CNRS Nantes University UFIP UFIP
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***  SV 7bkx  ***

elNémo ID: 22051400012391105

Job options:

ID        	=	 22051400012391105
JOBID     	=	 SV 7bkx
USERID    	=	 Lili_Mip_7BKX
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 SV 7bkx

CRYST1   51.610  135.662   39.654  90.00  90.00  90.00 P 21 21 2     4
ATOM      1  N   LYS A   1      20.552  22.629  12.797  1.00 78.15      A    N  
ANISOU    1  N   LYS A   1     9000   8660  12030  -1360   2150  -3590  A    N  
ATOM      2  CA  LYS A   1      20.269  23.782  13.740  1.00 75.24      A    C  
ANISOU    2  CA  LYS A   1     8580   8420  11590  -1220   1890  -3470  A    C  
ATOM      3  C   LYS A   1      19.218  24.733  13.119  1.00 72.29      A    C  
ANISOU    3  C   LYS A   1     8700   8050  10710  -1440   2030  -3110  A    C  
ATOM      4  O   LYS A   1      18.483  25.371  13.909  1.00 70.00      A    O  
ANISOU    4  O   LYS A   1     8470   7900  10230  -1280   1730  -2860  A    O  
ATOM      5  CB  LYS A   1      21.586  24.456  14.162  1.00 76.05      A    C  
ANISOU    5  CB  LYS A   1     8230   8430  12240  -1220   2010  -3960  A    C  
ATOM      6  N   GLU A   2      19.079  24.811  11.782  1.00 71.13      A    N  
ANISOU    6  N   GLU A   2     8930   7740  10350  -1780   2430  -3070  A    N  
ATOM      7  CA  GLU A   2      17.990  25.613  11.143  1.00 70.47      A    C  
ANISOU    7  CA  GLU A   2     9380   7620   9770  -1960   2460  -2700  A    C  
ATOM      8  C   GLU A   2      17.324  24.853   9.996  1.00 67.87      A    C  
ANISOU    8  C   GLU A   2     9510   7200   9080  -2140   2560  -2480  A    C  
ATOM      9  O   GLU A   2      17.964  24.061   9.314  1.00 70.75      A    O  
ANISOU    9  O   GLU A   2     9860   7460   9570  -2300   2860  -2710  A    O  
ATOM     10  CB  GLU A   2      18.489  26.948  10.577  1.00 71.81      A    C  
ANISOU   10  CB  GLU A   2     9730   7610   9950  -2260   2840  -2860  A    C  
ATOM     11  CG  GLU A   2      18.824  28.030  11.594  1.00 71.19      A    C  
ANISOU   11  CG  GLU A   2     9330   7610  10110  -2120   2720  -2980  A    C  
ATOM     12  CD  GLU A   2      17.953  28.285  12.829  1.00 68.65      A    C  
ANISOU   12  CD  GLU A   2     8880   7520   9690  -1780   2200  -2690  A    C  
ATOM     13  OE1 GLU A   2      16.739  28.715  12.703  1.00 60.70      A    O  
ANISOU   13  OE1 GLU A   2     8220   6530   8310  -1770   2010  -2310  A    O  
ATOM     14  OE2 GLU A   2      18.548  28.167  13.940  1.00 68.33      A    O1-
ANISOU   14  OE2 GLU A   2     8390   7600   9980  -1530   2000  -2900  A    O1-
ATOM     15  N   PRO A   3      16.007  25.070   9.756  1.00 63.50      A    N  
ANISOU   15  N   PRO A   3     9350   6680   8100  -2130   2300  -2070  A    N  
ATOM     16  CA  PRO A   3      15.372  24.780   8.474  1.00 64.39      A    C  
ANISOU   16  CA  PRO A   3    10010   6640   7820  -2380   2410  -1870  A    C  
ATOM     17  C   PRO A   3      15.505  25.947   7.499  1.00 69.21      A    C  
ANISOU   17  C   PRO A   3    11110   6990   8190  -2730   2720  -1880  A    C  
ATOM     18  O   PRO A   3      16.054  26.944   7.843  1.00 68.04      A    O  
ANISOU   18  O   PRO A   3    10830   6810   8210  -2770   2860  -2030  A    O  
ATOM     19  CB  PRO A   3      13.885  24.740   8.815  1.00 60.22      A    C  
ANISOU   19  CB  PRO A   3     9630   6230   7020  -2170   1930  -1460  A    C  
ATOM     20  CG  PRO A   3      13.786  25.810   9.853  1.00 60.47      A    C  
ANISOU   20  CG  PRO A   3     9420   6360   7200  -1990   1740  -1430  A    C  
ATOM     21  CD  PRO A   3      15.035  25.626  10.703  1.00 61.11      A    C  
ANISOU   21  CD  PRO A   3     8980   6540   7700  -1870   1880  -1790  A    C  
ATOM     22  N   CYS A   4      14.873  25.820   6.350  1.00 74.53      A    N  
ANISOU   22  N   CYS A   4    12380   7490   8450  -2960   2750  -1680  A    N  
ATOM     23  CA  CYS A   4      14.862  26.864   5.316  1.00 80.29      A    C  
ANISOU   23  CA  CYS A   4    13740   7920   8850  -3320   2990  -1620  A    C  
ATOM     24  C   CYS A   4      13.416  27.321   5.178  1.00 79.48      A    C  
ANISOU   24  C   CYS A   4    14010   7790   8390  -3200   2460  -1190  A    C  
ATOM     25  O   CYS A   4      12.674  26.810   4.339  1.00 79.04      A    O  
ANISOU   25  O   CYS A   4    14410   7630   8000  -3300   2300   -980  A    O  
ATOM     26  CB  CYS A   4      15.524  26.366   4.032  1.00 85.60      A    C  
ANISOU   26  CB  CYS A   4    14850   8340   9340  -3730   3510  -1820  A    C  
ATOM     27  SG  CYS A   4      14.707  24.951   3.254  1.00 90.40      A    S  
ANISOU   27  SG  CYS A   4    15780   8950   9620  -3750   3310  -1620  A    S  
ATOM     28  N   PRO A   5      13.016  28.358   5.948  1.00 76.54      A    N  
ANISOU   28  N   PRO A   5    13480   7480   8120  -3020   2200  -1070  A    N  
ATOM     29  CA  PRO A   5      11.607  28.664   6.153  1.00 78.41      A    C  
ANISOU   29  CA  PRO A   5    13840   7740   8210  -2810   1640   -710  A    C  
ATOM     30  C   PRO A   5      11.000  29.138   4.841  1.00 86.89      A    C  
ANISOU   30  C   PRO A   5    15710   8480   8830  -3070   1540   -490  A    C  
ATOM     31  O   PRO A   5      11.734  29.455   3.916  1.00 96.36      A    O  
ANISOU   31  O   PRO A   5    17380   9420   9810  -3420   1950   -620  A    O  
ATOM     32  CB  PRO A   5      11.581  29.748   7.240  1.00 76.93      A    C  
ANISOU   32  CB  PRO A   5    13290   7660   8280  -2610   1510   -720  A    C  
ATOM     33  CG  PRO A   5      13.039  30.086   7.550  1.00 77.07      A    C  
ANISOU   33  CG  PRO A   5    13020   7700   8560  -2740   2000  -1090  A    C  
ATOM     34  CD  PRO A   5      13.895  29.377   6.525  1.00 78.68      A    C  
ANISOU   34  CD  PRO A   5    13480   7750   8660  -3050   2460  -1300  A    C  
ATOM     35  N   PRO A   6       9.658  29.231   4.717  1.00 92.62      A    N  
ANISOU   35  N   PRO A   6    16630   9150   9410  -2920    990   -190  A    N  
ATOM     36  CA  PRO A   6       9.017  29.515   3.434  1.00101.56      A    C  
ANISOU   36  CA  PRO A   6    18560   9930  10100  -3130    780     30  A    C  
ATOM     37  C   PRO A   6       9.274  30.931   2.905  1.00109.15      A    C  
ANISOU   37  C   PRO A   6    20060  10560  10850  -3360    880     70  A    C  
ATOM     38  O   PRO A   6       9.913  31.724   3.594  1.00111.40      A    O  
ANISOU   38  O   PRO A   6    20030  10910  11380  -3330   1120    -70  A    O  
ATOM     39  CB  PRO A   6       7.507  29.432   3.716  1.00100.18      A    C  
ANISOU   39  CB  PRO A   6    18280   9790   9990  -2830    100    290  A    C  
ATOM     40  CG  PRO A   6       7.401  28.784   5.075  1.00 93.38      A    C  
ANISOU   40  CG  PRO A   6    16590   9330   9560  -2510     70    190  A    C  
ATOM     41  CD  PRO A   6       8.679  29.153   5.802  1.00 90.75      A    C  
ANISOU   41  CD  PRO A   6    15890   9140   9450  -2540    540    -60  A    C  
ATOM     42  N   GLU A   7       8.721  31.203   1.717  0.80112.63      A    N  
ANISOU   42  N   GLU A   7    21320  10630  10830  -3570    640    270  A    N  
ATOM     43  CA  GLU A   7       8.690  32.525   1.041  0.80112.56      A    C  
ANISOU   43  CA  GLU A   7    22030  10220  10520  -3780    590    400  A    C  
ATOM     44  C   GLU A   7       7.953  33.567   1.908  0.80110.66      A    C  
ANISOU   44  C   GLU A   7    21440  10010  10600  -3470    140    540  A    C  
ATOM     45  O   GLU A   7       8.626  34.454   2.502  0.80103.54      A    O  
ANISOU   45  O   GLU A   7    20300   9140   9900  -3480    440    400  A    O  
ATOM     46  CB  GLU A   7       8.006  32.320  -0.311  0.80115.80      A    C  
ANISOU   46  CB  GLU A   7    23360  10250  10390  -3980    250    630  A    C  
ATOM     47  N   ASN A   8       6.621  33.438   1.994  1.00113.17      A    N  
ANISOU   47  N   ASN A   8    21700  10310  10990  -3190   -550    760  A    N  
ATOM     48  CA  ASN A   8       5.672  34.458   2.527  1.00112.84      A    C  
ANISOU   48  CA  ASN A   8    21490  10170  11220  -2920  -1090    920  A    C  
ATOM     49  C   ASN A   8       5.864  34.624   4.038  1.00108.92      A    C  
ANISOU   49  C   ASN A   8    20070  10060  11260  -2650   -930    750  A    C  
ATOM     50  O   ASN A   8       6.313  35.738   4.424  1.00100.90      A    O  
ANISOU   50  O   ASN A   8    19010   8980  10350  -2680   -750    700  A    O  
ATOM     51  CB  ASN A   8       4.215  34.092   2.215  1.00114.29      A    C  
ANISOU   51  CB  ASN A   8    21770  10230  11430  -2710  -1840   1120  A    C  
ATOM     52  N   LEU A   9       5.481  33.568   4.806  0.70104.46      A    N  
ANISOU   52  N   LEU A   9    18860   9850  10980  -2410  -1010    690  A    N  
ATOM     53  CA  LEU A   9       5.575  33.329   6.292  1.00 95.92      A    C  
ANISOU   53  CA  LEU A   9    16920   9170  10350  -2150   -880    540  A    C  
ATOM     54  C   LEU A   9       4.267  33.734   7.017  1.00 90.56      A    C  
ANISOU   54  C   LEU A   9    15880   8500  10030  -1850  -1390    630  A    C  
ATOM     55  O   LEU A   9       4.294  33.976   8.262  1.00 84.27      A    O  
ANISOU   55  O   LEU A   9    14490   7940   9590  -1660  -1280    510  A    O  
ATOM     56  CB  LEU A   9       6.792  34.054   6.899  1.00 95.61      A    C  
ANISOU   56  CB  LEU A   9    16670   9240  10420  -2240   -380    340  A    C  
ATOM     57  CG  LEU A   9       8.099  33.263   7.052  1.00 94.58      A    C  
ANISOU   57  CG  LEU A   9    16330   9330  10280  -2370    170     90  A    C  
ATOM     58  CD1 LEU A   9       7.952  32.066   8.011  1.00 86.89      A    C  
ANISOU   58  CD1 LEU A   9    14740   8720   9560  -2120    130     10  A    C  
ATOM     59  CD2 LEU A   9       8.631  32.821   5.695  1.00 97.39      A    C  
ANISOU   59  CD2 LEU A   9    17320   9450  10230  -2700    430     90  A    C  
ATOM     60  N   GLN A  10       3.139  33.789   6.306  1.00 96.62      A    N  
ANISOU   60  N   GLN A  10    16960   8990  10750  -1790  -1920    810  A    N  
ATOM     61  CA  GLN A  10       1.933  34.527   6.782  1.00103.47      A    C  
ANISOU   61  CA  GLN A  10    17580   9730  12010  -1550  -2420    870  A    C  
ATOM     62  C   GLN A  10       1.192  33.669   7.821  1.00 97.12      A    C  
ANISOU   62  C   GLN A  10    16070   9220  11610  -1310  -2490    760  A    C  
ATOM     63  O   GLN A  10       0.901  32.500   7.519  1.00104.02      A    O  
ANISOU   63  O   GLN A  10    16940  10180  12400  -1300  -2550    770  A    O  
ATOM     64  CB  GLN A  10       1.045  34.939   5.597  1.00105.48      A    C  
ANISOU   64  CB  GLN A  10    18450   9530  12100  -1580  -3030   1060  A    C  
ATOM     65  N   LEU A  11       0.886  34.247   8.987  1.00 92.78      A    N  
ANISOU   65  N   LEU A  11    14990   8790  11480  -1130  -2460    660  A    N  
ATOM     66  CA  LEU A  11       0.127  33.620  10.104  1.00 88.94      A    C  
ANISOU   66  CA  LEU A  11    13870   8530  11400   -930  -2480    530  A    C  
ATOM     67  C   LEU A  11      -1.130  34.446  10.416  1.00 86.24      A    C  
ANISOU   67  C   LEU A  11    13280   7960  11530   -750  -2900    510  A    C  
ATOM     68  O   LEU A  11      -0.992  35.504  11.028  1.00 89.81      A    O  
ANISOU   68  O   LEU A  11    13570   8380  12180   -720  -2820    450  A    O  
ATOM     69  CB  LEU A  11       1.063  33.571  11.318  1.00 90.68      A    C  
ANISOU   69  CB  LEU A  11    13700   9100  11660   -910  -1970    380  A    C  
ATOM     70  CG  LEU A  11       0.707  32.537  12.388  1.00 92.78      A    C  
ANISOU   70  CG  LEU A  11    13480   9640  12130   -780  -1820    260  A    C  
ATOM     71  CD1 LEU A  11       1.821  32.434  13.426  1.00 89.39      A    C  
ANISOU   71  CD1 LEU A  11    12810   9510  11640   -790  -1380    130  A    C  
ATOM     72  CD2 LEU A  11      -0.632  32.868  13.041  1.00 93.40      A    C  
ANISOU   72  CD2 LEU A  11    13190   9620  12680   -620  -2070    180  A    C  
ATOM     73  N   THR A  12      -2.324  33.961  10.090  1.00 85.26      A    N  
ANISOU   73  N   THR A  12    13070   7680  11650   -650  -3320    510  A    N  
ATOM     74  CA  THR A  12      -3.569  34.782  10.080  1.00 86.20      A    C  
ANISOU   74  CA  THR A  12    13020   7470  12260   -490  -3830    470  A    C  
ATOM     75  C   THR A  12      -4.290  34.731  11.437  1.00 83.53      A    C  
ANISOU   75  C   THR A  12    11970   7270  12500   -340  -3670    240  A    C  
ATOM     76  O   THR A  12      -3.957  33.942  12.314  1.00 82.75      A    O  
ANISOU   76  O   THR A  12    11570   7510  12360   -350  -3220    130  A    O  
ATOM     77  CB  THR A  12      -4.420  34.415   8.850  1.00 91.59      A    C  
ANISOU   77  CB  THR A  12    14060   7820  12920   -470  -4440    580  A    C  
ATOM     78  CG2 THR A  12      -3.580  34.175   7.609  1.00 92.66      A    C  
ANISOU   78  CG2 THR A  12    14950   7880  12380   -670  -4450    780  A    C  
ATOM     79  OG1 THR A  12      -5.221  33.257   9.086  1.00 89.28      A    O  
ANISOU   79  OG1 THR A  12    13390   7640  12880   -380  -4500    450  A    O  
ATOM     80  N   PRO A  13      -5.238  35.655  11.713  1.00 87.43      A    N  
ANISOU   80  N   PRO A  13    12180   7500  13540   -210  -3980    130  A    N  
ATOM     81  CA  PRO A  13      -5.978  35.664  12.981  1.00 85.22      A    C  
ANISOU   81  CA  PRO A  13    11250   7300  13830   -110  -3780   -140  A    C  
ATOM     82  C   PRO A  13      -6.918  34.487  13.275  1.00 79.39      A    C  
ANISOU   82  C   PRO A  13    10140   6620  13400    -50  -3780   -310  A    C  
ATOM     83  O   PRO A  13      -7.601  34.072  12.423  1.00 80.19      A    O  
ANISOU   83  O   PRO A  13    10350   6520  13610    -10  -4210   -280  A    O  
ATOM     84  CB  PRO A  13      -6.837  36.948  12.879  1.00 91.06      A    C  
ANISOU   84  CB  PRO A  13    11840   7640  15120     20  -4230   -210  A    C  
ATOM     85  CG  PRO A  13      -6.055  37.845  11.945  1.00 90.91      A    C  
ANISOU   85  CG  PRO A  13    12440   7440  14660    -50  -4440     40  A    C  
ATOM     86  CD  PRO A  13      -5.498  36.876  10.922  1.00 93.32      A    C  
ANISOU   86  CD  PRO A  13    13270   7830  14360   -170  -4480    240  A    C  
ATOM     87  N   ARG A  14      -6.939  34.019  14.520  1.00 78.78      A    N  
ANISOU   87  N   ARG A  14     9660   6800  13470    -70  -3270   -500  A    N  
ATOM     88  CA  ARG A  14      -7.747  32.854  14.998  1.00 80.56      A    C  
ANISOU   88  CA  ARG A  14     9540   7100  13970    -60  -3110   -690  A    C  
ATOM     89  C   ARG A  14      -7.223  31.532  14.417  1.00 75.35      A    C  
ANISOU   89  C   ARG A  14     9190   6650  12800   -130  -3040   -530  A    C  
ATOM     90  O   ARG A  14      -7.797  30.472  14.780  1.00 74.64      A    O  
ANISOU   90  O   ARG A  14     8870   6630  12870   -140  -2870   -670  A    O  
ATOM     91  CB  ARG A  14      -9.228  33.063  14.674  1.00 82.82      A    C  
ANISOU   91  CB  ARG A  14     9490   7010  14970     50  -3580   -900  A    C  
ATOM     92  CG  ARG A  14      -9.908  34.048  15.618  1.00 87.21      A    C  
ANISOU   92  CG  ARG A  14     9560   7390  16180    100  -3470  -1170  A    C  
ATOM     93  CD  ARG A  14     -11.421  34.084  15.478  1.00 91.12      A    C  
ANISOU   93  CD  ARG A  14     9590   7510  17520    210  -3840  -1470  A    C  
ATOM     94  NE  ARG A  14     -12.007  32.759  15.678  1.00 90.87      A    N  
ANISOU   94  NE  ARG A  14     9340   7570  17620    160  -3630  -1650  A    N  
ATOM     95  CZ  ARG A  14     -12.250  32.192  16.866  1.00 89.92      A    C  
ANISOU   95  CZ  ARG A  14     8890   7600  17670     50  -3010  -1900  A    C  
ATOM     96  NH1 ARG A  14     -11.953  32.824  17.993  1.00 83.22      A    N1+
ANISOU   96  NH1 ARG A  14     7900   6860  16870    -20  -2540  -2010  A    N1+
ATOM     97  NH2 ARG A  14     -12.801  30.985  16.918  1.00 91.47      A    N  
ANISOU   97  NH2 ARG A  14     8940   7830  17980     -0  -2850  -2040  A    N  
ATOM     98  N   ALA A  15      -6.163  31.582  13.594  1.00 72.04      A    N  
ANISOU   98  N   ALA A  15     9260   6310  11810   -200  -3100   -280  A    N  
ATOM     99  CA  ALA A  15      -5.630  30.451  12.792  1.00 71.43      A    C  
ANISOU   99  CA  ALA A  15     9540   6360  11250   -280  -3090   -130  A    C  
ATOM    100  C   ALA A  15      -5.229  29.267  13.694  1.00 68.12      A    C  
ANISOU  100  C   ALA A  15     8940   6270  10670   -320  -2580   -200  A    C  
ATOM    101  O   ALA A  15      -5.277  28.120  13.225  1.00 72.24      A    O  
ANISOU  101  O   ALA A  15     9580   6860  11010   -360  -2580   -160  A    O  
ATOM    102  CB  ALA A  15      -4.454  30.936  11.984  1.00 70.25      A    C  
ANISOU  102  CB  ALA A  15     9900   6220  10570   -380  -3100     90  A    C  
ATOM    103  N   LEU A  16      -4.849  29.541  14.940  1.00 62.53      A    N  
ANISOU  103  N   LEU A  16     8000   5750  10010   -320  -2180   -310  A    N  
ATOM    104  CA  LEU A  16      -4.389  28.538  15.918  1.00 59.77      A    C  
ANISOU  104  CA  LEU A  16     7560   5680   9470   -350  -1720   -370  A    C  
ATOM    105  C   LEU A  16      -5.522  28.181  16.868  1.00 62.39      A    C  
ANISOU  105  C   LEU A  16     7520   5950  10240   -330  -1550   -600  A    C  
ATOM    106  O   LEU A  16      -5.274  27.398  17.817  1.00 58.93      A    O  
ANISOU  106  O   LEU A  16     7040   5690   9660   -370  -1160   -670  A    O  
ATOM    107  CB  LEU A  16      -3.217  29.098  16.725  1.00 54.44      A    C  
ANISOU  107  CB  LEU A  16     6940   5200   8540   -370  -1410   -350  A    C  
ATOM    108  CG  LEU A  16      -2.021  29.584  15.917  1.00 55.40      A    C  
ANISOU  108  CG  LEU A  16     7390   5370   8290   -420  -1480   -180  A    C  
ATOM    109  CD1 LEU A  16      -0.936  30.126  16.839  1.00 53.85      A    C  
ANISOU  109  CD1 LEU A  16     7160   5360   7940   -440  -1180   -230  A    C  
ATOM    110  CD2 LEU A  16      -1.471  28.502  15.000  1.00 56.22      A    C  
ANISOU  110  CD2 LEU A  16     7780   5550   8030   -480  -1490    -60  A    C  
ATOM    111  N   VAL A  17      -6.705  28.756  16.679  1.00 66.95      A    N  
ANISOU  111  N   VAL A  17     7830   6250  11360   -280  -1820   -750  A    N  
ATOM    112  CA  VAL A  17      -7.784  28.622  17.700  1.00 67.38      A    C  
ANISOU  112  CA  VAL A  17     7470   6200  11930   -300  -1570  -1040  A    C  
ATOM    113  C   VAL A  17      -8.163  27.144  17.776  1.00 64.84      A    C  
ANISOU  113  C   VAL A  17     7130   5950  11560   -350  -1380  -1100  A    C  
ATOM    114  O   VAL A  17      -8.189  26.475  16.699  1.00 60.83      A    O  
ANISOU  114  O   VAL A  17     6790   5420  10900   -330  -1670   -980  A    O  
ATOM    115  CB  VAL A  17      -9.018  29.486  17.371  1.00 75.91      A    C  
ANISOU  115  CB  VAL A  17     8210   6930  13710   -220  -1940  -1240  A    C  
ATOM    116  CG1 VAL A  17      -9.796  28.909  16.185  1.00 76.09      A    C  
ANISOU  116  CG1 VAL A  17     8230   6740  13930   -170  -2420  -1230  A    C  
ATOM    117  CG2 VAL A  17      -9.923  29.669  18.601  1.00 76.86      A    C  
ANISOU  117  CG2 VAL A  17     7880   6940  14390   -270  -1570  -1590  A    C  
ATOM    118  N   GLY A  18      -8.472  26.665  18.981  1.00 62.38      A    N  
ANISOU  118  N   GLY A  18     6660   5690  11350   -430   -900  -1300  A    N  
ATOM    119  CA  GLY A  18      -9.130  25.363  19.154  1.00 62.57      A    C  
ANISOU  119  CA  GLY A  18     6610   5690  11470   -490   -690  -1430  A    C  
ATOM    120  C   GLY A  18      -8.138  24.256  19.471  1.00 62.37      A    C  
ANISOU  120  C   GLY A  18     6940   5930  10820   -540   -400  -1250  A    C  
ATOM    121  O   GLY A  18      -7.202  24.524  20.272  1.00 63.33      A    O  
ANISOU  121  O   GLY A  18     7250   6230  10580   -550   -160  -1170  A    O  
ATOM    122  N   LYS A  19      -8.388  23.043  18.963  1.00 57.44      A    N  
ANISOU  122  N   LYS A  19     6390   5310  10120   -560   -420  -1230  A    N  
ATOM    123  CA  LYS A  19      -7.867  21.805  19.595  1.00 58.55      A    C  
ANISOU  123  CA  LYS A  19     6780   5620   9850   -620    -40  -1170  A    C  
ATOM    124  C   LYS A  19      -6.808  21.215  18.688  1.00 51.22      A    C  
ANISOU  124  C   LYS A  19     6160   4870   8430   -570   -250   -890  A    C  
ATOM    125  O   LYS A  19      -7.039  21.230  17.468  1.00 54.76      A    O  
ANISOU  125  O   LYS A  19     6600   5250   8960   -530   -620   -820  A    O  
ATOM    126  CB  LYS A  19      -8.934  20.741  19.849  1.00 64.61      A    C  
ANISOU  126  CB  LYS A  19     7410   6240  10900   -720    220  -1380  A    C  
ATOM    127  CG  LYS A  19      -8.626  19.910  21.088  1.00 70.17      A    C  
ANISOU  127  CG  LYS A  19     8350   7020  11280   -820    740  -1410  A    C  
ATOM    128  CD  LYS A  19      -9.751  19.049  21.540  1.00 75.23      A    C  
ANISOU  128  CD  LYS A  19     8860   7470  12250   -960   1100  -1680  A    C  
ATOM    129  CE  LYS A  19     -10.134  18.027  20.500  1.00 77.62      A    C  
ANISOU  129  CE  LYS A  19     9120   7740  12630   -940    900  -1650  A    C  
ATOM    130  NZ  LYS A  19     -10.325  16.714  21.148  1.00 83.01      A    N1+
ANISOU  130  NZ  LYS A  19    10010   8380  13150  -1070   1360  -1720  A    N1+
ATOM    131  N   TRP A  20      -5.677  20.795  19.260  1.00 45.36      A    N  
ANISOU  131  N   TRP A  20     5690   4330   7210   -560    -40   -760  A    N  
ATOM    132  CA  TRP A  20      -4.559  20.207  18.466  1.00 44.51      A    C  
ANISOU  132  CA  TRP A  20     5850   4390   6680   -520   -190   -540  A    C  
ATOM    133  C   TRP A  20      -3.931  19.035  19.196  1.00 41.68      A    C  
ANISOU  133  C   TRP A  20     5710   4140   5980   -520     90   -490  A    C  
ATOM    134  O   TRP A  20      -3.936  19.020  20.422  1.00 40.54      A    O  
ANISOU  134  O   TRP A  20     5620   4000   5780   -550    360   -570  A    O  
ATOM    135  CB  TRP A  20      -3.459  21.224  18.210  1.00 45.64      A    C  
ANISOU  135  CB  TRP A  20     6090   4640   6620   -470   -340   -410  A    C  
ATOM    136  CG  TRP A  20      -3.915  22.474  17.555  1.00 48.88      A    C  
ANISOU  136  CG  TRP A  20     6360   4910   7300   -460   -630   -430  A    C  
ATOM    137  CD1 TRP A  20      -4.458  23.564  18.162  1.00 48.79      A    C  
ANISOU  137  CD1 TRP A  20     6140   4800   7600   -450   -610   -550  A    C  
ATOM    138  CD2 TRP A  20      -3.865  22.761  16.154  1.00 53.18      A    C  
ANISOU  138  CD2 TRP A  20     7020   5380   7810   -460   -980   -310  A    C  
ATOM    139  CE2 TRP A  20      -4.355  24.069  15.994  1.00 53.43      A    C  
ANISOU  139  CE2 TRP A  20     6920   5250   8130   -440  -1210   -350  A    C  
ATOM    140  CE3 TRP A  20      -3.456  22.041  15.031  1.00 56.96      A    C  
ANISOU  140  CE3 TRP A  20     7730   5880   8030   -490  -1120   -180  A    C  
ATOM    141  NE1 TRP A  20      -4.720  24.525  17.229  1.00 52.54      A    N  
ANISOU  141  NE1 TRP A  20     6580   5130   8250   -430   -970   -510  A    N  
ATOM    142  CZ2 TRP A  20      -4.433  24.684  14.758  1.00 58.05      A    C  
ANISOU  142  CZ2 TRP A  20     7660   5680   8720   -440  -1600   -250  A    C  
ATOM    143  CZ3 TRP A  20      -3.549  22.645  13.801  1.00 59.99      A    C  
ANISOU  143  CZ3 TRP A  20     8280   6120   8400   -520  -1480    -90  A    C  
ATOM    144  CH2 TRP A  20      -4.025  23.949  13.673  1.00 62.33      A    C  
ANISOU  144  CH2 TRP A  20     8490   6240   8950   -490  -1730   -110  A    C  
ATOM    145  N   TYR A  21      -3.287  18.167  18.441  1.00 40.37      A    N  
ANISOU  145  N   TYR A  21     5710   4060   5570   -500      0   -360  A    N  
ATOM    146  CA  TYR A  21      -2.538  17.031  18.998  1.00 40.13      A    C  
ANISOU  146  CA  TYR A  21     5910   4120   5220   -480    190   -300  A    C  
ATOM    147  C   TYR A  21      -1.103  17.080  18.481  1.00 36.63      A    C  
ANISOU  147  C   TYR A  21     5600   3820   4500   -410     50   -180  A    C  
ATOM    148  O   TYR A  21      -0.871  17.041  17.278  1.00 34.42      A    O  
ANISOU  148  O   TYR A  21     5330   3550   4190   -430   -120   -110  A    O  
ATOM    149  CB  TYR A  21      -3.255  15.742  18.614  1.00 42.85      A    C  
ANISOU  149  CB  TYR A  21     6280   4390   5620   -530    270   -330  A    C  
ATOM    150  CG  TYR A  21      -4.733  15.750  18.920  1.00 43.50      A    C  
ANISOU  150  CG  TYR A  21     6160   4290   6080   -610    410   -510  A    C  
ATOM    151  CD1 TYR A  21      -5.203  15.421  20.173  1.00 42.77      A    C  
ANISOU  151  CD1 TYR A  21     6120   4110   6010   -680    760   -640  A    C  
ATOM    152  CD2 TYR A  21      -5.657  16.080  17.937  1.00 45.10      A    C  
ANISOU  152  CD2 TYR A  21     6120   4380   6640   -640    170   -590  A    C  
ATOM    153  CE1 TYR A  21      -6.557  15.435  20.463  1.00 46.34      A    C  
ANISOU  153  CE1 TYR A  21     6360   4370   6880   -790    960   -870  A    C  
ATOM    154  CE2 TYR A  21      -7.020  16.075  18.202  1.00 47.93      A    C  
ANISOU  154  CE2 TYR A  21     6220   4550   7440   -710    280   -810  A    C  
ATOM    155  CZ  TYR A  21      -7.477  15.741  19.472  1.00 49.07      A    C  
ANISOU  155  CZ  TYR A  21     6380   4610   7660   -800    710   -970  A    C  
ATOM    156  OH  TYR A  21      -8.824  15.714  19.736  1.00 53.42      A    O  
ANISOU  156  OH  TYR A  21     6650   4940   8710   -900    890  -1250  A    O  
ATOM    157  N   LEU A  22      -0.169  17.188  19.414  1.00 34.19      A    N  
ANISOU  157  N   LEU A  22     5400   3600   3990   -340    130   -170  A    N  
ATOM    158  CA  LEU A  22       1.255  17.305  19.094  1.00 34.87      A    C  
ANISOU  158  CA  LEU A  22     5550   3800   3900   -280     20   -120  A    C  
ATOM    159  C   LEU A  22       1.813  15.897  19.039  1.00 33.75      A    C  
ANISOU  159  C   LEU A  22     5560   3670   3590   -230     60    -80  A    C  
ATOM    160  O   LEU A  22       2.333  15.448  20.042  1.00 38.81      A    O  
ANISOU  160  O   LEU A  22     6340   4320   4090   -150    110    -90  A    O  
ATOM    161  CB  LEU A  22       1.923  18.164  20.162  1.00 34.72      A    C  
ANISOU  161  CB  LEU A  22     5530   3840   3820   -220     30   -170  A    C  
ATOM    162  CG  LEU A  22       3.113  18.979  19.694  1.00 38.63      A    C  
ANISOU  162  CG  LEU A  22     5960   4420   4300   -190    -90   -180  A    C  
ATOM    163  CD1 LEU A  22       3.810  19.651  20.861  1.00 39.70      A    C  
ANISOU  163  CD1 LEU A  22     6100   4610   4380   -110    -90   -250  A    C  
ATOM    164  CD2 LEU A  22       4.089  18.174  18.932  1.00 39.78      A    C  
ANISOU  164  CD2 LEU A  22     6160   4600   4360   -160   -130   -160  A    C  
ATOM    165  N   ARG A  23       1.783  15.268  17.879  1.00 34.95      A    N  
ANISOU  165  N   ARG A  23     5710   3810   3750   -280     20    -40  A    N  
ATOM    166  CA  ARG A  23       2.056  13.815  17.755  1.00 33.94      A    C  
ANISOU  166  CA  ARG A  23     5710   3670   3520   -250     80    -10  A    C  
ATOM    167  C   ARG A  23       3.428  13.550  17.152  1.00 31.59      A    C  
ANISOU  167  C   ARG A  23     5430   3430   3150   -210     20    -20  A    C  
ATOM    168  O   ARG A  23       3.844  12.393  17.254  1.00 32.71      A    O  
ANISOU  168  O   ARG A  23     5660   3550   3220   -160     60    -20  A    O  
ATOM    169  CB  ARG A  23       0.950  13.123  16.952  1.00 35.82      A    C  
ANISOU  169  CB  ARG A  23     5940   3830   3840   -350    110      0  A    C  
ATOM    170  CG  ARG A  23      -0.423  13.158  17.608  1.00 35.44      A    C  
ANISOU  170  CG  ARG A  23     5840   3680   3950   -400    220    -50  A    C  
ATOM    171  CD  ARG A  23      -0.411  12.230  18.810  1.00 38.69      A    C  
ANISOU  171  CD  ARG A  23     6430   4040   4230   -360    420    -60  A    C  
ATOM    172  NE  ARG A  23      -1.764  12.098  19.306  1.00 40.58      A    N  
ANISOU  172  NE  ARG A  23     6630   4150   4640   -450    620   -150  A    N  
ATOM    173  CZ  ARG A  23      -2.228  12.606  20.411  1.00 43.10      A    C  
ANISOU  173  CZ  ARG A  23     6980   4400   4990   -490    780   -230  A    C  
ATOM    174  NH1 ARG A  23      -1.464  13.320  21.241  1.00 43.63      A    N1+
ANISOU  174  NH1 ARG A  23     7140   4530   4900   -420    750   -210  A    N1+
ATOM    175  NH2 ARG A  23      -3.501  12.408  20.639  1.00 46.08      A    N  
ANISOU  175  NH2 ARG A  23     7270   4640   5600   -600    990   -360  A    N  
ATOM    176  N   THR A  24       4.140  14.552  16.641  1.00 28.37      A    N  
ANISOU  176  N   THR A  24     4940   3070   2770   -240    -40    -60  A    N  
ATOM    177  CA  THR A  24       5.410  14.339  15.904  1.00 30.09      A    C  
ANISOU  177  CA  THR A  24     5140   3310   2980   -260    -20   -130  A    C  
ATOM    178  C   THR A  24       6.382  15.487  16.182  1.00 31.00      A    C  
ANISOU  178  C   THR A  24     5150   3470   3160   -230    -50   -220  A    C  
ATOM    179  O   THR A  24       5.971  16.636  16.132  1.00 30.75      A    O  
ANISOU  179  O   THR A  24     5080   3450   3150   -290    -80   -200  A    O  
ATOM    180  CB  THR A  24       5.162  14.194  14.395  1.00 29.54      A    C  
ANISOU  180  CB  THR A  24     5140   3200   2890   -430     10   -100  A    C  
ATOM    181  CG2 THR A  24       6.405  13.848  13.615  1.00 28.91      A    C  
ANISOU  181  CG2 THR A  24     5070   3100   2820   -490    120   -210  A    C  
ATOM    182  OG1 THR A  24       4.115  13.261  14.171  1.00 30.28      A    O  
ANISOU  182  OG1 THR A  24     5310   3240   2960   -450     20    -30  A    O  
ATOM    183  N   THR A  25       7.624  15.146  16.476  1.00 32.81      A    N  
ANISOU  183  N   THR A  25     5300   3710   3450   -140    -60   -340  A    N  
ATOM    184  CA  THR A  25       8.695  16.081  16.860  1.00 35.17      A    C  
ANISOU  184  CA  THR A  25     5460   4040   3860    -90    -90   -480  A    C  
ATOM    185  C   THR A  25      10.010  15.514  16.335  1.00 39.08      A    C  
ANISOU  185  C   THR A  25     5840   4500   4510    -90    -30   -670  A    C  
ATOM    186  O   THR A  25      10.090  14.291  16.059  1.00 39.19      A    O  
ANISOU  186  O   THR A  25     5900   4460   4530    -60    -10   -670  A    O  
ATOM    187  CB  THR A  25       8.749  16.350  18.359  1.00 36.54      A    C  
ANISOU  187  CB  THR A  25     5630   4250   4010     80   -240   -490  A    C  
ATOM    188  CG2 THR A  25       7.416  16.744  18.968  1.00 37.03      A    C  
ANISOU  188  CG2 THR A  25     5800   4320   3950     50   -240   -350  A    C  
ATOM    189  OG1 THR A  25       9.264  15.173  18.967  1.00 44.11      A    O  
ANISOU  189  OG1 THR A  25     6640   5150   4960    230   -350   -530  A    O  
ATOM    190  N   SER A  26      10.969  16.397  16.124  1.00 41.90      A    N  
ANISOU  190  N   SER A  26     6050   4850   5020   -140     30   -840  A    N  
ATOM    191  CA  SER A  26      12.362  16.032  15.783  1.00 45.53      A    C  
ANISOU  191  CA  SER A  26     6320   5240   5740   -130    110  -1110  A    C  
ATOM    192  C   SER A  26      13.223  16.777  16.764  1.00 48.35      A    C  
ANISOU  192  C   SER A  26     6470   5620   6280     10    -40  -1280  A    C  
ATOM    193  O   SER A  26      13.230  18.001  16.685  1.00 48.70      A    O  
ANISOU  193  O   SER A  26     6480   5700   6330    -90     30  -1300  A    O  
ATOM    194  CB  SER A  26      12.743  16.388  14.395  1.00 45.72      A    C  
ANISOU  194  CB  SER A  26     6360   5200   5810   -390    400  -1220  A    C  
ATOM    195  OG  SER A  26      14.052  15.891  14.172  1.00 48.65      A    O  
ANISOU  195  OG  SER A  26     6510   5480   6490   -380    520  -1520  A    O  
ATOM    196  N   PRO A  27      14.241  16.131  17.332  1.00 57.29      A    N  
ANISOU  196  N   PRO A  27     7420   6690   7660    190   -200  -1480  A    N  
ATOM    197  CA  PRO A  27      14.246  15.635  18.691  1.00 57.62      A    C  
ANISOU  197  CA  PRO A  27     7510   6720   7660    460   -550  -1430  A    C  
ATOM    198  C   PRO A  27      12.892  15.000  18.990  1.00 49.40      A    C  
ANISOU  198  C   PRO A  27     6790   5710   6260    470   -580  -1120  A    C  
ATOM    199  O   PRO A  27      11.934  15.731  19.072  1.00 46.06      A    O  
ANISOU  199  O   PRO A  27     6490   5370   5640    370   -500   -960  A    O  
ATOM    200  CB  PRO A  27      14.672  17.005  19.309  1.00 59.05      A    C  
ANISOU  200  CB  PRO A  27     7560   6960   7920    480   -630  -1560  A    C  
ATOM    201  CG  PRO A  27      15.636  17.563  18.266  1.00 63.34      A    C  
ANISOU  201  CG  PRO A  27     7830   7460   8780    300   -360  -1830  A    C  
ATOM    202  CD  PRO A  27      15.618  16.557  17.097  1.00 67.03      A    C  
ANISOU  202  CD  PRO A  27     8340   7850   9280    170   -120  -1840  A    C  
ATOM    203  N   ASP A  28      12.875  13.675  19.125  1.00 47.27      A    N  
ANISOU  203  N   ASP A  28     6630   5360   5970    580   -680  -1080  A    N  
ATOM    204  CA  ASP A  28      11.743  12.883  19.668  1.00 47.19      A    C  
ANISOU  204  CA  ASP A  28     6930   5330   5660    620   -720   -830  A    C  
ATOM    205  C   ASP A  28      11.667  13.145  21.173  1.00 46.53      A    C  
ANISOU  205  C   ASP A  28     7030   5220   5420    790   -980   -780  A    C  
ATOM    206  O   ASP A  28      12.603  12.755  21.878  1.00 54.14      A    O  
ANISOU  206  O   ASP A  28     7990   6090   6500    990  -1270   -900  A    O  
ATOM    207  CB  ASP A  28      11.874  11.382  19.339  1.00 49.54      A    C  
ANISOU  207  CB  ASP A  28     7300   5520   6010    690   -730   -820  A    C  
ATOM    208  CG  ASP A  28      10.692  10.493  19.762  1.00 50.41      A    C  
ANISOU  208  CG  ASP A  28     7740   5590   5830    690   -710   -580  A    C  
ATOM    209  OD1 ASP A  28       9.900  10.910  20.653  1.00 51.27      A    O  
ANISOU  209  OD1 ASP A  28     8060   5720   5710    690   -740   -450  A    O  
ATOM    210  OD2 ASP A  28      10.569   9.350  19.223  1.00 52.16      A    O1-
ANISOU  210  OD2 ASP A  28     8010   5740   6070    680   -630   -550  A    O1-
ATOM    211  N   ILE A  29      10.543  13.653  21.657  1.00 42.68      A    N  
ANISOU  211  N   ILE A  29     6740   4790   4680    710   -890   -610  A    N  
ATOM    212  CA  ILE A  29      10.354  14.130  23.054  1.00 44.02      A    C  
ANISOU  212  CA  ILE A  29     7130   4940   4660    790  -1050   -580  A    C  
ATOM    213  C   ILE A  29       9.413  13.177  23.764  1.00 44.70      A    C  
ANISOU  213  C   ILE A  29     7610   4920   4450    800  -1020   -400  A    C  
ATOM    214  O   ILE A  29       9.094  13.415  24.932  1.00 46.65      A    O  
ANISOU  214  O   ILE A  29     8150   5110   4470    830  -1090   -360  A    O  
ATOM    215  CB  ILE A  29       9.760  15.559  23.058  1.00 43.55      A    C  
ANISOU  215  CB  ILE A  29     6960   5000   4580    650   -890   -560  A    C  
ATOM    216  CG1 ILE A  29       8.300  15.584  22.597  1.00 40.86      A    C  
ANISOU  216  CG1 ILE A  29     6700   4690   4140    470   -620   -410  A    C  
ATOM    217  CG2 ILE A  29      10.615  16.464  22.206  1.00 43.93      A    C  
ANISOU  217  CG2 ILE A  29     6660   5130   4900    600   -860   -720  A    C  
ATOM    218  CD1 ILE A  29       7.624  16.925  22.726  1.00 40.44      A    C  
ANISOU  218  CD1 ILE A  29     6560   4700   4100    360   -510   -400  A    C  
ATOM    219  N   PHE A  30       8.927  12.158  23.075  1.00 47.54      A    N  
ANISOU  219  N   PHE A  30     8020   5240   4810    750   -870   -320  A    N  
ATOM    220  CA  PHE A  30       7.805  11.333  23.580  1.00 48.93      A    C  
ANISOU  220  CA  PHE A  30     8550   5310   4730    690   -730   -160  A    C  
ATOM    221  C   PHE A  30       8.282  10.316  24.601  1.00 56.81      A    C  
ANISOU  221  C   PHE A  30     9930   6110   5540    860   -970   -130  A    C  
ATOM    222  O   PHE A  30       7.512   9.396  24.862  1.00 62.16      A    O  
ANISOU  222  O   PHE A  30    10920   6670   6030    810   -830    -10  A    O  
ATOM    223  CB  PHE A  30       7.073  10.725  22.397  1.00 43.42      A    C  
ANISOU  223  CB  PHE A  30     7730   4640   4120    550   -490   -100  A    C  
ATOM    224  CG  PHE A  30       6.426  11.827  21.615  1.00 41.91      A    C  
ANISOU  224  CG  PHE A  30     7280   4590   4050    390   -320   -110  A    C  
ATOM    225  CD1 PHE A  30       5.506  12.648  22.226  1.00 40.02      A    C  
ANISOU  225  CD1 PHE A  30     7100   4360   3740    300   -200    -90  A    C  
ATOM    226  CD2 PHE A  30       6.826  12.118  20.335  1.00 38.14      A    C  
ANISOU  226  CD2 PHE A  30     6540   4200   3760    320   -290   -170  A    C  
ATOM    227  CE1 PHE A  30       4.879  13.655  21.533  1.00 38.35      A    C  
ANISOU  227  CE1 PHE A  30     6660   4240   3670    170   -100   -100  A    C  
ATOM    228  CE2 PHE A  30       6.200  13.127  19.649  1.00 38.28      A    C  
ANISOU  228  CE2 PHE A  30     6400   4300   3850    170   -180   -160  A    C  
ATOM    229  CZ  PHE A  30       5.217  13.880  20.243  1.00 36.61      A    C  
ANISOU  229  CZ  PHE A  30     6230   4090   3590    110   -120   -120  A    C  
ATOM    230  N   LYS A  31       9.483  10.481  25.147  1.00 66.07      A    N  
ANISOU  230  N   LYS A  31    11090   7230   6780   1050  -1330   -240  A    N  
ATOM    231  CA  LYS A  31       9.878   9.774  26.391  1.00 79.77      A    C  
ANISOU  231  CA  LYS A  31    13300   8740   8260   1230  -1660   -200  A    C  
ATOM    232  C   LYS A  31       9.660  10.735  27.567  1.00 78.84      A    C  
ANISOU  232  C   LYS A  31    13450   8620   7890   1200  -1720   -190  A    C  
ATOM    233  O   LYS A  31       9.188  10.295  28.603  1.00 80.33      A    O  
ANISOU  233  O   LYS A  31    14190   8620   7700   1180  -1730    -90  A    O  
ATOM    234  CB  LYS A  31      11.301   9.228  26.232  1.00 88.00      A    C  
ANISOU  234  CB  LYS A  31    14170   9680   9590   1480  -2070   -340  A    C  
ATOM    235  CG  LYS A  31      11.495   8.321  25.022  1.00 92.44      A    C  
ANISOU  235  CG  LYS A  31    14450  10250  10430   1470  -1940   -380  A    C  
ATOM    236  CD  LYS A  31      10.727   7.004  25.092  1.00 98.97      A    C  
ANISOU  236  CD  LYS A  31    15660  10920  11030   1440  -1810   -200  A    C  
ATOM    237  CE  LYS A  31      11.241   6.062  26.168  1.00106.22      A    C  
ANISOU  237  CE  LYS A  31    17050  11540  11770   1670  -2230   -150  A    C  
ATOM    238  NZ  LYS A  31      10.877   4.648  25.901  1.00105.61      A    N1+
ANISOU  238  NZ  LYS A  31    17210  11290  11630   1670  -2140    -40  A    N1+
ATOM    239  N   GLN A  32       9.902  12.026  27.360  1.00 77.59      A    N  
ANISOU  239  N   GLN A  32    12940   8640   7900   1150  -1690   -310  A    N  
ATOM    240  CA  GLN A  32       9.749  13.073  28.396  1.00 76.10      A    C  
ANISOU  240  CA  GLN A  32    12930   8460   7520   1110  -1730   -340  A    C  
ATOM    241  C   GLN A  32       8.270  13.388  28.631  1.00 72.67      A    C  
ANISOU  241  C   GLN A  32    12690   8050   6870    860  -1280   -230  A    C  
ATOM    242  O   GLN A  32       7.924  13.870  29.727  1.00 76.24      A    O  
ANISOU  242  O   GLN A  32    13500   8430   7040    800  -1250   -230  A    O  
ATOM    243  CB  GLN A  32      10.515  14.319  27.969  1.00 77.76      A    C  
ANISOU  243  CB  GLN A  32    12650   8850   8040   1140  -1810   -510  A    C  
ATOM    244  CG  GLN A  32      12.023  14.136  28.059  1.00 85.60      A    C  
ANISOU  244  CG  GLN A  32    13470   9780   9280   1380  -2270   -700  A    C  
ATOM    245  CD  GLN A  32      12.634  13.649  26.770  1.00 89.21      A    C  
ANISOU  245  CD  GLN A  32    13490  10280  10130   1410  -2230   -790  A    C  
ATOM    246  NE2 GLN A  32      12.685  14.529  25.776  1.00 86.34      A    N  
ANISOU  246  NE2 GLN A  32    12690  10090  10030   1280  -1970   -880  A    N  
ATOM    247  OE1 GLN A  32      13.047  12.495  26.663  1.00 96.97      A    O  
ANISOU  247  OE1 GLN A  32    14550  11120  11180   1550  -2410   -790  A    O  
ATOM    248  N   VAL A  33       7.419  13.141  27.644  1.00 66.54      A    N  
ANISOU  248  N   VAL A  33    11700   7350   6230    720   -950   -170  A    N  
ATOM    249  CA  VAL A  33       6.010  13.619  27.678  1.00 61.63      A    C  
ANISOU  249  CA  VAL A  33    11090   6750   5570    490   -530   -140  A    C  
ATOM    250  C   VAL A  33       5.230  12.886  26.588  1.00 58.16      A    C  
ANISOU  250  C   VAL A  33    10480   6330   5290    390   -290    -70  A    C  
ATOM    251  O   VAL A  33       5.862  12.374  25.664  1.00 61.55      A    O  
ANISOU  251  O   VAL A  33    10690   6820   5880    480   -420    -70  A    O  
ATOM    252  CB  VAL A  33       5.968  15.151  27.537  1.00 59.26      A    C  
ANISOU  252  CB  VAL A  33    10450   6620   5450    420   -470   -230  A    C  
ATOM    253  CG1 VAL A  33       6.717  15.633  26.301  1.00 60.69      A    C  
ANISOU  253  CG1 VAL A  33    10140   6960   5960    480   -590   -290  A    C  
ATOM    254  CG2 VAL A  33       4.547  15.674  27.561  1.00 59.27      A    C  
ANISOU  254  CG2 VAL A  33    10410   6610   5500    200    -90   -240  A    C  
ATOM    255  N   SER A  34       3.914  12.775  26.724  1.00 54.04      A    N  
ANISOU  255  N   SER A  34    10060   5740   4730    200     60    -50  A    N  
ATOM    256  CA  SER A  34       3.099  11.870  25.883  1.00 55.33      A    C  
ANISOU  256  CA  SER A  34    10140   5870   5010    110    280    -10  A    C  
ATOM    257  C   SER A  34       1.684  12.423  25.800  1.00 49.46      A    C  
ANISOU  257  C   SER A  34     9250   5110   4430   -100    620    -80  A    C  
ATOM    258  O   SER A  34       1.335  13.254  26.654  1.00 44.84      A    O  
ANISOU  258  O   SER A  34     8760   4490   3790   -180    740   -150  A    O  
ATOM    259  CB  SER A  34       3.091  10.447  26.448  1.00 61.96      A    C  
ANISOU  259  CB  SER A  34    11450   6510   5590    140    300     70  A    C  
ATOM    260  OG  SER A  34       4.198  10.239  27.299  1.00 68.71      A    O  
ANISOU  260  OG  SER A  34    12630   7280   6200    320    -20    100  A    O  
ATOM    261  N   ASN A  35       0.902  11.964  24.820  1.00 45.16      A    N  
ANISOU  261  N   ASN A  35     8490   4580   4100   -180    760    -80  A    N  
ATOM    262  CA  ASN A  35      -0.545  12.311  24.758  1.00 49.43      A    C  
ANISOU  262  CA  ASN A  35     8870   5040   4870   -370   1070   -190  A    C  
ATOM    263  C   ASN A  35      -0.735  13.828  24.992  1.00 47.64      A    C  
ANISOU  263  C   ASN A  35     8410   4890   4810   -410   1070   -280  A    C  
ATOM    264  O   ASN A  35      -1.450  14.185  25.921  1.00 52.74      A    O  
ANISOU  264  O   ASN A  35     9180   5410   5450   -540   1330   -390  A    O  
ATOM    265  CB  ASN A  35      -1.351  11.554  25.811  1.00 53.76      A    C  
ANISOU  265  CB  ASN A  35     9810   5370   5250   -520   1430   -240  A    C  
ATOM    266  CG  ASN A  35      -2.849  11.654  25.611  1.00 59.40      A    C  
ANISOU  266  CG  ASN A  35    10300   5970   6300   -720   1780   -410  A    C  
ATOM    267  ND2 ASN A  35      -3.613  11.431  26.667  1.00 70.41      A    N  
ANISOU  267  ND2 ASN A  35    11990   7150   7610   -900   2180   -530  A    N  
ATOM    268  OD1 ASN A  35      -3.314  11.917  24.509  1.00 62.37      A    O  
ANISOU  268  OD1 ASN A  35    10250   6420   7030   -720   1690   -450  A    O  
ATOM    269  N   ILE A  36      -0.106  14.674  24.185  1.00 44.00      A    N  
ANISOU  269  N   ILE A  36     7650   4590   4480   -320    800   -250  A    N  
ATOM    270  CA  ILE A  36      -0.205  16.167  24.299  1.00 42.12      A    C  
ANISOU  270  CA  ILE A  36     7180   4410   4410   -340    770   -320  A    C  
ATOM    271  C   ILE A  36      -1.439  16.634  23.539  1.00 42.44      A    C  
ANISOU  271  C   ILE A  36     6890   4400   4840   -450    850   -410  A    C  
ATOM    272  O   ILE A  36      -1.459  16.523  22.295  1.00 38.42      A    O  
ANISOU  272  O   ILE A  36     6190   3940   4470   -430    670   -350  A    O  
ATOM    273  CB  ILE A  36       1.051  16.833  23.736  1.00 39.07      A    C  
ANISOU  273  CB  ILE A  36     6650   4190   4000   -220    470   -270  A    C  
ATOM    274  CG1 ILE A  36       2.302  16.250  24.378  1.00 39.88      A    C  
ANISOU  274  CG1 ILE A  36     7020   4320   3820    -80    320   -220  A    C  
ATOM    275  CG2 ILE A  36       1.004  18.341  23.873  1.00 39.47      A    C  
ANISOU  275  CG2 ILE A  36     6500   4290   4210   -240    440   -340  A    C  
ATOM    276  CD1 ILE A  36       3.586  16.747  23.763  1.00 39.22      A    C  
ANISOU  276  CD1 ILE A  36     6760   4370   3780     30     70   -220  A    C  
ATOM    277  N   THR A  37      -2.399  17.188  24.266  1.00 47.66      A    N  
ANISOU  277  N   THR A  37     7490   4940   5680   -570   1090   -560  A    N  
ATOM    278  CA  THR A  37      -3.556  17.935  23.716  1.00 51.79      A    C  
ANISOU  278  CA  THR A  37     7640   5380   6660   -650   1110   -690  A    C  
ATOM    279  C   THR A  37      -3.349  19.446  23.961  1.00 53.89      A    C  
ANISOU  279  C   THR A  37     7730   5690   7060   -630   1020   -750  A    C  
ATOM    280  O   THR A  37      -3.003  19.842  25.096  1.00 55.19      A    O  
ANISOU  280  O   THR A  37     8080   5850   7040   -660   1170   -790  A    O  
ATOM    281  CB  THR A  37      -4.874  17.451  24.346  1.00 55.29      A    C  
ANISOU  281  CB  THR A  37     8070   5610   7330   -820   1500   -900  A    C  
ATOM    282  CG2 THR A  37      -6.084  17.728  23.465  1.00 53.26      A    C  
ANISOU  282  CG2 THR A  37     7390   5230   7620   -870   1450  -1050  A    C  
ATOM    283  OG1 THR A  37      -4.739  16.055  24.669  1.00 57.80      A    O  
ANISOU  283  OG1 THR A  37     8730   5880   7350   -850   1670   -830  A    O  
ATOM    284  N   GLU A  38      -3.546  20.272  22.942  1.00 50.40      A    N  
ANISOU  284  N   GLU A  38     7000   5260   6900   -590    770   -730  A    N  
ATOM    285  CA  GLU A  38      -3.469  21.739  23.068  1.00 49.31      A    C  
ANISOU  285  CA  GLU A  38     6680   5120   6930   -580    680   -790  A    C  
ATOM    286  C   GLU A  38      -4.871  22.285  22.827  1.00 52.88      A    C  
ANISOU  286  C   GLU A  38     6790   5380   7920   -650    700   -970  A    C  
ATOM    287  O   GLU A  38      -5.535  21.707  21.980  1.00 59.15      A    O  
ANISOU  287  O   GLU A  38     7470   6090   8920   -650    590   -980  A    O  
ATOM    288  CB  GLU A  38      -2.459  22.290  22.068  1.00 47.19      A    C  
ANISOU  288  CB  GLU A  38     6390   4990   6550   -470    340   -620  A    C  
ATOM    289  CG  GLU A  38      -0.991  21.930  22.338  1.00 44.48      A    C  
ANISOU  289  CG  GLU A  38     6290   4820   5790   -400    310   -510  A    C  
ATOM    290  CD  GLU A  38      -0.136  22.265  21.140  1.00 42.98      A    C  
ANISOU  290  CD  GLU A  38     6080   4720   5540   -350     50   -390  A    C  
ATOM    291  OE1 GLU A  38      -0.197  21.467  20.186  1.00 42.78      A    O  
ANISOU  291  OE1 GLU A  38     6090   4680   5480   -350    -30   -310  A    O  
ATOM    292  OE2 GLU A  38       0.492  23.373  21.108  1.00 42.44      A    O1-
ANISOU  292  OE2 GLU A  38     5950   4690   5480   -330    -30   -400  A    O1-
ATOM    293  N   PHE A  39      -5.326  23.285  23.591  1.00 54.91      A    N  
ANISOU  293  N   PHE A  39     6900   5540   8420   -700    860  -1150  A    N  
ATOM    294  CA  PHE A  39      -6.545  24.065  23.266  1.00 60.08      A    C  
ANISOU  294  CA  PHE A  39     7160   5980   9690   -740    800  -1350  A    C  
ATOM    295  C   PHE A  39      -6.229  25.560  23.441  1.00 58.15      A    C  
ANISOU  295  C   PHE A  39     6780   5740   9560   -700    680  -1360  A    C  
ATOM    296  O   PHE A  39      -5.763  26.050  24.515  1.00 55.42      A    O  
ANISOU  296  O   PHE A  39     6560   5460   9040   -740    920  -1420  A    O  
ATOM    297  CB  PHE A  39      -7.762  23.598  24.079  1.00 71.04      A    C  
ANISOU  297  CB  PHE A  39     8410   7160  11420   -900   1220  -1640  A    C  
ATOM    298  CG  PHE A  39      -9.068  24.208  23.606  1.00 84.41      A    C  
ANISOU  298  CG  PHE A  39     9630   8600  13840   -910   1110  -1890  A    C  
ATOM    299  CD1 PHE A  39      -9.832  23.596  22.616  1.00 92.15      A    C  
ANISOU  299  CD1 PHE A  39    10410   9460  15150   -880    880  -1940  A    C  
ATOM    300  CD2 PHE A  39      -9.522  25.425  24.114  1.00 89.14      A    C  
ANISOU  300  CD2 PHE A  39     9960   9060  14850   -940   1190  -2100  A    C  
ATOM    301  CE1 PHE A  39     -11.013  24.176  22.163  1.00 96.60      A    C  
ANISOU  301  CE1 PHE A  39    10510   9750  16440   -860    690  -2190  A    C  
ATOM    302  CE2 PHE A  39     -10.695  26.006  23.651  1.00 91.86      A    C  
ANISOU  302  CE2 PHE A  39     9830   9130  15940   -930   1030  -2350  A    C  
ATOM    303  CZ  PHE A  39     -11.440  25.382  22.677  1.00 95.36      A    C  
ANISOU  303  CZ  PHE A  39    10080   9450  16710   -880    750  -2400  A    C  
ATOM    304  N   TYR A  40      -6.421  26.292  22.367  1.00 56.16      A    N  
ANISOU  304  N   TYR A  40     6340   5420   9580   -610    290  -1310  A    N  
ATOM    305  CA  TYR A  40      -6.102  27.734  22.308  1.00 62.38      A    C  
ANISOU  305  CA  TYR A  40     7030   6190  10490   -560    120  -1290  A    C  
ATOM    306  C   TYR A  40      -7.386  28.507  21.991  1.00 68.39      A    C  
ANISOU  306  C   TYR A  40     7400   6660  11930   -550    -40  -1500  A    C  
ATOM    307  O   TYR A  40      -8.058  28.152  20.973  1.00 65.83      A    O  
ANISOU  307  O   TYR A  40     6960   6190  11860   -500   -360  -1490  A    O  
ATOM    308  CB  TYR A  40      -5.018  28.011  21.261  1.00 59.50      A    C  
ANISOU  308  CB  TYR A  40     6870   5950   9780   -470   -230  -1020  A    C  
ATOM    309  CG  TYR A  40      -3.694  27.374  21.585  1.00 59.44      A    C  
ANISOU  309  CG  TYR A  40     7170   6200   9210   -460    -90   -870  A    C  
ATOM    310  CD1 TYR A  40      -2.925  27.845  22.624  1.00 58.75      A    C  
ANISOU  310  CD1 TYR A  40     7170   6240   8920   -480    110   -910  A    C  
ATOM    311  CD2 TYR A  40      -3.225  26.285  20.871  1.00 57.62      A    C  
ANISOU  311  CD2 TYR A  40     7140   6070   8690   -440   -180   -720  A    C  
ATOM    312  CE1 TYR A  40      -1.713  27.266  22.945  1.00 56.03      A    C  
ANISOU  312  CE1 TYR A  40     7070   6090   8120   -450    170   -810  A    C  
ATOM    313  CE2 TYR A  40      -2.013  25.703  21.179  1.00 57.37      A    C  
ANISOU  313  CE2 TYR A  40     7340   6240   8220   -420    -80   -620  A    C  
ATOM    314  CZ  TYR A  40      -1.262  26.189  22.222  1.00 53.88      A    C  
ANISOU  314  CZ  TYR A  40     6960   5900   7610   -410     70   -670  A    C  
ATOM    315  OH  TYR A  40      -0.087  25.605  22.542  1.00 51.56      A    O  
ANISOU  315  OH  TYR A  40     6870   5770   6950   -370    100   -600  A    O  
ATOM    316  N   SER A  41      -7.673  29.531  22.814  1.00 72.04      A    N  
ANISOU  316  N   SER A  41     7660   7020  12690   -590    140  -1690  A    N  
ATOM    317  CA  SER A  41      -8.602  30.648  22.505  1.00 73.65      A    C  
ANISOU  317  CA  SER A  41     7490   6940  13550   -550    -90  -1870  A    C  
ATOM    318  C   SER A  41      -7.807  31.878  22.014  1.00 67.52      A    C  
ANISOU  318  C   SER A  41     6810   6200  12640   -450   -400  -1690  A    C  
ATOM    319  O   SER A  41      -6.833  32.305  22.704  1.00 67.02      A    O  
ANISOU  319  O   SER A  41     6930   6330  12200   -490   -180  -1620  A    O  
ATOM    320  CB  SER A  41      -9.483  30.948  23.704  1.00 80.27      A    C  
ANISOU  320  CB  SER A  41     8030   7610  14850   -680    360  -2250  A    C  
ATOM    321  OG  SER A  41      -8.706  31.391  24.817  1.00 79.89      A    O  
ANISOU  321  OG  SER A  41     8180   7730  14450   -760    720  -2250  A    O  
ATOM    322  N   ALA A  42      -8.200  32.418  20.854  1.00 63.22      A    N  
ANISOU  322  N   ALA A  42     6190   5450  12380   -350   -910  -1610  A    N  
ATOM    323  CA  ALA A  42      -7.639  33.630  20.208  1.00 64.65      A    C  
ANISOU  323  CA  ALA A  42     6500   5570  12490   -270  -1260  -1440  A    C  
ATOM    324  C   ALA A  42      -8.146  34.942  20.861  1.00 62.38      A    C  
ANISOU  324  C   ALA A  42     5890   5080  12720   -260  -1200  -1660  A    C  
ATOM    325  O   ALA A  42      -9.367  35.126  20.995  1.00 65.49      A    O  
ANISOU  325  O   ALA A  42     5890   5200  13790   -240  -1260  -1940  A    O  
ATOM    326  CB  ALA A  42      -8.004  33.623  18.733  1.00 66.07      A    C  
ANISOU  326  CB  ALA A  42     6800   5540  12770   -170  -1850  -1290  A    C  
ATOM    327  N   HIS A  43      -7.224  35.850  21.157  1.00 59.40      A    N  
ANISOU  327  N   HIS A  43     5660   4820  12090   -270  -1110  -1570  A    N  
ATOM    328  CA  HIS A  43      -7.435  37.221  21.690  1.00 60.29      A    C  
ANISOU  328  CA  HIS A  43     5550   4770  12590   -260  -1060  -1730  A    C  
ATOM    329  C   HIS A  43      -6.559  38.166  20.864  1.00 58.53      A    C  
ANISOU  329  C   HIS A  43     5610   4530  12100   -200  -1380  -1470  A    C  
ATOM    330  O   HIS A  43      -5.693  38.738  21.460  1.00 58.45      A    O  
ANISOU  330  O   HIS A  43     5690   4690  11830   -260  -1130  -1450  A    O  
ATOM    331  CB  HIS A  43      -7.099  37.266  23.201  1.00 57.60      A    C  
ANISOU  331  CB  HIS A  43     5140   4630  12130   -390   -480  -1910  A    C  
ATOM    332  CG  HIS A  43      -7.959  36.352  24.014  1.00 58.64      A    C  
ANISOU  332  CG  HIS A  43     5070   4730  12480   -490   -100  -2170  A    C  
ATOM    333  CD2 HIS A  43      -7.970  34.999  24.131  1.00 59.49      A    C  
ANISOU  333  CD2 HIS A  43     5330   4980  12300   -550     70  -2140  A    C  
ATOM    334  ND1 HIS A  43      -9.056  36.802  24.727  1.00 60.94      A    N  
ANISOU  334  ND1 HIS A  43     4960   4770  13430   -560    130  -2540  A    N  
ATOM    335  CE1 HIS A  43      -9.682  35.797  25.315  1.00 63.02      A    C  
ANISOU  335  CE1 HIS A  43     5150   5020  13780   -680    490  -2740  A    C  
ATOM    336  NE2 HIS A  43      -9.036  34.655  24.956  1.00 64.96      A    N  
ANISOU  336  NE2 HIS A  43     5750   5510  13430   -670    450  -2480  A    N  
ATOM    337  N   GLY A  44      -6.771  38.241  19.540  1.00 64.53      A    N  
ANISOU  337  N   GLY A  44     6550   5090  12880   -110  -1910  -1290  A    N  
ATOM    338  CA  GLY A  44      -5.984  39.020  18.546  1.00 68.83      A    C  
ANISOU  338  CA  GLY A  44     7490   5550  13110    -90  -2220  -1020  A    C  
ATOM    339  C   GLY A  44      -4.631  38.370  18.235  1.00 72.46      A    C  
ANISOU  339  C   GLY A  44     8370   6330  12830   -180  -2030   -790  A    C  
ATOM    340  O   GLY A  44      -4.580  37.317  17.583  1.00 80.87      A    O  
ANISOU  340  O   GLY A  44     9630   7470  13630   -190  -2130   -670  A    O  
ATOM    341  N   ASN A  45      -3.554  38.961  18.729  1.00 76.12      A    N  
ANISOU  341  N   ASN A  45     8930   6970  13010   -240  -1740   -770  A    N  
ATOM    342  CA  ASN A  45      -2.165  38.440  18.621  1.00 75.50      A    C  
ANISOU  342  CA  ASN A  45     9160   7190  12330   -330  -1510   -630  A    C  
ATOM    343  C   ASN A  45      -1.848  37.592  19.850  1.00 68.89      A    C  
ANISOU  343  C   ASN A  45     8140   6670  11360   -360  -1100   -770  A    C  
ATOM    344  O   ASN A  45      -0.810  36.942  19.883  1.00 73.12      A    O  
ANISOU  344  O   ASN A  45     8860   7450  11470   -400   -920   -700  A    O  
ATOM    345  CB  ASN A  45      -1.160  39.588  18.471  1.00 78.06      A    C  
ANISOU  345  CB  ASN A  45     9670   7500  12490   -390  -1440   -580  A    C  
ATOM    346  CG  ASN A  45      -1.180  40.166  17.073  1.00 80.61      A    C  
ANISOU  346  CG  ASN A  45    10370   7520  12730   -400  -1810   -380  A    C  
ATOM    347  ND2 ASN A  45      -0.895  41.456  16.952  1.00 84.71      A    N  
ANISOU  347  ND2 ASN A  45    10990   7870  13330   -430  -1850   -360  A    N  
ATOM    348  OD1 ASN A  45      -1.444  39.439  16.112  1.00 79.92      A    O  
ANISOU  348  OD1 ASN A  45    10530   7350  12490   -400  -2060   -240  A    O  
ATOM    349  N   ASP A  46      -2.701  37.657  20.849  1.00 64.69      A    N  
ANISOU  349  N   ASP A  46     7280   6100  11190   -340   -940   -980  A    N  
ATOM    350  CA  ASP A  46      -2.533  36.876  22.090  1.00 63.58      A    C  
ANISOU  350  CA  ASP A  46     7060   6200  10900   -390   -550  -1120  A    C  
ATOM    351  C   ASP A  46      -3.368  35.609  21.852  1.00 65.33      A    C  
ANISOU  351  C   ASP A  46     7240   6390  11190   -380   -590  -1130  A    C  
ATOM    352  O   ASP A  46      -4.485  35.717  21.239  1.00 64.08      A    O  
ANISOU  352  O   ASP A  46     6920   5970  11460   -330   -860  -1170  A    O  
ATOM    353  CB  ASP A  46      -2.875  37.729  23.327  1.00 65.50      A    C  
ANISOU  353  CB  ASP A  46     7050   6400  11440   -430   -280  -1360  A    C  
ATOM    354  CG  ASP A  46      -1.828  38.791  23.720  1.00 67.10      A    C  
ANISOU  354  CG  ASP A  46     7320   6700  11470   -460   -180  -1360  A    C  
ATOM    355  OD1 ASP A  46      -0.637  38.412  23.897  1.00 71.12      A    O  
ANISOU  355  OD1 ASP A  46     8030   7460  11540   -480    -70  -1290  A    O  
ATOM    356  OD2 ASP A  46      -2.196  39.989  23.877  1.00 70.60      A    O1-
ANISOU  356  OD2 ASP A  46     7580   6970  12270   -460   -200  -1470  A    O1-
ATOM    357  N   TYR A  47      -2.835  34.437  22.210  1.00 57.73      A    N  
ANISOU  357  N   TYR A  47     6430   5660   9840   -410   -400  -1080  A    N  
ATOM    358  CA  TYR A  47      -3.685  33.260  22.483  1.00 53.57      A    C  
ANISOU  358  CA  TYR A  47     5830   5110   9410   -430   -280  -1170  A    C  
ATOM    359  C   TYR A  47      -3.478  32.899  23.944  1.00 53.86      A    C  
ANISOU  359  C   TYR A  47     5900   5290   9280   -510    140  -1320  A    C  
ATOM    360  O   TYR A  47      -2.410  33.209  24.451  1.00 48.92      A    O  
ANISOU  360  O   TYR A  47     5430   4830   8330   -510    230  -1280  A    O  
ATOM    361  CB  TYR A  47      -3.355  32.118  21.545  1.00 51.09      A    C  
ANISOU  361  CB  TYR A  47     5740   4880   8790   -400   -440   -980  A    C  
ATOM    362  CG  TYR A  47      -3.766  32.278  20.110  1.00 50.79      A    C  
ANISOU  362  CG  TYR A  47     5740   4660   8900   -350   -860   -850  A    C  
ATOM    363  CD1 TYR A  47      -3.049  33.058  19.234  1.00 50.48      A    C  
ANISOU  363  CD1 TYR A  47     5900   4590   8690   -340  -1090   -680  A    C  
ATOM    364  CD2 TYR A  47      -4.822  31.547  19.604  1.00 50.90      A    C  
ANISOU  364  CD2 TYR A  47     5650   4520   9160   -340  -1020   -890  A    C  
ATOM    365  CE1 TYR A  47      -3.395  33.141  17.896  1.00 52.12      A    C  
ANISOU  365  CE1 TYR A  47     6270   4590   8940   -320  -1490   -550  A    C  
ATOM    366  CE2 TYR A  47      -5.213  31.659  18.286  1.00 52.71      A    C  
ANISOU  366  CE2 TYR A  47     5970   4560   9490   -290  -1460   -770  A    C  
ATOM    367  CZ  TYR A  47      -4.482  32.441  17.418  1.00 52.85      A    C  
ANISOU  367  CZ  TYR A  47     6260   4530   9280   -280  -1710   -590  A    C  
ATOM    368  OH  TYR A  47      -4.837  32.480  16.097  1.00 58.89      A    O  
ANISOU  368  OH  TYR A  47     7230   5080  10060   -260  -2160   -450  A    O  
ATOM    369  N   TYR A  48      -4.494  32.334  24.593  1.00 58.61      A    N  
ANISOU  369  N   TYR A  48     6380   5780  10120   -580    390  -1500  A    N  
ATOM    370  CA  TYR A  48      -4.389  31.743  25.951  1.00 61.55      A    C  
ANISOU  370  CA  TYR A  48     6900   6240  10240   -690    810  -1630  A    C  
ATOM    371  C   TYR A  48      -4.948  30.339  25.827  1.00 60.28      A    C  
ANISOU  371  C   TYR A  48     6820   6050  10030   -730    910  -1630  A    C  
ATOM    372  O   TYR A  48      -5.797  30.106  24.938  1.00 62.66      A    O  
ANISOU  372  O   TYR A  48     6920   6200  10690   -700    720  -1650  A    O  
ATOM    373  CB  TYR A  48      -5.157  32.535  27.015  1.00 66.62      A    C  
ANISOU  373  CB  TYR A  48     7350   6720  11240   -820   1140  -1930  A    C  
ATOM    374  CG  TYR A  48      -4.682  33.951  27.202  1.00 68.90      A    C  
ANISOU  374  CG  TYR A  48     7540   7010  11620   -790   1070  -1960  A    C  
ATOM    375  CD1 TYR A  48      -3.661  34.260  28.083  1.00 69.82      A    C  
ANISOU  375  CD1 TYR A  48     7890   7310  11330   -820   1220  -1940  A    C  
ATOM    376  CD2 TYR A  48      -5.258  34.989  26.491  1.00 71.19      A    C  
ANISOU  376  CD2 TYR A  48     7510   7110  12430   -730    830  -2000  A    C  
ATOM    377  CE1 TYR A  48      -3.197  35.558  28.226  1.00 67.78      A    C  
ANISOU  377  CE1 TYR A  48     7530   7060  11160   -810   1160  -1980  A    C  
ATOM    378  CE2 TYR A  48      -4.818  36.294  26.634  1.00 70.95      A    C  
ANISOU  378  CE2 TYR A  48     7410   7070  12490   -710    780  -2020  A    C  
ATOM    379  CZ  TYR A  48      -3.790  36.584  27.510  1.00 70.00      A    C  
ANISOU  379  CZ  TYR A  48     7500   7150  11950   -750    970  -2020  A    C  
ATOM    380  OH  TYR A  48      -3.372  37.882  27.651  1.00 68.28      A    O  
ANISOU  380  OH  TYR A  48     7190   6910  11850   -740    930  -2060  A    O  
ATOM    381  N   GLY A  49      -4.465  29.417  26.636  1.00 57.70      A    N  
ANISOU  381  N   GLY A  49     6810   5850   9260   -790   1150  -1610  A    N  
ATOM    382  CA  GLY A  49      -4.739  28.032  26.275  1.00 60.12      A    C  
ANISOU  382  CA  GLY A  49     7250   6150   9440   -790   1170  -1540  A    C  
ATOM    383  C   GLY A  49      -4.401  27.041  27.350  1.00 62.16      A    C  
ANISOU  383  C   GLY A  49     7890   6470   9260   -880   1480  -1550  A    C  
ATOM    384  O   GLY A  49      -3.787  27.410  28.376  1.00 59.96      A    O  
ANISOU  384  O   GLY A  49     7840   6250   8690   -920   1620  -1580  A    O  
ATOM    385  N   THR A  50      -4.710  25.796  27.019  1.00 62.17      A    N  
ANISOU  385  N   THR A  50     8000   6450   9180   -890   1510  -1490  A    N  
ATOM    386  CA  THR A  50      -4.454  24.606  27.853  1.00 65.97      A    C  
ANISOU  386  CA  THR A  50     8900   6940   9220   -960   1760  -1460  A    C  
ATOM    387  C   THR A  50      -3.698  23.594  26.986  1.00 61.80      A    C  
ANISOU  387  C   THR A  50     8520   6560   8400   -820   1470  -1220  A    C  
ATOM    388  O   THR A  50      -4.030  23.476  25.776  1.00 56.93      A    O  
ANISOU  388  O   THR A  50     7650   5940   8040   -760   1250  -1150  A    O  
ATOM    389  CB  THR A  50      -5.762  24.051  28.450  1.00 69.02      A    C  
ANISOU  389  CB  THR A  50     9280   7080   9860  -1160   2220  -1710  A    C  
ATOM    390  CG2 THR A  50      -5.510  23.154  29.642  1.00 70.46      A    C  
ANISOU  390  CG2 THR A  50    10020   7220   9540  -1290   2560  -1720  A    C  
ATOM    391  OG1 THR A  50      -6.582  25.154  28.857  1.00 74.89      A    O  
ANISOU  391  OG1 THR A  50     9720   7670  11060  -1280   2430  -1970  A    O  
ATOM    392  N   VAL A  51      -2.700  22.977  27.608  1.00 57.40      A    N  
ANISOU  392  N   VAL A  51     8360   6100   7350   -780   1460  -1100  A    N  
ATOM    393  CA  VAL A  51      -1.935  21.812  27.133  1.00 62.34      A    C  
ANISOU  393  CA  VAL A  51     9190   6830   7660   -670   1270   -910  A    C  
ATOM    394  C   VAL A  51      -2.089  20.696  28.175  1.00 66.36      A    C  
ANISOU  394  C   VAL A  51    10160   7220   7840   -760   1540   -930  A    C  
ATOM    395  O   VAL A  51      -1.549  20.849  29.286  1.00 68.99      A    O  
ANISOU  395  O   VAL A  51    10840   7540   7840   -780   1590   -950  A    O  
ATOM    396  CB  VAL A  51      -0.475  22.232  26.900  1.00 60.68      A    C  
ANISOU  396  CB  VAL A  51     9020   6810   7230   -510    930   -780  A    C  
ATOM    397  CG1 VAL A  51       0.451  21.038  26.679  1.00 61.47      A    C  
ANISOU  397  CG1 VAL A  51     9360   6980   7020   -390    760   -630  A    C  
ATOM    398  CG2 VAL A  51      -0.412  23.226  25.750  1.00 58.42      A    C  
ANISOU  398  CG2 VAL A  51     8350   6590   7250   -450    720   -750  A    C  
ATOM    399  N   THR A  52      -2.825  19.630  27.844  1.00 68.35      A    N  
ANISOU  399  N   THR A  52    10440   7370   8160   -820   1690   -940  A    N  
ATOM    400  CA  THR A  52      -2.973  18.427  28.709  1.00 69.82      A    C  
ANISOU  400  CA  THR A  52    11120   7400   8010   -920   1960   -930  A    C  
ATOM    401  C   THR A  52      -1.956  17.402  28.205  1.00 66.84      A    C  
ANISOU  401  C   THR A  52    10930   7140   7330   -740   1650   -720  A    C  
ATOM    402  O   THR A  52      -2.103  16.933  27.085  1.00 70.00      A    O  
ANISOU  402  O   THR A  52    11080   7590   7920   -690   1520   -650  A    O  
ATOM    403  CB  THR A  52      -4.431  17.957  28.756  1.00 73.01      A    C  
ANISOU  403  CB  THR A  52    11430   7590   8720  -1130   2390  -1130  A    C  
ATOM    404  CG2 THR A  52      -5.432  19.077  28.576  1.00 77.59      A    C  
ANISOU  404  CG2 THR A  52    11530   8100   9850  -1230   2530  -1360  A    C  
ATOM    405  OG1 THR A  52      -4.659  17.014  27.720  1.00 76.46      A    O  
ANISOU  405  OG1 THR A  52    11720   8050   9290  -1070   2280  -1040  A    O  
ATOM    406  N   ASP A  53      -0.903  17.171  28.978  1.00 66.25      A    N  
ANISOU  406  N   ASP A  53    11260   7080   6830   -650   1490   -620  A    N  
ATOM    407  CA  ASP A  53       0.204  16.237  28.672  1.00 66.19      A    C  
ANISOU  407  CA  ASP A  53    11440   7140   6570   -460   1160   -450  A    C  
ATOM    408  C   ASP A  53       0.166  15.088  29.711  1.00 75.27      A    C  
ANISOU  408  C   ASP A  53    13220   8080   7300   -520   1300   -410  A    C  
ATOM    409  O   ASP A  53      -0.405  15.280  30.816  1.00 74.00      A    O  
ANISOU  409  O   ASP A  53    13410   7750   6960   -690   1610   -510  A    O  
ATOM    410  CB  ASP A  53       1.492  17.061  28.660  1.00 65.16      A    C  
ANISOU  410  CB  ASP A  53    11190   7180   6390   -290    780   -420  A    C  
ATOM    411  CG  ASP A  53       2.096  17.193  30.040  1.00 68.84      A    C  
ANISOU  411  CG  ASP A  53    12130   7560   6470   -260    710   -440  A    C  
ATOM    412  OD1 ASP A  53       1.890  18.241  30.689  1.00 62.87      A    O  
ANISOU  412  OD1 ASP A  53    11360   6800   5720   -350    820   -550  A    O  
ATOM    413  OD2 ASP A  53       2.759  16.214  30.477  1.00 78.07      A    O1-
ANISOU  413  OD2 ASP A  53    13700   8640   7330   -160    510   -350  A    O1-
ATOM    414  N   TYR A  54       0.718  13.912  29.395  1.00 76.45      A    N  
ANISOU  414  N   TYR A  54    13550   8200   7290   -390   1120   -280  A    N  
ATOM    415  CA  TYR A  54       0.879  12.784  30.349  1.00 77.37      A    C  
ANISOU  415  CA  TYR A  54    14340   8090   6970   -400   1160   -200  A    C  
ATOM    416  C   TYR A  54       2.367  12.695  30.681  1.00 77.32      A    C  
ANISOU  416  C   TYR A  54    14530   8120   6720   -150    640   -110  A    C  
ATOM    417  O   TYR A  54       3.191  12.834  29.798  1.00 70.56      A    O  
ANISOU  417  O   TYR A  54    13270   7450   6090     30    320    -80  A    O  
ATOM    418  CB  TYR A  54       0.309  11.486  29.770  1.00 77.61      A    C  
ANISOU  418  CB  TYR A  54    14420   8020   7050   -450   1340   -150  A    C  
ATOM    419  CG  TYR A  54       0.622  10.264  30.592  1.00 86.15      A    C  
ANISOU  419  CG  TYR A  54    16190   8850   7690   -430   1310    -40  A    C  
ATOM    420  CD1 TYR A  54       1.802   9.541  30.416  1.00 88.06      A    C  
ANISOU  420  CD1 TYR A  54    16570   9100   7790   -180    850     90  A    C  
ATOM    421  CD2 TYR A  54      -0.246   9.842  31.597  1.00 95.35      A    C  
ANISOU  421  CD2 TYR A  54    17920   9730   8580   -670   1750   -100  A    C  
ATOM    422  CE1 TYR A  54       2.094   8.430  31.206  1.00 89.20      A    C  
ANISOU  422  CE1 TYR A  54    17400   8970   7520   -140    770    200  A    C  
ATOM    423  CE2 TYR A  54       0.033   8.736  32.395  1.00 93.30      A    C  
ANISOU  423  CE2 TYR A  54    18400   9200   7850   -670   1720     20  A    C  
ATOM    424  CZ  TYR A  54       1.208   8.030  32.200  1.00 92.55      A    C  
ANISOU  424  CZ  TYR A  54    18450   9110   7610   -380   1190    180  A    C  
ATOM    425  OH  TYR A  54       1.462   6.952  33.000  1.00 97.45      A    O  
ANISOU  425  OH  TYR A  54    19840   9410   7780   -360   1110    300  A    O  
ATOM    426  N   SER A  55       2.714  12.519  31.947  1.00 85.04      A    N  
ANISOU  426  N   SER A  55    16140   8900   7260   -150    550    -90  A    N  
ATOM    427  CA  SER A  55       4.132  12.510  32.388  1.00 88.15      A    C  
ANISOU  427  CA  SER A  55    16730   9300   7460    110    -20    -40  A    C  
ATOM    428  C   SER A  55       4.527  11.110  32.824  1.00 90.19      A    C  
ANISOU  428  C   SER A  55    17580   9300   7390    210   -230     90  A    C  
ATOM    429  O   SER A  55       3.785  10.466  33.555  1.00 94.34      A    O  
ANISOU  429  O   SER A  55    18700   9570   7570     40     70    130  A    O  
ATOM    430  CB  SER A  55       4.376  13.501  33.494  1.00 91.76      A    C  
ANISOU  430  CB  SER A  55    17470   9710   7680     60   -100   -120  A    C  
ATOM    431  OG  SER A  55       5.721  13.401  33.951  1.00 91.29      A    O  
ANISOU  431  OG  SER A  55    17620   9610   7450    320   -690   -100  A    O  
ATOM    432  N   PRO A  56       5.722  10.620  32.425  1.00 93.27      A    N  
ANISOU  432  N   PRO A  56    17840   9720   7880    500   -750    130  A    N  
ATOM    433  CA  PRO A  56       6.183   9.284  32.819  1.00 97.16      A    C  
ANISOU  433  CA  PRO A  56    18870   9940   8100    640  -1030    250  A    C  
ATOM    434  C   PRO A  56       6.685   9.194  34.273  1.00105.33      A    C  
ANISOU  434  C   PRO A  56    20720  10690   8620    710  -1370    290  A    C  
ATOM    435  O   PRO A  56       7.773   8.678  34.470  1.00113.24      A    O  
ANISOU  435  O   PRO A  56    21880  11560   9580    980  -1960    320  A    O  
ATOM    436  CB  PRO A  56       7.364   9.073  31.866  1.00 95.59      A    C  
ANISOU  436  CB  PRO A  56    18130   9890   8310    930  -1480    220  A    C  
ATOM    437  CG  PRO A  56       7.936  10.476  31.726  1.00 92.98      A    C  
ANISOU  437  CG  PRO A  56    17310   9800   8220    980  -1630     70  A    C  
ATOM    438  CD  PRO A  56       6.702  11.343  31.592  1.00 89.26      A    C  
ANISOU  438  CD  PRO A  56    16660   9470   7780    690  -1070     40  A    C  
ATOM    439  N   GLU A  57       5.905   9.707  35.237  1.00106.29      A    N  
ANISOU  439  N   GLU A  57    21320  10690   8370    450  -1030    270  A    N  
ATOM    440  CA  GLU A  57       6.179   9.689  36.707  1.00107.32      A    C  
ANISOU  440  CA  GLU A  57    22360  10510   7900    430  -1260    300  A    C  
ATOM    441  C   GLU A  57       5.083  10.467  37.444  1.00101.54      A    C  
ANISOU  441  C   GLU A  57    21930   9730   6920     70   -660    210  A    C  
ATOM    442  O   GLU A  57       4.559   9.941  38.445  1.00117.25      A    O  
ANISOU  442  O   GLU A  57    24800  11370   8370   -140   -420    260  A    O  
ATOM    443  CB  GLU A  57       7.544  10.281  37.074  1.00111.08      A    C  
ANISOU  443  CB  GLU A  57    22770  11030   8410    730  -2000    230  A    C  
ATOM    444  CG  GLU A  57       7.975  11.452  36.212  1.00111.88      A    C  
ANISOU  444  CG  GLU A  57    21910  11530   9070    820  -2050     80  A    C  
ATOM    445  CD  GLU A  57       9.386  11.930  36.500  1.00116.12      A    C  
ANISOU  445  CD  GLU A  57    22310  12090   9720   1120  -2770    -20  A    C  
ATOM    446  OE1 GLU A  57       9.536  13.102  36.924  1.00114.10      A    O  
ANISOU  446  OE1 GLU A  57    21940  11950   9460   1070  -2790   -150  A    O  
ATOM    447  OE2 GLU A  57      10.331  11.132  36.294  1.00117.08      A    O1-
ANISOU  447  OE2 GLU A  57    22420  12090   9980   1400  -3300    -10  A    O1-
ATOM    448  N   TYR A  58       4.769  11.675  36.987  1.00 87.87      A    N  
ANISOU  448  N   TYR A  58    19510   8300   5570    -20   -410     70  A    N  
ATOM    449  CA  TYR A  58       3.592  12.467  37.421  1.00 86.54      A    C  
ANISOU  449  CA  TYR A  58    19400   8120   5360   -380    250    -70  A    C  
ATOM    450  C   TYR A  58       2.403  12.078  36.553  1.00 84.21      A    C  
ANISOU  450  C   TYR A  58    18690   7880   5430   -570    840   -100  A    C  
ATOM    451  O   TYR A  58       2.578  11.305  35.556  1.00 81.53      A    O  
ANISOU  451  O   TYR A  58    17990   7630   5350   -410    690     -0  A    O  
ATOM    452  CB  TYR A  58       3.897  13.961  37.334  1.00 86.06      A    C  
ANISOU  452  CB  TYR A  58    18790   8330   5580   -350    150   -210  A    C  
ATOM    453  CG  TYR A  58       5.282  14.310  37.823  1.00 93.35      A    C  
ANISOU  453  CG  TYR A  58    19860   9270   6340    -70   -560   -200  A    C  
ATOM    454  CD1 TYR A  58       5.773  13.747  38.994  1.00 98.43      A    C  
ANISOU  454  CD1 TYR A  58    21420   9590   6390    -30   -900   -130  A    C  
ATOM    455  CD2 TYR A  58       6.101  15.209  37.150  1.00 92.89      A    C  
ANISOU  455  CD2 TYR A  58    19060   9510   6720    140   -900   -280  A    C  
ATOM    456  CE1 TYR A  58       7.048  14.014  39.460  1.00 99.20      A    C  
ANISOU  456  CE1 TYR A  58    21660   9670   6370    240  -1620   -140  A    C  
ATOM    457  CE2 TYR A  58       7.377  15.507  37.618  1.00 97.35      A    C  
ANISOU  457  CE2 TYR A  58    19730  10070   7190    380  -1540   -320  A    C  
ATOM    458  CZ  TYR A  58       7.849  14.904  38.777  1.00100.67      A    C  
ANISOU  458  CZ  TYR A  58    21030  10170   7060    450  -1930   -260  A    C  
ATOM    459  OH  TYR A  58       9.092  15.143  39.285  1.00106.96      A    O  
ANISOU  459  OH  TYR A  58    21950  10910   7780    710  -2640   -320  A    O  
ATOM    460  N   GLY A  59       1.227  12.636  36.836  1.00 84.11      A    N  
ANISOU  460  N   GLY A  59    18650   7820   5490   -900   1470   -260  A    N  
ATOM    461  CA  GLY A  59       0.031  12.239  36.055  1.00 88.67      A    C  
ANISOU  461  CA  GLY A  59    18830   8400   6460  -1080   2010   -330  A    C  
ATOM    462  C   GLY A  59      -0.144  12.925  34.679  1.00 84.30      A    C  
ANISOU  462  C   GLY A  59    17250   8200   6580   -980   1960   -390  A    C  
ATOM    463  O   GLY A  59       0.755  13.681  34.189  1.00 74.11      A    O  
ANISOU  463  O   GLY A  59    15520   7170   5480   -750   1510   -360  A    O  
ATOM    464  N   LEU A  60      -1.312  12.668  34.086  1.00 83.50      A    N  
ANISOU  464  N   LEU A  60    16820   8070   6840  -1160   2430   -500  A    N  
ATOM    465  CA  LEU A  60      -2.164  13.686  33.422  1.00 84.68      A    C  
ANISOU  465  CA  LEU A  60    16240   8370   7560  -1270   2680   -680  A    C  
ATOM    466  C   LEU A  60      -2.006  15.037  34.126  1.00 81.43      A    C  
ANISOU  466  C   LEU A  60    15810   8010   7120  -1320   2690   -800  A    C  
ATOM    467  O   LEU A  60      -2.889  15.354  34.913  1.00 85.93      A    O  
ANISOU  467  O   LEU A  60    16600   8380   7680  -1610   3200  -1000  A    O  
ATOM    468  CB  LEU A  60      -3.627  13.221  33.478  1.00 91.03      A    C  
ANISOU  468  CB  LEU A  60    17040   8950   8590  -1570   3330   -880  A    C  
ATOM    469  CG  LEU A  60      -4.217  12.698  32.167  1.00 96.89      A    C  
ANISOU  469  CG  LEU A  60    17210   9790   9820  -1530   3350   -890  A    C  
ATOM    470  CD1 LEU A  60      -4.321  13.826  31.138  1.00 99.24      A    C  
ANISOU  470  CD1 LEU A  60    16700  10340  10670  -1410   3120   -950  A    C  
ATOM    471  CD2 LEU A  60      -3.425  11.514  31.600  1.00 95.62      A    C  
ANISOU  471  CD2 LEU A  60    17210   9680   9440  -1320   2990   -640  A    C  
ATOM    472  N   GLU A  61      -0.929  15.783  33.844  1.00 78.24      A    N  
ANISOU  472  N   GLU A  61    15140   7840   6740  -1080   2180   -720  A    N  
ATOM    473  CA  GLU A  61      -0.764  17.230  34.187  1.00 75.85      A    C  
ANISOU  473  CA  GLU A  61    14610   7650   6560  -1100   2150   -840  A    C  
ATOM    474  C   GLU A  61      -1.511  18.097  33.183  1.00 73.83      A    C  
ANISOU  474  C   GLU A  61    13570   7540   6940  -1130   2290   -960  A    C  
ATOM    475  O   GLU A  61      -1.819  17.633  32.091  1.00 80.27      A    O  
ANISOU  475  O   GLU A  61    14010   8430   8060  -1070   2230   -910  A    O  
ATOM    476  CB  GLU A  61       0.685  17.732  34.209  1.00 75.10      A    C  
ANISOU  476  CB  GLU A  61    14480   7740   6310   -830   1560   -730  A    C  
ATOM    477  CG  GLU A  61       1.676  16.853  33.496  1.00 78.28      A    C  
ANISOU  477  CG  GLU A  61    14840   8240   6660   -560   1090   -550  A    C  
ATOM    478  CD  GLU A  61       3.090  17.396  33.385  1.00 83.77      A    C  
ANISOU  478  CD  GLU A  61    15370   9110   7350   -300    540   -510  A    C  
ATOM    479  OE1 GLU A  61       3.882  17.192  34.321  1.00 88.78      A    O  
ANISOU  479  OE1 GLU A  61    16500   9640   7590   -210    250   -480  A    O  
ATOM    480  OE2 GLU A  61       3.416  17.993  32.333  1.00 88.89      A    O1-
ANISOU  480  OE2 GLU A  61    15400   9980   8390   -190    390   -520  A    O1-
ATOM    481  N   ALA A  62      -1.774  19.336  33.564  1.00 75.59      A    N  
ANISOU  481  N   ALA A  62    13600   7790   7330  -1230   2430  -1120  A    N  
ATOM    482  CA  ALA A  62      -2.368  20.393  32.719  1.00 75.81      A    C  
ANISOU  482  CA  ALA A  62    12920   7930   7960  -1230   2470  -1240  A    C  
ATOM    483  C   ALA A  62      -1.516  21.648  32.896  1.00 75.39      A    C  
ANISOU  483  C   ALA A  62    12710   8040   7900  -1120   2180  -1240  A    C  
ATOM    484  O   ALA A  62      -0.860  21.795  33.960  1.00 77.64      A    O  
ANISOU  484  O   ALA A  62    13460   8290   7750  -1130   2130  -1240  A    O  
ATOM    485  CB  ALA A  62      -3.813  20.652  33.078  1.00 79.59      A    C  
ANISOU  485  CB  ALA A  62    13270   8190   8780  -1510   3030  -1510  A    C  
ATOM    486  N   HIS A  63      -1.467  22.467  31.850  1.00 72.07      A    N  
ANISOU  486  N   HIS A  63    11700   7780   7900  -1000   1970  -1230  A    N  
ATOM    487  CA  HIS A  63      -0.626  23.680  31.791  1.00 67.74      A    C  
ANISOU  487  CA  HIS A  63    10940   7400   7410   -890   1700  -1230  A    C  
ATOM    488  C   HIS A  63      -1.411  24.783  31.094  1.00 67.69      A    C  
ANISOU  488  C   HIS A  63    10370   7390   7960   -930   1780  -1340  A    C  
ATOM    489  O   HIS A  63      -2.031  24.527  30.043  1.00 68.54      A    O  
ANISOU  489  O   HIS A  63    10150   7490   8400   -910   1740  -1310  A    O  
ATOM    490  CB  HIS A  63       0.710  23.436  31.094  1.00 62.00      A    C  
ANISOU  490  CB  HIS A  63    10150   6870   6540   -640   1220  -1040  A    C  
ATOM    491  CG  HIS A  63       1.413  22.182  31.461  1.00 61.82      A    C  
ANISOU  491  CG  HIS A  63    10580   6820   6090   -550   1050   -920  A    C  
ATOM    492  CD2 HIS A  63       1.319  20.931  30.950  1.00 60.64      A    C  
ANISOU  492  CD2 HIS A  63    10530   6630   5880   -510   1020   -800  A    C  
ATOM    493  ND1 HIS A  63       2.399  22.145  32.416  1.00 63.66      A    N  
ANISOU  493  ND1 HIS A  63    11210   7040   5940   -470    840   -910  A    N  
ATOM    494  CE1 HIS A  63       2.879  20.915  32.504  1.00 65.23      A    C  
ANISOU  494  CE1 HIS A  63    11750   7180   5850   -370    660   -790  A    C  
ATOM    495  NE2 HIS A  63       2.232  20.145  31.594  1.00 61.52      A    N  
ANISOU  495  NE2 HIS A  63    11100   6700   5580   -400    790   -720  A    N  
ATOM    496  N   ARG A  64      -1.372  25.953  31.714  1.00 69.30      A    N  
ANISOU  496  N   ARG A  64    10510   7590   8240   -990   1870  -1480  A    N  
ATOM    497  CA  ARG A  64      -1.815  27.235  31.139  1.00 68.60      A    C  
ANISOU  497  CA  ARG A  64     9910   7510   8650   -990   1850  -1580  A    C  
ATOM    498  C   ARG A  64      -0.598  27.813  30.404  1.00 62.25      A    C  
ANISOU  498  C   ARG A  64     8950   6910   7790   -790   1420  -1420  A    C  
ATOM    499  O   ARG A  64       0.541  27.819  30.949  1.00 60.35      A    O  
ANISOU  499  O   ARG A  64     8960   6780   7190   -720   1250  -1370  A    O  
ATOM    500  CB  ARG A  64      -2.395  28.152  32.238  1.00 69.08      A    C  
ANISOU  500  CB  ARG A  64    10000   7430   8820  -1180   2210  -1830  A    C  
ATOM    501  N   VAL A  65      -0.860  28.329  29.218  1.00 58.21      A    N  
ANISOU  501  N   VAL A  65     8040   6420   7660   -730   1250  -1370  A    N  
ATOM    502  CA  VAL A  65       0.171  28.779  28.257  1.00 57.33      A    C  
ANISOU  502  CA  VAL A  65     7780   6460   7540   -580    900  -1230  A    C  
ATOM    503  C   VAL A  65      -0.447  29.964  27.565  1.00 56.27      A    C  
ANISOU  503  C   VAL A  65     7290   6240   7850   -590    850  -1280  A    C  
ATOM    504  O   VAL A  65      -1.696  29.975  27.447  1.00 58.15      A    O  
ANISOU  504  O   VAL A  65     7350   6310   8440   -670    990  -1380  A    O  
ATOM    505  CB  VAL A  65       0.505  27.655  27.248  1.00 55.02      A    C  
ANISOU  505  CB  VAL A  65     7550   6240   7120   -490    710  -1050  A    C  
ATOM    506  CG1 VAL A  65       0.810  26.368  27.974  1.00 57.58      A    C  
ANISOU  506  CG1 VAL A  65     8230   6580   7070   -480    770  -1010  A    C  
ATOM    507  CG2 VAL A  65      -0.625  27.403  26.268  1.00 53.50      A    C  
ANISOU  507  CG2 VAL A  65     7140   5930   7260   -520    700  -1030  A    C  
ATOM    508  N   ASN A  66       0.384  30.877  27.090  1.00 57.32      A    N  
ANISOU  508  N   ASN A  66     7310   6460   8000   -520    660  -1230  A    N  
ATOM    509  CA  ASN A  66      -0.087  31.920  26.158  1.00 60.35      A    C  
ANISOU  509  CA  ASN A  66     7420   6740   8770   -520    520  -1220  A    C  
ATOM    510  C   ASN A  66       0.928  32.072  25.031  1.00 56.51      A    C  
ANISOU  510  C   ASN A  66     6970   6350   8160   -440    260  -1060  A    C  
ATOM    511  O   ASN A  66       2.118  31.828  25.216  1.00 59.67      A    O  
ANISOU  511  O   ASN A  66     7500   6900   8270   -400    230  -1030  A    O  
ATOM    512  CB  ASN A  66      -0.458  33.216  26.878  1.00 70.77      A    C  
ANISOU  512  CB  ASN A  66     8570   7970  10350   -580    660  -1400  A    C  
ATOM    513  CG  ASN A  66       0.578  33.722  27.858  1.00 75.88      A    C  
ANISOU  513  CG  ASN A  66     9350   8750  10730   -590    740  -1470  A    C  
ATOM    514  ND2 ASN A  66       1.164  34.844  27.497  1.00 84.61      A    N  
ANISOU  514  ND2 ASN A  66    10330   9870  11940   -560    630  -1470  A    N  
ATOM    515  OD1 ASN A  66       0.812  33.139  28.925  1.00 75.35      A    O  
ANISOU  515  OD1 ASN A  66     9520   8740  10370   -630    900  -1540  A    O  
ATOM    516  N   LEU A  67       0.387  32.329  23.859  1.00 56.12      A    N  
ANISOU  516  N   LEU A  67     6820   6170   8340   -430     80   -970  A    N  
ATOM    517  CA  LEU A  67       1.104  32.671  22.626  1.00 52.77      A    C  
ANISOU  517  CA  LEU A  67     6460   5750   7840   -400   -130   -820  A    C  
ATOM    518  C   LEU A  67       1.112  34.186  22.615  1.00 54.29      A    C  
ANISOU  518  C   LEU A  67     6540   5840   8250   -420   -160   -880  A    C  
ATOM    519  O   LEU A  67       0.162  34.784  23.136  1.00 55.87      A    O  
ANISOU  519  O   LEU A  67     6560   5900   8770   -440   -110  -1000  A    O  
ATOM    520  CB  LEU A  67       0.345  32.095  21.423  1.00 52.03      A    C  
ANISOU  520  CB  LEU A  67     6410   5520   7840   -400   -330   -700  A    C  
ATOM    521  CG  LEU A  67       0.598  30.613  21.150  1.00 53.42      A    C  
ANISOU  521  CG  LEU A  67     6730   5810   7750   -390   -310   -620  A    C  
ATOM    522  CD1 LEU A  67       0.737  29.819  22.446  1.00 57.16      A    C  
ANISOU  522  CD1 LEU A  67     7240   6410   8070   -380    -80   -710  A    C  
ATOM    523  CD2 LEU A  67      -0.499  30.017  20.306  1.00 53.95      A    C  
ANISOU  523  CD2 LEU A  67     6780   5730   7990   -390   -480   -560  A    C  
ATOM    524  N   THR A  68       2.181  34.770  22.122  1.00 48.43      A    N  
ANISOU  524  N   THR A  68     5890   5140   7370   -440   -210   -830  A    N  
ATOM    525  CA  THR A  68       2.106  36.095  21.544  1.00 47.21      A    C  
ANISOU  525  CA  THR A  68     5710   4820   7410   -460   -310   -810  A    C  
ATOM    526  C   THR A  68       2.652  35.998  20.142  1.00 44.31      A    C  
ANISOU  526  C   THR A  68     5590   4380   6870   -510   -460   -650  A    C  
ATOM    527  O   THR A  68       3.824  35.806  20.009  1.00 44.96      A    O  
ANISOU  527  O   THR A  68     5770   4600   6720   -540   -340   -660  A    O  
ATOM    528  CB  THR A  68       2.845  37.127  22.393  1.00 50.72      A    C  
ANISOU  528  CB  THR A  68     6060   5340   7880   -490   -150   -950  A    C  
ATOM    529  CG2 THR A  68       2.908  38.481  21.693  1.00 48.88      A    C  
ANISOU  529  CG2 THR A  68     5850   4910   7810   -530   -240   -920  A    C  
ATOM    530  OG1 THR A  68       2.094  37.193  23.606  1.00 51.46      A    O  
ANISOU  530  OG1 THR A  68     5980   5440   8140   -480    -10  -1100  A    O  
ATOM    531  N   VAL A  69       1.815  36.260  19.165  1.00 46.75      A    N  
ANISOU  531  N   VAL A  69     5990   4460   7320   -510   -700   -540  A    N  
ATOM    532  CA  VAL A  69       2.136  36.151  17.725  1.00 51.56      A    C  
ANISOU  532  CA  VAL A  69     6930   4940   7720   -580   -870   -370  A    C  
ATOM    533  C   VAL A  69       2.664  37.477  17.168  1.00 55.90      A    C  
ANISOU  533  C   VAL A  69     7670   5310   8260   -660   -890   -330  A    C  
ATOM    534  O   VAL A  69       1.952  38.482  17.318  1.00 57.50      A    O  
ANISOU  534  O   VAL A  69     7770   5320   8750   -620  -1030   -350  A    O  
ATOM    535  CB  VAL A  69       0.844  35.741  17.027  1.00 53.40      A    C  
ANISOU  535  CB  VAL A  69     7210   4970   8120   -530  -1190   -270  A    C  
ATOM    536  CG1 VAL A  69       0.995  35.718  15.514  1.00 56.73      A    C  
ANISOU  536  CG1 VAL A  69     8050   5190   8310   -610  -1420    -90  A    C  
ATOM    537  CG2 VAL A  69       0.391  34.405  17.568  1.00 52.76      A    C  
ANISOU  537  CG2 VAL A  69     6960   5050   8040   -480  -1100   -320  A    C  
ATOM    538  N   SER A  70       3.819  37.452  16.489  1.00 57.48      A    N  
ANISOU  538  N   SER A  70     8140   5540   8170   -780   -740   -300  A    N  
ATOM    539  CA  SER A  70       4.371  38.592  15.719  1.00 61.83      A    C  
ANISOU  539  CA  SER A  70     8980   5870   8640   -910   -720   -260  A    C  
ATOM    540  C   SER A  70       4.767  38.130  14.318  1.00 63.81      A    C  
ANISOU  540  C   SER A  70     9710   5980   8560  -1060   -750   -120  A    C  
ATOM    541  O   SER A  70       5.947  37.777  14.095  1.00 61.93      A    O  
ANISOU  541  O   SER A  70     9570   5860   8110  -1190   -440   -200  A    O  
ATOM    542  CB  SER A  70       5.517  39.226  16.429  1.00 66.13      A    C  
ANISOU  542  CB  SER A  70     9370   6560   9190   -960   -400   -430  A    C  
ATOM    543  OG  SER A  70       5.340  39.106  17.838  1.00 75.21      A    O  
ANISOU  543  OG  SER A  70    10110   7940  10530   -840   -320   -580  A    O  
ATOM    544  N   GLY A  71       3.800  38.182  13.403  1.00 65.68      A    N  
ANISOU  544  N   GLY A  71    10240   5950   8770  -1060  -1110     60  A    N  
ATOM    545  CA  GLY A  71       3.984  37.867  11.980  1.00 67.55      A    C  
ANISOU  545  CA  GLY A  71    11040   5970   8660  -1220  -1200    210  A    C  
ATOM    546  C   GLY A  71       4.313  36.400  11.759  1.00 66.17      A    C  
ANISOU  546  C   GLY A  71    10860   6010   8280  -1250  -1070    200  A    C  
ATOM    547  O   GLY A  71       3.385  35.558  11.696  1.00 64.28      A    O  
ANISOU  547  O   GLY A  71    10530   5790   8110  -1140  -1330    260  A    O  
ATOM    548  N   ARG A  72       5.596  36.120  11.570  1.00 66.92      A    N  
ANISOU  548  N   ARG A  72    11050   6210   8160  -1410   -670     90  A    N  
ATOM    549  CA  ARG A  72       6.096  34.781  11.182  1.00 68.98      A    C  
ANISOU  549  CA  ARG A  72    11370   6620   8210  -1480   -510     60  A    C  
ATOM    550  C   ARG A  72       6.322  33.983  12.467  1.00 59.70      A    C  
ANISOU  550  C   ARG A  72     9650   5800   7240  -1300   -370    -90  A    C  
ATOM    551  O   ARG A  72       6.474  32.785  12.377  1.00 49.58      A    O  
ANISOU  551  O   ARG A  72     8320   4650   5860  -1290   -320   -110  A    O  
ATOM    552  CB  ARG A  72       7.407  34.859  10.382  1.00 80.10      A    C  
ANISOU  552  CB  ARG A  72    13120   7950   9370  -1750   -110    -40  A    C  
ATOM    553  CG  ARG A  72       7.474  35.964   9.332  1.00 94.66      A    C  
ANISOU  553  CG  ARG A  72    15560   9420  10990  -1970   -120     60  A    C  
ATOM    554  CD  ARG A  72       8.419  37.128   9.660  1.00102.57      A    C  
ANISOU  554  CD  ARG A  72    16510  10370  12090  -2080    220   -100  A    C  
ATOM    555  NE  ARG A  72       8.578  38.115   8.578  1.00111.47      A    N  
ANISOU  555  NE  ARG A  72    18310  11090  12950  -2340    280      0  A    N  
ATOM    556  CZ  ARG A  72       9.011  37.870   7.326  1.00114.65      A    C  
ANISOU  556  CZ  ARG A  72    19340  11250  12970  -2640    470     40  A    C  
ATOM    557  NH1 ARG A  72       9.322  36.647   6.916  1.00117.01      A    N1+
ANISOU  557  NH1 ARG A  72    19670  11670  13120  -2710    630    -20  A    N1+
ATOM    558  NH2 ARG A  72       9.114  38.872   6.472  1.00117.04      A    N  
ANISOU  558  NH2 ARG A  72    20290  11160  13020  -2870    520    130  A    N  
ATOM    559  N   THR A  73       6.400  34.657  13.615  1.00 56.93      A    N  
ANISOU  559  N   THR A  73     8930   5570   7120  -1190   -320   -200  A    N  
ATOM    560  CA  THR A  73       6.907  34.057  14.864  1.00 52.49      A    C  
ANISOU  560  CA  THR A  73     7950   5310   6680  -1050   -160   -370  A    C  
ATOM    561  C   THR A  73       5.857  34.224  15.937  1.00 51.54      A    C  
ANISOU  561  C   THR A  73     7540   5250   6790   -880   -340   -360  A    C  
ATOM    562  O   THR A  73       4.897  34.998  15.754  1.00 53.43      A    O  
ANISOU  562  O   THR A  73     7820   5310   7170   -860   -550   -270  A    O  
ATOM    563  CB  THR A  73       8.245  34.645  15.326  1.00 56.14      A    C  
ANISOU  563  CB  THR A  73     8270   5860   7200  -1120    130   -580  A    C  
ATOM    564  CG2 THR A  73       9.326  34.566  14.265  1.00 55.88      A    C  
ANISOU  564  CG2 THR A  73     8510   5720   7010  -1340    390   -660  A    C  
ATOM    565  OG1 THR A  73       8.043  35.995  15.774  1.00 59.46      A    O  
ANISOU  565  OG1 THR A  73     8620   6190   7780  -1110    110   -610  A    O  
ATOM    566  N   LEU A  74       6.028  33.439  16.985  1.00 48.11      A    N  
ANISOU  566  N   LEU A  74     6840   5050   6390   -760   -260   -460  A    N  
ATOM    567  CA  LEU A  74       5.313  33.620  18.245  1.00 44.29      A    C  
ANISOU  567  CA  LEU A  74     6090   4650   6090   -640   -300   -520  A    C  
ATOM    568  C   LEU A  74       6.242  33.171  19.363  1.00 45.24      A    C  
ANISOU  568  C   LEU A  74     6040   4990   6160   -570   -150   -680  A    C  
ATOM    569  O   LEU A  74       7.290  32.544  19.102  1.00 40.50      A    O  
ANISOU  569  O   LEU A  74     5480   4480   5430   -590    -60   -740  A    O  
ATOM    570  CB  LEU A  74       3.994  32.860  18.224  1.00 45.09      A    C  
ANISOU  570  CB  LEU A  74     6170   4700   6270   -570   -470   -420  A    C  
ATOM    571  CG  LEU A  74       4.083  31.339  18.099  1.00 44.92      A    C  
ANISOU  571  CG  LEU A  74     6200   4790   6070   -540   -440   -390  A    C  
ATOM    572  CD1 LEU A  74       4.446  30.695  19.435  1.00 46.35      A    C  
ANISOU  572  CD1 LEU A  74     6230   5170   6210   -450   -310   -500  A    C  
ATOM    573  CD2 LEU A  74       2.776  30.754  17.615  1.00 43.36      A    C  
ANISOU  573  CD2 LEU A  74     6040   4470   5970   -520   -630   -280  A    C  
ATOM    574  N   LYS A  75       5.927  33.710  20.536  1.00 47.40      A    N  
ANISOU  574  N   LYS A  75     6140   5310   6560   -500   -120   -770  A    N  
ATOM    575  CA  LYS A  75       6.552  33.427  21.819  1.00 46.69      A    C  
ANISOU  575  CA  LYS A  75     5930   5400   6410   -430    -50   -920  A    C  
ATOM    576  C   LYS A  75       5.539  32.575  22.562  1.00 45.25      A    C  
ANISOU  576  C   LYS A  75     5750   5240   6200   -370    -70   -880  A    C  
ATOM    577  O   LYS A  75       4.372  32.924  22.561  1.00 44.08      A    O  
ANISOU  577  O   LYS A  75     5560   4970   6220   -390    -80   -840  A    O  
ATOM    578  CB  LYS A  75       6.947  34.742  22.495  1.00 52.70      A    C  
ANISOU  578  CB  LYS A  75     6570   6160   7300   -450     20  -1060  A    C  
ATOM    579  CG  LYS A  75       8.283  35.291  22.005  1.00 58.33      A    C  
ANISOU  579  CG  LYS A  75     7260   6880   8020   -510    100  -1170  A    C  
ATOM    580  CD  LYS A  75       8.636  36.620  22.567  1.00 64.71      A    C  
ANISOU  580  CD  LYS A  75     7940   7670   8970   -540    180  -1320  A    C  
ATOM    581  CE  LYS A  75       9.665  37.338  21.720  1.00 71.55      A    C  
ANISOU  581  CE  LYS A  75     8830   8460   9890   -660    310  -1400  A    C  
ATOM    582  NZ  LYS A  75       9.814  38.750  22.150  1.00 75.34      A    N1+
ANISOU  582  NZ  LYS A  75     9200   8890  10540   -710    390  -1520  A    N1+
ATOM    583  N   PHE A  76       6.011  31.459  23.105  1.00 43.04      A    N  
ANISOU  583  N   PHE A  76     5540   5080   5740   -300    -70   -910  A    N  
ATOM    584  CA  PHE A  76       5.215  30.473  23.845  1.00 42.82      A    C  
ANISOU  584  CA  PHE A  76     5590   5060   5620   -260    -40   -880  A    C  
ATOM    585  C   PHE A  76       5.718  30.488  25.287  1.00 42.99      A    C  
ANISOU  585  C   PHE A  76     5670   5160   5500   -210    -10  -1020  A    C  
ATOM    586  O   PHE A  76       6.915  30.373  25.512  1.00 44.88      A    O  
ANISOU  586  O   PHE A  76     5920   5490   5650   -150   -100  -1090  A    O  
ATOM    587  CB  PHE A  76       5.364  29.143  23.113  1.00 40.51      A    C  
ANISOU  587  CB  PHE A  76     5410   4790   5190   -230   -100   -780  A    C  
ATOM    588  CG  PHE A  76       4.814  27.960  23.841  1.00 40.41      A    C  
ANISOU  588  CG  PHE A  76     5530   4780   5040   -190    -60   -750  A    C  
ATOM    589  CD1 PHE A  76       5.584  27.278  24.751  1.00 41.97      A    C  
ANISOU  589  CD1 PHE A  76     5860   5050   5030   -110   -100   -810  A    C  
ATOM    590  CD2 PHE A  76       3.510  27.572  23.659  1.00 40.81      A    C  
ANISOU  590  CD2 PHE A  76     5580   4740   5190   -240     -0   -690  A    C  
ATOM    591  CE1 PHE A  76       5.064  26.189  25.418  1.00 43.03      A    C  
ANISOU  591  CE1 PHE A  76     6200   5150   5000   -100    -50   -770  A    C  
ATOM    592  CE2 PHE A  76       2.993  26.484  24.335  1.00 42.08      A    C  
ANISOU  592  CE2 PHE A  76     5890   4880   5220   -240     90   -690  A    C  
ATOM    593  CZ  PHE A  76       3.764  25.809  25.223  1.00 42.94      A    C  
ANISOU  593  CZ  PHE A  76     6200   5050   5070   -170     80   -710  A    C  
ATOM    594  N   TYR A  77       4.803  30.619  26.226  1.00 44.93      A    N  
ANISOU  594  N   TYR A  77     5960   5350   5760   -250    110  -1060  A    N  
ATOM    595  CA  TYR A  77       5.087  30.665  27.677  1.00 52.85      A    C  
ANISOU  595  CA  TYR A  77     7120   6390   6580   -240    160  -1190  A    C  
ATOM    596  C   TYR A  77       4.154  29.702  28.384  1.00 49.34      A    C  
ANISOU  596  C   TYR A  77     6900   5860   5990   -290    300  -1170  A    C  
ATOM    597  O   TYR A  77       2.960  29.725  28.163  1.00 48.08      A    O  
ANISOU  597  O   TYR A  77     6650   5590   6020   -380    460  -1160  A    O  
ATOM    598  CB  TYR A  77       4.891  32.070  28.260  1.00 58.97      A    C  
ANISOU  598  CB  TYR A  77     7760   7130   7520   -310    270  -1320  A    C  
ATOM    599  CG  TYR A  77       5.169  32.173  29.744  1.00 70.79      A    C  
ANISOU  599  CG  TYR A  77     9470   8640   8790   -330    320  -1460  A    C  
ATOM    600  CD1 TYR A  77       6.471  32.207  30.234  1.00 75.71      A    C  
ANISOU  600  CD1 TYR A  77    10170   9360   9240   -240    120  -1540  A    C  
ATOM    601  CD2 TYR A  77       4.133  32.249  30.672  1.00 79.54      A    C  
ANISOU  601  CD2 TYR A  77    10710   9640   9880   -450    560  -1540  A    C  
ATOM    602  CE1 TYR A  77       6.737  32.325  31.590  1.00 80.11      A    C  
ANISOU  602  CE1 TYR A  77    10980   9910   9550   -250    110  -1670  A    C  
ATOM    603  CE2 TYR A  77       4.381  32.364  32.032  1.00 82.70      A    C  
ANISOU  603  CE2 TYR A  77    11390  10030  10010   -500    630  -1670  A    C  
ATOM    604  CZ  TYR A  77       5.688  32.397  32.493  1.00 84.52      A    C  
ANISOU  604  CZ  TYR A  77    11740  10360  10020   -390    370  -1720  A    C  
ATOM    605  OH  TYR A  77       5.939  32.521  33.832  1.00 88.73      A    O  
ANISOU  605  OH  TYR A  77    12600  10850  10260   -440    370  -1850  A    O  
ATOM    606  N   MET A  78       4.733  28.830  29.162  1.00 56.31      A    N  
ANISOU  606  N   MET A  78     8070   6770   6550   -230    230  -1170  A    N  
ATOM    607  CA  MET A  78       3.981  27.896  30.020  1.00 67.65      A    C  
ANISOU  607  CA  MET A  78     9830   8100   7770   -300    390  -1170  A    C  
ATOM    608  C   MET A  78       4.140  28.394  31.464  1.00 69.88      A    C  
ANISOU  608  C   MET A  78    10380   8340   7820   -360    470  -1310  A    C  
ATOM    609  O   MET A  78       5.244  28.895  31.805  1.00 62.41      A    O  
ANISOU  609  O   MET A  78     9440   7480   6790   -270    240  -1370  A    O  
ATOM    610  CB  MET A  78       4.514  26.467  29.866  1.00 66.99      A    C  
ANISOU  610  CB  MET A  78     9980   8030   7430   -190    220  -1050  A    C  
ATOM    611  CG  MET A  78       3.580  25.567  29.118  1.00 70.75      A    C  
ANISOU  611  CG  MET A  78    10430   8450   8000   -240    360   -940  A    C  
ATOM    612  SD  MET A  78       4.087  23.828  29.091  1.00 71.45      A    S  
ANISOU  612  SD  MET A  78    10840   8520   7790   -130    210   -820  A    S  
ATOM    613  CE  MET A  78       5.832  24.017  28.713  1.00 71.26      A    C  
ANISOU  613  CE  MET A  78    10680   8630   7770     60   -180   -840  A    C  
ATOM    614  N   ASN A  79       3.083  28.281  32.266  1.00 76.49      A    N  
ANISOU  614  N   ASN A  79    11430   9030   8590   -530    790  -1380  A    N  
ATOM    615  CA  ASN A  79       3.075  28.816  33.654  1.00 83.92      A    C  
ANISOU  615  CA  ASN A  79    12690   9900   9300   -640    940  -1530  A    C  
ATOM    616  C   ASN A  79       3.951  27.914  34.534  1.00 81.61      A    C  
ANISOU  616  C   ASN A  79    12940   9580   8500   -570    700  -1490  A    C  
ATOM    617  O   ASN A  79       4.975  28.382  35.064  1.00 80.89      A    O  
ANISOU  617  O   ASN A  79    12940   9550   8250   -470    420  -1550  A    O  
ATOM    618  CB  ASN A  79       1.641  28.973  34.162  1.00 92.18      A    C  
ANISOU  618  CB  ASN A  79    13780  10760  10480   -880   1420  -1670  A    C  
ATOM    619  CG  ASN A  79       1.497  30.172  35.073  1.00103.82      A    C  
ANISOU  619  CG  ASN A  79    15270  12180  11990  -1020   1620  -1870  A    C  
ATOM    620  ND2 ASN A  79       1.995  30.041  36.292  1.00112.43      A    N  
ANISOU  620  ND2 ASN A  79    16880  13220  12620  -1080   1610  -1930  A    N  
ATOM    621  OD1 ASN A  79       0.970  31.213  34.675  1.00105.72      A    O  
ANISOU  621  OD1 ASN A  79    15090  12410  12670  -1070   1750  -1970  A    O  
ATOM    622  N  AASP A  80       3.634  26.633  34.595  0.53 81.83      A    N  
ANISOU  622  N  AASP A  80    13290   9510   8300   -580    740  -1380  A    N  
ATOM    623  N  BASP A  80       3.509  26.655  34.644  0.47 82.21      A    N  
ANISOU  623  N  BASP A  80    13350   9540   8350   -600    790  -1390  A    N  
ATOM    624  CA AASP A  80       4.150  25.699  35.629  0.53 84.04      A    C  
ANISOU  624  CA AASP A  80    14230   9660   8040   -550    580  -1340  A    C  
ATOM    625  CA BASP A  80       4.055  25.522  35.444  0.47 84.71      A    C  
ANISOU  625  CA BASP A  80    14280   9750   8160   -540    600  -1320  A    C  
ATOM    626  C  AASP A  80       5.619  25.335  35.349  0.53 83.79      A    C  
ANISOU  626  C  AASP A  80    14170   9740   7930   -270     10  -1270  A    C  
ATOM    627  C  BASP A  80       5.583  25.434  35.327  0.47 83.89      A    C  
ANISOU  627  C  BASP A  80    14140   9760   7960   -280     30  -1280  A    C  
ATOM    628  O  AASP A  80       6.307  24.974  36.319  0.53 84.67      A    O  
ANISOU  628  O  AASP A  80    14770   9760   7640   -210   -260  -1280  A    O  
ATOM    629  O  BASP A  80       6.254  25.388  36.369  0.47 84.70      A    O  
ANISOU  629  O  BASP A  80    14690   9790   7700   -240   -210  -1330  A    O  
ATOM    630  CB AASP A  80       3.222  24.487  35.690  0.53 84.63      A    C  
ANISOU  630  CB AASP A  80    14630   9570   7960   -670    870  -1260  A    C  
ATOM    631  CB BASP A  80       3.410  24.215  34.958  0.47 82.82      A    C  
ANISOU  631  CB BASP A  80    14160   9420   7890   -570    740  -1190  A    C  
ATOM    632  CG AASP A  80       2.017  24.701  34.793  0.53 80.96      A    C  
ANISOU  632  CG AASP A  80    13680   9110   7970   -790   1240  -1300  A    C  
ATOM    633  CG BASP A  80       3.881  22.954  35.665  0.47 84.59      A    C  
ANISOU  633  CG BASP A  80    15040   9490   7610   -500    540  -1080  A    C  
ATOM    634  OD1AASP A  80       1.236  25.650  35.051  0.53 77.66      A    O  
ANISOU  634  OD1AASP A  80    13070   8640   7790   -960   1570  -1460  A    O  
ATOM    635  OD1BASP A  80       5.053  22.909  36.081  0.47 85.27      A    O  
ANISOU  635  OD1BASP A  80    15320   9600   7470   -330     90  -1070  A    O  
ATOM    636  OD2AASP A  80       1.943  24.004  33.788  0.53 76.17      A    O1-
ANISOU  636  OD2AASP A  80    12840   8560   7540   -700   1150  -1170  A    O1-
ATOM    637  OD2BASP A  80       3.070  22.017  35.783  0.47 84.97      A    O1-
ANISOU  637  OD2BASP A  80    15380   9380   7520   -630    830  -1030  A    O1-
ATOM    638  N   THR A  81       6.094  25.398  34.094  1.00 81.58      A    N  
ANISOU  638  N   THR A  81    13360   9630   8010   -130   -160  -1210  A    N  
ATOM    639  CA  THR A  81       7.496  24.997  33.734  1.00 83.80      A    C  
ANISOU  639  CA  THR A  81    13540   9990   8310    120   -640  -1200  A    C  
ATOM    640  C   THR A  81       7.921  25.626  32.390  1.00 78.58      A    C  
ANISOU  640  C   THR A  81    12250   9510   8100    190   -680  -1220  A    C  
ATOM    641  O   THR A  81       7.038  25.941  31.592  1.00 76.78      A    O  
ANISOU  641  O   THR A  81    11750   9310   8110     70   -390  -1160  A    O  
ATOM    642  CB  THR A  81       7.622  23.463  33.664  1.00 86.21      A    C  
ANISOU  642  CB  THR A  81    14170  10190   8400    220   -800  -1060  A    C  
ATOM    643  CG2 THR A  81       6.360  22.764  33.211  1.00 84.69      A    C  
ANISOU  643  CG2 THR A  81    14020   9930   8220     70   -410   -940  A    C  
ATOM    644  OG1 THR A  81       8.626  23.112  32.715  1.00 86.14      A    O  
ANISOU  644  OG1 THR A  81    13810  10280   8640    420  -1100  -1050  A    O  
ATOM    645  N   HIS A  82       9.226  25.763  32.123  1.00 74.27      A    N  
ANISOU  645  N   HIS A  82    11490   9040   7690    360  -1020  -1300  A    N  
ATOM    646  CA  HIS A  82       9.752  26.733  31.126  1.00 70.88      A    C  
ANISOU  646  CA  HIS A  82    10540   8740   7660    360  -1000  -1390  A    C  
ATOM    647  C   HIS A  82      10.719  26.095  30.135  1.00 67.01      A    C  
ANISOU  647  C   HIS A  82     9800   8290   7370    500  -1200  -1410  A    C  
ATOM    648  O   HIS A  82      11.316  26.861  29.387  1.00 62.09      A    O  
ANISOU  648  O   HIS A  82     8800   7740   7050    490  -1170  -1510  A    O  
ATOM    649  CB  HIS A  82      10.382  27.931  31.845  1.00 70.84      A    C  
ANISOU  649  CB  HIS A  82    10450   8770   7700    370  -1110  -1580  A    C  
ATOM    650  CG  HIS A  82       9.426  28.474  32.841  1.00 77.71      A    C  
ANISOU  650  CG  HIS A  82    11590   9580   8360    220   -880  -1590  A    C  
ATOM    651  CD2 HIS A  82       9.395  28.379  34.191  1.00 81.36      A    C  
ANISOU  651  CD2 HIS A  82    12510   9940   8460    190   -970  -1650  A    C  
ATOM    652  ND1 HIS A  82       8.248  29.098  32.456  1.00 77.30      A    N  
ANISOU  652  ND1 HIS A  82    11380   9530   8460     40   -490  -1540  A    N  
ATOM    653  CE1 HIS A  82       7.565  29.428  33.539  1.00 80.16      A    C  
ANISOU  653  CE1 HIS A  82    12040   9800   8620    -90   -310  -1600  A    C  
ATOM    654  NE2 HIS A  82       8.249  29.001  34.616  1.00 83.67      A    N  
ANISOU  654  NE2 HIS A  82    12900  10190   8710    -10   -570  -1650  A    N  
ATOM    655  N   GLU A  83      10.819  24.771  30.060  1.00 68.19      A    N  
ANISOU  655  N   GLU A  83    10140   8370   7390    590  -1330  -1310  A    N  
ATOM    656  CA  GLU A  83      11.831  24.146  29.173  1.00 69.77      A    C  
ANISOU  656  CA  GLU A  83    10090   8590   7830    720  -1510  -1380  A    C  
ATOM    657  C   GLU A  83      11.362  24.176  27.704  1.00 64.08      A    C  
ANISOU  657  C   GLU A  83     9090   7930   7320    600  -1220  -1280  A    C  
ATOM    658  O   GLU A  83      12.245  23.990  26.863  1.00 64.68      A    O  
ANISOU  658  O   GLU A  83     8910   8020   7640    640  -1270  -1380  A    O  
ATOM    659  CB  GLU A  83      12.290  22.781  29.717  1.00 78.19      A    C  
ANISOU  659  CB  GLU A  83    11460   9530   8720    890  -1840  -1350  A    C  
ATOM    660  CG  GLU A  83      11.471  21.552  29.310  1.00 81.41      A    C  
ANISOU  660  CG  GLU A  83    12090   9870   8970    860  -1690  -1140  A    C  
ATOM    661  CD  GLU A  83      10.487  21.022  30.353  1.00 87.93      A    C  
ANISOU  661  CD  GLU A  83    13460  10580   9370    800  -1610   -990  A    C  
ATOM    662  OE1 GLU A  83      10.055  21.846  31.217  1.00 87.03      A    O  
ANISOU  662  OE1 GLU A  83    13520  10460   9090    700  -1520  -1020  A    O  
ATOM    663  OE2 GLU A  83      10.139  19.782  30.302  1.00 85.44      A    O1-
ANISOU  663  OE2 GLU A  83    13410  10160   8900    820  -1610   -860  A    O1-
ATOM    664  N   TYR A  84      10.092  24.476  27.368  1.00 59.52      A    N  
ANISOU  664  N   TYR A  84     8550   7370   6690    440   -920  -1130  A    N  
ATOM    665  CA  TYR A  84       9.670  24.620  25.943  1.00 56.94      A    C  
ANISOU  665  CA  TYR A  84     8010   7080   6550    330   -720  -1050  A    C  
ATOM    666  C   TYR A  84       9.344  26.076  25.621  1.00 55.64      A    C  
ANISOU  666  C   TYR A  84     7650   6950   6550    210   -560  -1080  A    C  
ATOM    667  O   TYR A  84       8.882  26.329  24.490  1.00 49.01      A    O  
ANISOU  667  O   TYR A  84     6700   6090   5830    100   -420  -1000  A    O  
ATOM    668  CB  TYR A  84       8.484  23.726  25.601  1.00 56.04      A    C  
ANISOU  668  CB  TYR A  84     8060   6910   6320    260   -570   -860  A    C  
ATOM    669  CG  TYR A  84       8.799  22.261  25.743  1.00 58.68      A    C  
ANISOU  669  CG  TYR A  84     8580   7200   6520    370   -700   -810  A    C  
ATOM    670  CD1 TYR A  84       9.393  21.553  24.714  1.00 57.40      A    C  
ANISOU  670  CD1 TYR A  84     8290   7040   6480    410   -740   -820  A    C  
ATOM    671  CD2 TYR A  84       8.549  21.589  26.927  1.00 63.12      A    C  
ANISOU  671  CD2 TYR A  84     9490   7680   6810    430   -780   -780  A    C  
ATOM    672  CE1 TYR A  84       9.710  20.213  24.848  1.00 59.32      A    C  
ANISOU  672  CE1 TYR A  84     8690   7220   6630    520   -870   -780  A    C  
ATOM    673  CE2 TYR A  84       8.861  20.244  27.082  1.00 63.08      A    C  
ANISOU  673  CE2 TYR A  84     9710   7590   6670    540   -930   -730  A    C  
ATOM    674  CZ  TYR A  84       9.450  19.555  26.038  1.00 61.78      A    C  
ANISOU  674  CZ  TYR A  84     9350   7440   6680    600   -990   -730  A    C  
ATOM    675  OH  TYR A  84       9.752  18.228  26.163  1.00 66.41      A    O  
ANISOU  675  OH  TYR A  84    10130   7930   7170    710  -1140   -690  A    O  
ATOM    676  N   ASP A  85       9.582  26.973  26.574  1.00 53.19      A    N  
ANISOU  676  N   ASP A  85     7330   6650   6230    220   -600  -1200  A    N  
ATOM    677  CA  ASP A  85       9.296  28.427  26.446  1.00 54.74      A    C  
ANISOU  677  CA  ASP A  85     7360   6860   6580    110   -460  -1250  A    C  
ATOM    678  C   ASP A  85      10.386  29.021  25.570  1.00 54.00      A    C  
ANISOU  678  C   ASP A  85     7010   6800   6710    100   -470  -1370  A    C  
ATOM    679  O   ASP A  85      11.525  29.090  26.039  1.00 62.99      A    O  
ANISOU  679  O   ASP A  85     8060   7960   7910    190   -620  -1560  A    O  
ATOM    680  CB  ASP A  85       9.359  29.206  27.769  1.00 56.12      A    C  
ANISOU  680  CB  ASP A  85     7600   7040   6680    120   -490  -1370  A    C  
ATOM    681  CG  ASP A  85       8.293  28.895  28.815  1.00 58.87      A    C  
ANISOU  681  CG  ASP A  85     8230   7330   6800     70   -400  -1310  A    C  
ATOM    682  OD1 ASP A  85       7.389  28.066  28.543  1.00 60.56      A    O  
ANISOU  682  OD1 ASP A  85     8570   7490   6950     40   -290  -1180  A    O  
ATOM    683  OD2 ASP A  85       8.367  29.515  29.913  1.00 67.04      A    O1-
ANISOU  683  OD2 ASP A  85     9380   8350   7740     60   -400  -1430  A    O1-
ATOM    684  N   SER A  86      10.035  29.495  24.387  1.00 47.49      A    N  
ANISOU  684  N   SER A  86     6100   5930   6010    -20   -320  -1290  A    N  
ATOM    685  CA  SER A  86      10.996  30.082  23.441  1.00 46.02      A    C  
ANISOU  685  CA  SER A  86     5750   5730   6010    -90   -240  -1410  A    C  
ATOM    686  C   SER A  86      10.206  30.826  22.372  1.00 42.81      A    C  
ANISOU  686  C   SER A  86     5380   5240   5650   -240    -90  -1260  A    C  
ATOM    687  O   SER A  86       8.964  30.779  22.419  1.00 38.37      A    O  
ANISOU  687  O   SER A  86     4920   4630   5030   -260   -100  -1100  A    O  
ATOM    688  CB  SER A  86      11.841  28.995  22.860  1.00 50.28      A    C  
ANISOU  688  CB  SER A  86     6270   6270   6570    -50   -280  -1470  A    C  
ATOM    689  OG  SER A  86      12.794  29.470  21.886  1.00 55.92      A    O  
ANISOU  689  OG  SER A  86     6840   6930   7470   -160   -120  -1620  A    O  
ATOM    690  N   GLU A  87      10.914  31.481  21.452  1.00 40.81      A    N  
ANISOU  690  N   GLU A  87     5080   4920   5510   -360     40  -1340  A    N  
ATOM    691  CA  GLU A  87      10.333  31.860  20.155  1.00 42.57      A    C  
ANISOU  691  CA  GLU A  87     5460   5010   5710   -510    130  -1190  A    C  
ATOM    692  C   GLU A  87      10.204  30.629  19.252  1.00 40.55      A    C  
ANISOU  692  C   GLU A  87     5350   4730   5330   -540    130  -1080  A    C  
ATOM    693  O   GLU A  87      11.163  29.853  19.179  1.00 41.64      A    O  
ANISOU  693  O   GLU A  87     5420   4910   5490   -510    170  -1210  A    O  
ATOM    694  CB  GLU A  87      11.239  32.854  19.468  1.00 46.58      A    C  
ANISOU  694  CB  GLU A  87     5950   5420   6330   -660    320  -1330  A    C  
ATOM    695  CG  GLU A  87      10.618  33.589  18.282  1.00 51.16      A    C  
ANISOU  695  CG  GLU A  87     6780   5810   6850   -830    380  -1160  A    C  
ATOM    696  CD  GLU A  87      11.252  34.969  18.115  1.00 56.02      A    C  
ANISOU  696  CD  GLU A  87     7380   6320   7580   -950    550  -1290  A    C  
ATOM    697  OE1 GLU A  87      10.783  35.931  18.796  1.00 60.25      A    O  
ANISOU  697  OE1 GLU A  87     7830   6850   8210   -910    490  -1280  A    O  
ATOM    698  OE2 GLU A  87      12.278  35.050  17.419  1.00 58.07      A    O1-
ANISOU  698  OE2 GLU A  87     7690   6510   7870  -1100    780  -1440  A    O1-
ATOM    699  N   TYR A  88       9.102  30.552  18.510  1.00 37.69      A    N  
ANISOU  699  N   TYR A  88     5170   4270   4890   -590     70   -870  A    N  
ATOM    700  CA  TYR A  88       8.861  29.559  17.444  1.00 38.54      A    C  
ANISOU  700  CA  TYR A  88     5460   4320   4860   -660     70   -750  A    C  
ATOM    701  C   TYR A  88       8.424  30.272  16.165  1.00 42.18      A    C  
ANISOU  701  C   TYR A  88     6180   4580   5260   -830     80   -620  A    C  
ATOM    702  O   TYR A  88       7.519  31.119  16.166  1.00 42.75      A    O  
ANISOU  702  O   TYR A  88     6300   4550   5390   -830    -50   -520  A    O  
ATOM    703  CB  TYR A  88       7.819  28.506  17.867  1.00 34.76      A    C  
ANISOU  703  CB  TYR A  88     4990   3900   4320   -550    -70   -620  A    C  
ATOM    704  CG  TYR A  88       8.229  27.680  19.068  1.00 34.46      A    C  
ANISOU  704  CG  TYR A  88     4820   4000   4270   -390    -90   -720  A    C  
ATOM    705  CD1 TYR A  88       8.048  28.146  20.361  1.00 33.89      A    C  
ANISOU  705  CD1 TYR A  88     4640   3990   4250   -300   -130   -780  A    C  
ATOM    706  CD2 TYR A  88       8.774  26.417  18.905  1.00 34.49      A    C  
ANISOU  706  CD2 TYR A  88     4850   4050   4210   -350    -90   -750  A    C  
ATOM    707  CE1 TYR A  88       8.397  27.368  21.443  1.00 34.35      A    C  
ANISOU  707  CE1 TYR A  88     4680   4140   4230   -170   -200   -850  A    C  
ATOM    708  CE2 TYR A  88       9.166  25.646  19.974  1.00 32.56      A    C  
ANISOU  708  CE2 TYR A  88     4540   3890   3940   -200   -170   -820  A    C  
ATOM    709  CZ  TYR A  88       8.978  26.127  21.235  1.00 32.86      A    C  
ANISOU  709  CZ  TYR A  88     4540   3970   3970   -110   -240   -860  A    C  
ATOM    710  OH  TYR A  88       9.382  25.364  22.250  1.00 33.15      A    O  
ANISOU  710  OH  TYR A  88     4610   4060   3930     30   -350   -920  A    O  
ATOM    711  N   GLU A  89       8.976  29.796  15.067  1.00 44.42      A    N  
ANISOU  711  N   GLU A  89     6670   4790   5420   -970    200   -630  A    N  
ATOM    712  CA  GLU A  89       8.684  30.272  13.706  1.00 49.46      A    C  
ANISOU  712  CA  GLU A  89     7690   5200   5900  -1170    210   -510  A    C  
ATOM    713  C   GLU A  89       7.711  29.298  13.055  1.00 49.26      A    C  
ANISOU  713  C   GLU A  89     7850   5130   5740  -1160     20   -330  A    C  
ATOM    714  O   GLU A  89       7.946  28.091  13.158  1.00 43.48      A    O  
ANISOU  714  O   GLU A  89     7030   4510   4980  -1110     70   -370  A    O  
ATOM    715  CB  GLU A  89      10.023  30.264  12.985  1.00 55.85      A    C  
ANISOU  715  CB  GLU A  89     8620   5940   6660  -1370    540   -690  A    C  
ATOM    716  CG  GLU A  89       9.950  30.641  11.534  1.00 66.10      A    C  
ANISOU  716  CG  GLU A  89    10420   6970   7720  -1630    630   -590  A    C  
ATOM    717  CD  GLU A  89      11.340  30.798  10.940  1.00 77.51      A    C  
ANISOU  717  CD  GLU A  89    11960   8330   9160  -1870   1060   -830  A    C  
ATOM    718  OE1 GLU A  89      12.292  30.031  11.396  1.00 75.10      A    O  
ANISOU  718  OE1 GLU A  89    11320   8170   9050  -1820   1250  -1070  A    O  
ATOM    719  OE2 GLU A  89      11.478  31.702  10.044  1.00 87.90      A    O1-
ANISOU  719  OE2 GLU A  89    13690   9390  10320  -2110   1210   -800  A    O1-
ATOM    720  N   ILE A  90       6.675  29.797  12.401  1.00 48.88      A    N  
ANISOU  720  N   ILE A  90     8050   4890   5630  -1200   -220   -150  A    N  
ATOM    721  CA  ILE A  90       5.782  28.938  11.601  1.00 49.36      A    C  
ANISOU  721  CA  ILE A  90     8330   4860   5560  -1220   -420     -0  A    C  
ATOM    722  C   ILE A  90       6.525  28.487  10.342  1.00 51.59      A    C  
ANISOU  722  C   ILE A  90     9000   5030   5570  -1440   -240    -10  A    C  
ATOM    723  O   ILE A  90       7.148  29.300   9.661  1.00 57.64      A    O  
ANISOU  723  O   ILE A  90    10070   5630   6200  -1640    -80    -40  A    O  
ATOM    724  CB  ILE A  90       4.462  29.635  11.273  1.00 52.92      A    C  
ANISOU  724  CB  ILE A  90     8910   5110   6080  -1170   -800    150  A    C  
ATOM    725  CG1 ILE A  90       3.560  28.688  10.474  1.00 55.35      A    C  
ANISOU  725  CG1 ILE A  90     9410   5320   6290  -1180  -1050    270  A    C  
ATOM    726  CG2 ILE A  90       4.701  30.930  10.514  1.00 58.64      A    C  
ANISOU  726  CG2 ILE A  90    10000   5580   6700  -1320   -840    210  A    C  
ATOM    727  CD1 ILE A  90       2.670  27.843  11.331  1.00 58.46      A    C  
ANISOU  727  CD1 ILE A  90     9430   5860   6920   -990  -1160    250  A    C  
ATOM    728  N   LEU A  91       6.474  27.205  10.043  1.00 48.76      A    N  
ANISOU  728  N   LEU A  91     8660   4750   5120  -1450   -210    -10  A    N  
ATOM    729  CA  LEU A  91       7.139  26.635   8.863  1.00 49.35      A    C  
ANISOU  729  CA  LEU A  91     9100   4710   4940  -1680     -0    -40  A    C  
ATOM    730  C   LEU A  91       6.088  26.230   7.849  1.00 49.97      A    C  
ANISOU  730  C   LEU A  91     9560   4610   4810  -1740   -300    140  A    C  
ATOM    731  O   LEU A  91       6.451  26.175   6.686  1.00 55.57      A    O  
ANISOU  731  O   LEU A  91    10740   5140   5230  -1990   -180    160  A    O  
ATOM    732  CB  LEU A  91       7.972  25.420   9.252  1.00 47.46      A    C  
ANISOU  732  CB  LEU A  91     8580   4660   4780  -1640    260   -210  A    C  
ATOM    733  CG  LEU A  91       9.224  25.686  10.057  1.00 46.00      A    C  
ANISOU  733  CG  LEU A  91     8060   4610   4810  -1600    540   -450  A    C  
ATOM    734  CD1 LEU A  91      10.130  24.489   9.944  1.00 47.29      A    C  
ANISOU  734  CD1 LEU A  91     8100   4840   5030  -1630    780   -630  A    C  
ATOM    735  CD2 LEU A  91       9.941  26.954   9.612  1.00 49.33      A    C  
ANISOU  735  CD2 LEU A  91     8680   4860   5200  -1800    760   -540  A    C  
ATOM    736  N   ALA A  92       4.879  25.897   8.289  1.00 48.23      A    N  
ANISOU  736  N   ALA A  92     9140   4440   4740  -1550   -640    250  A    N  
ATOM    737  CA  ALA A  92       3.844  25.336   7.403  1.00 50.51      A    C  
ANISOU  737  CA  ALA A  92     9710   4580   4900  -1580   -970    380  A    C  
ATOM    738  C   ALA A  92       2.491  25.500   8.066  1.00 51.38      A    C  
ANISOU  738  C   ALA A  92     9520   4690   5310  -1360  -1350    440  A    C  
ATOM    739  O   ALA A  92       2.398  25.398   9.284  1.00 53.12      A    O  
ANISOU  739  O   ALA A  92     9290   5110   5790  -1190  -1250    360  A    O  
ATOM    740  CB  ALA A  92       4.131  23.892   7.081  1.00 51.39      A    C  
ANISOU  740  CB  ALA A  92     9830   4800   4900  -1630   -790    330  A    C  
ATOM    741  N   VAL A  93       1.501  25.765   7.237  1.00 57.89      A    N  
ANISOU  741  N   VAL A  93    10630   5270   6100  -1380  -1770    560  A    N  
ATOM    742  CA  VAL A  93       0.113  26.148   7.597  1.00 61.41      A    C  
ANISOU  742  CA  VAL A  93    10840   5600   6890  -1190  -2200    580  A    C  
ATOM    743  C   VAL A  93      -0.757  25.324   6.657  1.00 64.67      A    C  
ANISOU  743  C   VAL A  93    11480   5860   7230  -1220  -2550    640  A    C  
ATOM    744  O   VAL A  93      -0.417  25.222   5.440  1.00 65.83      A    O  
ANISOU  744  O   VAL A  93    12190   5840   6990  -1410  -2620    730  A    O  
ATOM    745  CB  VAL A  93      -0.112  27.662   7.417  1.00 67.03      A    C  
ANISOU  745  CB  VAL A  93    11730   6070   7670  -1190  -2460    650  A    C  
ATOM    746  CG1 VAL A  93      -1.490  27.983   6.858  1.00 70.59      A    C  
ANISOU  746  CG1 VAL A  93    12280   6210   8320  -1100  -3070    720  A    C  
ATOM    747  CG2 VAL A  93       0.148  28.417   8.715  1.00 66.11      A    C  
ANISOU  747  CG2 VAL A  93    11160   6110   7840  -1070  -2240    550  A    C  
ATOM    748  N   ASP A  94      -1.770  24.693   7.229  1.00 64.46      A    N  
ANISOU  748  N   ASP A  94    11040   5900   7550  -1060  -2690    570  A    N  
ATOM    749  CA  ASP A  94      -2.601  23.687   6.541  1.00 60.48      A    C  
ANISOU  749  CA  ASP A  94    10620   5300   7060  -1070  -2960    560  A    C  
ATOM    750  C   ASP A  94      -3.858  23.538   7.390  1.00 60.58      A    C  
ANISOU  750  C   ASP A  94    10090   5310   7620   -870  -3150    430  A    C  
ATOM    751  O   ASP A  94      -3.824  23.910   8.574  1.00 56.33      A    O  
ANISOU  751  O   ASP A  94     9150   4910   7340   -770  -2910    350  A    O  
ATOM    752  CB  ASP A  94      -1.804  22.412   6.296  1.00 59.83      A    C  
ANISOU  752  CB  ASP A  94    10650   5410   6670  -1190  -2590    550  A    C  
ATOM    753  CG  ASP A  94      -2.593  21.390   5.479  1.00 61.20      A    C  
ANISOU  753  CG  ASP A  94    10960   5480   6810  -1220  -2860    550  A    C  
ATOM    754  OD1 ASP A  94      -3.631  20.866   6.015  1.00 58.73      A    O  
ANISOU  754  OD1 ASP A  94    10240   5190   6880  -1080  -3000    450  A    O  
ATOM    755  OD2 ASP A  94      -2.200  21.171   4.284  1.00 61.79      A    O1-
ANISOU  755  OD2 ASP A  94    11580   5430   6470  -1410  -2920    630  A    O1-
ATOM    756  N   LYS A  95      -4.950  23.114   6.763  1.00 65.56      A    N  
ANISOU  756  N   LYS A  95    10740   5750   8430   -840  -3570    400  A    N  
ATOM    757  CA  LYS A  95      -6.253  22.936   7.442  1.00 67.16      A    C  
ANISOU  757  CA  LYS A  95    10410   5880   9230   -680  -3750    210  A    C  
ATOM    758  C   LYS A  95      -6.077  21.862   8.528  1.00 62.03      A    C  
ANISOU  758  C   LYS A  95     9370   5530   8660   -660  -3210    100  A    C  
ATOM    759  O   LYS A  95      -6.727  21.971   9.576  1.00 64.12      A    O  
ANISOU  759  O   LYS A  95     9180   5820   9370   -560  -3080    -60  A    O  
ATOM    760  CB  LYS A  95      -7.355  22.638   6.408  1.00 73.13      A    C  
ANISOU  760  CB  LYS A  95    11290   6350  10150   -660  -4340    180  A    C  
ATOM    761  CG  LYS A  95      -6.950  21.822   5.176  1.00 75.16      A    C  
ANISOU  761  CG  LYS A  95    12080   6570   9900   -810  -4450    300  A    C  
ATOM    762  N   ASP A  96      -5.190  20.893   8.334  1.00 57.32      A    N  
ANISOU  762  N   ASP A  96     8980   5130   7660   -760  -2880    170  A    N  
ATOM    763  CA  ASP A  96      -5.114  19.727   9.258  1.00 57.26      A    C  
ANISOU  763  CA  ASP A  96     8690   5350   7720   -740  -2450     70  A    C  
ATOM    764  C   ASP A  96      -3.844  19.689  10.121  1.00 55.61      A    C  
ANISOU  764  C   ASP A  96     8470   5400   7260   -740  -1980    120  A    C  
ATOM    765  O   ASP A  96      -3.794  18.812  11.045  1.00 53.45      A    O  
ANISOU  765  O   ASP A  96     7990   5280   7050   -710  -1650     40  A    O  
ATOM    766  CB  ASP A  96      -5.303  18.447   8.466  1.00 60.12      A    C  
ANISOU  766  CB  ASP A  96     9200   5700   7930   -810  -2490     80  A    C  
ATOM    767  CG  ASP A  96      -6.703  18.368   7.881  1.00 63.85      A    C  
ANISOU  767  CG  ASP A  96     9560   5930   8770   -770  -2960    -30  A    C  
ATOM    768  OD1 ASP A  96      -7.667  18.524   8.663  1.00 64.88      A    O  
ANISOU  768  OD1 ASP A  96     9260   5990   9400   -670  -2980   -210  A    O  
ATOM    769  OD2 ASP A  96      -6.801  18.212   6.650  1.00 66.22      A    O1-
ANISOU  769  OD2 ASP A  96    10220   6080   8860   -850  -3310     40  A    O1-
ATOM    770  N   TYR A  97      -2.911  20.626   9.933  1.00 51.81      A    N  
ANISOU  770  N   TYR A  97     8190   4930   6560   -780  -1950    210  A    N  
ATOM    771  CA  TYR A  97      -1.677  20.699  10.744  1.00 48.82      A    C  
ANISOU  771  CA  TYR A  97     7770   4770   6000   -780  -1560    210  A    C  
ATOM    772  C   TYR A  97      -0.979  22.041  10.588  1.00 49.12      A    C  
ANISOU  772  C   TYR A  97     7960   4760   5940   -820  -1590    260  A    C  
ATOM    773  O   TYR A  97      -1.039  22.671   9.529  1.00 51.63      A    O  
ANISOU  773  O   TYR A  97     8590   4890   6130   -900  -1850    350  A    O  
ATOM    774  CB  TYR A  97      -0.686  19.618  10.334  1.00 45.95      A    C  
ANISOU  774  CB  TYR A  97     7600   4530   5330   -860  -1320    240  A    C  
ATOM    775  CG  TYR A  97      -0.214  19.666   8.911  1.00 47.93      A    C  
ANISOU  775  CG  TYR A  97     8270   4670   5270  -1030  -1420    320  A    C  
ATOM    776  CD1 TYR A  97      -0.941  19.062   7.893  1.00 51.97      A    C  
ANISOU  776  CD1 TYR A  97     8990   5040   5720  -1100  -1660    350  A    C  
ATOM    777  CD2 TYR A  97       0.973  20.283   8.582  1.00 50.24      A    C  
ANISOU  777  CD2 TYR A  97     8780   4970   5340  -1130  -1240    330  A    C  
ATOM    778  CE1 TYR A  97      -0.528  19.115   6.568  1.00 54.47      A    C  
ANISOU  778  CE1 TYR A  97     9780   5210   5700  -1280  -1750    420  A    C  
ATOM    779  CE2 TYR A  97       1.420  20.321   7.271  1.00 56.56      A    C  
ANISOU  779  CE2 TYR A  97    10030   5630   5830  -1340  -1260    380  A    C  
ATOM    780  CZ  TYR A  97       0.664  19.745   6.254  1.00 56.85      A    C  
ANISOU  780  CZ  TYR A  97    10340   5510   5750  -1420  -1520    440  A    C  
ATOM    781  OH  TYR A  97       1.127  19.763   4.973  1.00 56.60      A    O  
ANISOU  781  OH  TYR A  97    10830   5320   5350  -1650  -1520    480  A    O  
ATOM    782  N   PHE A  98      -0.239  22.391  11.618  1.00 44.77      A    N  
ANISOU  782  N   PHE A  98     7230   4370   5410   -760  -1320    210  A    N  
ATOM    783  CA  PHE A  98       0.788  23.452  11.585  1.00 46.33      A    C  
ANISOU  783  CA  PHE A  98     7550   4580   5470   -810  -1220    230  A    C  
ATOM    784  C   PHE A  98       2.115  22.843  12.002  1.00 41.52      A    C  
ANISOU  784  C   PHE A  98     6910   4170   4690   -830   -880    170  A    C  
ATOM    785  O   PHE A  98       2.129  22.022  12.946  1.00 38.35      A    O  
ANISOU  785  O   PHE A  98     6300   3920   4360   -730   -740    110  A    O  
ATOM    786  CB  PHE A  98       0.393  24.567  12.561  1.00 50.53      A    C  
ANISOU  786  CB  PHE A  98     7820   5100   6270   -710  -1260    170  A    C  
ATOM    787  CG  PHE A  98      -0.582  25.551  11.983  1.00 59.56      A    C  
ANISOU  787  CG  PHE A  98     9030   6000   7600   -710  -1630    220  A    C  
ATOM    788  CD1 PHE A  98      -1.721  25.128  11.316  1.00 66.02      A    C  
ANISOU  788  CD1 PHE A  98     9880   6640   8560   -700  -1950    240  A    C  
ATOM    789  CD2 PHE A  98      -0.378  26.920  12.132  1.00 66.26      A    C  
ANISOU  789  CD2 PHE A  98     9890   6760   8530   -710  -1680    230  A    C  
ATOM    790  CE1 PHE A  98      -2.618  26.048  10.781  1.00 75.03      A    C  
ANISOU  790  CE1 PHE A  98    11080   7510   9920   -670  -2360    270  A    C  
ATOM    791  CE2 PHE A  98      -1.282  27.836  11.605  1.00 71.38      A    C  
ANISOU  791  CE2 PHE A  98    10610   7140   9380   -690  -2070    270  A    C  
ATOM    792  CZ  PHE A  98      -2.394  27.403  10.915  1.00 72.56      A    C  
ANISOU  792  CZ  PHE A  98    10800   7100   9670   -660  -2430    290  A    C  
ATOM    793  N   ILE A  99       3.197  23.332  11.421  1.00 38.94      A    N  
ANISOU  793  N   ILE A  99     6780   3820   4190   -950   -750    160  A    N  
ATOM    794  CA  ILE A  99       4.576  22.946  11.796  1.00 36.83      A    C  
ANISOU  794  CA  ILE A  99     6440   3700   3850   -960   -450     40  A    C  
ATOM    795  C   ILE A  99       5.282  24.186  12.322  1.00 39.81      A    C  
ANISOU  795  C   ILE A  99     6720   4100   4300   -950   -360    -40  A    C  
ATOM    796  O   ILE A  99       5.280  25.198  11.597  1.00 43.53      A    O  
ANISOU  796  O   ILE A  99     7420   4420   4710  -1080   -410     10  A    O  
ATOM    797  CB  ILE A  99       5.319  22.351  10.600  1.00 38.23      A    C  
ANISOU  797  CB  ILE A  99     6900   3810   3810  -1140   -300     20  A    C  
ATOM    798  CG1 ILE A  99       4.500  21.247   9.940  1.00 39.71      A    C  
ANISOU  798  CG1 ILE A  99     7220   3950   3910  -1170   -430    100  A    C  
ATOM    799  CG2 ILE A  99       6.690  21.839  11.020  1.00 39.33      A    C  
ANISOU  799  CG2 ILE A  99     6870   4080   3990  -1130     -0   -160  A    C  
ATOM    800  CD1 ILE A  99       5.211  20.539   8.799  1.00 41.65      A    C  
ANISOU  800  CD1 ILE A  99     7760   4130   3940  -1360   -240     60  A    C  
ATOM    801  N   PHE A 100       5.837  24.129  13.539  1.00 38.06      A    N  
ANISOU  801  N   PHE A 100     6220   4040   4200   -820   -250   -150  A    N  
ATOM    802  CA  PHE A 100       6.668  25.213  14.098  1.00 38.23      A    C  
ANISOU  802  CA  PHE A 100     6120   4100   4310   -820   -140   -260  A    C  
ATOM    803  C   PHE A 100       8.086  24.725  14.344  1.00 37.61      A    C  
ANISOU  803  C   PHE A 100     5920   4110   4260   -810     60   -440  A    C  
ATOM    804  O   PHE A 100       8.275  23.524  14.444  1.00 36.72      A    O  
ANISOU  804  O   PHE A 100     5770   4060   4120   -750     80   -470  A    O  
ATOM    805  CB  PHE A 100       6.068  25.682  15.412  1.00 40.20      A    C  
ANISOU  805  CB  PHE A 100     6140   4420   4710   -660   -240   -260  A    C  
ATOM    806  CG  PHE A 100       4.869  26.556  15.230  1.00 40.92      A    C  
ANISOU  806  CG  PHE A 100     6270   4380   4900   -670   -420   -160  A    C  
ATOM    807  CD1 PHE A 100       5.008  27.932  15.137  1.00 45.23      A    C  
ANISOU  807  CD1 PHE A 100     6840   4840   5510   -730   -430   -170  A    C  
ATOM    808  CD2 PHE A 100       3.617  26.011  15.154  1.00 43.51      A    C  
ANISOU  808  CD2 PHE A 100     6590   4650   5290   -630   -570    -80  A    C  
ATOM    809  CE1 PHE A 100       3.900  28.757  14.993  1.00 46.01      A    C  
ANISOU  809  CE1 PHE A 100     6950   4780   5750   -710   -640    -90  A    C  
ATOM    810  CE2 PHE A 100       2.510  26.830  15.026  1.00 44.68      A    C  
ANISOU  810  CE2 PHE A 100     6710   4650   5620   -620   -770    -30  A    C  
ATOM    811  CZ  PHE A 100       2.651  28.196  14.950  1.00 46.46      A    C  
ANISOU  811  CZ  PHE A 100     6960   4780   5920   -660   -820    -30  A    C  
ATOM    812  N   TYR A 101       9.031  25.649  14.515  1.00 38.22      A    N  
ANISOU  812  N   TYR A 101     5910   4180   4420   -860    190   -590  A    N  
ATOM    813  CA  TYR A 101      10.452  25.362  14.815  1.00 39.73      A    C  
ANISOU  813  CA  TYR A 101     5920   4440   4740   -840    360   -830  A    C  
ATOM    814  C   TYR A 101      10.962  26.356  15.864  1.00 40.90      A    C  
ANISOU  814  C   TYR A 101     5830   4650   5050   -750    340   -970  A    C  
ATOM    815  O   TYR A 101      10.833  27.568  15.707  1.00 40.96      A    O  
ANISOU  815  O   TYR A 101     5900   4590   5080   -840    390   -950  A    O  
ATOM    816  CB  TYR A 101      11.283  25.415  13.534  1.00 44.16      A    C  
ANISOU  816  CB  TYR A 101     6650   4860   5270  -1080    630   -950  A    C  
ATOM    817  CG  TYR A 101      12.651  24.794  13.651  1.00 47.38      A    C  
ANISOU  817  CG  TYR A 101     6830   5290   5890  -1070    820  -1240  A    C  
ATOM    818  CD1 TYR A 101      13.707  25.491  14.221  1.00 53.85      A    C  
ANISOU  818  CD1 TYR A 101     7380   6120   6960  -1050    920  -1500  A    C  
ATOM    819  CD2 TYR A 101      12.872  23.492  13.236  1.00 51.31      A    C  
ANISOU  819  CD2 TYR A 101     7330   5780   6380  -1080    880  -1280  A    C  
ATOM    820  CE1 TYR A 101      14.954  24.916  14.366  1.00 57.78      A    C  
ANISOU  820  CE1 TYR A 101     7610   6610   7740  -1020   1040  -1810  A    C  
ATOM    821  CE2 TYR A 101      14.110  22.897  13.375  1.00 53.30      A    C  
ANISOU  821  CE2 TYR A 101     7320   6020   6900  -1050   1010  -1570  A    C  
ATOM    822  CZ  TYR A 101      15.151  23.609  13.929  1.00 54.42      A    C  
ANISOU  822  CZ  TYR A 101     7180   6160   7330  -1010   1090  -1850  A    C  
ATOM    823  OH  TYR A 101      16.372  23.032  14.019  1.00 54.11      A    O  
ANISOU  823  OH  TYR A 101     6850   6080   7630   -980   1190  -2190  A    O  
ATOM    824  N   GLY A 102      11.650  25.860  16.871  1.00 41.33      A    N  
ANISOU  824  N   GLY A 102     5650   4810   5240   -580    280  -1120  A    N  
ATOM    825  CA  GLY A 102      12.235  26.739  17.892  1.00 43.48      A    C  
ANISOU  825  CA  GLY A 102     5720   5140   5660   -490    230  -1280  A    C  
ATOM    826  C   GLY A 102      13.475  26.137  18.491  1.00 44.16      A    C  
ANISOU  826  C   GLY A 102     5570   5270   5940   -370    180  -1540  A    C  
ATOM    827  O   GLY A 102      13.858  25.002  18.131  1.00 45.97      A    O  
ANISOU  827  O   GLY A 102     5780   5480   6210   -340    190  -1590  A    O  
ATOM    828  N   HIS A 103      14.056  26.910  19.374  1.00 44.67      A    N  
ANISOU  828  N   HIS A 103     5450   5370   6160   -290    110  -1710  A    N  
ATOM    829  CA  HIS A 103      15.275  26.629  20.148  1.00 47.05      A    C  
ANISOU  829  CA  HIS A 103     5480   5690   6700   -140    -30  -2010  A    C  
ATOM    830  C   HIS A 103      15.004  26.804  21.629  1.00 46.71      A    C  
ANISOU  830  C   HIS A 103     5440   5730   6570     60   -330  -1970  A    C  
ATOM    831  O   HIS A 103      15.678  27.567  22.288  1.00 55.83      A    O  
ANISOU  831  O   HIS A 103     6430   6900   7890    100   -400  -2180  A    O  
ATOM    832  CB  HIS A 103      16.376  27.550  19.674  1.00 46.88      A    C  
ANISOU  832  CB  HIS A 103     5240   5590   6980   -280    190  -2310  A    C  
ATOM    833  CG  HIS A 103      16.668  27.431  18.216  1.00 46.75      A    C  
ANISOU  833  CG  HIS A 103     5300   5450   7010   -520    550  -2370  A    C  
ATOM    834  CD2 HIS A 103      16.157  28.086  17.155  1.00 45.34      A    C  
ANISOU  834  CD2 HIS A 103     5380   5190   6670   -770    820  -2220  A    C  
ATOM    835  ND1 HIS A 103      17.676  26.618  17.723  1.00 50.98      A    N  
ANISOU  835  ND1 HIS A 103     5660   5900   7810   -550    670  -2630  A    N  
ATOM    836  CE1 HIS A 103      17.743  26.785  16.399  1.00 51.32      A    C  
ANISOU  836  CE1 HIS A 103     5870   5820   7810   -830   1050  -2650  A    C  
ATOM    837  NE2 HIS A 103      16.858  27.723  16.028  1.00 46.72      A    N  
ANISOU  837  NE2 HIS A 103     5580   5220   6950   -970   1130  -2390  A    N  
ATOM    838  N   PRO A 104      14.046  26.067  22.209  1.00 47.20      A    N  
ANISOU  838  N   PRO A 104     5730   5830   6370    160   -480  -1740  A    N  
ATOM    839  CA  PRO A 104      13.804  26.128  23.643  1.00 50.85      A    C  
ANISOU  839  CA  PRO A 104     6290   6340   6690    310   -730  -1720  A    C  
ATOM    840  C   PRO A 104      14.947  25.508  24.433  1.00 59.06      A    C  
ANISOU  840  C   PRO A 104     7230   7340   7860    510  -1040  -1940  A    C  
ATOM    841  O   PRO A 104      15.736  24.721  23.888  1.00 62.49      A    O  
ANISOU  841  O   PRO A 104     7520   7720   8500    560  -1080  -2080  A    O  
ATOM    842  CB  PRO A 104      12.569  25.222  23.821  1.00 47.01      A    C  
ANISOU  842  CB  PRO A 104     6090   5850   5920    330   -740  -1450  A    C  
ATOM    843  CG  PRO A 104      12.709  24.218  22.705  1.00 46.10      A    C  
ANISOU  843  CG  PRO A 104     5960   5700   5860    290   -660  -1400  A    C  
ATOM    844  CD  PRO A 104      13.240  25.034  21.556  1.00 45.69      A    C  
ANISOU  844  CD  PRO A 104     5730   5620   6010    130   -430  -1520  A    C  
ATOM    845  N   PRO A 105      14.983  25.777  25.756  1.00 65.70      A    N  
ANISOU  845  N   PRO A 105     8180   8200   8580    630  -1290  -1990  A    N  
ATOM    846  CA  PRO A 105      15.931  25.138  26.672  1.00 69.89      A    C  
ANISOU  846  CA  PRO A 105     8720   8660   9180    860  -1710  -2170  A    C  
ATOM    847  C   PRO A 105      16.063  23.612  26.546  1.00 73.68      A    C  
ANISOU  847  C   PRO A 105     9330   9050   9610    990  -1890  -2100  A    C  
ATOM    848  O   PRO A 105      17.162  23.117  26.700  1.00 82.18      A    O  
ANISOU  848  O   PRO A 105    10240  10030  10950   1150  -2180  -2330  A    O  
ATOM    849  CB  PRO A 105      15.345  25.442  28.067  1.00 71.35      A    C  
ANISOU  849  CB  PRO A 105     9240   8850   9020    910  -1890  -2070  A    C  
ATOM    850  CG  PRO A 105      14.582  26.758  27.881  1.00 69.15      A    C  
ANISOU  850  CG  PRO A 105     8910   8660   8710    710  -1550  -2000  A    C  
ATOM    851  CD  PRO A 105      14.095  26.745  26.442  1.00 67.28      A    C  
ANISOU  851  CD  PRO A 105     8530   8450   8580    560  -1210  -1870  A    C  
ATOM    852  N   ALA A 106      14.954  22.909  26.313  1.00 67.57      A    N  
ANISOU  852  N   ALA A 106     8840   8280   8550    930  -1730  -1810  A    N  
ATOM    853  CA  ALA A 106      14.906  21.434  26.207  1.00 65.45      A    C  
ANISOU  853  CA  ALA A 106     8740   7930   8200   1030  -1860  -1710  A    C  
ATOM    854  C   ALA A 106      15.589  20.978  24.915  1.00 62.88      A    C  
ANISOU  854  C   ALA A 106     8100   7580   8220    990  -1720  -1840  A    C  
ATOM    855  O   ALA A 106      15.909  19.774  24.828  1.00 65.63      A    O  
ANISOU  855  O   ALA A 106     8490   7830   8620   1120  -1880  -1850  A    O  
ATOM    856  CB  ALA A 106      13.483  20.930  26.273  1.00 64.69      A    C  
ANISOU  856  CB  ALA A 106     9000   7840   7730    940  -1670  -1400  A    C  
ATOM    857  N   ALA A 107      15.843  21.878  23.963  1.00 58.26      A    N  
ANISOU  857  N   ALA A 107     7230   7050   7860    820  -1420  -1960  A    N  
ATOM    858  CA  ALA A 107      16.513  21.510  22.699  1.00 55.97      A    C  
ANISOU  858  CA  ALA A 107     6680   6710   7880    730  -1200  -2110  A    C  
ATOM    859  C   ALA A 107      17.076  22.738  22.015  1.00 58.05      A    C  
ANISOU  859  C   ALA A 107     6670   6990   8400    550   -930  -2320  A    C  
ATOM    860  O   ALA A 107      16.608  23.117  20.955  1.00 55.63      A    O  
ANISOU  860  O   ALA A 107     6420   6700   8020    320   -580  -2220  A    O  
ATOM    861  CB  ALA A 107      15.557  20.796  21.794  1.00 54.67      A    C  
ANISOU  861  CB  ALA A 107     6710   6560   7500    600   -970  -1860  A    C  
ATOM    862  N   PRO A 108      18.117  23.374  22.596  1.00 63.28      A    N  
ANISOU  862  N   PRO A 108     7060   7620   9360    630  -1090  -2640  A    N  
ATOM    863  CA  PRO A 108      18.645  24.638  22.072  1.00 62.35      A    C  
ANISOU  863  CA  PRO A 108     6710   7500   9480    450   -800  -2850  A    C  
ATOM    864  C   PRO A 108      19.061  24.597  20.594  1.00 59.36      A    C  
ANISOU  864  C   PRO A 108     6200   7040   9320    210   -360  -2990  A    C  
ATOM    865  O   PRO A 108      18.916  25.591  19.878  1.00 58.45      A    O  
ANISOU  865  O   PRO A 108     6120   6920   9170    -30    -10  -2980  A    O  
ATOM    866  CB  PRO A 108      19.843  24.892  23.015  1.00 67.94      A    C  
ANISOU  866  CB  PRO A 108     7100   8150  10560    640  -1130  -3220  A    C  
ATOM    867  CG  PRO A 108      19.440  24.234  24.326  1.00 66.91      A    C  
ANISOU  867  CG  PRO A 108     7240   8040  10140    900  -1620  -3050  A    C  
ATOM    868  CD  PRO A 108      18.764  22.966  23.858  1.00 66.19      A    C  
ANISOU  868  CD  PRO A 108     7390   7930   9820    910  -1580  -2790  A    C  
ATOM    869  N   SER A 109      19.516  23.446  20.120  1.00 58.46      A    N  
ANISOU  869  N   SER A 109     6000   6830   9380    250   -360  -3100  A    N  
ATOM    870  CA  SER A 109      19.995  23.316  18.718  1.00 60.97      A    C  
ANISOU  870  CA  SER A 109     6220   7040   9900    -10    100  -3270  A    C  
ATOM    871  C   SER A 109      18.807  23.172  17.747  1.00 58.46      A    C  
ANISOU  871  C   SER A 109     6310   6760   9140   -220    360  -2900  A    C  
ATOM    872  O   SER A 109      19.032  23.174  16.510  1.00 60.37      A    O  
ANISOU  872  O   SER A 109     6600   6900   9440   -480    770  -2990  A    O  
ATOM    873  CB  SER A 109      20.994  22.173  18.588  1.00 65.90      A    C  
ANISOU  873  CB  SER A 109     6560   7530  10950    100     20  -3590  A    C  
ATOM    874  OG  SER A 109      20.516  21.015  19.256  1.00 64.97      A    O  
ANISOU  874  OG  SER A 109     6600   7440  10650    360   -380  -3360  A    O  
ATOM    875  N   GLY A 110      17.576  23.009  18.251  1.00 54.04      A    N  
ANISOU  875  N   GLY A 110     6040   6320   8170   -120    150  -2510  A    N  
ATOM    876  CA  GLY A 110      16.406  23.045  17.361  1.00 52.98      A    C  
ANISOU  876  CA  GLY A 110     6250   6210   7680   -300    340  -2180  A    C  
ATOM    877  C   GLY A 110      15.378  22.013  17.738  1.00 51.80      A    C  
ANISOU  877  C   GLY A 110     6310   6120   7250   -160    120  -1880  A    C  
ATOM    878  O   GLY A 110      15.751  20.855  18.034  1.00 56.49      A    O  
ANISOU  878  O   GLY A 110     6830   6690   7940     -0    -40  -1950  A    O  
ATOM    879  N   LEU A 111      14.115  22.416  17.662  1.00 47.30      A    N  
ANISOU  879  N   LEU A 111     5990   5610   6380   -220    120  -1590  A    N  
ATOM    880  CA  LEU A 111      12.970  21.527  17.884  1.00 41.66      A    C  
ANISOU  880  CA  LEU A 111     5480   4930   5410   -140    -20  -1310  A    C  
ATOM    881  C   LEU A 111      11.900  21.844  16.858  1.00 39.59      A    C  
ANISOU  881  C   LEU A 111     5450   4640   4950   -330    130  -1100  A    C  
ATOM    882  O   LEU A 111      11.417  22.987  16.884  1.00 39.61      A    O  
ANISOU  882  O   LEU A 111     5490   4650   4910   -400    140  -1030  A    O  
ATOM    883  CB  LEU A 111      12.487  21.764  19.303  1.00 40.01      A    C  
ANISOU  883  CB  LEU A 111     5300   4800   5100     40   -250  -1230  A    C  
ATOM    884  CG  LEU A 111      11.300  20.905  19.672  1.00 38.97      A    C  
ANISOU  884  CG  LEU A 111     5380   4680   4740    100   -340   -990  A    C  
ATOM    885  CD1 LEU A 111      11.630  19.422  19.372  1.00 39.68      A    C  
ANISOU  885  CD1 LEU A 111     5510   4720   4840    160   -370  -1000  A    C  
ATOM    886  CD2 LEU A 111      10.886  21.112  21.134  1.00 39.21      A    C  
ANISOU  886  CD2 LEU A 111     5500   4750   4650    230   -510   -940  A    C  
ATOM    887  N   ALA A 112      11.541  20.853  16.028  1.00 36.94      A    N  
ANISOU  887  N   ALA A 112     5250   4260   4520   -400    190  -1010  A    N  
ATOM    888  CA  ALA A 112      10.424  20.881  15.071  1.00 36.02      A    C  
ANISOU  888  CA  ALA A 112     5380   4100   4210   -560    240   -800  A    C  
ATOM    889  C   ALA A 112       9.219  20.181  15.721  1.00 36.47      A    C  
ANISOU  889  C   ALA A 112     5500   4210   4150   -430     60   -600  A    C  
ATOM    890  O   ALA A 112       9.412  19.078  16.260  1.00 39.46      A    O  
ANISOU  890  O   ALA A 112     5840   4610   4540   -300     10   -630  A    O  
ATOM    891  CB  ALA A 112      10.851  20.195  13.791  1.00 37.76      A    C  
ANISOU  891  CB  ALA A 112     5720   4230   4400   -730    430   -860  A    C  
ATOM    892  N   LEU A 113       8.015  20.762  15.622  1.00 33.90      A    N  
ANISOU  892  N   LEU A 113     5280   3860   3740   -470    -10   -440  A    N  
ATOM    893  CA  LEU A 113       6.775  20.284  16.264  1.00 33.25      A    C  
ANISOU  893  CA  LEU A 113     5220   3790   3620   -380   -120   -310  A    C  
ATOM    894  C   LEU A 113       5.666  20.289  15.236  1.00 34.75      A    C  
ANISOU  894  C   LEU A 113     5550   3890   3770   -500   -170   -180  A    C  
ATOM    895  O   LEU A 113       5.504  21.322  14.545  1.00 35.27      A    O  
ANISOU  895  O   LEU A 113     5690   3880   3830   -610   -210   -150  A    O  
ATOM    896  CB  LEU A 113       6.450  21.232  17.411  1.00 36.40      A    C  
ANISOU  896  CB  LEU A 113     5520   4230   4080   -300   -170   -330  A    C  
ATOM    897  CG  LEU A 113       7.595  21.352  18.397  1.00 39.28      A    C  
ANISOU  897  CG  LEU A 113     5780   4670   4480   -190   -180   -470  A    C  
ATOM    898  CD1 LEU A 113       7.748  22.734  18.922  1.00 42.76      A    C  
ANISOU  898  CD1 LEU A 113     6120   5130   5000   -190   -190   -530  A    C  
ATOM    899  CD2 LEU A 113       7.437  20.383  19.543  1.00 42.12      A    C  
ANISOU  899  CD2 LEU A 113     6200   5050   4760    -50   -250   -460  A    C  
ATOM    900  N   ILE A 114       5.009  19.150  15.048  1.00 32.22      A    N  
ANISOU  900  N   ILE A 114     5290   3560   3400   -490   -180   -120  A    N  
ATOM    901  CA  ILE A 114       3.827  19.058  14.172  1.00 31.16      A    C  
ANISOU  901  CA  ILE A 114     5260   3320   3260   -580   -290    -20  A    C  
ATOM    902  C   ILE A 114       2.606  18.928  15.051  1.00 32.08      A    C  
ANISOU  902  C   ILE A 114     5260   3420   3510   -500   -350     -0  A    C  
ATOM    903  O   ILE A 114       2.478  17.945  15.849  1.00 34.26      A    O  
ANISOU  903  O   ILE A 114     5510   3740   3770   -420   -250    -20  A    O  
ATOM    904  CB  ILE A 114       3.995  17.919  13.189  1.00 34.26      A    C  
ANISOU  904  CB  ILE A 114     5800   3680   3540   -660   -250     -0  A    C  
ATOM    905  CG1 ILE A 114       5.379  17.999  12.553  1.00 36.03      A    C  
ANISOU  905  CG1 ILE A 114     6100   3910   3680   -760   -100    -90  A    C  
ATOM    906  CG2 ILE A 114       2.872  17.859  12.133  1.00 34.26      A    C  
ANISOU  906  CG2 ILE A 114     5950   3550   3520   -770   -410     80  A    C  
ATOM    907  CD1 ILE A 114       5.553  16.947  11.482  1.00 37.86      A    C  
ANISOU  907  CD1 ILE A 114     6500   4090   3800   -880    -10   -100  A    C  
ATOM    908  N   HIS A 115       1.732  19.908  14.905  1.00 33.53      A    N  
ANISOU  908  N   HIS A 115     5390   3510   3840   -530   -480     20  A    N  
ATOM    909  CA  HIS A 115       0.418  20.018  15.571  1.00 34.96      A    C  
ANISOU  909  CA  HIS A 115     5420   3630   4240   -490   -520    -20  A    C  
ATOM    910  C   HIS A 115      -0.638  19.544  14.574  1.00 37.02      A    C  
ANISOU  910  C   HIS A 115     5710   3750   4600   -550   -700     10  A    C  
ATOM    911  O   HIS A 115      -0.750  20.170  13.559  1.00 36.22      A    O  
ANISOU  911  O   HIS A 115     5720   3550   4490   -610   -910     70  A    O  
ATOM    912  CB  HIS A 115       0.210  21.451  16.041  1.00 36.32      A    C  
ANISOU  912  CB  HIS A 115     5470   3760   4580   -470   -580    -50  A    C  
ATOM    913  CG  HIS A 115       1.329  21.935  16.890  1.00 34.92      A    C  
ANISOU  913  CG  HIS A 115     5270   3710   4290   -420   -440    -90  A    C  
ATOM    914  CD2 HIS A 115       2.604  22.273  16.605  1.00 37.25      A    C  
ANISOU  914  CD2 HIS A 115     5640   4070   4430   -440   -410    -90  A    C  
ATOM    915  ND1 HIS A 115       1.201  22.054  18.240  1.00 36.72      A    N  
ANISOU  915  ND1 HIS A 115     5410   3980   4570   -360   -310   -170  A    N  
ATOM    916  CE1 HIS A 115       2.351  22.461  18.767  1.00 37.05      A    C  
ANISOU  916  CE1 HIS A 115     5460   4130   4490   -320   -260   -210  A    C  
ATOM    917  NE2 HIS A 115       3.213  22.659  17.782  1.00 36.94      A    N  
ANISOU  917  NE2 HIS A 115     5520   4130   4390   -360   -320   -180  A    N  
ATOM    918  N   TYR A 116      -1.377  18.469  14.882  1.00 37.58      A    N  
ANISOU  918  N   TYR A 116     5720   3800   4760   -540   -610    -30  A    N  
ATOM    919  CA  TYR A 116      -2.413  17.920  13.969  1.00 39.16      A    C  
ANISOU  919  CA  TYR A 116     5910   3870   5090   -590   -790    -40  A    C  
ATOM    920  C   TYR A 116      -3.806  18.326  14.448  1.00 42.14      A    C  
ANISOU  920  C   TYR A 116     6030   4100   5880   -570   -860   -180  A    C  
ATOM    921  O   TYR A 116      -4.007  18.346  15.640  1.00 42.98      A    O  
ANISOU  921  O   TYR A 116     6000   4230   6100   -540   -620   -270  A    O  
ATOM    922  CB  TYR A 116      -2.268  16.410  13.886  1.00 36.22      A    C  
ANISOU  922  CB  TYR A 116     5630   3550   4580   -600   -630    -40  A    C  
ATOM    923  CG  TYR A 116      -0.943  15.911  13.351  1.00 35.54      A    C  
ANISOU  923  CG  TYR A 116     5750   3580   4170   -630   -550     50  A    C  
ATOM    924  CD1 TYR A 116      -0.739  15.661  12.011  1.00 36.72      A    C  
ANISOU  924  CD1 TYR A 116     6100   3680   4180   -730   -680    100  A    C  
ATOM    925  CD2 TYR A 116       0.088  15.584  14.202  1.00 35.69      A    C  
ANISOU  925  CD2 TYR A 116     5790   3720   4050   -560   -340     40  A    C  
ATOM    926  CE1 TYR A 116       0.453  15.155  11.515  1.00 36.20      A    C  
ANISOU  926  CE1 TYR A 116     6200   3680   3870   -780   -540    120  A    C  
ATOM    927  CE2 TYR A 116       1.297  15.096  13.731  1.00 35.28      A    C  
ANISOU  927  CE2 TYR A 116     5860   3740   3800   -580   -270     60  A    C  
ATOM    928  CZ  TYR A 116       1.459  14.826  12.390  1.00 36.24      A    C  
ANISOU  928  CZ  TYR A 116     6140   3810   3820   -700   -330     90  A    C  
ATOM    929  OH  TYR A 116       2.635  14.291  11.968  1.00 38.15      A    O  
ANISOU  929  OH  TYR A 116     6480   4100   3920   -730   -200     60  A    O  
ATOM    930  N   ARG A 117      -4.744  18.614  13.528  1.00 49.56      A    N  
ANISOU  930  N   ARG A 117     6910   4860   7060   -590  -1190   -210  A    N  
ATOM    931  CA  ARG A 117      -6.190  18.784  13.875  1.00 53.04      A    C  
ANISOU  931  CA  ARG A 117     7030   5110   8010   -570  -1270   -400  A    C  
ATOM    932  C   ARG A 117      -6.764  17.422  14.265  1.00 51.72      A    C  
ANISOU  932  C   ARG A 117     6770   4950   7930   -610  -1010   -510  A    C  
ATOM    933  O   ARG A 117      -7.530  17.386  15.237  1.00 51.39      A    O  
ANISOU  933  O   ARG A 117     6480   4830   8210   -620   -770   -700  A    O  
ATOM    934  CB  ARG A 117      -7.027  19.397  12.750  1.00 57.85      A    C  
ANISOU  934  CB  ARG A 117     7610   5490   8880   -550  -1780   -420  A    C  
ATOM    935  CG  ARG A 117      -6.929  20.906  12.613  1.00 63.32      A    C  
ANISOU  935  CG  ARG A 117     8310   6080   9670   -510  -2040   -380  A    C  
ATOM    936  CD  ARG A 117      -7.260  21.638  13.900  1.00 67.35      A    C  
ANISOU  936  CD  ARG A 117     8490   6590  10510   -470  -1800   -530  A    C  
ATOM    937  NE  ARG A 117      -7.297  23.095  13.785  1.00 69.06      A    N  
ANISOU  937  NE  ARG A 117     8670   6680  10890   -410  -2060   -520  A    N  
ATOM    938  CZ  ARG A 117      -7.571  23.916  14.801  1.00 67.71      A    C  
ANISOU  938  CZ  ARG A 117     8230   6470  11020   -390  -1890   -660  A    C  
ATOM    939  NH1 ARG A 117      -7.830  23.422  16.005  1.00 64.80      A    N1+
ANISOU  939  NH1 ARG A 117     7660   6180  10780   -420  -1440   -830  A    N1+
ATOM    940  NH2 ARG A 117      -7.599  25.230  14.611  1.00 69.15      A    N  
ANISOU  940  NH2 ARG A 117     8390   6520  11360   -340  -2150   -640  A    N  
ATOM    941  N   GLN A 118      -6.354  16.321  13.626  1.00 50.72      A    N  
ANISOU  941  N   GLN A 118     6850   4900   7530   -640   -990   -420  A    N  
ATOM    942  CA  GLN A 118      -6.888  14.990  14.073  1.00 55.83      A    C  
ANISOU  942  CA  GLN A 118     7420   5530   8260   -690   -710   -530  A    C  
ATOM    943  C   GLN A 118      -5.844  14.256  14.941  1.00 52.53      A    C  
ANISOU  943  C   GLN A 118     7210   5290   7460   -680   -330   -440  A    C  
ATOM    944  O   GLN A 118      -4.633  14.330  14.649  1.00 52.03      A    O  
ANISOU  944  O   GLN A 118     7360   5370   7050   -650   -370   -280  A    O  
ATOM    945  CB  GLN A 118      -7.394  14.195  12.863  1.00 55.06      A    C  
ANISOU  945  CB  GLN A 118     7370   5340   8210   -730   -950   -550  A    C  
ATOM    946  CG  GLN A 118      -8.461  14.947  12.077  1.00 56.91      A    C  
ANISOU  946  CG  GLN A 118     7420   5360   8850   -710  -1410   -660  A    C  
ATOM    947  CD  GLN A 118      -7.894  15.917  11.064  1.00 59.02      A    C  
ANISOU  947  CD  GLN A 118     7940   5600   8880   -690  -1820   -480  A    C  
ATOM    948  NE2 GLN A 118      -8.469  17.125  10.997  1.00 58.58      A    N  
ANISOU  948  NE2 GLN A 118     7730   5380   9140   -630  -2140   -540  A    N  
ATOM    949  OE1 GLN A 118      -6.955  15.583  10.333  1.00 58.08      A    O  
ANISOU  949  OE1 GLN A 118     8160   5590   8320   -740  -1840   -310  A    O  
ATOM    950  N   SER A 119      -6.300  13.583  15.989  1.00 50.02      A    N  
ANISOU  950  N   SER A 119     6840   4930   7240   -710     20   -550  A    N  
ATOM    951  CA  SER A 119      -5.466  12.712  16.859  1.00 48.37      A    C  
ANISOU  951  CA  SER A 119     6880   4820   6680   -700    340   -470  A    C  
ATOM    952  C   SER A 119      -4.683  11.619  16.100  1.00 45.91      A    C  
ANISOU  952  C   SER A 119     6770   4600   6070   -680    290   -340  A    C  
ATOM    953  O   SER A 119      -3.585  11.243  16.573  1.00 42.27      A    O  
ANISOU  953  O   SER A 119     6520   4240   5300   -620    390   -230  A    O  
ATOM    954  CB  SER A 119      -6.297  12.078  17.882  1.00 46.76      A    C  
ANISOU  954  CB  SER A 119     6650   4490   6620   -780    700   -630  A    C  
ATOM    955  OG  SER A 119      -5.473  11.255  18.659  1.00 46.88      A    O  
ANISOU  955  OG  SER A 119     6980   4560   6260   -750    930   -530  A    O  
ATOM    956  N   CYS A 120      -5.235  11.078  15.018  1.00 49.20      A    N  
ANISOU  956  N   CYS A 120     7130   4960   6600   -730    140   -360  A    N  
ATOM    957  CA  CYS A 120      -4.615  10.022  14.188  1.00 50.28      A    C  
ANISOU  957  CA  CYS A 120     7450   5150   6500   -750    120   -270  A    C  
ATOM    958  C   CYS A 120      -4.885  10.394  12.747  1.00 53.05      A    C  
ANISOU  958  C   CYS A 120     7780   5460   6910   -800   -230   -260  A    C  
ATOM    959  O   CYS A 120      -5.971  10.185  12.214  1.00 52.57      A    O  
ANISOU  959  O   CYS A 120     7590   5270   7110   -850   -380   -370  A    O  
ATOM    960  CB  CYS A 120      -5.151   8.608  14.462  1.00 58.44      A    C  
ANISOU  960  CB  CYS A 120     8520   6110   7580   -800    370   -340  A    C  
ATOM    961  SG  CYS A 120      -4.373   7.319  13.424  1.00 56.74      A    S  
ANISOU  961  SG  CYS A 120     8510   5950   7100   -820    350   -240  A    S  
ATOM    962  N   PRO A 121      -3.956  11.121  12.112  1.00 57.12      A    N  
ANISOU  962  N   PRO A 121     8440   6050   7210   -790   -410   -140  A    N  
ATOM    963  CA  PRO A 121      -4.253  11.730  10.822  1.00 57.99      A    C  
ANISOU  963  CA  PRO A 121     8630   6080   7330   -850   -770   -110  A    C  
ATOM    964  C   PRO A 121      -4.144  10.670   9.716  1.00 57.07      A    C  
ANISOU  964  C   PRO A 121     8700   5940   7040   -940   -810    -90  A    C  
ATOM    965  O   PRO A 121      -3.200   9.878   9.741  1.00 51.55      A    O  
ANISOU  965  O   PRO A 121     8130   5340   6110   -960   -580    -50  A    O  
ATOM    966  CB  PRO A 121      -3.201  12.823  10.670  1.00 51.66      A    C  
ANISOU  966  CB  PRO A 121     7970   5350   6310   -840   -830    -10  A    C  
ATOM    967  CG  PRO A 121      -2.445  12.814  11.969  1.00 51.40      A    C  
ANISOU  967  CG  PRO A 121     7860   5450   6220   -750   -540     -0  A    C  
ATOM    968  CD  PRO A 121      -2.613  11.449  12.587  1.00 53.44      A    C  
ANISOU  968  CD  PRO A 121     8090   5730   6490   -730   -280    -50  A    C  
ATOM    969  N   LYS A 122      -5.043  10.765   8.745  1.00 60.97      A    N  
ANISOU  969  N   LYS A 122     9220   6290   7660  -1000  -1140   -140  A    N  
ATOM    970  CA  LYS A 122      -5.119   9.843   7.582  1.00 66.59      A    C  
ANISOU  970  CA  LYS A 122    10140   6950   8220  -1120  -1240   -140  A    C  
ATOM    971  C   LYS A 122      -3.880  10.080   6.714  1.00 65.43      A    C  
ANISOU  971  C   LYS A 122    10360   6850   7650  -1220  -1230    -20  A    C  
ATOM    972  O   LYS A 122      -3.151  11.101   6.958  1.00 59.16      A    O  
ANISOU  972  O   LYS A 122     9620   6100   6750  -1190  -1210     60  A    O  
ATOM    973  CB  LYS A 122      -6.497   9.994   6.922  1.00 71.20      A    C  
ANISOU  973  CB  LYS A 122    10630   7330   9100  -1130  -1660   -250  A    C  
ATOM    974  CG  LYS A 122      -7.655   9.660   7.868  1.00 78.29      A    C  
ANISOU  974  CG  LYS A 122    11100   8160  10480  -1060  -1550   -450  A    C  
ATOM    975  CD  LYS A 122      -7.299   8.549   8.892  1.00 81.49      A    C  
ANISOU  975  CD  LYS A 122    11420   8690  10840  -1050  -1020   -470  A    C  
ATOM    976  CE  LYS A 122      -8.327   8.275   9.973  1.00 84.57      A    C  
ANISOU  976  CE  LYS A 122    11470   9000  11660  -1030   -790   -670  A    C  
ATOM    977  NZ  LYS A 122      -9.614   7.831   9.391  1.00 88.96      A    N1+
ANISOU  977  NZ  LYS A 122    11820   9370  12610  -1080  -1010   -880  A    N1+
ATOM    978  N   GLU A 123      -3.615   9.113   5.831  1.00 65.85      A    N  
ANISOU  978  N   GLU A 123    10630   6890   7500  -1340  -1170    -20  A    N  
ATOM    979  CA  GLU A 123      -2.371   8.960   5.026  1.00 70.60      A    C  
ANISOU  979  CA  GLU A 123    11570   7530   7720  -1480  -1010     40  A    C  
ATOM    980  C   GLU A 123      -2.236  10.131   4.046  1.00 66.19      A    C  
ANISOU  980  C   GLU A 123    11370   6840   6940  -1600  -1300    110  A    C  
ATOM    981  O   GLU A 123      -1.094  10.415   3.633  1.00 64.91      A    O  
ANISOU  981  O   GLU A 123    11460   6700   6510  -1720  -1090    140  A    O  
ATOM    982  CB  GLU A 123      -2.349   7.610   4.292  1.00 73.98      A    C  
ANISOU  982  CB  GLU A 123    12140   7940   8030  -1600   -890    -20  A    C  
ATOM    983  CG  GLU A 123      -1.134   7.459   3.376  1.00 83.05      A    C  
ANISOU  983  CG  GLU A 123    13640   9080   8830  -1780   -680    -10  A    C  
ATOM    984  CD  GLU A 123      -0.694   6.052   2.976  1.00 88.56      A    C  
ANISOU  984  CD  GLU A 123    14400   9800   9440  -1880   -400    -80  A    C  
ATOM    985  OE1 GLU A 123       0.494   5.902   2.584  1.00 90.56      A    O  
ANISOU  985  OE1 GLU A 123    14820  10070   9520  -2000   -110   -120  A    O  
ATOM    986  OE2 GLU A 123      -1.521   5.112   3.043  1.00 85.42      A    O1-
ANISOU  986  OE2 GLU A 123    13880   9390   9190  -1840   -440   -130  A    O1-
ATOM    987  N   ASP A 124      -3.357  10.748   3.667  1.00 63.87      A    N  
ANISOU  987  N   ASP A 124    11100   6380   6780  -1570  -1750    110  A    N  
ATOM    988  CA  ASP A 124      -3.375  11.959   2.801  1.00 70.17      A    C  
ANISOU  988  CA  ASP A 124    12290   7000   7380  -1660  -2110    200  A    C  
ATOM    989  C   ASP A 124      -2.631  13.067   3.551  1.00 64.89      A    C  
ANISOU  989  C   ASP A 124    11520   6410   6720  -1590  -1950    260  A    C  
ATOM    990  O   ASP A 124      -1.677  13.660   2.971  1.00 63.78      A    O  
ANISOU  990  O   ASP A 124    11750   6230   6250  -1740  -1840    320  A    O  
ATOM    991  CB  ASP A 124      -4.799  12.394   2.400  1.00 77.64      A    C  
ANISOU  991  CB  ASP A 124    13210   7720   8570  -1600  -2710    170  A    C  
ATOM    992  CG  ASP A 124      -5.842  12.375   3.520  1.00 83.49      A    C  
ANISOU  992  CG  ASP A 124    13360   8490   9870  -1390  -2770     50  A    C  
ATOM    993  OD1 ASP A 124      -5.698  11.544   4.450  1.00 90.04      A    O  
ANISOU  993  OD1 ASP A 124    13860   9500  10850  -1330  -2360    -20  A    O  
ATOM    994  OD2 ASP A 124      -6.811  13.176   3.455  1.00 86.62      A    O1-
ANISOU  994  OD2 ASP A 124    13650   8700  10560  -1300  -3230     10  A    O1-
ATOM    995  N   ILE A 125      -3.049  13.309   4.796  1.00 57.81      A    N  
ANISOU  995  N   ILE A 125    10160   5620   6190  -1400  -1900    220  A    N  
ATOM    996  CA  ILE A 125      -2.494  14.399   5.634  1.00 56.56      A    C  
ANISOU  996  CA  ILE A 125     9870   5540   6090  -1320  -1780    250  A    C  
ATOM    997  C   ILE A 125      -0.998  14.143   5.795  1.00 50.10      A    C  
ANISOU  997  C   ILE A 125     9140   4880   5020  -1380  -1340    260  A    C  
ATOM    998  O   ILE A 125      -0.194  15.058   5.562  1.00 53.35      A    O  
ANISOU  998  O   ILE A 125     9750   5260   5260  -1460  -1280    300  A    O  
ATOM    999  CB  ILE A 125      -3.278  14.544   6.945  1.00 56.60      A    C  
ANISOU  999  CB  ILE A 125     9390   5600   6510  -1130  -1760    180  A    C  
ATOM   1000  CG1 ILE A 125      -4.727  14.962   6.657  1.00 61.95      A    C  
ANISOU 1000  CG1 ILE A 125     9950   6070   7520  -1070  -2220    110  A    C  
ATOM   1001  CG2 ILE A 125      -2.601  15.565   7.831  1.00 55.49      A    C  
ANISOU 1001  CG2 ILE A 125     9130   5560   6400  -1050  -1600    200  A    C  
ATOM   1002  CD1 ILE A 125      -5.763  14.226   7.476  1.00 64.75      A    C  
ANISOU 1002  CD1 ILE A 125     9880   6430   8290   -980  -2140    -50  A    C  
ATOM   1003  N   ILE A 126      -0.616  12.912   6.036  1.00 49.60      A    N  
ANISOU 1003  N   ILE A 126     8970   4930   4940  -1380  -1050    210  A    N  
ATOM   1004  CA  ILE A 126       0.809  12.572   6.281  1.00 46.75      A    C  
ANISOU 1004  CA  ILE A 126     8620   4700   4450  -1410   -660    170  A    C  
ATOM   1005  C   ILE A 126       1.599  12.899   5.022  1.00 47.14      A    C  
ANISOU 1005  C   ILE A 126     9090   4630   4180  -1650   -590    170  A    C  
ATOM   1006  O   ILE A 126       2.743  13.392   5.139  1.00 46.32      A    O  
ANISOU 1006  O   ILE A 126     9020   4570   4020  -1700   -350    120  A    O  
ATOM   1007  CB  ILE A 126       0.946  11.104   6.714  1.00 46.13      A    C  
ANISOU 1007  CB  ILE A 126     8370   4710   4440  -1350   -430    110  A    C  
ATOM   1008  CG1 ILE A 126       0.098  10.769   7.945  1.00 46.91      A    C  
ANISOU 1008  CG1 ILE A 126     8140   4870   4810  -1160   -450    100  A    C  
ATOM   1009  CG2 ILE A 126       2.407  10.745   6.944  1.00 46.47      A    C  
ANISOU 1009  CG2 ILE A 126     8390   4840   4420  -1360    -90     40  A    C  
ATOM   1010  CD1 ILE A 126       0.287  11.711   9.106  1.00 45.83      A    C  
ANISOU 1010  CD1 ILE A 126     7810   4810   4800  -1030   -430    110  A    C  
ATOM   1011  N   LYS A 127       1.012  12.665   3.844  1.00 54.75      A    N  
ANISOU 1011  N   LYS A 127    10410   5440   4960  -1810   -800    200  A    N  
ATOM   1012  CA  LYS A 127       1.736  12.858   2.544  1.00 56.41      A    C  
ANISOU 1012  CA  LYS A 127    11140   5500   4790  -2090   -690    190  A    C  
ATOM   1013  C   LYS A 127       1.972  14.364   2.349  1.00 56.08      A    C  
ANISOU 1013  C   LYS A 127    11340   5340   4630  -2150   -810    260  A    C  
ATOM   1014  O   LYS A 127       3.152  14.735   2.096  1.00 56.69      A    O  
ANISOU 1014  O   LYS A 127    11590   5400   4550  -2310   -460    190  A    O  
ATOM   1015  CB  LYS A 127       1.072  12.109   1.377  1.00 63.78      A    C  
ANISOU 1015  CB  LYS A 127    12440   6280   5510  -2250   -880    200  A    C  
ATOM   1016  CG  LYS A 127       1.480  10.622   1.262  1.00 67.31      A    C  
ANISOU 1016  CG  LYS A 127    12790   6820   5970  -2310   -550     90  A    C  
ATOM   1017  CD  LYS A 127       0.626   9.700   0.368  1.00 69.94      A    C  
ANISOU 1017  CD  LYS A 127    13350   7050   6180  -2410   -760     80  A    C  
ATOM   1018  N   ARG A 128       0.958  15.206   2.593  1.00 55.16      A    N  
ANISOU 1018  N   ARG A 128    11170   5140   4650  -2020  -1240    360  A    N  
ATOM   1019  CA  ARG A 128       1.114  16.688   2.659  1.00 56.10      A    C  
ANISOU 1019  CA  ARG A 128    11420   5160   4730  -2020  -1370    430  A    C  
ATOM   1020  C   ARG A 128       2.173  17.095   3.693  1.00 56.97      A    C  
ANISOU 1020  C   ARG A 128    11190   5460   4990  -1940   -980    350  A    C  
ATOM   1021  O   ARG A 128       2.966  17.992   3.334  1.00 60.02      A    O  
ANISOU 1021  O   ARG A 128    11850   5750   5200  -2090   -830    350  A    O  
ATOM   1022  CB  ARG A 128      -0.209  17.373   3.016  1.00 60.33      A    C  
ANISOU 1022  CB  ARG A 128    11780   5600   5530  -1830  -1890    500  A    C  
ATOM   1023  CG  ARG A 128      -1.280  17.287   1.931  1.00 65.17      A    C  
ANISOU 1023  CG  ARG A 128    12770   5960   6030  -1900  -2410    560  A    C  
ATOM   1024  CD  ARG A 128      -2.451  18.233   2.146  1.00 66.71      A    C  
ANISOU 1024  CD  ARG A 128    12830   5980   6530  -1720  -2960    610  A    C  
ATOM   1025  NE  ARG A 128      -3.496  17.705   3.021  1.00 67.41      A    N  
ANISOU 1025  NE  ARG A 128    12330   6170   7120  -1500  -3080    500  A    N  
ATOM   1026  CZ  ARG A 128      -4.196  18.428   3.910  1.00 68.07      A    C  
ANISOU 1026  CZ  ARG A 128    11990   6240   7630  -1310  -3260    460  A    C  
ATOM   1027  NH1 ARG A 128      -3.985  19.723   4.037  1.00 71.87      A    N1+
ANISOU 1027  NH1 ARG A 128    12560   6630   8120  -1280  -3370    520  A    N1+
ATOM   1028  NH2 ARG A 128      -5.116  17.868   4.682  1.00 68.69      A    N  
ANISOU 1028  NH2 ARG A 128    11560   6380   8160  -1160  -3280    320  A    N  
ATOM   1029  N   VAL A 129       2.165  16.524   4.935  1.00 52.92      A    N  
ANISOU 1029  N   VAL A 129    10150   5170   4780  -1720   -850    290  A    N  
ATOM   1030  CA  VAL A 129       3.182  16.856   5.987  1.00 48.17      A    C  
ANISOU 1030  CA  VAL A 129     9230   4740   4330  -1620   -540    210  A    C  
ATOM   1031  C   VAL A 129       4.580  16.592   5.415  1.00 46.79      A    C  
ANISOU 1031  C   VAL A 129     9240   4550   3990  -1820   -140     90  A    C  
ATOM   1032  O   VAL A 129       5.441  17.459   5.536  1.00 47.11      A    O  
ANISOU 1032  O   VAL A 129     9290   4580   4030  -1880     40     20  A    O  
ATOM   1033  CB  VAL A 129       3.015  16.080   7.322  1.00 45.28      A    C  
ANISOU 1033  CB  VAL A 129     8400   4570   4240  -1390   -460    170  A    C  
ATOM   1034  CG1 VAL A 129       4.156  16.370   8.283  1.00 41.65      A    C  
ANISOU 1034  CG1 VAL A 129     7690   4250   3880  -1300   -210     70  A    C  
ATOM   1035  CG2 VAL A 129       1.703  16.344   8.026  1.00 44.21      A    C  
ANISOU 1035  CG2 VAL A 129     8040   4440   4330  -1220   -740    220  A    C  
ATOM   1036  N   LYS A 130       4.799  15.405   4.868  1.00 50.04      A    N  
ANISOU 1036  N   LYS A 130     9730   4960   4310  -1910     20     20  A    N  
ATOM   1037  CA  LYS A 130       6.079  14.985   4.219  1.00 55.44      A    C  
ANISOU 1037  CA  LYS A 130    10570   5600   4890  -2130    440   -150  A    C  
ATOM   1038  C   LYS A 130       6.480  16.076   3.227  1.00 57.24      A    C  
ANISOU 1038  C   LYS A 130    11280   5620   4850  -2410    530   -150  A    C  
ATOM   1039  O   LYS A 130       7.703  16.422   3.164  1.00 57.36      A    O  
ANISOU 1039  O   LYS A 130    11290   5610   4900  -2540    920   -330  A    O  
ATOM   1040  CB  LYS A 130       5.956  13.632   3.489  1.00 55.78      A    C  
ANISOU 1040  CB  LYS A 130    10750   5610   4830  -2240    540   -190  A    C  
ATOM   1041  N   LYS A 131       5.498  16.639   2.518  1.00 57.94      A    N  
ANISOU 1041  N   LYS A 131    11780   5540   4690  -2480    170     20  A    N  
ATOM   1042  CA  LYS A 131       5.851  17.594   1.441  1.00 67.24      A    C  
ANISOU 1042  CA  LYS A 131    13560   6460   5520  -2790    240     40  A    C  
ATOM   1043  C   LYS A 131       6.287  18.853   2.154  1.00 63.61      A    C  
ANISOU 1043  C   LYS A 131    12920   6030   5220  -2700    290     30  A    C  
ATOM   1044  O   LYS A 131       7.424  19.324   1.880  1.00 72.08      A    O  
ANISOU 1044  O   LYS A 131    14140   7020   6220  -2910    710   -120  A    O  
ATOM   1045  CB  LYS A 131       4.769  17.845   0.371  1.00 70.75      A    C  
ANISOU 1045  CB  LYS A 131    14600   6660   5630  -2910   -200    230  A    C  
ATOM   1046  CG  LYS A 131       5.292  18.327  -0.998  1.00 70.78      A    C  
ANISOU 1046  CG  LYS A 131    15410   6340   5140  -3310    -20    220  A    C  
ATOM   1047  N   SER A 132       5.435  19.365   3.029  1.00 61.15      A    N  
ANISOU 1047  N   SER A 132    12300   5810   5120  -2430    -90    160  A    N  
ATOM   1048  CA  SER A 132       5.757  20.584   3.806  1.00 57.52      A    C  
ANISOU 1048  CA  SER A 132    11630   5390   4830  -2330    -70    150  A    C  
ATOM   1049  C   SER A 132       7.163  20.447   4.394  1.00 58.57      A    C  
ANISOU 1049  C   SER A 132    11440   5670   5150  -2350    420    -70  A    C  
ATOM   1050  O   SER A 132       7.902  21.422   4.350  1.00 62.27      A    O  
ANISOU 1050  O   SER A 132    12000   6060   5600  -2470    630   -160  A    O  
ATOM   1051  CB  SER A 132       4.750  20.817   4.842  1.00 56.92      A    C  
ANISOU 1051  CB  SER A 132    11140   5440   5040  -2030   -430    250  A    C  
ATOM   1052  OG  SER A 132       3.474  20.953   4.262  1.00 56.66      A    O  
ANISOU 1052  OG  SER A 132    11360   5240   4930  -2010   -900    410  A    O  
ATOM   1053  N   LEU A 133       7.558  19.279   4.917  1.00 60.33      A    N  
ANISOU 1053  N   LEU A 133    11290   6070   5560  -2230    590   -200  A    N  
ATOM   1054  CA  LEU A 133       8.879  19.188   5.593  1.00 59.12      A    C  
ANISOU 1054  CA  LEU A 133    10760   6030   5670  -2190    950   -440  A    C  
ATOM   1055  C   LEU A 133      10.003  19.326   4.565  1.00 63.19      A    C  
ANISOU 1055  C   LEU A 133    11590   6360   6060  -2540   1410   -650  A    C  
ATOM   1056  O   LEU A 133      10.902  20.161   4.821  1.00 62.98      A    O  
ANISOU 1056  O   LEU A 133    11450   6310   6170  -2600   1650   -810  A    O  
ATOM   1057  CB  LEU A 133       9.014  17.911   6.420  1.00 56.69      A    C  
ANISOU 1057  CB  LEU A 133    10020   5920   5600  -1970    960   -510  A    C  
ATOM   1058  CG  LEU A 133       8.127  17.842   7.664  1.00 54.84      A    C  
ANISOU 1058  CG  LEU A 133     9460   5850   5520  -1650    630   -370  A    C  
ATOM   1059  CD1 LEU A 133       8.204  16.464   8.286  1.00 49.26      A    C  
ANISOU 1059  CD1 LEU A 133     8480   5270   4970  -1480    640   -420  A    C  
ATOM   1060  CD2 LEU A 133       8.516  18.914   8.678  1.00 56.19      A    C  
ANISOU 1060  CD2 LEU A 133     9370   6100   5870  -1520    600   -420  A    C  
ATOM   1061  N   LYS A 134       9.983  18.570   3.456  1.00 70.08      A    N  
ANISOU 1061  N   LYS A 134    12840   7100   6690  -2780   1560   -670  A    N  
ATOM   1062  CA  LYS A 134      11.054  18.682   2.416  1.00 75.32      A    C  
ANISOU 1062  CA  LYS A 134    13860   7540   7220  -3170   2080   -900  A    C  
ATOM   1063  C   LYS A 134      11.170  20.146   2.012  1.00 73.13      A    C  
ANISOU 1063  C   LYS A 134    13980   7070   6730  -3360   2140   -860  A    C  
ATOM   1064  O   LYS A 134      12.297  20.659   2.030  1.00 72.10      A    O  
ANISOU 1064  O   LYS A 134    13770   6860   6760  -3520   2570  -1120  A    O  
ATOM   1065  CB  LYS A 134      10.825  17.840   1.159  1.00 84.17      A    C  
ANISOU 1065  CB  LYS A 134    15480   8500   8000  -3440   2210   -900  A    C  
ATOM   1066  CG  LYS A 134      11.333  16.403   1.234  1.00 91.94      A    C  
ANISOU 1066  CG  LYS A 134    16140   9580   9220  -3410   2450  -1100  A    C  
ATOM   1067  CD  LYS A 134      12.793  16.235   1.640  1.00100.58      A    C  
ANISOU 1067  CD  LYS A 134    16790  10690  10740  -3440   2930  -1480  A    C  
ATOM   1068  CE  LYS A 134      13.711  16.041   0.449  1.00115.46      A    C  
ANISOU 1068  CE  LYS A 134    19040  12310  12520  -3890   3540  -1780  A    C  
ATOM   1069  NZ  LYS A 134      15.038  15.519   0.855  1.00121.63      A    N1+
ANISOU 1069  NZ  LYS A 134    19270  13100  13840  -3880   3960  -2200  A    N1+
ATOM   1070  N   ASN A 135      10.016  20.759   1.726  1.00 73.27      A    N  
ANISOU 1070  N   ASN A 135    14380   7000   6460  -3330   1690   -560  A    N  
ATOM   1071  CA  ASN A 135       9.818  22.157   1.257  1.00 75.08      A    C  
ANISOU 1071  CA  ASN A 135    15110   6990   6430  -3490   1590   -430  A    C  
ATOM   1072  C   ASN A 135      10.435  23.165   2.230  1.00 77.27      A    C  
ANISOU 1072  C   ASN A 135    14970   7370   7020  -3360   1710   -540  A    C  
ATOM   1073  O   ASN A 135      10.381  24.359   1.905  1.00 79.77      A    O  
ANISOU 1073  O   ASN A 135    15670   7480   7150  -3490   1680   -450  A    O  
ATOM   1074  CB  ASN A 135       8.327  22.491   1.119  1.00 75.90      A    C  
ANISOU 1074  CB  ASN A 135    15470   7030   6340  -3330    930   -100  A    C  
ATOM   1075  CG  ASN A 135       7.716  22.219  -0.245  1.00 79.74      A    C  
ANISOU 1075  CG  ASN A 135    16720   7240   6340  -3580    750     40  A    C  
ATOM   1076  ND2 ASN A 135       8.166  21.187  -0.948  1.00 75.04      A    N  
ANISOU 1076  ND2 ASN A 135    16320   6610   5590  -3800   1070    -90  A    N  
ATOM   1077  OD1 ASN A 135       6.801  22.933  -0.645  1.00 82.66      A    O  
ANISOU 1077  OD1 ASN A 135    17500   7410   6500  -3560    270    270  A    O  
ATOM   1078  N   VAL A 136      10.899  22.739   3.413  1.00 75.58      A    N  
ANISOU 1078  N   VAL A 136    14040   7440   7240  -3090   1770   -690  A    N  
ATOM   1079  CA  VAL A 136      11.573  23.635   4.398  1.00 69.84      A    C  
ANISOU 1079  CA  VAL A 136    12890   6810   6840  -2960   1880   -830  A    C  
ATOM   1080  C   VAL A 136      12.802  22.944   5.001  1.00 68.22      A    C  
ANISOU 1080  C   VAL A 136    12140   6750   7040  -2900   2240  -1170  A    C  
ATOM   1081  O   VAL A 136      13.298  23.420   6.043  1.00 66.21      A    O  
ANISOU 1081  O   VAL A 136    11410   6630   7110  -2710   2230  -1300  A    O  
ATOM   1082  CB  VAL A 136      10.575  24.101   5.468  1.00 69.71      A    C  
ANISOU 1082  CB  VAL A 136    12560   6970   6960  -2610   1380   -600  A    C  
ATOM   1083  CG1 VAL A 136       9.388  24.816   4.845  1.00 70.64      A    C  
ANISOU 1083  CG1 VAL A 136    13170   6900   6770  -2650   1000   -310  A    C  
ATOM   1084  CG2 VAL A 136      10.102  22.949   6.342  1.00 68.34      A    C  
ANISOU 1084  CG2 VAL A 136    11930   7050   6990  -2300   1150   -560  A    C  
ATOM   1085  N   CYS A 137      13.321  21.910   4.337  1.00 68.54      A    N  
ANISOU 1085  N   CYS A 137    12250   6720   7070  -3070   2540  -1350  A    N  
ATOM   1086  CA  CYS A 137      14.673  21.341   4.567  1.00 73.91      A    C  
ANISOU 1086  CA  CYS A 137    12500   7420   8160  -3120   2970  -1750  A    C  
ATOM   1087  C   CYS A 137      14.707  20.477   5.824  1.00 71.53      A    C  
ANISOU 1087  C   CYS A 137    11560   7390   8230  -2710   2690  -1790  A    C  
ATOM   1088  O   CYS A 137      15.761  20.417   6.455  1.00 77.35      A    O  
ANISOU 1088  O   CYS A 137    11830   8160   9400  -2620   2850  -2100  A    O  
ATOM   1089  CB  CYS A 137      15.741  22.415   4.731  1.00 82.15      A    C  
ANISOU 1089  CB  CYS A 137    13410   8360   9440  -3260   3330  -2040  A    C  
ATOM   1090  SG  CYS A 137      16.032  23.385   3.230  1.00 94.71      A    S  
ANISOU 1090  SG  CYS A 137    15800   9560  10620  -3820   3830  -2100  A    S  
ATOM   1091  N   LEU A 138      13.611  19.832   6.189  1.00 67.22      A    N  
ANISOU 1091  N   LEU A 138    11000   6990   7550  -2470   2270  -1490  A    N  
ATOM   1092  CA  LEU A 138      13.650  18.763   7.204  1.00 67.91      A    C  
ANISOU 1092  CA  LEU A 138    10620   7270   7920  -2140   2060  -1520  A    C  
ATOM   1093  C   LEU A 138      13.012  17.593   6.505  1.00 71.15      A    C  
ANISOU 1093  C   LEU A 138    11260   7660   8120  -2200   2020  -1400  A    C  
ATOM   1094  O   LEU A 138      12.513  17.832   5.398  1.00 70.84      A    O  
ANISOU 1094  O   LEU A 138    11720   7470   7720  -2470   2090  -1280  A    O  
ATOM   1095  CB  LEU A 138      12.855  19.171   8.444  1.00 63.66      A    C  
ANISOU 1095  CB  LEU A 138     9860   6920   7400  -1820   1620  -1300  A    C  
ATOM   1096  CG  LEU A 138      13.154  20.575   8.965  1.00 62.86      A    C  
ANISOU 1096  CG  LEU A 138     9670   6830   7390  -1800   1610  -1350  A    C  
ATOM   1097  CD1 LEU A 138      12.042  21.051   9.870  1.00 57.60      A    C  
ANISOU 1097  CD1 LEU A 138     8950   6290   6640  -1570   1210  -1070  A    C  
ATOM   1098  CD2 LEU A 138      14.490  20.632   9.676  1.00 62.49      A    C  
ANISOU 1098  CD2 LEU A 138     9180   6810   7760  -1710   1770  -1690  A    C  
ATOM   1099  N   ASP A 139      12.991  16.422   7.130  1.00 77.12      A    N  
ANISOU 1099  N   ASP A 139    11710   8530   9060  -1970   1890  -1420  A    N  
ATOM   1100  CA  ASP A 139      12.322  15.234   6.540  1.00 80.43      A    C  
ANISOU 1100  CA  ASP A 139    12320   8940   9300  -2010   1850  -1300  A    C  
ATOM   1101  C   ASP A 139      11.848  14.314   7.660  1.00 71.81      A    C  
ANISOU 1101  C   ASP A 139    10920   8010   8360  -1660   1540  -1180  A    C  
ATOM   1102  O   ASP A 139      12.642  14.086   8.588  1.00 66.62      A    O  
ANISOU 1102  O   ASP A 139     9890   7410   8020  -1460   1510  -1350  A    O  
ATOM   1103  CB  ASP A 139      13.224  14.526   5.521  1.00 94.98      A    C  
ANISOU 1103  CB  ASP A 139    14260  10620  11210  -2280   2280  -1570  A    C  
ATOM   1104  CG  ASP A 139      14.477  13.903   6.115  1.00103.82      A    C  
ANISOU 1104  CG  ASP A 139    14880  11740  12830  -2150   2460  -1910  A    C  
ATOM   1105  OD1 ASP A 139      15.037  14.486   7.100  1.00101.89      A    O  
ANISOU 1105  OD1 ASP A 139    14280  11560  12870  -1950   2350  -2020  A    O  
ATOM   1106  OD2 ASP A 139      14.872  12.833   5.600  1.00103.59      A    O1-
ANISOU 1106  OD2 ASP A 139    14820  11620  12920  -2240   2670  -2080  A    O1-
ATOM   1107  N   TYR A 140      10.606  13.823   7.518  1.00 69.13      A    N  
ANISOU 1107  N   TYR A 140    10770   7710   7790  -1620   1310   -930  A    N  
ATOM   1108  CA  TYR A 140       9.909  12.836   8.385  1.00 71.61      A    C  
ANISOU 1108  CA  TYR A 140    10910   8140   8160  -1360   1070   -800  A    C  
ATOM   1109  C   TYR A 140      10.853  11.748   8.890  1.00 75.16      A    C  
ANISOU 1109  C   TYR A 140    11080   8590   8890  -1220   1170   -990  A    C  
ATOM   1110  O   TYR A 140      10.479  11.081   9.900  1.00 83.15      A    O  
ANISOU 1110  O   TYR A 140    11950   9680   9970   -960    950   -890  A    O  
ATOM   1111  CB  TYR A 140       8.766  12.121   7.655  1.00 70.28      A    C  
ANISOU 1111  CB  TYR A 140    11000   7940   7760  -1450    980   -630  A    C  
ATOM   1112  CG  TYR A 140       7.386  12.398   8.202  1.00 69.94      A    C  
ANISOU 1112  CG  TYR A 140    10980   7960   7630  -1310    660   -390  A    C  
ATOM   1113  CD1 TYR A 140       7.124  12.390   9.566  1.00 67.37      A    C  
ANISOU 1113  CD1 TYR A 140    10400   7740   7450  -1060    510   -340  A    C  
ATOM   1114  CD2 TYR A 140       6.331  12.683   7.357  1.00 72.22      A    C  
ANISOU 1114  CD2 TYR A 140    11550   8180   7710  -1450    510   -250  A    C  
ATOM   1115  CE1 TYR A 140       5.866  12.674  10.068  1.00 61.80      A    C  
ANISOU 1115  CE1 TYR A 140     9700   7070   6710   -970    290   -180  A    C  
ATOM   1116  CE2 TYR A 140       5.055  12.930   7.842  1.00 69.45      A    C  
ANISOU 1116  CE2 TYR A 140    11150   7850   7380  -1330    220   -100  A    C  
ATOM   1117  CZ  TYR A 140       4.818  12.928   9.205  1.00 66.73      A    C  
ANISOU 1117  CZ  TYR A 140    10520   7620   7210  -1100    150    -80  A    C  
ATOM   1118  OH  TYR A 140       3.559  13.209   9.667  1.00 70.06      A    O  
ANISOU 1118  OH  TYR A 140    10880   8040   7700  -1010    -60     20  A    O  
ATOM   1119  N   LYS A 141      11.964  11.533   8.181  1.00 75.47      A    N  
ANISOU 1119  N   LYS A 141    11070   8520   9090  -1380   1480  -1260  A    N  
ATOM   1120  CA  LYS A 141      13.034  10.571   8.547  1.00 76.68      A    C  
ANISOU 1120  CA  LYS A 141    10910   8620   9610  -1260   1570  -1510  A    C  
ATOM   1121  C   LYS A 141      13.474  10.798   9.996  1.00 72.00      A    C  
ANISOU 1121  C   LYS A 141     9990   8100   9270   -930   1290  -1550  A    C  
ATOM   1122  O   LYS A 141      13.531   9.816  10.744  1.00 71.04      A    O  
ANISOU 1122  O   LYS A 141     9730   7980   9280   -690   1100  -1540  A    O  
ATOM   1123  CB  LYS A 141      14.232  10.730   7.605  1.00 81.23      A    C  
ANISOU 1123  CB  LYS A 141    11430   9030  10400  -1520   2000  -1870  A    C  
ATOM   1124  N   TYR A 142      13.772  12.040  10.389  1.00 70.04      A    N  
ANISOU 1124  N   TYR A 142     9660   7890   9060   -930   1260  -1590  A    N  
ATOM   1125  CA  TYR A 142      14.429  12.333  11.691  1.00 68.03      A    C  
ANISOU 1125  CA  TYR A 142     9100   7670   9070   -650   1010  -1700  A    C  
ATOM   1126  C   TYR A 142      13.374  12.722  12.728  1.00 59.87      A    C  
ANISOU 1126  C   TYR A 142     8180   6780   7790   -460    690  -1400  A    C  
ATOM   1127  O   TYR A 142      13.749  13.207  13.798  1.00 57.04      A    O  
ANISOU 1127  O   TYR A 142     7670   6460   7550   -270    480  -1440  A    O  
ATOM   1128  CB  TYR A 142      15.538  13.377  11.521  1.00 80.65      A    C  
ANISOU 1128  CB  TYR A 142    10500   9210  10940   -760   1200  -2000  A    C  
ATOM   1129  CG  TYR A 142      16.741  12.873  10.760  1.00 93.02      A    C  
ANISOU 1129  CG  TYR A 142    11850  10610  12880   -910   1540  -2390  A    C  
ATOM   1130  CD1 TYR A 142      17.538  11.870  11.297  1.00101.62      A    C  
ANISOU 1130  CD1 TYR A 142    12620  11610  14380   -680   1400  -2620  A    C  
ATOM   1131  CD2 TYR A 142      17.061  13.354   9.497  1.00 96.31      A    C  
ANISOU 1131  CD2 TYR A 142    12430  10910  13250  -1280   2000  -2550  A    C  
ATOM   1132  CE1 TYR A 142      18.619  11.356  10.604  1.00107.69      A    C  
ANISOU 1132  CE1 TYR A 142    13140  12200  15580   -820   1710  -3020  A    C  
ATOM   1133  CE2 TYR A 142      18.146  12.855   8.793  1.00103.68      A    C  
ANISOU 1133  CE2 TYR A 142    13170  11660  14560  -1460   2380  -2950  A    C  
ATOM   1134  CZ  TYR A 142      18.925  11.854   9.352  1.00109.36      A    C  
ANISOU 1134  CZ  TYR A 142    13490  12310  15760  -1220   2240  -3200  A    C  
ATOM   1135  OH  TYR A 142      20.007  11.343   8.703  1.00118.66      A    O  
ANISOU 1135  OH  TYR A 142    14410  13280  17400  -1370   2610  -3650  A    O  
ATOM   1136  N   PHE A 143      12.097  12.462  12.451  1.00 52.03      A    N  
ANISOU 1136  N   PHE A 143     7450   5830   6480   -520    650  -1120  A    N  
ATOM   1137  CA  PHE A 143      11.010  12.748  13.409  1.00 46.16      A    C  
ANISOU 1137  CA  PHE A 143     6800   5190   5550   -380    410   -880  A    C  
ATOM   1138  C   PHE A 143      10.541  11.462  14.082  1.00 44.89      A    C  
ANISOU 1138  C   PHE A 143     6700   5010   5340   -200    270   -770  A    C  
ATOM   1139  O   PHE A 143      10.368  10.399  13.424  1.00 45.18      A    O  
ANISOU 1139  O   PHE A 143     6810   5000   5360   -260    370   -760  A    O  
ATOM   1140  CB  PHE A 143       9.827  13.429  12.734  1.00 44.96      A    C  
ANISOU 1140  CB  PHE A 143     6870   5060   5150   -550    440   -680  A    C  
ATOM   1141  CG  PHE A 143      10.063  14.848  12.266  1.00 45.70      A    C  
ANISOU 1141  CG  PHE A 143     6990   5150   5230   -700    520   -730  A    C  
ATOM   1142  CD1 PHE A 143      10.865  15.113  11.180  1.00 45.29      A    C  
ANISOU 1142  CD1 PHE A 143     7000   5000   5210   -930    770   -890  A    C  
ATOM   1143  CD2 PHE A 143       9.448  15.918  12.906  1.00 44.18      A    C  
ANISOU 1143  CD2 PHE A 143     6790   5010   4980   -650    370   -610  A    C  
ATOM   1144  CE1 PHE A 143      11.054  16.417  10.737  1.00 48.46      A    C  
ANISOU 1144  CE1 PHE A 143     7490   5360   5560  -1090    870   -920  A    C  
ATOM   1145  CE2 PHE A 143       9.642  17.218  12.462  1.00 45.30      A    C  
ANISOU 1145  CE2 PHE A 143     6990   5120   5100   -790    440   -640  A    C  
ATOM   1146  CZ  PHE A 143      10.446  17.470  11.374  1.00 43.95      A    C  
ANISOU 1146  CZ  PHE A 143     6910   4850   4930  -1010    680   -790  A    C  
ATOM   1147  N   GLY A 144      10.293  11.588  15.381  1.00 41.05      A    N  
ANISOU 1147  N   GLY A 144     6220   4560   4810    -10     60   -690  A    N  
ATOM   1148  CA  GLY A 144       9.580  10.594  16.187  1.00 39.93      A    C  
ANISOU 1148  CA  GLY A 144     6240   4390   4540    130    -50   -540  A    C  
ATOM   1149  C   GLY A 144       8.123  10.929  16.325  1.00 37.44      A    C  
ANISOU 1149  C   GLY A 144     6080   4120   4030     50    -20   -340  A    C  
ATOM   1150  O   GLY A 144       7.805  12.115  16.309  1.00 38.88      A    O  
ANISOU 1150  O   GLY A 144     6220   4370   4180    -20    -20   -320  A    O  
ATOM   1151  N   ASN A 145       7.308   9.899  16.556  1.00 38.07      A    N  
ANISOU 1151  N   ASN A 145     6310   4150   4000     70      0   -230  A    N  
ATOM   1152  CA  ASN A 145       5.840   9.969  16.725  1.00 37.30      A    C  
ANISOU 1152  CA  ASN A 145     6330   4060   3790    -10     60   -100  A    C  
ATOM   1153  C   ASN A 145       5.494   9.499  18.112  1.00 40.62      A    C  
ANISOU 1153  C   ASN A 145     6930   4410   4100    110     30    -40  A    C  
ATOM   1154  O   ASN A 145       6.241   8.695  18.662  1.00 47.96      A    O  
ANISOU 1154  O   ASN A 145     7960   5260   5000    250    -60    -70  A    O  
ATOM   1155  CB  ASN A 145       5.102   9.179  15.665  1.00 36.10      A    C  
ANISOU 1155  CB  ASN A 145     6220   3870   3630   -150    180    -60  A    C  
ATOM   1156  CG  ASN A 145       5.557   9.648  14.298  1.00 40.72      A    C  
ANISOU 1156  CG  ASN A 145     6730   4490   4260   -290    210   -120  A    C  
ATOM   1157  ND2 ASN A 145       6.067   8.670  13.555  1.00 41.64      A    N  
ANISOU 1157  ND2 ASN A 145     6860   4560   4400   -330    300   -180  A    N  
ATOM   1158  OD1 ASN A 145       5.501  10.876  13.966  1.00 35.68      A    O  
ANISOU 1158  OD1 ASN A 145     6040   3890   3620   -370    180   -120  A    O  
ATOM   1159  N   ASP A 146       4.420  10.049  18.641  1.00 38.45      A    N  
ANISOU 1159  N   ASP A 146     6710   4140   3770     50    100     10  A    N  
ATOM   1160  CA  ASP A 146       3.904   9.660  19.944  1.00 41.07      A    C  
ANISOU 1160  CA  ASP A 146     7280   4370   3960    100    150     50  A    C  
ATOM   1161  C   ASP A 146       3.243   8.273  19.873  1.00 43.47      A    C  
ANISOU 1161  C   ASP A 146     7760   4550   4210     60    290    100  A    C  
ATOM   1162  O   ASP A 146       2.010   8.188  19.670  1.00 47.12      A    O  
ANISOU 1162  O   ASP A 146     8200   4980   4730    -80    470    100  A    O  
ATOM   1163  CB  ASP A 146       2.941  10.692  20.492  1.00 38.91      A    C  
ANISOU 1163  CB  ASP A 146     6980   4110   3700     10    240     40  A    C  
ATOM   1164  CG  ASP A 146       2.673  10.375  21.952  1.00 40.80      A    C  
ANISOU 1164  CG  ASP A 146     7530   4220   3750     40    330     50  A    C  
ATOM   1165  OD1 ASP A 146       3.200   9.310  22.415  1.00 43.72      A    O  
ANISOU 1165  OD1 ASP A 146     8170   4490   3950    140    270    100  A    O  
ATOM   1166  OD2 ASP A 146       1.834  11.043  22.550  1.00 37.88      A    O1-
ANISOU 1166  OD2 ASP A 146     7180   3820   3390    -60    470     10  A    O1-
ATOM   1167  N   THR A 147       4.005   7.214  20.095  1.00 46.78      A    N  
ANISOU 1167  N   THR A 147     8340   4890   4550    180    210    120  A    N  
ATOM   1168  CA  THR A 147       3.480   5.799  20.018  1.00 48.90      A    C  
ANISOU 1168  CA  THR A 147     8800   5020   4760    150    350    160  A    C  
ATOM   1169  C   THR A 147       2.570   5.468  21.226  1.00 48.34      A    C  
ANISOU 1169  C   THR A 147     9070   4790   4500    100    530    210  A    C  
ATOM   1170  O   THR A 147       1.806   4.556  21.132  1.00 52.65      A    O  
ANISOU 1170  O   THR A 147     9740   5230   5040     10    730    220  A    O  
ATOM   1171  CB  THR A 147       4.627   4.783  19.926  1.00 47.83      A    C  
ANISOU 1171  CB  THR A 147     8740   4800   4630    300    190    160  A    C  
ATOM   1172  CG2 THR A 147       5.549   4.956  18.740  1.00 45.43      A    C  
ANISOU 1172  CG2 THR A 147     8120   4610   4540    320    110     70  A    C  
ATOM   1173  OG1 THR A 147       5.357   4.983  21.129  1.00 51.30      A    O  
ANISOU 1173  OG1 THR A 147     9390   5160   4940    470    -20    170  A    O  
ATOM   1174  N   SER A 148       2.545   6.224  22.311  1.00 51.06      A    N  
ANISOU 1174  N   SER A 148     9580   5110   4710    110    510    210  A    N  
ATOM   1175  CA  SER A 148       1.510   6.031  23.353  1.00 51.02      A    C  
ANISOU 1175  CA  SER A 148     9910   4930   4540    -10    790    210  A    C  
ATOM   1176  C   SER A 148       0.086   6.289  22.822  1.00 48.67      A    C  
ANISOU 1176  C   SER A 148     9370   4650   4470   -220   1090    120  A    C  
ATOM   1177  O   SER A 148      -0.846   6.009  23.569  1.00 54.94      A    O  
ANISOU 1177  O   SER A 148    10400   5280   5200   -360   1400     70  A    O  
ATOM   1178  CB  SER A 148       1.795   6.851  24.589  1.00 56.53      A    C  
ANISOU 1178  CB  SER A 148    10850   5590   5040     20    710    200  A    C  
ATOM   1179  OG  SER A 148       1.769   8.264  24.316  1.00 61.60      A    O  
ANISOU 1179  OG  SER A 148    11130   6420   5860     -0    660    130  A    O  
ATOM   1180  N   VAL A 149      -0.124   6.855  21.636  1.00 47.59      A    N  
ANISOU 1180  N   VAL A 149     8810   4680   4600   -260   1020     80  A    N  
ATOM   1181  CA  VAL A 149      -1.482   7.070  21.045  1.00 47.32      A    C  
ANISOU 1181  CA  VAL A 149     8520   4630   4840   -430   1210    -30  A    C  
ATOM   1182  C   VAL A 149      -1.455   6.450  19.654  1.00 49.49      A    C  
ANISOU 1182  C   VAL A 149     8590   4960   5240   -440   1110    -10  A    C  
ATOM   1183  O   VAL A 149      -1.115   7.161  18.669  1.00 48.88      A    O  
ANISOU 1183  O   VAL A 149     8270   5030   5280   -420    900     -0  A    O  
ATOM   1184  CB  VAL A 149      -1.853   8.563  20.970  1.00 50.72      A    C  
ANISOU 1184  CB  VAL A 149     8670   5150   5460   -470   1140   -100  A    C  
ATOM   1185  CG1 VAL A 149      -3.251   8.771  20.369  1.00 50.03      A    C  
ANISOU 1185  CG1 VAL A 149     8290   5000   5720   -620   1270   -240  A    C  
ATOM   1186  CG2 VAL A 149      -1.707   9.217  22.344  1.00 52.41      A    C  
ANISOU 1186  CG2 VAL A 149     9090   5310   5510   -460   1240   -120  A    C  
ATOM   1187  N   HIS A 150      -1.768   5.154  19.586  1.00 48.73      A    N  
ANISOU 1187  N   HIS A 150     8650   4750   5110   -480   1270    -10  A    N  
ATOM   1188  CA  HIS A 150      -1.458   4.304  18.425  1.00 47.60      A    C  
ANISOU 1188  CA  HIS A 150     8430   4650   5010   -460   1180     20  A    C  
ATOM   1189  C   HIS A 150      -2.178   4.927  17.243  1.00 44.60      A    C  
ANISOU 1189  C   HIS A 150     7720   4350   4880   -570   1090    -50  A    C  
ATOM   1190  O   HIS A 150      -3.340   5.386  17.411  1.00 48.65      A    O  
ANISOU 1190  O   HIS A 150     8090   4800   5600   -670   1190   -160  A    O  
ATOM   1191  CB  HIS A 150      -1.832   2.798  18.640  1.00 48.16      A    C  
ANISOU 1191  CB  HIS A 150     8730   4550   5020   -510   1410     30  A    C  
ATOM   1192  CG  HIS A 150      -1.891   2.001  17.372  1.00 44.19      A    C  
ANISOU 1192  CG  HIS A 150     8090   4080   4630   -550   1380     10  A    C  
ATOM   1193  CD2 HIS A 150      -0.926   1.403  16.645  1.00 46.67      A    C  
ANISOU 1193  CD2 HIS A 150     8410   4440   4880   -470   1250     60  A    C  
ATOM   1194  ND1 HIS A 150      -3.066   1.863  16.670  1.00 46.89      A    N  
ANISOU 1194  ND1 HIS A 150     8230   4390   5200   -700   1470   -110  A    N  
ATOM   1195  CE1 HIS A 150      -2.826   1.213  15.546  1.00 49.42      A    C  
ANISOU 1195  CE1 HIS A 150     8480   4750   5550   -720   1390   -100  A    C  
ATOM   1196  NE2 HIS A 150      -1.521   0.844  15.530  1.00 46.62      A    N  
ANISOU 1196  NE2 HIS A 150     8260   4440   5010   -590   1290     -0  A    N  
ATOM   1197  N   CYS A 151      -1.489   4.917  16.116  1.00 41.47      A    N  
ANISOU 1197  N   CYS A 151     7230   4060   4470   -540    900    -10  A    N  
ATOM   1198  CA  CYS A 151      -1.946   5.530  14.871  1.00 42.93      A    C  
ANISOU 1198  CA  CYS A 151     7210   4300   4800   -630    730    -50  A    C  
ATOM   1199  C   CYS A 151      -1.240   4.818  13.733  1.00 44.77      A    C  
ANISOU 1199  C   CYS A 151     7500   4570   4940   -650    670    -20  A    C  
ATOM   1200  O   CYS A 151      -0.016   4.915  13.639  1.00 44.03      A    O  
ANISOU 1200  O   CYS A 151     7460   4550   4730   -580    610     20  A    O  
ATOM   1201  CB  CYS A 151      -1.641   7.018  14.873  1.00 45.76      A    C  
ANISOU 1201  CB  CYS A 151     7460   4750   5180   -600    550    -30  A    C  
ATOM   1202  SG  CYS A 151      -2.291   7.806  13.390  1.00 46.03      A    S  
ANISOU 1202  SG  CYS A 151     7350   4780   5360   -710    290    -70  A    S  
ATOM   1203  N   ARG A 152      -1.978   4.058  12.941  1.00 49.72      A    N  
ANISOU 1203  N   ARG A 152     8100   5140   5650   -760    690    -80  A    N  
ATOM   1204  CA  ARG A 152      -1.362   3.216  11.893  1.00 51.77      A    C  
ANISOU 1204  CA  ARG A 152     8440   5410   5820   -810    690    -70  A    C  
ATOM   1205  C   ARG A 152      -0.577   4.114  10.917  1.00 51.06      A    C  
ANISOU 1205  C   ARG A 152     8360   5410   5630   -850    510    -50  A    C  
ATOM   1206  O   ARG A 152       0.395   3.623  10.336  1.00 52.52      A    O  
ANISOU 1206  O   ARG A 152     8630   5610   5720   -870    570    -60  A    O  
ATOM   1207  CB  ARG A 152      -2.462   2.414  11.212  1.00 57.58      A    C  
ANISOU 1207  CB  ARG A 152     9140   6060   6680   -930    720   -150  A    C  
ATOM   1208  CG  ARG A 152      -3.548   3.284  10.578  1.00 64.49      A    C  
ANISOU 1208  CG  ARG A 152     9880   6900   7720  -1010    490   -220  A    C  
ATOM   1209  CD  ARG A 152      -4.782   2.454  10.242  1.00 66.56      A    C  
ANISOU 1209  CD  ARG A 152    10050   7040   8200  -1110    530   -350  A    C  
ATOM   1210  NE  ARG A 152      -4.312   1.300   9.491  1.00 66.16      A    N  
ANISOU 1210  NE  ARG A 152    10140   6990   8010  -1170    610   -340  A    N  
ATOM   1211  CZ  ARG A 152      -4.489   0.014   9.810  1.00 71.03      A    C  
ANISOU 1211  CZ  ARG A 152    10790   7540   8660  -1180    870   -380  A    C  
ATOM   1212  NH1 ARG A 152      -5.182  -0.347  10.880  1.00 72.66      A    N1+
ANISOU 1212  NH1 ARG A 152    10940   7650   9010  -1160   1090   -440  A    N1+
ATOM   1213  NH2 ARG A 152      -3.970  -0.914   9.027  1.00 68.21      A    N  
ANISOU 1213  NH2 ARG A 152    10560   7180   8180  -1230    920   -370  A    N  
ATOM   1214  N   TYR A 153      -0.925   5.394  10.743  1.00 50.01      A    N  
ANISOU 1214  N   TYR A 153     8170   5300   5540   -880    330    -40  A    N  
ATOM   1215  CA  TYR A 153      -0.238   6.263   9.742  1.00 46.85      A    C  
ANISOU 1215  CA  TYR A 153     7850   4940   5010   -960    190    -20  A    C  
ATOM   1216  C   TYR A 153       0.995   6.951  10.319  1.00 43.38      A    C  
ANISOU 1216  C   TYR A 153     7400   4580   4510   -870    240      0  A    C  
ATOM   1217  O   TYR A 153       1.648   7.649   9.532  1.00 48.58      A    O  
ANISOU 1217  O   TYR A 153     8140   5250   5070   -960    190     -0  A    O  
ATOM   1218  CB  TYR A 153      -1.205   7.291   9.167  1.00 47.84      A    C  
ANISOU 1218  CB  TYR A 153     7960   5000   5210  -1030    -80    -10  A    C  
ATOM   1219  CG  TYR A 153      -2.454   6.626   8.674  1.00 50.40      A    C  
ANISOU 1219  CG  TYR A 153     8250   5230   5670  -1100   -180    -80  A    C  
ATOM   1220  CD1 TYR A 153      -2.422   5.780   7.570  1.00 52.14      A    C  
ANISOU 1220  CD1 TYR A 153     8640   5400   5770  -1220   -190   -100  A    C  
ATOM   1221  CD2 TYR A 153      -3.637   6.751   9.375  1.00 53.33      A    C  
ANISOU 1221  CD2 TYR A 153     8410   5530   6320  -1050   -220   -150  A    C  
ATOM   1222  CE1 TYR A 153      -3.552   5.114   7.141  1.00 53.40      A    C  
ANISOU 1222  CE1 TYR A 153     8750   5460   6080  -1280   -300   -180  A    C  
ATOM   1223  CE2 TYR A 153      -4.785   6.113   8.947  1.00 57.18      A    C  
ANISOU 1223  CE2 TYR A 153     8810   5910   7010  -1110   -300   -250  A    C  
ATOM   1224  CZ  TYR A 153      -4.734   5.285   7.837  1.00 57.44      A    C  
ANISOU 1224  CZ  TYR A 153     9010   5910   6910  -1210   -360   -260  A    C  
ATOM   1225  OH  TYR A 153      -5.872   4.642   7.450  1.00 64.78      A    O  
ANISOU 1225  OH  TYR A 153     9830   6720   8060  -1270   -460   -390  A    O  
ATOM   1226  N   LEU A 154       1.301   6.784  11.608  1.00 41.56      A    N  
ANISOU 1226  N   LEU A 154     7090   4380   4320   -720    330     10  A    N  
ATOM   1227  CA  LEU A 154       2.405   7.502  12.302  1.00 39.53      A    C  
ANISOU 1227  CA  LEU A 154     6790   4190   4040   -610    330     10  A    C  
ATOM   1228  C   LEU A 154       3.377   6.489  12.921  1.00 41.72      A    C  
ANISOU 1228  C   LEU A 154     7090   4450   4310   -480    430    -20  A    C  
ATOM   1229  O   LEU A 154       3.839   6.745  14.095  1.00 43.62      A    O  
ANISOU 1229  O   LEU A 154     7320   4700   4550   -330    390    -10  A    O  
ATOM   1230  CB  LEU A 154       1.823   8.470  13.353  1.00 37.02      A    C  
ANISOU 1230  CB  LEU A 154     6400   3890   3780   -530    260     40  A    C  
ATOM   1231  CG  LEU A 154       1.061   9.720  12.863  1.00 35.76      A    C  
ANISOU 1231  CG  LEU A 154     6180   3730   3680   -620    110     50  A    C  
ATOM   1232  CD1 LEU A 154       0.457  10.475  14.034  1.00 36.02      A    C  
ANISOU 1232  CD1 LEU A 154     6110   3760   3820   -550    110     40  A    C  
ATOM   1233  CD2 LEU A 154       1.904  10.657  12.043  1.00 36.00      A    C  
ANISOU 1233  CD2 LEU A 154     6250   3790   3640   -690     30     50  A    C  
ATOM   1234  N   GLU A 155       3.746   5.427  12.193  1.00 44.67      A    N  
ANISOU 1234  N   GLU A 155     7510   4770   4690   -530    520    -70  A    N  
ATOM   1235  CA  GLU A 155       4.471   4.258  12.812  1.00 48.60      A    C  
ANISOU 1235  CA  GLU A 155     8040   5200   5220   -390    580   -100  A    C  
ATOM   1236  C   GLU A 155       5.701   3.819  12.000  1.00 49.73      A    C  
ANISOU 1236  C   GLU A 155     8120   5320   5460   -420    650   -230  A    C  
ATOM   1237  O   GLU A 155       5.531   3.550  10.839  1.00 43.16      A    O  
ANISOU 1237  O   GLU A 155     7330   4470   4600   -600    760   -270  A    O  
ATOM   1238  CB  GLU A 155       3.694   2.955  12.874  1.00 49.82      A    C  
ANISOU 1238  CB  GLU A 155     8300   5270   5360   -400    680    -60  A    C  
ATOM   1239  CG  GLU A 155       2.202   3.045  12.897  1.00 50.90      A    C  
ANISOU 1239  CG  GLU A 155     8460   5390   5480   -500    710     -0  A    C  
ATOM   1240  CD  GLU A 155       1.642   1.995  13.836  1.00 48.40      A    C  
ANISOU 1240  CD  GLU A 155     8280   4960   5150   -430    830     30  A    C  
ATOM   1241  OE1 GLU A 155       1.605   2.273  15.075  1.00 50.70      A    O  
ANISOU 1241  OE1 GLU A 155     8660   5210   5380   -330    830     80  A    O  
ATOM   1242  OE2 GLU A 155       1.322   0.876  13.356  1.00 54.50      A    O1-
ANISOU 1242  OE2 GLU A 155     9110   5660   5950   -490    950     10  A    O1-
TER   
HETATM 1243  C1  NAG A   1      -5.055  11.424  26.698  1.00 89.22      B    C  
ANISOU 1243  C1  NAG A   1    14180   9360  10350  -1120   2590   -750  B    C  
HETATM 1244  C2  NAG A   1      -5.584  10.209  27.488  1.00100.16      B    C  
ANISOU 1244  C2  NAG A   1    16050  10480  11520  -1300   3030   -810  B    C  
HETATM 1245  N2  NAG A   1      -4.987   8.997  26.922  1.00 99.09      B    N  
ANISOU 1245  N2  NAG A   1    16080  10380  11180  -1170   2830   -620  B    N  
HETATM 1246  C3  NAG A   1      -7.121  10.191  27.455  1.00108.72      B    C  
ANISOU 1246  C3  NAG A   1    16860  11370  13080  -1550   3500  -1110  B    C  
HETATM 1247  O3  NAG A   1      -7.700   9.158  28.263  1.00117.29      B    O  
ANISOU 1247  O3  NAG A   1    18420  12170  13980  -1770   4010  -1210  B    O  
HETATM 1248  C4  NAG A   1      -7.664  11.546  27.918  1.00113.25      B    C  
ANISOU 1248  C4  NAG A   1    17170  11920  13950  -1650   3650  -1320  B    C  
HETATM 1249  O4  NAG A   1      -9.104  11.528  27.884  1.00118.09      B    O  
ANISOU 1249  O4  NAG A   1    17460  12310  15100  -1880   4090  -1660  B    O  
HETATM 1250  C5  NAG A   1      -7.072  12.606  26.977  1.00109.33      B    C  
ANISOU 1250  C5  NAG A   1    16200  11700  13640  -1420   3110  -1210  B    C  
HETATM 1251  O5  NAG A   1      -5.653  12.623  27.215  1.00 99.48      B    O  
ANISOU 1251  O5  NAG A   1    15290  10620  11890  -1240   2770   -940  B    O  
HETATM 1252  C6  NAG A   1      -7.688  14.001  27.074  1.00111.23      B    C  
ANISOU 1252  C6  NAG A   1    16030  11920  14320  -1490   3160  -1420  B    C  
HETATM 1253  O6  NAG A   1      -6.701  14.951  27.477  1.00114.88      B    O  
ANISOU 1253  O6  NAG A   1    16600  12540  14510  -1370   2920  -1290  B    O  
HETATM 1254  C7  NAG A   1      -3.727   8.604  27.215  1.00 96.67      B    C  
ANISOU 1254  C7  NAG A   1    16150  10130  10450   -980   2520   -400  B    C  
HETATM 1255  O7  NAG A   1      -3.006   9.191  28.044  1.00 92.94      B    O  
ANISOU 1255  O7  NAG A   1    15950   9680   9690   -920   2380   -340  B    O  
HETATM 1256  C8  NAG A   1      -3.248   7.408  26.424  1.00 92.68      B    C  
ANISOU 1256  C8  NAG A   1    15680   9660   9880   -860   2330   -260  B    C  
HETATM 1257  C1  NAG A   2      -9.671  11.655  29.192  1.00122.62      B    C  
ANISOU 1257  C1  NAG A   2    18380  12620  15590  -2160   4680  -1890  B    C  
HETATM 1258  C2  NAG A   2     -11.021  12.361  29.136  1.00127.14      B    C  
ANISOU 1258  C2  NAG A   2    18390  13010  16900  -2350   5030  -2310  B    C  
HETATM 1259  N2  NAG A   2     -10.979  13.538  28.262  1.00117.23      B    N  
ANISOU 1259  N2  NAG A   2    16500  11960  16080  -2150   4540  -2300  B    N  
HETATM 1260  C3  NAG A   2     -11.441  12.628  30.596  1.00136.59      B    C  
ANISOU 1260  C3  NAG A   2    20010  13940  17950  -2660   5680  -2540  B    C  
HETATM 1261  O3  NAG A   2     -12.619  13.448  30.730  1.00142.18      B    O  
ANISOU 1261  O3  NAG A   2    20200  14450  19370  -2860   6050  -2980  B    O  
HETATM 1262  C4  NAG A   2     -11.652  11.261  31.266  1.00140.59      B    C  
ANISOU 1262  C4  NAG A   2    21170  14180  18060  -2890   6180  -2560  B    C  
HETATM 1263  O4  NAG A   2     -12.047  11.387  32.654  1.00141.61      B    O  
ANISOU 1263  O4  NAG A   2    21840  14010  17960  -3230   6850  -2780  B    O  
HETATM 1264  C5  NAG A   2     -10.372  10.412  31.124  1.00138.28      B    C  
ANISOU 1264  C5  NAG A   2    21410  14070  17060  -2650   5730  -2110  B    C  
HETATM 1265  O5  NAG A   2      -9.862  10.372  29.778  1.00130.42      B    O  
ANISOU 1265  O5  NAG A   2    19920  13380  16250  -2330   5090  -1890  B    O  
HETATM 1266  C6  NAG A   2     -10.610   8.975  31.572  1.00140.29      B    C  
ANISOU 1266  C6  NAG A   2    22270  14050  16980  -2830   6150  -2100  B    C  
HETATM 1267  O6  NAG A   2     -10.233   8.852  32.944  1.00143.23      B    O  
ANISOU 1267  O6  NAG A   2    23510  14210  16700  -3000   6450  -2040  B    O  
HETATM 1268  C7  NAG A   2     -11.281  13.460  26.954  1.00112.48      B    C  
ANISOU 1268  C7  NAG A   2    15390  11450  15900  -2010   4150  -2290  B    C  
HETATM 1269  O7  NAG A   2     -11.652  12.409  26.444  1.00110.70      B    O  
ANISOU 1269  O7  NAG A   2    15140  11160  15760  -2040   4210  -2310  B    O  
HETATM 1270  C8  NAG A   2     -11.120  14.715  26.132  1.00105.62      B    C  
ANISOU 1270  C8  NAG A   2    14020  10750  15360  -1810   3630  -2250  B    C  
HETATM 1271  C1  NAG A 201       6.681   8.623  12.295  1.00 52.45      C    C  
ANISOU 1271  C1  NAG A 201     8230   5910   5790   -490    410   -280  C    C  
HETATM 1272  C2  NAG A 201       7.747   7.533  12.123  1.00 60.36      C    C  
ANISOU 1272  C2  NAG A 201     9170   6840   6930   -440    510   -420  C    C  
HETATM 1273  N2  NAG A 201       8.835   7.543  13.083  1.00 66.69      C    N  
ANISOU 1273  N2  NAG A 201     9820   7620   7900   -240    420   -530  C    N  
HETATM 1274  C3  NAG A 201       8.372   7.530  10.734  1.00 67.95      C    C  
ANISOU 1274  C3  NAG A 201    10150   7750   7910   -660    710   -560  C    C  
HETATM 1275  O3  NAG A 201       9.394   6.530  10.758  1.00 73.43      C    O  
ANISOU 1275  O3  NAG A 201    10720   8360   8820   -580    810   -730  C    O  
HETATM 1276  C4  NAG A 201       7.275   7.235   9.697  1.00 71.29      C    C  
ANISOU 1276  C4  NAG A 201    10790   8160   8140   -850    760   -450  C    C  
HETATM 1277  O4  NAG A 201       7.742   7.208   8.313  1.00 79.30      C    O  
ANISOU 1277  O4  NAG A 201    11940   9100   9090  -1110    960   -570  C    O  
HETATM 1278  C5  NAG A 201       6.129   8.253   9.903  1.00 69.63      C    C  
ANISOU 1278  C5  NAG A 201    10650   8000   7800   -870    580   -290  C    C  
HETATM 1279  O5  NAG A 201       5.686   8.504  11.302  1.00 63.11      C    O  
ANISOU 1279  O5  NAG A 201     9720   7230   7030   -660    440   -200  C    O  
HETATM 1280  C6  NAG A 201       4.910   7.706   9.190  1.00 64.01      C    C  
ANISOU 1280  C6  NAG A 201    10090   7250   6980   -980    530   -200  C    C  
HETATM 1281  O6  NAG A 201       4.006   8.796   9.337  1.00 72.64      C    O  
ANISOU 1281  O6  NAG A 201    11210   8360   8030   -980    340   -100  C    O  
HETATM 1282  C7  NAG A 201       8.773   6.868  14.234  1.00 77.01      C    C  
ANISOU 1282  C7  NAG A 201    11170   8890   9210    -30    270   -470  C    C  
HETATM 1283  O7  NAG A 201       7.740   6.291  14.658  1.00 78.57      C    O  
ANISOU 1283  O7  NAG A 201    11530   9070   9260    -10    260   -310  C    O  
HETATM 1284  C8  NAG A 201      10.094   6.870  14.952  1.00 79.05      C    C  
ANISOU 1284  C8  NAG A 201    11270   9080   9680    170    110   -630  C    C  
HETATM 1285  C1  NAG A 202       1.892  31.136  37.205  1.00118.12      D    C  
ANISOU 1285  C1  NAG A 202    17670  13880  13330  -1230   1810  -2140  D    C  
HETATM 1286  C2  NAG A 202       2.795  32.371  37.017  1.00118.87      D    C  
ANISOU 1286  C2  NAG A 202    17430  14140  13600  -1100   1540  -2190  D    C  
HETATM 1287  N2  NAG A 202       4.260  32.221  36.915  1.00118.53      D    N  
ANISOU 1287  N2  NAG A 202    17450  14260  13330   -880   1020  -2100  D    N  
HETATM 1288  C3  NAG A 202       2.466  33.215  38.267  1.00124.06      D    C  
ANISOU 1288  C3  NAG A 202    18330  14670  14130  -1330   1850  -2420  D    C  
HETATM 1289  O3  NAG A 202       3.323  34.338  38.479  1.00125.13      D    O  
ANISOU 1289  O3  NAG A 202    18300  14930  14310  -1260   1640  -2520  D    O  
HETATM 1290  C4  NAG A 202       1.029  33.705  38.166  1.00126.50      D    C  
ANISOU 1290  C4  NAG A 202    18360  14820  14890  -1540   2370  -2580  D    C  
HETATM 1291  O4  NAG A 202       0.710  34.604  39.238  1.00128.22      D    O  
ANISOU 1291  O4  NAG A 202    18730  14920  15070  -1760   2710  -2840  D    O  
HETATM 1292  C5  NAG A 202       0.130  32.472  38.179  1.00127.61      D    C  
ANISOU 1292  C5  NAG A 202    18750  14800  14930  -1650   2650  -2540  D    C  
HETATM 1293  O5  NAG A 202       0.527  31.550  37.161  1.00121.07      D    O  
ANISOU 1293  O5  NAG A 202    17800  14100  14100  -1440   2300  -2300  D    O  
HETATM 1294  C6  NAG A 202      -1.331  32.825  37.935  1.00127.33      D    C  
ANISOU 1294  C6  NAG A 202    18330  14580  15460  -1840   3130  -2740  D    C  
HETATM 1295  O6  NAG A 202      -2.100  32.355  39.042  1.00133.66      D    O  
ANISOU 1295  O6  NAG A 202    19630  15140  16020  -2150   3660  -2930  D    O  
HETATM 1296  C7  NAG A 202       4.998  31.188  36.465  1.00115.78      D    C  
ANISOU 1296  C7  NAG A 202    17200  13980  12810   -690    670  -1940  D    C  
HETATM 1297  O7  NAG A 202       4.513  30.190  35.980  1.00120.65      D    O  
ANISOU 1297  O7  NAG A 202    17870  14550  13420   -680    740  -1810  D    O  
HETATM 1298  C8  NAG A 202       6.500  31.274  36.629  1.00110.37      D    C  
ANISOU 1298  C8  NAG A 202    16550  13410  11980   -490    180  -1960  D    C  
HETATM 1299  C1  PAM A 203       5.110  19.918  26.991  1.00 76.74      E    C  
ANISOU 1299  C1  PAM A 203    11680   9190   8290    130   -150   -490  E    C  
HETATM 1300  O1  PAM A 203       5.210  20.079  28.248  1.00 82.22      E    O  
ANISOU 1300  O1  PAM A 203    12670   9810   8760    140   -170   -540  E    O  
HETATM 1301  C2  PAM A 203       3.917  20.515  26.261  1.00 73.94      E    C  
ANISOU 1301  C2  PAM A 203    11070   8840   8190    -10     80   -480  E    C  
HETATM 1302  O2  PAM A 203       5.924  19.288  26.328  1.00 76.78      E    O  
ANISOU 1302  O2  PAM A 203    11610   9230   8330    240   -330   -460  E    O  
HETATM 1303  C3  PAM A 203       4.061  20.949  24.827  1.00 71.01      E    C  
ANISOU 1303  C3  PAM A 203    10370   8550   8070    -20      0   -450  E    C  
HETATM 1304  C4  PAM A 203       5.480  20.855  24.269  1.00 70.56      E    C  
ANISOU 1304  C4  PAM A 203    10220   8580   8010     90   -210   -470  E    C  
HETATM 1305  C5  PAM A 203       5.989  22.078  23.524  1.00 66.67      E    C  
ANISOU 1305  C5  PAM A 203     9460   8160   7710     60   -250   -520  E    C  
HETATM 1306  C6  PAM A 203       4.942  22.941  22.878  1.00 62.58      E    C  
ANISOU 1306  C6  PAM A 203     8810   7610   7370    -60   -150   -480  E    C  
HETATM 1307  C7  PAM A 203       5.526  24.135  22.155  1.00 58.38      E    C  
ANISOU 1307  C7  PAM A 203     8100   7110   6980   -100   -190   -530  E    C  
HETATM 1308  C8  PAM A 203       4.550  24.770  21.252  1.00 59.84      E    C  
ANISOU 1308  C8  PAM A 203     8210   7210   7320   -200   -170   -460  E    C  
HETATM 1309  C9  PAM A 203       5.116  25.132  19.924  1.00 57.25      E    C  
ANISOU 1309  C9  PAM A 203     7870   6860   7020   -260   -220   -420  E    C  
HETATM 1310  C10 PAM A 203       4.530  25.902  19.066  1.00 57.50      E    C  
ANISOU 1310  C10 PAM A 203     7900   6790   7160   -340   -270   -360  E    C  
HETATM 1311  C11 PAM A 203       3.492  26.901  19.415  1.00 55.59      E    C  
ANISOU 1311  C11 PAM A 203     7550   6460   7110   -360   -310   -370  E    C  
HETATM 1312  C12 PAM A 203       2.138  26.339  19.516  1.00 55.09      E    C  
ANISOU 1312  C12 PAM A 203     7450   6310   7170   -360   -330   -340  E    C  
HETATM 1313  C13 PAM A 203       1.192  26.944  18.496  1.00 57.59      E    C  
ANISOU 1313  C13 PAM A 203     7750   6450   7690   -400   -520   -280  E    C  
HETATM 1314  C14 PAM A 203      -0.029  26.128  18.161  1.00 56.17      E    C  
ANISOU 1314  C14 PAM A 203     7530   6160   7650   -410   -600   -260  E    C  
HETATM 1315  C15 PAM A 203       0.180  25.077  17.142  1.00 55.80      E    C  
ANISOU 1315  C15 PAM A 203     7660   6130   7410   -440   -680   -160  E    C  
HETATM 1316  C16 PAM A 203      -0.936  24.891  16.121  1.00 56.91      E    C  
ANISOU 1316  C16 PAM A 203     7820   6080   7720   -470   -920   -120  E    C  
HETATM 1317  C1  NAG A 204       2.170  35.482  28.280  1.00 94.91      F    C  
ANISOU 1317  C1  NAG A 204    11700  11290  13070   -560    660  -1560  F    C  
HETATM 1318  C2  NAG A 204       2.965  36.491  27.478  1.00 98.48      F    C  
ANISOU 1318  C2  NAG A 204    12030  11770  13620   -520    510  -1510  F    C  
HETATM 1319  N2  NAG A 204       4.060  35.756  26.891  1.00106.02      F    N  
ANISOU 1319  N2  NAG A 204    13110  12860  14320   -450    350  -1410  F    N  
HETATM 1320  C3  NAG A 204       3.597  37.637  28.257  1.00 97.51      F    C  
ANISOU 1320  C3  NAG A 204    11840  11690  13520   -550    590  -1670  F    C  
HETATM 1321  O3  NAG A 204       2.785  38.733  27.867  1.00 88.25      F    O  
ANISOU 1321  O3  NAG A 204    10460  10330  12740   -590    620  -1700  F    O  
HETATM 1322  C4  NAG A 204       3.718  37.384  29.779  1.00100.81      F    C  
ANISOU 1322  C4  NAG A 204    12430  12170  13700   -600    740  -1830  F    C  
HETATM 1323  O4  NAG A 204       5.092  37.390  30.180  1.00103.44      F    O  
ANISOU 1323  O4  NAG A 204    12860  12660  13780   -540    610  -1890  F    O  
HETATM 1324  C5  NAG A 204       3.155  36.035  30.233  1.00 99.26      F    C  
ANISOU 1324  C5  NAG A 204    12460  11970  13290   -610    820  -1790  F    C  
HETATM 1325  O5  NAG A 204       1.887  35.827  29.616  1.00 95.52      F    O  
ANISOU 1325  O5  NAG A 204    11840  11340  13110   -650    890  -1740  F    O  
HETATM 1326  C6  NAG A 204       2.943  36.017  31.723  1.00 99.99      F    C  
ANISOU 1326  C6  NAG A 204    12770  12030  13190   -710   1030  -1960  F    C  
HETATM 1327  O6  NAG A 204       1.897  36.965  31.959  1.00105.43      F    O  
ANISOU 1327  O6  NAG A 204    13250  12560  14240   -830   1280  -2110  F    O  
HETATM 1328  C7  NAG A 204       3.925  34.870  25.915  1.00101.08      F    C  
ANISOU 1328  C7  NAG A 204    12540  12220  13640   -420    240  -1250  F    C  
HETATM 1329  O7  NAG A 204       2.858  34.616  25.346  1.00109.26      F    O  
ANISOU 1329  O7  NAG A 204    13530  13140  14840   -430    220  -1170  F    O  
HETATM 1330  C8  NAG A 204       5.234  34.212  25.633  1.00 92.65      F    C  
ANISOU 1330  C8  NAG A 204    11580  11300  12330   -360    150  -1220  F    C  
HETATM 1331  C1  GOL A 205      -8.973  11.364  14.721  1.00 93.28      G    C  
ANISOU 1331  C1  GOL A 205    11960  10050  13440   -880     10   -940  G    C  
HETATM 1332  O1  GOL A 205      -8.269  10.423  15.526  1.00 92.22      G    O  
ANISOU 1332  O1  GOL A 205    12080  10010  12950   -900    400   -850  G    O  
HETATM 1333  C2  GOL A 205     -10.023  12.123  15.514  1.00 98.95      G    C  
ANISOU 1333  C2  GOL A 205    12340  10590  14660   -920    130  -1200  G    C  
HETATM 1334  O2  GOL A 205      -9.458  13.320  16.071  1.00 87.99      G    O  
ANISOU 1334  O2  GOL A 205    10980   9280  13170   -860    100  -1110  G    O  
HETATM 1335  C3  GOL A 205     -11.256  12.438  14.682  1.00101.53      G    C  
ANISOU 1335  C3  GOL A 205    12320  10710  15550   -920   -240  -1420  G    C  
HETATM 1336  O3  GOL A 205     -12.330  12.928  15.483  1.00107.82      G    O  
ANISOU 1336  O3  GOL A 205    12740  11300  16930   -970    -40  -1740  G    O  
HETATM 1337 ZN    ZN A 206       3.526  18.401  31.012  1.00 78.17      H   ZN  
HETATM 1338 ZN    ZN A 207      16.409  28.712  14.677  1.00 58.96      I   ZN  
HETATM 1339 ZN    ZN A 208      -0.000  -0.000  14.601  0.50 49.67      J   ZN  
HETATM 1340  O   HOH A 301       3.873   4.005   9.924  1.00 46.42      K    O  
HETATM 1341  O   HOH A 302       1.497   3.086  19.236  1.00 47.11      K    O  
HETATM 1342  O   HOH A 303       7.851  36.012  18.210  1.00 55.15      K    O  
HETATM 1343  O   HOH A 304       1.033   4.388  16.373  1.00 43.78      K    O  
HETATM 1344  O   HOH A 305      -1.647   9.704  17.286  1.00 42.52      K    O  
HETATM 1345  O   HOH A 306       5.392  18.130  30.546  1.00 59.56      K    O  
HETATM 1346  O   HOH A 307       1.031   9.042  17.325  1.00 39.54      K    O  
HETATM 1347  O   HOH A 308      -4.554  16.209  11.376  1.00 50.74      K    O  
HETATM 1348  O   HOH A 309       1.171  13.538  21.763  1.00 38.04      K    O  
HETATM 1349  O   HOH A 310       2.494   6.776  16.437  1.00 39.51      K    O  
HETATM 1350  O   HOH A 311      -8.215  11.259  11.107  1.00 56.34      K    O  
HETATM 1351  O   HOH A 312       3.509  23.523   3.300  1.00 53.92      K    O  
HETATM 1352  O   HOH A 313      -7.264  15.887   3.506  1.00 64.04      K    O  
HETATM 1353  O   HOH A 314     -12.535  31.197  13.465  1.00 66.99      K    O  
HETATM 1354  O   HOH A 315      14.094  29.100  13.392  1.00 60.83      K    O  
HETATM 1355  O   HOH A 316      -2.307  36.757  16.109  1.00 61.00      K    O  
HETATM 1356  O   HOH A 317       1.432   7.203   6.808  1.00 55.54      K    O  
HETATM 1357  O   HOH A 318      14.976  12.043  18.267  1.00 61.58      K    O  
HETATM 1358  O   HOH A 319      14.181  30.133  24.248  1.00 59.07      K    O  
HETATM 1359  O   HOH A 320      -2.621   3.996  22.085  1.00 55.96      K    O  
HETATM 1360  O   HOH A 321      -3.127  41.583  15.123  1.00 66.26      K    O  
HETATM 1361  O   HOH A 322      -4.813   3.923  13.570  1.00 56.88      K    O  
HETATM 1362  O   HOH A 323       1.060  31.295  31.249  1.00 63.47      K    O  
HETATM 1363  O   HOH A 324      13.448  29.560  15.809  1.00 52.41      K    O  
HETATM 1364  O   HOH A 325      15.718  19.736  13.957  1.00 62.85      K    O  
HETATM 1365  O   HOH A 326       1.034   1.667  23.783  1.00 66.33      K    O  
CONECT  267 1243
CONECT  412 1337
CONECT  480 1337
CONECT  514 1317
CONECT  620 1285
CONECT  837 1338
CONECT 1157 1271
CONECT 1243  267 1244 1251
CONECT 1244 1243 1245 1246
CONECT 1245 1244 1254
CONECT 1246 1244 1247 1248
CONECT 1247 1246
CONECT 1248 1246 1249 1250
CONECT 1249 1248 1257
CONECT 1250 1248 1251 1252
CONECT 1251 1243 1250
CONECT 1252 1250 1253
CONECT 1253 1252
CONECT 1254 1245 1255 1256
CONECT 1255 1254
CONECT 1256 1254
CONECT 1257 1249 1258 1265
CONECT 1258 1257 1259 1260
CONECT 1259 1258 1268
CONECT 1260 1258 1261 1262
CONECT 1261 1260
CONECT 1262 1260 1263 1264
CONECT 1263 1262
CONECT 1264 1262 1265 1266
CONECT 1265 1257 1264
CONECT 1266 1264 1267
CONECT 1267 1266
CONECT 1268 1259 1269 1270
CONECT 1269 1268
CONECT 1270 1268
CONECT 1271 1157 1272 1279
CONECT 1272 1271 1273 1274
CONECT 1273 1272 1282
CONECT 1274 1272 1275 1276
CONECT 1275 1274
CONECT 1276 1274 1277 1278
CONECT 1277 1276
CONECT 1278 1276 1279 1280
CONECT 1279 1271 1278
CONECT 1280 1278 1281
CONECT 1281 1280
CONECT 1282 1273 1283 1284
CONECT 1283 1282
CONECT 1284 1282
CONECT 1285  620 1286 1293
CONECT 1286 1285 1287 1288
CONECT 1287 1286 1296
CONECT 1288 1286 1289 1290
CONECT 1289 1288
CONECT 1290 1288 1291 1292
CONECT 1291 1290
CONECT 1292 1290 1293 1294
CONECT 1293 1285 1292
CONECT 1294 1292 1295
CONECT 1295 1294
CONECT 1296 1287 1297 1298
CONECT 1297 1296
CONECT 1298 1296
CONECT 1299 1300 1301 1302
CONECT 1300 1299
CONECT 1301 1299 1303
CONECT 1302 1299
CONECT 1303 1301 1304
CONECT 1304 1303 1305
CONECT 1305 1304 1306
CONECT 1306 1305 1307
CONECT 1307 1306 1308
CONECT 1308 1307 1309
CONECT 1309 1308 1310
CONECT 1310 1309 1311
CONECT 1311 1310 1312
CONECT 1312 1311 1313
CONECT 1313 1312 1314
CONECT 1314 1313 1315
CONECT 1315 1314 1316
CONECT 1316 1315
CONECT 1317  514 1318 1325
CONECT 1318 1317 1319 1320
CONECT 1319 1318 1328
CONECT 1320 1318 1321 1322
CONECT 1321 1320
CONECT 1322 1320 1323 1324
CONECT 1323 1322
CONECT 1324 1322 1325 1326
CONECT 1325 1317 1324
CONECT 1326 1324 1327
CONECT 1327 1326
CONECT 1328 1319 1329 1330
CONECT 1329 1328
CONECT 1330 1328
CONECT 1331 1332 1333
CONECT 1332 1331
CONECT 1333 1331 1334 1335
CONECT 1334 1333
CONECT 1335 1333 1336
CONECT 1336 1335
CONECT 1337  412  480
CONECT 1338  837
END



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