1195  N   LYS B 577    21629   5813   4534   1997   -540    -30  B    N  
ATOM   1196  CA  LYS B 577     -19.427  13.525 -54.004  1.00 86.85      B    C  
ANISOU 1196  CA  LYS B 577    22605   5894   4499   2272   -236    -64  B    C  
ATOM   1197  C   LYS B 577     -18.138  13.230 -53.229  1.00 88.01      B    C  
ANISOU 1197  C   LYS B 577    22094   6386   4960   2488    606    116  B    C  
ATOM   1198  O   LYS B 577     -17.912  12.091 -52.810  1.00 88.37      B    O  
ANISOU 1198  O   LYS B 577    22169   6400   5007   2585    721     65  B    O  
ATOM   1199  CB  LYS B 577     -19.202  13.298 -55.504  1.00 90.36      B    C  
ANISOU 1199  CB  LYS B 577    24449   5779   4106   2637    -60    -47  B    C  
ATOM   1200  CG  LYS B 577     -20.376  13.727 -56.379  1.00 97.88      B    C  
ANISOU 1200  CG  LYS B 577    26114   6362   4714   2431   -902   -174  B    C  
ATOM   1201  CD  LYS B 577     -20.063  13.603 -57.888  1.00105.12      B    C  
ANISOU 1201  CD  LYS B 577    28524   6690   4726   2828   -678   -145  B    C  
ATOM   1202  CE  LYS B 577     -19.711  12.202 -58.320  1.00110.80      B    C  
ANISOU 1202  CE  LYS B 577    30278   6958   4861   3154   -472   -223  B    C  
ATOM   1203  NZ  LYS B 577     -19.462  12.116 -59.789  1.00116.15      B    N1+
ANISOU 1203  NZ  LYS B 577    32542   7005   4585   3574   -267   -200  B    N1+
ATOM   1204  N   GLU B 578     -17.280  14.248 -53.063  1.00 87.95      B    N  
ANISOU 1204  N   GLU B 578    21517   6682   5218   2554   1168    359  B    N  
ATOM   1205  CA  GLU B 578     -16.014  14.088 -52.347  1.00 87.99      B    C  
ANISOU 1205  CA  GLU B 578    20818   7027   5589   2718   1915    613  B    C  
ATOM   1206  C   GLU B 578     -15.963  15.141 -51.266  1.00 85.76      B    C  
ANISOU 1206  C   GLU B 578    19402   7206   5978   2356   1797    690  B    C  
ATOM   1207  O   GLU B 578     -15.576  16.284 -51.530  1.00 86.46      B    O  
ANISOU 1207  O   GLU B 578    19316   7384   6151   2321   2014    881  B    O  
ATOM   1208  CB  GLU B 578     -14.822  14.246 -53.314  1.00 92.73      B    C  
ANISOU 1208  CB  GLU B 578    21921   7483   5829   3191   2799    947  B    C  
ATOM   1209  CG  GLU B 578     -13.462  14.133 -52.640  1.00100.31      B    C  
ANISOU 1209  CG  GLU B 578    22074   8805   7234   3365   3576   1317  B    C  
ATOM   1210  CD  GLU B 578     -13.226  12.866 -51.846  1.00108.03      B    C  
ANISOU 1210  CD  GLU B 578    22793   9873   8380   3457   3651   1256  B    C  
ATOM   1211  OE1 GLU B 578     -12.960  11.817 -52.476  1.00111.23      B    O  
ANISOU 1211  OE1 GLU B 578    24018   9949   8294   3891   3995   1259  B    O  
ATOM   1212  OE2 GLU B 578     -13.287  12.924 -50.596  1.00109.60      B    O1-
ANISOU 1212  OE2 GLU B 578    22032  10443   9169   3120   3382   1214  B    O1-
ATOM   1213  N   ILE B 579     -16.426  14.784 -50.069  1.00 82.91      B    N  
ANISOU 1213  N   ILE B 579    18356   7091   6054   2078   1412    537  B    N  
ATOM   1214  CA  ILE B 579     -16.480  15.724 -48.961  1.00 80.67      B    C  
ANISOU 1214  CA  ILE B 579    17123   7185   6344   1749   1242    573  B    C  
ATOM   1215  C   ILE B 579     -15.108  15.947 -48.341  1.00 78.15      B    C  
ANISOU 1215  C   ILE B 579    16137   7163   6394   1800   1848    893  B    C  
ATOM   1216  O   ILE B 579     -14.450  15.003 -47.893  1.00 78.22      B    O  
ANISOU 1216  O   ILE B 579    15934   7269   6516   1945   2162    982  B    O  
ATOM   1217  CB  ILE B 579     -17.510  15.273 -47.890  1.00 81.03      B    C  
ANISOU 1217  CB  ILE B 579    16728   7363   6697   1468    641    323  B    C  
ATOM   1218  CG1 ILE B 579     -18.874  14.935 -48.518  1.00 81.93      B    C  
ANISOU 1218  CG1 ILE B 579    17435   7178   6516   1387     -8     92  B    C  
ATOM   1219  CG2 ILE B 579     -17.653  16.318 -46.786  1.00 81.28      B    C  
ANISOU 1219  CG2 ILE B 579    15945   7713   7223   1183    470    347  B    C  
ATOM   1220  CD1 ILE B 579     -19.830  14.243 -47.552  1.00 82.95      B    C  
ANISOU 1220  CD1 ILE B 579    17159   7412   6946   1154   -517    -73  B    C  
ATOM   1221  N   GLN B 580     -14.686  17.204 -48.304  1.00 75.59      B    N  
ANISOU 1221  N   GLN B 580    15476   6968   6278   1659   1969   1092  B    N  
ATOM   1222  CA  GLN B 580     -13.437  17.593 -47.672  1.00 73.58      B    C  
ANISOU 1222  CA  GLN B 580    14515   6989   6454   1597   2404   1452  B    C  
ATOM   1223  C   GLN B 580     -13.834  17.934 -46.241  1.00 69.74      B    C  
ANISOU 1223  C   GLN B 580    13326   6748   6423   1222   1930   1307  B    C  
ATOM   1224  O   GLN B 580     -14.326  19.033 -46.002  1.00 69.85      B    O  
ANISOU 1224  O   GLN B 580    13225   6773   6541    976   1588   1233  B    O  
ATOM   1225  CB  GLN B 580     -12.871  18.842 -48.377  1.00 76.27      B    C  
ANISOU 1225  CB  GLN B 580    14920   7285   6773   1574   2681   1749  B    C  
ATOM   1226  CG  GLN B 580     -11.465  19.214 -47.944  1.00 81.77      B    C  
ANISOU 1226  CG  GLN B 580    14927   8223   7920   1508   3160   2239  B    C  
ATOM   1227  CD  GLN B 580     -10.605  19.543 -49.135  1.00 89.55      B    C  
ANISOU 1227  CD  GLN B 580    16237   9085   8702   1791   3823   2652  B    C  
ATOM   1228  NE2 GLN B 580      -9.552  18.761 -49.337  1.00 90.70      B    N  
ANISOU 1228  NE2 GLN B 580    16240   9305   8917   2124   4492   3026  B    N  
ATOM   1229  OE1 GLN B 580     -10.871  20.494 -49.891  1.00 92.64      B    O  
ANISOU 1229  OE1 GLN B 580    17018   9309   8871   1748   3777   2669  B    O  
ATOM   1230  N   TRP B 581     -13.693  16.988 -45.310  1.00 66.48      B    N  
ANISOU 1230  N   TRP B 581    12535   6492   6231   1210   1904   1252  B    N  
ATOM   1231  CA  TRP B 581     -14.110  17.217 -43.930  1.00 64.00      B    C  
ANISOU 1231  CA  TRP B 581    11660   6374   6282    900   1477   1105  B    C  
ATOM   1232  C   TRP B 581     -13.230  18.169 -43.147  1.00 62.13      B    C  
ANISOU 1232  C   TRP B 581    10831   6325   6449    645   1525   1377  B    C  
ATOM   1233  O   TRP B 581     -12.012  18.176 -43.296  1.00 62.63      B    O  
ANISOU 1233  O   TRP B 581    10627   6480   6691    697   1945   1758  B    O  
ATOM   1234  CB  TRP B 581     -14.197  15.904 -43.139  1.00 63.31      B    C  
ANISOU 1234  CB  TRP B 581    11379   6382   6295    959   1432    980  B    C  
ATOM   1235  CG  TRP B 581     -15.288  14.965 -43.558  1.00 62.99      B    C  
ANISOU 1235  CG  TRP B 581    11845   6148   5940   1077   1173    676  B    C  
ATOM   1236  CD1 TRP B 581     -15.136  13.769 -44.190  1.00 63.89      B    C  
ANISOU 1236  CD1 TRP B 581    12417   6093   5767   1352   1393    655  B    C  
ATOM   1237  CD2 TRP B 581     -16.697  15.128 -43.340  1.00 62.07      B    C  
ANISOU 1237  CD2 TRP B 581    11825   5966   5791    909    615    393  B    C  
ATOM   1238  CE2 TRP B 581     -17.337  13.984 -43.855  1.00 63.00      B    C  
ANISOU 1238  CE2 TRP B 581    12418   5880   5639   1029    460    230  B    C  
ATOM   1239  CE3 TRP B 581     -17.485  16.157 -42.828  1.00 61.35      B    C  
ANISOU 1239  CE3 TRP B 581    11502   5942   5865    695    245    299  B    C  
ATOM   1240  NE1 TRP B 581     -16.365  13.188 -44.403  1.00 64.00      B    N  
ANISOU 1240  NE1 TRP B 581    12836   5915   5566   1304    934    367  B    N  
ATOM   1241  CZ2 TRP B 581     -18.721  13.829 -43.829  1.00 62.77      B    C  
ANISOU 1241  CZ2 TRP B 581    12523   5750   5579    887    -90     22  B    C  
ATOM   1242  CZ3 TRP B 581     -18.850  15.986 -42.776  1.00 61.69      B    C  
ANISOU 1242  CZ3 TRP B 581    11658   5908   5875    627   -215     96  B    C  
ATOM   1243  CH2 TRP B 581     -19.454  14.829 -43.260  1.00 62.17      B    C  
ANISOU 1243  CH2 TRP B 581    12080   5800   5739    697   -396    -18  B    C  
ATOM   1244  N   LYS B 582     -13.860  18.935 -42.267  1.00 59.76      B    N  
ANISOU 1244  N   LYS B 582    10335   6066   6306    372   1076   1208  B    N  
ATOM   1245  CA  LYS B 582     -13.212  19.790 -41.287  1.00 58.07      B    C  
ANISOU 1245  CA  LYS B 582     9657   5967   6442     70    947   1393  B    C  
ATOM   1246  C   LYS B 582     -13.777  19.356 -39.916  1.00 55.57      B    C  
ANISOU 1246  C   LYS B 582     9092   5750   6271    -43    598   1155  B    C  
ATOM   1247  O   LYS B 582     -14.946  18.981 -39.829  1.00 54.39      B    O  
ANISOU 1247  O   LYS B 582     9152   5553   5961     49    378    845  B    O  
ATOM   1248  CB  LYS B 582     -13.485  21.273 -41.560  1.00 60.42      B    C  
ANISOU 1248  CB  LYS B 582    10143   6126   6687   -111    745   1408  B    C  
ATOM   1249  CG  LYS B 582     -12.359  21.969 -42.323  1.00 66.14      B    C  
ANISOU 1249  CG  LYS B 582    10811   6821   7497   -174   1082   1830  B    C  
ATOM   1250  CD  LYS B 582     -12.374  21.666 -43.825  1.00 71.69      B    C  
ANISOU 1250  CD  LYS B 582    11981   7401   7858    147   1481   1888  B    C  
ATOM   1251  CE  LYS B 582     -11.218  22.316 -44.550  1.00 75.98      B    C  
ANISOU 1251  CE  LYS B 582    12433   7927   8508    119   1904   2370  B    C  
ATOM   1252  NZ  LYS B 582     -11.325  22.150 -46.026  1.00 78.38      B    N1+
ANISOU 1252  NZ  LYS B 582    13328   8060   8395    467   2303   2411  B    N1+
ATOM   1253  N   THR B 583     -12.946  19.348 -38.860  1.00 54.40      B    N  
ANISOU 1253  N   THR B 583     8502   5733   6436   -237    546   1337  B    N  
ATOM   1254  CA  THR B 583     -13.413  18.916 -37.539  1.00 53.80      B    C  
ANISOU 1254  CA  THR B 583     8256   5729   6456   -318    253   1133  B    C  
ATOM   1255  C   THR B 583     -13.322  20.029 -36.496  1.00 51.92      B    C  
ANISOU 1255  C   THR B 583     7945   5433   6349   -619   -107   1154  B    C  
ATOM   1256  O   THR B 583     -12.439  20.885 -36.563  1.00 52.89      B    O  
ANISOU 1256  O   THR B 583     7955   5513   6626   -847   -137   1439  B    O  
ATOM   1257  CB  THR B 583     -12.714  17.624 -37.083  1.00 56.04      B    C  
ANISOU 1257  CB  THR B 583     8214   6172   6905   -223    448   1252  B    C  
ATOM   1258  CG2 THR B 583     -12.777  16.517 -38.126  1.00 55.86      B    C  
ANISOU 1258  CG2 THR B 583     8401   6135   6689    105    811   1229  B    C  
ATOM   1259  OG1 THR B 583     -11.355  17.930 -36.794  1.00 58.80      B    O  
ANISOU 1259  OG1 THR B 583     8161   6614   7568   -401    538   1658  B    O  
ATOM   1260  N   HIS B 584     -14.266  20.035 -35.561  1.00 49.17      B    N  
ANISOU 1260  N   HIS B 584     7712   5049   5920   -611   -379    875  B    N  
ATOM   1261  CA  HIS B 584     -14.350  21.015 -34.489  1.00 48.07      B    C  
ANISOU 1261  CA  HIS B 584     7679   4786   5797   -820   -719    837  B    C  
ATOM   1262  C   HIS B 584     -14.583  20.238 -33.199  1.00 46.76      B    C  
ANISOU 1262  C   HIS B 584     7397   4694   5674   -794   -841    709  B    C  
ATOM   1263  O   HIS B 584     -15.473  19.391 -33.156  1.00 46.07      B    O  
ANISOU 1263  O   HIS B 584     7318   4682   5506   -570   -749    507  B    O  
ATOM   1264  CB  HIS B 584     -15.513  21.996 -34.741  1.00 48.68      B    C  
ANISOU 1264  CB  HIS B 584     8165   4688   5643   -721   -853    621  B    C  
ATOM   1265  CG  HIS B 584     -15.766  22.948 -33.612  1.00 51.79      B    C  
ANISOU 1265  CG  HIS B 584     8815   4898   5964   -836  -1158    542  B    C  
ATOM   1266  CD2 HIS B 584     -16.812  23.017 -32.753  1.00 52.94      B    C  
ANISOU 1266  CD2 HIS B 584     9175   4974   5967   -659  -1256    320  B    C  
ATOM   1267  ND1 HIS B 584     -14.871  23.956 -33.303  1.00 54.02      B    N  
ANISOU 1267  ND1 HIS B 584     9209   5011   6304  -1150  -1382    733  B    N  
ATOM   1268  CE1 HIS B 584     -15.397  24.605 -32.276  1.00 54.32      B    C  
ANISOU 1268  CE1 HIS B 584     9620   4844   6174  -1146  -1634    581  B    C  
ATOM   1269  NE2 HIS B 584     -16.560  24.073 -31.904  1.00 53.94      B    N  
ANISOU 1269  NE2 HIS B 584     9639   4859   5998   -821  -1521    339  B    N  
ATOM   1270  N   GLU B 585     -13.787  20.514 -32.166  1.00 46.32      B    N  
ANISOU 1270  N   GLU B 585     7253   4597   5749  -1041  -1078    852  B    N  
ATOM   1271  CA  GLU B 585     -13.876  19.824 -30.884  1.00 47.21      B    C  
ANISOU 1271  CA  GLU B 585     7310   4750   5877  -1032  -1213    761  B    C  
ATOM   1272  C   GLU B 585     -14.603  20.625 -29.809  1.00 47.11      B    C  
ANISOU 1272  C   GLU B 585     7738   4517   5644  -1040  -1490    568  B    C  
ATOM   1273  O   GLU B 585     -14.406  21.836 -29.711  1.00 47.67      B    O  
ANISOU 1273  O   GLU B 585     8116   4365   5632  -1220  -1725    618  B    O  
ATOM   1274  CB  GLU B 585     -12.471  19.411 -30.401  1.00 50.73      B    C  
ANISOU 1274  CB  GLU B 585     7379   5289   6607  -1271  -1311   1080  B    C  
ATOM   1275  CG  GLU B 585     -11.871  18.272 -31.217  1.00 57.89      B    C  
ANISOU 1275  CG  GLU B 585     7865   6429   7701  -1116   -932   1255  B    C  
ATOM   1276  CD  GLU B 585     -10.984  17.300 -30.454  1.00 66.96      B    C  
ANISOU 1276  CD  GLU B 585     8632   7721   9090  -1169   -960   1461  B    C  
ATOM   1277  OE1 GLU B 585      -9.795  17.636 -30.239  1.00 68.05      B    O  
ANISOU 1277  OE1 GLU B 585     8471   7875   9511  -1435  -1120   1839  B    O  
ATOM   1278  OE2 GLU B 585     -11.471  16.202 -30.077  1.00 67.55      B    O1-
ANISOU 1278  OE2 GLU B 585     8687   7885   9095   -957   -842   1280  B    O1-
ATOM   1279  N   VAL B 586     -15.474  19.971 -29.020  1.00 46.03      B    N  
ANISOU 1279  N   VAL B 586     7683   4415   5390   -820  -1436    364  B    N  
ATOM   1280  CA  VAL B 586     -16.197  20.638 -27.935  1.00 46.62      B    C  
ANISOU 1280  CA  VAL B 586     8227   4270   5218   -729  -1597    207  B    C  
ATOM   1281  C   VAL B 586     -15.912  19.932 -26.602  1.00 48.55      B    C  
ANISOU 1281  C   VAL B 586     8489   4515   5443   -757  -1715    202  B    C  
ATOM   1282  O   VAL B 586     -16.253  18.768 -26.464  1.00 47.65      B    O  
ANISOU 1282  O   VAL B 586     8104   4595   5405   -594  -1510    151  B    O  
ATOM   1283  CB  VAL B 586     -17.708  20.742 -28.230  1.00 46.98      B    C  
ANISOU 1283  CB  VAL B 586     8419   4314   5116   -372  -1373     17  B    C  
ATOM   1284  CG1 VAL B 586     -18.466  21.260 -27.010  1.00 47.56      B    C  
ANISOU 1284  CG1 VAL B 586     8959   4177   4933   -172  -1415    -99  B    C  
ATOM   1285  CG2 VAL B 586     -17.971  21.625 -29.455  1.00 47.50      B    C  
ANISOU 1285  CG2 VAL B 586     8574   4318   5156   -360  -1342     28  B    C  
ATOM   1286  N   PHE B 587     -15.288  20.623 -25.630  1.00 50.90      B    N  
ANISOU 1286  N   PHE B 587     9155   4564   5621   -980  -2080    263  B    N  
ATOM   1287  CA  PHE B 587     -14.897  20.000 -24.367  1.00 54.36      B    C  
ANISOU 1287  CA  PHE B 587     9673   4966   6015  -1040  -2261    284  B    C  
ATOM   1288  C   PHE B 587     -15.706  20.396 -23.113  1.00 58.26      B    C  
ANISOU 1288  C   PHE B 587    10845   5181   6111   -822  -2318    100  B    C  
ATOM   1289  O   PHE B 587     -15.299  19.992 -22.022  1.00 58.49      B    O  
ANISOU 1289  O   PHE B 587    11055   5120   6048   -897  -2524    126  B    O  
ATOM   1290  CB  PHE B 587     -13.402  20.210 -24.078  1.00 54.52      B    C  
ANISOU 1290  CB  PHE B 587     9573   4913   6229  -1492  -2704    563  B    C  
ATOM   1291  CG  PHE B 587     -12.497  19.768 -25.199  1.00 55.54      B    C  
ANISOU 1291  CG  PHE B 587     9016   5318   6767  -1651  -2572    826  B    C  
ATOM   1292  CD1 PHE B 587     -12.318  18.423 -25.475  1.00 56.30      B    C  
ANISOU 1292  CD1 PHE B 587     8591   5722   7079  -1501  -2274    881  B    C  
ATOM   1293  CD2 PHE B 587     -11.843  20.699 -25.992  1.00 56.75      B    C  
ANISOU 1293  CD2 PHE B 587     9093   5400   7068  -1915  -2702   1037  B    C  
ATOM   1294  CE1 PHE B 587     -11.504  18.016 -26.519  1.00 57.00      B    C  
ANISOU 1294  CE1 PHE B 587     8135   6030   7492  -1559  -2071   1139  B    C  
ATOM   1295  CE2 PHE B 587     -11.040  20.287 -27.046  1.00 57.43      B    C  
ANISOU 1295  CE2 PHE B 587     8575   5736   7511  -1988  -2478   1318  B    C  
ATOM   1296  CZ  PHE B 587     -10.873  18.944 -27.295  1.00 57.09      B    C  
ANISOU 1296  CZ  PHE B 587     8061   5986   7646  -1784  -2146   1366  B    C  
ATOM   1297  N   ASP B 588     -16.805  21.174 -23.230  1.00 60.57      B    N  
ANISOU 1297  N   ASP B 588    11540   5319   6156   -527  -2128    -55  B    N  
ATOM   1298  CA  ASP B 588     -17.649  21.409 -22.056  1.00 63.56      B    C  
ANISOU 1298  CA  ASP B 588    12545   5452   6151   -202  -2037   -189  B    C  
ATOM   1299  C   ASP B 588     -18.878  20.494 -22.193  1.00 64.87      B    C  
ANISOU 1299  C   ASP B 588    12348   5893   6407    214  -1526   -252  B    C  
ATOM   1300  O   ASP B 588     -19.466  20.360 -23.283  1.00 65.27      B    O  
ANISOU 1300  O   ASP B 588    11977   6157   6667    319  -1294   -250  B    O  
ATOM   1301  CB  ASP B 588     -17.980  22.888 -21.806  1.00 68.45      B    C  
ANISOU 1301  CB  ASP B 588    13957   5650   6400   -107  -2171   -262  B    C  
ATOM   1302  CG  ASP B 588     -18.874  23.509 -22.841  1.00 76.06      B    C  
ANISOU 1302  CG  ASP B 588    14817   6675   7407    144  -1878   -305  B    C  
ATOM   1303  OD1 ASP B 588     -18.786  23.103 -24.012  1.00 77.84      B    O  
ANISOU 1303  OD1 ASP B 588    14398   7208   7970     36  -1770   -248  B    O  
ATOM   1304  OD2 ASP B 588     -19.654  24.413 -22.481  1.00 79.38      B    O1-
ANISOU 1304  OD2 ASP B 588    15850   6809   7501    472  -1756   -382  B    O1-
ATOM   1305  N   ALA B 589     -19.178  19.760 -21.133  1.00 65.07      B    N  
ANISOU 1305  N   ALA B 589    12493   5918   6311    396  -1395   -272  B    N  
ATOM   1306  CA  ALA B 589     -20.244  18.767 -21.149  1.00 65.64      B    C  
ANISOU 1306  CA  ALA B 589    12168   6248   6524    721   -953   -266  B    C  
ATOM   1307  C   ALA B 589     -21.657  19.335 -21.355  1.00 65.80      B    C  
ANISOU 1307  C   ALA B 589    12304   6231   6466   1154   -582   -264  B    C  
ATOM   1308  O   ALA B 589     -22.524  18.638 -21.903  1.00 66.53      B    O  
ANISOU 1308  O   ALA B 589    11867   6586   6824   1315   -299   -197  B    O  
ATOM   1309  CB  ALA B 589     -20.186  17.945 -19.879  1.00 65.88      B    C  
ANISOU 1309  CB  ALA B 589    12369   6247   6416    811   -899   -255  B    C  
ATOM   1310  N   LYS B 590     -21.875  20.589 -20.937  1.00 64.82      B    N  
ANISOU 1310  N   LYS B 590    12872   5764   5993   1334   -610   -308  B    N  
ATOM   1311  CA  LYS B 590     -23.164  21.280 -21.042  1.00 65.06      B    C  
ANISOU 1311  CA  LYS B 590    13082   5715   5924   1811   -238   -264  B    C  
ATOM   1312  C   LYS B 590     -23.480  21.918 -22.403  1.00 64.15      B    C  
ANISOU 1312  C   LYS B 590    12672   5690   6013   1774   -267   -248  B    C  
ATOM   1313  O   LYS B 590     -24.571  22.466 -22.554  1.00 64.63      B    O  
ANISOU 1313  O   LYS B 590    12807   5707   6042   2179     28   -172  B    O  
ATOM   1314  CB  LYS B 590     -23.285  22.360 -19.960  1.00 67.72      B    C  
ANISOU 1314  CB  LYS B 590    14424   5580   5725   2098   -216   -317  B    C  
ATOM   1315  CG  LYS B 590     -23.542  21.812 -18.563  1.00 74.11      B    C  
ANISOU 1315  CG  LYS B 590    15637   6266   6255   2379     16   -292  B    C  
ATOM   1316  CD  LYS B 590     -23.797  22.963 -17.574  1.00 80.66      B    C  
ANISOU 1316  CD  LYS B 590    17618   6559   6471   2751     86   -344  B    C  
ATOM   1317  CE  LYS B 590     -23.872  22.501 -16.137  1.00 86.35      B    C  
ANISOU 1317  CE  LYS B 590    18928   7074   6809   3014    267   -333  B    C  
ATOM   1318  NZ  LYS B 590     -24.002  23.650 -15.199  1.00 90.22      B    N1+
ANISOU 1318  NZ  LYS B 590    20710   6958   6611   3371    287   -405  B    N1+
ATOM   1319  N   SER B 591     -22.538  21.914 -23.357  1.00 62.69      B    N  
ANISOU 1319  N   SER B 591    12200   5604   6014   1331   -599   -288  B    N  
ATOM   1320  CA  SER B 591     -22.792  22.520 -24.670  1.00 61.66      B    C  
ANISOU 1320  CA  SER B 591    11862   5532   6032   1295   -632   -272  B    C  
ATOM   1321  C   SER B 591     -23.685  21.668 -25.537  1.00 58.69      B    C  
ANISOU 1321  C   SER B 591    10809   5490   6001   1415   -418   -187  B    C  
ATOM   1322  O   SER B 591     -23.428  20.482 -25.718  1.00 58.35      B    O  
ANISOU 1322  O   SER B 591    10302   5687   6182   1239   -427   -171  B    O  
ATOM   1323  CB  SER B 591     -21.499  22.791 -25.427  1.00 63.38      B    C  
ANISOU 1323  CB  SER B 591    12013   5737   6332    814   -994   -292  B    C  
ATOM   1324  OG  SER B 591     -21.207  24.177 -25.398  1.00 66.83      B    O  
ANISOU 1324  OG  SER B 591    13053   5828   6512    760  -1198   -320  B    O  
ATOM   1325  N   LYS B 592     -24.730  22.281 -26.073  1.00 56.21      B    N  
ANISOU 1325  N   LYS B 592    10470   5160   5725   1709   -264   -113  B    N  
ATOM   1326  CA  LYS B 592     -25.630  21.620 -27.010  1.00 55.02      B    C  
ANISOU 1326  CA  LYS B 592     9715   5276   5912   1779   -175      7  B    C  
ATOM   1327  C   LYS B 592     -25.512  22.252 -28.422  1.00 52.43      B    C  
ANISOU 1327  C   LYS B 592     9344   4937   5642   1629   -381    -14  B    C  
ATOM   1328  O   LYS B 592     -26.311  21.919 -29.286  1.00 51.20      B    O  
ANISOU 1328  O   LYS B 592     8804   4932   5717   1689   -386     91  B    O  
ATOM   1329  CB  LYS B 592     -27.078  21.737 -26.526  1.00 58.20      B    C  
ANISOU 1329  CB  LYS B 592    10018   5701   6394   2268    166    204  B    C  
ATOM   1330  CG  LYS B 592     -27.389  20.886 -25.307  1.00 64.63      B    C  
ANISOU 1330  CG  LYS B 592    10748   6586   7223   2441    438    289  B    C  
ATOM   1331  CD  LYS B 592     -28.794  21.186 -24.779  1.00 71.04      B    C  
ANISOU 1331  CD  LYS B 592    11488   7395   8110   2992    862    559  B    C  
ATOM   1332  CE  LYS B 592     -29.871  20.866 -25.791  1.00 75.84      B    C  
ANISOU 1332  CE  LYS B 592    11410   8240   9166   3040    849    809  B    C  
ATOM   1333  NZ  LYS B 592     -31.227  20.910 -25.182  1.00 79.14      B    N1+
ANISOU 1333  NZ  LYS B 592    11571   8722   9778   3559   1298   1179  B    N1+
ATOM   1334  N   SER B 593     -24.554  23.182 -28.641  1.00 51.48      B    N  
ANISOU 1334  N   SER B 593     9638   4611   5311   1426   -574   -118  B    N  
ATOM   1335  CA  SER B 593     -24.372  23.851 -29.917  1.00 51.32      B    C  
ANISOU 1335  CA  SER B 593     9646   4548   5304   1293   -735   -122  B    C  
ATOM   1336  C   SER B 593     -22.962  24.403 -30.116  1.00 50.45      B    C  
ANISOU 1336  C   SER B 593     9815   4291   5065    918   -959   -186  B    C  
ATOM   1337  O   SER B 593     -22.248  24.651 -29.142  1.00 50.52      B    O  
ANISOU 1337  O   SER B 593    10135   4139   4920    797  -1049   -223  B    O  
ATOM   1338  CB  SER B 593     -25.413  24.960 -30.104  1.00 53.16      B    C  
ANISOU 1338  CB  SER B 593    10131   4620   5446   1659   -645    -54  B    C  
ATOM   1339  OG  SER B 593     -25.439  25.854 -29.006  1.00 56.79      B    O  
ANISOU 1339  OG  SER B 593    11168   4795   5615   1884   -549    -87  B    O  
ATOM   1340  N   ALA B 594     -22.582  24.629 -31.393  1.00 49.19      B    N  
ANISOU 1340  N   ALA B 594     9560   4162   4967    731  -1064   -161  B    N  
ATOM   1341  CA  ALA B 594     -21.323  25.243 -31.795  1.00 48.61      B    C  
ANISOU 1341  CA  ALA B 594     9674   3962   4835    385  -1236   -133  B    C  
ATOM   1342  C   ALA B 594     -21.555  26.191 -32.981  1.00 48.91      B    C  
ANISOU 1342  C   ALA B 594     9890   3885   4808    408  -1284    -99  B    C  
ATOM   1343  O   ALA B 594     -22.455  25.951 -33.791  1.00 48.76      B    O  
ANISOU 1343  O   ALA B 594     9700   3973   4854    604  -1216    -92  B    O  
ATOM   1344  CB  ALA B 594     -20.317  24.185 -32.187  1.00 48.48      B    C  
ANISOU 1344  CB  ALA B 594     9259   4160   5002    107  -1227    -76  B    C  
ATOM   1345  N   SER B 595     -20.728  27.241 -33.103  1.00 48.75      B    N  
ANISOU 1345  N   SER B 595    10217   3632   4672    177  -1440    -50  B    N  
ATOM   1346  CA  SER B 595     -20.801  28.193 -34.213  1.00 50.35      B    C  
ANISOU 1346  CA  SER B 595    10637   3696   4796    162  -1488      2  B    C  
ATOM   1347  C   SER B 595     -19.501  28.114 -34.978  1.00 50.80      B    C  
ANISOU 1347  C   SER B 595    10540   3801   4960   -220  -1524    147  B    C  
ATOM   1348  O   SER B 595     -18.428  28.167 -34.378  1.00 51.26      B    O  
ANISOU 1348  O   SER B 595    10584   3807   5085   -529  -1643    244  B    O  
ATOM   1349  CB  SER B 595     -21.011  29.609 -33.702  1.00 53.19      B    C  
ANISOU 1349  CB  SER B 595    11605   3687   4916    243  -1620    -23  B    C  
ATOM   1350  OG  SER B 595     -22.399  29.852 -33.576  1.00 57.31      B    O  
ANISOU 1350  OG  SER B 595    12242   4179   5356    708  -1489    -83  B    O  
ATOM   1351  N   LEU B 596     -19.590  27.925 -36.288  1.00 50.22      B    N  
ANISOU 1351  N   LEU B 596    10340   3828   4915   -188  -1415    198  B    N  
ATOM   1352  CA  LEU B 596     -18.424  27.715 -37.131  1.00 50.72      B    C  
ANISOU 1352  CA  LEU B 596    10233   3962   5076   -454  -1324    381  B    C  
ATOM   1353  C   LEU B 596     -18.363  28.710 -38.288  1.00 52.22      B    C  
ANISOU 1353  C   LEU B 596    10715   3982   5143   -487  -1321    481  B    C  
ATOM   1354  O   LEU B 596     -19.371  28.927 -38.960  1.00 52.30      B    O  
ANISOU 1354  O   LEU B 596    10903   3949   5019   -234  -1325    384  B    O  
ATOM   1355  CB  LEU B 596     -18.470  26.267 -37.678  1.00 50.36      B    C  
ANISOU 1355  CB  LEU B 596     9821   4188   5125   -346  -1119    364  B    C  
ATOM   1356  CG  LEU B 596     -18.663  25.174 -36.607  1.00 51.53      B    C  
ANISOU 1356  CG  LEU B 596     9678   4511   5392   -287  -1108    262  B    C  
ATOM   1357  CD1 LEU B 596     -19.173  23.875 -37.199  1.00 51.62      B    C  
ANISOU 1357  CD1 LEU B 596     9472   4708   5433   -117   -976    195  B    C  
ATOM   1358  CD2 LEU B 596     -17.411  25.012 -35.775  1.00 52.29      B    C  
ANISOU 1358  CD2 LEU B 596     9589   4639   5639   -566  -1139    402  B    C  
ATOM   1359  N   LEU B 597     -17.182  29.303 -38.532  1.00 53.28      B    N  
ANISOU 1359  N   LEU B 597    10878   4019   5349   -808  -1327    714  B    N  
ATOM   1360  CA  LEU B 597     -16.994  30.212 -39.660  1.00 55.71      B    C  
ANISOU 1360  CA  LEU B 597    11455   4163   5550   -865  -1284    855  B    C  
ATOM   1361  C   LEU B 597     -16.842  29.437 -40.969  1.00 56.79      B    C  
ANISOU 1361  C   LEU B 597    11450   4465   5662   -737   -980    939  B    C  
ATOM   1362  O   LEU B 597     -15.940  28.611 -41.096  1.00 57.04      B    O  
ANISOU 1362  O   LEU B 597    11144   4675   5852   -830   -756   1108  B    O  
ATOM   1363  CB  LEU B 597     -15.734  31.037 -39.462  1.00 56.99      B    C  
ANISOU 1363  CB  LEU B 597    11639   4167   5848  -1288  -1387   1149  B    C  
ATOM   1364  CG  LEU B 597     -15.864  32.286 -38.645  1.00 59.40      B    C  
ANISOU 1364  CG  LEU B 597    12391   4133   6048  -1447  -1743   1107  B    C  
ATOM   1365  CD1 LEU B 597     -14.509  32.848 -38.383  1.00 60.78      B    C  
ANISOU 1365  CD1 LEU B 597    12485   4175   6434  -1954  -1918   1451  B    C  
ATOM   1366  CD2 LEU B 597     -16.690  33.322 -39.375  1.00 60.28      B    C  
ANISOU 1366  CD2 LEU B 597    13003   4001   5899  -1253  -1780   1018  B    C  
ATOM   1367  N   VAL B 598     -17.727  29.697 -41.936  1.00 57.18      B    N  
ANISOU 1367  N   VAL B 598    11806   4429   5492   -500   -977    839  B    N  
ATOM   1368  CA  VAL B 598     -17.698  29.087 -43.266  1.00 57.68      B    C  
ANISOU 1368  CA  VAL B 598    11943   4552   5421   -352   -742    898  B    C  
ATOM   1369  C   VAL B 598     -17.563  30.173 -44.344  1.00 59.15      B    C  
ANISOU 1369  C   VAL B 598    12539   4514   5420   -376   -702   1045  B    C  
ATOM   1370  O   VAL B 598     -17.997  31.316 -44.155  1.00 58.59      B    O  
ANISOU 1370  O   VAL B 598    12742   4241   5278   -404   -926   1005  B    O  
ATOM   1371  CB  VAL B 598     -18.876  28.118 -43.537  1.00 57.82      B    C  
ANISOU 1371  CB  VAL B 598    11972   4665   5331    -62   -828    663  B    C  
ATOM   1372  CG1 VAL B 598     -18.943  27.029 -42.480  1.00 58.19      B    C  
ANISOU 1372  CG1 VAL B 598    11615   4923   5570    -58   -836    553  B    C  
ATOM   1373  CG2 VAL B 598     -20.201  28.860 -43.641  1.00 58.18      B    C  
ANISOU 1373  CG2 VAL B 598    12281   4569   5255    123  -1120    519  B    C  
ATOM   1374  N   SER B 599     -16.939  29.821 -45.465  1.00 60.62      B    N  
ANISOU 1374  N   SER B 599    12816   4714   5503   -338   -386   1231  B    N  
ATOM   1375  CA  SER B 599     -16.656  30.774 -46.514  1.00 62.68      B    C  
ANISOU 1375  CA  SER B 599    13463   4768   5585   -366   -275   1423  B    C  
ATOM   1376  C   SER B 599     -17.811  31.038 -47.507  1.00 63.50      B    C  
ANISOU 1376  C   SER B 599    14078   4704   5343    -95   -445   1248  B    C  
ATOM   1377  O   SER B 599     -17.819  32.095 -48.140  1.00 64.76      B    O  
ANISOU 1377  O   SER B 599    14605   4649   5353   -123   -477   1354  B    O  
ATOM   1378  CB  SER B 599     -15.390  30.360 -47.255  1.00 66.11      B    C  
ANISOU 1378  CB  SER B 599    13791   5270   6056   -411    214   1773  B    C  
ATOM   1379  OG  SER B 599     -14.452  31.427 -47.250  1.00 70.98      B    O  
ANISOU 1379  OG  SER B 599    14343   5780   6845   -716    297   2119  B    O  
ATOM   1380  N   ASP B 600     -18.769  30.113 -47.656  1.00 62.81      B    N  
ANISOU 1380  N   ASP B 600    14024   4693   5147    138   -595   1016  B    N  
ATOM   1381  CA  ASP B 600     -19.881  30.297 -48.602  1.00 62.73      B    C  
ANISOU 1381  CA  ASP B 600    14467   4518   4848    360   -849    897  B    C  
ATOM   1382  C   ASP B 600     -21.189  30.109 -47.855  1.00 61.50      B    C  
ANISOU 1382  C   ASP B 600    14108   4435   4824    477  -1248    675  B    C  
ATOM   1383  O   ASP B 600     -21.516  28.985 -47.485  1.00 61.19      B    O  
ANISOU 1383  O   ASP B 600    13802   4560   4887    525  -1302    563  B    O  
ATOM   1384  CB  ASP B 600     -19.784  29.268 -49.754  1.00 65.17      B    C  
ANISOU 1384  CB  ASP B 600    15102   4791   4867    524   -686    909  B    C  
ATOM   1385  CG  ASP B 600     -20.794  29.458 -50.877  1.00 71.18      B    C  
ANISOU 1385  CG  ASP B 600    16432   5328   5285    710  -1000    831  B    C  
ATOM   1386  OD1 ASP B 600     -21.599  30.413 -50.800  1.00 72.19      B    O  
ANISOU 1386  OD1 ASP B 600    16637   5356   5436    736  -1326    790  B    O  
ATOM   1387  OD2 ASP B 600     -20.765  28.660 -51.846  1.00 74.45      B    O1-
ANISOU 1387  OD2 ASP B 600    17267   5636   5385    846   -930    828  B    O1-
ATOM   1388  N   LEU B 601     -21.952  31.187 -47.664  1.00 60.57      B    N  
ANISOU 1388  N   LEU B 601    14121   4184   4707    551  -1503    645  B    N  
ATOM   1389  CA  LEU B 601     -23.193  31.129 -46.897  1.00 60.95      B    C  
ANISOU 1389  CA  LEU B 601    13930   4305   4924    718  -1803    516  B    C  
ATOM   1390  C   LEU B 601     -24.400  30.535 -47.637  1.00 61.62      B    C  
ANISOU 1390  C   LEU B 601    14088   4384   4941    910  -2128    476  B    C  
ATOM   1391  O   LEU B 601     -25.420  30.228 -47.009  1.00 61.89      B    O  
ANISOU 1391  O   LEU B 601    13796   4530   5191   1040  -2348    437  B    O  
ATOM   1392  CB  LEU B 601     -23.542  32.514 -46.348  1.00 61.01      B    C  
ANISOU 1392  CB  LEU B 601    14075   4150   4958    786  -1902    535  B    C  
ATOM   1393  CG  LEU B 601     -22.458  33.220 -45.537  1.00 62.28      B    C  
ANISOU 1393  CG  LEU B 601    14245   4237   5180    547  -1719    588  B    C  
ATOM   1394  CD1 LEU B 601     -22.938  34.572 -45.095  1.00 63.05      B    C  
ANISOU 1394  CD1 LEU B 601    14644   4092   5221    658  -1863    588  B    C  
ATOM   1395  CD2 LEU B 601     -22.055  32.401 -44.319  1.00 62.92      B    C  
ANISOU 1395  CD2 LEU B 601    13887   4530   5490    433  -1622    518  B    C  
ATOM   1396  N   SER B 602     -24.287  30.341 -48.942  1.00 61.88      B    N  
ANISOU 1396  N   SER B 602    14552   4274   4683    921  -2172    520  B    N  
ATOM   1397  CA  SER B 602     -25.388  29.803 -49.736  1.00 62.49      B    C  
ANISOU 1397  CA  SER B 602    14799   4281   4662   1046  -2589    508  B    C  
ATOM   1398  C   SER B 602     -25.243  28.344 -50.137  1.00 62.91      B    C  
ANISOU 1398  C   SER B 602    14911   4379   4614    987  -2615    446  B    C  
ATOM   1399  O   SER B 602     -26.101  27.847 -50.867  1.00 64.64      B    O  
ANISOU 1399  O   SER B 602    15368   4479   4713   1035  -3036    449  B    O  
ATOM   1400  CB  SER B 602     -25.612  30.663 -50.972  1.00 63.98      B    C  
ANISOU 1400  CB  SER B 602    15587   4194   4528   1134  -2756    595  B    C  
ATOM   1401  OG  SER B 602     -26.274  31.858 -50.601  1.00 66.80      B    O  
ANISOU 1401  OG  SER B 602    15868   4495   5019   1259  -2910    651  B    O  
ATOM   1402  N   ALA B 603     -24.174  27.659 -49.702  1.00 60.60      B    N  
ANISOU 1402  N   ALA B 603    14447   4220   4357    884  -2211    410  B    N  
ATOM   1403  CA  ALA B 603     -23.986  26.263 -50.086  1.00 59.34      B    C  
ANISOU 1403  CA  ALA B 603    14423   4063   4062    871  -2194    351  B    C  
ATOM   1404  C   ALA B 603     -24.608  25.314 -49.051  1.00 56.62      B    C  
ANISOU 1404  C   ALA B 603    13518   3932   4062    819  -2385    266  B    C  
ATOM   1405  O   ALA B 603     -24.880  25.714 -47.913  1.00 55.36      B    O  
ANISOU 1405  O   ALA B 603    12840   3955   4240    806  -2367    262  B    O  
ATOM   1406  CB  ALA B 603     -22.502  25.969 -50.257  1.00 59.89      B    C  
ANISOU 1406  CB  ALA B 603    14616   4153   3988    845  -1613    414  B    C  
ATOM   1407  N   VAL B 604     -24.886  24.079 -49.460  1.00 55.21      B    N  
ANISOU 1407  N   VAL B 604    13513   3693   3773    801  -2582    211  B    N  
ATOM   1408  CA  VAL B 604     -25.420  23.074 -48.551  1.00 54.60      B    C  
ANISOU 1408  CA  VAL B 604    12938   3796   4011    727  -2751    159  B    C  
ATOM   1409  C   VAL B 604     -24.251  22.436 -47.821  1.00 53.29      B    C  
ANISOU 1409  C   VAL B 604    12531   3802   3916    688  -2249    109  B    C  
ATOM   1410  O   VAL B 604     -23.365  21.897 -48.477  1.00 54.53      B    O  
ANISOU 1410  O   VAL B 604    13088   3850   3782    730  -1963    106  B    O  
ATOM   1411  CB  VAL B 604     -26.220  21.979 -49.316  1.00 56.23      B    C  
ANISOU 1411  CB  VAL B 604    13488   3811   4065    674  -3256    143  B    C  
ATOM   1412  CG1 VAL B 604     -26.659  20.867 -48.364  1.00 56.96      B    C  
ANISOU 1412  CG1 VAL B 604    13066   4080   4495    565  -3388    118  B    C  
ATOM   1413  CG2 VAL B 604     -27.420  22.589 -50.031  1.00 57.95      B    C  
ANISOU 1413  CG2 VAL B 604    13886   3862   4271    684  -3846    250  B    C  
ATOM   1414  N   TYR B 605     -24.245  22.451 -46.484  1.00 50.36      B    N  
ANISOU 1414  N   TYR B 605    11543   3680   3912    639  -2131     93  B    N  
ATOM   1415  CA  TYR B 605     -23.203  21.768 -45.710  1.00 48.85      B    C  
ANISOU 1415  CA  TYR B 605    11081   3655   3825    586  -1735     65  B    C  
ATOM   1416  C   TYR B 605     -23.779  20.522 -45.084  1.00 47.76      B    C  
ANISOU 1416  C   TYR B 605    10650   3621   3875    542  -1918      1  B    C  
ATOM   1417  O   TYR B 605     -24.963  20.477 -44.749  1.00 47.95      B    O  
ANISOU 1417  O   TYR B 605    10431   3682   4107    528  -2282     16  B    O  
ATOM   1418  CB  TYR B 605     -22.626  22.652 -44.561  1.00 48.02      B    C  
ANISOU 1418  CB  TYR B 605    10565   3718   3963    531  -1487    100  B    C  
ATOM   1419  CG  TYR B 605     -21.826  23.815 -45.086  1.00 47.70      B    C  
ANISOU 1419  CG  TYR B 605    10783   3569   3772    512  -1275    201  B    C  
ATOM   1420  CD1 TYR B 605     -22.454  24.916 -45.633  1.00 48.01      B    C  
ANISOU 1420  CD1 TYR B 605    11084   3454   3704    569  -1481    227  B    C  
ATOM   1421  CD2 TYR B 605     -20.438  23.786 -45.093  1.00 48.37      B    C  
ANISOU 1421  CD2 TYR B 605    10841   3694   3841    436   -870    319  B    C  
ATOM   1422  CE1 TYR B 605     -21.733  25.977 -46.151  1.00 49.01      B    C  
ANISOU 1422  CE1 TYR B 605    11482   3455   3687    532  -1297    338  B    C  
ATOM   1423  CE2 TYR B 605     -19.700  24.846 -45.620  1.00 48.88      B    C  
ANISOU 1423  CE2 TYR B 605    11115   3650   3806    384   -679    476  B    C  
ATOM   1424  CZ  TYR B 605     -20.357  25.944 -46.142  1.00 49.90      B    C  
ANISOU 1424  CZ  TYR B 605    11547   3609   3803    423   -897    470  B    C  
ATOM   1425  OH  TYR B 605     -19.682  27.009 -46.703  1.00 51.29      B    O  
ANISOU 1425  OH  TYR B 605    11969   3648   3869    359   -727    636  B    O  
ATOM   1426  N   VAL B 606     -22.942  19.498 -44.954  1.00 46.73      B    N  
ANISOU 1426  N   VAL B 606    10535   3532   3689    531  -1649    -31  B    N  
ATOM   1427  CA  VAL B 606     -23.296  18.263 -44.264  1.00 46.66      B    C  
ANISOU 1427  CA  VAL B 606    10256   3618   3856    476  -1759    -87  B    C  
ATOM   1428  C   VAL B 606     -22.536  18.264 -42.933  1.00 44.18      B    C  
ANISOU 1428  C   VAL B 606     9428   3553   3806    442  -1421    -80  B    C  
ATOM   1429  O   VAL B 606     -21.392  18.716 -42.863  1.00 44.01      B    O  
ANISOU 1429  O   VAL B 606     9396   3578   3746    450  -1065    -19  B    O  
ATOM   1430  CB  VAL B 606     -23.050  16.983 -45.101  1.00 49.10      B    C  
ANISOU 1430  CB  VAL B 606    11059   3728   3870    511  -1775   -134  B    C  
ATOM   1431  CG1 VAL B 606     -21.614  16.915 -45.613  1.00 50.43      B    C  
ANISOU 1431  CG1 VAL B 606    11532   3848   3780    651  -1232    -86  B    C  
ATOM   1432  CG2 VAL B 606     -23.414  15.731 -44.309  1.00 49.65      B    C  
ANISOU 1432  CG2 VAL B 606    10842   3880   4142    426  -1906   -182  B    C  
ATOM   1433  N   VAL B 607     -23.202  17.844 -41.862  1.00 42.26      B    N  
ANISOU 1433  N   VAL B 607     8753   3458   3844    394  -1559   -104  B    N  
ATOM   1434  CA  VAL B 607     -22.647  17.853 -40.521  1.00 41.13      B    C  
ANISOU 1434  CA  VAL B 607     8187   3517   3924    364  -1320   -104  B    C  
ATOM   1435  C   VAL B 607     -22.967  16.540 -39.805  1.00 40.34      B    C  
ANISOU 1435  C   VAL B 607     7836   3509   3981    328  -1373   -138  B    C  
ATOM   1436  O   VAL B 607     -24.075  16.013 -39.947  1.00 40.77      B    O  
ANISOU 1436  O   VAL B 607     7851   3521   4120    303  -1684   -126  B    O  
ATOM   1437  CB  VAL B 607     -23.292  19.027 -39.731  1.00 41.67      B    C  
ANISOU 1437  CB  VAL B 607     8029   3647   4158    397  -1404    -79  B    C  
ATOM   1438  CG1 VAL B 607     -22.847  19.022 -38.278  1.00 42.74      B    C  
ANISOU 1438  CG1 VAL B 607     7840   3932   4467    373  -1224    -89  B    C  
ATOM   1439  CG2 VAL B 607     -22.998  20.387 -40.381  1.00 41.88      B    C  
ANISOU 1439  CG2 VAL B 607     8331   3552   4029    419  -1374    -43  B    C  
ATOM   1440  N   GLN B 608     -22.001  16.013 -39.039  1.00 38.55      B    N  
ANISOU 1440  N   GLN B 608     7425   3402   3821    309  -1100   -143  B    N  
ATOM   1441  CA  GLN B 608     -22.177  14.861 -38.156  1.00 37.50      B    C  
ANISOU 1441  CA  GLN B 608     7032   3368   3847    279  -1104   -167  B    C  
ATOM   1442  C   GLN B 608     -21.498  15.179 -36.830  1.00 36.22      B    C  
ANISOU 1442  C   GLN B 608     6548   3371   3842    258   -900   -147  B    C  
ATOM   1443  O   GLN B 608     -20.518  15.915 -36.782  1.00 35.82      B    O  
ANISOU 1443  O   GLN B 608     6517   3337   3755    231   -734    -98  B    O  
ATOM   1444  CB  GLN B 608     -21.595  13.568 -38.745  1.00 38.77      B    C  
ANISOU 1444  CB  GLN B 608     7439   3438   3854    302  -1007   -190  B    C  
ATOM   1445  CG  GLN B 608     -22.384  13.024 -39.927  1.00 42.00      B    C  
ANISOU 1445  CG  GLN B 608     8280   3614   4066    295  -1309   -224  B    C  
ATOM   1446  CD  GLN B 608     -21.713  11.800 -40.487  1.00 46.58      B    C  
ANISOU 1446  CD  GLN B 608     9243   4039   4414    369  -1169   -257  B    C  
ATOM   1447  NE2 GLN B 608     -22.399  10.665 -40.461  1.00 45.91      B    N  
ANISOU 1447  NE2 GLN B 608     9265   3837   4342    287  -1446   -294  B    N  
ATOM   1448  OE1 GLN B 608     -20.582  11.858 -40.954  1.00 48.95      B    O  
ANISOU 1448  OE1 GLN B 608     9762   4308   4530    513   -801   -218  B    O  
ATOM   1449  N   VAL B 609     -22.027  14.626 -35.748  1.00 34.33      B    N  
ANISOU 1449  N   VAL B 609     6034   3232   3778    252   -942   -158  B    N  
ATOM   1450  CA  VAL B 609     -21.493  14.807 -34.423  1.00 32.77      B    C  
ANISOU 1450  CA  VAL B 609     5621   3148   3683    237   -805   -147  B    C  
ATOM   1451  C   VAL B 609     -21.318  13.416 -33.765  1.00 32.56      B    C  
ANISOU 1451  C   VAL B 609     5426   3199   3747    221   -741   -153  B    C  
ATOM   1452  O   VAL B 609     -22.145  12.512 -33.952  1.00 32.64      B    O  
ANISOU 1452  O   VAL B 609     5406   3185   3811    220   -860   -159  B    O  
ATOM   1453  CB  VAL B 609     -22.439  15.702 -33.561  1.00 33.16      B    C  
ANISOU 1453  CB  VAL B 609     5579   3210   3810    318   -870   -136  B    C  
ATOM   1454  CG1 VAL B 609     -21.821  16.008 -32.190  1.00 32.92      B    C  
ANISOU 1454  CG1 VAL B 609     5495   3221   3792    308   -762   -140  B    C  
ATOM   1455  CG2 VAL B 609     -22.788  16.999 -34.284  1.00 34.32      B    C  
ANISOU 1455  CG2 VAL B 609     5923   3253   3865    366   -955   -126  B    C  
ATOM   1456  N   ARG B 610     -20.228  13.241 -33.045  1.00 31.57      B    N  
ANISOU 1456  N   ARG B 610     5201   3146   3648    185   -592   -124  B    N  
ATOM   1457  CA  ARG B 610     -19.991  12.024 -32.276  1.00 31.88      B    C  
ANISOU 1457  CA  ARG B 610     5086   3257   3771    186   -526   -120  B    C  
ATOM   1458  C   ARG B 610     -19.499  12.446 -30.876  1.00 31.51      B    C  
ANISOU 1458  C   ARG B 610     4906   3281   3786    149   -500    -90  B    C  
ATOM   1459  O   ARG B 610     -19.152  13.620 -30.656  1.00 31.68      B    O  
ANISOU 1459  O   ARG B 610     5001   3267   3767    101   -543    -68  B    O  
ATOM   1460  CB  ARG B 610     -19.042  11.041 -32.986  1.00 32.66      B    C  
ANISOU 1460  CB  ARG B 610     5265   3333   3810    217   -377    -82  B    C  
ATOM   1461  CG  ARG B 610     -17.609  11.528 -33.082  1.00 35.29      B    C  
ANISOU 1461  CG  ARG B 610     5537   3715   4157    203   -202     50  B    C  
ATOM   1462  CD  ARG B 610     -16.722  10.399 -33.514  1.00 36.95      B    C  
ANISOU 1462  CD  ARG B 610     5766   3925   4348    317     25    139  B    C  
ATOM   1463  NE  ARG B 610     -15.335  10.821 -33.647  1.00 40.27      B    N  
ANISOU 1463  NE  ARG B 610     6029   4416   4856    323    231    362  B    N  
ATOM   1464  CZ  ARG B 610     -14.326  10.000 -33.936  1.00 44.89      B    C  
ANISOU 1464  CZ  ARG B 610     6546   5031   5478    474    510    535  B    C  
ATOM   1465  NH1 ARG B 610     -14.548   8.705 -34.138  1.00 45.77      B    N1+
ANISOU 1465  NH1 ARG B 610     6836   5070   5485    639    606    459  B    N1+
ATOM   1466  NH2 ARG B 610     -13.089  10.470 -34.038  1.00 44.68      B    N  
ANISOU 1466  NH2 ARG B 610     6276   5092   5608    469    699    822  B    N  
ATOM   1467  N   CYS B 611     -19.566  11.535 -29.916  1.00 30.54      B    N  
ANISOU 1467  N   CYS B 611     4657   3216   3731    165   -470    -89  B    N  
ATOM   1468  CA  CYS B 611     -19.246  11.861 -28.544  1.00 30.72      B    C  
ANISOU 1468  CA  CYS B 611     4654   3261   3759    145   -487    -69  B    C  
ATOM   1469  C   CYS B 611     -18.468  10.756 -27.828  1.00 30.71      B    C  
ANISOU 1469  C   CYS B 611     4524   3324   3820    122   -439    -18  B    C  
ATOM   1470  O   CYS B 611     -18.433   9.610 -28.277  1.00 30.09      B    O  
ANISOU 1470  O   CYS B 611     4376   3272   3787    158   -361    -14  B    O  
ATOM   1471  CB  CYS B 611     -20.522  12.231 -27.795  1.00 31.37      B    C  
ANISOU 1471  CB  CYS B 611     4783   3315   3822    261   -488   -102  B    C  
ATOM   1472  SG  CYS B 611     -21.612  10.829 -27.452  1.00 33.76      B    S  
ANISOU 1472  SG  CYS B 611     4889   3680   4257    334   -416    -68  B    S  
ATOM   1473  N   ARG B 612     -17.813  11.122 -26.746  1.00 30.53      B    N  
ANISOU 1473  N   ARG B 612     4527   3293   3779     59   -518     28  B    N  
ATOM   1474  CA  ARG B 612     -17.013  10.214 -25.945  1.00 31.61      B    C  
ANISOU 1474  CA  ARG B 612     4549   3482   3978     31   -524    105  B    C  
ATOM   1475  C   ARG B 612     -16.936  10.813 -24.546  1.00 33.68      B    C  
ANISOU 1475  C   ARG B 612     5000   3663   4133    -13   -682    106  B    C  
ATOM   1476  O   ARG B 612     -16.982  12.032 -24.398  1.00 34.16      B    O  
ANISOU 1476  O   ARG B 612     5280   3614   4087    -66   -808     86  B    O  
ATOM   1477  CB  ARG B 612     -15.592  10.164 -26.530  1.00 33.46      B    C  
ANISOU 1477  CB  ARG B 612     4607   3772   4334    -58   -521    272  B    C  
ATOM   1478  CG  ARG B 612     -14.681   9.122 -25.922  1.00 37.68      B    C  
ANISOU 1478  CG  ARG B 612     4954   4378   4984    -50   -507    407  B    C  
ATOM   1479  CD  ARG B 612     -13.245   9.287 -26.370  1.00 41.89      B    C  
ANISOU 1479  CD  ARG B 612     5238   4979   5700   -123   -496    669  B    C  
ATOM   1480  NE  ARG B 612     -12.445   8.129 -25.974  1.00 46.79      B    N  
ANISOU 1480  NE  ARG B 612     5639   5680   6459    -43   -425    831  B    N  
ATOM   1481  CZ  ARG B 612     -11.150   7.978 -26.255  1.00 50.99      B    C  
ANISOU 1481  CZ  ARG B 612     5856   6302   7217    -42   -358   1144  B    C  
ATOM   1482  NH1 ARG B 612     -10.498   8.908 -26.947  1.00 49.42      B    N1+
ANISOU 1482  NH1 ARG B 612     5512   6125   7142   -145   -346   1341  B    N1+
ATOM   1483  NH2 ARG B 612     -10.499   6.895 -25.848  1.00 52.32      B    N  
ANISOU 1483  NH2 ARG B 612     5829   6538   7513     75   -284   1303  B    N  
ATOM   1484  N   ARG B 613     -16.700   9.987 -23.506  1.00 33.84      B    N  
ANISOU 1484  N   ARG B 613     5011   3697   4148      6   -703    139  B    N  
ATOM   1485  CA  ARG B 613     -16.499  10.516 -22.161  1.00 34.23      B    C  
ANISOU 1485  CA  ARG B 613     5352   3617   4035    -35   -892    148  B    C  
ATOM   1486  C   ARG B 613     -15.334  11.500 -22.148  1.00 36.30      B    C  
ANISOU 1486  C   ARG B 613     5679   3796   4315   -268  -1200    264  B    C  
ATOM   1487  O   ARG B 613     -14.323  11.264 -22.817  1.00 36.07      B    O  
ANISOU 1487  O   ARG B 613     5325   3874   4506   -392  -1238    424  B    O  
ATOM   1488  CB  ARG B 613     -16.268   9.390 -21.163  1.00 33.25      B    C  
ANISOU 1488  CB  ARG B 613     5205   3519   3908      6   -889    193  B    C  
ATOM   1489  CG  ARG B 613     -17.586   8.878 -20.631  1.00 33.91      B    C  
ANISOU 1489  CG  ARG B 613     5403   3591   3892    213   -648    108  B    C  
ATOM   1490  CD  ARG B 613     -17.418   7.630 -19.795  1.00 35.44      B    C  
ANISOU 1490  CD  ARG B 613     5554   3815   4098    258   -603    160  B    C  
ATOM   1491  NE  ARG B 613     -16.612   7.868 -18.588  1.00 35.99      B    N  
ANISOU 1491  NE  ARG B 613     5909   3761   4004    189   -856    215  B    N  
ATOM   1492  CZ  ARG B 613     -16.523   7.007 -17.579  1.00 37.94      B    C  
ANISOU 1492  CZ  ARG B 613     6263   3979   4175    248   -853    258  B    C  
ATOM   1493  NH1 ARG B 613     -17.206   5.868 -17.605  1.00 36.72      B    N1+
ANISOU 1493  NH1 ARG B 613     5935   3910   4105    372   -585    259  B    N1+
ATOM   1494  NH2 ARG B 613     -15.764   7.285 -16.529  1.00 37.99      B    N  
ANISOU 1494  NH2 ARG B 613     6586   3840   4010    163  -1157    316  B    N  
ATOM   1495  N   LEU B 614     -15.534  12.649 -21.486  1.00 37.81      B    N  
ANISOU 1495  N   LEU B 614     6307   3777   4280   -312  -1394    210  B    N  
ATOM   1496  CA  LEU B 614     -14.535  13.695 -21.359  1.00 39.90      B    C  
ANISOU 1496  CA  LEU B 614     6731   3890   4537   -590  -1778    331  B    C  
ATOM   1497  C   LEU B 614     -13.269  13.156 -20.701  1.00 41.40      B    C  
ANISOU 1497  C   LEU B 614     6749   4101   4879   -807  -2087    546  B    C  
ATOM   1498  O   LEU B 614     -12.179  13.552 -21.088  1.00 43.07      B    O  
ANISOU 1498  O   LEU B 614     6717   4331   5316  -1072  -2332    776  B    O  
ATOM   1499  CB  LEU B 614     -15.119  14.845 -20.536  1.00 40.77      B    C  
ANISOU 1499  CB  LEU B 614     7513   3694   4282   -542  -1935    205  B    C  
ATOM   1500  CG  LEU B 614     -14.270  16.108 -20.397  1.00 43.50      B    C  
ANISOU 1500  CG  LEU B 614     8186   3788   4555   -858  -2400    306  B    C  
ATOM   1501  CD1 LEU B 614     -13.888  16.675 -21.773  1.00 43.95      B    C  
ANISOU 1501  CD1 LEU B 614     7883   3952   4862  -1016  -2370    408  B    C  
ATOM   1502  CD2 LEU B 614     -15.020  17.156 -19.589  1.00 44.37      B    C  
ANISOU 1502  CD2 LEU B 614     9102   3541   4217   -713  -2481    141  B    C  
ATOM   1503  N   ASP B 615     -13.400  12.214 -19.757  1.00 40.81      B    N  
ANISOU 1503  N   ASP B 615     6745   4038   4723   -693  -2063    518  B    N  
ATOM   1504  CA  ASP B 615     -12.238  11.613 -19.112  1.00 40.78      B    C  
ANISOU 1504  CA  ASP B 615     6558   4059   4876   -872  -2369    743  B    C  
ATOM   1505  C   ASP B 615     -11.519  10.551 -19.978  1.00 40.99      B    C  
ANISOU 1505  C   ASP B 615     5910   4373   5292   -839  -2152    937  B    C  
ATOM   1506  O   ASP B 615     -10.568   9.950 -19.509  1.00 40.92      B    O  
ANISOU 1506  O   ASP B 615     5668   4418   5463   -932  -2351   1164  B    O  
ATOM   1507  CB  ASP B 615     -12.622  11.029 -17.733  1.00 41.42      B    C  
ANISOU 1507  CB  ASP B 615     7045   4010   4682   -745  -2432    650  B    C  
ATOM   1508  CG  ASP B 615     -13.562   9.828 -17.757  1.00 43.90      B    C  
ANISOU 1508  CG  ASP B 615     7217   4482   4981   -433  -1960    516  B    C  
ATOM   1509  OD1 ASP B 615     -13.813   9.288 -18.858  1.00 43.75      B    O  
ANISOU 1509  OD1 ASP B 615     6771   4670   5181   -337  -1638    500  B    O  
ATOM   1510  OD2 ASP B 615     -14.037   9.415 -16.664  1.00 44.97      B    O1-
ANISOU 1510  OD2 ASP B 615     7711   4504   4870   -294  -1930    445  B    O1-
ATOM   1511  N   GLY B 616     -12.022  10.282 -21.186  1.00 40.93      B    N  
ANISOU 1511  N   GLY B 616     5658   4518   5376   -671  -1746    851  B    N  
ATOM   1512  CA  GLY B 616     -11.447   9.300 -22.094  1.00 41.08      B    C  
ANISOU 1512  CA  GLY B 616     5193   4746   5671   -562  -1471   1007  B    C  
ATOM   1513  C   GLY B 616     -11.680   7.841 -21.735  1.00 40.97      B    C  
ANISOU 1513  C   GLY B 616     5104   4809   5653   -352  -1267    959  B    C  
ATOM   1514  O   GLY B 616     -11.129   6.961 -22.407  1.00 42.06      B    O  
ANISOU 1514  O   GLY B 616     4922   5075   5982   -224  -1040   1101  B    O  
ATOM   1515  N   LEU B 617     -12.466   7.547 -20.669  1.00 39.46      B    N  
ANISOU 1515  N   LEU B 617     5239   4521   5234   -288  -1317    785  B    N  
ATOM   1516  CA  LEU B 617     -12.728   6.156 -20.263  1.00 38.97      B    C  
ANISOU 1516  CA  LEU B 617     5134   4508   5166   -114  -1137    754  B    C  
ATOM   1517  C   LEU B 617     -13.949   5.593 -20.979  1.00 38.45      B    C  
ANISOU 1517  C   LEU B 617     5106   4468   5036     61   -791    555  B    C  
ATOM   1518  O   LEU B 617     -15.030   5.416 -20.390  1.00 38.74      B    O  
ANISOU 1518  O   LEU B 617     5363   4441   4914    138   -707    416  B    O  
ATOM   1519  CB  LEU B 617     -12.859   5.997 -18.740  1.00 39.24      B    C  
ANISOU 1519  CB  LEU B 617     5489   4418   5005   -132  -1350    731  B    C  
ATOM   1520  CG  LEU B 617     -11.600   6.372 -17.970  1.00 42.51      B    C  
ANISOU 1520  CG  LEU B 617     5891   4770   5490   -343  -1803    964  B    C  
ATOM   1521  CD1 LEU B 617     -11.846   6.407 -16.451  1.00 43.50      B    C  
ANISOU 1521  CD1 LEU B 617     6526   4695   5309   -360  -2059    904  B    C  
ATOM   1522  CD2 LEU B 617     -10.456   5.421 -18.305  1.00 43.58      B    C  
ANISOU 1522  CD2 LEU B 617     5533   5068   5956   -316  -1787   1241  B    C  
ATOM   1523  N   GLY B 618     -13.744   5.271 -22.244  1.00 36.55      B    N  
ANISOU 1523  N   GLY B 618     4657   4304   4926    125   -597    586  B    N  
ATOM   1524  CA  GLY B 618     -14.779   4.722 -23.093  1.00 35.30      B    C  
ANISOU 1524  CA  GLY B 618     4562   4130   4719    239   -367    432  B    C  
ATOM   1525  C   GLY B 618     -14.455   4.883 -24.567  1.00 34.06      B    C  
ANISOU 1525  C   GLY B 618     4320   3996   4624    283   -225    462  B    C  
ATOM   1526  O   GLY B 618     -13.399   5.419 -24.935  1.00 34.86      B    O  
ANISOU 1526  O   GLY B 618     4255   4153   4836    244   -241    633  B    O  
ATOM   1527  N   TYR B 619     -15.372   4.428 -25.416  1.00 31.72      B    N  
ANISOU 1527  N   TYR B 619     4156   3639   4257    353   -101    329  B    N  
ATOM   1528  CA  TYR B 619     -15.219   4.504 -26.859  1.00 31.09      B    C  
ANISOU 1528  CA  TYR B 619     4139   3523   4150    424     34    330  B    C  
ATOM   1529  C   TYR B 619     -15.924   5.731 -27.393  1.00 30.54      B    C  
ANISOU 1529  C   TYR B 619     4151   3434   4021    330    -54    232  B    C  
ATOM   1530  O   TYR B 619     -16.811   6.291 -26.748  1.00 30.29      B    O  
ANISOU 1530  O   TYR B 619     4152   3396   3960    254   -179    144  B    O  
ATOM   1531  CB  TYR B 619     -15.832   3.247 -27.543  1.00 30.88      B    C  
ANISOU 1531  CB  TYR B 619     4334   3366   4031    533    130    241  B    C  
ATOM   1532  CG  TYR B 619     -15.147   1.956 -27.179  1.00 32.43      B    C  
ANISOU 1532  CG  TYR B 619     4530   3539   4254    675    253    333  B    C  
ATOM   1533  CD1 TYR B 619     -13.898   1.634 -27.703  1.00 33.95      B    C  
ANISOU 1533  CD1 TYR B 619     4668   3751   4482    871    476    510  B    C  
ATOM   1534  CD2 TYR B 619     -15.726   1.067 -26.285  1.00 32.96      B    C  
ANISOU 1534  CD2 TYR B 619     4635   3564   4325    641    178    285  B    C  
ATOM   1535  CE1 TYR B 619     -13.263   0.438 -27.367  1.00 35.57      B    C  
ANISOU 1535  CE1 TYR B 619     4877   3924   4713   1054    613    621  B    C  
ATOM   1536  CE2 TYR B 619     -15.104  -0.128 -25.947  1.00 34.13      B    C  
ANISOU 1536  CE2 TYR B 619     4816   3668   4483    783    284    371  B    C  
ATOM   1537  CZ  TYR B 619     -13.860  -0.427 -26.463  1.00 36.52      B    C  
ANISOU 1537  CZ  TYR B 619     5073   3987   4815    998    493    534  B    C  
ATOM   1538  OH  TYR B 619     -13.278  -1.636 -26.149  1.00 39.68      B    O  
ANISOU 1538  OH  TYR B 619     5526   4328   5223   1189    621    636  B    O  
ATOM   1539  N   TRP B 620     -15.568   6.113 -28.610  1.00 30.93      B    N  
ANISOU 1539  N   TRP B 620     4264   3455   4032    376     48    266  B    N  
ATOM   1540  CA  TRP B 620     -16.280   7.161 -29.321  1.00 31.64      B    C  
ANISOU 1540  CA  TRP B 620     4478   3499   4045    311    -30    173  B    C  
ATOM   1541  C   TRP B 620     -17.586   6.514 -29.780  1.00 31.02      B    C  
ANISOU 1541  C   TRP B 620     4590   3312   3884    327   -103     31  B    C  
ATOM   1542  O   TRP B 620     -17.590   5.355 -30.206  1.00 30.30      B    O  
ANISOU 1542  O   TRP B 620     4648   3129   3738    405    -42     18  B    O  
ATOM   1543  CB  TRP B 620     -15.500   7.574 -30.589  1.00 32.20      B    C  
ANISOU 1543  CB  TRP B 620     4618   3544   4072    382    135    274  B    C  
ATOM   1544  CG  TRP B 620     -14.418   8.587 -30.337  1.00 33.93      B    C  
ANISOU 1544  CG  TRP B 620     4611   3858   4424    287    137    467  B    C  
ATOM   1545  CD1 TRP B 620     -13.076   8.353 -30.262  1.00 35.36      B    C  
ANISOU 1545  CD1 TRP B 620     4542   4126   4767    330    285    732  B    C  
ATOM   1546  CD2 TRP B 620     -14.600   9.984 -30.057  1.00 34.07      B    C  
ANISOU 1546  CD2 TRP B 620     4624   3870   4450    112    -57    450  B    C  
ATOM   1547  CE2 TRP B 620     -13.323  10.543 -29.858  1.00 35.44      B    C  
ANISOU 1547  CE2 TRP B 620     4564   4108   4793      1    -68    708  B    C  
ATOM   1548  CE3 TRP B 620     -15.717  10.826 -30.004  1.00 34.38      B    C  
ANISOU 1548  CE3 TRP B 620     4844   3840   4380     54   -218    274  B    C  
ATOM   1549  NE1 TRP B 620     -12.409   9.527 -29.986  1.00 35.93      B    N  
ANISOU 1549  NE1 TRP B 620     4426   4248   4979    137    148    903  B    N  
ATOM   1550  CZ2 TRP B 620     -13.136  11.903 -29.568  1.00 36.64      B    C  
ANISOU 1550  CZ2 TRP B 620     4727   4220   4975   -212   -288    763  B    C  
ATOM   1551  CZ3 TRP B 620     -15.533  12.167 -29.692  1.00 35.61      B    C  
ANISOU 1551  CZ3 TRP B 620     5034   3960   4538    -89   -375    311  B    C  
ATOM   1552  CH2 TRP B 620     -14.257  12.695 -29.492  1.00 36.13      B    C  
ANISOU 1552  CH2 TRP B 620     4937   4053   4738   -241   -431    537  B    C  
ATOM   1553  N   SER B 621     -18.681   7.271 -29.760  1.00 30.42      B    N  
ANISOU 1553  N   SER B 621     4530   3221   3807    255   -250    -44  B    N  
ATOM   1554  CA  SER B 621     -19.931   6.806 -30.335  1.00 31.09      B    C  
ANISOU 1554  CA  SER B 621     4730   3204   3879    225   -388   -102  B    C  
ATOM   1555  C   SER B 621     -19.748   6.767 -31.863  1.00 32.37      B    C  
ANISOU 1555  C   SER B 621     5192   3225   3882    263   -397   -133  B    C  
ATOM   1556  O   SER B 621     -18.808   7.379 -32.406  1.00 32.92      B    O  
ANISOU 1556  O   SER B 621     5324   3311   3873    329   -248    -96  B    O  
ATOM   1557  CB  SER B 621     -21.040   7.809 -30.018  1.00 31.75      B    C  
ANISOU 1557  CB  SER B 621     4703   3324   4035    187   -506   -102  B    C  
ATOM   1558  OG  SER B 621     -20.883   9.042 -30.712  1.00 32.35      B    O  
ANISOU 1558  OG  SER B 621     4872   3386   4035    196   -526   -122  B    O  
ATOM   1559  N   ASN B 622     -20.687   6.123 -32.586  1.00 32.59      B    N  
ANISOU 1559  N   ASN B 622     5435   3090   3857    209   -597   -171  B    N  
ATOM   1560  CA  ASN B 622     -20.733   6.270 -34.042  1.00 33.60      B    C  
ANISOU 1560  CA  ASN B 622     5957   3032   3775    238   -677   -212  B    C  
ATOM   1561  C   ASN B 622     -21.095   7.736 -34.339  1.00 34.45      B    C  
ANISOU 1561  C   ASN B 622     5975   3208   3907    208   -749   -208  B    C  
ATOM   1562  O   ASN B 622     -21.631   8.470 -33.470  1.00 33.80      B    O  
ANISOU 1562  O   ASN B 622     5574   3268   4000    162   -793   -179  B    O  
ATOM   1563  CB  ASN B 622     -21.836   5.387 -34.640  1.00 35.30      B    C  
ANISOU 1563  CB  ASN B 622     6442   3022   3947    113  -1019   -233  B    C  
ATOM   1564  CG  ASN B 622     -21.529   3.932 -34.572  1.00 39.01      B    C  
ANISOU 1564  CG  ASN B 622     7159   3337   4328    141   -990   -250  B    C  
ATOM   1565  ND2 ASN B 622     -22.570   3.091 -34.483  1.00 40.81      B    N  
ANISOU 1565  ND2 ASN B 622     7436   3421   4648    -51  -1325   -218  B    N  
ATOM   1566  OD1 ASN B 622     -20.363   3.542 -34.612  1.00 39.11      B    O  
ANISOU 1566  OD1 ASN B 622     7310   3345   4206    335   -672   -256  B    O  
ATOM   1567  N   TRP B 623     -20.792   8.182 -35.557  1.00 35.33      B    N  
ANISOU 1567  N   TRP B 623     6422   3193   3808    269   -731   -228  B    N  
ATOM   1568  CA  TRP B 623     -21.169   9.507 -35.996  1.00 35.94      B    C  
ANISOU 1568  CA  TRP B 623     6493   3288   3874    245   -824   -224  B    C  
ATOM   1569  C   TRP B 623     -22.707   9.520 -36.104  1.00 36.58      B    C  
ANISOU 1569  C   TRP B 623     6521   3306   4070    125  -1208   -213  B    C  
ATOM   1570  O   TRP B 623     -23.315   8.521 -36.519  1.00 36.37      B    O  
ANISOU 1570  O   TRP B 623     6686   3118   4014     41  -1454   -212  B    O  
ATOM   1571  CB  TRP B 623     -20.545   9.778 -37.391  1.00 36.36      B    C  
ANISOU 1571  CB  TRP B 623     7000   3175   3640    349   -714   -227  B    C  
ATOM   1572  CG  TRP B 623     -19.071  10.070 -37.358  1.00 37.25      B    C  
ANISOU 1572  CG  TRP B 623     7050   3382   3720    472   -307   -134  B    C  
ATOM   1573  CD1 TRP B 623     -18.050   9.219 -37.695  1.00 38.67      B    C  
ANISOU 1573  CD1 TRP B 623     7406   3507   3780    643      4    -64  B    C  
ATOM   1574  CD2 TRP B 623     -18.452  11.282 -36.898  1.00 36.56      B    C  
ANISOU 1574  CD2 TRP B 623     6671   3453   3766    427   -181    -45  B    C  
ATOM   1575  CE2 TRP B 623     -17.057  11.118 -37.028  1.00 37.36      B    C  
ANISOU 1575  CE2 TRP B 623     6717   3608   3871    533    175    116  B    C  
ATOM   1576  CE3 TRP B 623     -18.947  12.517 -36.439  1.00 36.28      B    C  
ANISOU 1576  CE3 TRP B 623     6458   3488   3839    316   -343    -61  B    C  
ATOM   1577  NE1 TRP B 623     -16.835   9.850 -37.508  1.00 38.79      B    N  
ANISOU 1577  NE1 TRP B 623     7167   3672   3900    701    324    109  B    N  
ATOM   1578  CZ2 TRP B 623     -16.152  12.126 -36.677  1.00 37.28      B    C  
ANISOU 1578  CZ2 TRP B 623     6425   3725   4014    457    302    282  B    C  
ATOM   1579  CZ3 TRP B 623     -18.048  13.524 -36.122  1.00 36.72      B    C  
ANISOU 1579  CZ3 TRP B 623     6355   3625   3972    261   -213     51  B    C  
ATOM   1580  CH2 TRP B 623     -16.669  13.315 -36.212  1.00 36.71      B    C  
ANISOU 1580  CH2 TRP B 623     6247   3683   4018    294     70    229  B    C  
ATOM   1581  N   SER B 624     -23.328  10.628 -35.729  1.00 37.03      B    N  
ANISOU 1581  N   SER B 624     6330   3471   4271    120  -1272   -168  B    N  
ATOM   1582  CA  SER B 624     -24.775  10.778 -35.836  1.00 38.40      B    C  
ANISOU 1582  CA  SER B 624     6354   3618   4620     50  -1598    -73  B    C  
ATOM   1583  C   SER B 624     -25.215  10.709 -37.306  1.00 41.86      B    C  
ANISOU 1583  C   SER B 624     7199   3823   4882    -19  -1931    -77  B    C  
ATOM   1584  O   SER B 624     -24.384  10.891 -38.206  1.00 41.85      B    O  
ANISOU 1584  O   SER B 624     7618   3698   4585     47  -1823   -168  B    O  
ATOM   1585  CB  SER B 624     -25.193  12.126 -35.253  1.00 37.71      B    C  
ANISOU 1585  CB  SER B 624     6009   3661   4659    149  -1516    -13  B    C  
ATOM   1586  OG  SER B 624     -24.706  13.204 -36.035  1.00 36.23      B    O  
ANISOU 1586  OG  SER B 624     6080   3408   4278    204  -1479    -70  B    O  
ATOM   1587  N   SER B 625     -26.527  10.496 -37.563  1.00 44.44      B    N  
ANISOU 1587  N   SER B 625     7407   4080   5398   -147  -2346     61  B    N  
ATOM   1588  CA  SER B 625     -27.014  10.521 -38.934  1.00 48.31      B    C  
ANISOU 1588  CA  SER B 625     8324   4317   5714   -240  -2763     77  B    C  
ATOM   1589  C   SER B 625     -26.857  11.960 -39.471  1.00 49.19      B    C  
ANISOU 1589  C   SER B 625     8539   4450   5700   -104  -2678     53  B    C  
ATOM   1590  O   SER B 625     -26.942  12.931 -38.703  1.00 49.60      B    O  
ANISOU 1590  O   SER B 625     8217   4702   5925     12  -2459     99  B    O  
ATOM   1591  CB  SER B 625     -28.436   9.974 -39.051  1.00 53.24      B    C  
ANISOU 1591  CB  SER B 625     8735   4860   6634   -459  -3302    297  B    C  
ATOM   1592  OG  SER B 625     -29.349  10.684 -38.231  1.00 59.92      B    O  
ANISOU 1592  OG  SER B 625     8937   5942   7887   -402  -3271    515  B    O  
ATOM   1593  N   PRO B 626     -26.384  12.090 -40.714  1.00 49.06      B    N  
ANISOU 1593  N   PRO B 626     9119   4207   5314    -80  -2752    -42  B    N  
ATOM   1594  CA  PRO B 626     -26.061  13.428 -41.230  1.00 49.16      B    C  
ANISOU 1594  CA  PRO B 626     9276   4226   5176     48  -2614    -65  B    C  
ATOM   1595  C   PRO B 626     -27.176  14.450 -41.152  1.00 49.92      B    C  
ANISOU 1595  C   PRO B 626     9059   4394   5515     60  -2866     80  B    C  
ATOM   1596  O   PRO B 626     -28.344  14.118 -41.338  1.00 50.83      B    O  
ANISOU 1596  O   PRO B 626     9021   4454   5840    -58  -3315    237  B    O  
ATOM   1597  CB  PRO B 626     -25.682  13.178 -42.692  1.00 49.79      B    C  
ANISOU 1597  CB  PRO B 626    10112   3992   4814     63  -2743   -141  B    C  
ATOM   1598  CG  PRO B 626     -25.322  11.742 -42.769  1.00 50.38      B    C  
ANISOU 1598  CG  PRO B 626    10483   3919   4740     20  -2741   -209  B    C  
ATOM   1599  CD  PRO B 626     -26.118  11.033 -41.705  1.00 48.76      B    C  
ANISOU 1599  CD  PRO B 626     9729   3859   4939   -141  -2940   -123  B    C  
ATOM   1600  N   ALA B 627     -26.801  15.698 -40.891  1.00 48.99      B    N  
ANISOU 1600  N   ALA B 627     8852   4381   5379    202  -2590     61  B    N  
ATOM   1601  CA  ALA B 627     -27.711  16.840 -40.902  1.00 49.67      B    C  
ANISOU 1601  CA  ALA B 627     8745   4502   5626    293  -2748    192  B    C  
ATOM   1602  C   ALA B 627     -27.261  17.737 -42.052  1.00 50.22      B    C  
ANISOU 1602  C   ALA B 627     9321   4395   5364    344  -2768    131  B    C  
ATOM   1603  O   ALA B 627     -26.060  17.869 -42.302  1.00 49.62      B    O  
ANISOU 1603  O   ALA B 627     9543   4281   5028    366  -2444     12  B    O  
ATOM   1604  CB  ALA B 627     -27.631  17.606 -39.586  1.00 49.10      B    C  
ANISOU 1604  CB  ALA B 627     8273   4635   5747    442  -2396    214  B    C  
ATOM   1605  N   TYR B 628     -28.213  18.342 -42.765  1.00 51.47      B    N  
ANISOU 1605  N   TYR B 628     9560   4446   5550    367  -3141    253  B    N  
ATOM   1606  CA  TYR B 628     -27.888  19.194 -43.892  1.00 53.06      B    C  
ANISOU 1606  CA  TYR B 628    10280   4457   5423    420  -3190    213  B    C  
ATOM   1607  C   TYR B 628     -28.484  20.591 -43.679  1.00 53.48      B    C  
ANISOU 1607  C   TYR B 628    10138   4562   5621    581  -3202    325  B    C  
ATOM   1608  O   TYR B 628     -29.551  20.721 -43.068  1.00 53.22      B    O  
ANISOU 1608  O   TYR B 628     9633   4646   5941    654  -3360    500  B    O  
ATOM   1609  CB  TYR B 628     -28.443  18.583 -45.200  1.00 54.25      B    C  
ANISOU 1609  CB  TYR B 628    10912   4334   5365    302  -3716    250  B    C  
ATOM   1610  CG  TYR B 628     -27.962  17.176 -45.472  1.00 56.01      B    C  
ANISOU 1610  CG  TYR B 628    11461   4429   5392    176  -3745    143  B    C  
ATOM   1611  CD1 TYR B 628     -28.589  16.083 -44.892  1.00 57.77      B    C  
ANISOU 1611  CD1 TYR B 628    11350   4706   5894     22  -3997    213  B    C  
ATOM   1612  CD2 TYR B 628     -26.868  16.940 -46.292  1.00 56.92      B    C  
ANISOU 1612  CD2 TYR B 628    12233   4354   5040    240  -3478      2  B    C  
ATOM   1613  CE1 TYR B 628     -28.127  14.789 -45.102  1.00 59.01      B    C  
ANISOU 1613  CE1 TYR B 628    11865   4709   5846    -77  -4015    107  B    C  
ATOM   1614  CE2 TYR B 628     -26.385  15.652 -46.496  1.00 58.12      B    C  
ANISOU 1614  CE2 TYR B 628    12738   4364   4982    198  -3432    -89  B    C  
ATOM   1615  CZ  TYR B 628     -27.028  14.577 -45.909  1.00 60.04      B    C  
ANISOU 1615  CZ  TYR B 628    12693   4637   5481     32  -3728    -54  B    C  
ATOM   1616  OH  TYR B 628     -26.569  13.290 -46.087  1.00 62.87      B    O  
ANISOU 1616  OH  TYR B 628    13453   4819   5615     -1  -3695   -148  B    O  
ATOM   1617  N   THR B 629     -27.814  21.618 -44.189  1.00 54.12      B    N  
ANISOU 1617  N   THR B 629    10585   4540   5438    656  -3016    262  B    N  
ATOM   1618  CA  THR B 629     -28.370  22.971 -44.125  1.00 56.53      B    C  
ANISOU 1618  CA  THR B 629    10831   4828   5819    824  -3055    362  B    C  
ATOM   1619  C   THR B 629     -29.344  23.167 -45.294  1.00 61.66      B    C  
ANISOU 1619  C   THR B 629    11712   5300   6415    836  -3570    499  B    C  
ATOM   1620  O   THR B 629     -29.233  22.467 -46.314  1.00 62.64      B    O  
ANISOU 1620  O   THR B 629    12258   5248   6294    700  -3834    459  B    O  
ATOM   1621  CB  THR B 629     -27.271  24.014 -44.206  1.00 55.23      B    C  
ANISOU 1621  CB  THR B 629    10987   4592   5406    857  -2699    268  B    C  
ATOM   1622  CG2 THR B 629     -26.381  24.031 -42.972  1.00 54.93      B    C  
ANISOU 1622  CG2 THR B 629    10705   4704   5462    825  -2292    186  B    C  
ATOM   1623  OG1 THR B 629     -26.503  23.783 -45.381  1.00 54.21      B    O  
ANISOU 1623  OG1 THR B 629    11379   4295   4925    765  -2676    209  B    O  
ATOM   1624  N   LEU B 630     -30.295  24.113 -45.172  1.00 64.46      B    N  
ANISOU 1624  N   LEU B 630    11848   5669   6975   1018  -3727    678  B    N  
ATOM   1625  CA  LEU B 630     -31.204  24.394 -46.289  1.00 67.75      B    C  
ANISOU 1625  CA  LEU B 630    12466   5912   7363   1031  -4261    848  B    C  
ATOM   1626  C   LEU B 630     -30.886  25.746 -46.923  1.00 69.27      B    C  
ANISOU 1626  C   LEU B 630    13114   5935   7271   1174  -4174    819  B    C  
ATOM   1627  O   LEU B 630     -30.063  26.501 -46.381  1.00 70.46      B    O  
ANISOU 1627  O   LEU B 630    13342   6114   7315   1259  -3716    701  B    O  
ATOM   1628  CB  LEU B 630     -32.685  24.287 -45.895  1.00 69.51      B    C  
ANISOU 1628  CB  LEU B 630    12059   6261   8089   1124  -4615   1174  B    C  
ATOM   1629  CG  LEU B 630     -33.226  25.364 -44.962  1.00 72.69      B    C  
ANISOU 1629  CG  LEU B 630    12053   6800   8766   1470  -4323   1338  B    C  
ATOM   1630  CD1 LEU B 630     -34.236  26.228 -45.663  1.00 73.83      B    C  
ANISOU 1630  CD1 LEU B 630    12190   6838   9025   1648  -4711   1613  B    C  
ATOM   1631  CD2 LEU B 630     -33.878  24.733 -43.743  1.00 74.25      B    C  
ANISOU 1631  CD2 LEU B 630    11530   7250   9430   1557  -4166   1527  B    C  
TER   
HETATM 1632  C1  PEG B 700     -14.305  -2.477 -29.310  1.00 62.51      D    C  
HETATM 1633  O1  PEG B 700     -14.934  -2.142 -30.539  1.00 63.41      D    O  
HETATM 1634  C2  PEG B 700     -14.124  -3.950 -29.155  1.00 61.61      D    C  
HETATM 1635  O2  PEG B 700     -15.384  -4.599 -29.110  1.00 60.61      D    O  
HETATM 1636  C3  PEG B 700     -15.271  -5.992 -28.893  1.00 59.93      D    C  
HETATM 1637  C4  PEG B 700     -16.553  -6.535 -28.363  1.00 59.68      D    C  
HETATM 1638  O4  PEG B 700     -17.565  -6.544 -29.353  1.00 60.08      D    O  
HETATM 1639  O   HOH B 801     -17.999   3.704 -35.413  1.00 76.25      F    O  
HETATM 1640  O   HOH B 802     -22.433 -11.405 -29.484  1.00 56.55      F    O  
HETATM 1641  O   HOH B 803     -25.779   5.780 -24.730  1.00 30.86      F    O  
HETATM 1642  O   HOH B 804     -21.361   5.554 -16.416  1.00 36.30      F    O  
HETATM 1643  O   HOH B 805     -17.186   4.080 -20.777  1.00 27.74      F    O  
HETATM 1644  O   HOH B 806      -8.896 -19.154 -11.123  1.00 56.54      F    O  
HETATM 1645  O   HOH B 807     -15.693 -19.872 -23.288  1.00 41.68      F    O  
HETATM 1646  O   HOH B 808     -22.264  -9.919 -15.398  1.00 37.95      F    O  
HETATM 1647  O   HOH B 809     -17.389  -1.160 -31.896  1.00 62.04      F    O  
HETATM 1648  O   HOH B 810     -25.416  11.835 -21.183  1.00 46.08      F    O  
HETATM 1649  O   HOH B 811     -15.480   4.404 -15.300  1.00 37.84      F    O  
HETATM 1650  O   HOH B 812      -6.158 -13.282 -22.870  1.00 50.57      F    O  
HETATM 1651  O   HOH B 813     -23.288  13.454 -20.069  1.00 47.24      F    O  
HETATM 1652  O   HOH B 814     -30.211  13.956 -23.917  1.00 58.01      F    O  
HETATM 1653  O   HOH B 815      -8.224 -12.108 -30.066  1.00 44.74      F    O  
HETATM 1654  O   HOH B 816     -26.306  -9.454 -27.234  1.00 56.94      F    O  
HETATM 1655  O   HOH B 817     -28.103  11.223 -45.445  1.00 46.13      F    O  
HETATM 1656  O   HOH B 818     -18.623   6.362 -13.790  1.00 36.56      F    O  
HETATM 1657  O   HOH B 819     -19.901  -1.455 -31.731  1.00 52.64      F    O  
HETATM 1658  O   HOH B 820     -25.476  13.380 -16.181  1.00 48.75      F    O  
HETATM 1659  O   HOH B 821     -19.032  32.195 -41.851  1.00 49.42      F    O  
HETATM 1660  O   HOH B 822     -30.304  20.537 -40.504  1.00 46.96      F    O  
HETATM 1661  O   HOH B 823     -30.187  11.721 -27.495  1.00 53.90      F    O  
HETATM 1662  O   HOH B 824     -28.702  32.506 -51.554  1.00 42.26      F    O  
HETATM 1663  O   HOH B 825     -15.832   3.763 -31.478  1.00 51.36      F    O  
HETATM 1664  O   HOH B 826     -16.987   6.983 -34.371  1.00 34.80      F    O  
HETATM 1665  O   HOH B 827     -13.780  16.353 -28.634  1.00 45.66      F    O  
HETATM 1666  O   HOH B 828     -30.588  20.241 -32.006  1.00 48.67      F    O  
HETATM 1667  O   HOH B 829     -22.475 -19.461 -12.643  1.00 71.58      F    O  
HETATM 1668  O   HOH B 830     -30.756  24.566 -42.253  1.00 54.65      F    O  
HETATM 1669  O   HOH B 831     -22.443 -15.350 -23.915  1.00 43.59      F    O  
HETATM 1670  O   HOH B 832     -15.727  27.920 -33.944  1.00 61.43      F    O  
HETATM 1671  O   HOH B 833     -11.823  -9.386 -10.968  1.00 32.60      F    O  
HETATM 1672  O   HOH B 834     -16.998   7.209 -24.154  1.00 31.01      F    O  
HETATM 1673  O   HOH B 835     -12.651 -12.420  -7.788  1.00 47.82      F    O  
HETATM 1674  O   HOH B 836     -17.191  -3.665 -31.042  1.00 62.07      F    O  
HETATM 1675  O   HOH B 837     -19.351 -16.938 -41.867  1.00 55.73      F    O  
HETATM 1676  O   HOH B 838     -23.428   1.314 -28.459  1.00 39.36      F    O  
HETATM 1677  O   HOH B 839     -23.629  -8.565 -28.128  1.00 57.28      F    O  
HETATM 1678  O   HOH B 840     -26.941  30.508 -38.758  1.00 60.92      F    O  
HETATM 1679  O   HOH B 841     -22.758   4.703 -31.251  1.00 27.29      F    O  
HETATM 1680  O   HOH B 842     -11.365   2.000 -15.559  1.00 40.03      F    O  
HETATM 1681  O   HOH B 843     -23.544 -17.035 -19.699  1.00 67.46      F    O  
HETATM 1682  O   HOH B 844     -19.836   4.957 -18.843  1.00 40.81      F    O  
HETATM 1683  O   HOH B 845     -16.453 -16.417 -11.653  1.00 49.96      F    O  
HETATM 1684  O   HOH B 846     -13.276 -15.213  -7.290  1.00 51.54      F    O  
HETATM 1685  O   HOH B 847     -28.915   9.216 -28.591  1.00 48.13      F    O  
HETATM 1686  O   HOH B 848     -16.011  11.923 -18.449  1.00 34.43      F    O  
HETATM 1687  O   HOH B 849     -22.349  -4.958 -25.654  1.00 33.94      F    O  
HETATM 1688  O   HOH B 850     -25.741   6.996 -36.251  1.00 43.95      F    O  
HETATM 1689  O   HOH B 851     -15.825  20.913 -47.632  1.00 52.37      F    O  
HETATM 1690  O   HOH B 852     -24.669  34.051 -49.620  1.00 41.14      F    O  
HETATM 1691  O   HOH B 853     -11.818  22.629 -32.353  1.00 60.93      F    O  
HETATM 1692  O   HOH B 854     -11.079 -21.685 -10.478  1.00 59.62      F    O  
HETATM 1693  O   HOH B 855      -5.312 -12.238 -30.113  1.00 63.32      F    O  
HETATM 1694  O   HOH B 856     -30.888   0.689 -19.331  1.00 46.39      F    O  
HETATM 1695  O   HOH B 857     -21.819 -18.913 -19.044  1.00 55.83      F    O  
HETATM 1696  O   HOH B 858     -29.684  27.071 -43.345  1.00 50.82      F    O  
HETATM 1697  O   HOH B 859     -14.661   8.120 -38.403  1.00 70.40      F    O  
HETATM 1698  O   HOH B 860     -30.750  20.552 -47.924  1.00 60.30      F    O  
HETATM 1699  O   HOH B 861     -13.184 -26.061 -26.760  1.00 71.92      F    O  
HETATM 1700  O   HOH B 862      -9.800  12.856 -22.647  1.00 71.82      F    O  
HETATM 1701  O   HOH B 863      -6.438  -9.630 -23.497  1.00 55.90      F    O  
HETATM 1702  O   HOH B 864     -16.434  10.610 -15.465  1.00 45.95      F    O  
HETATM 1703  O   HOH B 865     -11.461  -4.150 -23.667  1.00 47.05      F    O  
HETATM 1704  O   HOH B 866     -11.593  -1.076 -17.777  1.00 39.77      F    O  
HETATM 1705  O   HOH B 867     -13.538  12.567 -40.474  1.00 62.50      F    O  
HETATM 1706  O   HOH B 868      -5.819  -5.471 -17.097  1.00 53.81      F    O  
HETATM 1707  O   HOH B 869     -30.201  20.898 -29.389  1.00 55.29      F    O  
HETATM 1708  O   HOH B 870     -22.092  15.576 -21.116  1.00 38.01      F    O  
HETATM 1709  O   HOH B 871     -16.256   8.188 -42.274  1.00 69.13      F    O  
HETATM 1710  O   HOH B 872     -18.513   5.747 -22.604  1.00 31.58      F    O  
HETATM 1711  O   HOH B 873     -35.139  20.910 -31.276  1.00 78.72      F    O  
HETATM 1712  O   HOH B 874      -8.844  16.512 -37.582  1.00 75.88      F    O  
HETATM 1713  O   HOH B 875     -15.261  23.612 -25.810  1.00 55.20      F    O  
HETATM 1714  O   HOH B 876     -24.149 -13.009 -17.897  1.00 43.89      F    O  
HETATM 1715  O   HOH B 877     -28.225  10.600 -34.771  1.00 61.24      F    O  
HETATM 1716  O   HOH B 878     -20.366 -21.639 -30.371  1.00 40.69      F    O  
HETATM 1717  O   HOH B 879     -25.777  -0.037 -28.027  1.00 48.94      F    O  
HETATM 1718  O   HOH B 880     -31.106  17.698 -42.165  1.00 50.94      F    O  
HETATM 1719  O   HOH B 881     -18.371  13.000 -15.097  1.00 43.89      F    O  
HETATM 1720  O   HOH B 882     -13.234   4.672 -29.929  1.00 32.37      F    O  
HETATM 1721  O   HOH B 883     -28.387   6.485 -24.503  1.00 43.60      F    O  
HETATM 1722  O   HOH B 884     -15.167  26.160 -42.764  1.00 64.41      F    O  
HETATM 1723  O   HOH B 885     -14.873  28.287 -36.745  1.00 55.53      F    O  
HETATM 1724  O   HOH B 886     -25.212  25.334 -25.964  1.00 51.33      F    O  
HETATM 1725  O   HOH B 887     -25.176   4.516 -35.353  1.00 61.02      F    O  
HETATM 1726  O   HOH B 888      -9.148   9.569 -16.777  1.00 62.33      F    O  
HETATM 1727  O   HOH B 889     -22.963  27.439 -53.665  1.00 52.05      F    O  
HETATM 1728  O   HOH B 890      -1.943 -14.504 -12.684  1.00 71.80      F    O  
HETATM 1729  O   HOH B 891     -29.283  13.328 -35.734  1.00 51.93      F    O  
HETATM 1730  O   HOH B 892      -8.597 -21.838 -11.500  1.00 73.42      F    O  
HETATM 1731  O   HOH B 893     -16.329   1.271 -32.447  1.00 65.31      F    O  
HETATM 1732  O   HOH B 894      -7.818  -7.713  -5.145  1.00 82.09      F    O  
HETATM 1733  O   HOH B 895     -29.881   8.179 -26.281  1.00 41.63      F    O  
HETATM 1734  O   HOH B 896     -12.946  24.027 -36.681  1.00 69.27      F    O  
HETATM 1735  O   HOH B 897     -13.322  24.098 -27.747  1.00 68.82      F    O  
HETATM 1736  O   HOH B 898     -10.674  -0.118 -11.945  1.00 47.85      F    O  
HETATM 1737  O   HOH B 899     -10.776 -15.315 -37.338  1.00 68.07      F    O  
HETATM 1738  O   HOH B 900     -25.757 -14.014 -21.686  1.00 63.21      F    O  
HETATM 1739  O   HOH B 901      -9.774 -32.904 -22.059  1.00 66.12      F    O  
HETATM 1740  O   HOH B 902      -7.347   8.689 -26.186  1.00 74.90      F    O  
HETATM 1741  O   HOH B 903     -15.234 -25.164 -24.884  1.00 61.14      F    O  
HETATM 1742  O   HOH B 904     -22.177   0.045 -32.497  1.00 52.34      F    O  
HETATM 1743  O   HOH B 905      -4.476  -9.033  -7.346  1.00 72.34      F    O  
HETATM 1744  O   HOH B 906     -10.141  11.831 -32.703  1.00 62.41      F    O  
HETATM 1745  O   HOH B 907     -22.116  28.015 -28.564  1.00 66.73      F    O  
HETATM 1746  O   HOH B 908      -3.221  -6.362  -6.937  1.00 75.59      F    O  
HETATM 1747  O   HOH B 909      -9.064  15.635 -35.012  1.00 78.82      F    O  
HETATM 1748  O   HOH B 910     -13.148  29.640 -43.296  1.00 65.50      F    O  
HETATM 1749  O   HOH B 911     -28.833  30.439 -37.083  1.00 68.02      F    O  
HETATM 1750  O   HOH B 912     -23.634   2.033 -31.008  1.00 45.50      F    O  
HETATM 1751  O   HOH B 913     -33.253  22.867 -31.146  1.00 66.20      F    O  
HETATM 1752  O   HOH B 914     -14.918  14.152 -16.657  1.00 47.85      F    O  
HETATM 1753  O   HOH B 915      -7.784 -28.943 -32.032  1.00 83.38      F    O  
HETATM 1754  O   HOH B 916     -22.800  -3.725 -27.811  1.00 51.77      F    O  
HETATM 1755  O   HOH B 917     -12.249  14.832 -16.953  1.00 66.55      F    O  
HETATM 1756  O   HOH B 918     -13.901  32.291 -43.326  1.00 60.89      F    O  
HETATM 1757  O   HOH B 919     -15.620   4.770 -33.761  1.00 51.49      F    O  
HETATM 1758  O   HOH B 920     -15.507 -26.294 -16.497  1.00 59.83      F    O  
HETATM 1759  O   HOH B 921     -30.787  29.401 -34.021  1.00 82.08      F    O  
HETATM 1760  O   HOH B 922      -8.705  15.472 -24.647  1.00 73.04      F    O  
HETATM 1761  O   HOH B 923     -16.377   5.537 -40.088  1.00 76.04      F    O  
HETATM 1762  O   HOH B 924      -8.805  13.928 -38.580  1.00 80.69      F    O  
HETATM 1763  O   HOH B 925     -18.111 -26.018 -17.333  1.00 71.23      F    O  
HETATM 1764  O   HOH B 926     -24.723  -2.097 -32.291  1.00 67.82      F    O  
CONECT 1632 1633 1634
CONECT 1633 1632
CONECT 1634 1632 1635
CONECT 1635 1634 1636
CONECT 1636 1635 1637
CONECT 1637 1636 1638
CONECT 1638 1637
END



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