CNRS Nantes University UFIP UFIP
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***  5ac7  ***

elNémo ID: 200122155342124928

Job options:

ID        	=	 200122155342124928
JOBID     	=	 5ac7
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 5ac7

ATOM      1  N   MET A   1      31.230 -21.465 -36.862  1.00 51.55      A    N  
ANISOU    1  N   MET A   1     5258   6313   8017    163   -997   -663  A    N  
ATOM      2  CA  MET A   1      30.476 -20.726 -37.865  1.00 41.81      A    C  
ANISOU    2  CA  MET A   1     4150   5182   6553    -62   -564   -556  A    C  
ATOM      3  C   MET A   1      29.084 -20.287 -37.377  1.00 32.28      A    C  
ANISOU    3  C   MET A   1     3456   3710   5099   -149   -518   -237  A    C  
ATOM      4  O   MET A   1      28.402 -21.016 -36.668  1.00 33.31      A    O  
ANISOU    4  O   MET A   1     3833   3630   5192     -9   -716   -113  A    O  
ATOM      5  CB  MET A   1      30.377 -21.585 -39.122  1.00 41.70      A    C  
ANISOU    5  CB  MET A   1     3940   5295   6607    106   -396   -753  A    C  
ATOM      6  CG  MET A   1      29.021 -21.688 -39.731  1.00 41.80      A    C  
ANISOU    6  CG  MET A   1     4316   5138   6427     87   -210   -542  A    C  
ATOM      7  SD  MET A   1      29.005 -23.151 -40.774  1.00 72.37      A    S  
ANISOU    7  SD  MET A   1     8015   9040  10443    413   -225   -793  A    S  
ATOM      8  CE  MET A   1      30.383 -22.823 -41.872  1.00 40.95      A    C  
ANISOU    8  CE  MET A   1     3428   5603   6528    286     72  -1237  A    C  
ATOM      9  N   ILE A   2      28.674 -19.084 -37.757  1.00 33.18      A    N  
ANISOU    9  N   ILE A   2     3724   3849   5032   -402   -291   -135  A    N  
ATOM     10  CA  ILE A   2      27.343 -18.575 -37.424  1.00 29.28      A    C  
ANISOU   10  CA  ILE A   2     3626   3154   4345   -426   -246     52  A    C  
ATOM     11  C   ILE A   2      26.278 -19.233 -38.300  1.00 29.18      A    C  
ANISOU   11  C   ILE A   2     3711   3086   4291   -308    -99    101  A    C  
ATOM     12  O   ILE A   2      26.428 -19.279 -39.515  1.00 28.32      A    O  
ANISOU   12  O   ILE A   2     3487   3074   4197   -366     76     38  A    O  
ATOM     13  CB  ILE A   2      27.253 -17.039 -37.627  1.00 28.59      A    C  
ANISOU   13  CB  ILE A   2     3710   3030   4123   -685   -170    102  A    C  
ATOM     14  CG1 ILE A   2      28.313 -16.321 -36.787  1.00 29.53      A    C  
ANISOU   14  CG1 ILE A   2     3763   3192   4264   -849   -337     72  A    C  
ATOM     15  CG2 ILE A   2      25.836 -16.540 -37.312  1.00 27.41      A    C  
ANISOU   15  CG2 ILE A   2     3901   2683   3832   -606   -169    181  A    C  
ATOM     16  CD1 ILE A   2      28.212 -16.620 -35.291  1.00 34.15      A    C  
ANISOU   16  CD1 ILE A   2     4469   3667   4837   -710   -562    101  A    C  
ATOM     17  N   ILE A   3      25.196 -19.720 -37.693  1.00 21.73      A    N  
ANISOU   17  N   ILE A   3     2981   2021   3255   -199   -163    210  A    N  
ATOM     18  CA  ILE A   3      24.114 -20.370 -38.442  1.00 19.91      A    C  
ANISOU   18  CA  ILE A   3     2844   1740   2979   -113    -56    275  A    C  
ATOM     19  C   ILE A   3      22.770 -19.685 -38.168  1.00 23.48      A    C  
ANISOU   19  C   ILE A   3     3505   2144   3272   -145     22    338  A    C  
ATOM     20  O   ILE A   3      22.094 -19.992 -37.183  1.00 26.32      A    O  
ANISOU   20  O   ILE A   3     3960   2536   3505   -143    -42    377  A    O  
ATOM     21  CB  ILE A   3      24.006 -21.884 -38.091  1.00 21.08      A    C  
ANISOU   21  CB  ILE A   3     3014   1828   3166     25   -254    320  A    C  
ATOM     22  CG1 ILE A   3      25.353 -22.588 -38.298  1.00 22.85      A    C  
ANISOU   22  CG1 ILE A   3     2991   2076   3615    162   -425    155  A    C  
ATOM     23  CG2 ILE A   3      22.880 -22.562 -38.906  1.00 23.61      A    C  
ANISOU   23  CG2 ILE A   3     3448   2094   3427     73   -164    406  A    C  
ATOM     24  CD1 ILE A   3      25.366 -24.101 -37.947  1.00 26.41      A    C  
ANISOU   24  CD1 ILE A   3     3534   2355   4147    338   -782    174  A    C  
ATOM     25  N   PRO A   4      22.391 -18.726 -39.022  1.00 20.58      A    N  
ANISOU   25  N   PRO A   4     3206   1718   2897   -198    129    317  A    N  
ATOM     26  CA  PRO A   4      21.094 -18.067 -38.891  1.00 21.24      A    C  
ANISOU   26  CA  PRO A   4     3433   1737   2900   -143    140    289  A    C  
ATOM     27  C   PRO A   4      19.956 -19.067 -39.070  1.00 26.16      A    C  
ANISOU   27  C   PRO A   4     4045   2414   3480    -55    200    345  A    C  
ATOM     28  O   PRO A   4      20.081 -20.023 -39.861  1.00 24.81      A    O  
ANISOU   28  O   PRO A   4     3842   2224   3359    -45    231    431  A    O  
ATOM     29  CB  PRO A   4      21.120 -17.030 -40.023  1.00 21.13      A    C  
ANISOU   29  CB  PRO A   4     3543   1562   2922   -236    127    282  A    C  
ATOM     30  CG  PRO A   4      22.597 -16.817 -40.302  1.00 23.33      A    C  
ANISOU   30  CG  PRO A   4     3738   1903   3223   -441    139    297  A    C  
ATOM     31  CD  PRO A   4      23.166 -18.179 -40.152  1.00 18.79      A    C  
ANISOU   31  CD  PRO A   4     2934   1489   2715   -350    202    294  A    C  
ATOM     32  N   ALA A   5      18.875 -18.863 -38.316  1.00 25.45      A    N  
ANISOU   32  N   ALA A   5     3962   2428   3281    -11    211    263  A    N  
ATOM     33  CA  ALA A   5      17.760 -19.814 -38.255  1.00 24.30      A    C  
ANISOU   33  CA  ALA A   5     3772   2424   3036    -20    268    315  A    C  
ATOM     34  C   ALA A   5      16.401 -19.143 -38.466  1.00 31.71      A    C  
ANISOU   34  C   ALA A   5     4644   3429   3974     88    315    144  A    C  
ATOM     35  O   ALA A   5      16.135 -18.078 -37.904  1.00 29.27      A    O  
ANISOU   35  O   ALA A   5     4306   3158   3658    186    285    -87  A    O  
ATOM     36  CB  ALA A   5      17.757 -20.541 -36.903  1.00 25.56      A    C  
ANISOU   36  CB  ALA A   5     3938   2790   2983   -175    235    357  A    C  
ATOM     37  N   LEU A   6      15.539 -19.796 -39.242  1.00 26.22      A    N  
ANISOU   37  N   LEU A   6     3915   2746   3303     95    347    221  A    N  
ATOM     38  CA  LEU A   6      14.162 -19.351 -39.466  1.00 29.02      A    C  
ANISOU   38  CA  LEU A   6     4137   3200   3690    214    356     35  A    C  
ATOM     39  C   LEU A   6      13.176 -20.478 -39.182  1.00 26.61      A    C  
ANISOU   39  C   LEU A   6     3692   3203   3217     56    452    103  A    C  
ATOM     40  O   LEU A   6      13.398 -21.632 -39.581  1.00 27.77      A    O  
ANISOU   40  O   LEU A   6     3953   3282   3317    -90    430    370  A    O  
ATOM     41  CB  LEU A   6      13.963 -18.871 -40.917  1.00 25.40      A    C  
ANISOU   41  CB  LEU A   6     3800   2412   3438    335    232     70  A    C  
ATOM     42  CG  LEU A   6      14.703 -17.635 -41.414  1.00 28.80      A    C  
ANISOU   42  CG  LEU A   6     4435   2518   3991    391     70     23  A    C  
ATOM     43  CD1 LEU A   6      14.262 -17.325 -42.843  1.00 32.09      A    C  
ANISOU   43  CD1 LEU A   6     4836   2826   4530    346    -65     86  A    C  
ATOM     44  CD2 LEU A   6      14.474 -16.416 -40.498  1.00 28.75      A    C  
ANISOU   44  CD2 LEU A   6     4386   2528   4011    558    -52   -287  A    C  
ATOM     45  N   ASN A   7      12.084 -20.156 -38.499  1.00 27.33      A    N  
ANISOU   45  N   ASN A   7     3528   3653   3203     67    538   -168  A    N  
ATOM     46  CA  ASN A   7      10.980 -21.097 -38.325  1.00 26.92      A    C  
ANISOU   46  CA  ASN A   7     3294   3972   2965   -156    639   -133  A    C  
ATOM     47  C   ASN A   7       9.859 -20.724 -39.284  1.00 31.18      A    C  
ANISOU   47  C   ASN A   7     3641   4485   3721     56    582   -301  A    C  
ATOM     48  O   ASN A   7       9.522 -19.546 -39.413  1.00 32.41      A    O  
ANISOU   48  O   ASN A   7     3669   4567   4079    373    492   -639  A    O  
ATOM     49  CB  ASN A   7      10.452 -21.088 -36.882  1.00 30.22      A    C  
ANISOU   49  CB  ASN A   7     3478   4955   3048   -383    817   -370  A    C  
ATOM     50  CG  ASN A   7      11.524 -21.440 -35.860  1.00 35.33      A    C  
ANISOU   50  CG  ASN A   7     4365   5598   3459   -628    806   -194  A    C  
ATOM     51  ND2 ASN A   7      11.592 -20.667 -34.781  1.00 50.04      A    N  
ANISOU   51  ND2 ASN A   7     6124   7721   5168   -623    903   -493  A    N  
ATOM     52  OD1 ASN A   7      12.302 -22.364 -36.059  1.00 46.88      A    O  
ANISOU   52  OD1 ASN A   7     6112   6798   4901   -784    667    172  A    O  
ATOM     53  N   LEU A   8       9.272 -21.728 -39.930  1.00 27.22      A    N  
ANISOU   53  N   LEU A   8     3146   4010   3184   -114    568    -74  A    N  
ATOM     54  CA  LEU A   8       8.257 -21.505 -40.955  1.00 29.01      A    C  
ANISOU   54  CA  LEU A   8     3232   4157   3634     64    459   -174  A    C  
ATOM     55  C   LEU A   8       6.958 -22.249 -40.650  1.00 32.22      A    C  
ANISOU   55  C   LEU A   8     3298   5083   3861   -190    567   -240  A    C  
ATOM     56  O   LEU A   8       6.954 -23.464 -40.415  1.00 32.60      A    O  
ANISOU   56  O   LEU A   8     3462   5283   3640   -590    619     73  A    O  
ATOM     57  CB  LEU A   8       8.782 -21.940 -42.326  1.00 25.52      A    C  
ANISOU   57  CB  LEU A   8     3153   3197   3346     92    301    169  A    C  
ATOM     58  CG  LEU A   8      10.091 -21.284 -42.768  1.00 31.11      A    C  
ANISOU   58  CG  LEU A   8     4170   3473   4179    233    224    244  A    C  
ATOM     59  CD1 LEU A   8      10.666 -22.012 -43.990  1.00 34.82      A    C  
ANISOU   59  CD1 LEU A   8     4950   3596   4684    155    159    556  A    C  
ATOM     60  CD2 LEU A   8       9.864 -19.821 -43.086  1.00 33.07      A    C  
ANISOU   60  CD2 LEU A   8     4402   3509   4653    520     47    -36  A    C  
ATOM     61  N   ILE A   9       5.856 -21.505 -40.628  1.00 32.07      A    N  
ANISOU   61  N   ILE A   9     2853   5346   3988     30    559   -675  A    N  
ATOM     62  CA  ILE A   9       4.527 -22.103 -40.620  1.00 34.23      A    C  
ANISOU   62  CA  ILE A   9     2723   6123   4160   -183    637   -784  A    C  
ATOM     63  C   ILE A   9       3.817 -21.594 -41.865  1.00 37.13      A    C  
ANISOU   63  C   ILE A   9     3008   6162   4936    184    356   -911  A    C  
ATOM     64  O   ILE A   9       3.541 -20.400 -41.969  1.00 37.15      A    O  
ANISOU   64  O   ILE A   9     2829   6049   5237    632    184  -1342  A    O  
ATOM     65  CB  ILE A   9       3.711 -21.731 -39.362  1.00 38.41      A    C  
ANISOU   65  CB  ILE A   9     2671   7455   4470   -276    896  -1311  A    C  
ATOM     66  CG1 ILE A   9       4.459 -22.118 -38.087  1.00 43.21      A    C  
ANISOU   66  CG1 ILE A   9     3468   8305   4643   -665   1105  -1172  A    C  
ATOM     67  CG2 ILE A   9       2.332 -22.391 -39.397  1.00 45.92      A    C  
ANISOU   67  CG2 ILE A   9     3238   8920   5289   -563    955  -1398  A    C  
ATOM     68  CD1 ILE A   9       3.729 -21.677 -36.805  1.00 48.41      A    C  
ANISOU   68  CD1 ILE A   9     3836   9476   5081   -752   1205  -1612  A    C  
ATOM     69  N  AGLY A  10       3.522 -22.503 -42.790  0.46 36.36      A    N  
ANISOU   69  N  AGLY A  10     3090   5875   4848    -10    247   -541  A    N  
ATOM     70  N  BGLY A  10       3.536 -22.486 -42.813  0.54 36.14      A    N  
ANISOU   70  N  BGLY A  10     3071   5833   4829     -1    241   -539  A    N  
ATOM     71  CA AGLY A  10       3.118 -22.104 -44.121  0.46 39.15      A    C  
ANISOU   71  CA AGLY A  10     3557   5754   5564    286    -80   -532  A    C  
ATOM     72  CA BGLY A  10       2.803 -22.131 -44.021  0.54 40.54      A    C  
ANISOU   72  CA BGLY A  10     3594   6072   5737    272    -64   -610  A    C  
ATOM     73  C  AGLY A  10       4.250 -21.274 -44.691  0.46 34.89      A    C  
ANISOU   73  C  AGLY A  10     3495   4556   5206    560   -260   -435  A    C  
ATOM     74  C  BGLY A  10       3.260 -20.884 -44.770  0.54 39.55      A    C  
ANISOU   74  C  BGLY A  10     3740   5318   5970    734   -385   -744  A    C  
ATOM     75  O  AGLY A  10       5.424 -21.576 -44.469  0.46 31.02      A    O  
ANISOU   75  O  AGLY A  10     3342   3900   4545    413   -126   -165  A    O  
ATOM     76  O  BGLY A  10       2.437 -20.047 -45.151  0.54 43.48      A    O  
ANISOU   76  O  BGLY A  10     4000   5733   6786   1086   -678  -1114  A    O  
ATOM     77  N  AGLY A  11       3.909 -20.211 -45.404  0.46 44.76      A    N  
ANISOU   77  N  AGLY A  11     5188   5983   5835   2296  -1676  -1820  A    N  
ATOM     78  N  BGLY A  11       4.569 -20.756 -44.976  0.54 44.26      A    N  
ANISOU   78  N  BGLY A  11     5245   6006   5564   2460  -1581  -1844  A    N  
ATOM     79  CA AGLY A  11       4.923 -19.324 -45.931  0.46 43.46      A    C  
ANISOU   79  CA AGLY A  11     4898   6359   5255   2453  -1336  -1659  A    C  
ATOM     80  CA BGLY A  11       5.126 -19.650 -45.738  0.54 43.37      A    C  
ANISOU   80  CA BGLY A  11     4956   6344   5177   2507  -1331  -1677  A    C  
ATOM     81  C  AGLY A  11       5.264 -18.207 -44.967  0.46 42.93      A    C  
ANISOU   81  C  AGLY A  11     4398   6536   5376   2051   -896  -1429  A    C  
ATOM     82  C  BGLY A  11       5.529 -18.453 -44.897  0.54 42.31      A    C  
ANISOU   82  C  BGLY A  11     4376   6501   5198   2121   -886  -1433  A    C  
ATOM     83  O  AGLY A  11       5.754 -17.162 -45.391  0.46 39.53      A    O  
ANISOU   83  O  AGLY A  11     3815   6407   4800   1982   -691  -1234  A    O  
ATOM     84  O  BGLY A  11       6.281 -17.592 -45.345  0.54 38.86      A    O  
ANISOU   84  O  BGLY A  11     3821   6430   4512   2121   -676  -1226  A    O  
ATOM     85  N   THR A  12       5.014 -18.409 -43.672  1.00 42.10      A    N  
ANISOU   85  N   THR A  12     4160   6257   5580   1791   -779  -1445  A    N  
ATOM     86  CA  THR A  12       5.231 -17.318 -42.724  1.00 39.59      A    C  
ANISOU   86  CA  THR A  12     3576   6068   5399   1421   -423  -1263  A    C  
ATOM     87  C   THR A  12       6.410 -17.549 -41.777  1.00 38.67      A    C  
ANISOU   87  C   THR A  12     3456   6213   5025   1400   -236  -1159  A    C  
ATOM     88  O   THR A  12       6.552 -18.619 -41.176  1.00 36.61      A    O  
ANISOU   88  O   THR A  12     3317   5859   4734   1523   -291  -1261  A    O  
ATOM     89  CB  THR A  12       3.950 -17.064 -41.877  1.00 39.66      A    C  
ANISOU   89  CB  THR A  12     3435   5681   5952   1101   -350  -1294  A    C  
ATOM     90  CG2 THR A  12       4.114 -15.839 -40.982  1.00 42.05      A    C  
ANISOU   90  CG2 THR A  12     3633   6044   6300    799      5  -1141  A    C  
ATOM     91  OG1 THR A  12       2.833 -16.861 -42.749  1.00 40.59      A    O  
ANISOU   91  OG1 THR A  12     3491   5576   6354   1090   -563  -1304  A    O  
ATOM     92  N   VAL A  13       7.258 -16.533 -41.650  1.00 32.85      A    N  
ANISOU   92  N   VAL A  13     2573   5788   4120   1234    -61   -936  A    N  
ATOM     93  CA  VAL A  13       8.382 -16.581 -40.726  1.00 27.90      A    C  
ANISOU   93  CA  VAL A  13     1872   5442   3285   1142     52   -781  A    C  
ATOM     94  C   VAL A  13       7.866 -16.239 -39.327  1.00 36.91      A    C  
ANISOU   94  C   VAL A  13     2962   6370   4691    803    198   -875  A    C  
ATOM     95  O   VAL A  13       7.266 -15.181 -39.132  1.00 37.17      A    O  
ANISOU   95  O   VAL A  13     2970   6228   4925    531    307   -877  A    O  
ATOM     96  CB  VAL A  13       9.492 -15.610 -41.146  1.00 31.77      A    C  
ANISOU   96  CB  VAL A  13     2200   6348   3521   1046    101   -463  A    C  
ATOM     97  CG1 VAL A  13      10.648 -15.661 -40.155  1.00 31.76      A    C  
ANISOU   97  CG1 VAL A  13     2074   6664   3330    896    140   -244  A    C  
ATOM     98  CG2 VAL A  13       9.983 -15.943 -42.583  1.00 36.09      A    C  
ANISOU   98  CG2 VAL A  13     2824   7129   3761   1436     38   -360  A    C  
ATOM     99  N   VAL A  14       8.092 -17.131 -38.361  1.00 34.14      A    N  
ANISOU   99  N   VAL A  14     2690   5976   4305    831    222   -937  A    N  
ATOM    100  CA  VAL A  14       7.460 -16.998 -37.044  1.00 36.41      A    C  
ANISOU  100  CA  VAL A  14     3139   5888   4808    517    374   -993  A    C  
ATOM    101  C   VAL A  14       8.411 -17.196 -35.873  1.00 37.22      A    C  
ANISOU  101  C   VAL A  14     3314   6159   4670    373    416   -884  A    C  
ATOM    102  O   VAL A  14       9.494 -17.777 -36.009  1.00 34.03      A    O  
ANISOU  102  O   VAL A  14     2793   6152   3985    566    315   -762  A    O  
ATOM    103  CB  VAL A  14       6.283 -18.006 -36.865  1.00 30.91      A    C  
ANISOU  103  CB  VAL A  14     2559   4749   4436    616    351  -1151  A    C  
ATOM    104  CG1 VAL A  14       5.195 -17.744 -37.869  1.00 33.52      A    C  
ANISOU  104  CG1 VAL A  14     2805   4869   5062    662    258  -1207  A    C  
ATOM    105  CG2 VAL A  14       6.769 -19.444 -36.961  1.00 33.63      A    C  
ANISOU  105  CG2 VAL A  14     3009   5150   4617    918    174  -1217  A    C  
ATOM    106  N   ARG A  15       8.004 -16.677 -34.719  1.00 41.27      A    N  
ANISOU  106  N   ARG A  15     4041   6379   5262     71    571   -898  A    N  
ATOM    107  CA  ARG A  15       8.624 -17.058 -33.462  1.00 44.96      A    C  
ANISOU  107  CA  ARG A  15     4676   6876   5530    -57    589   -841  A    C  
ATOM    108  C   ARG A  15       7.674 -17.991 -32.735  1.00 37.88      A    C  
ANISOU  108  C   ARG A  15     3951   5585   4857     48    737   -967  A    C  
ATOM    109  O   ARG A  15       6.483 -17.709 -32.613  1.00 40.56      A    O  
ANISOU  109  O   ARG A  15     4362   5558   5489     15    920  -1024  A    O  
ATOM    110  CB  ARG A  15       8.953 -15.841 -32.591  1.00 45.87      A    C  
ANISOU  110  CB  ARG A  15     5042   6915   5470   -460    615   -749  A    C  
ATOM    111  CG  ARG A  15       9.613 -16.215 -31.271  1.00 48.13      A    C  
ANISOU  111  CG  ARG A  15     5561   7223   5505   -614    570   -682  A    C  
ATOM    112  CD  ARG A  15      10.137 -14.993 -30.538  1.00 57.08      A    C  
ANISOU  112  CD  ARG A  15     7026   8285   6377  -1055    448   -574  A    C  
ATOM    113  NE  ARG A  15       9.074 -14.150 -30.001  1.00 58.48      A    N  
ANISOU  113  NE  ARG A  15     7684   7915   6622  -1128    689   -731  A    N  
ATOM    114  CZ  ARG A  15       8.934 -12.858 -30.281  1.00 56.47      A    C  
ANISOU  114  CZ  ARG A  15     7647   7481   6327  -1337    655   -716  A    C  
ATOM    115  NH1 ARG A  15       9.787 -12.267 -31.107  1.00 50.95      A    N1+
ANISOU  115  NH1 ARG A  15     6677   7121   5559  -1563    366   -531  A    N1+
ATOM    116  NH2 ARG A  15       7.945 -12.158 -29.735  1.00 61.00      A    N  
ANISOU  116  NH2 ARG A  15     8720   7542   6916  -1284    932   -845  A    N  
ATOM    117  N   VAL A  15A      8.198 -19.121 -32.282  1.00 37.25      A    N  
ANISOU  117  N   VAL A  15A    3900   5603   4650    194    664   -952  A    N  
ATOM    118  CA  VAL A  15A      7.413 -20.057 -31.504  1.00 38.62      A    C  
ANISOU  118  CA  VAL A  15A    4237   5417   5018    252    783  -1008  A    C  
ATOM    119  C   VAL A  15A      8.034 -20.227 -30.122  1.00 38.19      A    C  
ANISOU  119  C   VAL A  15A    4412   5397   4702    127    855   -928  A    C  
ATOM    120  O   VAL A  15A      9.224 -19.991 -29.937  1.00 37.85      A    O  
ANISOU  120  O   VAL A  15A    4338   5715   4328     51    708   -821  A    O  
ATOM    121  CB  VAL A  15A      7.315 -21.421 -32.182  1.00 40.55      A    C  
ANISOU  121  CB  VAL A  15A    4429   5616   5360    559    593  -1074  A    C  
ATOM    122  CG1 VAL A  15A      6.407 -21.344 -33.400  1.00 44.22      A    C  
ANISOU  122  CG1 VAL A  15A    4774   5908   6120    637    479  -1162  A    C  
ATOM    123  CG2 VAL A  15A      8.704 -21.906 -32.558  1.00 45.52      A    C  
ANISOU  123  CG2 VAL A  15A    4995   6697   5605    818    417  -1016  A    C  
ATOM    124  N   VAL A  15B      7.220 -20.640 -29.162  1.00 40.15      A    N  
ANISOU  124  N   VAL A  15B    4863   5293   5101    103   1069   -926  A    N  
ATOM    125  CA  VAL A  15B      7.712 -20.937 -27.825  1.00 42.42      A    C  
ANISOU  125  CA  VAL A  15B    5426   5572   5121     29   1140   -855  A    C  
ATOM    126  C   VAL A  15B      7.404 -22.388 -27.505  1.00 41.90      A    C  
ANISOU  126  C   VAL A  15B    5372   5344   5203    219   1147   -828  A    C  
ATOM    127  O   VAL A  15B      6.431 -22.945 -28.021  1.00 40.47      A    O  
ANISOU  127  O   VAL A  15B    5070   4907   5399    305   1168   -841  A    O  
ATOM    128  CB  VAL A  15B      7.094 -19.997 -26.776  1.00 44.67      A    C  
ANISOU  128  CB  VAL A  15B    6073   5565   5336   -138   1441   -837  A    C  
ATOM    129  CG1 VAL A  15B      7.567 -18.589 -27.027  1.00 51.17      A    C  
ANISOU  129  CG1 VAL A  15B    7011   6489   5941   -358   1344   -864  A    C  
ATOM    130  CG2 VAL A  15B      5.575 -20.053 -26.825  1.00 39.45      A    C  
ANISOU  130  CG2 VAL A  15B    5349   4545   5095    -25   1767   -800  A    C  
ATOM    131  N   ARG A  15C      8.247 -23.014 -26.688  1.00 37.79      A    N  
ANISOU  131  N   ARG A  15C    5000   4965   4394    258   1076   -758  A    N  
ATOM    132  CA  ARG A  15C      8.030 -24.407 -26.310  1.00 38.33      A    C  
ANISOU  132  CA  ARG A  15C    5144   4849   4568    438   1070   -713  A    C  
ATOM    133  C   ARG A  15C      7.103 -24.476 -25.102  1.00 39.38      A    C  
ANISOU  133  C   ARG A  15C    5510   4631   4821    333   1399   -609  A    C  
ATOM    134  O   ARG A  15C      7.242 -23.703 -24.154  1.00 41.05      A    O  
ANISOU  134  O   ARG A  15C    5979   4848   4771    203   1579   -575  A    O  
ATOM    135  CB  ARG A  15C      9.358 -25.113 -26.009  1.00 49.11      A    C  
ANISOU  135  CB  ARG A  15C    6547   6548   5565    601    865   -639  A    C  
ATOM    136  CG  ARG A  15C      9.228 -26.621 -25.776  1.00 55.05      A    C  
ANISOU  136  CG  ARG A  15C    7430   7085   6400    844    812   -603  A    C  
ATOM    137  CD  ARG A  15C     10.552 -27.280 -25.356  1.00 55.99      A    C  
ANISOU  137  CD  ARG A  15C    7595   7553   6124   1065    657   -483  A    C  
ATOM    138  NE  ARG A  15C     11.413 -27.563 -26.500  1.00 70.70      A    N  
ANISOU  138  NE  ARG A  15C    9256   9771   7835   1411    445   -485  A    N  
ATOM    139  CZ  ARG A  15C     12.351 -26.738 -26.955  1.00 74.60      A    C  
ANISOU  139  CZ  ARG A  15C    9463  10782   8098   1398    358   -381  A    C  
ATOM    140  NH1 ARG A  15C     12.561 -25.570 -26.359  1.00 79.61      A    N1+
ANISOU  140  NH1 ARG A  15C   10040  11574   8632    985    384   -303  A    N1+
ATOM    141  NH2 ARG A  15C     13.081 -27.083 -28.007  1.00 70.86      A    N  
ANISOU  141  NH2 ARG A  15C    8800  10652   7471   1813    239   -323  A    N  
ATOM    142  N   LEU A  16       6.158 -25.405 -25.139  1.00 38.29      A    N  
ANISOU  142  N   LEU A  16     5318   4176   5057    394   1460   -525  A    N  
ATOM    143  CA  LEU A  16       5.182 -25.540 -24.070  1.00 40.26      A    C  
ANISOU  143  CA  LEU A  16     5691   4133   5472    336   1825   -320  A    C  
ATOM    144  C   LEU A  16       5.549 -26.679 -23.122  1.00 44.91      A    C  
ANISOU  144  C   LEU A  16     6498   4650   5914    414   1817   -197  A    C  
ATOM    145  O   LEU A  16       6.512 -27.413 -23.370  1.00 42.81      A    O  
ANISOU  145  O   LEU A  16     6279   4538   5450    538   1512   -279  A    O  
ATOM    146  CB  LEU A  16       3.785 -25.745 -24.659  1.00 47.71      A    C  
ANISOU  146  CB  LEU A  16     6344   4792   6992    278   1903   -171  A    C  
ATOM    147  CG  LEU A  16       2.933 -24.475 -24.767  1.00 59.29      A    C  
ANISOU  147  CG  LEU A  16     7682   6234   8612    233   2226   -108  A    C  
ATOM    148  CD1 LEU A  16       3.644 -23.398 -25.554  1.00 59.37      A    C  
ANISOU  148  CD1 LEU A  16     7693   6486   8380    213   2061   -372  A    C  
ATOM    149  CD2 LEU A  16       1.574 -24.773 -25.375  1.00 60.98      A    C  
ANISOU  149  CD2 LEU A  16     7504   6228   9437    162   2246    135  A    C  
ATOM    150  N   HIS A  17       4.782 -26.807 -22.038  1.00 41.60      A    N  
ANISOU  150  N   HIS A  17     6218   4018   5571    395   2188     38  A    N  
ATOM    151  CA  HIS A  17       5.058 -27.766 -20.969  1.00 50.13      A    C  
ANISOU  151  CA  HIS A  17     7547   5020   6479    465   2250    198  A    C  
ATOM    152  C   HIS A  17       5.306 -29.183 -21.480  1.00 49.99      A    C  
ANISOU  152  C   HIS A  17     7469   4879   6645    531   1885    211  A    C  
ATOM    153  O   HIS A  17       6.153 -29.901 -20.948  1.00 52.20      A    O  
ANISOU  153  O   HIS A  17     7973   5236   6627    655   1758    217  A    O  
ATOM    154  CB  HIS A  17       3.897 -27.779 -19.963  1.00 50.51      A    C  
ANISOU  154  CB  HIS A  17     7654   4829   6709    469   2751    538  A    C  
ATOM    155  CG  HIS A  17       4.147 -28.625 -18.750  1.00 65.42      A    C  
ANISOU  155  CG  HIS A  17     9843   6646   8368    551   2881    734  A    C  
ATOM    156  CD2 HIS A  17       3.485 -29.701 -18.261  1.00 70.52      A    C  
ANISOU  156  CD2 HIS A  17    10437   7053   9305    546   3005   1078  A    C  
ATOM    157  ND1 HIS A  17       5.182 -28.383 -17.871  1.00 72.69      A    N  
ANISOU  157  ND1 HIS A  17    11180   7750   8690    623   2861    620  A    N  
ATOM    158  CE1 HIS A  17       5.151 -29.277 -16.898  1.00 73.70      A    C  
ANISOU  158  CE1 HIS A  17    11514   7764   8727    704   2993    855  A    C  
ATOM    159  NE2 HIS A  17       4.131 -30.089 -17.112  1.00 72.68      A    N  
ANISOU  159  NE2 HIS A  17    11105   7375   9135    662   3099   1141  A    N  
ATOM    160  N   GLN A  18       4.581 -29.576 -22.522  1.00 54.58      A    N  
ANISOU  160  N   GLN A  18     7808   5245   7687    462   1681    219  A    N  
ATOM    161  CA  GLN A  18       4.641 -30.953 -22.998  1.00 63.14      A    C  
ANISOU  161  CA  GLN A  18     8983   6066   8943    519   1300    237  A    C  
ATOM    162  C   GLN A  18       5.482 -31.108 -24.260  1.00 64.18      A    C  
ANISOU  162  C   GLN A  18     9152   6334   8901    722    875    -76  A    C  
ATOM    163  O   GLN A  18       5.440 -32.151 -24.915  1.00 67.26      A    O  
ANISOU  163  O   GLN A  18     9711   6435   9411    820    511   -117  A    O  
ATOM    164  CB  GLN A  18       3.226 -31.484 -23.234  1.00 68.45      A    C  
ANISOU  164  CB  GLN A  18     9459   6315  10233    271   1261    529  A    C  
ATOM    165  CG  GLN A  18       2.450 -31.691 -21.944  1.00 77.07      A    C  
ANISOU  165  CG  GLN A  18    10514   7273  11495    153   1690    961  A    C  
ATOM    166  CD  GLN A  18       1.006 -32.085 -22.179  1.00 86.20      A    C  
ANISOU  166  CD  GLN A  18    11327   8103  13324   -142   1671   1387  A    C  
ATOM    167  NE2 GLN A  18       0.566 -33.144 -21.505  1.00 86.97      A    N  
ANISOU  167  NE2 GLN A  18    11483   7912  13651   -272   1668   1775  A    N  
ATOM    168  OE1 GLN A  18       0.294 -31.449 -22.956  1.00 91.51      A    O  
ANISOU  168  OE1 GLN A  18    11656   8792  14321   -272   1637   1418  A    O  
ATOM    169  N   GLY A  19       6.255 -30.076 -24.588  1.00 61.34      A    N  
ANISOU  169  N   GLY A  19     8683   6396   8226    804    918   -267  A    N  
ATOM    170  CA  GLY A  19       7.204 -30.148 -25.687  1.00 60.34      A    C  
ANISOU  170  CA  GLY A  19     8555   6520   7851   1074    608   -484  A    C  
ATOM    171  C   GLY A  19       6.681 -29.599 -27.000  1.00 59.73      A    C  
ANISOU  171  C   GLY A  19     8283   6406   8006   1028    456   -631  A    C  
ATOM    172  O   GLY A  19       7.453 -29.307 -27.922  1.00 53.33      A    O  
ANISOU  172  O   GLY A  19     7417   5897   6948   1256    296   -786  A    O  
ATOM    173  N   ASP A  20       5.363 -29.462 -27.091  1.00 60.24      A    N  
ANISOU  173  N   ASP A  20     8210   6132   8544    750    512   -527  A    N  
ATOM    174  CA  ASP A  20       4.733 -28.911 -28.282  1.00 59.21      A    C  
ANISOU  174  CA  ASP A  20     7876   5948   8673    667    354   -624  A    C  
ATOM    175  C   ASP A  20       5.144 -27.450 -28.496  1.00 54.34      A    C  
ANISOU  175  C   ASP A  20     7043   5747   7857    652    568   -727  A    C  
ATOM    176  O   ASP A  20       5.521 -26.758 -27.548  1.00 53.05      A    O  
ANISOU  176  O   ASP A  20     6888   5792   7475    582    869   -671  A    O  
ATOM    177  CB  ASP A  20       3.212 -29.045 -28.176  1.00 64.73      A    C  
ANISOU  177  CB  ASP A  20     8383   6255   9957    343    388   -370  A    C  
ATOM    178  CG  ASP A  20       2.687 -28.712 -26.784  1.00 75.05      A    C  
ANISOU  178  CG  ASP A  20     9581   7564  11372    191    885    -77  A    C  
ATOM    179  OD1 ASP A  20       2.888 -29.518 -25.847  1.00 71.24      A    O  
ANISOU  179  OD1 ASP A  20     9300   6967  10800    216    962     61  A    O  
ATOM    180  OD2 ASP A  20       2.052 -27.648 -26.630  1.00 84.43      A    O1-
ANISOU  180  OD2 ASP A  20    10523   8853  12705     95   1218     32  A    O1-
ATOM    181  N   TYR A  21       5.089 -26.996 -29.746  1.00 72.62      A    N  
ANISOU  181  N   TYR A  21     7969   9669   9955  -1194   3004   1690  A    N  
ATOM    182  CA  TYR A  21       5.450 -25.623 -30.092  1.00 72.95      A    C  
ANISOU  182  CA  TYR A  21     7930   9956   9833  -1144   2789   1480  A    C  
ATOM    183  C   TYR A  21       4.221 -24.761 -30.376  1.00 82.85      A    C  
ANISOU  183  C   TYR A  21     9055  11266  11158  -1247   2802    905  A    C  
ATOM    184  O   TYR A  21       3.337 -25.161 -31.132  1.00 94.67      A    O  
ANISOU  184  O   TYR A  21    10472  12548  12950  -1295   2878    620  A    O  
ATOM    185  CB  TYR A  21       6.379 -25.603 -31.305  1.00 68.72      A    C  
ANISOU  185  CB  TYR A  21     7457   9155   9499   -913   2663   1539  A    C  
ATOM    186  CG  TYR A  21       7.850 -25.723 -30.963  1.00 77.11      A    C  
ANISOU  186  CG  TYR A  21     8573  10378  10347   -736   2495   2050  A    C  
ATOM    187  CD1 TYR A  21       8.563 -24.626 -30.496  1.00 74.68      A    C  
ANISOU  187  CD1 TYR A  21     8213  10543   9619   -791   2245   2099  A    C  
ATOM    188  CD2 TYR A  21       8.526 -26.930 -31.108  1.00 83.43      A    C  
ANISOU  188  CD2 TYR A  21     9464  10866  11370   -519   2606   2448  A    C  
ATOM    189  CE1 TYR A  21       9.906 -24.723 -30.182  1.00 78.38      A    C  
ANISOU  189  CE1 TYR A  21     8668  11249   9865   -667   2036   2527  A    C  
ATOM    190  CE2 TYR A  21       9.871 -27.036 -30.797  1.00 85.41      A    C  
ANISOU  190  CE2 TYR A  21     9663  11322  11468   -292   2437   2934  A    C  
ATOM    191  CZ  TYR A  21      10.554 -25.928 -30.334  1.00 86.37      A    C  
ANISOU  191  CZ  TYR A  21     9678  11998  11140   -383   2115   2974  A    C  
ATOM    192  OH  TYR A  21      11.890 -26.021 -30.021  1.00 95.74      A    O  
ANISOU  192  OH  TYR A  21    10726  13491  12160   -198   1907   3435  A    O  
ATOM    193  N   ALA A  22       4.169 -23.578 -29.769  1.00 74.00      A    N  
ANISOU  193  N   ALA A  22     7921  10463   9733  -1294   2714    717  A    N  
ATOM    194  CA  ALA A  22       3.080 -22.638 -30.019  1.00 62.05      A    C  
ANISOU  194  CA  ALA A  22     6288   8972   8317  -1270   2741    229  A    C  
ATOM    195  C   ALA A  22       3.603 -21.352 -30.652  1.00 57.84      A    C  
ANISOU  195  C   ALA A  22     5830   8419   7726  -1078   2535     28  A    C  
ATOM    196  O   ALA A  22       4.646 -20.831 -30.262  1.00 53.01      A    O  
ANISOU  196  O   ALA A  22     5385   7947   6811  -1132   2447    143  A    O  
ATOM    197  CB  ALA A  22       2.337 -22.330 -28.738  1.00 63.19      A    C  
ANISOU  197  CB  ALA A  22     6407   9360   8241  -1462   2965    128  A    C  
ATOM    198  N   ARG A  23       2.863 -20.854 -31.633  1.00 55.03      A    N  
ANISOU  198  N   ARG A  23     5322   7941   7645   -882   2474   -235  A    N  
ATOM    199  CA  ARG A  23       3.185 -19.622 -32.340  1.00 51.23      A    C  
ANISOU  199  CA  ARG A  23     4896   7381   7189   -645   2342   -386  A    C  
ATOM    200  C   ARG A  23       3.080 -18.397 -31.420  1.00 50.91      A    C  
ANISOU  200  C   ARG A  23     4983   7395   6966   -692   2611   -590  A    C  
ATOM    201  O   ARG A  23       2.139 -18.291 -30.638  1.00 50.06      A    O  
ANISOU  201  O   ARG A  23     4774   7371   6877   -781   2916   -731  A    O  
ATOM    202  CB  ARG A  23       2.239 -19.484 -33.534  1.00 54.27      A    C  
ANISOU  202  CB  ARG A  23     4991   7736   7892   -424   2245   -505  A    C  
ATOM    203  CG  ARG A  23       2.393 -18.245 -34.394  1.00 56.94      A    C  
ANISOU  203  CG  ARG A  23     5323   7990   8320   -105   2141   -564  A    C  
ATOM    204  CD  ARG A  23       1.102 -18.052 -35.182  1.00 63.63      A    C  
ANISOU  204  CD  ARG A  23     5735   9008   9432    100   2132   -583  A    C  
ATOM    205  NE  ARG A  23       1.327 -17.580 -36.540  1.00 63.04      A    N  
ANISOU  205  NE  ARG A  23     5563   8954   9436    344   1861   -489  A    N  
ATOM    206  CZ  ARG A  23       1.052 -18.284 -37.633  1.00 53.36      A    C  
ANISOU  206  CZ  ARG A  23     4097   7950   8227    249   1594   -449  A    C  
ATOM    207  NH1 ARG A  23       0.537 -19.504 -37.533  1.00 55.66      A    N1+
ANISOU  207  NH1 ARG A  23     4252   8392   8504   -102   1611   -534  A    N1+
ATOM    208  NH2 ARG A  23       1.290 -17.764 -38.827  1.00 53.11      A    N  
ANISOU  208  NH2 ARG A  23     3981   8001   8199    448   1352   -342  A    N  
ATOM    209  N   GLN A  24       4.049 -17.487 -31.508  1.00 50.70      A    N  
ANISOU  209  N   GLN A  24     5201   7305   6759   -682   2561   -642  A    N  
ATOM    210  CA  GLN A  24       4.018 -16.253 -30.716  1.00 55.30      A    C  
ANISOU  210  CA  GLN A  24     5991   7856   7164   -814   2925   -929  A    C  
ATOM    211  C   GLN A  24       3.773 -15.028 -31.596  1.00 59.11      A    C  
ANISOU  211  C   GLN A  24     6508   8003   7949   -450   3052  -1088  A    C  
ATOM    212  O   GLN A  24       2.794 -14.318 -31.408  1.00 67.11      A    O  
ANISOU  212  O   GLN A  24     7447   8852   9199   -269   3438  -1254  A    O  
ATOM    213  CB  GLN A  24       5.317 -16.063 -29.935  1.00 53.39      A    C  
ANISOU  213  CB  GLN A  24     6029   7861   6395  -1230   2885   -902  A    C  
ATOM    214  CG  GLN A  24       5.184 -16.266 -28.452  1.00 66.18      A    C  
ANISOU  214  CG  GLN A  24     7724   9809   7613  -1656   3074   -939  A    C  
ATOM    215  CD  GLN A  24       6.230 -15.506 -27.653  1.00 67.73      A    C  
ANISOU  215  CD  GLN A  24     8215  10228   7290  -2075   3037  -1053  A    C  
ATOM    216  NE2 GLN A  24       5.929 -15.253 -26.384  1.00 63.66      A    N  
ANISOU  216  NE2 GLN A  24     7825   9877   6486  -2418   3202  -1231  A    N  
ATOM    217  OE1 GLN A  24       7.298 -15.163 -28.162  1.00 66.12      A    O  
ANISOU  217  OE1 GLN A  24     8105  10077   6941  -2129   2850   -997  A    O  
ATOM    218  N   ARG A  25       4.665 -14.764 -32.545  1.00 50.18      A    N  
ANISOU  218  N   ARG A  25     5481   6755   6828   -312   2763   -986  A    N  
ATOM    219  CA  ARG A  25       4.433 -13.662 -33.474  1.00 51.14      A    C  
ANISOU  219  CA  ARG A  25     5615   6559   7256     77   2877  -1033  A    C  
ATOM    220  C   ARG A  25       4.930 -13.996 -34.869  1.00 44.53      A    C  
ANISOU  220  C   ARG A  25     4670   5718   6533    315   2410   -798  A    C  
ATOM    221  O   ARG A  25       5.797 -14.848 -35.046  1.00 45.06      A    O  
ANISOU  221  O   ARG A  25     4784   5930   6408    135   2073   -669  A    O  
ATOM    222  CB  ARG A  25       5.089 -12.366 -32.979  1.00 55.22      A    C  
ANISOU  222  CB  ARG A  25     6553   6825   7604   -102   3271  -1304  A    C  
ATOM    223  CG  ARG A  25       6.538 -12.170 -33.390  1.00 55.23      A    C  
ANISOU  223  CG  ARG A  25     6810   6848   7327   -294   2990  -1267  A    C  
ATOM    224  CD  ARG A  25       7.065 -10.813 -32.935  1.00 69.86      A    C  
ANISOU  224  CD  ARG A  25     9094   8431   9019   -557   3471  -1610  A    C  
ATOM    225  NE  ARG A  25       6.754  -9.741 -33.879  1.00 80.97      A    N  
ANISOU  225  NE  ARG A  25    10581   9332  10852   -100   3647  -1559  A    N  
ATOM    226  CZ  ARG A  25       7.631  -8.828 -34.291  1.00 86.65      A    C  
ANISOU  226  CZ  ARG A  25    11619   9791  11511   -194   3716  -1630  A    C  
ATOM    227  NH1 ARG A  25       8.881  -8.850 -33.844  1.00 85.70      A    N1+
ANISOU  227  NH1 ARG A  25    11745   9919  10898   -757   3623  -1810  A    N1+
ATOM    228  NH2 ARG A  25       7.260  -7.892 -35.153  1.00 91.40      A    N  
ANISOU  228  NH2 ARG A  25    12254   9961  12514    243   3849  -1453  A    N  
ATOM    229  N   ASP A  26       4.350 -13.325 -35.857  1.00 45.65      A    N  
ANISOU  229  N   ASP A  26     4640   5713   6993    734   2435   -701  A    N  
ATOM    230  CA  ASP A  26       4.756 -13.474 -37.244  1.00 44.86      A    C  
ANISOU  230  CA  ASP A  26     4440   5648   6956    934   2032   -496  A    C  
ATOM    231  C   ASP A  26       5.721 -12.358 -37.593  1.00 43.94      A    C  
ANISOU  231  C   ASP A  26     4670   5233   6792   1011   2122   -524  A    C  
ATOM    232  O   ASP A  26       5.439 -11.187 -37.332  1.00 47.16      A    O  
ANISOU  232  O   ASP A  26     5224   5335   7360   1184   2567   -605  A    O  
ATOM    233  CB  ASP A  26       3.542 -13.438 -38.174  1.00 48.62      A    C  
ANISOU  233  CB  ASP A  26     4443   6306   7723   1303   1957   -284  A    C  
ATOM    234  CG  ASP A  26       2.496 -14.465 -37.806  1.00 48.20      A    C  
ANISOU  234  CG  ASP A  26     4026   6577   7710   1158   1926   -300  A    C  
ATOM    235  OD1 ASP A  26       2.852 -15.468 -37.155  1.00 47.43      A    O  
ANISOU  235  OD1 ASP A  26     4061   6531   7428    791   1857   -421  A    O  
ATOM    236  OD2 ASP A  26       1.318 -14.268 -38.163  1.00 57.25      A    O1-
ANISOU  236  OD2 ASP A  26     4724   7954   9073   1414   1995   -145  A    O1-
ATOM    237  N   TYR A  27       6.864 -12.712 -38.165  1.00 44.83      A    N  
ANISOU  237  N   TYR A  27     4932   5390   6709    873   1778   -465  A    N  
ATOM    238  CA  TYR A  27       7.829 -11.701 -38.572  1.00 46.36      A    C  
ANISOU  238  CA  TYR A  27     5442   5334   6838    897   1843   -492  A    C  
ATOM    239  C   TYR A  27       7.510 -11.184 -39.964  1.00 52.79      A    C  
ANISOU  239  C   TYR A  27     6101   6062   7896   1328   1723   -250  A    C  
ATOM    240  O   TYR A  27       7.756 -10.013 -40.266  1.00 53.92      A    O  
ANISOU  240  O   TYR A  27     6457   5882   8149   1510   1981   -223  A    O  
ATOM    241  CB  TYR A  27       9.252 -12.249 -38.527  1.00 38.12      A    C  
ANISOU  241  CB  TYR A  27     4584   4436   5465    560   1556   -492  A    C  
ATOM    242  CG  TYR A  27       9.774 -12.523 -37.129  1.00 46.46      A    C  
ANISOU  242  CG  TYR A  27     5780   5689   6185    108   1681   -629  A    C  
ATOM    243  CD1 TYR A  27      10.176 -11.482 -36.290  1.00 48.54      A    C  
ANISOU  243  CD1 TYR A  27     6355   5862   6228   -205   2048   -894  A    C  
ATOM    244  CD2 TYR A  27       9.870 -13.825 -36.649  1.00 44.49      A    C  
ANISOU  244  CD2 TYR A  27     5353   5741   5809    -51   1476   -478  A    C  
ATOM    245  CE1 TYR A  27      10.659 -11.735 -35.010  1.00 45.95      A    C  
ANISOU  245  CE1 TYR A  27     6106   5880   5474   -717   2130  -1003  A    C  
ATOM    246  CE2 TYR A  27      10.360 -14.092 -35.379  1.00 46.70      A    C  
ANISOU  246  CE2 TYR A  27     5695   6320   5729   -453   1560   -486  A    C  
ATOM    247  CZ  TYR A  27      10.754 -13.046 -34.563  1.00 50.81      A    C  
ANISOU  247  CZ  TYR A  27     6473   6887   5945   -812   1847   -747  A    C  
ATOM    248  OH  TYR A  27      11.241 -13.328 -33.305  1.00 50.54      A    O  
ANISOU  248  OH  TYR A  27     6449   7311   5443  -1301   1895   -733  A    O  
ATOM    249  N   GLY A  28       6.957 -12.056 -40.803  1.00 51.32      A    N  
ANISOU  249  N   GLY A  28     5548   6186   7765   1443   1369    -69  A    N  
ATOM    250  CA  GLY A  28       6.581 -11.683 -42.156  1.00 54.64      A    C  
ANISOU  250  CA  GLY A  28     5728   6721   8312   1783   1190    215  A    C  
ATOM    251  C   GLY A  28       6.379 -12.876 -43.072  1.00 47.38      A    C  
ANISOU  251  C   GLY A  28     4508   6227   7265   1636    754    281  A    C  
ATOM    252  O   GLY A  28       6.582 -14.013 -42.661  1.00 44.77      A    O  
ANISOU  252  O   GLY A  28     4209   5984   6819   1308    651    106  A    O  
ATOM    253  N   ASN A  29       5.977 -12.606 -44.311  1.00 42.53      A    N  
ANISOU  253  N   ASN A  29     3615   5886   6661   1850    552    547  A    N  
ATOM    254  CA  ASN A  29       5.730 -13.646 -45.313  1.00 45.14      A    C  
ANISOU  254  CA  ASN A  29     3666   6691   6795   1602    185    553  A    C  
ATOM    255  C   ASN A  29       6.814 -13.683 -46.383  1.00 41.41      A    C  
ANISOU  255  C   ASN A  29     3420   6192   6122   1500    -45    562  A    C  
ATOM    256  O   ASN A  29       6.559 -14.072 -47.521  1.00 43.38      A    O  
ANISOU  256  O   ASN A  29     3429   6873   6181   1366   -304    641  A    O  
ATOM    257  CB  ASN A  29       4.373 -13.430 -45.985  1.00 51.72      A    C  
ANISOU  257  CB  ASN A  29     3898   8092   7661   1801     81    871  A    C  
ATOM    258  CG  ASN A  29       3.219 -13.682 -45.053  1.00 64.17      A    C  
ANISOU  258  CG  ASN A  29     5160   9812   9409   1822    279    840  A    C  
ATOM    259  ND2 ASN A  29       2.136 -12.930 -45.230  1.00 72.08      A    N  
ANISOU  259  ND2 ASN A  29     5911  10965  10510   2071    341   1111  A    N  
ATOM    260  OD1 ASN A  29       3.290 -14.552 -44.190  1.00 65.86      A    O  
ANISOU  260  OD1 ASN A  29     5535   9882   9607   1498    365    517  A    O  
ATOM    261  N   ASP A  30       8.021 -13.278 -46.003  1.00 43.54      A    N  
ANISOU  261  N   ASP A  30     4133   6017   6391   1503     65    465  A    N  
ATOM    262  CA  ASP A  30       9.120 -13.088 -46.945  1.00 39.27      A    C  
ANISOU  262  CA  ASP A  30     3822   5401   5696   1463    -90    502  A    C  
ATOM    263  C   ASP A  30      10.360 -13.891 -46.581  1.00 37.30      A    C  
ANISOU  263  C   ASP A  30     3887   4936   5348   1168    -94    276  A    C  
ATOM    264  O   ASP A  30      11.422 -13.314 -46.350  1.00 38.48      A    O  
ANISOU  264  O   ASP A  30     4328   4829   5463   1182    -20    273  A    O  
ATOM    265  CB  ASP A  30       9.480 -11.598 -47.009  1.00 51.15      A    C  
ANISOU  265  CB  ASP A  30     5525   6602   7307   1790     93    698  A    C  
ATOM    266  CG  ASP A  30       9.876 -11.027 -45.638  1.00 57.85      A    C  
ANISOU  266  CG  ASP A  30     6691   7021   8267   1761    447    515  A    C  
ATOM    267  OD1 ASP A  30       9.497 -11.614 -44.593  1.00 51.72      A    O  
ANISOU  267  OD1 ASP A  30     5865   6269   7517   1604    545    339  A    O  
ATOM    268  OD2 ASP A  30      10.578  -9.994 -45.607  1.00 62.82      A    O1-
ANISOU  268  OD2 ASP A  30     7633   7317   8919   1829    653    528  A    O1-
ATOM    269  N   PRO A  31      10.250 -15.230 -46.526  1.00 31.43      A    N  
ANISOU  269  N   PRO A  31     3069   4303   4571    895   -132    119  A    N  
ATOM    270  CA  PRO A  31      11.448 -15.960 -46.108  1.00 25.04      A    C  
ANISOU  270  CA  PRO A  31     2510   3263   3740    729    -54     41  A    C  
ATOM    271  C   PRO A  31      12.609 -15.851 -47.102  1.00 27.22      A    C  
ANISOU  271  C   PRO A  31     2968   3468   3905    711   -142     72  A    C  
ATOM    272  O   PRO A  31      13.767 -15.850 -46.680  1.00 27.02      A    O  
ANISOU  272  O   PRO A  31     3125   3279   3864    697    -76    123  A    O  
ATOM    273  CB  PRO A  31      10.959 -17.408 -46.013  1.00 29.38      A    C  
ANISOU  273  CB  PRO A  31     2954   3863   4346    481     32    -95  A    C  
ATOM    274  CG  PRO A  31       9.796 -17.472 -46.929  1.00 31.35      A    C  
ANISOU  274  CG  PRO A  31     2929   4463   4520    385    -99   -166  A    C  
ATOM    275  CD  PRO A  31       9.122 -16.135 -46.800  1.00 32.84      A    C  
ANISOU  275  CD  PRO A  31     2943   4797   4738    706   -181     29  A    C  
ATOM    276  N   LEU A  32      12.324 -15.771 -48.397  1.00 26.76      A    N  
ANISOU  276  N   LEU A  32     2825   3609   3732    681   -289     65  A    N  
ATOM    277  CA  LEU A  32      13.437 -15.811 -49.354  1.00 27.87      A    C  
ANISOU  277  CA  LEU A  32     3152   3683   3753    615   -328     58  A    C  
ATOM    278  C   LEU A  32      14.335 -14.573 -49.215  1.00 23.24      A    C  
ANISOU  278  C   LEU A  32     2755   2930   3147    812   -341    214  A    C  
ATOM    279  O   LEU A  32      15.544 -14.736 -49.050  1.00 25.04      A    O  
ANISOU  279  O   LEU A  32     3151   3002   3360    756   -272    217  A    O  
ATOM    280  CB  LEU A  32      12.934 -15.967 -50.795  1.00 28.78      A    C  
ANISOU  280  CB  LEU A  32     3137   4141   3656    454   -480      6  A    C  
ATOM    281  CG  LEU A  32      14.050 -15.965 -51.855  1.00 29.10      A    C  
ANISOU  281  CG  LEU A  32     3386   4130   3542    359   -487    -26  A    C  
ATOM    282  CD1 LEU A  32      15.045 -17.083 -51.620  1.00 28.59      A    C  
ANISOU  282  CD1 LEU A  32     3523   3735   3605    209   -221   -192  A    C  
ATOM    283  CD2 LEU A  32      13.468 -16.054 -53.264  1.00 34.36      A    C  
ANISOU  283  CD2 LEU A  32     3902   5262   3893    118   -650    -77  A    C  
ATOM    284  N   PRO A  33      13.762 -13.349 -49.240  1.00 28.12      A    N  
ANISOU  284  N   PRO A  33     3332   3569   3783   1036   -368    363  A    N  
ATOM    285  CA  PRO A  33      14.641 -12.181 -49.066  1.00 32.02      A    C  
ANISOU  285  CA  PRO A  33     4079   3817   4270   1138   -269    446  A    C  
ATOM    286  C   PRO A  33      15.367 -12.191 -47.734  1.00 32.05      A    C  
ANISOU  286  C   PRO A  33     4235   3652   4290    995   -110    337  A    C  
ATOM    287  O   PRO A  33      16.526 -11.777 -47.667  1.00 26.64      A    O  
ANISOU  287  O   PRO A  33     3738   2884   3502    881    -67    335  A    O  
ATOM    288  CB  PRO A  33      13.679 -10.990 -49.142  1.00 35.23      A    C  
ANISOU  288  CB  PRO A  33     4415   4178   4795   1438   -175    643  A    C  
ATOM    289  CG  PRO A  33      12.534 -11.486 -49.904  1.00 43.29      A    C  
ANISOU  289  CG  PRO A  33     5075   5595   5779   1507   -366    766  A    C  
ATOM    290  CD  PRO A  33      12.381 -12.928 -49.548  1.00 36.37      A    C  
ANISOU  290  CD  PRO A  33     4093   4862   4865   1213   -433    511  A    C  
ATOM    291  N   ARG A  34      14.708 -12.671 -46.683  1.00 31.69      A    N  
ANISOU  291  N   ARG A  34     4076   3639   4325    953    -30    264  A    N  
ATOM    292  CA  ARG A  34      15.393 -12.827 -45.405  1.00 25.24      A    C  
ANISOU  292  CA  ARG A  34     3342   2817   3430    751     86    208  A    C  
ATOM    293  C   ARG A  34      16.573 -13.777 -45.471  1.00 21.00      A    C  
ANISOU  293  C   ARG A  34     2781   2390   2809    617     11    299  A    C  
ATOM    294  O   ARG A  34      17.645 -13.463 -44.963  1.00 24.99      A    O  
ANISOU  294  O   ARG A  34     3355   2986   3154    457     40    357  A    O  
ATOM    295  CB  ARG A  34      14.426 -13.323 -44.326  1.00 26.55      A    C  
ANISOU  295  CB  ARG A  34     3367   3044   3675    721    184    148  A    C  
ATOM    296  CG  ARG A  34      13.502 -12.260 -43.841  1.00 35.75      A    C  
ANISOU  296  CG  ARG A  34     4577   4075   4931    832    391     68  A    C  
ATOM    297  CD  ARG A  34      12.616 -12.795 -42.720  1.00 40.15      A    C  
ANISOU  297  CD  ARG A  34     4993   4719   5542    764    512     -9  A    C  
ATOM    298  NE  ARG A  34      11.546 -11.857 -42.419  1.00 41.63      A    N  
ANISOU  298  NE  ARG A  34     5171   4752   5896    949    770    -65  A    N  
ATOM    299  CZ  ARG A  34      11.663 -10.852 -41.564  1.00 43.90      A    C  
ANISOU  299  CZ  ARG A  34     5698   4834   6148    842   1117   -220  A    C  
ATOM    300  NH1 ARG A  34      12.808 -10.669 -40.917  1.00 38.10      A    N1+
ANISOU  300  NH1 ARG A  34     5196   4149   5130    468   1167   -348  A    N1+
ATOM    301  NH2 ARG A  34      10.633 -10.042 -41.346  1.00 44.61      A    N  
ANISOU  301  NH2 ARG A  34     5775   4701   6474   1079   1459   -244  A    N  
ATOM    302  N   LEU A  35      16.377 -14.958 -46.055  1.00 21.81      A    N  
ANISOU  302  N   LEU A  35     2765   2502   3017    654    -31    320  A    N  
ATOM    303  CA  LEU A  35      17.469 -15.918 -46.161  1.00 24.69      A    C  
ANISOU  303  CA  LEU A  35     3106   2876   3401    611     26    459  A    C  
ATOM    304  C   LEU A  35      18.589 -15.366 -47.042  1.00 22.76      A    C  
ANISOU  304  C   LEU A  35     2972   2626   3051    613    -30    505  A    C  
ATOM    305  O   LEU A  35      19.769 -15.584 -46.760  1.00 23.39      A    O  
ANISOU  305  O   LEU A  35     3004   2802   3080    576     19    691  A    O  
ATOM    306  CB  LEU A  35      16.991 -17.252 -46.739  1.00 23.41      A    C  
ANISOU  306  CB  LEU A  35     2885   2596   3414    608    139    395  A    C  
ATOM    307  CG  LEU A  35      16.667 -18.483 -45.901  1.00 42.02      A    C  
ANISOU  307  CG  LEU A  35     5143   4879   5943    583    345    481  A    C  
ATOM    308  CD1 LEU A  35      16.863 -19.674 -46.826  1.00 42.87      A    C  
ANISOU  308  CD1 LEU A  35     5317   4748   6225    537    592    405  A    C  
ATOM    309  CD2 LEU A  35      17.519 -18.623 -44.621  1.00 27.79      A    C  
ANISOU  309  CD2 LEU A  35     3239   3213   4106    623    410    822  A    C  
ATOM    310  N   GLN A  36      18.218 -14.665 -48.113  1.00 23.75      A    N  
ANISOU  310  N   GLN A  36     3198   2695   3129    662   -126    392  A    N  
ATOM    311  CA  GLN A  36      19.240 -14.113 -49.005  1.00 25.92      A    C  
ANISOU  311  CA  GLN A  36     3598   2957   3292    647   -162    433  A    C  
ATOM    312  C   GLN A  36      20.050 -13.015 -48.324  1.00 27.51      A    C  
ANISOU  312  C   GLN A  36     3900   3196   3355    545   -140    489  A    C  
ATOM    313  O   GLN A  36      21.246 -12.891 -48.576  1.00 23.96      A    O  
ANISOU  313  O   GLN A  36     3474   2823   2806    456   -129    574  A    O  
ATOM    314  CB  GLN A  36      18.611 -13.587 -50.291  1.00 22.30      A    C  
ANISOU  314  CB  GLN A  36     3203   2499   2771    713   -270    374  A    C  
ATOM    315  CG  GLN A  36      18.010 -14.703 -51.114  1.00 21.66      A    C  
ANISOU  315  CG  GLN A  36     3027   2499   2705    638   -275    253  A    C  
ATOM    316  CD  GLN A  36      17.661 -14.260 -52.509  1.00 25.15      A    C  
ANISOU  316  CD  GLN A  36     3483   3116   2956    609   -412    245  A    C  
ATOM    317  NE2 GLN A  36      18.115 -15.015 -53.502  1.00 23.97      A    N  
ANISOU  317  NE2 GLN A  36     3392   3013   2703    422   -342    110  A    N  
ATOM    318  OE1 GLN A  36      17.002 -13.241 -52.698  1.00 26.96      A    O  
ANISOU  318  OE1 GLN A  36     3667   3447   3129    757   -536    391  A    O  
ATOM    319  N   ASP A  37      19.407 -12.237 -47.453  1.00 21.35      A    N  
ANISOU  319  N   ASP A  37     3180   2374   2558    509    -83    413  A    N  
ATOM    320  CA  ASP A  37      20.111 -11.222 -46.687  1.00 23.71      A    C  
ANISOU  320  CA  ASP A  37     3621   2709   2679    268     30    363  A    C  
ATOM    321  C   ASP A  37      21.169 -11.909 -45.811  1.00 27.40      A    C  
ANISOU  321  C   ASP A  37     3896   3537   2979     42     -1    505  A    C  
ATOM    322  O   ASP A  37      22.345 -11.529 -45.807  1.00 24.02      A    O  
ANISOU  322  O   ASP A  37     3465   3311   2352   -178     -3    570  A    O  
ATOM    323  CB  ASP A  37      19.105 -10.413 -45.858  1.00 25.02      A    C  
ANISOU  323  CB  ASP A  37     3908   2709   2889    248    215    204  A    C  
ATOM    324  CG  ASP A  37      19.756  -9.444 -44.896  1.00 30.63      A    C  
ANISOU  324  CG  ASP A  37     4812   3459   3366   -149    434     40  A    C  
ATOM    325  OD1 ASP A  37      20.798  -8.841 -45.209  1.00 29.63      A    O  
ANISOU  325  OD1 ASP A  37     4819   3368   3072   -372    471     20  A    O  
ATOM    326  OD2 ASP A  37      19.211  -9.290 -43.792  1.00 35.46      A    O1-
ANISOU  326  OD2 ASP A  37     5449   4096   3929   -307    601   -104  A    O1-
ATOM    327  N   TYR A  38      20.744 -12.939 -45.087  1.00 23.80      A    N  
ANISOU  327  N   TYR A  38     3437   2335   3270    493    137    446  A    N  
ATOM    328  CA  TYR A  38      21.667 -13.757 -44.301  1.00 24.03      A    C  
ANISOU  328  CA  TYR A  38     3553   2422   3153    396    131    294  A    C  
ATOM    329  C   TYR A  38      22.808 -14.338 -45.141  1.00 24.41      A    C  
ANISOU  329  C   TYR A  38     3594   2551   3129    350    127    411  A    C  
ATOM    330  O   TYR A  38      23.979 -14.237 -44.774  1.00 23.14      A    O  
ANISOU  330  O   TYR A  38     3416   2307   3070    284    111    389  A    O  
ATOM    331  CB  TYR A  38      20.903 -14.903 -43.637  1.00 22.90      A    C  
ANISOU  331  CB  TYR A  38     3457   2425   2818    376    131    161  A    C  
ATOM    332  CG  TYR A  38      19.933 -14.480 -42.554  1.00 21.55      A    C  
ANISOU  332  CG  TYR A  38     3300   2198   2691    378    216    -20  A    C  
ATOM    333  CD1 TYR A  38      19.931 -13.191 -42.042  1.00 21.65      A    C  
ANISOU  333  CD1 TYR A  38     3301   2008   2915    391    289   -136  A    C  
ATOM    334  CD2 TYR A  38      19.022 -15.395 -42.038  1.00 24.28      A    C  
ANISOU  334  CD2 TYR A  38     3659   2677   2888    349    263   -101  A    C  
ATOM    335  CE1 TYR A  38      19.039 -12.824 -41.011  1.00 28.13      A    C  
ANISOU  335  CE1 TYR A  38     4135   2774   3778    379    449   -383  A    C  
ATOM    336  CE2 TYR A  38      18.148 -15.046 -41.021  1.00 24.49      A    C  
ANISOU  336  CE2 TYR A  38     3692   2675   2937    326    420   -295  A    C  
ATOM    337  CZ  TYR A  38      18.145 -13.773 -40.519  1.00 26.66      A    C  
ANISOU  337  CZ  TYR A  38     3964   2765   3402    344    532   -457  A    C  
ATOM    338  OH  TYR A  38      17.247 -13.467 -39.497  1.00 28.94      A    O  
ANISOU  338  OH  TYR A  38     4259   3028   3709    308    767   -720  A    O  
ATOM    339  N   ALA A  39      22.446 -14.988 -46.248  1.00 23.77      A    N  
ANISOU  339  N   ALA A  39     3513   2636   2883    370    149    507  A    N  
ATOM    340  CA  ALA A  39      23.419 -15.641 -47.120  1.00 22.39      A    C  
ANISOU  340  CA  ALA A  39     3333   2552   2621    319    231    544  A    C  
ATOM    341  C   ALA A  39      24.404 -14.641 -47.719  1.00 27.35      A    C  
ANISOU  341  C   ALA A  39     3914   3094   3382    277    317    706  A    C  
ATOM    342  O   ALA A  39      25.618 -14.886 -47.724  1.00 28.88      A    O  
ANISOU  342  O   ALA A  39     4039   3244   3690    227    404    676  A    O  
ATOM    343  CB  ALA A  39      22.701 -16.406 -48.253  1.00 22.96      A    C  
ANISOU  343  CB  ALA A  39     3457   2837   2429    305    251    565  A    C  
ATOM    344  N   ALA A  40      23.881 -13.535 -48.249  1.00 24.27      A    N  
ANISOU  344  N   ALA A  40     3530   2660   3033    292    290    906  A    N  
ATOM    345  CA  ALA A  40      24.713 -12.505 -48.874  1.00 23.91      A    C  
ANISOU  345  CA  ALA A  40     3443   2513   3129    229    371   1125  A    C  
ATOM    346  C   ALA A  40      25.727 -11.926 -47.887  1.00 31.17      A    C  
ANISOU  346  C   ALA A  40     4274   3190   4380    197    369   1031  A    C  
ATOM    347  O   ALA A  40      26.839 -11.573 -48.277  1.00 26.73      A    O  
ANISOU  347  O   ALA A  40     3631   2566   3958    112    477   1135  A    O  
ATOM    348  CB  ALA A  40      23.857 -11.390 -49.447  1.00 25.86      A    C  
ANISOU  348  CB  ALA A  40     3692   2687   3447    258    279   1405  A    C  
ATOM    349  N   GLN A  41      25.349 -11.833 -46.611  1.00 27.84      A    N  
ANISOU  349  N   GLN A  41     3867   2645   4068    235    252    825  A    N  
ATOM    350  CA  GLN A  41      26.269 -11.308 -45.597  1.00 29.71      A    C  
ANISOU  350  CA  GLN A  41     4053   2678   4556    157    191    700  A    C  
ATOM    351  C   GLN A  41      27.352 -12.313 -45.214  1.00 30.87      A    C  
ANISOU  351  C   GLN A  41     4137   2897   4694     91    157    611  A    C  
ATOM    352  O   GLN A  41      28.311 -11.961 -44.524  1.00 33.68      A    O  
ANISOU  352  O   GLN A  41     4415   3110   5273     -5     60    559  A    O  
ATOM    353  CB  GLN A  41      25.509 -10.868 -44.339  1.00 25.37      A    C  
ANISOU  353  CB  GLN A  41     3582   2006   4052    171    101    469  A    C  
ATOM    354  CG  GLN A  41      24.638  -9.640 -44.551  1.00 29.25      A    C  
ANISOU  354  CG  GLN A  41     4053   2294   4766    247    143    527  A    C  
ATOM    355  CD  GLN A  41      24.043  -9.145 -43.251  1.00 34.93      A    C  
ANISOU  355  CD  GLN A  41     4835   2858   5579    240    141    207  A    C  
ATOM    356  NE2 GLN A  41      22.719  -9.198 -43.140  1.00 35.34      A    N  
ANISOU  356  NE2 GLN A  41     4886   2936   5607    355    209    135  A    N  
ATOM    357  OE1 GLN A  41      24.768  -8.723 -42.356  1.00 32.70      A    O  
ANISOU  357  OE1 GLN A  41     4593   2441   5389    113     89      7  A    O  
ATOM    358  N   GLY A  42      27.205 -13.561 -45.654  1.00 24.01      A    N  
ANISOU  358  N   GLY A  42     3279   2220   3623    135    213    595  A    N  
ATOM    359  CA  GLY A  42      28.278 -14.528 -45.504  1.00 24.43      A    C  
ANISOU  359  CA  GLY A  42     3209   2285   3790    100    208    552  A    C  
ATOM    360  C   GLY A  42      27.996 -15.741 -44.636  1.00 28.83      A    C  
ANISOU  360  C   GLY A  42     3808   2899   4248    116     60    432  A    C  
ATOM    361  O   GLY A  42      28.916 -16.503 -44.359  1.00 28.74      A    O  
ANISOU  361  O   GLY A  42     3657   2833   4430     94     -4    432  A    O  
ATOM    362  N   ALA A  43      26.748 -15.924 -44.203  1.00 30.25      A    N  
ANISOU  362  N   ALA A  43     4148   3165   4182    149      6    361  A    N  
ATOM    363  CA  ALA A  43      26.363 -17.101 -43.408  1.00 29.29      A    C  
ANISOU  363  CA  ALA A  43     4083   3105   3943    138   -115    294  A    C  
ATOM    364  C   ALA A  43      26.838 -18.389 -44.053  1.00 29.10      A    C  
ANISOU  364  C   ALA A  43     3948   3096   4014    179    -47    305  A    C  
ATOM    365  O   ALA A  43      26.569 -18.640 -45.221  1.00 26.09      A    O  
ANISOU  365  O   ALA A  43     3562   2796   3556    231    142    281  A    O  
ATOM    366  CB  ALA A  43      24.846 -17.155 -43.214  1.00 25.89      A    C  
ANISOU  366  CB  ALA A  43     3793   2783   3262    171    -84    228  A    C  
ATOM    367  N   GLY A  44      27.534 -19.220 -43.289  1.00 26.45      A    N  
ANISOU  367  N   GLY A  44     3525   2670   3855    142   -213    337  A    N  
ATOM    368  CA  GLY A  44      28.099 -20.433 -43.850  1.00 32.30      A    C  
ANISOU  368  CA  GLY A  44     4106   3337   4832    199   -132    324  A    C  
ATOM    369  C   GLY A  44      27.122 -21.591 -43.956  1.00 30.24      A    C  
ANISOU  369  C   GLY A  44     3935   3125   4430    229   -109    258  A    C  
ATOM    370  O   GLY A  44      27.329 -22.492 -44.759  1.00 25.16      A    O  
ANISOU  370  O   GLY A  44     3196   2426   3940    283     50    161  A    O  
ATOM    371  N   VAL A  45      26.099 -21.586 -43.108  1.00 25.12      A    N  
ANISOU  371  N   VAL A  45     3457   2563   3524    175   -243    286  A    N  
ATOM    372  CA  VAL A  45      25.029 -22.588 -43.113  1.00 25.39      A    C  
ANISOU  372  CA  VAL A  45     3571   2646   3432    172   -228    245  A    C  
ATOM    373  C   VAL A  45      23.749 -21.856 -42.720  1.00 22.97      A    C  
ANISOU  373  C   VAL A  45     3427   2498   2801    137   -215    220  A    C  
ATOM    374  O   VAL A  45      23.810 -20.873 -41.989  1.00 25.41      A    O  
ANISOU  374  O   VAL A  45     3804   2831   3020     90   -272    238  A    O  
ATOM    375  CB  VAL A  45      25.301 -23.773 -42.125  1.00 26.67      A    C  
ANISOU  375  CB  VAL A  45     3692   2671   3771    110   -438    380  A    C  
ATOM    376  CG1 VAL A  45      24.115 -24.686 -42.038  1.00 25.12      A    C  
ANISOU  376  CG1 VAL A  45     3581   2512   3450     75   -415    361  A    C  
ATOM    377  CG2 VAL A  45      26.511 -24.583 -42.547  1.00 30.18      A    C  
ANISOU  377  CG2 VAL A  45     3902   2888   4679    179   -439    398  A    C  
ATOM    378  N   LEU A  46      22.606 -22.304 -43.233  1.00 21.59      A    N  
ANISOU  378  N   LEU A  46     3289   2413   2503    153   -128    151  A    N  
ATOM    379  CA  LEU A  46      21.299 -21.762 -42.874  1.00 22.43      A    C  
ANISOU  379  CA  LEU A  46     3472   2639   2411    133    -94    128  A    C  
ATOM    380  C   LEU A  46      20.408 -22.872 -42.323  1.00 26.72      A    C  
ANISOU  380  C   LEU A  46     4036   3201   2914     55   -120    144  A    C  
ATOM    381  O   LEU A  46      20.360 -23.980 -42.878  1.00 26.50      A    O  
ANISOU  381  O   LEU A  46     3958   3118   2995     52   -128    120  A    O  
ATOM    382  CB  LEU A  46      20.635 -21.114 -44.103  1.00 19.65      A    C  
ANISOU  382  CB  LEU A  46     3088   2380   1998    210     -1     84  A    C  
ATOM    383  CG  LEU A  46      21.466 -19.961 -44.670  1.00 22.64      A    C  
ANISOU  383  CG  LEU A  46     3451   2730   2420    260     39    127  A    C  
ATOM    384  CD1 LEU A  46      21.053 -19.721 -46.113  1.00 23.01      A    C  
ANISOU  384  CD1 LEU A  46     3486   2886   2370    291     93    151  A    C  
ATOM    385  CD2 LEU A  46      21.249 -18.696 -43.860  1.00 23.83      A    C  
ANISOU  385  CD2 LEU A  46     3629   2834   2592    267     33    138  A    C  
ATOM    386  N   HIS A  47      19.713 -22.573 -41.231  1.00 23.26      A    N  
ANISOU  386  N   HIS A  47     3674   2830   2332    -27   -103    164  A    N  
ATOM    387  CA  HIS A  47      18.875 -23.550 -40.532  1.00 23.56      A    C  
ANISOU  387  CA  HIS A  47     3739   2899   2315   -145    -95    222  A    C  
ATOM    388  C   HIS A  47      17.392 -23.187 -40.691  1.00 26.37      A    C  
ANISOU  388  C   HIS A  47     4032   3365   2625   -133     63    131  A    C  
ATOM    389  O   HIS A  47      16.992 -22.064 -40.396  1.00 26.17      A    O  
ANISOU  389  O   HIS A  47     4010   3391   2543    -99    177     49  A    O  
ATOM    390  CB  HIS A  47      19.280 -23.598 -39.049  1.00 19.42      A    C  
ANISOU  390  CB  HIS A  47     3361   2397   1621   -307   -175    339  A    C  
ATOM    391  CG  HIS A  47      18.495 -24.570 -38.216  1.00 23.23      A    C  
ANISOU  391  CG  HIS A  47     3900   2927   2002   -475   -152    463  A    C  
ATOM    392  CD2 HIS A  47      17.536 -24.367 -37.279  1.00 28.08      A    C  
ANISOU  392  CD2 HIS A  47     4606   3689   2376   -621     18    444  A    C  
ATOM    393  ND1 HIS A  47      18.719 -25.930 -38.241  1.00 29.85      A    N  
ANISOU  393  ND1 HIS A  47     4695   3632   3016   -531   -289    642  A    N  
ATOM    394  CE1 HIS A  47      17.915 -26.525 -37.373  1.00 34.51      A    C  
ANISOU  394  CE1 HIS A  47     5356   4291   3466   -714   -232    773  A    C  
ATOM    395  NE2 HIS A  47      17.189 -25.601 -36.771  1.00 29.56      A    N  
ANISOU  395  NE2 HIS A  47     4816   3858   2558   -780    -26    649  A    N  
ATOM    396  N   LEU A  48      16.591 -24.128 -41.185  1.00 23.77      A    N  
ANISOU  396  N   LEU A  48     3610   3035   2388   -160     65    135  A    N  
ATOM    397  CA  LEU A  48      15.148 -23.936 -41.285  1.00 22.58      A    C  
ANISOU  397  CA  LEU A  48     3334   2972   2274   -169    182     81  A    C  
ATOM    398  C   LEU A  48      14.409 -24.986 -40.490  1.00 27.34      A    C  
ANISOU  398  C   LEU A  48     3922   3580   2887   -336    244    158  A    C  
ATOM    399  O   LEU A  48      14.751 -26.169 -40.542  1.00 27.03      A    O  
ANISOU  399  O   LEU A  48     3906   3438   2926   -414    135    243  A    O  
ATOM    400  CB  LEU A  48      14.679 -24.010 -42.741  1.00 23.97      A    C  
ANISOU  400  CB  LEU A  48     3378   3168   2563    -89     92     24  A    C  
ATOM    401  CG  LEU A  48      15.361 -23.105 -43.753  1.00 27.90      A    C  
ANISOU  401  CG  LEU A  48     3897   3680   3022     38     26      3  A    C  
ATOM    402  CD1 LEU A  48      14.802 -23.399 -45.134  1.00 24.77      A    C  
ANISOU  402  CD1 LEU A  48     3421   3359   2633     37    -93    -30  A    C  
ATOM    403  CD2 LEU A  48      15.143 -21.648 -43.384  1.00 26.95      A    C  
ANISOU  403  CD2 LEU A  48     3744   3570   2925    129    112     14  A    C  
ATOM    404  N   VAL A  49      13.377 -24.566 -39.763  1.00 23.41      A    N  
ANISOU  404  N   VAL A  49     3362   3176   2357   -398    449    127  A    N  
ATOM    405  CA  VAL A  49      12.463 -25.519 -39.166  1.00 24.24      A    C  
ANISOU  405  CA  VAL A  49     3403   3303   2504   -574    557    210  A    C  
ATOM    406  C   VAL A  49      11.089 -25.382 -39.836  1.00 31.38      A    C  
ANISOU  406  C   VAL A  49     4018   4239   3664   -530    634    127  A    C  
ATOM    407  O   VAL A  49      10.487 -24.303 -39.835  1.00 29.30      A    O  
ANISOU  407  O   VAL A  49     3621   4027   3484   -428    781     22  A    O  
ATOM    408  CB  VAL A  49      12.333 -25.315 -37.652  1.00 33.08      A    C  
ANISOU  408  CB  VAL A  49     4675   4532   3363   -750    785    254  A    C  
ATOM    409  CG1 VAL A  49      11.387 -26.353 -37.066  1.00 34.89      A    C  
ANISOU  409  CG1 VAL A  49     4834   4790   3633   -966    927    388  A    C  
ATOM    410  CG2 VAL A  49      13.715 -25.398 -36.981  1.00 33.55      A    C  
ANISOU  410  CG2 VAL A  49     5009   4574   3162   -821    615    375  A    C  
ATOM    411  N   ASP A  50      10.624 -26.474 -40.439  1.00 29.17      A    N  
ANISOU  411  N   ASP A  50     3620   3898   3565   -607    506    171  A    N  
ATOM    412  CA  ASP A  50       9.329 -26.503 -41.110  1.00 27.96      A    C  
ANISOU  412  CA  ASP A  50     3166   3773   3684   -608    495    120  A    C  
ATOM    413  C   ASP A  50       8.282 -27.024 -40.144  1.00 30.09      A    C  
ANISOU  413  C   ASP A  50     3291   4068   4073   -794    747    189  A    C  
ATOM    414  O   ASP A  50       8.086 -28.235 -40.016  1.00 32.86      A    O  
ANISOU  414  O   ASP A  50     3632   4339   4515   -971    702    288  A    O  
ATOM    415  CB  ASP A  50       9.395 -27.377 -42.360  1.00 28.88      A    C  
ANISOU  415  CB  ASP A  50     3243   3817   3913   -632    204     78  A    C  
ATOM    416  CG  ASP A  50       8.037 -27.610 -42.987  1.00 31.21      A    C  
ANISOU  416  CG  ASP A  50     3226   4145   4489   -701    117     50  A    C  
ATOM    417  OD1 ASP A  50       7.095 -26.822 -42.721  1.00 34.14      A    O  
ANISOU  417  OD1 ASP A  50     3354   4588   5030   -652    250     68  A    O  
ATOM    418  OD2 ASP A  50       7.919 -28.579 -43.770  1.00 35.17      A    O1-
ANISOU  418  OD2 ASP A  50     3703   4579   5080   -810    -92    -11  A    O1-
ATOM    419  N   LEU A  51       7.613 -26.103 -39.456  1.00 31.68      A    N  
ANISOU  419  N   LEU A  51     3370   4358   4308   -765   1048    126  A    N  
ATOM    420  CA  LEU A  51       6.646 -26.478 -38.438  1.00 35.01      A    C  
ANISOU  420  CA  LEU A  51     3661   4837   4806   -961   1394    169  A    C  
ATOM    421  C   LEU A  51       5.347 -27.012 -39.038  1.00 40.34      A    C  
ANISOU  421  C   LEU A  51     3928   5472   5927  -1022   1357    188  A    C  
ATOM    422  O   LEU A  51       4.610 -27.734 -38.377  1.00 40.14      A    O  
ANISOU  422  O   LEU A  51     3780   5458   6013  -1238   1581    276  A    O  
ATOM    423  CB  LEU A  51       6.352 -25.289 -37.522  1.00 38.92      A    C  
ANISOU  423  CB  LEU A  51     4143   5428   5218   -915   1801     14  A    C  
ATOM    424  CG  LEU A  51       7.579 -24.827 -36.741  1.00 43.33      A    C  
ANISOU  424  CG  LEU A  51     5120   6044   5301   -934   1839    -17  A    C  
ATOM    425  CD1 LEU A  51       7.354 -23.444 -36.169  1.00 46.91      A    C  
ANISOU  425  CD1 LEU A  51     5547   6539   5738   -839   2183   -273  A    C  
ATOM    426  CD2 LEU A  51       7.875 -25.835 -35.642  1.00 44.02      A    C  
ANISOU  426  CD2 LEU A  51     5474   6215   5036  -1235   1934    176  A    C  
ATOM    427  N   THR A  52       5.067 -26.665 -40.289  1.00 36.51      A    N  
ANISOU  427  N   THR A  52     3233   4951   5689   -864   1053    132  A    N  
ATOM    428  CA  THR A  52       3.885 -27.207 -40.954  1.00 42.18      A    C  
ANISOU  428  CA  THR A  52     3559   5637   6831   -951    910    159  A    C  
ATOM    429  C   THR A  52       4.055 -28.704 -41.180  1.00 39.16      A    C  
ANISOU  429  C   THR A  52     3282   5161   6435  -1169    717    228  A    C  
ATOM    430  O   THR A  52       3.173 -29.500 -40.854  1.00 42.09      A    O  
ANISOU  430  O   THR A  52     3427   5487   7078  -1375    824    298  A    O  
ATOM    431  CB  THR A  52       3.616 -26.511 -42.298  1.00 42.83      A    C  
ANISOU  431  CB  THR A  52     3438   5730   7107   -774    536    127  A    C  
ATOM    432  CG2 THR A  52       2.451 -27.180 -43.006  1.00 43.94      A    C  
ANISOU  432  CG2 THR A  52     3190   5850   7655   -914    296    165  A    C  
ATOM    433  OG1 THR A  52       3.296 -25.132 -42.067  1.00 43.63      A    O  
ANISOU  433  OG1 THR A  52     3355   5842   7381   -567    721     93  A    O  
ATOM    434  N   GLY A  53       5.206 -29.078 -41.728  1.00 39.31      A    N  
ANISOU  434  N   GLY A  53     3667   6078   5193   -433    607    450  A    N  
ATOM    435  CA  GLY A  53       5.555 -30.472 -41.925  1.00 41.05      A    C  
ANISOU  435  CA  GLY A  53     3960   6203   5435   -708    311    502  A    C  
ATOM    436  C   GLY A  53       5.729 -31.235 -40.625  1.00 40.54      A    C  
ANISOU  436  C   GLY A  53     4052   6127   5224   -904    471    630  A    C  
ATOM    437  O   GLY A  53       5.462 -32.432 -40.574  1.00 45.31      A    O  
ANISOU  437  O   GLY A  53     4600   6662   5954  -1150    352    775  A    O  
ATOM    438  N   ALA A  54       6.174 -30.551 -39.572  1.00 37.51      A    N  
ANISOU  438  N   ALA A  54     3912   5794   4545   -837    733    586  A    N  
ATOM    439  CA  ALA A  54       6.323 -31.186 -38.262  1.00 38.76      A    C  
ANISOU  439  CA  ALA A  54     4264   5995   4467  -1052    877    749  A    C  
ATOM    440  C   ALA A  54       4.982 -31.666 -37.720  1.00 46.14      A    C  
ANISOU  440  C   ALA A  54     4917   7062   5552  -1196   1172    956  A    C  
ATOM    441  O   ALA A  54       4.911 -32.675 -37.022  1.00 48.86      A    O  
ANISOU  441  O   ALA A  54     5327   7397   5841  -1446   1182   1176  A    O  
ATOM    442  CB  ALA A  54       6.969 -30.229 -37.266  1.00 40.79      A    C  
ANISOU  442  CB  ALA A  54     4892   6319   4289  -1022   1089    630  A    C  
ATOM    443  N   LYS A  55       3.921 -30.934 -38.039  1.00 48.46      A    N  
ANISOU  443  N   LYS A  55     4864   7478   6072  -1028   1427    935  A    N  
ATOM    444  CA  LYS A  55       2.595 -31.288 -37.565  1.00 53.11      A    C  
ANISOU  444  CA  LYS A  55     5068   8233   6877  -1140   1759   1172  A    C  
ATOM    445  C   LYS A  55       1.998 -32.403 -38.424  1.00 52.73      A    C  
ANISOU  445  C   LYS A  55     4645   8171   7218  -1393   1394   1351  A    C  
ATOM    446  O   LYS A  55       1.282 -33.265 -37.921  1.00 53.54      A    O  
ANISOU  446  O   LYS A  55     4553   8339   7451  -1674   1516   1598  A    O  
ATOM    447  CB  LYS A  55       1.682 -30.060 -37.552  1.00 54.55      A    C  
ANISOU  447  CB  LYS A  55     4952   8546   7229   -816   2215   1144  A    C  
ATOM    448  CG  LYS A  55       0.467 -30.225 -36.634  1.00 71.94      A    C  
ANISOU  448  CG  LYS A  55     6833  10939   9563   -879   2780   1389  A    C  
ATOM    449  CD  LYS A  55      -0.138 -28.890 -36.207  1.00 85.85      A    C  
ANISOU  449  CD  LYS A  55     8603  12693  11324   -498   3303   1221  A    C  
ATOM    450  CE  LYS A  55      -0.855 -28.195 -37.355  1.00 93.59      A    C  
ANISOU  450  CE  LYS A  55     9079  13685  12798   -176   3146   1275  A    C  
ATOM    451  NZ  LYS A  55      -1.476 -26.908 -36.924  1.00100.19      A    N1+
ANISOU  451  NZ  LYS A  55     9945  14441  13683    224   3632   1157  A    N1+
ATOM    452  N   ASP A  56       2.319 -32.393 -39.715  1.00 52.19      A    N  
ANISOU  452  N   ASP A  56     4531   8003   7294  -1342    953   1219  A    N  
ATOM    453  CA  ASP A  56       1.819 -33.396 -40.653  1.00 53.43      A    C  
ANISOU  453  CA  ASP A  56     4449   8114   7739  -1646    561   1312  A    C  
ATOM    454  C   ASP A  56       2.793 -33.546 -41.822  1.00 53.65      A    C  
ANISOU  454  C   ASP A  56     4785   7917   7682  -1611    122   1067  A    C  
ATOM    455  O   ASP A  56       2.812 -32.710 -42.726  1.00 50.45      A    O  
ANISOU  455  O   ASP A  56     4292   7584   7293  -1404    -21    949  A    O  
ATOM    456  CB  ASP A  56       0.416 -33.009 -41.145  1.00 62.61      A    C  
ANISOU  456  CB  ASP A  56     4962   9559   9269  -1655    588   1509  A    C  
ATOM    457  CG  ASP A  56      -0.136 -33.967 -42.195  1.00 69.74      A    C  
ANISOU  457  CG  ASP A  56     5682  10425  10390  -2039     96   1559  A    C  
ATOM    458  OD1 ASP A  56       0.446 -35.055 -42.395  1.00 68.52      A    O  
ANISOU  458  OD1 ASP A  56     5878  10002  10154  -2351   -152   1471  A    O  
ATOM    459  OD2 ASP A  56      -1.179 -33.636 -42.801  1.00 75.04      A    O1-
ANISOU  459  OD2 ASP A  56     5964  11275  11271  -1990    -25   1649  A    O1-
ATOM    460  N   PRO A  57       3.605 -34.617 -41.805  1.00 56.14      A    N  
ANISOU  460  N   PRO A  57     5470   7941   7919  -1794    -49   1019  A    N  
ATOM    461  CA  PRO A  57       4.656 -34.853 -42.808  1.00 51.78      A    C  
ANISOU  461  CA  PRO A  57     5263   7125   7287  -1726   -340    783  A    C  
ATOM    462  C   PRO A  57       4.135 -34.875 -44.248  1.00 49.92      A    C  
ANISOU  462  C   PRO A  57     4904   6908   7153  -1860   -665    659  A    C  
ATOM    463  O   PRO A  57       4.907 -34.608 -45.176  1.00 49.38      A    O  
ANISOU  463  O   PRO A  57     5091   6719   6952  -1718   -823    438  A    O  
ATOM    464  CB  PRO A  57       5.233 -36.221 -42.407  1.00 54.64      A    C  
ANISOU  464  CB  PRO A  57     5934   7143   7685  -1931   -374    860  A    C  
ATOM    465  CG  PRO A  57       4.224 -36.820 -41.470  1.00 60.82      A    C  
ANISOU  465  CG  PRO A  57     6492   8021   8595  -2222   -206   1145  A    C  
ATOM    466  CD  PRO A  57       3.586 -35.666 -40.773  1.00 60.83      A    C  
ANISOU  466  CD  PRO A  57     6183   8414   8516  -2042     90   1230  A    C  
ATOM    467  N   ALA A  58       2.848 -35.159 -44.430  1.00 55.09      A    N  
ANISOU  467  N   ALA A  58     5165   7747   8019  -2158   -769    827  A    N  
ATOM    468  CA  ALA A  58       2.236 -35.096 -45.754  1.00 60.73      A    C  
ANISOU  468  CA  ALA A  58     5717   8575   8782  -2354  -1156    773  A    C  
ATOM    469  C   ALA A  58       2.237 -33.663 -46.278  1.00 59.41      A    C  
ANISOU  469  C   ALA A  58     5366   8663   8543  -1964  -1169    760  A    C  
ATOM    470  O   ALA A  58       2.187 -33.434 -47.488  1.00 57.19      A    O  
ANISOU  470  O   ALA A  58     5125   8440   8166  -2025  -1507    675  A    O  
ATOM    471  CB  ALA A  58       0.817 -35.646 -45.718  1.00 64.23      A    C  
ANISOU  471  CB  ALA A  58     5776   9178   9452  -2660  -1228    978  A    C  
ATOM    472  N   LYS A  59       2.300 -32.703 -45.360  1.00 53.18      A    N  
ANISOU  472  N   LYS A  59     4435   7999   7771  -1586   -786    846  A    N  
ATOM    473  CA  LYS A  59       2.252 -31.292 -45.724  1.00 47.29      A    C  
ANISOU  473  CA  LYS A  59     3533   7420   7015  -1190   -714    863  A    C  
ATOM    474  C   LYS A  59       3.619 -30.622 -45.597  1.00 42.75      A    C  
ANISOU  474  C   LYS A  59     3432   6643   6166   -876   -560    614  A    C  
ATOM    475  O   LYS A  59       3.709 -29.397 -45.440  1.00 39.99      A    O  
ANISOU  475  O   LYS A  59     3045   6350   5801   -533   -343    615  A    O  
ATOM    476  CB  LYS A  59       1.215 -30.557 -44.870  1.00 47.94      A    C  
ANISOU  476  CB  LYS A  59     3111   7747   7357   -983   -331   1131  A    C  
ATOM    477  CG  LYS A  59      -0.229 -30.958 -45.174  1.00 54.30      A    C  
ANISOU  477  CG  LYS A  59     3361   8790   8482  -1212   -493   1421  A    C  
ATOM    478  CD  LYS A  59      -1.230 -30.089 -44.427  1.00 69.72      A    C  
ANISOU  478  CD  LYS A  59     4896  10902  10693   -873    -30   1644  A    C  
ATOM    479  CE  LYS A  59      -0.876 -28.610 -44.540  1.00 78.87      A    C  
ANISOU  479  CE  LYS A  59     6085  12038  11843   -354    208   1612  A    C  
ATOM    480  NZ  LYS A  59      -0.781 -28.141 -45.958  1.00 86.61      A    N1+
ANISOU  480  NZ  LYS A  59     7079  13044  12786   -285   -266   1626  A    N1+
ATOM    481  N   ARG A  60       4.671 -31.437 -45.666  1.00 40.02      A    N  
ANISOU  481  N   ARG A  60     3515   6042   5648  -1002   -657    427  A    N  
ATOM    482  CA  ARG A  60       6.046 -30.959 -45.701  1.00 37.44      A    C  
ANISOU  482  CA  ARG A  60     3572   5547   5105   -771   -584    234  A    C  
ATOM    483  C   ARG A  60       6.139 -29.891 -46.791  1.00 40.64      A    C  
ANISOU  483  C   ARG A  60     3972   6025   5443   -564   -701    168  A    C  
ATOM    484  O   ARG A  60       5.663 -30.104 -47.914  1.00 36.66      A    O  
ANISOU  484  O   ARG A  60     3401   5584   4942   -703   -996    179  A    O  
ATOM    485  CB  ARG A  60       7.015 -32.126 -45.965  1.00 33.89      A    C  
ANISOU  485  CB  ARG A  60     3478   4809   4589   -921   -706    105  A    C  
ATOM    486  CG  ARG A  60       8.488 -31.736 -46.085  1.00 34.44      A    C  
ANISOU  486  CG  ARG A  60     3847   4731   4507   -692   -639    -34  A    C  
ATOM    487  CD  ARG A  60       9.078 -31.404 -44.730  1.00 48.52      A    C  
ANISOU  487  CD  ARG A  60     5662   6552   6220   -594   -435     59  A    C  
ATOM    488  NE  ARG A  60       9.083 -32.567 -43.847  1.00 54.49      A    N  
ANISOU  488  NE  ARG A  60     6457   7203   7044   -771   -409    213  A    N  
ATOM    489  CZ  ARG A  60       9.027 -32.495 -42.522  1.00 60.58      A    C  
ANISOU  489  CZ  ARG A  60     7213   8084   7721   -816   -255    370  A    C  
ATOM    490  NH1 ARG A  60       8.953 -31.312 -41.923  1.00 56.05      A    N1+
ANISOU  490  NH1 ARG A  60     6626   7699   6972   -708    -80    334  A    N1+
ATOM    491  NH2 ARG A  60       9.038 -33.605 -41.797  1.00 68.69      A    N  
ANISOU  491  NH2 ARG A  60     8293   9003   8802   -986   -253    565  A    N  
ATOM    492  N   GLN A  61       6.707 -28.732 -46.467  1.00 32.11      A    N  
ANISOU  492  N   GLN A  61     2987   4935   4276   -279   -489    120  A    N  
ATOM    493  CA  GLN A  61       6.678 -27.620 -47.420  1.00 37.44      A    C  
ANISOU  493  CA  GLN A  61     3641   5660   4925    -68   -559    127  A    C  
ATOM    494  C   GLN A  61       7.784 -27.729 -48.457  1.00 32.72      A    C  
ANISOU  494  C   GLN A  61     3384   4926   4124    -83   -728    -43  A    C  
ATOM    495  O   GLN A  61       8.635 -26.837 -48.582  1.00 30.36      A    O  
ANISOU  495  O   GLN A  61     3268   4545   3721    100   -609   -115  A    O  
ATOM    496  CB  GLN A  61       6.785 -26.286 -46.693  1.00 34.40      A    C  
ANISOU  496  CB  GLN A  61     3271   5247   4553    220   -219    135  A    C  
ATOM    497  CG  GLN A  61       5.769 -26.111 -45.592  1.00 37.96      A    C  
ANISOU  497  CG  GLN A  61     3452   5795   5176    280     92    268  A    C  
ATOM    498  CD  GLN A  61       5.670 -24.670 -45.181  1.00 40.76      A    C  
ANISOU  498  CD  GLN A  61     3857   6059   5570    599    462    259  A    C  
ATOM    499  NE2 GLN A  61       6.234 -24.344 -44.033  1.00 38.46      A    N  
ANISOU  499  NE2 GLN A  61     3875   5650   5090    585    779     93  A    N  
ATOM    500  OE1 GLN A  61       5.124 -23.849 -45.910  1.00 52.13      A    O  
ANISOU  500  OE1 GLN A  61     5102   7514   7191    838    450    408  A    O  
ATOM    501  N   ILE A  62       7.771 -28.830 -49.197  1.00 31.23      A    N  
ANISOU  501  N   ILE A  62     3303   4685   3876   -326   -963   -116  A    N  
ATOM    502  CA  ILE A  62       8.822 -29.101 -50.177  1.00 30.25      A    C  
ANISOU  502  CA  ILE A  62     3548   4397   3549   -342  -1024   -304  A    C  
ATOM    503  C   ILE A  62       8.939 -28.020 -51.262  1.00 32.62      A    C  
ANISOU  503  C   ILE A  62     3923   4786   3684   -200  -1103   -281  A    C  
ATOM    504  O   ILE A  62      10.058 -27.580 -51.548  1.00 32.45      A    O  
ANISOU  504  O   ILE A  62     4138   4649   3545    -60   -954   -380  A    O  
ATOM    505  CB  ILE A  62       8.624 -30.484 -50.837  1.00 38.87      A    C  
ANISOU  505  CB  ILE A  62     4829   5361   4579   -659  -1213   -429  A    C  
ATOM    506  CG1 ILE A  62       8.929 -31.601 -49.832  1.00 36.57      A    C  
ANISOU  506  CG1 ILE A  62     4583   4860   4453   -750  -1072   -448  A    C  
ATOM    507  CG2 ILE A  62       9.510 -30.626 -52.076  1.00 41.46      A    C  
ANISOU  507  CG2 ILE A  62     5574   5533   4646   -662  -1217   -640  A    C  
ATOM    508  CD1 ILE A  62      10.330 -31.556 -49.240  1.00 37.06      A    C  
ANISOU  508  CD1 ILE A  62     4794   4748   4538   -517   -822   -485  A    C  
ATOM    509  N   PRO A  63       7.806 -27.561 -51.853  1.00 34.67      A    N  
ANISOU  509  N   PRO A  63     3948   5266   3958   -234  -1339    -90  A    N  
ATOM    510  CA  PRO A  63       7.963 -26.510 -52.872  1.00 32.98      A    C  
ANISOU  510  CA  PRO A  63     3833   5123   3576    -85  -1422      1  A    C  
ATOM    511  C   PRO A  63       8.634 -25.240 -52.335  1.00 37.00      A    C  
ANISOU  511  C   PRO A  63     4367   5523   4167    245  -1107     34  A    C  
ATOM    512  O   PRO A  63       9.506 -24.662 -52.990  1.00 32.63      A    O  
ANISOU  512  O   PRO A  63     4078   4882   3437    330  -1037    -16  A    O  
ATOM    513  CB  PRO A  63       6.518 -26.228 -53.304  1.00 37.11      A    C  
ANISOU  513  CB  PRO A  63     3966   5930   4205   -144  -1743    315  A    C  
ATOM    514  CG  PRO A  63       5.809 -27.511 -53.061  1.00 42.06      A    C  
ANISOU  514  CG  PRO A  63     4450   6625   4906   -500  -1936    277  A    C  
ATOM    515  CD  PRO A  63       6.410 -28.033 -51.781  1.00 37.83      A    C  
ANISOU  515  CD  PRO A  63     3980   5873   4521   -443  -1582     98  A    C  
ATOM    516  N   LEU A  64       8.245 -24.818 -51.138  1.00 31.52      A    N  
ANISOU  516  N   LEU A  64     3442   4816   3717    391   -887    103  A    N  
ATOM    517  CA  LEU A  64       8.848 -23.637 -50.536  1.00 30.06      A    C  
ANISOU  517  CA  LEU A  64     3366   4477   3579    625   -577     81  A    C  
ATOM    518  C   LEU A  64      10.328 -23.864 -50.268  1.00 30.17      A    C  
ANISOU  518  C   LEU A  64     3685   4336   3443    541   -453   -141  A    C  
ATOM    519  O   LEU A  64      11.171 -23.030 -50.596  1.00 29.75      A    O  
ANISOU  519  O   LEU A  64     3824   4172   3308    619   -348   -168  A    O  
ATOM    520  CB  LEU A  64       8.133 -23.279 -49.241  1.00 32.73      A    C  
ANISOU  520  CB  LEU A  64     3491   4807   4138    746   -310    137  A    C  
ATOM    521  CG  LEU A  64       8.710 -22.070 -48.496  1.00 32.40      A    C  
ANISOU  521  CG  LEU A  64     3666   4549   4097    915     43     47  A    C  
ATOM    522  CD1 LEU A  64       8.758 -20.829 -49.414  1.00 35.98      A    C  
ANISOU  522  CD1 LEU A  64     4205   4882   4584   1138     61    184  A    C  
ATOM    523  CD2 LEU A  64       7.907 -21.800 -47.235  1.00 33.03      A    C  
ANISOU  523  CD2 LEU A  64     3611   4606   4332   1017    377     62  A    C  
ATOM    524  N   ILE A  65      10.639 -25.012 -49.681  1.00 26.04      A    N  
ANISOU  524  N   ILE A  65     3170   3804   2919    376   -469   -248  A    N  
ATOM    525  CA  ILE A  65      12.021 -25.343 -49.354  1.00 27.37      A    C  
ANISOU  525  CA  ILE A  65     3519   3858   3022    320   -376   -368  A    C  
ATOM    526  C   ILE A  65      12.884 -25.364 -50.617  1.00 30.28      A    C  
ANISOU  526  C   ILE A  65     4080   4165   3260    335   -402   -427  A    C  
ATOM    527  O   ILE A  65      14.017 -24.893 -50.604  1.00 31.24      A    O  
ANISOU  527  O   ILE A  65     4293   4216   3359    369   -270   -449  A    O  
ATOM    528  CB  ILE A  65      12.109 -26.706 -48.626  1.00 27.60      A    C  
ANISOU  528  CB  ILE A  65     3504   3866   3118    176   -412   -391  A    C  
ATOM    529  CG1 ILE A  65      11.540 -26.585 -47.212  1.00 32.97      A    C  
ANISOU  529  CG1 ILE A  65     4058   4613   3856    140   -309   -325  A    C  
ATOM    530  CG2 ILE A  65      13.552 -27.220 -48.581  1.00 29.01      A    C  
ANISOU  530  CG2 ILE A  65     3798   3929   3297    168   -355   -431  A    C  
ATOM    531  CD1 ILE A  65      11.157 -27.930 -46.596  1.00 31.97      A    C  
ANISOU  531  CD1 ILE A  65     3852   4487   3807    -19   -368   -270  A    C  
ATOM    532  N   LYS A  66      12.336 -25.885 -51.711  1.00 27.65      A    N  
ANISOU  532  N   LYS A  66     3815   3874   2815    270   -565   -444  A    N  
ATOM    533  CA  LYS A  66      13.056 -25.902 -52.985  1.00 27.69      A    C  
ANISOU  533  CA  LYS A  66     4082   3827   2610    265   -537   -518  A    C  
ATOM    534  C   LYS A  66      13.426 -24.489 -53.425  1.00 32.19      A    C  
ANISOU  534  C   LYS A  66     4711   4412   3107    397   -447   -408  A    C  
ATOM    535  O   LYS A  66      14.547 -24.249 -53.874  1.00 34.75      A    O  
ANISOU  535  O   LYS A  66     5189   4659   3355    425   -265   -447  A    O  
ATOM    536  CB  LYS A  66      12.220 -26.573 -54.084  1.00 31.74      A    C  
ANISOU  536  CB  LYS A  66     4736   4413   2911     92   -778   -561  A    C  
ATOM    537  CG  LYS A  66      12.461 -28.050 -54.229  1.00 40.22      A    C  
ANISOU  537  CG  LYS A  66     6003   5326   3953    -75   -751   -766  A    C  
ATOM    538  CD  LYS A  66      11.649 -28.639 -55.391  1.00 45.17      A    C  
ANISOU  538  CD  LYS A  66     6873   6011   4279   -352  -1019   -855  A    C  
ATOM    539  CE  LYS A  66      11.731 -30.163 -55.397  1.00 51.31      A    C  
ANISOU  539  CE  LYS A  66     7893   6538   5065   -560   -970  -1092  A    C  
ATOM    540  NZ  LYS A  66      10.775 -30.798 -56.357  1.00 57.96      A    N1+
ANISOU  540  NZ  LYS A  66     8928   7445   5651   -925  -1263  -1177  A    N1+
ATOM    541  N   THR A  67      12.485 -23.556 -53.291  1.00 30.90      A    N  
ANISOU  541  N   THR A  67     4407   4323   3009    491   -536   -241  A    N  
ATOM    542  CA  THR A  67      12.725 -22.193 -53.740  1.00 33.48      A    C  
ANISOU  542  CA  THR A  67     4825   4595   3299    627   -443    -99  A    C  
ATOM    543  C   THR A  67      13.736 -21.510 -52.835  1.00 33.46      A    C  
ANISOU  543  C   THR A  67     4860   4432   3422    650   -185   -165  A    C  
ATOM    544  O   THR A  67      14.542 -20.712 -53.303  1.00 28.04      A    O  
ANISOU  544  O   THR A  67     4329   3651   2675    659    -54   -121  A    O  
ATOM    545  CB  THR A  67      11.434 -21.347 -53.798  1.00 34.86      A    C  
ANISOU  545  CB  THR A  67     4818   4833   3596    788   -561    153  A    C  
ATOM    546  CG2 THR A  67      10.335 -22.086 -54.530  1.00 37.56      A    C  
ANISOU  546  CG2 THR A  67     5022   5406   3844    684   -911    269  A    C  
ATOM    547  OG1 THR A  67      10.993 -21.028 -52.479  1.00 45.63      A    O  
ANISOU  547  OG1 THR A  67     5994   6120   5225    891   -393    138  A    O  
ATOM    548  N   LEU A  68      13.717 -21.828 -51.543  1.00 27.65      A    N  
ANISOU  548  N   LEU A  68     4000   3677   2828    605   -128   -256  A    N  
ATOM    549  CA  LEU A  68      14.680 -21.227 -50.641  1.00 26.94      A    C  
ANISOU  549  CA  LEU A  68     3975   3474   2786    527     39   -320  A    C  
ATOM    550  C   LEU A  68      16.095 -21.736 -50.921  1.00 28.31      A    C  
ANISOU  550  C   LEU A  68     4168   3661   2927    411     74   -356  A    C  
ATOM    551  O   LEU A  68      17.038 -20.953 -50.964  1.00 28.48      A    O  
ANISOU  551  O   LEU A  68     4255   3611   2955    334    184   -326  A    O  
ATOM    552  CB  LEU A  68      14.283 -21.484 -49.183  1.00 24.25      A    C  
ANISOU  552  CB  LEU A  68     3550   3150   2514    461     70   -390  A    C  
ATOM    553  CG  LEU A  68      12.926 -20.890 -48.793  1.00 25.21      A    C  
ANISOU  553  CG  LEU A  68     3616   3235   2726    619    163   -342  A    C  
ATOM    554  CD1 LEU A  68      12.489 -21.330 -47.382  1.00 27.17      A    C  
ANISOU  554  CD1 LEU A  68     3806   3530   2985    535    253   -417  A    C  
ATOM    555  CD2 LEU A  68      12.972 -19.366 -48.877  1.00 25.20      A    C  
ANISOU  555  CD2 LEU A  68     3806   3006   2763    729    366   -315  A    C  
ATOM    556  N   VAL A  69      16.246 -23.040 -51.129  1.00 24.72      A    N  
ANISOU  556  N   VAL A  69     3643   3273   2478    399     12   -400  A    N  
ATOM    557  CA  VAL A  69      17.553 -23.597 -51.476  1.00 34.14      A    C  
ANISOU  557  CA  VAL A  69     4807   4449   3714    376    126   -395  A    C  
ATOM    558  C   VAL A  69      18.094 -23.005 -52.775  1.00 34.49      A    C  
ANISOU  558  C   VAL A  69     5006   4463   3636    418    279   -363  A    C  
ATOM    559  O   VAL A  69      19.291 -22.711 -52.879  1.00 34.85      A    O  
ANISOU  559  O   VAL A  69     4983   4497   3761    379    446   -293  A    O  
ATOM    560  CB  VAL A  69      17.492 -25.134 -51.588  1.00 34.63      A    C  
ANISOU  560  CB  VAL A  69     4841   4487   3829    409    106   -459  A    C  
ATOM    561  CG1 VAL A  69      18.760 -25.679 -52.220  1.00 36.22      A    C  
ANISOU  561  CG1 VAL A  69     5035   4617   4111    481    334   -444  A    C  
ATOM    562  CG2 VAL A  69      17.286 -25.730 -50.208  1.00 28.22      A    C  
ANISOU  562  CG2 VAL A  69     3862   3704   3157    344    -10   -417  A    C  
ATOM    563  N   ALA A  70      17.213 -22.801 -53.755  1.00 36.47      A    N  
ANISOU  563  N   ALA A  70     5440   4730   3686    471    209   -367  A    N  
ATOM    564  CA  ALA A  70      17.629 -22.270 -55.051  1.00 37.89      A    C  
ANISOU  564  CA  ALA A  70     5832   4902   3660    488    345   -307  A    C  
ATOM    565  C   ALA A  70      18.085 -20.820 -54.954  1.00 34.31      A    C  
ANISOU  565  C   ALA A  70     5394   4379   3264    466    447   -159  A    C  
ATOM    566  O   ALA A  70      18.787 -20.328 -55.835  1.00 36.59      A    O  
ANISOU  566  O   ALA A  70     5817   4646   3440    444    632    -70  A    O  
ATOM    567  CB  ALA A  70      16.501 -22.394 -56.073  1.00 39.09      A    C  
ANISOU  567  CB  ALA A  70     6186   5135   3530    495    150   -290  A    C  
ATOM    568  N   GLY A  71      17.686 -20.135 -53.888  1.00 27.16      A    N  
ANISOU  568  N   GLY A  71     4397   3405   2519    449    369   -142  A    N  
ATOM    569  CA  GLY A  71      18.026 -18.734 -53.725  1.00 29.90      A    C  
ANISOU  569  CA  GLY A  71     4841   3593   2926    392    482    -41  A    C  
ATOM    570  C   GLY A  71      19.341 -18.506 -52.998  1.00 24.67      A    C  
ANISOU  570  C   GLY A  71     4070   2899   2403    170    589    -62  A    C  
ATOM    571  O   GLY A  71      19.774 -17.362 -52.865  1.00 27.79      A    O  
ANISOU  571  O   GLY A  71     4577   3135   2845     31    685      1  A    O  
ATOM    572  N   VAL A  72      19.954 -19.569 -52.481  1.00 24.17      A    N  
ANISOU  572  N   VAL A  72     3557   3101   2525    477     27   1100  A    N  
ATOM    573  CA  VAL A  72      21.198 -19.386 -51.725  1.00 21.45      A    C  
ANISOU  573  CA  VAL A  72     3231   2636   2285    406    184    961  A    C  
ATOM    574  C   VAL A  72      22.295 -20.323 -52.232  1.00 26.05      A    C  
ANISOU  574  C   VAL A  72     3771   3379   2748    256    321    830  A    C  
ATOM    575  O   VAL A  72      22.059 -21.118 -53.148  1.00 33.35      A    O  
ANISOU  575  O   VAL A  72     4730   4478   3462    207    334    797  A    O  
ATOM    576  CB  VAL A  72      20.975 -19.577 -50.211  1.00 23.43      A    C  
ANISOU  576  CB  VAL A  72     3422   2759   2721    513    193    797  A    C  
ATOM    577  CG1 VAL A  72      19.936 -18.557 -49.707  1.00 24.24      A    C  
ANISOU  577  CG1 VAL A  72     3586   2654   2971    697    175    899  A    C  
ATOM    578  CG2 VAL A  72      20.569 -21.013 -49.890  1.00 26.50      A    C  
ANISOU  578  CG2 VAL A  72     3679   3313   3077    541    171    640  A    C  
ATOM    579  N   ASN A  73      23.501 -20.213 -51.671  1.00 26.75      A    N  
ANISOU  579  N   ASN A  73     3788   3393   2984    172    428    763  A    N  
ATOM    580  CA  ASN A  73      24.646 -20.959 -52.206  1.00 25.61      A    C  
ANISOU  580  CA  ASN A  73     3533   3372   2827     71    624    682  A    C  
ATOM    581  C   ASN A  73      25.515 -21.590 -51.110  1.00 31.30      A    C  
ANISOU  581  C   ASN A  73     4038   4042   3811     80    623    560  A    C  
ATOM    582  O   ASN A  73      26.711 -21.810 -51.291  1.00 29.99      A    O  
ANISOU  582  O   ASN A  73     3692   3910   3794      2    777    564  A    O  
ATOM    583  CB  ASN A  73      25.509 -20.053 -53.077  1.00 24.89      A    C  
ANISOU  583  CB  ASN A  73     3493   3281   2682    -99    786    848  A    C  
ATOM    584  CG  ASN A  73      26.420 -20.843 -54.002  1.00 37.13      A    C  
ANISOU  584  CG  ASN A  73     4964   4994   4151   -175   1097    773  A    C  
ATOM    585  ND2 ASN A  73      27.659 -20.389 -54.155  1.00 31.53      A    N  
ANISOU  585  ND2 ASN A  73     4101   4278   3603   -315   1303    863  A    N  
ATOM    586  OD1 ASN A  73      26.019 -21.876 -54.542  1.00 35.46      A    O  
ANISOU  586  OD1 ASN A  73     4827   4894   3754   -115   1173    625  A    O  
ATOM    587  N   VAL A  74      24.906 -21.845 -49.966  1.00 25.13      A    N  
ANISOU  587  N   VAL A  74     3267   3180   3102    166    447    485  A    N  
ATOM    588  CA  VAL A  74      25.561 -22.530 -48.857  1.00 28.52      A    C  
ANISOU  588  CA  VAL A  74     3547   3562   3727    158    362    407  A    C  
ATOM    589  C   VAL A  74      24.630 -23.632 -48.402  1.00 27.32      A    C  
ANISOU  589  C   VAL A  74     3421   3443   3517    282    293    288  A    C  
ATOM    590  O   VAL A  74      23.433 -23.601 -48.746  1.00 26.56      A    O  
ANISOU  590  O   VAL A  74     3437   3390   3265    352    282    281  A    O  
ATOM    591  CB  VAL A  74      25.864 -21.575 -47.688  1.00 31.16      A    C  
ANISOU  591  CB  VAL A  74     3965   3724   4149     44    191    458  A    C  
ATOM    592  CG1 VAL A  74      26.981 -20.613 -48.072  1.00 28.26      A    C  
ANISOU  592  CG1 VAL A  74     3529   3310   3899   -145    228    592  A    C  
ATOM    593  CG2 VAL A  74      24.598 -20.834 -47.267  1.00 27.91      A    C  
ANISOU  593  CG2 VAL A  74     3813   3195   3596    127    149    438  A    C  
ATOM    594  N   PRO A  75      25.157 -24.612 -47.649  1.00 26.87      A    N  
ANISOU  594  N   PRO A  75     3238   3359   3613    295    225    235  A    N  
ATOM    595  CA  PRO A  75      24.310 -25.683 -47.114  1.00 28.35      A    C  
ANISOU  595  CA  PRO A  75     3472   3545   3754    373    153    149  A    C  
ATOM    596  C   PRO A  75      23.111 -25.175 -46.321  1.00 29.35      A    C  
ANISOU  596  C   PRO A  75     3769   3636   3746    383     72    152  A    C  
ATOM    597  O   PRO A  75      23.226 -24.276 -45.461  1.00 27.59      A    O  
ANISOU  597  O   PRO A  75     3662   3310   3512    322      8    184  A    O  
ATOM    598  CB  PRO A  75      25.262 -26.453 -46.193  1.00 27.78      A    C  
ANISOU  598  CB  PRO A  75     3261   3394   3900    353     29    175  A    C  
ATOM    599  CG  PRO A  75      26.589 -26.231 -46.766  1.00 32.26      A    C  
ANISOU  599  CG  PRO A  75     3602   3973   4680    328    124    241  A    C  
ATOM    600  CD  PRO A  75      26.577 -24.835 -47.325  1.00 29.27      A    C  
ANISOU  600  CD  PRO A  75     3311   3628   4181    233    199    296  A    C  
ATOM    601  N   VAL A  76      21.955 -25.758 -46.608  1.00 20.48      A    N  
ANISOU  601  N   VAL A  76     2667   2585   2531    446     95    113  A    N  
ATOM    602  CA  VAL A  76      20.747 -25.463 -45.846  1.00 24.46      A    C  
ANISOU  602  CA  VAL A  76     3249   3069   2976    485     89    127  A    C  
ATOM    603  C   VAL A  76      20.427 -26.729 -45.046  1.00 26.85      A    C  
ANISOU  603  C   VAL A  76     3546   3368   3286    452     40     82  A    C  
ATOM    604  O   VAL A  76      20.419 -27.834 -45.613  1.00 22.98      A    O  
ANISOU  604  O   VAL A  76     2989   2920   2822    440     17     41  A    O  
ATOM    605  CB  VAL A  76      19.574 -25.070 -46.770  1.00 26.19      A    C  
ANISOU  605  CB  VAL A  76     3420   3384   3148    558    121    194  A    C  
ATOM    606  CG1 VAL A  76      18.266 -24.969 -45.972  1.00 22.87      A    C  
ANISOU  606  CG1 VAL A  76     2971   2956   2763    631    172    226  A    C  
ATOM    607  CG2 VAL A  76      19.879 -23.739 -47.478  1.00 24.01      A    C  
ANISOU  607  CG2 VAL A  76     3194   3068   2862    584    149    289  A    C  
ATOM    608  N   GLN A  77      20.223 -26.604 -43.737  1.00 26.06      A    N  
ANISOU  608  N   GLN A  77     3570   3191   3140    412     33     85  A    N  
ATOM    609  CA  GLN A  77      19.778 -27.776 -42.987  1.00 22.24      A    C  
ANISOU  609  CA  GLN A  77     3111   2705   2633    354     -2     86  A    C  
ATOM    610  C   GLN A  77      18.342 -27.558 -42.546  1.00 22.86      A    C  
ANISOU  610  C   GLN A  77     3203   2833   2651    383    157    100  A    C  
ATOM    611  O   GLN A  77      17.925 -26.436 -42.231  1.00 23.62      A    O  
ANISOU  611  O   GLN A  77     3373   2890   2712    453    301     94  A    O  
ATOM    612  CB  GLN A  77      20.709 -28.083 -41.793  1.00 26.90      A    C  
ANISOU  612  CB  GLN A  77     3846   3184   3190    239   -150    121  A    C  
ATOM    613  CG  GLN A  77      20.850 -27.001 -40.778  1.00 32.43      A    C  
ANISOU  613  CG  GLN A  77     4789   3802   3731    157   -141    111  A    C  
ATOM    614  CD  GLN A  77      21.795 -27.394 -39.627  1.00 33.85      A    C  
ANISOU  614  CD  GLN A  77     5139   3890   3832    -27   -392    187  A    C  
ATOM    615  NE2 GLN A  77      21.456 -26.973 -38.417  1.00 25.69      A    N  
ANISOU  615  NE2 GLN A  77     4446   2788   2526   -166   -361    164  A    N  
ATOM    616  OE1 GLN A  77      22.821 -28.044 -39.837  1.00 28.54      A    O  
ANISOU  616  OE1 GLN A  77     4297   3199   3346    -43   -605    278  A    O  
ATOM    617  N   VAL A  78      17.561 -28.633 -42.570  1.00 21.48      A    N  
ANISOU  617  N   VAL A  78     2937   2723   2503    332    157    126  A    N  
ATOM    618  CA  VAL A  78      16.139 -28.513 -42.312  1.00 21.77      A    C  
ANISOU  618  CA  VAL A  78     2867   2843   2563    354    326    180  A    C  
ATOM    619  C   VAL A  78      15.665 -29.583 -41.340  1.00 23.42      A    C  
ANISOU  619  C   VAL A  78     3137   3042   2719    207    368    219  A    C  
ATOM    620  O   VAL A  78      15.975 -30.758 -41.525  1.00 26.57      A    O  
ANISOU  620  O   VAL A  78     3543   3408   3143     98    206    229  A    O  
ATOM    621  CB  VAL A  78      15.320 -28.624 -43.622  1.00 25.80      A    C  
ANISOU  621  CB  VAL A  78     3115   3492   3195    387    260    238  A    C  
ATOM    622  CG1 VAL A  78      13.831 -28.566 -43.318  1.00 26.21      A    C  
ANISOU  622  CG1 VAL A  78     2944   3645   3368    403    411    351  A    C  
ATOM    623  CG2 VAL A  78      15.716 -27.508 -44.605  1.00 25.89      A    C  
ANISOU  623  CG2 VAL A  78     3103   3512   3221    510    219    247  A    C  
ATOM    624  N   GLY A  79      14.935 -29.164 -40.316  1.00 25.98      A    N  
ANISOU  624  N   GLY A  79     3537   3367   2969    205    620    241  A    N  
ATOM    625  CA  GLY A  79      14.259 -30.083 -39.417  1.00 28.20      A    C  
ANISOU  625  CA  GLY A  79     3862   3668   3184     43    734    314  A    C  
ATOM    626  C   GLY A  79      12.786 -29.749 -39.308  1.00 33.12      A    C  
ANISOU  626  C   GLY A  79     4227   4413   3945    104   1056    385  A    C  
ATOM    627  O   GLY A  79      12.295 -28.841 -39.982  1.00 30.68      A    O  
ANISOU  627  O   GLY A  79     3683   4157   3815    297   1140    397  A    O  
ATOM    628  N   GLY A  80      12.086 -30.478 -38.440  1.00 31.23      A    N  
ANISOU  628  N   GLY A  80     4010   4209   3649    -61   1244    468  A    N  
ATOM    629  CA  GLY A  80      10.676 -30.251 -38.188  1.00 39.07      A    C  
ANISOU  629  CA  GLY A  80     4700   5327   4819    -18   1619    566  A    C  
ATOM    630  C   GLY A  80       9.920 -31.556 -38.322  1.00 48.43      A    C  
ANISOU  630  C   GLY A  80     5644   6619   6138   -264   1536    727  A    C  
ATOM    631  O   GLY A  80       9.428 -31.876 -39.399  1.00 47.36      A    O  
ANISOU  631  O   GLY A  80     5149   6588   6256   -289   1311    810  A    O  
ATOM    632  N   GLY A  81       9.837 -32.310 -37.228  1.00 50.23      A    N  
ANISOU  632  N   GLY A  81     6113   6806   6166   -490   1689    785  A    N  
ATOM    633  CA  GLY A  81       9.173 -33.602 -37.236  1.00 53.60      A    C  
ANISOU  633  CA  GLY A  81     6374   7287   6705   -779   1613    954  A    C  
ATOM    634  C   GLY A  81       9.572 -34.502 -38.397  1.00 51.53      A    C  
ANISOU  634  C   GLY A  81     6032   6970   6578   -884   1117    950  A    C  
ATOM    635  O   GLY A  81       8.721 -34.996 -39.126  1.00 54.32      A    O  
ANISOU  635  O   GLY A  81     6034   7429   7178  -1019   1005   1053  A    O  
ATOM    636  N   VAL A  82      10.874 -34.688 -38.589  1.00 40.16      A    N  
ANISOU  636  N   VAL A  82     4919   5356   4984   -829    828    827  A    N  
ATOM    637  CA  VAL A  82      11.380 -35.668 -39.552  1.00 35.81      A    C  
ANISOU  637  CA  VAL A  82     4399   4682   4527   -922    448    783  A    C  
ATOM    638  C   VAL A  82      11.370 -37.068 -38.937  1.00 39.88      A    C  
ANISOU  638  C   VAL A  82     5119   5023   5010  -1204    359    901  A    C  
ATOM    639  O   VAL A  82      12.155 -37.361 -38.026  1.00 40.93      A    O  
ANISOU  639  O   VAL A  82     5586   4996   4968  -1226    329    943  A    O  
ATOM    640  CB  VAL A  82      12.807 -35.318 -39.997  1.00 36.35      A    C  
ANISOU  640  CB  VAL A  82     4676   4617   4518   -718    246    624  A    C  
ATOM    641  CG1 VAL A  82      13.384 -36.434 -40.839  1.00 41.15      A    C  
ANISOU  641  CG1 VAL A  82     5376   5041   5219   -792    -37    555  A    C  
ATOM    642  CG2 VAL A  82      12.821 -34.000 -40.743  1.00 30.52      A    C  
ANISOU  642  CG2 VAL A  82     3759   4019   3818   -481    301    531  A    C  
ATOM    643  N   ARG A  83      10.487 -37.934 -39.427  1.00 29.87      A    N  
ANISOU  643  N   ARG A  83     3665   3770   3913  -1449    275    984  A    N  
ATOM    644  CA  ARG A  83      10.216 -39.191 -38.744  1.00 31.45      A    C  
ANISOU  644  CA  ARG A  83     4037   3806   4107  -1764    249   1144  A    C  
ATOM    645  C   ARG A  83      10.378 -40.463 -39.572  1.00 38.31      A    C  
ANISOU  645  C   ARG A  83     5022   4420   5114  -1957    -79   1098  A    C  
ATOM    646  O   ARG A  83      10.324 -41.556 -39.021  1.00 38.50      A    O  
ANISOU  646  O   ARG A  83     5256   4224   5148  -2195   -136   1227  A    O  
ATOM    647  CB  ARG A  83       8.804 -39.143 -38.153  1.00 49.19      A    C  
ANISOU  647  CB  ARG A  83     5984   6275   6431  -1983    563   1348  A    C  
ATOM    648  CG  ARG A  83       8.685 -38.104 -37.050  1.00 53.21      A    C  
ANISOU  648  CG  ARG A  83     6529   6937   6749  -1824    991   1378  A    C  
ATOM    649  CD  ARG A  83       7.352 -38.130 -36.346  1.00 71.37      A    C  
ANISOU  649  CD  ARG A  83     8571   9393   9152  -1947   1397   1524  A    C  
ATOM    650  NE  ARG A  83       7.330 -37.139 -35.275  1.00 82.00      A    N  
ANISOU  650  NE  ARG A  83    10054  10816  10286  -1746   1843   1504  A    N  
ATOM    651  CZ  ARG A  83       6.890 -35.893 -35.420  1.00 84.39      A    C  
ANISOU  651  CZ  ARG A  83    10095  11355  10615  -1542   2080   1390  A    C  
ATOM    652  NH1 ARG A  83       6.420 -35.486 -36.592  1.00 78.40      A    N1+
ANISOU  652  NH1 ARG A  83     8887  10676  10226  -1387   1962   1356  A    N1+
ATOM    653  NH2 ARG A  83       6.911 -35.057 -34.390  1.00 90.04      A    N  
ANISOU  653  NH2 ARG A  83    11012  12115  11084  -1351   2378   1314  A    N  
ATOM    654  N   THR A  84      10.582 -40.344 -40.879  1.00 35.93      A    N  
ANISOU  654  N   THR A  84     4644   4115   4892  -1867   -279    908  A    N  
ATOM    655  CA  THR A  84      10.742 -41.533 -41.721  1.00 38.59      A    C  
ANISOU  655  CA  THR A  84     5182   4166   5315  -2060   -544    801  A    C  
ATOM    656  C   THR A  84      11.887 -41.333 -42.707  1.00 35.66      A    C  
ANISOU  656  C   THR A  84     4992   3656   4903  -1785   -659    531  A    C  
ATOM    657  O   THR A  84      12.255 -40.201 -42.990  1.00 33.37      A    O  
ANISOU  657  O   THR A  84     4569   3570   4539  -1520   -582    455  A    O  
ATOM    658  CB  THR A  84       9.471 -41.842 -42.519  1.00 45.77      A    C  
ANISOU  658  CB  THR A  84     5836   5222   6333  -2386   -677    840  A    C  
ATOM    659  CG2 THR A  84       8.308 -42.151 -41.595  1.00 53.76      A    C  
ANISOU  659  CG2 THR A  84     6614   6383   7430  -2579   -502   1080  A    C  
ATOM    660  OG1 THR A  84       9.147 -40.699 -43.320  1.00 44.37      A    O  
ANISOU  660  OG1 THR A  84     5349   5360   6149  -2246   -697    794  A    O  
ATOM    661  N   GLU A  85      12.437 -42.417 -43.254  1.00 35.92      A    N  
ANISOU  661  N   GLU A  85     5334   3318   4994  -1849   -802    384  A    N  
ATOM    662  CA  GLU A  85      13.495 -42.247 -44.252  1.00 36.40      A    C  
ANISOU  662  CA  GLU A  85     5554   3250   5025  -1587   -817    113  A    C  
ATOM    663  C   GLU A  85      12.948 -41.596 -45.523  1.00 34.40      A    C  
ANISOU  663  C   GLU A  85     5175   3260   4637  -1660   -888    -29  A    C  
ATOM    664  O   GLU A  85      13.685 -40.912 -46.225  1.00 31.79      A    O  
ANISOU  664  O   GLU A  85     4870   2995   4212  -1418   -827   -190  A    O  
ATOM    665  CB  GLU A  85      14.179 -43.586 -44.586  1.00 34.37      A    C  
ANISOU  665  CB  GLU A  85     5660   2512   4888  -1583   -863    -43  A    C  
ATOM    666  CG  GLU A  85      13.312 -44.622 -45.241  1.00 44.39      A    C  
ANISOU  666  CG  GLU A  85     7033   3699   6136  -1872   -949   -129  A    C  
ATOM    667  CD  GLU A  85      14.073 -45.911 -45.520  1.00 52.86      A    C  
ANISOU  667  CD  GLU A  85     8418   4322   7345  -1759   -892   -298  A    C  
ATOM    668  OE1 GLU A  85      15.250 -45.847 -45.942  1.00 43.21      A    O  
ANISOU  668  OE1 GLU A  85     7308   2915   6194  -1444   -760   -480  A    O  
ATOM    669  OE2 GLU A  85      13.487 -46.993 -45.330  1.00 63.78      A    O1-
ANISOU  669  OE2 GLU A  85     9907   5529   8796  -1982   -955   -244  A    O1-
ATOM    670  N   GLU A  86      11.664 -41.793 -45.820  1.00 40.15      A    N  
ANISOU  670  N   GLU A  86     5750   4146   5361  -2017  -1038     69  A    N  
ATOM    671  CA  GLU A  86      11.097 -41.151 -47.007  1.00 37.76      A    C  
ANISOU  671  CA  GLU A  86     5313   4109   4927  -2118  -1194      6  A    C  
ATOM    672  C   GLU A  86      11.059 -39.634 -46.819  1.00 37.98      A    C  
ANISOU  672  C   GLU A  86     4986   4502   4942  -1823  -1067    132  A    C  
ATOM    673  O   GLU A  86      11.275 -38.876 -47.772  1.00 33.35      A    O  
ANISOU  673  O   GLU A  86     4396   4059   4216  -1714  -1126     42  A    O  
ATOM    674  CB  GLU A  86       9.701 -41.703 -47.335  1.00 45.74      A    C  
ANISOU  674  CB  GLU A  86     6149   5255   5976  -2448  -1372    140  A    C  
ATOM    675  CG  GLU A  86       8.751 -41.834 -46.157  1.00 57.82      A    C  
ANISOU  675  CG  GLU A  86     7343   6911   7713  -2579  -1282    435  A    C  
ATOM    676  CD  GLU A  86       8.634 -43.264 -45.613  1.00 55.69      A    C  
ANISOU  676  CD  GLU A  86     7313   6334   7514  -2768  -1271    444  A    C  
ATOM    677  OE1 GLU A  86       9.666 -43.876 -45.260  1.00 47.51      A    O  
ANISOU  677  OE1 GLU A  86     6628   4956   6466  -2635  -1189    321  A    O  
ATOM    678  OE2 GLU A  86       7.498 -43.774 -45.530  1.00 61.41      A    O1-
ANISOU  678  OE2 GLU A  86     7849   7150   8334  -3035  -1350    596  A    O1-
ATOM    679  N   ASP A  87      10.829 -39.187 -45.587  1.00 32.57      A    N  
ANISOU  679  N   ASP A  87     4066   3932   4378  -1701   -870    330  A    N  
ATOM    680  CA  ASP A  87      10.864 -37.755 -45.280  1.00 34.96      A    C  
ANISOU  680  CA  ASP A  87     4111   4492   4679  -1400   -697    414  A    C  
ATOM    681  C   ASP A  87      12.271 -37.176 -45.477  1.00 26.60      A    C  
ANISOU  681  C   ASP A  87     3273   3333   3499  -1076   -612    235  A    C  
ATOM    682  O   ASP A  87      12.440 -36.104 -46.069  1.00 32.04      A    O  
ANISOU  682  O   ASP A  87     3864   4183   4127   -900   -599    212  A    O  
ATOM    683  CB  ASP A  87      10.380 -37.513 -43.841  1.00 43.29      A    C  
ANISOU  683  CB  ASP A  87     4989   5629   5829  -1369   -441    612  A    C  
ATOM    684  CG  ASP A  87       9.663 -36.171 -43.667  1.00 63.91      A    C  
ANISOU  684  CG  ASP A  87     7222   8529   8530  -1187   -260    747  A    C  
ATOM    685  OD1 ASP A  87       9.559 -35.392 -44.645  1.00 65.23      A    O  
ANISOU  685  OD1 ASP A  87     7242   8832   8710  -1074   -384    731  A    O  
ATOM    686  OD2 ASP A  87       9.182 -35.904 -42.544  1.00 74.70      A    O1-
ANISOU  686  OD2 ASP A  87     8464   9965   9955  -1157     29    878  A    O1-
ATOM    687  N   VAL A  88      13.277 -37.878 -44.967  1.00 28.08      A    N  
ANISOU  687  N   VAL A  88     3730   3247   3692  -1004   -565    148  A    N  
ATOM    688  CA  VAL A  88      14.668 -37.485 -45.155  1.00 23.94      A    C  
ANISOU  688  CA  VAL A  88     3352   2613   3132   -726   -497     10  A    C  
ATOM    689  C   VAL A  88      15.011 -37.415 -46.647  1.00 25.97      A    C  
ANISOU  689  C   VAL A  88     3717   2867   3284   -709   -550   -192  A    C  
ATOM    690  O   VAL A  88      15.603 -36.448 -47.124  1.00 25.50      A    O  
ANISOU  690  O   VAL A  88     3615   2922   3151   -522   -476   -241  A    O  
ATOM    691  CB  VAL A  88      15.634 -38.479 -44.476  1.00 27.45      A    C  
ANISOU  691  CB  VAL A  88     4016   2726   3687   -669   -498     -5  A    C  
ATOM    692  CG1 VAL A  88      17.074 -38.112 -44.802  1.00 28.28      A    C  
ANISOU  692  CG1 VAL A  88     4173   2732   3840   -387   -433   -122  A    C  
ATOM    693  CG2 VAL A  88      15.413 -38.492 -42.959  1.00 28.47      A    C  
ANISOU  693  CG2 VAL A  88     4126   2865   3828   -717   -464    217  A    C  
ATOM    694  N   ALA A  89      14.620 -38.450 -47.380  1.00 26.52      A    N  
ANISOU  694  N   ALA A  89     3973   2790   3313   -947   -670   -308  A    N  
ATOM    695  CA  ALA A  89      14.940 -38.513 -48.809  1.00 28.07      A    C  
ANISOU  695  CA  ALA A  89     4394   2951   3320   -990   -695   -535  A    C  
ATOM    696  C   ALA A  89      14.280 -37.387 -49.596  1.00 30.92      A    C  
ANISOU  696  C   ALA A  89     4585   3659   3505  -1045   -810   -448  A    C  
ATOM    697  O   ALA A  89      14.872 -36.850 -50.537  1.00 27.39      A    O  
ANISOU  697  O   ALA A  89     4272   3263   2872   -957   -750   -567  A    O  
ATOM    698  CB  ALA A  89      14.533 -39.853 -49.381  1.00 29.99      A    C  
ANISOU  698  CB  ALA A  89     4950   2935   3508  -1299   -823   -694  A    C  
ATOM    699  N   ALA A  90      13.047 -37.047 -49.238  1.00 31.67      A    N  
ANISOU  699  N   ALA A  90     4374   3980   3681  -1192   -964   -213  A    N  
ATOM    700  CA  ALA A  90      12.346 -35.977 -49.935  1.00 31.54      A    C  
ANISOU  700  CA  ALA A  90     4135   4268   3582  -1215  -1114    -60  A    C  
ATOM    701  C   ALA A  90      13.049 -34.648 -49.719  1.00 29.11      A    C  
ANISOU  701  C   ALA A  90     3716   4059   3286   -863   -919    -12  A    C  
ATOM    702  O   ALA A  90      13.150 -33.837 -50.642  1.00 26.91      A    O  
ANISOU  702  O   ALA A  90     3464   3910   2851   -825   -989     11  A    O  
ATOM    703  CB  ALA A  90      10.889 -35.894 -49.487  1.00 32.68      A    C  
ANISOU  703  CB  ALA A  90     3871   4614   3931  -1392  -1273    221  A    C  
ATOM    704  N   LEU A  91      13.555 -34.418 -48.511  1.00 25.74      A    N  
ANISOU  704  N   LEU A  91     3210   3555   3015   -646   -698     13  A    N  
ATOM    705  CA  LEU A  91      14.262 -33.168 -48.227  1.00 23.68      A    C  
ANISOU  705  CA  LEU A  91     2889   3346   2764   -363   -534     44  A    C  
ATOM    706  C   LEU A  91      15.592 -33.087 -48.968  1.00 27.74      A    C  
ANISOU  706  C   LEU A  91     3641   3755   3143   -261   -450   -136  A    C  
ATOM    707  O   LEU A  91      15.892 -32.074 -49.581  1.00 26.40      A    O  
ANISOU  707  O   LEU A  91     3461   3687   2882   -166   -424   -104  A    O  
ATOM    708  CB  LEU A  91      14.500 -32.997 -46.723  1.00 19.00      A    C  
ANISOU  708  CB  LEU A  91     2233   2681   2304   -229   -358    102  A    C  
ATOM    709  CG  LEU A  91      13.240 -32.607 -45.954  1.00 24.10      A    C  
ANISOU  709  CG  LEU A  91     2614   3465   3078   -251   -294    291  A    C  
ATOM    710  CD1 LEU A  91      13.466 -32.814 -44.462  1.00 24.65      A    C  
ANISOU  710  CD1 LEU A  91     2762   3431   3172   -220   -112    310  A    C  
ATOM    711  CD2 LEU A  91      12.846 -31.158 -46.249  1.00 25.20      A    C  
ANISOU  711  CD2 LEU A  91     2560   3748   3268    -67   -241    403  A    C  
ATOM    712  N   LEU A  92      16.379 -34.158 -48.912  1.00 24.90      A    N  
ANISOU  712  N   LEU A  92     3480   3174   2807   -274   -382   -306  A    N  
ATOM    713  CA  LEU A  92      17.610 -34.229 -49.675  1.00 24.71      A    C  
ANISOU  713  CA  LEU A  92     3638   3037   2713   -169   -230   -484  A    C  
ATOM    714  C   LEU A  92      17.351 -34.056 -51.182  1.00 30.49      A    C  
ANISOU  714  C   LEU A  92     4559   3877   3150   -318   -277   -575  A    C  
ATOM    715  O   LEU A  92      18.092 -33.352 -51.864  1.00 28.39      A    O  
ANISOU  715  O   LEU A  92     4357   3668   2763   -228   -136   -613  A    O  
ATOM    716  CB  LEU A  92      18.323 -35.556 -49.417  1.00 27.70      A    C  
ANISOU  716  CB  LEU A  92     4178   3111   3236   -139   -139   -638  A    C  
ATOM    717  CG  LEU A  92      18.773 -35.774 -47.970  1.00 25.55      A    C  
ANISOU  717  CG  LEU A  92     3773   2714   3222    -11   -140   -510  A    C  
ATOM    718  CD1 LEU A  92      19.355 -37.152 -47.805  1.00 26.98      A    C  
ANISOU  718  CD1 LEU A  92     4109   2555   3588     22   -100   -611  A    C  
ATOM    719  CD2 LEU A  92      19.779 -34.725 -47.547  1.00 24.67      A    C  
ANISOU  719  CD2 LEU A  92     3503   2674   3196    191    -53   -427  A    C  
ATOM    720  N   LYS A  93      16.300 -34.685 -51.697  1.00 27.10      A    N  
ANISOU  720  N   LYS A  93     4234   3481   2582   -589   -495   -588  A    N  
ATOM    721  CA  LYS A  93      15.988 -34.547 -53.121  1.00 29.84      A    C  
ANISOU  721  CA  LYS A  93     4826   3938   2573   -804   -619   -651  A    C  
ATOM    722  C   LYS A  93      15.657 -33.103 -53.488  1.00 34.41      A    C  
ANISOU  722  C   LYS A  93     5220   4788   3067   -747   -728   -409  A    C  
ATOM    723  O   LYS A  93      15.878 -32.673 -54.622  1.00 34.94      A    O  
ANISOU  723  O   LYS A  93     5516   4942   2819   -840   -744   -433  A    O  
ATOM    724  CB  LYS A  93      14.837 -35.464 -53.520  1.00 32.09      A    C  
ANISOU  724  CB  LYS A  93     5238   4218   2739  -1174   -930   -665  A    C  
ATOM    725  CG  LYS A  93      14.726 -35.662 -55.033  1.00 43.87      A    C  
ANISOU  725  CG  LYS A  93     7061   5730   3879  -1379   -999   -767  A    C  
ATOM    726  CD  LYS A  93      13.708 -36.737 -55.370  1.00 50.84      A    C  
ANISOU  726  CD  LYS A  93     8034   6538   4745  -1690  -1243   -770  A    C  
ATOM    727  CE  LYS A  93      13.722 -37.084 -56.849  1.00 66.82      A    C  
ANISOU  727  CE  LYS A  93    10450   8524   6415  -1885  -1264   -897  A    C  
ATOM    728  NZ  LYS A  93      13.273 -35.940 -57.675  1.00 67.92      A    N1+
ANISOU  728  NZ  LYS A  93    10506   8935   6366  -1948  -1466   -662  A    N1+
ATOM    729  N   ALA A  94      15.127 -32.357 -52.528  1.00 29.90      A    N  
ANISOU  729  N   ALA A  94     4275   4321   2765   -597   -778   -174  A    N  
ATOM    730  CA  ALA A  94      14.780 -30.957 -52.744  1.00 34.05      A    C  
ANISOU  730  CA  ALA A  94     4608   5028   3300   -489   -860     73  A    C  
ATOM    731  C   ALA A  94      16.008 -30.050 -52.672  1.00 29.97      A    C  
ANISOU  731  C   ALA A  94     4149   4456   2782   -259   -594     35  A    C  
ATOM    732  O   ALA A  94      15.904 -28.836 -52.853  1.00 31.98      A    O  
ANISOU  732  O   ALA A  94     4306   4796   3048   -159   -625    225  A    O  
ATOM    733  CB  ALA A  94      13.724 -30.506 -51.720  1.00 33.06      A    C  
ANISOU  733  CB  ALA A  94     4080   4985   3498   -389   -931    308  A    C  
ATOM    734  N   GLY A  95      17.165 -30.629 -52.369  1.00 26.39      A    N  
ANISOU  734  N   GLY A  95     3822   3837   2366   -177   -347   -179  A    N  
ATOM    735  CA  GLY A  95      18.398 -29.873 -52.339  1.00 23.94      A    C  
ANISOU  735  CA  GLY A  95     3521   3483   2094    -11   -113   -199  A    C  
ATOM    736  C   GLY A  95      18.875 -29.465 -50.956  1.00 22.66      A    C  
ANISOU  736  C   GLY A  95     3155   3232   2222    173    -27   -145  A    C  
ATOM    737  O   GLY A  95      19.863 -28.760 -50.830  1.00 28.47      A    O  
ANISOU  737  O   GLY A  95     3862   3932   3024    269    110   -127  A    O  
ATOM    738  N   VAL A  96      18.166 -29.897 -49.917  1.00 24.57      A    N  
ANISOU  738  N   VAL A  96     3281   3443   2614    179   -115   -106  A    N  
ATOM    739  CA  VAL A  96      18.635 -29.730 -48.544  1.00 22.43      A    C  
ANISOU  739  CA  VAL A  96     2922   3070   2531    291    -50    -80  A    C  
ATOM    740  C   VAL A  96      19.953 -30.473 -48.336  1.00 22.98      A    C  
ANISOU  740  C   VAL A  96     3038   2986   2707    336     44   -195  A    C  
ATOM    741  O   VAL A  96      20.127 -31.592 -48.821  1.00 24.42      A    O  
ANISOU  741  O   VAL A  96     3313   3078   2888    296     75   -323  A    O  
ATOM    742  CB  VAL A  96      17.572 -30.232 -47.540  1.00 22.90      A    C  
ANISOU  742  CB  VAL A  96     2901   3130   2669    243   -117    -18  A    C  
ATOM    743  CG1 VAL A  96      18.083 -30.113 -46.105  1.00 22.85      A    C  
ANISOU  743  CG1 VAL A  96     2909   3016   2757    304    -60      5  A    C  
ATOM    744  CG2 VAL A  96      16.287 -29.446 -47.721  1.00 23.98      A    C  
ANISOU  744  CG2 VAL A  96     2888   3415   2809    248   -170    132  A    C  
ATOM    745  N   ALA A  97      20.899 -29.838 -47.653  1.00 20.58      A    N  
ANISOU  745  N   ALA A  97     2667   2630   2523    416     80   -141  A    N  
ATOM    746  CA  ALA A  97      22.222 -30.414 -47.445  1.00 25.18      A    C  
ANISOU  746  CA  ALA A  97     3189   3080   3299    479    135   -179  A    C  
ATOM    747  C   ALA A  97      22.247 -31.449 -46.317  1.00 26.80      A    C  
ANISOU  747  C   ALA A  97     3395   3140   3648    478     12   -146  A    C  
ATOM    748  O   ALA A  97      22.860 -32.521 -46.436  1.00 24.68      A    O  
ANISOU  748  O   ALA A  97     3108   2715   3555    540     45   -198  A    O  
ATOM    749  CB  ALA A  97      23.225 -29.302 -47.142  1.00 25.78      A    C  
ANISOU  749  CB  ALA A  97     3159   3168   3468    501    146    -83  A    C  
ATOM    750  N   ARG A  98      21.588 -31.106 -45.220  1.00 24.63      A    N  
ANISOU  750  N   ARG A  98     3167   2893   3300    413   -102    -51  A    N  
ATOM    751  CA  ARG A  98      21.546 -31.952 -44.030  1.00 32.29      A    C  
ANISOU  751  CA  ARG A  98     4196   3743   4331    361   -233     28  A    C  
ATOM    752  C   ARG A  98      20.152 -31.940 -43.455  1.00 26.44      A    C  
ANISOU  752  C   ARG A  98     3545   3078   3423    259   -221     60  A    C  
ATOM    753  O   ARG A  98      19.533 -30.891 -43.361  1.00 25.00      A    O  
ANISOU  753  O   ARG A  98     3363   3012   3125    262   -143     71  A    O  
ATOM    754  CB  ARG A  98      22.502 -31.464 -42.935  1.00 31.85      A    C  
ANISOU  754  CB  ARG A  98     4139   3629   4332    336   -382    156  A    C  
ATOM    755  CG  ARG A  98      23.785 -30.865 -43.405  1.00 41.09      A    C  
ANISOU  755  CG  ARG A  98     5141   4799   5673    401   -382    176  A    C  
ATOM    756  CD  ARG A  98      24.771 -30.845 -42.282  1.00 33.11      A    C  
ANISOU  756  CD  ARG A  98     4095   3700   4785    328   -638    347  A    C  
ATOM    757  NE  ARG A  98      24.752 -29.601 -41.518  1.00 33.63      A    N  
ANISOU  757  NE  ARG A  98     4316   3817   4645    176   -736    386  A    N  
ATOM    758  CZ  ARG A  98      25.853 -28.929 -41.202  1.00 34.96      A    C  
ANISOU  758  CZ  ARG A  98     4395   3965   4922     81   -914    493  A    C  
ATOM    759  NH1 ARG A  98      27.032 -29.377 -41.616  1.00 34.62      A    N1+
ANISOU  759  NH1 ARG A  98     4023   3888   5244    157   -983    599  A    N1+
ATOM    760  NH2 ARG A  98      25.778 -27.821 -40.480  1.00 31.88      A    N  
ANISOU  760  NH2 ARG A  98     4239   3572   4304    -97  -1006    492  A    N  
ATOM    761  N   VAL A  99      19.678 -33.098 -43.028  1.00 25.66      A    N  
ANISOU  761  N   VAL A  99     3510   2890   3350    174   -275     92  A    N  
ATOM    762  CA  VAL A  99      18.371 -33.183 -42.407  1.00 20.14      A    C  
ANISOU  762  CA  VAL A  99     2849   2270   2531     50   -222    153  A    C  
ATOM    763  C   VAL A  99      18.532 -33.318 -40.904  1.00 24.33      A    C  
ANISOU  763  C   VAL A  99     3546   2727   2971    -42   -272    280  A    C  
ATOM    764  O   VAL A  99      19.319 -34.141 -40.428  1.00 25.46      A    O  
ANISOU  764  O   VAL A  99     3774   2703   3196    -70   -438    362  A    O  
ATOM    765  CB  VAL A  99      17.570 -34.365 -42.988  1.00 24.51      A    C  
ANISOU  765  CB  VAL A  99     3386   2785   3140    -64   -247    125  A    C  
ATOM    766  CG1 VAL A  99      16.256 -34.496 -42.288  1.00 28.32      A    C  
ANISOU  766  CG1 VAL A  99     3836   3364   3560   -218   -175    232  A    C  
ATOM    767  CG2 VAL A  99      17.343 -34.127 -44.495  1.00 23.99      A    C  
ANISOU  767  CG2 VAL A  99     3237   2816   3063    -34   -232      0  A    C  
ATOM    768  N   VAL A 100      17.796 -32.497 -40.157  1.00 23.84      A    N  
ANISOU  768  N   VAL A 100     3552   2769   2736    -87   -120    306  A    N  
ATOM    769  CA  VAL A 100      17.894 -32.495 -38.709  1.00 24.91      A    C  
ANISOU  769  CA  VAL A 100     3946   2848   2671   -222   -127    403  A    C  
ATOM    770  C   VAL A 100      16.868 -33.476 -38.143  1.00 29.88      A    C  
ANISOU  770  C   VAL A 100     4626   3479   3246   -388    -31    505  A    C  
ATOM    771  O   VAL A 100      15.670 -33.347 -38.396  1.00 31.02      A    O  
ANISOU  771  O   VAL A 100     4612   3754   3422   -398    193    491  A    O  
ATOM    772  CB  VAL A 100      17.658 -31.073 -38.138  1.00 24.85      A    C  
ANISOU  772  CB  VAL A 100     4076   2902   2464   -195     70    336  A    C  
ATOM    773  CG1 VAL A 100      17.808 -31.064 -36.638  1.00 28.67      A    C  
ANISOU  773  CG1 VAL A 100     4938   3316   2639   -387     67    405  A    C  
ATOM    774  CG2 VAL A 100      18.617 -30.075 -38.820  1.00 26.01      A    C  
ANISOU  774  CG2 VAL A 100     4157   3032   2694    -67    -30    253  A    C  
ATOM    775  N   ILE A 101      17.348 -34.470 -37.406  1.00 24.56      A    N  
ANISOU  775  N   ILE A 101     4142   2657   2534   -526   -221    647  A    N  
ATOM    776  CA  ILE A 101      16.488 -35.505 -36.861  1.00 25.81      A    C  
ANISOU  776  CA  ILE A 101     4381   2780   2646   -727   -155    781  A    C  
ATOM    777  C   ILE A 101      16.235 -35.310 -35.377  1.00 34.36      A    C  
ANISOU  777  C   ILE A 101     5799   3881   3375   -925    -36    904  A    C  
ATOM    778  O   ILE A 101      17.162 -35.100 -34.607  1.00 41.15      A    O  
ANISOU  778  O   ILE A 101     6893   4669   4075   -962   -238    950  A    O  
ATOM    779  CB  ILE A 101      17.109 -36.880 -37.073  1.00 29.67      A    C  
ANISOU  779  CB  ILE A 101     4904   3029   3339   -763   -438    886  A    C  
ATOM    780  CG1 ILE A 101      17.355 -37.097 -38.570  1.00 41.76      A    C  
ANISOU  780  CG1 ILE A 101     6190   4519   5158   -585   -483    712  A    C  
ATOM    781  CG2 ILE A 101      16.212 -37.965 -36.511  1.00 39.97      A    C  
ANISOU  781  CG2 ILE A 101     6323   4261   4602  -1014   -384   1050  A    C  
ATOM    782  CD1 ILE A 101      18.273 -38.254 -38.839  1.00 55.61      A    C  
ANISOU  782  CD1 ILE A 101     7996   5972   7161   -524   -708    759  A    C  
ATOM    783  N   GLY A 102      14.976 -35.424 -34.984  1.00 38.26      A    N  
ANISOU  783  N   GLY A 102     3925   5242   5368    727    568   -360  A    N  
ATOM    784  CA  GLY A 102      14.590 -35.158 -33.616  1.00 45.33      A    C  
ANISOU  784  CA  GLY A 102     4700   6276   6246    598    783   -603  A    C  
ATOM    785  C   GLY A 102      14.262 -36.401 -32.814  1.00 44.61      A    C  
ANISOU  785  C   GLY A 102     4792   6375   5781    318    769   -579  A    C  
ATOM    786  O   GLY A 102      15.102 -37.285 -32.640  1.00 40.88      A    O  
ANISOU  786  O   GLY A 102     4629   5867   5038    243    629   -489  A    O  
ATOM    787  N   SER A 103      13.024 -36.451 -32.332  1.00 40.97      A    N  
ANISOU  787  N   SER A 103     4110   6090   5366    170    938   -636  A    N  
ATOM    788  CA  SER A 103      12.595 -37.439 -31.349  1.00 40.22      A    C  
ANISOU  788  CA  SER A 103     4141   6186   4956   -115   1049   -605  A    C  
ATOM    789  C   SER A 103      12.657 -38.884 -31.842  1.00 33.56      A    C  
ANISOU  789  C   SER A 103     3536   5259   3955   -272    833   -339  A    C  
ATOM    790  O   SER A 103      12.803 -39.803 -31.038  1.00 37.77      A    O  
ANISOU  790  O   SER A 103     4289   5855   4206   -470    880   -221  A    O  
ATOM    791  CB  SER A 103      11.171 -37.120 -30.894  1.00 54.85      A    C  
ANISOU  791  CB  SER A 103     5635   8210   6995   -237   1331   -733  A    C  
ATOM    792  OG  SER A 103      10.274 -37.159 -31.990  1.00 65.14      A    O  
ANISOU  792  OG  SER A 103     6672   9436   8641   -192   1194   -632  A    O  
ATOM    793  N   THR A 104      12.540 -39.089 -33.154  1.00 31.88      A    N  
ANISOU  793  N   THR A 104     3278   4908   3926   -184    604   -245  A    N  
ATOM    794  CA  THR A 104      12.645 -40.436 -33.720  1.00 31.12      A    C  
ANISOU  794  CA  THR A 104     3379   4697   3746   -329    400    -91  A    C  
ATOM    795  C   THR A 104      13.987 -41.093 -33.373  1.00 31.29      A    C  
ANISOU  795  C   THR A 104     3776   4571   3540   -323    303      4  A    C  
ATOM    796  O   THR A 104      14.070 -42.317 -33.208  1.00 31.40      A    O  
ANISOU  796  O   THR A 104     3967   4478   3484   -504    242    146  A    O  
ATOM    797  CB  THR A 104      12.462 -40.412 -35.256  1.00 35.06      A    C  
ANISOU  797  CB  THR A 104     3789   5134   4399   -199    148    -83  A    C  
ATOM    798  CG2 THR A 104      12.549 -41.816 -35.843  1.00 33.56      A    C  
ANISOU  798  CG2 THR A 104     3772   4820   4158   -369    -43    -36  A    C  
ATOM    799  OG1 THR A 104      11.177 -39.867 -35.560  1.00 35.90      A    O  
ANISOU  799  OG1 THR A 104     3511   5388   4742   -192    173   -137  A    O  
ATOM    800  N   ALA A 105      15.032 -40.283 -33.255  1.00 28.73      A    N  
ANISOU  800  N   ALA A 105     3534   4207   3176   -113    290    -76  A    N  
ATOM    801  CA  ALA A 105      16.350 -40.806 -32.900  1.00 32.76      A    C  
ANISOU  801  CA  ALA A 105     4335   4582   3531    -76    168    -11  A    C  
ATOM    802  C   ALA A 105      16.389 -41.341 -31.467  1.00 33.56      A    C  
ANISOU  802  C   ALA A 105     4579   4826   3347   -245    248     86  A    C  
ATOM    803  O   ALA A 105      17.254 -42.151 -31.121  1.00 32.51      A    O  
ANISOU  803  O   ALA A 105     4686   4577   3087   -261    100    242  A    O  
ATOM    804  CB  ALA A 105      17.402 -39.743 -33.088  1.00 32.12      A    C  
ANISOU  804  CB  ALA A 105     4236   4424   3546    173    152   -159  A    C  
ATOM    805  N   VAL A 106      15.459 -40.885 -30.632  1.00 32.14      A    N  
ANISOU  805  N   VAL A 106     4244   4905   3061   -360    490     10  A    N  
ATOM    806  CA  VAL A 106      15.353 -41.392 -29.263  1.00 36.06      A    C  
ANISOU  806  CA  VAL A 106     4894   5620   3188   -542    619    137  A    C  
ATOM    807  C   VAL A 106      14.448 -42.606 -29.221  1.00 41.35      A    C  
ANISOU  807  C   VAL A 106     5598   6237   3877   -808    708    415  A    C  
ATOM    808  O   VAL A 106      14.791 -43.631 -28.636  1.00 42.30      A    O  
ANISOU  808  O   VAL A 106     5965   6303   3802   -929    661    717  A    O  
ATOM    809  CB  VAL A 106      14.802 -40.327 -28.298  1.00 45.47      A    C  
ANISOU  809  CB  VAL A 106     5905   7151   4221   -562    912   -132  A    C  
ATOM    810  CG1 VAL A 106      14.990 -40.772 -26.856  1.00 50.70      A    C  
ANISOU  810  CG1 VAL A 106     6798   8117   4349   -711   1012    -10  A    C  
ATOM    811  CG2 VAL A 106      15.488 -38.998 -28.540  1.00 41.07      A    C  
ANISOU  811  CG2 VAL A 106     5204   6557   3842   -309    868   -473  A    C  
ATOM    812  N   LYS A 107      13.291 -42.483 -29.863  1.00 39.58      A    N  
ANISOU  812  N   LYS A 107     5093   6001   3945   -892    825    324  A    N  
ATOM    813  CA  LYS A 107      12.269 -43.523 -29.836  1.00 47.34      A    C  
ANISOU  813  CA  LYS A 107     6006   6925   5058  -1176    953    509  A    C  
ATOM    814  C   LYS A 107      12.663 -44.778 -30.623  1.00 44.60      A    C  
ANISOU  814  C   LYS A 107     5819   6223   4904  -1238    705    692  A    C  
ATOM    815  O   LYS A 107      12.376 -45.896 -30.202  1.00 44.22      A    O  
ANISOU  815  O   LYS A 107     5867   6043   4893  -1472    795    953  A    O  
ATOM    816  CB  LYS A 107      10.945 -42.962 -30.372  1.00 51.31      A    C  
ANISOU  816  CB  LYS A 107     6089   7517   5891  -1223   1092    298  A    C  
ATOM    817  CG  LYS A 107      10.313 -41.928 -29.444  1.00 62.93      A    C  
ANISOU  817  CG  LYS A 107     7345   9299   7268  -1230   1440    108  A    C  
ATOM    818  CD  LYS A 107       9.104 -41.232 -30.061  1.00 66.41      A    C  
ANISOU  818  CD  LYS A 107     7310   9784   8139  -1204   1528   -113  A    C  
ATOM    819  CE  LYS A 107       8.400 -40.367 -29.020  1.00 72.04      A    C  
ANISOU  819  CE  LYS A 107     7780  10770   8821  -1253   1955   -329  A    C  
ATOM    820  NZ  LYS A 107       7.602 -39.261 -29.623  1.00 75.05      A    N1+
ANISOU  820  NZ  LYS A 107     7688  11153   9675  -1081   1985   -589  A    N1+
ATOM    821  N   SER A 108      13.331 -44.597 -31.756  1.00 39.38      A    N  
ANISOU  821  N   SER A 108     5181   5390   4390  -1034    430    551  A    N  
ATOM    822  CA  SER A 108      13.595 -45.722 -32.655  1.00 42.41      A    C  
ANISOU  822  CA  SER A 108     5658   5450   5004  -1096    224    600  A    C  
ATOM    823  C   SER A 108      15.024 -45.737 -33.175  1.00 38.48      A    C  
ANISOU  823  C   SER A 108     5387   4763   4471   -863     -8    570  A    C  
ATOM    824  O   SER A 108      15.255 -45.506 -34.360  1.00 36.09      A    O  
ANISOU  824  O   SER A 108     5035   4394   4283   -727   -157    376  A    O  
ATOM    825  CB  SER A 108      12.626 -45.681 -33.836  1.00 42.84      A    C  
ANISOU  825  CB  SER A 108     5429   5518   5332  -1143    139    375  A    C  
ATOM    826  OG  SER A 108      11.303 -45.469 -33.384  1.00 47.88      A    O  
ANISOU  826  OG  SER A 108     5775   6344   6074  -1324    356    353  A    O  
ATOM    827  N   PRO A 109      15.989 -46.037 -32.297  1.00 39.98      A    N  
ANISOU  827  N   PRO A 109     5815   4881   4495   -816    -38    771  A    N  
ATOM    828  CA  PRO A 109      17.400 -45.906 -32.665  1.00 33.58      A    C  
ANISOU  828  CA  PRO A 109     5157   3903   3698   -577   -237    714  A    C  
ATOM    829  C   PRO A 109      17.817 -46.890 -33.749  1.00 36.81      A    C  
ANISOU  829  C   PRO A 109     5627   3950   4409   -579   -387    657  A    C  
ATOM    830  O   PRO A 109      18.681 -46.560 -34.558  1.00 35.18      A    O  
ANISOU  830  O   PRO A 109     5449   3647   4272   -381   -489    480  A    O  
ATOM    831  CB  PRO A 109      18.141 -46.194 -31.346  1.00 34.95      A    C  
ANISOU  831  CB  PRO A 109     5531   4109   3641   -564   -275    980  A    C  
ATOM    832  CG  PRO A 109      17.092 -46.114 -30.282  1.00 47.82      A    C  
ANISOU  832  CG  PRO A 109     7122   6034   5013   -769    -38   1132  A    C  
ATOM    833  CD  PRO A 109      15.831 -46.553 -30.928  1.00 44.74      A    C  
ANISOU  833  CD  PRO A 109     6549   5568   4884   -980    101   1087  A    C  
ATOM    834  N   ASP A 110      17.200 -48.066 -33.791  1.00 34.84      A    N  
ANISOU  834  N   ASP A 110     5374   3490   4372   -811   -362    769  A    N  
ATOM    835  CA  ASP A 110      17.547 -49.030 -34.830  1.00 38.06      A    C  
ANISOU  835  CA  ASP A 110     5809   3539   5114   -834   -483    619  A    C  
ATOM    836  C   ASP A 110      17.131 -48.511 -36.201  1.00 39.14      A    C  
ANISOU  836  C   ASP A 110     5798   3825   5250   -776   -535    245  A    C  
ATOM    837  O   ASP A 110      17.853 -48.679 -37.190  1.00 38.45      A    O  
ANISOU  837  O   ASP A 110     5769   3597   5245   -653   -631     25  A    O  
ATOM    838  CB  ASP A 110      16.914 -50.388 -34.547  1.00 50.03      A    C  
ANISOU  838  CB  ASP A 110     7310   4750   6949  -1118   -421    791  A    C  
ATOM    839  CG  ASP A 110      17.576 -51.100 -33.385  1.00 61.13      A    C  
ANISOU  839  CG  ASP A 110     8912   5925   8391  -1128   -416   1239  A    C  
ATOM    840  OD1 ASP A 110      18.784 -50.863 -33.155  1.00 63.88      A    O  
ANISOU  840  OD1 ASP A 110     9401   6227   8644   -891   -558   1308  A    O  
ATOM    841  OD2 ASP A 110      16.892 -51.894 -32.706  1.00 65.74      A    O1-
ANISOU  841  OD2 ASP A 110     9493   6374   9112  -1368   -275   1543  A    O1-
ATOM    842  N   VAL A 111      15.978 -47.851 -36.254  1.00 37.41      A    N  
ANISOU  842  N   VAL A 111     5377   3916   4920   -852   -468    183  A    N  
ATOM    843  CA  VAL A 111      15.518 -47.238 -37.495  1.00 32.23      A    C  
ANISOU  843  CA  VAL A 111     4569   3473   4204   -763   -565    -93  A    C  
ATOM    844  C   VAL A 111      16.484 -46.161 -37.958  1.00 31.32      A    C  
ANISOU  844  C   VAL A 111     4545   3466   3890   -455   -588   -138  A    C  
ATOM    845  O   VAL A 111      16.856 -46.112 -39.127  1.00 30.67      A    O  
ANISOU  845  O   VAL A 111     4500   3393   3761   -341   -677   -323  A    O  
ATOM    846  CB  VAL A 111      14.112 -46.617 -37.340  1.00 34.01      A    C  
ANISOU  846  CB  VAL A 111     4510   4003   4409   -860   -505   -104  A    C  
ATOM    847  CG1 VAL A 111      13.744 -45.783 -38.572  1.00 37.22      A    C  
ANISOU  847  CG1 VAL A 111     4763   4672   4706   -691   -656   -297  A    C  
ATOM    848  CG2 VAL A 111      13.079 -47.701 -37.091  1.00 39.89      A    C  
ANISOU  848  CG2 VAL A 111     5102   4625   5429  -1191   -460   -113  A    C  
ATOM    849  N   VAL A 112      16.903 -45.303 -37.037  1.00 29.56      A    N  
ANISOU  849  N   VAL A 112     4350   3328   3554   -332   -484     14  A    N  
ATOM    850  CA  VAL A 112      17.698 -44.143 -37.423  1.00 25.75      A    C  
ANISOU  850  CA  VAL A 112     3884   2923   2978    -61   -461    -35  A    C  
ATOM    851  C   VAL A 112      19.138 -44.565 -37.731  1.00 27.38      A    C  
ANISOU  851  C   VAL A 112     4284   2862   3258     62   -506    -78  A    C  
ATOM    852  O   VAL A 112      19.784 -43.973 -38.593  1.00 28.10      A    O  
ANISOU  852  O   VAL A 112     4394   2953   3329    247   -480   -172  A    O  
ATOM    853  CB  VAL A 112      17.647 -43.046 -36.337  1.00 32.72      A    C  
ANISOU  853  CB  VAL A 112     4677   3967   3787     13   -328     42  A    C  
ATOM    854  CG1 VAL A 112      18.674 -41.942 -36.618  1.00 32.36      A    C  
ANISOU  854  CG1 VAL A 112     4638   3889   3768    275   -283    -19  A    C  
ATOM    855  CG2 VAL A 112      16.241 -42.454 -36.285  1.00 31.43      A    C  
ANISOU  855  CG2 VAL A 112     4260   4053   3629    -58   -248     28  A    C  
ATOM    856  N   LYS A 113      19.630 -45.625 -37.087  1.00 28.85      A    N  
ANISOU  856  N   LYS A 113     4596   2799   3566    -38   -559     10  A    N  
ATOM    857  CA  LYS A 113      20.932 -46.173 -37.484  1.00 29.14      A    C  
ANISOU  857  CA  LYS A 113     4761   2534   3778     77   -612    -64  A    C  
ATOM    858  C   LYS A 113      20.935 -46.564 -38.969  1.00 33.55      A    C  
ANISOU  858  C   LYS A 113     5330   3035   4382     85   -614   -323  A    C  
ATOM    859  O   LYS A 113      21.952 -46.448 -39.655  1.00 34.62      A    O  
ANISOU  859  O   LYS A 113     5525   3051   4579    242   -566   -462  A    O  
ATOM    860  CB  LYS A 113      21.307 -47.397 -36.646  1.00 33.52      A    C  
ANISOU  860  CB  LYS A 113     5418   2786   4533    -31   -698    115  A    C  
ATOM    861  CG  LYS A 113      21.809 -47.101 -35.233  1.00 28.35      A    C  
ANISOU  861  CG  LYS A 113     4813   2188   3770     29   -748    368  A    C  
ATOM    862  CD  LYS A 113      22.280 -48.408 -34.600  1.00 31.73      A    C  
ANISOU  862  CD  LYS A 113     5355   2279   4423    -36   -868    617  A    C  
ATOM    863  CE  LYS A 113      22.692 -48.217 -33.147  1.00 34.43      A    C  
ANISOU  863  CE  LYS A 113     5771   2760   4551     14   -971    919  A    C  
ATOM    864  NZ  LYS A 113      23.188 -49.497 -32.554  1.00 39.30      A    N1+
ANISOU  864  NZ  LYS A 113     6501   3032   5400    -11  -1120   1260  A    N1+
ATOM    865  N   GLY A 114      19.795 -47.051 -39.448  1.00 28.61      A    N  
ANISOU  865  N   GLY A 114     4633   2515   3724    -98   -660   -420  A    N  
ATOM    866  CA  GLY A 114      19.649 -47.402 -40.849  1.00 35.73      A    C  
ANISOU  866  CA  GLY A 114     5537   3467   4573   -112   -699   -723  A    C  
ATOM    867  C   GLY A 114      19.773 -46.185 -41.752  1.00 33.65      A    C  
ANISOU  867  C   GLY A 114     5264   3517   4005    100   -650   -757  A    C  
ATOM    868  O   GLY A 114      20.285 -46.281 -42.876  1.00 33.22      A    O  
ANISOU  868  O   GLY A 114     5294   3494   3834    184   -616   -965  A    O  
ATOM    869  N   TRP A 115      19.295 -45.045 -41.267  1.00 29.42      A    N  
ANISOU  869  N   TRP A 115     4621   3205   3353    184   -617   -547  A    N  
ATOM    870  CA  TRP A 115      19.381 -43.798 -42.029  1.00 31.86      A    C  
ANISOU  870  CA  TRP A 115     4897   3753   3454    402   -549   -482  A    C  
ATOM    871  C   TRP A 115      20.840 -43.368 -42.201  1.00 28.29      A    C  
ANISOU  871  C   TRP A 115     4563   3114   3071    596   -377   -474  A    C  
ATOM    872  O   TRP A 115      21.239 -42.912 -43.280  1.00 29.72      A    O  
ANISOU  872  O   TRP A 115     4805   3400   3088    739   -279   -499  A    O  
ATOM    873  CB  TRP A 115      18.584 -42.674 -41.363  1.00 28.38      A    C  
ANISOU  873  CB  TRP A 115     4268   3498   3016    456   -522   -279  A    C  
ATOM    874  CG  TRP A 115      17.126 -42.948 -41.178  1.00 28.22      A    C  
ANISOU  874  CG  TRP A 115     4064   3667   2991    280   -651   -287  A    C  
ATOM    875  CD1 TRP A 115      16.428 -44.059 -41.584  1.00 33.95      A    C  
ANISOU  875  CD1 TRP A 115     4762   4418   3720     69   -806   -462  A    C  
ATOM    876  CD2 TRP A 115      16.188 -42.105 -40.517  1.00 32.22      A    C  
ANISOU  876  CD2 TRP A 115     4340   4333   3569    287   -611   -160  A    C  
ATOM    877  CE2 TRP A 115      14.936 -42.755 -40.554  1.00 34.55      A    C  
ANISOU  877  CE2 TRP A 115     4465   4755   3908     77   -741   -241  A    C  
ATOM    878  CE3 TRP A 115      16.281 -40.849 -39.897  1.00 26.09      A    C  
ANISOU  878  CE3 TRP A 115     3450   3581   2883    445   -456    -32  A    C  
ATOM    879  NE1 TRP A 115      15.108 -43.949 -41.208  1.00 34.29      A    N  
ANISOU  879  NE1 TRP A 115     4556   4630   3840    -61   -869   -429  A    N  
ATOM    880  CZ2 TRP A 115      13.788 -42.198 -39.997  1.00 35.62      A    C  
ANISOU  880  CZ2 TRP A 115     4316   5051   4169     30   -707   -177  A    C  
ATOM    881  CZ3 TRP A 115      15.132 -40.298 -39.338  1.00 30.40      A    C  
ANISOU  881  CZ3 TRP A 115     3727   4280   3545    401   -419      6  A    C  
ATOM    882  CH2 TRP A 115      13.908 -40.972 -39.395  1.00 34.42      A    C  
ANISOU  882  CH2 TRP A 115     4066   4924   4087    200   -537    -55  A    C  
ATOM    883  N   PHE A 116      21.640 -43.517 -41.151  1.00 31.50      A    N  
ANISOU  883  N   PHE A 116     4991   3262   3716    601   -337   -431  A    N  
ATOM    884  CA  PHE A 116      23.066 -43.223 -41.256  1.00 28.92      A    C  
ANISOU  884  CA  PHE A 116     4717   2718   3555    767   -196   -471  A    C  
ATOM    885  C   PHE A 116      23.734 -44.115 -42.294  1.00 31.98      A    C  
ANISOU  885  C   PHE A 116     5224   2960   3966    766   -142   -695  A    C  
ATOM    886  O   PHE A 116      24.590 -43.663 -43.045  1.00 33.88      A    O  
ANISOU  886  O   PHE A 116     5497   3165   4211    912     53   -755  A    O  
ATOM    887  CB  PHE A 116      23.763 -43.376 -39.897  1.00 32.68      A    C  
ANISOU  887  CB  PHE A 116     5167   2976   4273    765   -256   -411  A    C  
ATOM    888  CG  PHE A 116      23.660 -42.160 -39.035  1.00 30.12      A    C  
ANISOU  888  CG  PHE A 116     4714   2777   3951    841   -210   -306  A    C  
ATOM    889  CD1 PHE A 116      24.601 -41.149 -39.132  1.00 31.23      A    C  
ANISOU  889  CD1 PHE A 116     4689   2910   4267    932    -45   -318  A    C  
ATOM    890  CD2 PHE A 116      22.605 -42.007 -38.144  1.00 31.92      A    C  
ANISOU  890  CD2 PHE A 116     4880   3200   4049    722   -278   -210  A    C  
ATOM    891  CE1 PHE A 116      24.504 -40.014 -38.347  1.00 28.11      A    C  
ANISOU  891  CE1 PHE A 116     4129   2608   3945    956     10   -294  A    C  
ATOM    892  CE2 PHE A 116      22.497 -40.867 -37.366  1.00 31.95      A    C  
ANISOU  892  CE2 PHE A 116     4745   3322   4074    787   -203   -198  A    C  
ATOM    893  CZ  PHE A 116      23.453 -39.867 -37.470  1.00 30.75      A    C  
ANISOU  893  CZ  PHE A 116     4501   3058   4125    966    -79   -276  A    C  
ATOM    894  N   GLU A 117      23.341 -45.385 -42.352  1.00 32.26      A    N  
ANISOU  894  N   GLU A 117     5967   2153   4137    845    151   -359  A    N  
ATOM    895  CA  GLU A 117      23.924 -46.283 -43.327  1.00 32.97      A    C  
ANISOU  895  CA  GLU A 117     6098   2208   4220    992    113   -537  A    C  
ATOM    896  C   GLU A 117      23.501 -45.878 -44.743  1.00 37.61      A    C  
ANISOU  896  C   GLU A 117     6559   2898   4833    831    116   -726  A    C  
ATOM    897  O   GLU A 117      24.300 -45.935 -45.671  1.00 39.96      A    O  
ANISOU  897  O   GLU A 117     6716   3408   5059    975     57   -892  A    O  
ATOM    898  CB  GLU A 117      23.527 -47.729 -43.019  1.00 48.55      A    C  
ANISOU  898  CB  GLU A 117     8308   3875   6264    961    142   -503  A    C  
ATOM    899  CG  GLU A 117      23.929 -48.128 -41.596  1.00 65.84      A    C  
ANISOU  899  CG  GLU A 117    10643   5979   8395   1114    133   -309  A    C  
ATOM    900  CD  GLU A 117      23.438 -49.502 -41.182  1.00 74.09      A    C  
ANISOU  900  CD  GLU A 117    11966   6690   9494   1049    158   -244  A    C  
ATOM    901  OE1 GLU A 117      22.637 -50.107 -41.930  1.00 79.69      A    O  
ANISOU  901  OE1 GLU A 117    12751   7227  10301    837    191   -341  A    O  
ATOM    902  OE2 GLU A 117      23.842 -49.964 -40.092  1.00 72.16      A    O1-
ANISOU  902  OE2 GLU A 117    11873   6360   9182   1200    142    -97  A    O1-
ATOM    903  N   ARG A 118      22.257 -45.437 -44.897  1.00 38.09      A    N  
ANISOU  903  N   ARG A 118     6553   2945   4973    500    175   -679  A    N  
ATOM    904  CA  ARG A 118      21.742 -45.094 -46.222  1.00 39.34      A    C  
ANISOU  904  CA  ARG A 118     6502   3298   5146    298    171   -818  A    C  
ATOM    905  C   ARG A 118      22.219 -43.735 -46.711  1.00 33.93      A    C  
ANISOU  905  C   ARG A 118     5492   3017   4384    287    101   -790  A    C  
ATOM    906  O   ARG A 118      22.689 -43.603 -47.853  1.00 29.87      A    O  
ANISOU  906  O   ARG A 118     4803   2744   3803    299     54   -923  A    O  
ATOM    907  CB  ARG A 118      20.207 -45.121 -46.241  1.00 41.68      A    C  
ANISOU  907  CB  ARG A 118     6821   3491   5526    -35    252   -787  A    C  
ATOM    908  CG  ARG A 118      19.629 -44.632 -47.570  1.00 42.87      A    C  
ANISOU  908  CG  ARG A 118     6719   3904   5666   -228    237   -910  A    C  
ATOM    909  CD  ARG A 118      18.105 -44.756 -47.681  1.00 37.82      A    C  
ANISOU  909  CD  ARG A 118     6064   3232   5075   -546    314   -917  A    C  
ATOM    910  NE  ARG A 118      17.643 -44.017 -48.859  1.00 35.85      A    N  
ANISOU  910  NE  ARG A 118     5524   3313   4784   -673    277   -995  A    N  
ATOM    911  CZ  ARG A 118      16.372 -43.759 -49.157  1.00 33.70      A    C  
ANISOU  911  CZ  ARG A 118     5119   3177   4510   -910    315  -1007  A    C  
ATOM    912  NH1 ARG A 118      15.392 -44.186 -48.369  1.00 33.09      A    N1+
ANISOU  912  NH1 ARG A 118     5148   2962   4463  -1088    402   -959  A    N1+
ATOM    913  NH2 ARG A 118      16.085 -43.064 -50.252  1.00 34.29      A    N  
ANISOU  913  NH2 ARG A 118     4936   3568   4525   -971    262  -1061  A    N  
ATOM    914  N   PHE A 119      22.076 -42.724 -45.859  1.00 25.75      A    N  
ANISOU  914  N   PHE A 119     4388   2052   3343    245     93   -620  A    N  
ATOM    915  CA  PHE A 119      22.284 -41.344 -46.270  1.00 29.49      A    C  
ANISOU  915  CA  PHE A 119     4619   2827   3760    165     25   -568  A    C  
ATOM    916  C   PHE A 119      23.675 -40.816 -45.961  1.00 31.52      A    C  
ANISOU  916  C   PHE A 119     4787   3290   3899    328    -48   -537  A    C  
ATOM    917  O   PHE A 119      24.098 -39.829 -46.550  1.00 29.68      A    O  
ANISOU  917  O   PHE A 119     4367   3323   3588    239   -115   -520  A    O  
ATOM    918  CB  PHE A 119      21.252 -40.433 -45.610  1.00 29.72      A    C  
ANISOU  918  CB  PHE A 119     4629   2819   3845     20     42   -434  A    C  
ATOM    919  CG  PHE A 119      19.828 -40.751 -45.979  1.00 30.21      A    C  
ANISOU  919  CG  PHE A 119     4697   2801   3981   -169    107   -470  A    C  
ATOM    920  CD1 PHE A 119      19.366 -40.548 -47.279  1.00 30.35      A    C  
ANISOU  920  CD1 PHE A 119     4558   2988   3986   -301     83   -558  A    C  
ATOM    921  CD2 PHE A 119      18.948 -41.235 -45.027  1.00 30.92      A    C  
ANISOU  921  CD2 PHE A 119     4924   2702   4122   -235    191   -414  A    C  
ATOM    922  CE1 PHE A 119      18.047 -40.822 -47.611  1.00 30.49      A    C  
ANISOU  922  CE1 PHE A 119     4545   2998   4043   -481    140   -605  A    C  
ATOM    923  CE2 PHE A 119      17.628 -41.529 -45.347  1.00 33.25      A    C  
ANISOU  923  CE2 PHE A 119     5188   2994   4451   -444    256   -459  A    C  
ATOM    924  CZ  PHE A 119      17.172 -41.322 -46.646  1.00 31.95      A    C  
ANISOU  924  CZ  PHE A 119     4853   3012   4275   -562    228   -564  A    C  
ATOM    925  N   GLY A 120      24.378 -41.463 -45.035  1.00 30.19      A    N  
ANISOU  925  N   GLY A 120     4754   3018   3699    550    -39   -521  A    N  
ATOM    926  CA  GLY A 120      25.698 -41.007 -44.616  1.00 30.19      A    C  
ANISOU  926  CA  GLY A 120     4646   3266   3558    709   -105   -502  A    C  
ATOM    927  C   GLY A 120      25.663 -39.943 -43.533  1.00 30.94      A    C  
ANISOU  927  C   GLY A 120     4723   3390   3642    641   -122   -354  A    C  
ATOM    928  O   GLY A 120      24.694 -39.175 -43.409  1.00 28.61      A    O  
ANISOU  928  O   GLY A 120     4430   3010   3430    451   -110   -277  A    O  
ATOM    929  N   ALA A 121      26.738 -39.885 -42.745  1.00 24.58      A    N  
ANISOU  929  N   ALA A 121     3891   2732   2715    816   -159   -333  A    N  
ATOM    930  CA  ALA A 121      26.795 -39.030 -41.571  1.00 28.53      A    C  
ANISOU  930  CA  ALA A 121     4397   3255   3187    781   -174   -221  A    C  
ATOM    931  C   ALA A 121      26.797 -37.540 -41.911  1.00 29.92      A    C  
ANISOU  931  C   ALA A 121     4429   3600   3339    532   -238   -192  A    C  
ATOM    932  O   ALA A 121      26.386 -36.709 -41.094  1.00 26.25      A    O  
ANISOU  932  O   ALA A 121     4010   3058   2904    450   -248   -117  A    O  
ATOM    933  CB  ALA A 121      28.021 -39.377 -40.752  1.00 35.36      A    C  
ANISOU  933  CB  ALA A 121     5239   4299   3896   1032   -205   -227  A    C  
ATOM    934  N   GLN A 122      27.263 -37.194 -43.108  1.00 28.53      A    N  
ANISOU  934  N   GLN A 122     4097   3648   3094    413   -288   -251  A    N  
ATOM    935  CA  GLN A 122      27.329 -35.787 -43.484  1.00 29.84      A    C  
ANISOU  935  CA  GLN A 122     4176   3942   3220    155   -362   -195  A    C  
ATOM    936  C   GLN A 122      25.949 -35.222 -43.824  1.00 31.12      A    C  
ANISOU  936  C   GLN A 122     4428   3862   3535      7   -357   -132  A    C  
ATOM    937  O   GLN A 122      25.778 -34.010 -43.884  1.00 32.02      A    O  
ANISOU  937  O   GLN A 122     4555   3966   3646   -163   -426    -63  A    O  
ATOM    938  CB  GLN A 122      28.287 -35.582 -44.663  1.00 34.00      A    C  
ANISOU  938  CB  GLN A 122     4502   4830   3588     41   -418   -253  A    C  
ATOM    939  CG  GLN A 122      29.765 -35.748 -44.299  1.00 39.56      A    C  
ANISOU  939  CG  GLN A 122     5051   5899   4080    146   -449   -319  A    C  
ATOM    940  CD  GLN A 122      30.216 -34.820 -43.169  1.00 45.49      A    C  
ANISOU  940  CD  GLN A 122     5822   6699   4764     56   -492   -254  A    C  
ATOM    941  NE2 GLN A 122      31.157 -35.293 -42.362  1.00 49.39      A    N  
ANISOU  941  NE2 GLN A 122     6240   7405   5119    261   -491   -309  A    N  
ATOM    942  OE1 GLN A 122      29.727 -33.695 -43.027  1.00 40.63      A    O  
ANISOU  942  OE1 GLN A 122     5295   5935   4209   -176   -533   -168  A    O  
ATOM    943  N   ALA A 123      24.959 -36.088 -44.024  1.00 23.73      A    N  
ANISOU  943  N   ALA A 123     3564   2733   2720     74   -282   -160  A    N  
ATOM    944  CA  ALA A 123      23.631 -35.616 -44.422  1.00 25.76      A    C  
ANISOU  944  CA  ALA A 123     3855   2845   3088    -46   -278   -121  A    C  
ATOM    945  C   ALA A 123      22.648 -35.546 -43.262  1.00 22.59      A    C  
ANISOU  945  C   ALA A 123     3573   2233   2779     10   -228    -77  A    C  
ATOM    946  O   ALA A 123      21.476 -35.192 -43.450  1.00 24.09      A    O  
ANISOU  946  O   ALA A 123     3769   2343   3041    -50   -221    -62  A    O  
ATOM    947  CB  ALA A 123      23.057 -36.520 -45.533  1.00 23.76      A    C  
ANISOU  947  CB  ALA A 123     3558   2591   2878    -71   -229   -202  A    C  
ATOM    948  N   LEU A 124      23.109 -35.891 -42.060  1.00 25.28      A    N  
ANISOU  948  N   LEU A 124     3985   2529   3090    136   -194    -61  A    N  
ATOM    949  CA  LEU A 124      22.201 -36.025 -40.922  1.00 23.12      A    C  
ANISOU  949  CA  LEU A 124     3809   2103   2873    188   -130    -22  A    C  
ATOM    950  C   LEU A 124      22.719 -35.257 -39.723  1.00 25.31      A    C  
ANISOU  950  C   LEU A 124     4112   2420   3085    247   -169     11  A    C  
ATOM    951  O   LEU A 124      23.905 -35.332 -39.396  1.00 27.57      A    O  
ANISOU  951  O   LEU A 124     4376   2826   3273    313   -200      7  A    O  
ATOM    952  CB  LEU A 124      22.020 -37.507 -40.537  1.00 22.35      A    C  
ANISOU  952  CB  LEU A 124     3815   1880   2797    276    -26    -22  A    C  
ATOM    953  CG  LEU A 124      21.498 -38.457 -41.627  1.00 25.03      A    C  
ANISOU  953  CG  LEU A 124     4166   2146   3200    206     22    -87  A    C  
ATOM    954  CD1 LEU A 124      21.525 -39.902 -41.128  1.00 29.18      A    C  
ANISOU  954  CD1 LEU A 124     4870   2481   3735    294    104    -79  A    C  
ATOM    955  CD2 LEU A 124      20.090 -38.073 -42.014  1.00 26.73      A    C  
ANISOU  955  CD2 LEU A 124     4325   2348   3482     50     48    -95  A    C  
ATOM    956  N   VAL A 125      21.829 -34.511 -39.083  1.00 23.20      A    N  
ANISOU  956  N   VAL A 125     3874   2087   2852    233   -174     22  A    N  
ATOM    957  CA  VAL A 125      22.154 -33.800 -37.851  1.00 23.16      A    C  
ANISOU  957  CA  VAL A 125     3903   2111   2784    293   -205     23  A    C  
ATOM    958  C   VAL A 125      21.249 -34.335 -36.753  1.00 26.41      A    C  
ANISOU  958  C   VAL A 125     4358   2476   3200    374   -108     45  A    C  
ATOM    959  O   VAL A 125      20.022 -34.324 -36.879  1.00 29.95      A    O  
ANISOU  959  O   VAL A 125     4790   2885   3705    343    -67     32  A    O  
ATOM    960  CB  VAL A 125      21.970 -32.270 -37.985  1.00 22.20      A    C  
ANISOU  960  CB  VAL A 125     3799   1962   2673    221   -318     -8  A    C  
ATOM    961  CG1 VAL A 125      22.320 -31.570 -36.652  1.00 25.02      A    C  
ANISOU  961  CG1 VAL A 125     4204   2343   2957    279   -352    -45  A    C  
ATOM    962  CG2 VAL A 125      22.831 -31.719 -39.122  1.00 26.07      A    C  
ANISOU  962  CG2 VAL A 125     4261   2508   3135     77   -414      4  A    C  
ATOM    963  N   LEU A 126      21.858 -34.814 -35.673  1.00 22.75      A    N  
ANISOU  963  N   LEU A 126     3932   2063   2649    474    -72     81  A    N  
ATOM    964  CA  LEU A 126      21.100 -35.316 -34.541  1.00 22.46      A    C  
ANISOU  964  CA  LEU A 126     3937   2019   2576    528     20    127  A    C  
ATOM    965  C   LEU A 126      20.727 -34.149 -33.617  1.00 27.80      A    C  
ANISOU  965  C   LEU A 126     4579   2778   3205    560    -21     61  A    C  
ATOM    966  O   LEU A 126      21.604 -33.529 -33.007  1.00 30.28      A    O  
ANISOU  966  O   LEU A 126     4891   3175   3439    607    -86     27  A    O  
ATOM    967  CB  LEU A 126      21.931 -36.368 -33.805  1.00 25.67      A    C  
ANISOU  967  CB  LEU A 126     4421   2444   2890    644     66    215  A    C  
ATOM    968  CG  LEU A 126      21.383 -36.912 -32.495  1.00 34.61      A    C  
ANISOU  968  CG  LEU A 126     5617   3596   3938    690    154    304  A    C  
ATOM    969  CD1 LEU A 126      20.141 -37.694 -32.769  1.00 36.15      A    C  
ANISOU  969  CD1 LEU A 126     5863   3674   4197    562    256    352  A    C  
ATOM    970  CD2 LEU A 126      22.420 -37.777 -31.786  1.00 33.39      A    C  
ANISOU  970  CD2 LEU A 126     5553   3467   3666    850    162    405  A    C  
ATOM    971  N   ALA A 127      19.440 -33.831 -33.519  1.00 25.01      A    N  
ANISOU  971  N   ALA A 127     4188   2430   2884    542     11     21  A    N  
ATOM    972  CA  ALA A 127      19.010 -32.754 -32.633  1.00 29.29      A    C  
ANISOU  972  CA  ALA A 127     4701   3057   3372    622    -32    -77  A    C  
ATOM    973  C   ALA A 127      18.726 -33.308 -31.249  1.00 36.29      A    C  
ANISOU  973  C   ALA A 127     5569   4087   4131    679     65    -38  A    C  
ATOM    974  O   ALA A 127      17.968 -34.263 -31.081  1.00 38.32      A    O  
ANISOU  974  O   ALA A 127     5811   4382   4366    621    179     43  A    O  
ATOM    975  CB  ALA A 127      17.788 -32.044 -33.179  1.00 35.42      A    C  
ANISOU  975  CB  ALA A 127     5422   3825   4210    635    -64   -164  A    C  
ATOM    976  N   LEU A 128      19.364 -32.717 -30.254  1.00 29.07      A    N  
ANISOU  976  N   LEU A 128     4660   3269   3116    763     19    -90  A    N  
ATOM    977  CA  LEU A 128      19.164 -33.144 -28.881  1.00 24.80      A    C  
ANISOU  977  CA  LEU A 128     4091   2911   2423    824    101    -52  A    C  
ATOM    978  C   LEU A 128      18.648 -31.965 -28.069  1.00 31.55      A    C  
ANISOU  978  C   LEU A 128     4881   3902   3206    920     52   -229  A    C  
ATOM    979  O   LEU A 128      19.410 -31.047 -27.768  1.00 34.80      A    O  
ANISOU  979  O   LEU A 128     5324   4307   3590    967    -51   -341  A    O  
ATOM    980  CB  LEU A 128      20.466 -33.669 -28.286  1.00 27.81      A    C  
ANISOU  980  CB  LEU A 128     4520   3345   2700    873     96     41  A    C  
ATOM    981  CG  LEU A 128      21.085 -34.882 -28.967  1.00 36.19      A    C  
ANISOU  981  CG  LEU A 128     5665   4279   3807    852    131    195  A    C  
ATOM    982  CD1 LEU A 128      22.372 -35.285 -28.265  1.00 34.80      A    C  
ANISOU  982  CD1 LEU A 128     5514   4218   3491    972    107    265  A    C  
ATOM    983  CD2 LEU A 128      20.085 -36.002 -28.971  1.00 36.55      A    C  
ANISOU  983  CD2 LEU A 128     5765   4255   3867    777    255    322  A    C  
ATOM    984  N   ASP A 129      17.356 -31.975 -27.750  1.00 30.43      A    N  
ANISOU  984  N   ASP A 129     4645   3897   3021    944    120   -276  A    N  
ATOM    985  CA  ASP A 129      16.781 -30.981 -26.851  1.00 28.26      A    C  
ANISOU  985  CA  ASP A 129     4290   3805   2643   1085     83   -467  A    C  
ATOM    986  C   ASP A 129      17.064 -31.383 -25.416  1.00 37.06      A    C  
ANISOU  986  C   ASP A 129     5355   5170   3554   1116    155   -427  A    C  
ATOM    987  O   ASP A 129      16.502 -32.360 -24.915  1.00 37.20      A    O  
ANISOU  987  O   ASP A 129     5311   5361   3462   1045    286   -290  A    O  
ATOM    988  CB  ASP A 129      15.277 -30.846 -27.070  1.00 34.01      A    C  
ANISOU  988  CB  ASP A 129     4887   4673   3364   1126    127   -553  A    C  
ATOM    989  CG  ASP A 129      14.935 -30.356 -28.467  1.00 46.30      A    C  
ANISOU  989  CG  ASP A 129     6480   6017   5095   1130     40   -597  A    C  
ATOM    990  OD1 ASP A 129      15.851 -29.874 -29.157  1.00 47.07      A    O  
ANISOU  990  OD1 ASP A 129     6717   5856   5310   1109    -69   -589  A    O  
ATOM    991  OD2 ASP A 129      13.755 -30.446 -28.863  1.00 50.69      A    O1-
ANISOU  991  OD2 ASP A 129     6911   6705   5645   1146     81   -637  A    O1-
ATOM    992  N   VAL A 130      17.892 -30.601 -24.733  1.00 34.15      A    N  
ANISOU  992  N   VAL A 130     5018   4841   3116   1202     68   -549  A    N  
ATOM    993  CA AVAL A 130      18.396 -30.954 -23.417  0.70 31.82      A    C  
ANISOU  993  CA AVAL A 130     4678   4800   2614   1237    117   -505  A    C  
ATOM    994  CA BVAL A 130      18.323 -31.003 -23.403  0.30 32.52      A    C  
ANISOU  994  CA BVAL A 130     4760   4898   2698   1236    126   -499  A    C  
ATOM    995  C   VAL A 130      17.849 -30.079 -22.290  1.00 40.48      A    C  
ANISOU  995  C   VAL A 130     5666   6167   3548   1375     99   -735  A    C  
ATOM    996  O   VAL A 130      17.790 -28.858 -22.425  1.00 35.55      A    O  
ANISOU  996  O   VAL A 130     5080   5445   2983   1471    -20   -978  A    O  
ATOM    997  CB AVAL A 130      19.936 -30.863 -23.412  0.70 33.04      A    C  
ANISOU  997  CB AVAL A 130     4915   4876   2761   1219     36   -474  A    C  
ATOM    998  CB BVAL A 130      19.865 -31.131 -23.316  0.30 34.29      A    C  
ANISOU  998  CB BVAL A 130     5066   5065   2899   1216     64   -429  A    C  
ATOM    999  CG1AVAL A 130      20.494 -31.120 -22.027  0.70 34.21      A    C  
ANISOU  999  CG1AVAL A 130     4999   5328   2669   1284     68   -447  A    C  
ATOM   1000  CG1BVAL A 130      20.341 -32.312 -24.152  0.30 37.47      A    C  
ANISOU 1000  CG1BVAL A 130     5549   5295   3393   1131    112   -187  A    C  
ATOM   1001  CG2AVAL A 130      20.511 -31.829 -24.443  0.70 37.86      A    C  
ANISOU 1001  CG2AVAL A 130     5610   5282   3494   1127     58   -264  A    C  
ATOM   1002  CG2BVAL A 130      20.551 -29.845 -23.742  0.30 32.00      A    C  
ANISOU 1002  CG2BVAL A 130     4842   4621   2696   1212    -90   -634  A    C  
ATOM   1003  N   ARG A 131      17.469 -30.711 -21.190  1.00 34.87      A    N  
ANISOU 1003  N   ARG A 131     4089   3622   5537   1576   -450    206  A    N  
ATOM   1004  CA  ARG A 131      17.125 -30.020 -19.970  1.00 42.07      A    C  
ANISOU 1004  CA  ARG A 131     5222   4397   6366   1870   -181      0  A    C  
ATOM   1005  C   ARG A 131      18.070 -30.568 -18.916  1.00 39.48      A    C  
ANISOU 1005  C   ARG A 131     5392   4098   5512   1847    -10      2  A    C  
ATOM   1006  O   ARG A 131      18.109 -31.779 -18.693  1.00 39.00      A    O  
ANISOU 1006  O   ARG A 131     5343   4167   5310   1692    251    107  A    O  
ATOM   1007  CB  ARG A 131      15.672 -30.270 -19.582  1.00 44.98      A    C  
ANISOU 1007  CB  ARG A 131     5234   4802   7056   2021    319   -123  A    C  
ATOM   1008  CG  ARG A 131      15.164 -29.375 -18.474  1.00 65.53      A    C  
ANISOU 1008  CG  ARG A 131     7977   7297   9626   2374    603   -417  A    C  
ATOM   1009  CD  ARG A 131      13.823 -29.853 -17.969  1.00 74.33      A    C  
ANISOU 1009  CD  ARG A 131     8716   8535  10992   2479   1239   -526  A    C  
ATOM   1010  NE  ARG A 131      13.957 -30.981 -17.055  1.00 84.82      A    N  
ANISOU 1010  NE  ARG A 131    10283  10055  11890   2344   1758   -413  A    N  
ATOM   1011  CZ  ARG A 131      14.160 -30.857 -15.747  1.00 91.92      A    C  
ANISOU 1011  CZ  ARG A 131    11632  11005  12290   2498   2132   -555  A    C  
ATOM   1012  NH1 ARG A 131      14.257 -29.652 -15.200  1.00 94.25      A    N1+
ANISOU 1012  NH1 ARG A 131    12169  11170  12472   2830   2045   -867  A    N1+
ATOM   1013  NH2 ARG A 131      14.267 -31.937 -14.987  1.00 95.54      A    N  
ANISOU 1013  NH2 ARG A 131    12326  11622  12353   2316   2547   -384  A    N  
ATOM   1014  N   ILE A 132      18.855 -29.704 -18.287  1.00 36.95      A    N  
ANISOU 1014  N   ILE A 132     5495   3615   4931   1989   -231   -101  A    N  
ATOM   1015  CA  ILE A 132      19.725 -30.180 -17.218  1.00 37.86      A    C  
ANISOU 1015  CA  ILE A 132     6125   3705   4554   1987   -128   -112  A    C  
ATOM   1016  C   ILE A 132      18.915 -30.267 -15.936  1.00 43.86      A    C  
ANISOU 1016  C   ILE A 132     7081   4488   5095   2210    428   -288  A    C  
ATOM   1017  O   ILE A 132      18.393 -29.251 -15.463  1.00 42.54      A    O  
ANISOU 1017  O   ILE A 132     6964   4220   4981   2505    503   -536  A    O  
ATOM   1018  CB  ILE A 132      20.951 -29.271 -17.039  1.00 45.34      A    C  
ANISOU 1018  CB  ILE A 132     7462   4444   5322   2034   -635   -146  A    C  
ATOM   1019  CG1 ILE A 132      21.715 -29.176 -18.362  1.00 52.67      A    C  
ANISOU 1019  CG1 ILE A 132     8100   5462   6451   1715  -1077     48  A    C  
ATOM   1020  CG2 ILE A 132      21.855 -29.808 -15.942  1.00 46.51      A    C  
ANISOU 1020  CG2 ILE A 132     8154   4523   4995   2030   -602   -160  A    C  
ATOM   1021  CD1 ILE A 132      23.094 -28.581 -18.240  1.00 60.99      A    C  
ANISOU 1021  CD1 ILE A 132     9301   6518   7355   1460  -1381     24  A    C  
ATOM   1022  N   ASP A 133      18.772 -31.470 -15.382  1.00 42.20      A    N  
ANISOU 1022  N   ASP A 133     6969   4418   4648   2067    821   -169  A    N  
ATOM   1023  CA  ASP A 133      17.893 -31.618 -14.223  1.00 49.58      A    C  
ANISOU 1023  CA  ASP A 133     8043   5451   5346   2220   1441   -287  A    C  
ATOM   1024  C   ASP A 133      18.625 -31.283 -12.919  1.00 53.32      A    C  
ANISOU 1024  C   ASP A 133     9243   5816   5202   2376   1438   -420  A    C  
ATOM   1025  O   ASP A 133      19.798 -30.903 -12.936  1.00 45.03      A    O  
ANISOU 1025  O   ASP A 133     8545   4570   3995   2375    910   -423  A    O  
ATOM   1026  CB  ASP A 133      17.256 -33.028 -14.174  1.00 52.17      A    C  
ANISOU 1026  CB  ASP A 133     8136   5970   5716   1961   1884    -48  A    C  
ATOM   1027  CG  ASP A 133      18.230 -34.151 -13.777  1.00 49.53      A    C  
ANISOU 1027  CG  ASP A 133     8220   5599   5000   1703   1741    185  A    C  
ATOM   1028  OD1 ASP A 133      19.374 -33.898 -13.346  1.00 47.66      A    O  
ANISOU 1028  OD1 ASP A 133     8496   5204   4407   1738   1379    147  A    O  
ATOM   1029  OD2 ASP A 133      17.812 -35.329 -13.876  1.00 46.31      A    O1-
ANISOU 1029  OD2 ASP A 133     7608   5286   4702   1459   1963    411  A    O1-
ATOM   1030  N   GLU A 134      17.933 -31.430 -11.792  1.00 55.71      A    N  
ANISOU 1030  N   GLU A 134     9765   6254   5147   2498   2026   -527  A    N  
ATOM   1031  CA  GLU A 134      18.484 -31.019 -10.505  1.00 63.72      A    C  
ANISOU 1031  CA  GLU A 134    11514   7180   5517   2688   2045   -705  A    C  
ATOM   1032  C   GLU A 134      19.687 -31.862 -10.082  1.00 63.10      A    C  
ANISOU 1032  C   GLU A 134    11975   6978   5024   2435   1714   -453  A    C  
ATOM   1033  O   GLU A 134      20.399 -31.508  -9.145  1.00 63.43      A    O  
ANISOU 1033  O   GLU A 134    12480   6873   4748   2464   1434   -499  A    O  
ATOM   1034  CB  GLU A 134      17.405 -31.081  -9.422  1.00 74.32      A    C  
ANISOU 1034  CB  GLU A 134    12824   8790   6625   2733   2719   -813  A    C  
ATOM   1035  CG  GLU A 134      16.850 -32.473  -9.178  1.00 82.02      A    C  
ANISOU 1035  CG  GLU A 134    13696   9999   7467   2415   3256   -487  A    C  
ATOM   1036  CD  GLU A 134      15.792 -32.495  -8.091  1.00 99.43      A    C  
ANISOU 1036  CD  GLU A 134    15824  12508   9448   2412   3898   -590  A    C  
ATOM   1037  OE1 GLU A 134      16.105 -32.104  -6.944  1.00103.57      A    O  
ANISOU 1037  OE1 GLU A 134    16836  13048   9470   2489   3874   -738  A    O  
ATOM   1038  OE2 GLU A 134      14.649 -32.905  -8.384  1.00107.61      A    O1-
ANISOU 1038  OE2 GLU A 134    16280  13774  10831   2323   4406   -526  A    O1-
ATOM   1039  N   HIS A 135      19.909 -32.973 -10.777  1.00 57.48      A    N  
ANISOU 1039  N   HIS A 135    11005   6302   4534   2108   1612   -144  A    N  
ATOM   1040  CA  HIS A 135      21.032 -33.864 -10.484  1.00 58.29      A    C  
ANISOU 1040  CA  HIS A 135    11538   6251   4358   1875   1248     72  A    C  
ATOM   1041  C   HIS A 135      22.193 -33.687 -11.459  1.00 55.85      A    C  
ANISOU 1041  C   HIS A 135    11082   5755   4382   1801    552     91  A    C  
ATOM   1042  O   HIS A 135      23.223 -34.345 -11.333  1.00 58.90      A    O  
ANISOU 1042  O   HIS A 135    11653   5982   4745   1616    171    196  A    O  
ATOM   1043  CB  HIS A 135      20.577 -35.322 -10.505  1.00 56.53      A    C  
ANISOU 1043  CB  HIS A 135    11143   6162   4175   1550   1549    390  A    C  
ATOM   1044  CG  HIS A 135      19.456 -35.615  -9.560  1.00 68.76      A    C  
ANISOU 1044  CG  HIS A 135    12780   7934   5412   1534   2273    448  A    C  
ATOM   1045  CD2 HIS A 135      19.431 -35.692  -8.210  1.00 65.34      A    C  
ANISOU 1045  CD2 HIS A 135    12739   7523   4566   1486   2422    441  A    C  
ATOM   1046  ND1 HIS A 135      18.164 -35.846  -9.983  1.00 70.55      A    N  
ANISOU 1046  ND1 HIS A 135    12398   8403   6006   1485   2812    503  A    N  
ATOM   1047  CE1 HIS A 135      17.395 -36.067  -8.933  1.00 66.53      A    C  
ANISOU 1047  CE1 HIS A 135    12019   8090   5169   1434   3378    547  A    C  
ATOM   1048  NE2 HIS A 135      18.137 -35.977  -7.845  1.00 73.03      A    N  
ANISOU 1048  NE2 HIS A 135    13435   8803   5512   1420   3123    507  A    N  
ATOM   1049  N   GLY A 136      22.023 -32.798 -12.429  1.00 44.92      A    N  
ANISOU 1049  N   GLY A 136     9256   4390   3423   1907    382    -27  A    N  
ATOM   1050  CA  GLY A 136      23.083 -32.518 -13.376  1.00 44.99      A    C  
ANISOU 1050  CA  GLY A 136     9102   4283   3710   1813   -211      7  A    C  
ATOM   1051  C   GLY A 136      23.008 -33.388 -14.617  1.00 42.33      A    C  
ANISOU 1051  C   GLY A 136     8204   4114   3766   1558   -255    174  A    C  
ATOM   1052  O   GLY A 136      23.791 -33.214 -15.550  1.00 37.50      A    O  
ANISOU 1052  O   GLY A 136     7352   3509   3389   1440   -654    190  A    O  
ATOM   1053  N   THR A 137      22.075 -34.334 -14.633  1.00 39.36      A    N  
ANISOU 1053  N   THR A 137     7593   3896   3465   1448    161    284  A    N  
ATOM   1054  CA  THR A 137      21.901 -35.163 -15.818  1.00 34.15      A    C  
ANISOU 1054  CA  THR A 137     6407   3375   3193   1238     92    401  A    C  
ATOM   1055  C   THR A 137      21.424 -34.300 -16.980  1.00 33.42      A    C  
ANISOU 1055  C   THR A 137     5837   3383   3480   1295     -8    338  A    C  
ATOM   1056  O   THR A 137      20.530 -33.465 -16.826  1.00 32.15      A    O  
ANISOU 1056  O   THR A 137     5572   3228   3417   1475    213    244  A    O  
ATOM   1057  CB  THR A 137      20.891 -36.302 -15.599  1.00 38.38      A    C  
ANISOU 1057  CB  THR A 137     6758   4014   3809   1104    520    550  A    C  
ATOM   1058  CG2 THR A 137      20.836 -37.199 -16.841  1.00 33.12      A    C  
ANISOU 1058  CG2 THR A 137     5594   3439   3552    907    332    629  A    C  
ATOM   1059  OG1 THR A 137      21.277 -37.083 -14.466  1.00 42.31      A    O  
ANISOU 1059  OG1 THR A 137     7753   4402   3921   1015    595    664  A    O  
ATOM   1060  N   LYS A 138      22.023 -34.495 -18.150  1.00 30.14      A    N  
ANISOU 1060  N   LYS A 138     5136   3046   3271   1141   -358    378  A    N  
ATOM   1061  CA  LYS A 138      21.580 -33.789 -19.338  1.00 28.02      A    C  
ANISOU 1061  CA  LYS A 138     4450   2881   3316   1134   -498    374  A    C  
ATOM   1062  C   LYS A 138      20.469 -34.608 -19.983  1.00 32.56      A    C  
ANISOU 1062  C   LYS A 138     4580   3591   4202   1045   -272    433  A    C  
ATOM   1063  O   LYS A 138      20.732 -35.465 -20.824  1.00 30.82      A    O  
ANISOU 1063  O   LYS A 138     4132   3485   4091    873   -428    474  A    O  
ATOM   1064  CB  LYS A 138      22.746 -33.569 -20.310  1.00 28.96      A    C  
ANISOU 1064  CB  LYS A 138     4489   3074   3442    984   -946    403  A    C  
ATOM   1065  CG  LYS A 138      23.954 -32.868 -19.691  1.00 30.26      A    C  
ANISOU 1065  CG  LYS A 138     4933   3146   3419    922  -1099    312  A    C  
ATOM   1066  CD  LYS A 138      25.116 -32.826 -20.686  1.00 31.35      A    C  
ANISOU 1066  CD  LYS A 138     4791   3464   3656    631  -1223    286  A    C  
ATOM   1067  CE  LYS A 138      26.385 -32.350 -20.010  1.00 31.52      A    C  
ANISOU 1067  CE  LYS A 138     5013   3350   3615    565  -1309    180  A    C  
ATOM   1068  NZ  LYS A 138      26.917 -33.361 -19.028  1.00 29.32      A    N1+
ANISOU 1068  NZ  LYS A 138     4985   2944   3213    589  -1300     91  A    N1+
ATOM   1069  N   GLN A 139      19.234 -34.367 -19.557  1.00 30.92      A    N  
ANISOU 1069  N   GLN A 139     4234   3361   4153   1175     90    408  A    N  
ATOM   1070  CA  GLN A 139      18.095 -35.152 -20.008  1.00 34.49      A    C  
ANISOU 1070  CA  GLN A 139     4249   3895   4962   1092    321    475  A    C  
ATOM   1071  C   GLN A 139      17.752 -34.770 -21.427  1.00 42.49      A    C  
ANISOU 1071  C   GLN A 139     4848   4966   6329   1042      6    477  A    C  
ATOM   1072  O   GLN A 139      17.655 -33.585 -21.726  1.00 38.15      A    O  
ANISOU 1072  O   GLN A 139     4274   4358   5863   1157   -176    421  A    O  
ATOM   1073  CB  GLN A 139      16.863 -34.916 -19.126  1.00 44.50      A    C  
ANISOU 1073  CB  GLN A 139     5425   5141   6343   1248    836    431  A    C  
ATOM   1074  CG  GLN A 139      17.002 -35.304 -17.674  1.00 55.62      A    C  
ANISOU 1074  CG  GLN A 139     7264   6536   7332   1277   1229    453  A    C  
ATOM   1075  CD  GLN A 139      17.023 -36.802 -17.467  1.00 64.91      A    C  
ANISOU 1075  CD  GLN A 139     8448   7742   8474   1025   1352    661  A    C  
ATOM   1076  NE2 GLN A 139      17.161 -37.223 -16.214  1.00 68.25      A    N  
ANISOU 1076  NE2 GLN A 139     9293   8146   8491    992   1655    744  A    N  
ATOM   1077  OE1 GLN A 139      16.908 -37.576 -18.420  1.00 65.42      A    O  
ANISOU 1077  OE1 GLN A 139     8164   7828   8867    858   1142    746  A    O  
ATOM   1078  N   VAL A 140      17.560 -35.753 -22.299  1.00 39.96      A    N  
ANISOU 1078  N   VAL A 140     6500   5190   3493  -1376   -402   2010  A    N  
ATOM   1079  CA  VAL A 140      17.031 -35.453 -23.624  1.00 38.30      A    C  
ANISOU 1079  CA  VAL A 140     5611   5214   3725   -944   -514   1842  A    C  
ATOM   1080  C   VAL A 140      15.518 -35.376 -23.505  1.00 42.29      A    C  
ANISOU 1080  C   VAL A 140     5729   5811   4528   -663     83   1650  A    C  
ATOM   1081  O   VAL A 140      14.874 -36.312 -23.042  1.00 44.63      A    O  
ANISOU 1081  O   VAL A 140     5731   6123   5101   -853    375   1644  A    O  
ATOM   1082  CB  VAL A 140      17.439 -36.501 -24.668  1.00 36.97      A    C  
ANISOU 1082  CB  VAL A 140     4773   5303   3973   -946  -1055   1855  A    C  
ATOM   1083  CG1 VAL A 140      16.717 -36.241 -25.993  1.00 33.96      A    C  
ANISOU 1083  CG1 VAL A 140     3644   5243   4017   -391  -1134   1624  A    C  
ATOM   1084  CG2 VAL A 140      18.950 -36.470 -24.845  1.00 38.87      A    C  
ANISOU 1084  CG2 VAL A 140     5264   5422   4082  -1063  -1409   1760  A    C  
ATOM   1085  N   ALA A 141      14.954 -34.242 -23.893  1.00 43.69      A    N  
ANISOU 1085  N   ALA A 141     5920   6034   4646   -202    308   1505  A    N  
ATOM   1086  CA  ALA A 141      13.524 -34.049 -23.746  1.00 48.03      A    C  
ANISOU 1086  CA  ALA A 141     6112   6728   5412    126    886   1308  A    C  
ATOM   1087  C   ALA A 141      12.798 -34.498 -24.996  1.00 47.59      A    C  
ANISOU 1087  C   ALA A 141     5033   7111   5939    523    715   1056  A    C  
ATOM   1088  O   ALA A 141      13.034 -33.981 -26.079  1.00 51.14      A    O  
ANISOU 1088  O   ALA A 141     5270   7751   6408    964    382    992  A    O  
ATOM   1089  CB  ALA A 141      13.210 -32.595 -23.443  1.00 50.71      A    C  
ANISOU 1089  CB  ALA A 141     7029   6901   5339    497   1261   1262  A    C  
ATOM   1090  N   VAL A 142      11.920 -35.475 -24.844  1.00 50.29      A    N  
ANISOU 1090  N   VAL A 142     4728   7615   6763    379    954    901  A    N  
ATOM   1091  CA  VAL A 142      11.032 -35.847 -25.925  1.00 59.45      A    C  
ANISOU 1091  CA  VAL A 142     4848   9240   8501    777    845    536  A    C  
ATOM   1092  C   VAL A 142       9.652 -35.293 -25.593  1.00 74.13      A    C  
ANISOU 1092  C   VAL A 142     6436  11290  10439   1132   1491    318  A    C  
ATOM   1093  O   VAL A 142       8.739 -35.307 -26.420  1.00 83.94      A    O  
ANISOU 1093  O   VAL A 142     6827  12998  12069   1603   1485    -50  A    O  
ATOM   1094  CB  VAL A 142      10.993 -37.377 -26.125  1.00 67.74      A    C  
ANISOU 1094  CB  VAL A 142     5228  10346  10163    350    623    422  A    C  
ATOM   1095  CG1 VAL A 142      10.234 -38.042 -24.982  1.00 81.12      A    C  
ANISOU 1095  CG1 VAL A 142     6889  11829  12105   -108   1279    468  A    C  
ATOM   1096  CG2 VAL A 142      10.346 -37.710 -27.455  1.00 75.98      A    C  
ANISOU 1096  CG2 VAL A 142     5340  11769  11760    773    283    -34  A    C  
ATOM   1097  N   SER A 143       9.518 -34.788 -24.368  1.00 74.17      A    N  
ANISOU 1097  N   SER A 143     7171  10977  10033    953   2034    526  A    N  
ATOM   1098  CA  SER A 143       8.242 -34.276 -23.881  1.00 79.73      A    C  
ANISOU 1098  CA  SER A 143     7706  11842  10745   1271   2714    372  A    C  
ATOM   1099  C   SER A 143       8.406 -33.040 -22.981  1.00 73.84      A    C  
ANISOU 1099  C   SER A 143     8007  10771   9277   1437   3094    573  A    C  
ATOM   1100  O   SER A 143       7.725 -32.903 -21.960  1.00 75.71      A    O  
ANISOU 1100  O   SER A 143     8483  10925   9357   1392   3719    623  A    O  
ATOM   1101  CB  SER A 143       7.501 -35.381 -23.133  1.00 85.55      A    C  
ANISOU 1101  CB  SER A 143     7987  12568  11951    800   3189    356  A    C  
ATOM   1102  OG  SER A 143       7.169 -36.471 -23.984  1.00 84.21      A    O  
ANISOU 1102  OG  SER A 143     6773  12680  12542    667   2898     65  A    O  
ATOM   1103  N   GLY A 144       9.318 -32.151 -23.366  1.00 65.75      A    N  
ANISOU 1103  N   GLY A 144     7602   9548   7833   1625   2730    677  A    N  
ATOM   1104  CA  GLY A 144       9.538 -30.910 -22.648  1.00 65.19      A    C  
ANISOU 1104  CA  GLY A 144     8522   9116   7132   1789   3022    788  A    C  
ATOM   1105  C   GLY A 144       9.944 -31.060 -21.189  1.00 72.81      A    C  
ANISOU 1105  C   GLY A 144    10289   9691   7684   1269   3285    988  A    C  
ATOM   1106  O   GLY A 144      10.898 -31.769 -20.858  1.00 63.88      A    O  
ANISOU 1106  O   GLY A 144     9398   8377   6497    723   2944   1162  A    O  
ATOM   1107  N   TRP A 145       9.208 -30.383 -20.314  1.00 71.86      A    N  
ANISOU 1107  N   TRP A 145    10594   9485   7225   1514   3895    955  A    N  
ATOM   1108  CA  TRP A 145       9.537 -30.339 -18.891  1.00 77.40      A    C  
ANISOU 1108  CA  TRP A 145    12152   9851   7406   1181   4180   1113  A    C  
ATOM   1109  C   TRP A 145       8.731 -31.329 -18.044  1.00 81.37      A    C  
ANISOU 1109  C   TRP A 145    12321  10505   8092    972   4720   1224  A    C  
ATOM   1110  O   TRP A 145       8.985 -31.461 -16.844  1.00 84.39      A    O  
ANISOU 1110  O   TRP A 145    13374  10664   8026    741   4982   1399  A    O  
ATOM   1111  CB  TRP A 145       9.320 -28.917 -18.347  1.00 78.20      A    C  
ANISOU 1111  CB  TRP A 145    13079   9702   6930   1607   4532   1013  A    C  
ATOM   1112  CG  TRP A 145      10.374 -27.917 -18.755  1.00 81.82      A    C  
ANISOU 1112  CG  TRP A 145    14196   9791   7103   1626   4089    965  A    C  
ATOM   1113  CD1 TRP A 145      11.491 -27.576 -18.053  1.00 76.18      A    C  
ANISOU 1113  CD1 TRP A 145    14351   8663   5930   1234   3825    990  A    C  
ATOM   1114  CD2 TRP A 145      10.402 -27.129 -19.958  1.00 73.79      A    C  
ANISOU 1114  CD2 TRP A 145    12996   8782   6259   2070   3896    879  A    C  
ATOM   1115  CE2 TRP A 145      11.567 -26.339 -19.911  1.00 72.65      A    C  
ANISOU 1115  CE2 TRP A 145    13646   8153   5806   1855   3572    892  A    C  
ATOM   1116  CE3 TRP A 145       9.554 -27.016 -21.067  1.00 79.18      A    C  
ANISOU 1116  CE3 TRP A 145    12912   9858   7316   2664   3976    785  A    C  
ATOM   1117  NE1 TRP A 145      12.215 -26.633 -18.740  1.00 73.24      A    N  
ANISOU 1117  NE1 TRP A 145    14316   7999   5513   1321   3502    917  A    N  
ATOM   1118  CZ2 TRP A 145      11.909 -25.446 -20.930  1.00 73.66      A    C  
ANISOU 1118  CZ2 TRP A 145    13863   8107   6019   2191   3404    883  A    C  
ATOM   1119  CZ3 TRP A 145       9.898 -26.125 -22.085  1.00 74.82      A    C  
ANISOU 1119  CZ3 TRP A 145    12479   9189   6760   3091   3772    777  A    C  
ATOM   1120  CH2 TRP A 145      11.064 -25.355 -22.005  1.00 72.27      A    C  
ANISOU 1120  CH2 TRP A 145    12994   8310   6155   2840   3527    860  A    C  
ATOM   1121  N   GLN A 146       7.760 -32.013 -18.648  1.00 90.08      A    N  
ANISOU 1121  N   GLN A 146    12390  11987   9849   1070   4911   1111  A    N  
ATOM   1122  CA  GLN A 146       6.826 -32.833 -17.867  1.00105.72      A    C  
ANISOU 1122  CA  GLN A 146    13989  14088  12092    900   5573   1207  A    C  
ATOM   1123  C   GLN A 146       7.425 -34.177 -17.456  1.00109.91      A    C  
ANISOU 1123  C   GLN A 146    14484  14433  12843    254   5460   1469  A    C  
ATOM   1124  O   GLN A 146       7.510 -34.481 -16.266  1.00118.27      A    O  
ANISOU 1124  O   GLN A 146    16114  15279  13544     49   5883   1746  A    O  
ATOM   1125  CB  GLN A 146       5.513 -33.067 -18.637  1.00110.30      A    C  
ANISOU 1125  CB  GLN A 146    13394  15156  13360   1208   5850    922  A    C  
ATOM   1126  CG  GLN A 146       4.923 -34.480 -18.473  1.00113.38      A    C  
ANISOU 1126  CG  GLN A 146    12950  15655  14474    739   6172    963  A    C  
ATOM   1127  CD  GLN A 146       3.536 -34.633 -19.053  1.00117.77      A    C  
ANISOU 1127  CD  GLN A 146    12343  16719  15685   1014   6474    602  A    C  
ATOM   1128  NE2 GLN A 146       3.156 -35.872 -19.360  1.00119.45      A    N  
ANISOU 1128  NE2 GLN A 146    11695  17030  16660    560   6366    474  A    N  
ATOM   1129  OE1 GLN A 146       2.815 -33.654 -19.235  1.00120.41      A    O  
ANISOU 1129  OE1 GLN A 146    12633  17340  15779   1577   6522    368  A    O  
ATOM   1130  N   GLU A 147       7.843 -34.981 -18.430  1.00100.05      A    N  
ANISOU 1130  N   GLU A 147    12605  13267  12141     -3   4906   1392  A    N  
ATOM   1131  CA  GLU A 147       8.299 -36.323 -18.121  1.00 96.13      A    C  
ANISOU 1131  CA  GLU A 147    12008  12586  11931   -565   4846   1627  A    C  
ATOM   1132  C   GLU A 147       9.767 -36.463 -18.463  1.00 86.93      A    C  
ANISOU 1132  C   GLU A 147    11304  11238  10487   -798   4055   1739  A    C  
ATOM   1133  O   GLU A 147      10.279 -35.840 -19.402  1.00 67.94      A    O  
ANISOU 1133  O   GLU A 147     8844   8937   8032   -586   3476   1565  A    O  
ATOM   1134  CB  GLU A 147       7.490 -37.383 -18.876  1.00100.53      A    C  
ANISOU 1134  CB  GLU A 147    11375  13365  13457   -737   4928   1422  A    C  
ATOM   1135  CG  GLU A 147       7.671 -37.318 -20.380  1.00102.14      A    C  
ANISOU 1135  CG  GLU A 147    10881  13864  14065   -532   4204   1064  A    C  
ATOM   1136  CD  GLU A 147       6.876 -38.370 -21.126  1.00113.76      A    C  
ANISOU 1136  CD  GLU A 147    11150  15575  16499   -694   4220    752  A    C  
ATOM   1137  OE1 GLU A 147       7.103 -39.576 -20.886  1.00114.96      A    O  
ANISOU 1137  OE1 GLU A 147    11153  15470  17058  -1218   4264    898  A    O  
ATOM   1138  OE2 GLU A 147       6.022 -37.990 -21.957  1.00122.69      A    O1-
ANISOU 1138  OE2 GLU A 147    11483  17154  17982   -273   4187    334  A    O1-
ATOM   1139  N   ASN A 148      10.435 -37.287 -17.672  1.00 88.49      A    N  
ANISOU 1139  N   ASN A 148    11963  11178  10481  -1194   4077   2060  A    N  
ATOM   1140  CA  ASN A 148      11.818 -37.631 -17.907  1.00 83.14      A    C  
ANISOU 1140  CA  ASN A 148    11651  10374   9565  -1444   3361   2189  A    C  
ATOM   1141  C   ASN A 148      11.882 -38.743 -18.951  1.00 78.42      A    C  
ANISOU 1141  C   ASN A 148    10204   9868   9723  -1658   2973   2103  A    C  
ATOM   1142  O   ASN A 148      11.257 -39.788 -18.794  1.00 79.66      A    O  
ANISOU 1142  O   ASN A 148     9885   9956  10427  -1892   3362   2164  A    O  
ATOM   1143  CB  ASN A 148      12.470 -38.048 -16.588  1.00 87.22      A    C  
ANISOU 1143  CB  ASN A 148    13028  10639   9473  -1671   3558   2553  A    C  
ATOM   1144  CG  ASN A 148      13.899 -38.502 -16.754  1.00 88.61      A    C  
ANISOU 1144  CG  ASN A 148    13426  10792   9449  -1845   2723   2629  A    C  
ATOM   1145  ND2 ASN A 148      14.479 -39.019 -15.675  1.00 95.62      A    N  
ANISOU 1145  ND2 ASN A 148    14662  11646  10026  -1822   2612   2784  A    N  
ATOM   1146  OD1 ASN A 148      14.481 -38.390 -17.833  1.00 78.21      A    O  
ANISOU 1146  OD1 ASN A 148    11891   9544   8282  -1919   2179   2529  A    O  
ATOM   1147  N   SER A 149      12.628 -38.509 -20.024  1.00 64.96      A    N  
ANISOU 1147  N   SER A 149     7636   9175   7870   1629   2087   1525  A    N  
ATOM   1148  CA  SER A 149      12.734 -39.486 -21.103  1.00 69.76      A    C  
ANISOU 1148  CA  SER A 149     8032   9631   8842   1148   1864   1563  A    C  
ATOM   1149  C   SER A 149      13.501 -40.737 -20.688  1.00 68.27      A    C  
ANISOU 1149  C   SER A 149     8060   9220   8660    863   1843   1671  A    C  
ATOM   1150  O   SER A 149      13.406 -41.777 -21.344  1.00 67.73      A    O  
ANISOU 1150  O   SER A 149     7837   9027   8869    470   1732   1765  A    O  
ATOM   1151  CB  SER A 149      13.418 -38.864 -22.313  1.00 74.17      A    C  
ANISOU 1151  CB  SER A 149     8721   9962   9498   1107   1493   1272  A    C  
ATOM   1152  OG  SER A 149      14.630 -38.239 -21.927  1.00 76.87      A    O  
ANISOU 1152  OG  SER A 149     9532  10086   9591   1281   1362   1057  A    O  
ATOM   1153  N   GLY A 150      14.276 -40.626 -19.612  1.00 61.33      A    N  
ANISOU 1153  N   GLY A 150     7577   8269   7456   1085   1918   1642  A    N  
ATOM   1154  CA  GLY A 150      15.159 -41.701 -19.200  1.00 60.86      A    C  
ANISOU 1154  CA  GLY A 150     7788   7984   7352    907   1856   1719  A    C  
ATOM   1155  C   GLY A 150      16.321 -41.885 -20.162  1.00 54.40      A    C  
ANISOU 1155  C   GLY A 150     7136   6867   6666    741   1474   1480  A    C  
ATOM   1156  O   GLY A 150      16.918 -42.958 -20.230  1.00 57.79      A    O  
ANISOU 1156  O   GLY A 150     7698   7092   7168    547   1380   1545  A    O  
ATOM   1157  N   VAL A 151      16.634 -40.838 -20.923  1.00 38.81      A    N  
ANISOU 1157  N   VAL A 151     5165   4870   4712    838   1271   1220  A    N  
ATOM   1158  CA  VAL A 151      17.755 -40.871 -21.845  1.00 33.99      A    C  
ANISOU 1158  CA  VAL A 151     4683   4038   4195    712    954   1008  A    C  
ATOM   1159  C   VAL A 151      18.616 -39.610 -21.711  1.00 38.10      A    C  
ANISOU 1159  C   VAL A 151     5442   4524   4512    928    802    765  A    C  
ATOM   1160  O   VAL A 151      18.093 -38.494 -21.739  1.00 32.24      A    O  
ANISOU 1160  O   VAL A 151     4684   3866   3701   1108    842    684  A    O  
ATOM   1161  CB  VAL A 151      17.269 -41.004 -23.304  1.00 41.87      A    C  
ANISOU 1161  CB  VAL A 151     5414   5001   5494    483    814    960  A    C  
ATOM   1162  CG1 VAL A 151      18.434 -41.182 -24.221  1.00 36.32      A    C  
ANISOU 1162  CG1 VAL A 151     4854   4099   4848    378    546    777  A    C  
ATOM   1163  CG2 VAL A 151      16.298 -42.179 -23.454  1.00 45.24      A    C  
ANISOU 1163  CG2 VAL A 151     5591   5450   6146    208    921   1190  A    C  
ATOM   1164  N   SER A 152      19.932 -39.778 -21.569  1.00 29.63      A    N  
ANISOU 1164  N   SER A 152     4588   3322   3347    911    613    653  A    N  
ATOM   1165  CA  SER A 152      20.824 -38.618 -21.442  1.00 31.10      A    C  
ANISOU 1165  CA  SER A 152     4982   3463   3372   1027    429    433  A    C  
ATOM   1166  C   SER A 152      21.435 -38.251 -22.781  1.00 27.98      A    C  
ANISOU 1166  C   SER A 152     4499   2971   3162    851    218    291  A    C  
ATOM   1167  O   SER A 152      21.453 -39.075 -23.708  1.00 24.13      A    O  
ANISOU 1167  O   SER A 152     3849   2445   2875    679    184    337  A    O  
ATOM   1168  CB  SER A 152      21.935 -38.894 -20.415  1.00 29.26      A    C  
ANISOU 1168  CB  SER A 152     4995   3211   2910   1114    323    400  A    C  
ATOM   1169  OG  SER A 152      22.844 -39.869 -20.909  1.00 24.89      A    O  
ANISOU 1169  OG  SER A 152     4381   2592   2484    966    186    418  A    O  
ATOM   1170  N   LEU A 153      21.914 -37.010 -22.892  1.00 23.54      A    N  
ANISOU 1170  N   LEU A 153     4079   2351   2514    893     79    126  A    N  
ATOM   1171  CA  LEU A 153      22.659 -36.577 -24.071  1.00 25.92      A    C  
ANISOU 1171  CA  LEU A 153     4329   2570   2948    716   -101     22  A    C  
ATOM   1172  C   LEU A 153      23.769 -37.575 -24.409  1.00 26.12      A    C  
ANISOU 1172  C   LEU A 153     4264   2611   3049    578   -203     34  A    C  
ATOM   1173  O   LEU A 153      23.929 -37.985 -25.566  1.00 24.53      A    O  
ANISOU 1173  O   LEU A 153     3919   2397   3005    454   -234     40  A    O  
ATOM   1174  CB  LEU A 153      23.245 -35.167 -23.852  1.00 25.16      A    C  
ANISOU 1174  CB  LEU A 153     4466   2371   2724    732   -255   -133  A    C  
ATOM   1175  CG  LEU A 153      24.109 -34.627 -25.008  1.00 26.98      A    C  
ANISOU 1175  CG  LEU A 153     4651   2523   3078    508   -417   -198  A    C  
ATOM   1176  CD1 LEU A 153      23.982 -33.128 -25.110  1.00 30.56      A    C  
ANISOU 1176  CD1 LEU A 153     5346   2804   3463    521   -501   -294  A    C  
ATOM   1177  CD2 LEU A 153      25.592 -35.016 -24.817  1.00 25.99      A    C  
ANISOU 1177  CD2 LEU A 153     4471   2460   2943    356   -575   -233  A    C  
ATOM   1178  N   GLU A 154      24.544 -37.963 -23.399  1.00 22.19      A    N  
ANISOU 1178  N   GLU A 154     3870   2153   2408    645   -263     33  A    N  
ATOM   1179  CA  GLU A 154      25.697 -38.813 -23.653  1.00 20.48      A    C  
ANISOU 1179  CA  GLU A 154     3565   1979   2236    589   -375     37  A    C  
ATOM   1180  C   GLU A 154      25.273 -40.211 -24.101  1.00 24.94      A    C  
ANISOU 1180  C   GLU A 154     4046   2503   2926    587   -264    160  A    C  
ATOM   1181  O   GLU A 154      25.898 -40.792 -24.978  1.00 25.93      A    O  
ANISOU 1181  O   GLU A 154     4076   2623   3153    538   -324    139  A    O  
ATOM   1182  CB  GLU A 154      26.585 -38.888 -22.409  1.00 21.17      A    C  
ANISOU 1182  CB  GLU A 154     3784   2139   2120    701   -501     12  A    C  
ATOM   1183  CG  GLU A 154      27.303 -37.562 -22.074  1.00 26.96      A    C  
ANISOU 1183  CG  GLU A 154     4610   2885   2749    630   -706   -145  A    C  
ATOM   1184  CD  GLU A 154      26.522 -36.642 -21.108  1.00 33.67      A    C  
ANISOU 1184  CD  GLU A 154     5741   3657   3395    760   -670   -208  A    C  
ATOM   1185  OE1 GLU A 154      25.280 -36.763 -20.985  1.00 27.55      A    O  
ANISOU 1185  OE1 GLU A 154     5009   2855   2605    888   -440   -123  A    O  
ATOM   1186  OE2 GLU A 154      27.166 -35.784 -20.468  1.00 28.84      A    O1-
ANISOU 1186  OE2 GLU A 154     5308   3021   2629    740   -881   -348  A    O1-
ATOM   1187  N   GLN A 155      24.212 -40.747 -23.501  1.00 24.12      A    N  
ANISOU 1187  N   GLN A 155     3992   2366   2808    636    -98    292  A    N  
ATOM   1188  CA  GLN A 155      23.671 -42.033 -23.934  1.00 22.73      A    C  
ANISOU 1188  CA  GLN A 155     3767   2093   2778    560    -13    416  A    C  
ATOM   1189  C   GLN A 155      23.354 -42.005 -25.423  1.00 24.94      A    C  
ANISOU 1189  C   GLN A 155     3899   2323   3253    411    -63    345  A    C  
ATOM   1190  O   GLN A 155      23.706 -42.931 -26.173  1.00 24.01      A    O  
ANISOU 1190  O   GLN A 155     3790   2108   3224    365   -125    332  A    O  
ATOM   1191  CB  GLN A 155      22.415 -42.385 -23.139  1.00 23.89      A    C  
ANISOU 1191  CB  GLN A 155     3924   2243   2909    561    198    599  A    C  
ATOM   1192  CG  GLN A 155      21.833 -43.764 -23.474  1.00 25.45      A    C  
ANISOU 1192  CG  GLN A 155     4099   2294   3276    405    264    755  A    C  
ATOM   1193  CD  GLN A 155      20.564 -44.046 -22.700  1.00 35.58      A    C  
ANISOU 1193  CD  GLN A 155     5322   3628   4568    347    502    980  A    C  
ATOM   1194  NE2 GLN A 155      19.779 -44.995 -23.184  1.00 40.95      A    N  
ANISOU 1194  NE2 GLN A 155     5909   4190   5461    109    544   1112  A    N  
ATOM   1195  OE1 GLN A 155      20.279 -43.400 -21.694  1.00 32.68      A    O  
ANISOU 1195  OE1 GLN A 155     4991   3414   4013    509    647   1036  A    O  
ATOM   1196  N   LEU A 156      22.715 -40.934 -25.876  1.00 21.45      A    N  
ANISOU 1196  N   LEU A 156     3366   1939   2847    375    -49    290  A    N  
ATOM   1197  CA ALEU A 156      22.310 -40.885 -27.280  0.47 23.95      A    C  
ANISOU 1197  CA ALEU A 156     3565   2224   3312    259   -110    236  A    C  
ATOM   1198  CA BLEU A 156      22.314 -40.846 -27.282  0.53 24.24      A    C  
ANISOU 1198  CA BLEU A 156     3601   2263   3347    261   -111    234  A    C  
ATOM   1199  C   LEU A 156      23.500 -40.649 -28.207  1.00 22.77      A    C  
ANISOU 1199  C   LEU A 156     3432   2076   3142    248   -235    116  A    C  
ATOM   1200  O   LEU A 156      23.573 -41.263 -29.282  1.00 22.26      A    O  
ANISOU 1200  O   LEU A 156     3347   1962   3150    197   -288     79  A    O  
ATOM   1201  CB ALEU A 156      21.241 -39.814 -27.513  0.47 24.70      A    C  
ANISOU 1201  CB ALEU A 156     3563   2388   3433    275    -66    234  A    C  
ATOM   1202  CB BLEU A 156      21.305 -39.716 -27.487  0.53 24.53      A    C  
ANISOU 1202  CB BLEU A 156     3552   2369   3401    284    -70    226  A    C  
ATOM   1203  CG ALEU A 156      20.329 -40.130 -28.706  0.47 25.18      A    C  
ANISOU 1203  CG ALEU A 156     3469   2442   3656    159   -119    241  A    C  
ATOM   1204  CG BLEU A 156      19.887 -40.135 -27.116  0.53 28.75      A    C  
ANISOU 1204  CG BLEU A 156     3934   2963   4024    261     64    366  A    C  
ATOM   1205  CD1ALEU A 156      19.899 -41.585 -28.686  0.47 30.59      A    C  
ANISOU 1205  CD1ALEU A 156     4111   3047   4466     14   -108    332  A    C  
ATOM   1206  CD1BLEU A 156      18.890 -39.028 -27.397  0.53 33.72      A    C  
ANISOU 1206  CD1BLEU A 156     4442   3704   4667    358     97    358  A    C  
ATOM   1207  CD2ALEU A 156      19.107 -39.250 -28.698  0.47 28.83      A    C  
ANISOU 1207  CD2ALEU A 156     3789   3020   4145    234    -60    283  A    C  
ATOM   1208  CD2BLEU A 156      19.496 -41.404 -27.864  0.53 34.60      A    C  
ANISOU 1208  CD2BLEU A 156     4584   3620   4944     63      6    415  A    C  
ATOM   1209  N   VAL A 157      24.427 -39.779 -27.814  1.00 21.05      A    N  
ANISOU 1209  N   VAL A 157     3254   1925   2819    287   -284     58  A    N  
ATOM   1210  CA  VAL A 157      25.658 -39.624 -28.593  1.00 22.78      A    C  
ANISOU 1210  CA  VAL A 157     3425   2205   3026    253   -368     -9  A    C  
ATOM   1211  C   VAL A 157      26.394 -40.978 -28.723  1.00 25.73      A    C  
ANISOU 1211  C   VAL A 157     3789   2586   3402    340   -380      2  A    C  
ATOM   1212  O   VAL A 157      26.807 -41.363 -29.822  1.00 23.12      A    O  
ANISOU 1212  O   VAL A 157     3419   2271   3094    352   -391    -39  A    O  
ATOM   1213  CB  VAL A 157      26.609 -38.568 -27.989  1.00 24.22      A    C  
ANISOU 1213  CB  VAL A 157     3621   2463   3118    219   -448    -54  A    C  
ATOM   1214  CG1 VAL A 157      27.976 -38.635 -28.660  1.00 21.71      A    C  
ANISOU 1214  CG1 VAL A 157     3164   2280   2805    170   -507    -75  A    C  
ATOM   1215  CG2 VAL A 157      26.008 -37.136 -28.147  1.00 23.67      A    C  
ANISOU 1215  CG2 VAL A 157     3640   2318   3037    147   -457    -86  A    C  
ATOM   1216  N   GLU A 158      26.533 -41.720 -27.626  1.00 22.28      A    N  
ANISOU 1216  N   GLU A 158     3428   2124   2914    441   -373     60  A    N  
ATOM   1217  CA  GLU A 158      27.215 -43.013 -27.694  1.00 20.87      A    C  
ANISOU 1217  CA  GLU A 158     3298   1910   2721    580   -395     78  A    C  
ATOM   1218  C   GLU A 158      26.455 -44.030 -28.557  1.00 24.05      A    C  
ANISOU 1218  C   GLU A 158     3796   2118   3224    545   -368     82  A    C  
ATOM   1219  O   GLU A 158      27.064 -44.924 -29.165  1.00 22.82      A    O  
ANISOU 1219  O   GLU A 158     3713   1906   3053    672   -402     38  A    O  
ATOM   1220  CB  GLU A 158      27.427 -43.596 -26.292  1.00 20.00      A    C  
ANISOU 1220  CB  GLU A 158     3308   1781   2510    713   -400    169  A    C  
ATOM   1221  CG  GLU A 158      28.315 -42.726 -25.405  1.00 22.00      A    C  
ANISOU 1221  CG  GLU A 158     3498   2227   2634    762   -497    135  A    C  
ATOM   1222  CD  GLU A 158      29.774 -42.731 -25.805  1.00 25.59      A    C  
ANISOU 1222  CD  GLU A 158     3777   2879   3068    847   -611     75  A    C  
ATOM   1223  OE1 GLU A 158      30.172 -43.529 -26.696  1.00 22.81      A    O  
ANISOU 1223  OE1 GLU A 158     3381   2523   2762    953   -583     65  A    O  
ATOM   1224  OE2 GLU A 158      30.548 -41.958 -25.193  1.00 26.29      A    O1-
ANISOU 1224  OE2 GLU A 158     3766   3142   3081    820   -738     38  A    O1-
ATOM   1225  N   THR A 159      25.133 -43.906 -28.590  1.00 22.74      A    N  
ANISOU 1225  N   THR A 159     3634   1856   3151    388   -322    128  A    N  
ATOM   1226  CA  THR A 159      24.305 -44.795 -29.404  1.00 23.84      A    C  
ANISOU 1226  CA  THR A 159     3843   1809   3406    281   -351    123  A    C  
ATOM   1227  C   THR A 159      24.673 -44.695 -30.886  1.00 21.10      A    C  
ANISOU 1227  C   THR A 159     3490   1481   3045    303   -432    -20  A    C  
ATOM   1228  O   THR A 159      24.703 -45.712 -31.588  1.00 24.57      A    O  
ANISOU 1228  O   THR A 159     4088   1753   3495    335   -501    -82  A    O  
ATOM   1229  CB  THR A 159      22.818 -44.480 -29.237  1.00 28.47      A    C  
ANISOU 1229  CB  THR A 159     4323   2384   4110     90   -302    206  A    C  
ATOM   1230  CG2 THR A 159      21.957 -45.397 -30.131  1.00 28.29      A    C  
ANISOU 1230  CG2 THR A 159     4342   2179   4230    -85   -395    189  A    C  
ATOM   1231  OG1 THR A 159      22.458 -44.678 -27.864  1.00 25.61      A    O  
ANISOU 1231  OG1 THR A 159     3984   2022   3725     96   -180    363  A    O  
ATOM   1232  N   TYR A 160      24.982 -43.486 -31.352  1.00 19.86      A    N  
ANISOU 1232  N   TYR A 160     3201   1506   2840    299   -423    -67  A    N  
ATOM   1233  CA  TYR A 160      25.182 -43.285 -32.792  1.00 22.97      A    C  
ANISOU 1233  CA  TYR A 160     3601   1938   3187    314   -468   -167  A    C  
ATOM   1234  C   TYR A 160      26.631 -43.099 -33.241  1.00 25.66      A    C  
ANISOU 1234  C   TYR A 160     3897   2448   3404    467   -425   -207  A    C  
ATOM   1235  O   TYR A 160      26.900 -43.143 -34.440  1.00 25.25      A    O  
ANISOU 1235  O   TYR A 160     3884   2441   3269    530   -424   -274  A    O  
ATOM   1236  CB  TYR A 160      24.350 -42.092 -33.268  1.00 20.17      A    C  
ANISOU 1236  CB  TYR A 160     3155   1650   2860    194   -482   -159  A    C  
ATOM   1237  CG  TYR A 160      22.853 -42.352 -33.210  1.00 23.57      A    C  
ANISOU 1237  CG  TYR A 160     3557   1982   3418     67   -537   -127  A    C  
ATOM   1238  CD1 TYR A 160      22.227 -43.136 -34.159  1.00 26.96      A    C  
ANISOU 1238  CD1 TYR A 160     4056   2299   3887      1   -664   -194  A    C  
ATOM   1239  CD2 TYR A 160      22.073 -41.805 -32.189  1.00 23.28      A    C  
ANISOU 1239  CD2 TYR A 160     3410   1989   3448     19   -467    -28  A    C  
ATOM   1240  CE1 TYR A 160      20.857 -43.380 -34.110  1.00 27.49      A    C  
ANISOU 1240  CE1 TYR A 160     4024   2319   4101   -166   -741   -149  A    C  
ATOM   1241  CE2 TYR A 160      20.719 -42.038 -32.128  1.00 26.56      A    C  
ANISOU 1241  CE2 TYR A 160     3713   2389   3991    -93   -490     33  A    C  
ATOM   1242  CZ  TYR A 160      20.111 -42.822 -33.084  1.00 30.38      A    C  
ANISOU 1242  CZ  TYR A 160     4206   2782   4556   -213   -635    -19  A    C  
ATOM   1243  OH  TYR A 160      18.756 -43.046 -33.021  1.00 32.88      A    O  
ANISOU 1243  OH  TYR A 160     4340   3125   5029   -372   -683     57  A    O  
ATOM   1244  N   LEU A 161      27.568 -42.913 -32.313  1.00 21.44      A    N  
ANISOU 1244  N   LEU A 161     3265   2041   2840    533   -391   -159  A    N  
ATOM   1245  CA  LEU A 161      28.992 -42.890 -32.698  1.00 22.31      A    C  
ANISOU 1245  CA  LEU A 161     3251   2371   2856    679   -350   -173  A    C  
ATOM   1246  C   LEU A 161      29.436 -44.120 -33.523  1.00 25.96      A    C  
ANISOU 1246  C   LEU A 161     3837   2792   3233    930   -331   -246  A    C  
ATOM   1247  O   LEU A 161      30.192 -43.967 -34.492  1.00 28.37      A    O  
ANISOU 1247  O   LEU A 161     4061   3284   3433   1045   -255   -274  A    O  
ATOM   1248  CB  LEU A 161      29.884 -42.749 -31.454  1.00 23.92      A    C  
ANISOU 1248  CB  LEU A 161     3321   2719   3049    728   -377   -117  A    C  
ATOM   1249  CG  LEU A 161      29.961 -41.324 -30.887  1.00 24.25      A    C  
ANISOU 1249  CG  LEU A 161     3238   2860   3115    510   -410    -83  A    C  
ATOM   1250  CD1 LEU A 161      30.772 -41.320 -29.592  1.00 25.64      A    C  
ANISOU 1250  CD1 LEU A 161     3327   3160   3256    564   -500    -57  A    C  
ATOM   1251  CD2 LEU A 161      30.597 -40.394 -31.901  1.00 28.57      A    C  
ANISOU 1251  CD2 LEU A 161     3627   3581   3647    390   -360    -70  A    C  
ATOM   1252  N   PRO A 162      28.974 -45.340 -33.162  1.00 23.90      A    N  
ANISOU 1252  N   PRO A 162     3807   2275   2998   1027   -390   -271  A    N  
ATOM   1253  CA  PRO A 162      29.433 -46.466 -33.981  1.00 24.81      A    C  
ANISOU 1253  CA  PRO A 162     4120   2302   3006   1303   -393   -369  A    C  
ATOM   1254  C   PRO A 162      28.885 -46.491 -35.409  1.00 26.88      A    C  
ANISOU 1254  C   PRO A 162     4533   2481   3198   1275   -417   -487  A    C  
ATOM   1255  O   PRO A 162      29.406 -47.254 -36.222  1.00 32.11      A    O  
ANISOU 1255  O   PRO A 162     5374   3116   3711   1551   -403   -594  A    O  
ATOM   1256  CB  PRO A 162      28.945 -47.696 -33.194  1.00 30.74      A    C  
ANISOU 1256  CB  PRO A 162     5140   2723   3816   1338   -473   -347  A    C  
ATOM   1257  CG  PRO A 162      28.859 -47.210 -31.776  1.00 24.10      A    C  
ANISOU 1257  CG  PRO A 162     4159   1944   3054   1223   -463   -209  A    C  
ATOM   1258  CD  PRO A 162      28.316 -45.813 -31.927  1.00 25.56      A    C  
ANISOU 1258  CD  PRO A 162     4123   2288   3299    950   -435   -192  A    C  
ATOM   1259  N   VAL A 163      27.869 -45.697 -35.729  1.00 24.49      A    N  
ANISOU 1259  N   VAL A 163     4187   2149   2971    999   -464   -477  A    N  
ATOM   1260  CA  VAL A 163      27.474 -45.602 -37.141  1.00 28.96      A    C  
ANISOU 1260  CA  VAL A 163     4884   2697   3422   1008   -508   -585  A    C  
ATOM   1261  C   VAL A 163      27.976 -44.299 -37.763  1.00 31.08      A    C  
ANISOU 1261  C   VAL A 163     4946   3269   3594    979   -385   -520  A    C  
ATOM   1262  O   VAL A 163      27.542 -43.912 -38.848  1.00 28.48      A    O  
ANISOU 1262  O   VAL A 163     4707   2957   3159    954   -415   -565  A    O  
ATOM   1263  CB  VAL A 163      25.935 -45.735 -37.353  1.00 25.87      A    C  
ANISOU 1263  CB  VAL A 163     4612   2065   3151    754   -690   -626  A    C  
ATOM   1264  CG1 VAL A 163      25.456 -47.152 -36.980  1.00 33.21      A    C  
ANISOU 1264  CG1 VAL A 163     5730   2727   4162    701   -793   -649  A    C  
ATOM   1265  CG2 VAL A 163      25.178 -44.682 -36.596  1.00 27.75      A    C  
ANISOU 1265  CG2 VAL A 163     4611   2383   3549    508   -675   -497  A    C  
ATOM   1266  N   GLY A 164      28.902 -43.629 -37.080  1.00 26.24      A    N  
ANISOU 1266  N   GLY A 164     4076   2885   3011    969   -264   -407  A    N  
ATOM   1267  CA  GLY A 164      29.608 -42.504 -37.680  1.00 26.88      A    C  
ANISOU 1267  CA  GLY A 164     3968   3241   3002    919   -130   -318  A    C  
ATOM   1268  C   GLY A 164      29.026 -41.124 -37.418  1.00 29.92      A    C  
ANISOU 1268  C   GLY A 164     4268   3615   3485    628   -157   -223  A    C  
ATOM   1269  O   GLY A 164      29.322 -40.190 -38.152  1.00 28.17      A    O  
ANISOU 1269  O   GLY A 164     3997   3527   3180    551    -70   -143  A    O  
ATOM   1270  N   LEU A 165      28.205 -40.993 -36.381  1.00 26.76      A    N  
ANISOU 1270  N   LEU A 165     3879   3048   3240    491   -259   -217  A    N  
ATOM   1271  CA  LEU A 165      27.626 -39.690 -35.994  1.00 27.18      A    C  
ANISOU 1271  CA  LEU A 165     3895   3065   3369    285   -287   -145  A    C  
ATOM   1272  C   LEU A 165      28.657 -38.565 -36.011  1.00 29.15      A    C  
ANISOU 1272  C   LEU A 165     4006   3482   3586    164   -203    -45  A    C  
ATOM   1273  O   LEU A 165      29.745 -38.710 -35.453  1.00 24.71      A    O  
ANISOU 1273  O   LEU A 165     3273   3078   3037    171   -166    -17  A    O  
ATOM   1274  CB  LEU A 165      27.022 -39.766 -34.588  1.00 20.73      A    C  
ANISOU 1274  CB  LEU A 165     3066   2128   2681    227   -349   -140  A    C  
ATOM   1275  CG  LEU A 165      26.486 -38.435 -34.024  1.00 22.81      A    C  
ANISOU 1275  CG  LEU A 165     3335   2343   2989     91   -371    -89  A    C  
ATOM   1276  CD1 LEU A 165      25.229 -38.022 -34.772  1.00 25.53      A    C  
ANISOU 1276  CD1 LEU A 165     3765   2595   3340     83   -416    -92  A    C  
ATOM   1277  CD2 LEU A 165      26.211 -38.532 -32.522  1.00 21.25      A    C  
ANISOU 1277  CD2 LEU A 165     3133   2090   2851     93   -392    -83  A    C  
ATOM   1278  N   LYS A 166      28.309 -37.441 -36.626  1.00 24.35      A    N  
ANISOU 1278  N   LYS A 166     3473   2835   2943     40   -193     21  A    N  
ATOM   1279  CA  LYS A 166      29.258 -36.347 -36.802  1.00 22.25      A    C  
ANISOU 1279  CA  LYS A 166     3118   2684   2654   -140   -114    145  A    C  
ATOM   1280  C   LYS A 166      28.677 -35.015 -36.339  1.00 27.04      A    C  
ANISOU 1280  C   LYS A 166     3863   3091   3321   -321   -195    191  A    C  
ATOM   1281  O   LYS A 166      29.358 -34.224 -35.692  1.00 30.77      A    O  
ANISOU 1281  O   LYS A 166     4283   3560   3849   -519   -220    243  A    O  
ATOM   1282  CB  LYS A 166      29.687 -36.246 -38.279  1.00 27.16      A    C  
ANISOU 1282  CB  LYS A 166     3761   3450   3110    -94     28    227  A    C  
ATOM   1283  CG  LYS A 166      30.596 -35.066 -38.585  1.00 42.01      A    C  
ANISOU 1283  CG  LYS A 166     5552   5438   4971   -340    139    412  A    C  
ATOM   1284  CD  LYS A 166      31.903 -35.119 -37.796  1.00 59.21      A    C  
ANISOU 1284  CD  LYS A 166     7406   7840   7249   -472    173    459  A    C  
ATOM   1285  CE  LYS A 166      32.736 -33.860 -38.039  1.00 78.67      A    C  
ANISOU 1285  CE  LYS A 166     9769  10380   9741   -822    251    662  A    C  
ATOM   1286  NZ  LYS A 166      33.957 -33.788 -37.183  1.00 87.48      A    N1+
ANISOU 1286  NZ  LYS A 166    10526  11724  10987  -1019    217    707  A    N1+
ATOM   1287  N   HIS A 167      27.417 -34.769 -36.679  1.00 28.75      A    N  
ANISOU 1287  N   HIS A 167     4267   3139   3519   -238   -258    164  A    N  
ATOM   1288  CA  HIS A 167      26.786 -33.480 -36.411  1.00 25.91      A    C  
ANISOU 1288  CA  HIS A 167     4091   2576   3177   -317   -323    207  A    C  
ATOM   1289  C   HIS A 167      25.694 -33.597 -35.364  1.00 25.81      A    C  
ANISOU 1289  C   HIS A 167     4118   2443   3245   -201   -411    115  A    C  
ATOM   1290  O   HIS A 167      24.759 -34.399 -35.515  1.00 24.41      A    O  
ANISOU 1290  O   HIS A 167     3894   2289   3090    -56   -439     61  A    O  
ATOM   1291  CB  HIS A 167      26.192 -32.897 -37.693  1.00 24.66      A    C  
ANISOU 1291  CB  HIS A 167     4113   2355   2901   -258   -317    287  A    C  
ATOM   1292  CG  HIS A 167      27.196 -32.709 -38.782  1.00 27.20      A    C  
ANISOU 1292  CG  HIS A 167     4426   2810   3098   -355   -184    416  A    C  
ATOM   1293  CD2 HIS A 167      27.402 -33.387 -39.936  1.00 27.21      A    C  
ANISOU 1293  CD2 HIS A 167     4410   2981   2948   -233    -97    430  A    C  
ATOM   1294  ND1 HIS A 167      28.157 -31.725 -38.737  1.00 25.19      A    N  
ANISOU 1294  ND1 HIS A 167     4185   2534   2853   -612   -112    561  A    N  
ATOM   1295  CE1 HIS A 167      28.913 -31.800 -39.819  1.00 30.94      A    C  
ANISOU 1295  CE1 HIS A 167     4857   3449   3450   -650     51    693  A    C  
ATOM   1296  NE2 HIS A 167      28.467 -32.792 -40.569  1.00 28.79      A    N  
ANISOU 1296  NE2 HIS A 167     4588   3297   3054   -388     68    607  A    N  
ATOM   1297  N   VAL A 168      25.799 -32.776 -34.322  1.00 23.75      A    N  
ANISOU 1297  N   VAL A 168     3950   2059   3016   -272   -457    103  A    N  
ATOM   1298  CA  VAL A 168      24.813 -32.770 -33.251  1.00 23.88      A    C  
ANISOU 1298  CA  VAL A 168     4020   1991   3063   -123   -496     31  A    C  
ATOM   1299  C   VAL A 168      24.368 -31.335 -32.965  1.00 24.13      A    C  
ANISOU 1299  C   VAL A 168     4327   1797   3046    -92   -550     38  A    C  
ATOM   1300  O   VAL A 168      25.193 -30.439 -32.770  1.00 28.16      A    O  
ANISOU 1300  O   VAL A 168     4993   2174   3533   -275   -600     53  A    O  
ATOM   1301  CB  VAL A 168      25.370 -33.409 -31.946  1.00 29.07      A    C  
ANISOU 1301  CB  VAL A 168     4579   2719   3747   -142   -503    -31  A    C  
ATOM   1302  CG1 VAL A 168      24.383 -33.204 -30.807  1.00 23.91      A    C  
ANISOU 1302  CG1 VAL A 168     4027   1986   3071     26   -503    -79  A    C  
ATOM   1303  CG2 VAL A 168      25.654 -34.902 -32.138  1.00 24.76      A    C  
ANISOU 1303  CG2 VAL A 168     3826   2341   3241   -102   -456    -37  A    C  
ATOM   1304  N   LEU A 169      23.059 -31.118 -32.977  1.00 24.81      A    N  
ANISOU 1304  N   LEU A 169     4472   1836   3118    142   -550     30  A    N  
ATOM   1305  CA  LEU A 169      22.504 -29.826 -32.626  1.00 27.76      A    C  
ANISOU 1305  CA  LEU A 169     5090   2041   3417    272   -579     19  A    C  
ATOM   1306  C   LEU A 169      21.977 -29.964 -31.220  1.00 33.41      A    C  
ANISOU 1306  C   LEU A 169     5798   2786   4111    442   -544    -66  A    C  
ATOM   1307  O   LEU A 169      21.014 -30.695 -30.992  1.00 32.56      A    O  
ANISOU 1307  O   LEU A 169     5535   2788   4047    638   -486    -59  A    O  
ATOM   1308  CB  LEU A 169      21.394 -29.414 -33.599  1.00 22.05      A    C  
ANISOU 1308  CB  LEU A 169     4400   1317   2661    479   -591     78  A    C  
ATOM   1309  CG  LEU A 169      20.897 -27.975 -33.672  1.00 31.82      A    C  
ANISOU 1309  CG  LEU A 169     5878   2416   3795    616   -613     89  A    C  
ATOM   1310  CD1 LEU A 169      20.028 -27.827 -34.907  1.00 34.45      A    C  
ANISOU 1310  CD1 LEU A 169     6202   2791   4097    789   -651    168  A    C  
ATOM   1311  CD2 LEU A 169      20.102 -27.591 -32.449  1.00 34.82      A    C  
ANISOU 1311  CD2 LEU A 169     6304   2797   4129    858   -578      7  A    C  
ATOM   1312  N   CYS A 170      22.609 -29.265 -30.279  1.00 28.07      A    N  
ANISOU 1312  N   CYS A 170     5298   2012   3357    367   -587   -133  A    N  
ATOM   1313  CA  CYS A 170      22.268 -29.408 -28.872  1.00 27.30      A    C  
ANISOU 1313  CA  CYS A 170     5255   1940   3180    537   -556   -217  A    C  
ATOM   1314  C   CYS A 170      21.587 -28.132 -28.371  1.00 32.35      A    C  
ANISOU 1314  C   CYS A 170     6155   2466   3673    751   -563   -263  A    C  
ATOM   1315  O   CYS A 170      22.234 -27.095 -28.184  1.00 35.55      A    O  
ANISOU 1315  O   CYS A 170     6809   2698   4001    626   -674   -303  A    O  
ATOM   1316  CB  CYS A 170      23.538 -29.740 -28.068  1.00 28.62      A    C  
ANISOU 1316  CB  CYS A 170     5446   2098   3330    323   -645   -279  A    C  
ATOM   1317  SG  CYS A 170      23.295 -29.808 -26.290  1.00 38.49      A    S  
ANISOU 1317  SG  CYS A 170     6859   3361   4404    541   -638   -387  A    S  
ATOM   1318  N   THR A 171      20.262 -28.184 -28.229  1.00 32.53      A    N  
ANISOU 1318  N   THR A 171     6110   2586   3663   1076   -449   -245  A    N  
ATOM   1319  CA  THR A 171      19.493 -27.038 -27.743  1.00 34.58      A    C  
ANISOU 1319  CA  THR A 171     6606   2772   3759   1352   -434   -287  A    C  
ATOM   1320  C   THR A 171      19.244 -27.142 -26.236  1.00 40.65      A    C  
ANISOU 1320  C   THR A 171     7475   3604   4366   1561   -358   -360  A    C  
ATOM   1321  O   THR A 171      18.724 -28.151 -25.757  1.00 39.28      A    O  
ANISOU 1321  O   THR A 171     7072   3633   4220   1694   -208   -320  A    O  
ATOM   1322  CB  THR A 171      18.122 -26.908 -28.452  1.00 38.14      A    C  
ANISOU 1322  CB  THR A 171     6904   3343   4243   1641   -350   -213  A    C  
ATOM   1323  CG2 THR A 171      17.413 -25.633 -28.004  1.00 39.74      A    C  
ANISOU 1323  CG2 THR A 171     7384   3460   4254   1946   -343   -258  A    C  
ATOM   1324  OG1 THR A 171      18.292 -26.894 -29.884  1.00 39.20      A    O  
ANISOU 1324  OG1 THR A 171     6964   3437   4492   1483   -429   -137  A    O  
ATOM   1325  N   ASP A 172      19.615 -26.109 -25.487  1.00 35.51      A    N  
ANISOU 1325  N   ASP A 172     4144   3408   5939    804   -859   -554  A    N  
ATOM   1326  CA  ASP A 172      19.251 -26.043 -24.071  1.00 35.75      A    C  
ANISOU 1326  CA  ASP A 172     4249   3301   6033    593   -646   -351  A    C  
ATOM   1327  C   ASP A 172      17.849 -25.461 -23.991  1.00 35.67      A    C  
ANISOU 1327  C   ASP A 172     4152   3328   6071    687   -580   -506  A    C  
ATOM   1328  O   ASP A 172      17.655 -24.267 -24.249  1.00 32.52      A    O  
ANISOU 1328  O   ASP A 172     3928   3055   5374    827   -587   -508  A    O  
ATOM   1329  CB  ASP A 172      20.246 -25.187 -23.268  1.00 40.98      A    C  
ANISOU 1329  CB  ASP A 172     5242   3982   6345    492   -570    -71  A    C  
ATOM   1330  CG  ASP A 172      19.926 -25.151 -21.765  1.00 40.68      A    C  
ANISOU 1330  CG  ASP A 172     5272   3892   6294    357   -371    118  A    C  
ATOM   1331  OD1 ASP A 172      18.792 -25.500 -21.356  1.00 35.76      A    O  
ANISOU 1331  OD1 ASP A 172     4489   3199   5900    353   -245     85  A    O  
ATOM   1332  OD2 ASP A 172      20.822 -24.764 -20.989  1.00 45.35      A    O1-
ANISOU 1332  OD2 ASP A 172     6054   4532   6644    289   -338    280  A    O1-
ATOM   1333  N   ILE A 173      16.870 -26.292 -23.648  1.00 33.64      A    N  
ANISOU 1333  N   ILE A 173     3610   2939   6233    620   -484   -631  A    N  
ATOM   1334  CA  ILE A 173      15.481 -25.863 -23.783  1.00 35.08      A    C  
ANISOU 1334  CA  ILE A 173     3637   3171   6523    735   -458   -865  A    C  
ATOM   1335  C   ILE A 173      15.098 -24.828 -22.726  1.00 34.50      A    C  
ANISOU 1335  C   ILE A 173     3817   3103   6190    678   -275   -626  A    C  
ATOM   1336  O   ILE A 173      14.075 -24.157 -22.862  1.00 35.23      A    O  
ANISOU 1336  O   ILE A 173     3868   3275   6242    796   -262   -776  A    O  
ATOM   1337  CB  ILE A 173      14.488 -27.041 -23.711  1.00 40.83      A    C  
ANISOU 1337  CB  ILE A 173     3921   3703   7888    668   -369  -1114  A    C  
ATOM   1338  CG1 ILE A 173      14.477 -27.664 -22.321  1.00 41.98      A    C  
ANISOU 1338  CG1 ILE A 173     4076   3581   8295    444    -37   -757  A    C  
ATOM   1339  CG2 ILE A 173      14.807 -28.085 -24.773  1.00 38.96      A    C  
ANISOU 1339  CG2 ILE A 173     3368   3458   7976    733   -566  -1449  A    C  
ATOM   1340  CD1 ILE A 173      13.529 -28.819 -22.222  1.00 51.48      A    C  
ANISOU 1340  CD1 ILE A 173     4815   4500  10245    372    149   -956  A    C  
ATOM   1341  N   SER A 174      15.917 -24.675 -21.690  1.00 35.72      A    N  
ANISOU 1341  N   SER A 174     4217   3209   6147    531   -150   -294  A    N  
ATOM   1342  CA  SER A 174      15.663 -23.608 -20.717  1.00 39.36      A    C  
ANISOU 1342  CA  SER A 174     4910   3726   6321    515    -16   -133  A    C  
ATOM   1343  C   SER A 174      16.146 -22.248 -21.222  1.00 38.34      A    C  
ANISOU 1343  C   SER A 174     5027   3722   5818    615   -114   -164  A    C  
ATOM   1344  O   SER A 174      15.815 -21.215 -20.639  1.00 36.02      A    O  
ANISOU 1344  O   SER A 174     4888   3465   5333    629    -20   -121  A    O  
ATOM   1345  CB  SER A 174      16.320 -23.925 -19.367  1.00 40.90      A    C  
ANISOU 1345  CB  SER A 174     5232   3894   6414    401    142    172  A    C  
ATOM   1346  OG  SER A 174      17.732 -23.772 -19.407  1.00 47.69      A    O  
ANISOU 1346  OG  SER A 174     6271   4823   7027    363     28    257  A    O  
ATOM   1347  N   ARG A 175      16.915 -22.242 -22.309  1.00 34.73      A    N  
ANISOU 1347  N   ARG A 175     4591   3311   5294    707   -267   -231  A    N  
ATOM   1348  CA  ARG A 175      17.467 -20.994 -22.840  1.00 30.13      A    C  
ANISOU 1348  CA  ARG A 175     4223   2786   4438    831   -273   -199  A    C  
ATOM   1349  C   ARG A 175      16.840 -20.596 -24.175  1.00 30.85      A    C  
ANISOU 1349  C   ARG A 175     4237   3009   4474   1146   -345   -362  A    C  
ATOM   1350  O   ARG A 175      16.957 -19.451 -24.614  1.00 34.27      A    O  
ANISOU 1350  O   ARG A 175     4831   3477   4713   1324   -260   -295  A    O  
ATOM   1351  CB  ARG A 175      18.973 -21.123 -23.000  1.00 37.08      A    C  
ANISOU 1351  CB  ARG A 175     5216   3628   5244    753   -328    -82  A    C  
ATOM   1352  CG  ARG A 175      19.640 -21.608 -21.755  1.00 44.04      A    C  
ANISOU 1352  CG  ARG A 175     6145   4462   6128    524   -289     47  A    C  
ATOM   1353  CD  ARG A 175      20.746 -20.692 -21.374  1.00 45.55      A    C  
ANISOU 1353  CD  ARG A 175     6518   4634   6154    460   -255     97  A    C  
ATOM   1354  NE  ARG A 175      21.243 -20.985 -20.038  1.00 43.98      A    N  
ANISOU 1354  NE  ARG A 175     6350   4486   5873    324   -231    161  A    N  
ATOM   1355  CZ  ARG A 175      22.191 -20.277 -19.445  1.00 44.71      A    C  
ANISOU 1355  CZ  ARG A 175     6537   4604   5846    265   -228    110  A    C  
ATOM   1356  NH1 ARG A 175      22.725 -19.247 -20.087  1.00 38.18      A    N1+
ANISOU 1356  NH1 ARG A 175     5775   3670   5063    282   -195     26  A    N1+
ATOM   1357  NH2 ARG A 175      22.604 -20.597 -18.225  1.00 49.30      A    N  
ANISOU 1357  NH2 ARG A 175     7119   5324   6288    227   -235    130  A    N  
ATOM   1358  N   ASP A 176      16.157 -21.548 -24.792  1.00 43.18      A    N  
ANISOU 1358  N   ASP A 176     5524   4651   6231   1248   -479   -590  A    N  
ATOM   1359  CA  ASP A 176      15.492 -21.348 -26.074  1.00 51.92      A    C  
ANISOU 1359  CA  ASP A 176     6489   5983   7256   1630   -599   -830  A    C  
ATOM   1360  C   ASP A 176      14.622 -20.079 -26.091  1.00 41.53      A    C  
ANISOU 1360  C   ASP A 176     5288   4759   5731   1836   -475   -813  A    C  
ATOM   1361  O   ASP A 176      13.647 -19.988 -25.351  1.00 39.60      A    O  
ANISOU 1361  O   ASP A 176     4980   4464   5603   1723   -401   -878  A    O  
ATOM   1362  CB  ASP A 176      14.645 -22.588 -26.387  1.00 64.69      A    C  
ANISOU 1362  CB  ASP A 176     7704   7644   9230   1650   -752  -1195  A    C  
ATOM   1363  CG  ASP A 176      14.195 -22.644 -27.826  1.00 77.41      A    C  
ANISOU 1363  CG  ASP A 176     9096   9574  10741   2101   -963  -1545  A    C  
ATOM   1364  OD1 ASP A 176      14.795 -21.941 -28.664  1.00 84.25      A    O  
ANISOU 1364  OD1 ASP A 176    10155  10629  11227   2381   -973  -1403  A    O  
ATOM   1365  OD2 ASP A 176      13.251 -23.408 -28.119  1.00 80.25      A    O1-
ANISOU 1365  OD2 ASP A 176     9100  10016  11377   2115  -1077  -1923  A    O1-
ATOM   1366  N   GLY A 177      15.002 -19.098 -26.913  1.00 40.31      A    N  
ANISOU 1366  N   GLY A 177     5308   4720   5288   2153   -411   -687  A    N  
ATOM   1367  CA  GLY A 177      14.211 -17.888 -27.091  1.00 39.22      A    C  
ANISOU 1367  CA  GLY A 177     5274   4674   4953   2424   -260   -644  A    C  
ATOM   1368  C   GLY A 177      14.324 -16.850 -25.976  1.00 34.51      A    C  
ANISOU 1368  C   GLY A 177     4921   3836   4354   2169    -16   -418  A    C  
ATOM   1369  O   GLY A 177      13.597 -15.853 -25.989  1.00 40.28      A    O  
ANISOU 1369  O   GLY A 177     5731   4602   4970   2353    133   -384  A    O  
ATOM   1370  N   THR A 178      15.246 -17.050 -25.033  1.00 33.01      A    N  
ANISOU 1370  N   THR A 178     4834   3430   4278   1786     21   -293  A    N  
ATOM   1371  CA  THR A 178      15.321 -16.159 -23.869  1.00 35.11      A    C  
ANISOU 1371  CA  THR A 178     5268   3519   4555   1557    202   -189  A    C  
ATOM   1372  C   THR A 178      16.284 -14.961 -23.972  1.00 35.94      A    C  
ANISOU 1372  C   THR A 178     5568   3449   4638   1589    416    -22  A    C  
ATOM   1373  O   THR A 178      16.182 -14.037 -23.173  1.00 43.71      A    O  
ANISOU 1373  O   THR A 178     6648   4300   5660   1474    578    -13  A    O  
ATOM   1374  CB  THR A 178      15.710 -16.937 -22.612  1.00 31.72      A    C  
ANISOU 1374  CB  THR A 178     4812   3005   4234   1188    141   -189  A    C  
ATOM   1375  CG2 THR A 178      14.695 -18.048 -22.349  1.00 33.73      A    C  
ANISOU 1375  CG2 THR A 178     4851   3334   4631   1137     44   -310  A    C  
ATOM   1376  OG1 THR A 178      17.012 -17.499 -22.785  1.00 30.84      A    O  
ANISOU 1376  OG1 THR A 178     4721   2841   4155   1079     61   -119  A    O  
ATOM   1377  N   LEU A 179      17.226 -14.999 -24.913  1.00 41.64      A    N  
ANISOU 1377  N   LEU A 179     6320   4151   5350   1740    435     90  A    N  
ATOM   1378  CA  LEU A 179      18.198 -13.908 -25.076  1.00 38.03      A    C  
ANISOU 1378  CA  LEU A 179     6000   3459   4991   1773    702    258  A    C  
ATOM   1379  C   LEU A 179      19.100 -13.792 -23.843  1.00 36.60      A    C  
ANISOU 1379  C   LEU A 179     5844   3079   4984   1360    708    179  A    C  
ATOM   1380  O   LEU A 179      19.674 -12.728 -23.582  1.00 36.76      A    O  
ANISOU 1380  O   LEU A 179     5920   2857   5191   1304    944    196  A    O  
ATOM   1381  CB  LEU A 179      17.497 -12.562 -25.342  1.00 35.71      A    C  
ANISOU 1381  CB  LEU A 179     5792   3089   4688   2041   1001    358  A    C  
ATOM   1382  CG  LEU A 179      16.526 -12.440 -26.515  1.00 40.49      A    C  
ANISOU 1382  CG  LEU A 179     6350   3985   5051   2494   1011    422  A    C  
ATOM   1383  CD1 LEU A 179      15.885 -11.055 -26.534  1.00 43.66      A    C  
ANISOU 1383  CD1 LEU A 179     6803   4341   5443   2592   1293    536  A    C  
ATOM   1384  CD2 LEU A 179      17.264 -12.692 -27.823  1.00 37.99      A    C  
ANISOU 1384  CD2 LEU A 179     5971   3851   4611   2668    991    566  A    C  
ATOM   1385  N   ALA A 180      19.209 -14.904 -23.110  1.00 41.81      A    N  
ANISOU 1385  N   ALA A 180     6432   3850   5604   1115    463     73  A    N  
ATOM   1386  CA  ALA A 180      19.964 -15.020 -21.860  1.00 47.52      A    C  
ANISOU 1386  CA  ALA A 180     7152   4518   6386    806    408    -30  A    C  
ATOM   1387  C   ALA A 180      21.469 -15.045 -22.062  1.00 46.99      A    C  
ANISOU 1387  C   ALA A 180     7085   4324   6443    709    413    -15  A    C  
ATOM   1388  O   ALA A 180      22.251 -14.668 -21.181  1.00 39.31      A    O  
ANISOU 1388  O   ALA A 180     6093   3275   5568    521    427   -160  A    O  
ATOM   1389  CB  ALA A 180      19.539 -16.308 -21.122  1.00 30.68      A    C  
ANISOU 1389  CB  ALA A 180     4939   2566   4152    675    206    -62  A    C  
ATOM   1390  N   GLY A 181      21.866 -15.511 -23.234  1.00 31.04      A    N  
ANISOU 1390  N   GLY A 181     5061   2314   4419    864    386    124  A    N  
ATOM   1391  CA  GLY A 181      23.214 -15.983 -23.427  1.00 32.91      A    C  
ANISOU 1391  CA  GLY A 181     5277   2491   4736    759    320    151  A    C  
ATOM   1392  C   GLY A 181      23.043 -17.486 -23.467  1.00 38.79      A    C  
ANISOU 1392  C   GLY A 181     5953   3440   5347    717     54    158  A    C  
ATOM   1393  O   GLY A 181      22.121 -18.027 -22.841  1.00 37.89      A    O  
ANISOU 1393  O   GLY A 181     5791   3447   5159    662    -38    101  A    O  
ATOM   1394  N   SER A 182      23.901 -18.155 -24.223  1.00 37.41      A    N  
ANISOU 1394  N   SER A 182     5752   3275   5186    757    -33    234  A    N  
ATOM   1395  CA  SER A 182      23.840 -19.607 -24.334  1.00 37.82      A    C  
ANISOU 1395  CA  SER A 182     5708   3472   5190    715   -260    223  A    C  
ATOM   1396  C   SER A 182      24.469 -20.235 -23.103  1.00 36.95      A    C  
ANISOU 1396  C   SER A 182     5581   3378   5082    447   -349    191  A    C  
ATOM   1397  O   SER A 182      25.173 -19.568 -22.342  1.00 35.80      A    O  
ANISOU 1397  O   SER A 182     5482   3174   4948    323   -288    132  A    O  
ATOM   1398  CB  SER A 182      24.542 -20.083 -25.607  1.00 42.79      A    C  
ANISOU 1398  CB  SER A 182     6312   4131   5817    889   -326    301  A    C  
ATOM   1399  OG  SER A 182      23.738 -19.825 -26.755  1.00 51.37      A    O  
ANISOU 1399  OG  SER A 182     7372   5332   6815   1245   -296    309  A    O  
ATOM   1400  N   ASN A 183      24.204 -21.522 -22.901  1.00 39.11      A    N  
ANISOU 1400  N   ASN A 183     5757   3739   5365    396   -477    211  A    N  
ATOM   1401  CA  ASN A 183      24.782 -22.244 -21.779  1.00 37.03      A    C  
ANISOU 1401  CA  ASN A 183     5478   3530   5063    233   -524    251  A    C  
ATOM   1402  C   ASN A 183      26.240 -22.561 -22.053  1.00 36.72      A    C  
ANISOU 1402  C   ASN A 183     5455   3475   5022    173   -609    282  A    C  
ATOM   1403  O   ASN A 183      26.566 -23.660 -22.520  1.00 32.39      A    O  
ANISOU 1403  O   ASN A 183     4837   2938   4533    173   -708    349  A    O  
ATOM   1404  CB  ASN A 183      24.012 -23.538 -21.510  1.00 35.13      A    C  
ANISOU 1404  CB  ASN A 183     5106   3320   4921    224   -543    317  A    C  
ATOM   1405  CG  ASN A 183      24.405 -24.186 -20.195  1.00 36.90      A    C  
ANISOU 1405  CG  ASN A 183     5330   3626   5064    150   -500    439  A    C  
ATOM   1406  ND2 ASN A 183      23.508 -24.995 -19.648  1.00 34.30      A    N  
ANISOU 1406  ND2 ASN A 183     4897   3283   4852    169   -390    545  A    N  
ATOM   1407  OD1 ASN A 183      25.507 -23.971 -19.683  1.00 35.61      A    O  
ANISOU 1407  OD1 ASN A 183     5239   3547   4746    112   -546    436  A    O  
ATOM   1408  N   VAL A 184      27.121 -21.617 -21.744  1.00 32.69      A    N  
ANISOU 1408  N   VAL A 184     5005   2922   4492    116   -565    199  A    N  
ATOM   1409  CA  VAL A 184      28.508 -21.746 -22.161  1.00 35.82      A    C  
ANISOU 1409  CA  VAL A 184     5397   3270   4943     68   -621    201  A    C  
ATOM   1410  C   VAL A 184      29.164 -22.986 -21.541  1.00 33.59      A    C  
ANISOU 1410  C   VAL A 184     5069   3129   4566     -4   -761    258  A    C  
ATOM   1411  O   VAL A 184      29.886 -23.708 -22.224  1.00 30.18      A    O  
ANISOU 1411  O   VAL A 184     4613   2673   4180     -6   -844    336  A    O  
ATOM   1412  CB  VAL A 184      29.314 -20.486 -21.806  1.00 36.50      A    C  
ANISOU 1412  CB  VAL A 184     5487   3249   5133      0   -519     28  A    C  
ATOM   1413  CG1 VAL A 184      30.780 -20.659 -22.177  1.00 34.00      A    C  
ANISOU 1413  CG1 VAL A 184     5128   2867   4924    -63   -565      8  A    C  
ATOM   1414  CG2 VAL A 184      28.717 -19.266 -22.515  1.00 36.26      A    C  
ANISOU 1414  CG2 VAL A 184     5501   3024   5253    105   -305     39  A    C  
ATOM   1415  N   SER A 185      28.890 -23.270 -20.272  1.00 30.69      A    N  
ANISOU 1415  N   SER A 185     4687   2922   4050    -15   -764    249  A    N  
ATOM   1416  CA  SER A 185      29.623 -24.363 -19.626  1.00 33.55      A    C  
ANISOU 1416  CA  SER A 185     5013   3440   4292    -12   -845    346  A    C  
ATOM   1417  C   SER A 185      29.135 -25.707 -20.173  1.00 34.53      A    C  
ANISOU 1417  C   SER A 185     5081   3495   4542      9   -840    557  A    C  
ATOM   1418  O   SER A 185      29.907 -26.663 -20.285  1.00 29.64      A    O  
ANISOU 1418  O   SER A 185     4428   2900   3936      0   -903    661  A    O  
ATOM   1419  CB  SER A 185      29.485 -24.306 -18.102  1.00 43.75      A    C  
ANISOU 1419  CB  SER A 185     6301   4984   5338     77   -813    315  A    C  
ATOM   1420  OG  SER A 185      28.173 -24.619 -17.693  1.00 49.10      A    O  
ANISOU 1420  OG  SER A 185     6978   5668   6009    148   -681    465  A    O  
ATOM   1421  N   LEU A 186      27.860 -25.780 -20.534  1.00 32.23      A    N  
ANISOU 1421  N   LEU A 186     4750   3109   4387     39   -763    581  A    N  
ATOM   1422  CA  LEU A 186      27.365 -26.984 -21.186  1.00 31.34      A    C  
ANISOU 1422  CA  LEU A 186     4508   2891   4510     52   -764    665  A    C  
ATOM   1423  C   LEU A 186      28.154 -27.261 -22.466  1.00 29.50      A    C  
ANISOU 1423  C   LEU A 186     4251   2598   4361     53   -910    610  A    C  
ATOM   1424  O   LEU A 186      28.619 -28.376 -22.681  1.00 26.05      A    O  
ANISOU 1424  O   LEU A 186     3728   2129   4039     35   -957    684  A    O  
ATOM   1425  CB  LEU A 186      25.879 -26.866 -21.512  1.00 32.42      A    C  
ANISOU 1425  CB  LEU A 186     4554   2946   4819     98   -690    589  A    C  
ATOM   1426  CG  LEU A 186      25.307 -27.941 -22.440  1.00 30.01      A    C  
ANISOU 1426  CG  LEU A 186     4036   2521   4845    126   -729    517  A    C  
ATOM   1427  CD1 LEU A 186      25.334 -29.328 -21.783  1.00 30.71      A    C  
ANISOU 1427  CD1 LEU A 186     3985   2512   5173     78   -601    691  A    C  
ATOM   1428  CD2 LEU A 186      23.898 -27.568 -22.828  1.00 33.81      A    C  
ANISOU 1428  CD2 LEU A 186     4409   2972   5466    202   -695    347  A    C  
ATOM   1429  N   TYR A 187      28.323 -26.255 -23.317  1.00 28.54      A    N  
ANISOU 1429  N   TYR A 187     5125   2252   3468    546  -1488   -535  A    N  
ATOM   1430  CA  TYR A 187      28.995 -26.537 -24.586  1.00 28.37      A    C  
ANISOU 1430  CA  TYR A 187     4936   2140   3705    132  -1400   -344  A    C  
ATOM   1431  C   TYR A 187      30.486 -26.792 -24.374  1.00 29.63      A    C  
ANISOU 1431  C   TYR A 187     4995   2275   3988    -75  -1518   -296  A    C  
ATOM   1432  O   TYR A 187      31.055 -27.636 -25.061  1.00 32.23      A    O  
ANISOU 1432  O   TYR A 187     5125   2731   4389   -266  -1322   -117  A    O  
ATOM   1433  CB  TYR A 187      28.758 -25.406 -25.595  1.00 33.31      A    C  
ANISOU 1433  CB  TYR A 187     5657   2511   4489     -7  -1555   -315  A    C  
ATOM   1434  CG  TYR A 187      27.292 -25.303 -25.932  1.00 29.53      A    C  
ANISOU 1434  CG  TYR A 187     5223   2132   3864    208  -1401   -345  A    C  
ATOM   1435  CD1 TYR A 187      26.648 -26.337 -26.607  1.00 26.21      A    C  
ANISOU 1435  CD1 TYR A 187     4594   1944   3420    158  -1083   -220  A    C  
ATOM   1436  CD2 TYR A 187      26.538 -24.214 -25.515  1.00 37.71      A    C  
ANISOU 1436  CD2 TYR A 187     6510   3042   4775    498  -1610   -518  A    C  
ATOM   1437  CE1 TYR A 187      25.298 -26.269 -26.878  1.00 26.65      A    C  
ANISOU 1437  CE1 TYR A 187     4631   2132   3363    335   -968   -236  A    C  
ATOM   1438  CE2 TYR A 187      25.191 -24.142 -25.787  1.00 37.64      A    C  
ANISOU 1438  CE2 TYR A 187     6499   3207   4598    733  -1456   -527  A    C  
ATOM   1439  CZ  TYR A 187      24.581 -25.174 -26.463  1.00 29.04      A    C  
ANISOU 1439  CZ  TYR A 187     5139   2379   3516    625  -1129   -371  A    C  
ATOM   1440  OH  TYR A 187      23.238 -25.106 -26.740  1.00 32.85      A    O  
ANISOU 1440  OH  TYR A 187     5560   3064   3858    830  -1004   -365  A    O  
ATOM   1441  N   GLU A 188      31.103 -26.089 -23.422  1.00 29.33      A    N  
ANISOU 1441  N   GLU A 188     5094   2099   3952      8  -1863   -475  A    N  
ATOM   1442  CA  GLU A 188      32.508 -26.351 -23.095  1.00 34.19      A    C  
ANISOU 1442  CA  GLU A 188     5571   2747   4674   -168  -2001   -438  A    C  
ATOM   1443  C   GLU A 188      32.656 -27.822 -22.736  1.00 35.53      A    C  
ANISOU 1443  C   GLU A 188     5590   3256   4652    -42  -1659   -352  A    C  
ATOM   1444  O   GLU A 188      33.569 -28.498 -23.210  1.00 32.03      A    O  
ANISOU 1444  O   GLU A 188     4945   2939   4287   -234  -1545   -183  A    O  
ATOM   1445  CB  GLU A 188      33.008 -25.475 -21.949  1.00 39.44      A    C  
ANISOU 1445  CB  GLU A 188     6423   3226   5338    -23  -2479   -719  A    C  
ATOM   1446  CG  GLU A 188      33.078 -24.002 -22.292  1.00 65.08      A    C  
ANISOU 1446  CG  GLU A 188     9722   6189   8817   -138  -2741   -679  A    C  
ATOM   1447  CD  GLU A 188      33.613 -23.138 -21.156  1.00 75.78      A    C  
ANISOU 1447  CD  GLU A 188    11205   7391  10196     52  -3160   -900  A    C  
ATOM   1448  OE1 GLU A 188      33.024 -23.157 -20.054  1.00 72.79      A    O  
ANISOU 1448  OE1 GLU A 188    11037   7095   9523    527  -3245  -1174  A    O  
ATOM   1449  OE2 GLU A 188      34.609 -22.416 -21.380  1.00 78.47      A    O1-
ANISOU 1449  OE2 GLU A 188    11427   7540  10847   -243  -3407   -780  A    O1-
ATOM   1450  N   GLU A 189      31.731 -28.321 -21.924  1.00 31.15      A    N  
ANISOU 1450  N   GLU A 189     5129   2863   3842    307  -1489   -429  A    N  
ATOM   1451  CA  GLU A 189      31.802 -29.710 -21.459  1.00 31.93      A    C  
ANISOU 1451  CA  GLU A 189     5113   3227   3790    440  -1184   -303  A    C  
ATOM   1452  C   GLU A 189      31.585 -30.736 -22.574  1.00 31.50      A    C  
ANISOU 1452  C   GLU A 189     4907   3206   3856    225   -877    -84  A    C  
ATOM   1453  O   GLU A 189      32.414 -31.639 -22.756  1.00 27.67      A    O  
ANISOU 1453  O   GLU A 189     4315   2810   3387    152   -774     19  A    O  
ATOM   1454  CB  GLU A 189      30.785 -29.957 -20.344  1.00 32.42      A    C  
ANISOU 1454  CB  GLU A 189     5262   3486   3571    866  -1054   -332  A    C  
ATOM   1455  CG  GLU A 189      30.773 -31.412 -19.858  1.00 35.24      A    C  
ANISOU 1455  CG  GLU A 189     5494   4074   3820    982   -725   -111  A    C  
ATOM   1456  CD  GLU A 189      29.787 -31.643 -18.718  1.00 45.51      A    C  
ANISOU 1456  CD  GLU A 189     6811   5645   4835   1423   -558    -23  A    C  
ATOM   1457  OE1 GLU A 189      29.294 -30.645 -18.142  1.00 41.05      A    O  
ANISOU 1457  OE1 GLU A 189     6383   5144   4070   1738   -738   -208  A    O  
ATOM   1458  OE2 GLU A 189      29.496 -32.823 -18.413  1.00 38.22      A    O1-
ANISOU 1458  OE2 GLU A 189     5763   4877   3885   1481   -254    258  A    O1-
ATOM   1459  N   VAL A 190      30.490 -30.621 -23.323  1.00 30.18      A    N  
ANISOU 1459  N   VAL A 190     4742   2975   3752    170   -765    -40  A    N  
ATOM   1460  CA  VAL A 190      30.204 -31.677 -24.302  1.00 26.63      A    C  
ANISOU 1460  CA  VAL A 190     4175   2539   3405     26   -544    105  A    C  
ATOM   1461  C   VAL A 190      31.196 -31.637 -25.462  1.00 28.67      A    C  
ANISOU 1461  C   VAL A 190     4353   2763   3778   -187   -599    153  A    C  
ATOM   1462  O   VAL A 190      31.571 -32.688 -25.983  1.00 25.73      A    O  
ANISOU 1462  O   VAL A 190     3912   2451   3413   -204   -480    229  A    O  
ATOM   1463  CB  VAL A 190      28.757 -31.616 -24.833  1.00 28.89      A    C  
ANISOU 1463  CB  VAL A 190     4443   2800   3735     28   -444    128  A    C  
ATOM   1464  CG1 VAL A 190      27.774 -31.684 -23.654  1.00 26.28      A    C  
ANISOU 1464  CG1 VAL A 190     4115   2617   3253    286   -348    169  A    C  
ATOM   1465  CG2 VAL A 190      28.518 -30.385 -25.719  1.00 26.51      A    C  
ANISOU 1465  CG2 VAL A 190     4198   2380   3494    -62   -591     48  A    C  
ATOM   1466  N   CYS A 191      31.662 -30.446 -25.842  1.00 28.87      A    N  
ANISOU 1466  N   CYS A 191     4384   2701   3885   -316   -793    138  A    N  
ATOM   1467  CA  CYS A 191      32.606 -30.359 -26.950  1.00 26.40      A    C  
ANISOU 1467  CA  CYS A 191     3924   2444   3663   -492   -806    289  A    C  
ATOM   1468  C   CYS A 191      33.932 -31.022 -26.604  1.00 33.01      A    C  
ANISOU 1468  C   CYS A 191     4632   3463   4448   -487   -801    365  A    C  
ATOM   1469  O   CYS A 191      34.541 -31.686 -27.443  1.00 30.88      A    O  
ANISOU 1469  O   CYS A 191     4229   3368   4134   -476   -687    496  A    O  
ATOM   1470  CB  CYS A 191      32.847 -28.908 -27.356  1.00 28.88      A    C  
ANISOU 1470  CB  CYS A 191     4237   2602   4136   -671  -1023    353  A    C  
ATOM   1471  SG  CYS A 191      31.414 -28.179 -28.177  1.00 32.66      A    S  
ANISOU 1471  SG  CYS A 191     4844   2925   4638   -637   -994    316  A    S  
ATOM   1472  N   ALA A 192      34.383 -30.829 -25.371  1.00 31.15      A    N  
ANISOU 1472  N   ALA A 192     4437   3222   4175   -432   -943    267  A    N  
ATOM   1473  CA  ALA A 192      35.638 -31.426 -24.936  1.00 28.91      A    C  
ANISOU 1473  CA  ALA A 192     4019   3145   3819   -396   -957    324  A    C  
ATOM   1474  C   ALA A 192      35.471 -32.932 -24.749  1.00 26.76      A    C  
ANISOU 1474  C   ALA A 192     3795   2995   3379   -173   -707    332  A    C  
ATOM   1475  O   ALA A 192      36.401 -33.706 -24.994  1.00 30.81      A    O  
ANISOU 1475  O   ALA A 192     4198   3705   3804   -104   -636    425  A    O  
ATOM   1476  CB  ALA A 192      36.116 -30.780 -23.646  1.00 28.60      A    C  
ANISOU 1476  CB  ALA A 192     4026   3067   3773   -354  -1229    171  A    C  
ATOM   1477  N   ARG A 193      34.288 -33.335 -24.297  1.00 27.23      A    N  
ANISOU 1477  N   ARG A 193     4007   2937   3402    -50   -589    263  A    N  
ATOM   1478  CA  ARG A 193      33.993 -34.747 -24.045  1.00 25.71      A    C  
ANISOU 1478  CA  ARG A 193     3872   2764   3135    112   -388    322  A    C  
ATOM   1479  C   ARG A 193      33.945 -35.546 -25.350  1.00 28.08      A    C  
ANISOU 1479  C   ARG A 193     4155   3022   3493     72   -304    372  A    C  
ATOM   1480  O   ARG A 193      34.317 -36.732 -25.377  1.00 28.87      A    O  
ANISOU 1480  O   ARG A 193     4300   3135   3534    212   -229    411  A    O  
ATOM   1481  CB  ARG A 193      32.664 -34.874 -23.280  1.00 25.01      A    C  
ANISOU 1481  CB  ARG A 193     3872   2587   3042    210   -288    330  A    C  
ATOM   1482  CG  ARG A 193      32.305 -36.283 -22.806  1.00 28.40      A    C  
ANISOU 1482  CG  ARG A 193     4336   2992   3464    337    -98    481  A    C  
ATOM   1483  CD  ARG A 193      33.195 -36.745 -21.657  1.00 26.21      A    C  
ANISOU 1483  CD  ARG A 193     4084   2880   2996    569    -67    525  A    C  
ATOM   1484  NE  ARG A 193      32.705 -38.002 -21.101  1.00 25.85      A    N  
ANISOU 1484  NE  ARG A 193     4080   2776   2967    695    126    742  A    N  
ATOM   1485  CZ  ARG A 193      33.356 -38.724 -20.200  1.00 27.97      A    C  
ANISOU 1485  CZ  ARG A 193     4390   3159   3077    932    205    846  A    C  
ATOM   1486  NH1 ARG A 193      34.544 -38.324 -19.753  1.00 26.78      A    N1+
ANISOU 1486  NH1 ARG A 193     4228   3224   2722   1077     90    710  A    N1+
ATOM   1487  NH2 ARG A 193      32.818 -39.857 -19.755  1.00 28.19      A    N  
ANISOU 1487  NH2 ARG A 193     4454   3079   3177   1014    382   1116  A    N  
ATOM   1488  N   TYR A 194      33.497 -34.893 -26.424  1.00 26.74      A    N  
ANISOU 1488  N   TYR A 194     3948   2797   3414    -61   -347    354  A    N  
ATOM   1489  CA  TYR A 194      33.406 -35.530 -27.752  1.00 25.41      A    C  
ANISOU 1489  CA  TYR A 194     3777   2627   3251    -19   -315    352  A    C  
ATOM   1490  C   TYR A 194      34.052 -34.688 -28.851  1.00 25.01      A    C  
ANISOU 1490  C   TYR A 194     3584   2755   3165    -70   -363    434  A    C  
ATOM   1491  O   TYR A 194      33.355 -34.091 -29.681  1.00 28.03      A    O  
ANISOU 1491  O   TYR A 194     3961   3082   3607   -135   -381    424  A    O  
ATOM   1492  CB  TYR A 194      31.943 -35.810 -28.120  1.00 25.34      A    C  
ANISOU 1492  CB  TYR A 194     3847   2403   3376    -66   -300    278  A    C  
ATOM   1493  CG  TYR A 194      31.288 -36.786 -27.182  1.00 25.60      A    C  
ANISOU 1493  CG  TYR A 194     3955   2279   3493    -39   -233    312  A    C  
ATOM   1494  CD1 TYR A 194      31.536 -38.151 -27.291  1.00 21.89      A    C  
ANISOU 1494  CD1 TYR A 194     3576   1690   3051     67   -236    320  A    C  
ATOM   1495  CD2 TYR A 194      30.426 -36.351 -26.174  1.00 27.91      A    C  
ANISOU 1495  CD2 TYR A 194     4226   2554   3826    -80   -171    372  A    C  
ATOM   1496  CE1 TYR A 194      30.943 -39.069 -26.406  1.00 23.13      A    C  
ANISOU 1496  CE1 TYR A 194     3782   1665   3340     57   -172    444  A    C  
ATOM   1497  CE2 TYR A 194      29.839 -37.260 -25.290  1.00 24.61      A    C  
ANISOU 1497  CE2 TYR A 194     3814   2056   3480    -42    -67    515  A    C  
ATOM   1498  CZ  TYR A 194      30.092 -38.613 -25.422  1.00 25.81      A    C  
ANISOU 1498  CZ  TYR A 194     4037   2043   3727    -12    -65    577  A    C  
ATOM   1499  OH  TYR A 194      29.520 -39.526 -24.552  1.00 28.11      A    O  
ANISOU 1499  OH  TYR A 194     4318   2217   4145     -8     37    804  A    O  
ATOM   1500  N   PRO A 195      35.395 -34.643 -28.874  1.00 26.01      A    N  
ANISOU 1500  N   PRO A 195     3559   3138   3187    -26   -374    564  A    N  
ATOM   1501  CA  PRO A 195      36.110 -33.823 -29.861  1.00 30.63      A    C  
ANISOU 1501  CA  PRO A 195     3924   3959   3755    -90   -392    769  A    C  
ATOM   1502  C   PRO A 195      35.836 -34.240 -31.313  1.00 35.39      A    C  
ANISOU 1502  C   PRO A 195     4526   4696   4226    122   -320    786  A    C  
ATOM   1503  O   PRO A 195      36.066 -33.436 -32.223  1.00 31.14      A    O  
ANISOU 1503  O   PRO A 195     3819   4337   3677     87   -302    990  A    O  
ATOM   1504  CB  PRO A 195      37.591 -34.037 -29.501  1.00 34.81      A    C  
ANISOU 1504  CB  PRO A 195     4245   4806   4176    -34   -399    930  A    C  
ATOM   1505  CG  PRO A 195      37.631 -35.241 -28.619  1.00 35.61      A    C  
ANISOU 1505  CG  PRO A 195     4518   4850   4162    167   -358    764  A    C  
ATOM   1506  CD  PRO A 195      36.303 -35.324 -27.934  1.00 29.47      A    C  
ANISOU 1506  CD  PRO A 195     3983   3698   3518     91   -362    575  A    C  
ATOM   1507  N   GLN A 196      35.340 -35.458 -31.529  1.00 29.49      A    N  
ANISOU 1507  N   GLN A 196     3969   3847   3388    356   -308    583  A    N  
ATOM   1508  CA  GLN A 196      35.064 -35.932 -32.886  1.00 30.44      A    C  
ANISOU 1508  CA  GLN A 196     4135   4077   3353    638   -319    510  A    C  
ATOM   1509  C   GLN A 196      33.700 -35.461 -33.407  1.00 32.99      A    C  
ANISOU 1509  C   GLN A 196     4545   4171   3816    527   -370    381  A    C  
ATOM   1510  O   GLN A 196      33.380 -35.624 -34.594  1.00 31.04      A    O  
ANISOU 1510  O   GLN A 196     4322   4034   3438    764   -410    306  A    O  
ATOM   1511  CB  GLN A 196      35.149 -37.465 -32.951  1.00 36.38      A    C  
ANISOU 1511  CB  GLN A 196     5095   4750   3980    960   -385    303  A    C  
ATOM   1512  CG  GLN A 196      33.980 -38.218 -32.305  1.00 31.09      A    C  
ANISOU 1512  CG  GLN A 196     4660   3595   3556    822   -477     85  A    C  
ATOM   1513  CD  GLN A 196      34.194 -38.513 -30.830  1.00 32.59      A    C  
ANISOU 1513  CD  GLN A 196     4886   3643   3855    669   -413    154  A    C  
ATOM   1514  NE2 GLN A 196      34.021 -39.777 -30.447  1.00 28.03      A    N  
ANISOU 1514  NE2 GLN A 196     4507   2808   3336    786   -476     61  A    N  
ATOM   1515  OE1 GLN A 196      34.507 -37.617 -30.042  1.00 29.37      A    O  
ANISOU 1515  OE1 GLN A 196     4342   3338   3479    473   -336    288  A    O  
ATOM   1516  N   ILE A 197      32.902 -34.869 -32.530  1.00 25.29      A    N  
ANISOU 1516  N   ILE A 197     3615   2930   3065    230   -379    347  A    N  
ATOM   1517  CA  ILE A 197      31.571 -34.391 -32.901  1.00 24.76      A    C  
ANISOU 1517  CA  ILE A 197     3605   2686   3116    139   -421    239  A    C  
ATOM   1518  C   ILE A 197      31.626 -32.904 -33.179  1.00 29.34      A    C  
ANISOU 1518  C   ILE A 197     4080   3345   3723      1   -400    416  A    C  
ATOM   1519  O   ILE A 197      32.272 -32.155 -32.440  1.00 26.50      A    O  
ANISOU 1519  O   ILE A 197     3655   2977   3436   -175   -408    561  A    O  
ATOM   1520  CB  ILE A 197      30.526 -34.655 -31.788  1.00 25.33      A    C  
ANISOU 1520  CB  ILE A 197     3771   2472   3380    -31   -434    130  A    C  
ATOM   1521  CG1 ILE A 197      30.290 -36.150 -31.596  1.00 28.00      A    C  
ANISOU 1521  CG1 ILE A 197     4213   2644   3781     53   -482     12  A    C  
ATOM   1522  CG2 ILE A 197      29.184 -33.921 -32.077  1.00 22.25      A    C  
ANISOU 1522  CG2 ILE A 197     3380   1988   3087   -121   -462     65  A    C  
ATOM   1523  CD1 ILE A 197      29.748 -36.839 -32.821  1.00 32.10      A    C  
ANISOU 1523  CD1 ILE A 197     4797   3099   4300    213   -629   -174  A    C  
ATOM   1524  N   ALA A 198      30.981 -32.483 -34.265  1.00 26.90      A    N  
ANISOU 1524  N   ALA A 198     3763   3091   3364     98   -410    403  A    N  
ATOM   1525  CA  ALA A 198      30.803 -31.066 -34.544  1.00 24.92      A    C  
ANISOU 1525  CA  ALA A 198     3462   2834   3172    -26   -406    577  A    C  
ATOM   1526  C   ALA A 198      29.482 -30.619 -33.928  1.00 22.80      A    C  
ANISOU 1526  C   ALA A 198     3323   2302   3037   -143   -462    404  A    C  
ATOM   1527  O   ALA A 198      28.413 -30.865 -34.490  1.00 24.74      A    O  
ANISOU 1527  O   ALA A 198     3608   2534   3257    -36   -482    246  A    O  
ATOM   1528  CB  ALA A 198      30.824 -30.787 -36.058  1.00 26.55      A    C  
ANISOU 1528  CB  ALA A 198     3582   3302   3202    211   -359    706  A    C  
ATOM   1529  N   PHE A 199      29.558 -29.989 -32.757  1.00 23.17      A    N  
ANISOU 1529  N   PHE A 199     3425   2179   3199   -317   -509    421  A    N  
ATOM   1530  CA  PHE A 199      28.362 -29.532 -32.061  1.00 24.07      A    C  
ANISOU 1530  CA  PHE A 199     3653   2125   3366   -334   -552    278  A    C  
ATOM   1531  C   PHE A 199      27.892 -28.185 -32.587  1.00 20.81      A    C  
ANISOU 1531  C   PHE A 199     3305   1635   2967   -326   -619    342  A    C  
ATOM   1532  O   PHE A 199      28.701 -27.296 -32.856  1.00 28.81      A    O  
ANISOU 1532  O   PHE A 199     4305   2596   4045   -423   -684    540  A    O  
ATOM   1533  CB  PHE A 199      28.616 -29.408 -30.547  1.00 22.26      A    C  
ANISOU 1533  CB  PHE A 199     3494   1786   3177   -395   -605    234  A    C  
ATOM   1534  CG  PHE A 199      28.669 -30.717 -29.829  1.00 23.45      A    C  
ANISOU 1534  CG  PHE A 199     3614   1986   3308   -360   -517    178  A    C  
ATOM   1535  CD1 PHE A 199      27.505 -31.347 -29.416  1.00 27.25      A    C  
ANISOU 1535  CD1 PHE A 199     4090   2458   3805   -304   -450    108  A    C  
ATOM   1536  CD2 PHE A 199      29.890 -31.313 -29.547  1.00 24.33      A    C  
ANISOU 1536  CD2 PHE A 199     3680   2166   3400   -382   -504    242  A    C  
ATOM   1537  CE1 PHE A 199      27.554 -32.570 -28.747  1.00 30.24      A    C  
ANISOU 1537  CE1 PHE A 199     4436   2838   4216   -295   -373    133  A    C  
ATOM   1538  CE2 PHE A 199      29.944 -32.532 -28.881  1.00 23.52      A    C  
ANISOU 1538  CE2 PHE A 199     3582   2076   3279   -321   -426    214  A    C  
ATOM   1539  CZ  PHE A 199      28.772 -33.158 -28.477  1.00 25.25      A    C  
ANISOU 1539  CZ  PHE A 199     3815   2227   3550   -291   -363    174  A    C  
ATOM   1540  N   GLN A 200      26.580 -28.037 -32.713  1.00 21.39      A    N  
ANISOU 1540  N   GLN A 200     3429   1699   2999   -216   -614    208  A    N  
ATOM   1541  CA  GLN A 200      25.967 -26.735 -32.936  1.00 24.79      A    C  
ANISOU 1541  CA  GLN A 200     3978   2026   3415   -150   -693    229  A    C  
ATOM   1542  C   GLN A 200      25.257 -26.319 -31.659  1.00 24.97      A    C  
ANISOU 1542  C   GLN A 200     4131   1944   3413    -74   -767     87  A    C  
ATOM   1543  O   GLN A 200      24.484 -27.094 -31.097  1.00 26.34      A    O  
ANISOU 1543  O   GLN A 200     4230   2243   3536     -2   -684    -14  A    O  
ATOM   1544  CB  GLN A 200      24.975 -26.787 -34.094  1.00 22.62      A    C  
ANISOU 1544  CB  GLN A 200     3653   1900   3042     12   -642    180  A    C  
ATOM   1545  CG  GLN A 200      25.565 -27.411 -35.348  1.00 22.17      A    C  
ANISOU 1545  CG  GLN A 200     3471   2032   2921     69   -577    264  A    C  
ATOM   1546  CD  GLN A 200      24.527 -27.616 -36.431  1.00 22.57      A    C  
ANISOU 1546  CD  GLN A 200     3476   2250   2849    284   -578    135  A    C  
ATOM   1547  NE2 GLN A 200      24.831 -28.489 -37.386  1.00 27.33      A    N  
ANISOU 1547  NE2 GLN A 200     3990   3040   3352    427   -573     86  A    N  
ATOM   1548  OE1 GLN A 200      23.468 -26.999 -36.412  1.00 27.70      A    O  
ANISOU 1548  OE1 GLN A 200     4174   2885   3467    369   -610     59  A    O  
ATOM   1549  N   SER A 201      25.543 -25.114 -31.184  1.00 27.55      A    N  
ANISOU 1549  N   SER A 201     4646   2044   3777    -66   -944    100  A    N  
ATOM   1550  CA  SER A 201      24.831 -24.558 -30.049  1.00 33.28      A    C  
ANISOU 1550  CA  SER A 201     5548   2700   4396    143  -1058    -72  A    C  
ATOM   1551  C   SER A 201      23.541 -23.927 -30.534  1.00 40.32      A    C  
ANISOU 1551  C   SER A 201     6512   3654   5154    381  -1051   -132  A    C  
ATOM   1552  O   SER A 201      23.477 -23.384 -31.645  1.00 36.66      A    O  
ANISOU 1552  O   SER A 201     6073   3129   4727    360  -1061    -32  A    O  
ATOM   1553  CB  SER A 201      25.687 -23.519 -29.321  1.00 32.63      A    C  
ANISOU 1553  CB  SER A 201     5692   2292   4415    101  -1353   -105  A    C  
ATOM   1554  OG  SER A 201      26.034 -22.459 -30.198  1.00 32.63      A    O  
ANISOU 1554  OG  SER A 201     5738   2111   4550    -20  -1465     45  A    O  
ATOM   1555  N   SER A 202      22.506 -24.002 -29.707  1.00 29.73      A    N  
ANISOU 1555  N   SER A 202     5179   2489   3627    649  -1016   -259  A    N  
ATOM   1556  CA  SER A 202      21.240 -23.373 -30.037  1.00 30.92      A    C  
ANISOU 1556  CA  SER A 202     5379   2765   3605    938  -1015   -318  A    C  
ATOM   1557  C   SER A 202      20.516 -22.919 -28.783  1.00 36.78      A    C  
ANISOU 1557  C   SER A 202     6250   3630   4095   1334  -1087   -451  A    C  
ATOM   1558  O   SER A 202      20.452 -23.662 -27.796  1.00 33.01      A    O  
ANISOU 1558  O   SER A 202     5636   3367   3538   1397   -981   -440  A    O  
ATOM   1559  CB  SER A 202      20.342 -24.328 -30.843  1.00 32.90      A    C  
ANISOU 1559  CB  SER A 202     5313   3341   3849    891   -806   -268  A    C  
ATOM   1560  OG  SER A 202      19.150 -23.657 -31.242  1.00 41.19      A    O  
ANISOU 1560  OG  SER A 202     6380   4550   4722   1178   -818   -317  A    O  
ATOM   1561  N   GLY A 203      20.003 -21.693 -28.820  1.00 34.15      A    N  
ANISOU 1561  N   GLY A 203     4084   3178   5714   -616     66    174  A    N  
ATOM   1562  CA  GLY A 203      19.156 -21.178 -27.759  1.00 36.87      A    C  
ANISOU 1562  CA  GLY A 203     4464   3607   5939   -468    282    530  A    C  
ATOM   1563  C   GLY A 203      19.881 -20.192 -26.868  1.00 38.50      A    C  
ANISOU 1563  C   GLY A 203     5019   3955   5656   -262    324    609  A    C  
ATOM   1564  O   GLY A 203      20.966 -20.477 -26.354  1.00 31.69      A    O  
ANISOU 1564  O   GLY A 203     4294   3044   4701   -219    289    607  A    O  
ATOM   1565  N   GLY A 204      19.288 -19.017 -26.696  1.00 33.67      A    N  
ANISOU 1565  N   GLY A 204     4543   3512   4739   -121    372    650  A    N  
ATOM   1566  CA  GLY A 204      19.788 -18.054 -25.737  1.00 28.37      A    C  
ANISOU 1566  CA  GLY A 204     4202   2931   3646    109    378    680  A    C  
ATOM   1567  C   GLY A 204      20.607 -16.874 -26.240  1.00 28.71      A    C  
ANISOU 1567  C   GLY A 204     4477   2983   3450     63    184    402  A    C  
ATOM   1568  O   GLY A 204      20.850 -15.951 -25.471  1.00 29.41      A    O  
ANISOU 1568  O   GLY A 204     4831   3096   3246    247    145    370  A    O  
ATOM   1569  N   ILE A 205      21.064 -16.893 -27.492  1.00 29.11      A    N  
ANISOU 1569  N   ILE A 205     4416   3010   3635   -150     56    209  A    N  
ATOM   1570  CA  ILE A 205      21.910 -15.795 -27.961  1.00 26.36      A    C  
ANISOU 1570  CA  ILE A 205     4224   2653   3140   -193    -87     54  A    C  
ATOM   1571  C   ILE A 205      21.133 -14.484 -27.895  1.00 31.83      A    C  
ANISOU 1571  C   ILE A 205     5068   3370   3654    -49    -27     85  A    C  
ATOM   1572  O   ILE A 205      20.053 -14.366 -28.480  1.00 29.21      A    O  
ANISOU 1572  O   ILE A 205     4604   3150   3346     -9     84    152  A    O  
ATOM   1573  CB  ILE A 205      22.420 -16.023 -29.405  1.00 25.68      A    C  
ANISOU 1573  CB  ILE A 205     3947   2624   3186   -351   -175    -73  A    C  
ATOM   1574  CG1 ILE A 205      23.362 -17.239 -29.468  1.00 25.14      A    C  
ANISOU 1574  CG1 ILE A 205     3777   2510   3267   -446   -250   -134  A    C  
ATOM   1575  CG2 ILE A 205      23.152 -14.782 -29.890  1.00 27.45      A    C  
ANISOU 1575  CG2 ILE A 205     4270   2841   3319   -370   -256   -100  A    C  
ATOM   1576  CD1 ILE A 205      24.558 -17.160 -28.517  1.00 28.90      A    C  
ANISOU 1576  CD1 ILE A 205     4416   2913   3653   -440   -333   -108  A    C  
ATOM   1577  N   GLY A 206      21.677 -13.506 -27.174  1.00 27.25      A    N  
ANISOU 1577  N   GLY A 206     4759   2681   2914     46   -122     15  A    N  
ATOM   1578  CA  GLY A 206      20.999 -12.235 -26.994  1.00 32.73      A    C  
ANISOU 1578  CA  GLY A 206     5649   3330   3457    226    -78     15  A    C  
ATOM   1579  C   GLY A 206      21.702 -11.024 -27.593  1.00 33.29      A    C  
ANISOU 1579  C   GLY A 206     5816   3213   3618    129   -206    -86  A    C  
ATOM   1580  O   GLY A 206      21.058 -10.058 -28.001  1.00 34.56      A    O  
ANISOU 1580  O   GLY A 206     6040   3332   3757    232   -119    -33  A    O  
ATOM   1581  N   ASP A 207      23.028 -11.055 -27.616  1.00 34.59      A    N  
ANISOU 1581  N   ASP A 207     5967   3255   3919    -57   -398   -185  A    N  
ATOM   1582  CA  ASP A 207      23.804  -9.936 -28.152  1.00 36.85      A    C  
ANISOU 1582  CA  ASP A 207     6274   3318   4409   -185   -518   -209  A    C  
ATOM   1583  C   ASP A 207      25.153 -10.441 -28.629  1.00 32.73      A    C  
ANISOU 1583  C   ASP A 207     5546   2811   4079   -424   -646   -189  A    C  
ATOM   1584  O   ASP A 207      25.450 -11.633 -28.492  1.00 32.45      A    O  
ANISOU 1584  O   ASP A 207     5404   2943   3983   -461   -648   -200  A    O  
ATOM   1585  CB  ASP A 207      23.974  -8.816 -27.116  1.00 45.37      A    C  
ANISOU 1585  CB  ASP A 207     7671   4098   5471    -76   -700   -405  A    C  
ATOM   1586  CG  ASP A 207      24.594  -9.293 -25.803  1.00 52.65      A    C  
ANISOU 1586  CG  ASP A 207     8740   5031   6234     -8   -915   -621  A    C  
ATOM   1587  OD1 ASP A 207      25.518 -10.136 -25.820  1.00 47.57      A    O  
ANISOU 1587  OD1 ASP A 207     7931   4489   5655   -173  -1005   -611  A    O  
ATOM   1588  OD2 ASP A 207      24.164  -8.793 -24.740  1.00 58.76      A    O1-
ANISOU 1588  OD2 ASP A 207     9802   5745   6780    268   -995   -802  A    O1-
ATOM   1589  N   ILE A 208      25.969  -9.542 -29.174  1.00 30.73      A    N  
ANISOU 1589  N   ILE A 208     5217   2371   4090   -569   -734   -119  A    N  
ATOM   1590  CA  ILE A 208      27.239  -9.936 -29.781  1.00 34.82      A    C  
ANISOU 1590  CA  ILE A 208     5476   2955   4801   -762   -812     -8  A    C  
ATOM   1591  C   ILE A 208      28.182 -10.527 -28.739  1.00 38.00      A    C  
ANISOU 1591  C   ILE A 208     5930   3330   5178   -846  -1044   -182  A    C  
ATOM   1592  O   ILE A 208      28.953 -11.449 -29.038  1.00 36.13      A    O  
ANISOU 1592  O   ILE A 208     5501   3280   4948   -919  -1053   -112  A    O  
ATOM   1593  CB  ILE A 208      27.907  -8.749 -30.508  1.00 39.42      A    C  
ANISOU 1593  CB  ILE A 208     5912   3319   5748   -891   -831    200  A    C  
ATOM   1594  CG1 ILE A 208      27.341  -8.622 -31.914  1.00 44.38      A    C  
ANISOU 1594  CG1 ILE A 208     6334   4183   6346   -764   -550    489  A    C  
ATOM   1595  CG2 ILE A 208      29.402  -8.948 -30.649  1.00 47.90      A    C  
ANISOU 1595  CG2 ILE A 208     6744   4383   7071  -1101   -988    303  A    C  
ATOM   1596  CD1 ILE A 208      27.632  -9.823 -32.782  1.00 38.60      A    C  
ANISOU 1596  CD1 ILE A 208     5350   3869   5448   -711   -459    571  A    C  
ATOM   1597  N   ASP A 209      28.099 -10.030 -27.508  1.00 35.39      A    N  
ANISOU 1597  N   ASP A 209     5863   2810   4772   -776  -1232   -420  A    N  
ATOM   1598  CA  ASP A 209      28.924 -10.577 -26.429  1.00 35.38      A    C  
ANISOU 1598  CA  ASP A 209     5915   2861   4667   -776  -1464   -602  A    C  
ATOM   1599  C   ASP A 209      28.645 -12.061 -26.171  1.00 33.26      A    C  
ANISOU 1599  C   ASP A 209     5604   2902   4132   -644  -1302   -535  A    C  
ATOM   1600  O   ASP A 209      29.552 -12.799 -25.766  1.00 32.74      A    O  
ANISOU 1600  O   ASP A 209     5449   2958   4034   -677  -1411   -547  A    O  
ATOM   1601  CB  ASP A 209      28.725  -9.786 -25.132  1.00 37.38      A    C  
ANISOU 1601  CB  ASP A 209     6485   2931   4788   -607  -1704   -922  A    C  
ATOM   1602  CG  ASP A 209      29.328  -8.398 -25.195  1.00 53.32      A    C  
ANISOU 1602  CG  ASP A 209     8454   4630   7174   -753  -1898  -1020  A    C  
ATOM   1603  OD1 ASP A 209      30.288  -8.195 -25.969  1.00 55.87      A    O  
ANISOU 1603  OD1 ASP A 209     8478   4889   7863  -1019  -1924   -838  A    O  
ATOM   1604  OD2 ASP A 209      28.848  -7.514 -24.458  1.00 58.59      A    O1-
ANISOU 1604  OD2 ASP A 209     9347   5142   7771   -568  -1989  -1246  A    O1-
ATOM   1605  N   ASP A 210      27.403 -12.497 -26.393  1.00 29.53      A    N  
ANISOU 1605  N   ASP A 210     5169   2537   3514   -498  -1047   -444  A    N  
ATOM   1606  CA  ASP A 210      27.035 -13.907 -26.218  1.00 34.89      A    C  
ANISOU 1606  CA  ASP A 210     5764   3416   4076   -405   -880   -345  A    C  
ATOM   1607  C   ASP A 210      27.690 -14.805 -27.259  1.00 35.56      A    C  
ANISOU 1607  C   ASP A 210     5587   3599   4325   -561   -833   -248  A    C  
ATOM   1608  O   ASP A 210      27.976 -15.967 -26.996  1.00 35.02      A    O  
ANISOU 1608  O   ASP A 210     5444   3619   4242   -526   -790   -205  A    O  
ATOM   1609  CB  ASP A 210      25.517 -14.106 -26.292  1.00 35.95      A    C  
ANISOU 1609  CB  ASP A 210     5927   3609   4122   -254   -642   -253  A    C  
ATOM   1610  CG  ASP A 210      24.782 -13.446 -25.154  1.00 37.19      A    C  
ANISOU 1610  CG  ASP A 210     6344   3748   4037     11   -634   -304  A    C  
ATOM   1611  OD1 ASP A 210      25.360 -13.316 -24.051  1.00 32.10      A    O  
ANISOU 1611  OD1 ASP A 210     5861   3115   3221    153   -797   -427  A    O  
ATOM   1612  OD2 ASP A 210      23.614 -13.048 -25.365  1.00 34.99      A    O1-
ANISOU 1612  OD2 ASP A 210     6102   3485   3706    125   -473   -229  A    O1-
ATOM   1613  N   ILE A 211      27.901 -14.272 -28.454  1.00 32.25      A    N  
ANISOU 1613  N   ILE A 211     5026   3177   4052   -679   -819   -190  A    N  
ATOM   1614  CA  ILE A 211      28.656 -14.991 -29.465  1.00 31.25      A    C  
ANISOU 1614  CA  ILE A 211     4658   3197   4018   -745   -794   -109  A    C  
ATOM   1615  C   ILE A 211      30.135 -15.060 -29.073  1.00 38.29      A    C  
ANISOU 1615  C   ILE A 211     5478   4092   4977   -840   -968    -80  A    C  
ATOM   1616  O   ILE A 211      30.772 -16.116 -29.183  1.00 32.04      A    O  
ANISOU 1616  O   ILE A 211     4573   3430   4170   -812   -956    -47  A    O  
ATOM   1617  CB  ILE A 211      28.483 -14.330 -30.838  1.00 28.21      A    C  
ANISOU 1617  CB  ILE A 211     4117   2896   3705   -749   -706      3  A    C  
ATOM   1618  CG1 ILE A 211      27.035 -14.528 -31.290  1.00 35.88      A    C  
ANISOU 1618  CG1 ILE A 211     5101   3950   4580   -631   -555    -48  A    C  
ATOM   1619  CG2 ILE A 211      29.472 -14.915 -31.847  1.00 29.12      A    C  
ANISOU 1619  CG2 ILE A 211     3983   3222   3859   -734   -696    109  A    C  
ATOM   1620  CD1 ILE A 211      26.699 -13.862 -32.572  1.00 38.58      A    C  
ANISOU 1620  CD1 ILE A 211     5296   4448   4913   -551   -455     62  A    C  
ATOM   1621  N   ALA A 212      30.679 -13.943 -28.597  1.00 33.64      A    N  
ANISOU 1621  N   ALA A 212     4944   3345   4494   -947  -1149   -105  A    N  
ATOM   1622  CA  ALA A 212      32.076 -13.923 -28.173  1.00 36.39      A    C  
ANISOU 1622  CA  ALA A 212     5174   3703   4949  -1064  -1364    -91  A    C  
ATOM   1623  C   ALA A 212      32.327 -14.967 -27.085  1.00 39.30      A    C  
ANISOU 1623  C   ALA A 212     5633   4197   5104   -939  -1420   -190  A    C  
ATOM   1624  O   ALA A 212      33.354 -15.638 -27.086  1.00 37.74      A    O  
ANISOU 1624  O   ALA A 212     5273   4149   4919   -956  -1473   -107  A    O  
ATOM   1625  CB  ALA A 212      32.469 -12.546 -27.676  1.00 35.79      A    C  
ANISOU 1625  CB  ALA A 212     5152   3363   5086  -1211  -1615   -187  A    C  
ATOM   1626  N   ALA A 213      31.375 -15.101 -26.167  1.00 35.36      A    N  
ANISOU 1626  N   ALA A 213     5372   3668   4396   -767  -1374   -313  A    N  
ATOM   1627  CA  ALA A 213      31.512 -16.029 -25.048  1.00 41.75      A    C  
ANISOU 1627  CA  ALA A 213     6259   4622   4983   -574  -1377   -331  A    C  
ATOM   1628  C   ALA A 213      31.613 -17.493 -25.493  1.00 37.07      A    C  
ANISOU 1628  C   ALA A 213     5521   4148   4418   -520  -1167   -160  A    C  
ATOM   1629  O   ALA A 213      32.125 -18.325 -24.757  1.00 34.20      A    O  
ANISOU 1629  O   ALA A 213     5142   3908   3944   -384  -1165    -97  A    O  
ATOM   1630  CB  ALA A 213      30.348 -15.859 -24.085  1.00 37.34      A    C  
ANISOU 1630  CB  ALA A 213     5946   4049   4192   -333  -1300   -403  A    C  
ATOM   1631  N   LEU A 214      31.141 -17.811 -26.692  1.00 32.13      A    N  
ANISOU 1631  N   LEU A 214     4787   3485   3937   -592  -1005   -103  A    N  
ATOM   1632  CA  LEU A 214      31.209 -19.195 -27.176  1.00 32.60      A    C  
ANISOU 1632  CA  LEU A 214     4725   3589   4071   -527   -854    -25  A    C  
ATOM   1633  C   LEU A 214      32.488 -19.516 -27.950  1.00 36.86      A    C  
ANISOU 1633  C   LEU A 214     5075   4260   4671   -568   -916     36  A    C  
ATOM   1634  O   LEU A 214      32.713 -20.669 -28.319  1.00 37.72      A    O  
ANISOU 1634  O   LEU A 214     5106   4399   4829   -470   -819     67  A    O  
ATOM   1635  CB  LEU A 214      29.995 -19.507 -28.066  1.00 30.21      A    C  
ANISOU 1635  CB  LEU A 214     4390   3206   3882   -532   -698    -71  A    C  
ATOM   1636  CG  LEU A 214      28.663 -19.720 -27.336  1.00 28.40      A    C  
ANISOU 1636  CG  LEU A 214     4264   2870   3657   -451   -562    -40  A    C  
ATOM   1637  CD1 LEU A 214      27.506 -19.772 -28.334  1.00 29.94      A    C  
ANISOU 1637  CD1 LEU A 214     4371   3018   3988   -500   -476   -114  A    C  
ATOM   1638  CD2 LEU A 214      28.679 -20.988 -26.458  1.00 30.87      A    C  
ANISOU 1638  CD2 LEU A 214     4562   3132   4036   -318   -440    104  A    C  
ATOM   1639  N   ARG A 215      33.331 -18.516 -28.192  1.00 36.18      A    N  
ANISOU 1639  N   ARG A 215     4720   3625   5403   -904  -1432    417  A    N  
ATOM   1640  CA  ARG A 215      34.466 -18.694 -29.103  1.00 41.42      A    C  
ANISOU 1640  CA  ARG A 215     4995   4394   6350   -800  -1382    588  A    C  
ATOM   1641  C   ARG A 215      35.483 -19.758 -28.678  1.00 44.66      A    C  
ANISOU 1641  C   ARG A 215     5145   4853   6970   -708  -1545    805  A    C  
ATOM   1642  O   ARG A 215      36.067 -20.434 -29.522  1.00 53.47      A    O  
ANISOU 1642  O   ARG A 215     5964   6042   8310   -465  -1394    866  A    O  
ATOM   1643  CB  ARG A 215      35.198 -17.366 -29.300  1.00 42.86      A    C  
ANISOU 1643  CB  ARG A 215     5064   4623   6600  -1024  -1487    695  A    C  
ATOM   1644  CG  ARG A 215      34.614 -16.495 -30.382  1.00 39.18      A    C  
ANISOU 1644  CG  ARG A 215     4656   4141   6092  -1005  -1259    590  A    C  
ATOM   1645  CD  ARG A 215      35.591 -15.386 -30.766  1.00 45.81      A    C  
ANISOU 1645  CD  ARG A 215     5288   5039   7078  -1232  -1368    795  A    C  
ATOM   1646  NE  ARG A 215      36.013 -14.602 -29.609  1.00 52.52      A    N  
ANISOU 1646  NE  ARG A 215     6291   5765   7901  -1550  -1727    843  A    N  
ATOM   1647  CZ  ARG A 215      35.872 -13.283 -29.504  1.00 57.45      A    C  
ANISOU 1647  CZ  ARG A 215     7145   6269   8415  -1676  -1773    781  A    C  
ATOM   1648  NH1 ARG A 215      35.321 -12.594 -30.494  1.00 52.32      A    N1+
ANISOU 1648  NH1 ARG A 215     6544   5553   7783  -1638  -1595    743  A    N1+
ATOM   1649  NH2 ARG A 215      36.294 -12.650 -28.412  1.00 56.02      A    N  
ANISOU 1649  NH2 ARG A 215     7142   6028   8116  -1831  -2006    770  A    N  
ATOM   1650  N   GLY A 216      35.703 -19.915 -27.382  1.00 36.57      A    N  
ANISOU 1650  N   GLY A 216     4228   3799   5867   -880  -1852    919  A    N  
ATOM   1651  CA  GLY A 216      36.717 -20.859 -26.937  1.00 43.71      A    C  
ANISOU 1651  CA  GLY A 216     4862   4745   7002   -795  -2060   1183  A    C  
ATOM   1652  C   GLY A 216      36.184 -22.234 -26.608  1.00 42.96      A    C  
ANISOU 1652  C   GLY A 216     4893   4512   6918   -608  -2056   1187  A    C  
ATOM   1653  O   GLY A 216      36.928 -23.106 -26.159  1.00 44.71      A    O  
ANISOU 1653  O   GLY A 216     4929   4711   7349   -511  -2259   1423  A    O  
ATOM   1654  N   THR A 217      34.891 -22.433 -26.828  1.00 38.30      A    N  
ANISOU 1654  N   THR A 217     4606   3820   6128   -567  -1849    956  A    N  
ATOM   1655  CA  THR A 217      34.219 -23.633 -26.339  1.00 38.43      A    C  
ANISOU 1655  CA  THR A 217     4808   3689   6103   -502  -1893    985  A    C  
ATOM   1656  C   THR A 217      34.440 -24.865 -27.212  1.00 40.38      A    C  
ANISOU 1656  C   THR A 217     4898   3776   6666   -161  -1763    980  A    C  
ATOM   1657  O   THR A 217      34.308 -25.981 -26.733  1.00 36.38      A    O  
ANISOU 1657  O   THR A 217     4477   3093   6254    -99  -1902   1104  A    O  
ATOM   1658  CB  THR A 217      32.699 -23.414 -26.202  1.00 39.47      A    C  
ANISOU 1658  CB  THR A 217     5289   3806   5902   -617  -1730    767  A    C  
ATOM   1659  CG2 THR A 217      32.423 -22.266 -25.252  1.00 43.10      A    C  
ANISOU 1659  CG2 THR A 217     5946   4396   6032   -899  -1841    718  A    C  
ATOM   1660  OG1 THR A 217      32.125 -23.115 -27.485  1.00 33.18      A    O  
ANISOU 1660  OG1 THR A 217     4475   3003   5127   -468  -1414    530  A    O  
ATOM   1661  N   GLY A 218      34.770 -24.669 -28.486  1.00 34.97      A    N  
ANISOU 1661  N   GLY A 218     4009   3146   6133     55  -1505    835  A    N  
ATOM   1662  CA  GLY A 218      34.945 -25.797 -29.387  1.00 39.38      A    C  
ANISOU 1662  CA  GLY A 218     4463   3552   6947    408  -1347    743  A    C  
ATOM   1663  C   GLY A 218      33.687 -26.091 -30.190  1.00 36.14      A    C  
ANISOU 1663  C   GLY A 218     4321   3036   6376    452  -1104    451  A    C  
ATOM   1664  O   GLY A 218      33.638 -27.042 -30.970  1.00 41.25      A    O  
ANISOU 1664  O   GLY A 218     4976   3517   7179    713   -978    303  A    O  
ATOM   1665  N   VAL A 219      32.666 -25.269 -29.990  1.00 30.29      A    N  
ANISOU 1665  N   VAL A 219     3799   2386   5325    200  -1054    358  A    N  
ATOM   1666  CA  VAL A 219      31.433 -25.344 -30.773  1.00 32.45      A    C  
ANISOU 1666  CA  VAL A 219     4273   2629   5426    201   -841    115  A    C  
ATOM   1667  C   VAL A 219      31.738 -25.060 -32.245  1.00 35.68      A    C  
ANISOU 1667  C   VAL A 219     4521   3156   5880    400   -574    -64  A    C  
ATOM   1668  O   VAL A 219      32.517 -24.162 -32.550  1.00 32.15      A    O  
ANISOU 1668  O   VAL A 219     3853   2904   5458    399   -516      3  A    O  
ATOM   1669  CB  VAL A 219      30.388 -24.352 -30.227  1.00 41.79      A    C  
ANISOU 1669  CB  VAL A 219     5649   3935   6295    -65   -834     78  A    C  
ATOM   1670  CG1 VAL A 219      29.386 -23.976 -31.283  1.00 50.57      A    C  
ANISOU 1670  CG1 VAL A 219     6837   5117   7261    -43   -598   -137  A    C  
ATOM   1671  CG2 VAL A 219      29.688 -24.942 -29.021  1.00 37.24      A    C  
ANISOU 1671  CG2 VAL A 219     5281   3276   5591   -243  -1006    191  A    C  
ATOM   1672  N   ARG A 220      31.159 -25.842 -33.154  1.00 34.38      A    N  
ANISOU 1672  N   ARG A 220     4468   2887   5709    544   -427   -276  A    N  
ATOM   1673  CA  ARG A 220      31.472 -25.694 -34.579  1.00 32.54      A    C  
ANISOU 1673  CA  ARG A 220     4101   2803   5460    740   -165   -461  A    C  
ATOM   1674  C   ARG A 220      30.429 -24.852 -35.307  1.00 36.92      A    C  
ANISOU 1674  C   ARG A 220     4773   3527   5728    589    -18   -585  A    C  
ATOM   1675  O   ARG A 220      30.699 -24.302 -36.378  1.00 45.50      A    O  
ANISOU 1675  O   ARG A 220     5730   4830   6726    662    178   -653  A    O  
ATOM   1676  CB  ARG A 220      31.608 -27.066 -35.239  1.00 33.39      A    C  
ANISOU 1676  CB  ARG A 220     4270   2694   5721   1021    -98   -664  A    C  
ATOM   1677  CG  ARG A 220      32.965 -27.738 -35.034  1.00 46.17      A    C  
ANISOU 1677  CG  ARG A 220     5645   4222   7675   1318   -141   -572  A    C  
ATOM   1678  CD  ARG A 220      33.880 -27.499 -36.233  1.00 63.16      A    C  
ANISOU 1678  CD  ARG A 220     7505   6646   9846   1594    154   -700  A    C  
ATOM   1679  NE  ARG A 220      34.797 -28.615 -36.459  1.00 83.26      A    N  
ANISOU 1679  NE  ARG A 220     9915   9037  12682   1999    201   -783  A    N  
ATOM   1680  CZ  ARG A 220      34.615 -29.563 -37.378  1.00 91.49      A    C  
ANISOU 1680  CZ  ARG A 220    11175  10003  13584   2190    368  -1048  A    C  
ATOM   1681  NH1 ARG A 220      33.550 -29.530 -38.172  1.00 90.55      A    N1+
ANISOU 1681  NH1 ARG A 220    11347   9901  13155   2042    478  -1279  A    N1+
ATOM   1682  NH2 ARG A 220      35.502 -30.543 -37.509  1.00 95.93      A    N  
ANISOU 1682  NH2 ARG A 220    11665  10465  14318   2525    416  -1065  A    N  
ATOM   1683  N   GLY A 221      29.244 -24.737 -34.724  1.00 32.34      A    N  
ANISOU 1683  N   GLY A 221     4412   2879   4998    381   -113   -581  A    N  
ATOM   1684  CA  GLY A 221      28.219 -23.877 -35.287  1.00 33.20      A    C  
ANISOU 1684  CA  GLY A 221     4596   3148   4871    256     -7   -654  A    C  
ATOM   1685  C   GLY A 221      27.403 -23.200 -34.211  1.00 31.14      A    C  
ANISOU 1685  C   GLY A 221     4445   2895   4492     48   -116   -554  A    C  
ATOM   1686  O   GLY A 221      27.054 -23.813 -33.211  1.00 34.70      A    O  
ANISOU 1686  O   GLY A 221     5007   3226   4951    -42   -250   -492  A    O  
ATOM   1687  N   VAL A 222      27.094 -21.923 -34.413  1.00 21.90      A    N  
ANISOU 1687  N   VAL A 222     3247   1869   3206    -19    -54   -534  A    N  
ATOM   1688  CA  VAL A 222      26.275 -21.176 -33.467  1.00 23.26      A    C  
ANISOU 1688  CA  VAL A 222     3530   2056   3253   -155   -115   -499  A    C  
ATOM   1689  C   VAL A 222      24.938 -20.807 -34.101  1.00 32.88      A    C  
ANISOU 1689  C   VAL A 222     4795   3378   4321   -168     -9   -580  A    C  
ATOM   1690  O   VAL A 222      24.880 -19.952 -34.993  1.00 28.62      A    O  
ANISOU 1690  O   VAL A 222     4193   2929   3754   -127     72   -581  A    O  
ATOM   1691  CB  VAL A 222      26.983 -19.890 -33.004  1.00 27.24      A    C  
ANISOU 1691  CB  VAL A 222     3994   2573   3784   -211   -176   -415  A    C  
ATOM   1692  CG1 VAL A 222      26.112 -19.136 -32.006  1.00 25.99      A    C  
ANISOU 1692  CG1 VAL A 222     3992   2408   3476   -303   -218   -453  A    C  
ATOM   1693  CG2 VAL A 222      28.336 -20.228 -32.397  1.00 29.05      A    C  
ANISOU 1693  CG2 VAL A 222     4124   2744   4168   -224   -316   -296  A    C  
ATOM   1694  N   ILE A 223      23.864 -21.452 -33.660  1.00 23.47      A    N  
ANISOU 1694  N   ILE A 223     3687   2191   3038   -243    -27   -606  A    N  
ATOM   1695  CA  ILE A 223      22.562 -21.161 -34.227  1.00 25.84      A    C  
ANISOU 1695  CA  ILE A 223     3975   2627   3216   -261     52   -648  A    C  
ATOM   1696  C   ILE A 223      21.990 -19.909 -33.595  1.00 33.61      A    C  
ANISOU 1696  C   ILE A 223     4959   3688   4123   -246     88   -629  A    C  
ATOM   1697  O   ILE A 223      22.003 -19.755 -32.372  1.00 26.73      A    O  
ANISOU 1697  O   ILE A 223     4157   2797   3201   -292     51   -618  A    O  
ATOM   1698  CB  ILE A 223      21.605 -22.345 -34.053  1.00 27.53      A    C  
ANISOU 1698  CB  ILE A 223     4236   2845   3377   -379     11   -653  A    C  
ATOM   1699  CG1 ILE A 223      22.199 -23.563 -34.762  1.00 30.38      A    C  
ANISOU 1699  CG1 ILE A 223     4651   3049   3842   -359    -40   -725  A    C  
ATOM   1700  CG2 ILE A 223      20.212 -22.011 -34.601  1.00 32.10      A    C  
ANISOU 1700  CG2 ILE A 223     4742   3618   3837   -419     70   -659  A    C  
ATOM   1701  CD1 ILE A 223      21.205 -24.569 -35.197  1.00 40.07      A    C  
ANISOU 1701  CD1 ILE A 223     5942   4259   5025   -490    -94   -771  A    C  
ATOM   1702  N   VAL A 224      21.524 -18.987 -34.432  1.00 22.67      A    N  
ANISOU 1702  N   VAL A 224     3510   2382   2722   -170    152   -631  A    N  
ATOM   1703  CA  VAL A 224      20.957 -17.735 -33.927  1.00 20.72      A    C  
ANISOU 1703  CA  VAL A 224     3275   2147   2448    -95    185   -638  A    C  
ATOM   1704  C   VAL A 224      19.625 -17.480 -34.611  1.00 25.02      A    C  
ANISOU 1704  C   VAL A 224     3709   2854   2941    -32    249   -616  A    C  
ATOM   1705  O   VAL A 224      19.570 -17.366 -35.853  1.00 26.53      A    O  
ANISOU 1705  O   VAL A 224     3830   3104   3147    -15    243   -561  A    O  
ATOM   1706  CB  VAL A 224      21.897 -16.528 -34.173  1.00 26.89      A    C  
ANISOU 1706  CB  VAL A 224     4089   2788   3339    -47    144   -603  A    C  
ATOM   1707  CG1 VAL A 224      21.307 -15.257 -33.539  1.00 24.49      A    C  
ANISOU 1707  CG1 VAL A 224     3863   2406   3037     54    153   -659  A    C  
ATOM   1708  CG2 VAL A 224      23.302 -16.807 -33.635  1.00 27.06      A    C  
ANISOU 1708  CG2 VAL A 224     4154   2695   3433   -133     53   -582  A    C  
ATOM   1709  N   GLY A 225      18.558 -17.419 -33.821  1.00 25.35      A    N  
ANISOU 1709  N   GLY A 225     3713   3014   2904     -2    310   -641  A    N  
ATOM   1710  CA  GLY A 225      17.236 -17.147 -34.351  1.00 25.25      A    C  
ANISOU 1710  CA  GLY A 225     3532   3194   2867     74    364   -590  A    C  
ATOM   1711  C   GLY A 225      16.782 -15.733 -34.033  1.00 29.69      A    C  
ANISOU 1711  C   GLY A 225     4078   3717   3487    303    427   -623  A    C  
ATOM   1712  O   GLY A 225      16.978 -14.814 -34.826  1.00 26.65      A    O  
ANISOU 1712  O   GLY A 225     3691   3219   3215    410    381   -565  A    O  
ATOM   1713  N   ARG A 226      16.201 -15.569 -32.849  1.00 29.27      A    N  
ANISOU 1713  N   ARG A 226     4025   3748   3348    380    534   -715  A    N  
ATOM   1714  CA  ARG A 226      15.555 -14.336 -32.430  1.00 29.99      A    C  
ANISOU 1714  CA  ARG A 226     4097   3816   3483    654    630   -804  A    C  
ATOM   1715  C   ARG A 226      16.429 -13.077 -32.525  1.00 29.50      A    C  
ANISOU 1715  C   ARG A 226     4243   3396   3572    777    544   -876  A    C  
ATOM   1716  O   ARG A 226      15.951 -12.028 -32.959  1.00 33.78      A    O  
ANISOU 1716  O   ARG A 226     4744   3830   4260   1003    543   -858  A    O  
ATOM   1717  CB  ARG A 226      15.046 -14.508 -30.984  1.00 26.14      A    C  
ANISOU 1717  CB  ARG A 226     3626   3501   2803    691    786   -943  A    C  
ATOM   1718  CG  ARG A 226      14.125 -13.408 -30.519  1.00 32.96      A    C  
ANISOU 1718  CG  ARG A 226     4422   4418   3682   1030    948  -1077  A    C  
ATOM   1719  CD  ARG A 226      13.620 -13.625 -29.082  1.00 34.47      A    C  
ANISOU 1719  CD  ARG A 226     4621   4868   3608   1064   1150  -1231  A    C  
ATOM   1720  NE  ARG A 226      12.766 -12.506 -28.678  1.00 40.66      A    N  
ANISOU 1720  NE  ARG A 226     5338   5661   4451   1402   1314  -1378  A    N  
ATOM   1721  CZ  ARG A 226      11.703 -12.592 -27.881  1.00 40.05      A    C  
ANISOU 1721  CZ  ARG A 226     5072   5907   4238   1479   1537  -1402  A    C  
ATOM   1722  NH1 ARG A 226      11.344 -13.748 -27.330  1.00 40.30      A    N1+
ANISOU 1722  NH1 ARG A 226     4972   6320   4022   1250   1630  -1280  A    N1+
ATOM   1723  NH2 ARG A 226      11.005 -11.498 -27.618  1.00 41.34      A    N  
ANISOU 1723  NH2 ARG A 226     5182   5999   4528   1778   1659  -1536  A    N  
ATOM   1724  N   ALA A 227      17.691 -13.164 -32.109  1.00 26.92      A    N  
ANISOU 1724  N   ALA A 227     4124   2873   3231    619    447   -930  A    N  
ATOM   1725  CA  ALA A 227      18.520 -11.953 -32.030  1.00 28.86      A    C  
ANISOU 1725  CA  ALA A 227     4575   2773   3617    675    337   -991  A    C  
ATOM   1726  C   ALA A 227      18.742 -11.347 -33.416  1.00 27.31      A    C  
ANISOU 1726  C   ALA A 227     4308   2452   3619    695    239   -792  A    C  
ATOM   1727  O   ALA A 227      18.841 -10.133 -33.557  1.00 32.17      A    O  
ANISOU 1727  O   ALA A 227     5032   2792   4399    815    163   -789  A    O  
ATOM   1728  CB  ALA A 227      19.869 -12.251 -31.356  1.00 27.10      A    C  
ANISOU 1728  CB  ALA A 227     4532   2420   3344    452    219  -1035  A    C  
ATOM   1729  N   LEU A 228      18.795 -12.191 -34.443  1.00 25.82      A    N  
ANISOU 1729  N   LEU A 228     3953   2458   3398    569    232   -624  A    N  
ATOM   1730  CA  LEU A 228      18.937 -11.676 -35.803  1.00 26.97      A    C  
ANISOU 1730  CA  LEU A 228     4021   2572   3654    566    154   -412  A    C  
ATOM   1731  C   LEU A 228      17.608 -11.111 -36.300  1.00 32.63      A    C  
ANISOU 1731  C   LEU A 228     4593   3371   4432    783    176   -328  A    C  
ATOM   1732  O   LEU A 228      17.564 -10.056 -36.934  1.00 32.85      A    O  
ANISOU 1732  O   LEU A 228     4634   3228   4620    884     84   -179  A    O  
ATOM   1733  CB  LEU A 228      19.444 -12.774 -36.740  1.00 22.72      A    C  
ANISOU 1733  CB  LEU A 228     3381   2242   3008    376    154   -310  A    C  
ATOM   1734  CG  LEU A 228      20.919 -13.150 -36.600  1.00 25.99      A    C  
ANISOU 1734  CG  LEU A 228     3872   2572   3429    208    118   -317  A    C  
ATOM   1735  CD1 LEU A 228      21.226 -14.386 -37.457  1.00 24.58      A    C  
ANISOU 1735  CD1 LEU A 228     3594   2611   3133    102    163   -292  A    C  
ATOM   1736  CD2 LEU A 228      21.842 -11.972 -36.988  1.00 24.08      A    C  
ANISOU 1736  CD2 LEU A 228     3689   2125   3337    160     18   -168  A    C  
ATOM   1737  N   LEU A 229      16.522 -11.814 -36.002  1.00 30.90      A    N  
ANISOU 1737  N   LEU A 229     4215   3420   4105    844    281   -386  A    N  
ATOM   1738  CA  LEU A 229      15.193 -11.366 -36.401  1.00 34.07      A    C  
ANISOU 1738  CA  LEU A 229     4406   3965   4576   1060    302   -286  A    C  
ATOM   1739  C   LEU A 229      14.817 -10.058 -35.727  1.00 38.18      A    C  
ANISOU 1739  C   LEU A 229     5004   4227   5275   1382    335   -390  A    C  
ATOM   1740  O   LEU A 229      14.156  -9.208 -36.328  1.00 39.36      A    O  
ANISOU 1740  O   LEU A 229     5044   4312   5599   1603    277   -245  A    O  
ATOM   1741  CB  LEU A 229      14.157 -12.442 -36.078  1.00 33.95      A    C  
ANISOU 1741  CB  LEU A 229     4172   4319   4409   1012    409   -315  A    C  
ATOM   1742  CG  LEU A 229      14.319 -13.661 -36.986  1.00 32.50      A    C  
ANISOU 1742  CG  LEU A 229     3921   4341   4085    720    330   -210  A    C  
ATOM   1743  CD1 LEU A 229      13.726 -14.903 -36.340  1.00 35.61      A    C  
ANISOU 1743  CD1 LEU A 229     4215   4981   4335    564    403   -273  A    C  
ATOM   1744  CD2 LEU A 229      13.657 -13.370 -38.342  1.00 33.53      A    C  
ANISOU 1744  CD2 LEU A 229     3867   4629   4245    742    210     20  A    C  
ATOM   1745  N   GLU A 230      15.242  -9.887 -34.478  1.00 35.22      A    N  
ANISOU 1745  N   GLU A 230     4838   3689   4853   1418    413   -648  A    N  
ATOM   1746  CA  GLU A 230      14.912  -8.666 -33.740  1.00 38.07      A    C  
ANISOU 1746  CA  GLU A 230     5338   3771   5355   1742    455   -836  A    C  
ATOM   1747  C   GLU A 230      15.967  -7.563 -33.942  1.00 38.20      A    C  
ANISOU 1747  C   GLU A 230     5651   3288   5575   1708    259   -821  A    C  
ATOM   1748  O   GLU A 230      15.851  -6.476 -33.380  1.00 38.38      A    O  
ANISOU 1748  O   GLU A 230     5786   3050   5748   1829    257   -947  A    O  
ATOM   1749  CB  GLU A 230      14.737  -8.977 -32.246  1.00 40.45      A    C  
ANISOU 1749  CB  GLU A 230     5732   4188   5449   1781    636  -1143  A    C  
ATOM   1750  CG  GLU A 230      13.464  -9.753 -31.903  1.00 48.02      A    C  
ANISOU 1750  CG  GLU A 230     6380   5623   6244   1894    855  -1150  A    C  
ATOM   1751  CD  GLU A 230      13.188  -9.816 -30.399  1.00 57.37      A    C  
ANISOU 1751  CD  GLU A 230     7620   6943   7233   1868   1036  -1390  A    C  
ATOM   1752  OE1 GLU A 230      14.131  -9.625 -29.596  1.00 52.73      A    O  
ANISOU 1752  OE1 GLU A 230     7315   6151   6567   1691    973  -1547  A    O  
ATOM   1753  OE2 GLU A 230      12.025 -10.064 -30.018  1.00 63.23      A    O1-
ANISOU 1753  OE2 GLU A 230     8100   8033   7893   2003   1234  -1393  A    O1-
ATOM   1754  N   GLY A 231      16.994  -7.837 -34.743  1.00 39.49      A    N  
ANISOU 1754  N   GLY A 231     5846   3414   5746   1402    114   -611  A    N  
ATOM   1755  CA  GLY A 231      17.961  -6.806 -35.090  1.00 38.25      A    C  
ANISOU 1755  CA  GLY A 231     5902   2838   5793   1311    -86   -503  A    C  
ATOM   1756  C   GLY A 231      18.949  -6.420 -33.997  1.00 39.84      A    C  
ANISOU 1756  C   GLY A 231     6323   2839   5973   1118   -120   -698  A    C  
ATOM   1757  O   GLY A 231      19.472  -5.310 -33.997  1.00 35.02      A    O  
ANISOU 1757  O   GLY A 231     5845   1925   5534   1051   -236   -643  A    O  
ATOM   1758  N   LYS A 232      19.228  -7.326 -33.063  1.00 36.14      A    N  
ANISOU 1758  N   LYS A 232     5867   2585   5281    990    -29   -886  A    N  
ATOM   1759  CA  LYS A 232      20.208  -7.018 -32.015  1.00 39.05      A    C  
ANISOU 1759  CA  LYS A 232     6389   2846   5602    777    -93  -1022  A    C  
ATOM   1760  C   LYS A 232      21.592  -6.789 -32.629  1.00 35.99      A    C  
ANISOU 1760  C   LYS A 232     6043   2309   5322    498   -282   -803  A    C  
ATOM   1761  O   LYS A 232      22.370  -5.972 -32.146  1.00 35.84      A    O  
ANISOU 1761  O   LYS A 232     6155   2088   5373    361   -399   -831  A    O  
ATOM   1762  CB  LYS A 232      20.266  -8.144 -30.977  1.00 41.59      A    C  
ANISOU 1762  CB  LYS A 232     6684   3459   5658    679      3  -1183  A    C  
ATOM   1763  CG  LYS A 232      18.934  -8.449 -30.302  1.00 36.38      A    C  
ANISOU 1763  CG  LYS A 232     5951   3025   4847    907    211  -1370  A    C  
ATOM   1764  CD  LYS A 232      18.543  -7.351 -29.311  1.00 47.61      A    C  
ANISOU 1764  CD  LYS A 232     7507   4293   6291   1051    268  -1613  A    C  
ATOM   1765  CE  LYS A 232      17.279  -7.725 -28.542  1.00 51.76      A    C  
ANISOU 1765  CE  LYS A 232     7924   5114   6628   1257    514  -1795  A    C  
ATOM   1766  NZ  LYS A 232      16.950  -6.741 -27.459  1.00 58.53      A    N1+
ANISOU 1766  NZ  LYS A 232     8932   5848   7460   1393    604  -2083  A    N1+
ATOM   1767  N   PHE A 233      21.886  -7.525 -33.697  1.00 28.60      A    N  
ANISOU 1767  N   PHE A 233     4990   1490   4385    412   -309   -586  A    N  
ATOM   1768  CA  PHE A 233      23.129  -7.352 -34.446  1.00 37.74      A    C  
ANISOU 1768  CA  PHE A 233     6123   2572   5645    154   -456   -332  A    C  
ATOM   1769  C   PHE A 233      22.920  -7.924 -35.839  1.00 34.79      A    C  
ANISOU 1769  C   PHE A 233     5559   2403   5257    153   -411    -81  A    C  
ATOM   1770  O   PHE A 233      21.895  -8.547 -36.099  1.00 29.76      A    O  
ANISOU 1770  O   PHE A 233     4795   2008   4503    318   -270   -129  A    O  
ATOM   1771  CB  PHE A 233      24.309  -8.046 -33.753  1.00 28.49      A    C  
ANISOU 1771  CB  PHE A 233     4926   1528   4372    -83   -492   -375  A    C  
ATOM   1772  CG  PHE A 233      24.025  -9.475 -33.355  1.00 28.96      A    C  
ANISOU 1772  CG  PHE A 233     4915   1851   4238    -48   -370   -502  A    C  
ATOM   1773  CD1 PHE A 233      24.110 -10.498 -34.279  1.00 21.79      A    C  
ANISOU 1773  CD1 PHE A 233     3825   1181   3275    -78   -285   -367  A    C  
ATOM   1774  CD2 PHE A 233      23.677  -9.786 -32.042  1.00 32.83      A    C  
ANISOU 1774  CD2 PHE A 233     5458   2440   4575     -2   -309   -726  A    C  
ATOM   1775  CE1 PHE A 233      23.844 -11.819 -33.917  1.00 27.72      A    C  
ANISOU 1775  CE1 PHE A 233     4497   2173   3864    -58   -173   -468  A    C  
ATOM   1776  CE2 PHE A 233      23.410 -11.114 -31.668  1.00 29.52      A    C  
ANISOU 1776  CE2 PHE A 233     4969   2266   3983     -3   -214   -787  A    C  
ATOM   1777  CZ  PHE A 233      23.489 -12.119 -32.600  1.00 27.19      A    C  
ANISOU 1777  CZ  PHE A 233     4562   2096   3673    -31   -164   -671  A    C  
ATOM   1778  N   THR A 234      23.888  -7.726 -36.727  1.00 32.87      A    N  
ANISOU 1778  N   THR A 234     5220   2190   5080    -64   -489    202  A    N  
ATOM   1779  CA  THR A 234      23.778  -8.271 -38.075  1.00 29.84      A    C  
ANISOU 1779  CA  THR A 234     4606   2148   4584    -93   -388    430  A    C  
ATOM   1780  C   THR A 234      24.568  -9.559 -38.222  1.00 28.24      A    C  
ANISOU 1780  C   THR A 234     4244   2271   4216   -214   -267    395  A    C  
ATOM   1781  O   THR A 234      25.441  -9.876 -37.414  1.00 26.64      A    O  
ANISOU 1781  O   THR A 234     4067   2016   4038   -321   -301    300  A    O  
ATOM   1782  CB  THR A 234      24.269  -7.259 -39.139  1.00 28.70      A    C  
ANISOU 1782  CB  THR A 234     4426   1912   4567   -242   -512    804  A    C  
ATOM   1783  CG2 THR A 234      23.510  -5.941 -39.017  1.00 39.24      A    C  
ANISOU 1783  CG2 THR A 234     5943   2837   6129    -94   -671    860  A    C  
ATOM   1784  OG1 THR A 234      25.666  -7.009 -38.945  1.00 31.67      A    O  
ANISOU 1784  OG1 THR A 234     4794   2209   5029   -512   -605    926  A    O  
ATOM   1785  N   VAL A 235      24.252 -10.309 -39.264  1.00 28.13      A    N  
ANISOU 1785  N   VAL A 235     4071   2584   4032   -188   -141    465  A    N  
ATOM   1786  CA  VAL A 235      25.019 -11.495 -39.594  1.00 29.54      A    C  
ANISOU 1786  CA  VAL A 235     4110   3042   4072   -259    -16    422  A    C  
ATOM   1787  C   VAL A 235      26.495 -11.135 -39.811  1.00 26.00      A    C  
ANISOU 1787  C   VAL A 235     3555   2613   3711   -447    -47    620  A    C  
ATOM   1788  O   VAL A 235      27.379 -11.821 -39.301  1.00 28.48      A    O  
ANISOU 1788  O   VAL A 235     3795   2981   4047   -488    -17    538  A    O  
ATOM   1789  CB  VAL A 235      24.424 -12.186 -40.828  1.00 28.00      A    C  
ANISOU 1789  CB  VAL A 235     3809   3173   3657   -212    101    450  A    C  
ATOM   1790  CG1 VAL A 235      25.381 -13.211 -41.385  1.00 24.38      A    C  
ANISOU 1790  CG1 VAL A 235     3223   2977   3066   -262    241    409  A    C  
ATOM   1791  CG2 VAL A 235      23.089 -12.833 -40.449  1.00 26.47      A    C  
ANISOU 1791  CG2 VAL A 235     3670   3001   3386    -76    121    246  A    C  
ATOM   1792  N   LYS A 236      26.762 -10.036 -40.519  1.00 25.25      A    N  
ANISOU 1792  N   LYS A 236     3434   2472   3690   -572   -128    916  A    N  
ATOM   1793  CA  LYS A 236      28.137  -9.557 -40.671  1.00 27.57      A    C  
ANISOU 1793  CA  LYS A 236     3595   2789   4089   -805   -180   1162  A    C  
ATOM   1794  C   LYS A 236      28.839  -9.374 -39.322  1.00 33.19      A    C  
ANISOU 1794  C   LYS A 236     4392   3226   4992   -899   -335   1050  A    C  
ATOM   1795  O   LYS A 236      29.981  -9.801 -39.128  1.00 33.77      A    O  
ANISOU 1795  O   LYS A 236     4286   3445   5101  -1017   -318   1106  A    O  
ATOM   1796  CB  LYS A 236      28.162  -8.221 -41.426  1.00 40.00      A    C  
ANISOU 1796  CB  LYS A 236     5189   4249   5761   -967   -313   1533  A    C  
ATOM   1797  CG  LYS A 236      29.181  -8.132 -42.539  1.00 47.41      A    C  
ANISOU 1797  CG  LYS A 236     5864   5547   6601  -1181   -219   1887  A    C  
ATOM   1798  CD  LYS A 236      28.719  -8.889 -43.759  1.00 50.06      A    C  
ANISOU 1798  CD  LYS A 236     6080   6333   6607  -1068      5   1889  A    C  
ATOM   1799  CE  LYS A 236      29.685  -8.722 -44.922  1.00 37.67      A    C  
ANISOU 1799  CE  LYS A 236     4251   5187   4875  -1274    135   2248  A    C  
ATOM   1800  NZ  LYS A 236      29.727  -7.332 -45.415  1.00 45.38      A    N1+
ANISOU 1800  NZ  LYS A 236     5263   6014   5966  -1499    -61   2676  A    N1+
ATOM   1801  N   GLU A 237      28.166  -8.706 -38.395  1.00 32.75      A    N  
ANISOU 1801  N   GLU A 237     4603   2791   5050   -843   -491    894  A    N  
ATOM   1802  CA  GLU A 237      28.770  -8.435 -37.094  1.00 33.61      A    C  
ANISOU 1802  CA  GLU A 237     4849   2635   5285   -960   -671    765  A    C  
ATOM   1803  C   GLU A 237      29.020  -9.729 -36.337  1.00 28.78      A    C  
ANISOU 1803  C   GLU A 237     4168   2209   4559   -884   -582    544  A    C  
ATOM   1804  O   GLU A 237      30.041  -9.884 -35.665  1.00 33.32      A    O  
ANISOU 1804  O   GLU A 237     4681   2776   5203  -1042   -698    570  A    O  
ATOM   1805  CB  GLU A 237      27.880  -7.490 -36.282  1.00 32.63      A    C  
ANISOU 1805  CB  GLU A 237     5034   2147   5218   -833   -785    553  A    C  
ATOM   1806  CG  GLU A 237      27.885  -6.060 -36.830  1.00 37.87      A    C  
ANISOU 1806  CG  GLU A 237     5758   2614   6016   -893   -902    749  A    C  
ATOM   1807  CD  GLU A 237      26.802  -5.180 -36.221  1.00 45.71      A    C  
ANISOU 1807  CD  GLU A 237     7001   3312   7056   -666   -930    520  A    C  
ATOM   1808  OE1 GLU A 237      25.780  -5.723 -35.750  1.00 41.88      A    O  
ANISOU 1808  OE1 GLU A 237     6584   2851   6479   -426   -809    274  A    O  
ATOM   1809  OE2 GLU A 237      26.968  -3.943 -36.230  1.00 48.47      A    O1-
ANISOU 1809  OE2 GLU A 237     7460   3414   7541   -725  -1067    596  A    O1-
ATOM   1810  N   ALA A 238      28.090 -10.665 -36.457  1.00 25.98      A    N  
ANISOU 1810  N   ALA A 238     3812   2015   4042   -664   -407    361  A    N  
ATOM   1811  CA  ALA A 238      28.213 -11.933 -35.756  1.00 24.83      A    C  
ANISOU 1811  CA  ALA A 238     3629   1998   3806   -594   -344    181  A    C  
ATOM   1812  C   ALA A 238      29.396 -12.739 -36.287  1.00 29.60      A    C  
ANISOU 1812  C   ALA A 238     3957   2855   4435   -646   -269    315  A    C  
ATOM   1813  O   ALA A 238      30.157 -13.329 -35.513  1.00 30.34      A    O  
ANISOU 1813  O   ALA A 238     3987   2958   4581   -686   -341    289  A    O  
ATOM   1814  CB  ALA A 238      26.925 -12.727 -35.882  1.00 24.41      A    C  
ANISOU 1814  CB  ALA A 238     3629   2050   3596   -394   -195      0  A    C  
ATOM   1815  N   ILE A 239      29.560 -12.745 -37.607  1.00 24.10      A    N  
ANISOU 1815  N   ILE A 239     3084   2381   3690   -631   -124    468  A    N  
ATOM   1816  CA  ILE A 239      30.683 -13.443 -38.236  1.00 27.91      A    C  
ANISOU 1816  CA  ILE A 239     3275   3152   4179   -631      5    578  A    C  
ATOM   1817  C   ILE A 239      32.026 -12.795 -37.892  1.00 29.48      A    C  
ANISOU 1817  C   ILE A 239     3292   3343   4564   -853   -137    820  A    C  
ATOM   1818  O   ILE A 239      33.005 -13.490 -37.594  1.00 33.98      A    O  
ANISOU 1818  O   ILE A 239     3644   4050   5217   -836   -125    850  A    O  
ATOM   1819  CB  ILE A 239      30.510 -13.488 -39.773  1.00 31.62      A    C  
ANISOU 1819  CB  ILE A 239     3617   3917   4480   -581    212    678  A    C  
ATOM   1820  CG1 ILE A 239      29.323 -14.385 -40.134  1.00 30.92      A    C  
ANISOU 1820  CG1 ILE A 239     3668   3880   4201   -388    329    427  A    C  
ATOM   1821  CG2 ILE A 239      31.792 -13.973 -40.461  1.00 33.42      A    C  
ANISOU 1821  CG2 ILE A 239     3512   4485   4703   -578    380    808  A    C  
ATOM   1822  CD1 ILE A 239      28.892 -14.293 -41.598  1.00 34.09      A    C  
ANISOU 1822  CD1 ILE A 239     4021   4555   4376   -371    475    506  A    C  
ATOM   1823  N   GLN A 240      32.073 -11.468 -37.931  1.00 34.84      A    N  
ANISOU 1823  N   GLN A 240     5947   2518   4774   -685    849    568  A    N  
ATOM   1824  CA  GLN A 240      33.299 -10.753 -37.591  1.00 38.57      A    C  
ANISOU 1824  CA  GLN A 240     6164   2844   5646  -1059    885    635  A    C  
ATOM   1825  C   GLN A 240      33.691 -11.058 -36.142  1.00 42.86      A    C  
ANISOU 1825  C   GLN A 240     6302   3556   6428  -1197    507    518  A    C  
ATOM   1826  O   GLN A 240      34.863 -11.267 -35.844  1.00 43.72      A    O  
ANISOU 1826  O   GLN A 240     5905   3820   6886  -1464    547    656  A    O  
ATOM   1827  CB  GLN A 240      33.126  -9.251 -37.831  1.00 47.73      A    C  
ANISOU 1827  CB  GLN A 240     7782   3626   6728  -1242    910    691  A    C  
ATOM   1828  CG  GLN A 240      33.072  -8.899 -39.325  1.00 58.80      A    C  
ANISOU 1828  CG  GLN A 240     9466   4904   7971  -1214   1308    897  A    C  
ATOM   1829  CD  GLN A 240      32.473  -7.530 -39.625  1.00 67.41      A    C  
ANISOU 1829  CD  GLN A 240    11016   5711   8887  -1176   1292    976  A    C  
ATOM   1830  NE2 GLN A 240      32.515  -7.137 -40.896  1.00 66.06      A    N  
ANISOU 1830  NE2 GLN A 240    10949   5560   8592  -1167   1542   1152  A    N  
ATOM   1831  OE1 GLN A 240      31.982  -6.835 -38.730  1.00 70.80      A    O  
ANISOU 1831  OE1 GLN A 240    11636   5975   9289  -1116   1057    863  A    O  
ATOM   1832  N   CYS A 241      32.703 -11.129 -35.255  1.00 37.14      A    N  
ANISOU 1832  N   CYS A 241     5757   2859   5496  -1019    145    317  A    N  
ATOM   1833  CA  CYS A 241      32.960 -11.495 -33.864  1.00 41.61      A    C  
ANISOU 1833  CA  CYS A 241     5970   3620   6221  -1169   -240    197  A    C  
ATOM   1834  C   CYS A 241      33.450 -12.936 -33.730  1.00 42.52      A    C  
ANISOU 1834  C   CYS A 241     5517   4104   6535  -1010   -205    281  A    C  
ATOM   1835  O   CYS A 241      34.465 -13.203 -33.079  1.00 39.92      A    O  
ANISOU 1835  O   CYS A 241     4637   3991   6540  -1265   -302    426  A    O  
ATOM   1836  CB  CYS A 241      31.701 -11.302 -33.017  1.00 42.21      A    C  
ANISOU 1836  CB  CYS A 241     6405   3637   5997   -964   -578    -39  A    C  
ATOM   1837  SG  CYS A 241      31.894 -11.875 -31.309  1.00 43.40      A    S  
ANISOU 1837  SG  CYS A 241     6154   4069   6266  -1164  -1071   -207  A    S  
ATOM   1838  N   TRP A 242      32.728 -13.862 -34.351  1.00 34.44      A    N  
ANISOU 1838  N   TRP A 242     4643   3162   5280   -616    -42    235  A    N  
ATOM   1839  CA  TRP A 242      33.061 -15.279 -34.252  1.00 36.29      A    C  
ANISOU 1839  CA  TRP A 242     4494   3642   5654   -410     82    292  A    C  
ATOM   1840  C   TRP A 242      34.478 -15.576 -34.729  1.00 41.49      A    C  
ANISOU 1840  C   TRP A 242     4675   4344   6746   -506    508    592  A    C  
ATOM   1841  O   TRP A 242      35.168 -16.408 -34.149  1.00 44.44      A    O  
ANISOU 1841  O   TRP A 242     4505   4942   7438   -437    524    760  A    O  
ATOM   1842  CB  TRP A 242      32.058 -16.113 -35.052  1.00 34.48      A    C  
ANISOU 1842  CB  TRP A 242     4679   3424   4998    -96    278    188  A    C  
ATOM   1843  CG  TRP A 242      32.249 -17.588 -34.901  1.00 34.04      A    C  
ANISOU 1843  CG  TRP A 242     4401   3519   5012    119    450    196  A    C  
ATOM   1844  CD1 TRP A 242      32.616 -18.465 -35.872  1.00 42.00      A    C  
ANISOU 1844  CD1 TRP A 242     5515   4440   6002    248   1030    285  A    C  
ATOM   1845  CD2 TRP A 242      32.074 -18.359 -33.704  1.00 35.10      A    C  
ANISOU 1845  CD2 TRP A 242     4240   3868   5230    230     92    118  A    C  
ATOM   1846  CE2 TRP A 242      32.353 -19.701 -34.028  1.00 40.67      A    C  
ANISOU 1846  CE2 TRP A 242     4884   4581   5986    460    496    187  A    C  
ATOM   1847  CE3 TRP A 242      31.711 -18.046 -32.388  1.00 33.44      A    C  
ANISOU 1847  CE3 TRP A 242     3853   3816   5038    141   -495     -5  A    C  
ATOM   1848  NE1 TRP A 242      32.688 -19.736 -35.359  1.00 47.91      A    N  
ANISOU 1848  NE1 TRP A 242     6084   5286   6833    465   1100    275  A    N  
ATOM   1849  CZ2 TRP A 242      32.286 -20.733 -33.087  1.00 41.67      A    C  
ANISOU 1849  CZ2 TRP A 242     4746   4879   6209    630    311    171  A    C  
ATOM   1850  CZ3 TRP A 242      31.644 -19.073 -31.449  1.00 38.24      A    C  
ANISOU 1850  CZ3 TRP A 242     4162   4645   5721    271   -722    -33  A    C  
ATOM   1851  CH2 TRP A 242      31.926 -20.400 -31.807  1.00 34.40      A    C  
ANISOU 1851  CH2 TRP A 242     3588   4172   5310    527   -333     70  A    C  
ATOM   1852  N   GLN A 243      34.909 -14.898 -35.785  1.00 43.37      A    N  
ANISOU 1852  N   GLN A 243     5085   4390   7003   -639    874    714  A    N  
ATOM   1853  CA  GLN A 243      36.268 -15.054 -36.294  1.00 53.19      A    C  
ANISOU 1853  CA  GLN A 243     5862   5691   8655   -733   1320   1044  A    C  
ATOM   1854  C   GLN A 243      37.184 -13.919 -35.837  1.00 58.25      A    C  
ANISOU 1854  C   GLN A 243     6179   6388   9565  -1228   1111   1232  A    C  
ATOM   1855  O   GLN A 243      37.323 -13.651 -34.643  1.00 62.67      A    O  
ANISOU 1855  O   GLN A 243     6470   7123  10218  -1497    635   1225  A    O  
ATOM   1856  CB  GLN A 243      36.242 -15.124 -37.816  1.00 57.80      A    C  
ANISOU 1856  CB  GLN A 243     6843   6057   9062   -620   1913   1077  A    C  
ATOM   1857  CG  GLN A 243      35.345 -16.227 -38.344  1.00 66.94      A    C  
ANISOU 1857  CG  GLN A 243     8429   7165   9841   -289   2147    892  A    C  
ATOM   1858  CD  GLN A 243      35.023 -16.061 -39.812  1.00 80.04      A    C  
ANISOU 1858  CD  GLN A 243    10652   8625  11136   -335   2601    871  A    C  
ATOM   1859  NE2 GLN A 243      34.075 -16.854 -40.300  1.00 87.76      A    N  
ANISOU 1859  NE2 GLN A 243    12125   9593  11627   -212   2724    700  A    N  
ATOM   1860  OE1 GLN A 243      35.609 -15.222 -40.500  1.00 81.28      A    O  
ANISOU 1860  OE1 GLN A 243    10815   8665  11404   -543   2822   1020  A    O  
TER   
HETATM 1861  O   HOH A2001      28.671 -18.144 -41.022  1.00 29.13      I    O  
HETATM 1862  O   HOH A2002      17.184 -15.488 -37.668  1.00 26.80      I    O  
HETATM 1863  O   HOH A2003      14.104 -18.422 -35.744  1.00 51.14      I    O  
HETATM 1864  O   HOH A2004      11.800 -17.566 -37.403  1.00 29.19      I    O  
HETATM 1865  O   HOH A2005      11.118 -19.577 -32.658  1.00 43.50      I    O  
HETATM 1866  O   HOH A2006       0.996 -19.219 -41.723  1.00 52.13      I    O  
HETATM 1867  O   HOH A2007       9.152 -12.489 -50.458  1.00 47.66      I    O  
HETATM 1868  O   HOH A2008      14.872  -9.753 -53.226  1.00 49.48      I    O  
HETATM 1869  O   HOH A2009      10.668 -21.920 -26.199  1.00 47.08      I    O  
HETATM 1870  O   HOH A2010      29.097 -17.991 -48.203  1.00 36.18      I    O  
HETATM 1871  O   HOH A2011      29.747 -23.853 -48.661  1.00 40.86      I    O  
HETATM 1872  O   HOH A2012       1.453 -25.876 -21.426  1.00 44.28      I    O  
HETATM 1873  O   HOH A2013       1.994 -28.377 -23.091  1.00 50.11      I    O  
HETATM 1874  O   HOH A2014       3.437 -27.335 -49.770  1.00 51.55      I    O  
HETATM 1875  O   HOH A2015       8.377 -27.624 -56.354  1.00 52.30      I    O  
HETATM 1876  O   HOH A2016      11.374 -24.487 -57.449  1.00 48.02      I    O  
HETATM 1877  O   HOH A2017      11.943 -17.672 -56.029  1.00 44.10      I    O  
HETATM 1878  O   HOH A2018      -0.375 -19.270 -30.749  1.00 47.95      I    O  
HETATM 1879  O   HOH A2019      -0.681 -21.491 -36.050  1.00 58.67      I    O  
HETATM 1880  O   HOH A2020      29.655 -19.657 -50.506  1.00 36.99      I    O  
HETATM 1881  O   HOH A2021      14.108 -31.107 -34.556  1.00 49.31      I    O  
HETATM 1882  O   HOH A2022       2.298 -11.135 -35.356  1.00 49.18      I    O  
HETATM 1883  O   HOH A2023      11.410 -42.383 -50.591  0.50 35.83      I    O  
HETATM 1884  O   HOH A2024      18.948 -36.862 -53.226  1.00 49.54      I    O  
HETATM 1885  O   HOH A2025      12.552 -16.148 -33.029  1.00 48.32      I    O  
HETATM 1886  O   HOH A2026       9.757 -15.209 -49.867  1.00 33.38      I    O  
HETATM 1887  O   HOH A2027      17.167 -11.014 -43.044  1.00 37.06      I    O  
HETATM 1888  O   HOH A2028      15.569 -11.829 -40.842  1.00 35.46      I    O  
HETATM 1889  O   HOH A2029      17.106 -10.446 -51.804  1.00 28.45      I    O  
HETATM 1890  O   HOH A2030      14.869 -12.842 -54.220  1.00 39.04      I    O  
HETATM 1891  O   HOH A2031      23.671 -36.192 -49.550  1.00 49.45      I    O  
HETATM 1892  O   HOH A2032      26.028 -35.652 -47.918  0.50 43.21      I    O  
HETATM 1893  O   HOH A2033      27.535 -14.712 -49.687  1.00 30.79      I    O  
HETATM 1894  O   HOH A2034      26.579 -17.431 -47.575  1.00 28.40      I    O  
HETATM 1895  O   HOH A2035      30.904 -11.961 -43.527  1.00 36.78      I    O  
HETATM 1896  O   HOH A2036      21.458  -9.469 -40.394  1.00 34.88      I    O  
HETATM 1897  O   HOH A2037      28.201 -35.676 -16.215  1.00 47.98      I    O  
HETATM 1898  O   HOH A2038      24.456 -38.805 -17.170  1.00 26.32      I    O  
HETATM 1899  O   HOH A2039      29.508 -22.808 -46.026  1.00 43.19      I    O  
HETATM 1900  O   HOH A2040      15.860 -26.027 -34.256  1.00 42.52      I    O  
HETATM 1901  O   HOH A2041      31.943 -46.162 -29.685  1.00 24.52      I    O  
HETATM 1902  O   HOH A2042      33.533 -43.866 -29.469  1.00 32.01      I    O  
HETATM 1903  O   HOH A2043       0.633 -24.732 -41.425  1.00 52.33      I    O  
HETATM 1904  O   HOH A2044       2.366 -27.784 -47.295  1.00 46.26      I    O  
HETATM 1905  O   HOH A2045      37.046 -28.874 -27.288  1.00 53.69      I    O  
HETATM 1906  O   HOH A2046      33.637 -33.892 -18.826  1.00 33.71      I    O  
HETATM 1907  O   HOH A2047      35.200 -29.956 -19.512  1.00 48.44      I    O  
HETATM 1908  O   HOH A2048       9.282 -24.897 -55.728  1.00 44.78      I    O  
HETATM 1909  O   HOH A2049       5.501 -25.410 -49.823  1.00 33.02      I    O  
HETATM 1910  O   HOH A2050      12.076 -32.382 -54.917  1.00 56.26      I    O  
HETATM 1911  O   HOH A2051      14.305 -19.201 -55.532  1.00 33.49      I    O  
HETATM 1912  O   HOH A2052      21.763 -24.340 -53.067  1.00 30.38      I    O  
HETATM 1913  O   HOH A2053      16.308 -17.795 -56.535  1.00 40.61      I    O  
HETATM 1914  O   HOH A2054      18.217 -19.040 -58.150  1.00 37.99      I    O  
HETATM 1915  O   HOH A2055      26.189  -5.060 -31.531  1.00 53.21      I    O  
HETATM 1916  O   HOH A2056      23.948 -23.809 -54.743  1.00 49.47      I    O  
HETATM 1917  O   HOH A2057      24.973 -18.309 -50.082  1.00 27.42      I    O  
HETATM 1918  O   HOH A2058      29.228 -22.074 -50.748  1.00 49.91      I    O  
HETATM 1919  O   HOH A2059      28.502 -18.203 -52.415  1.00 34.59      I    O  
HETATM 1920  O   HOH A2060      22.153 -24.850 -50.714  1.00 38.75      I    O  
HETATM 1921  O   HOH A2061      21.393 -26.928 -49.247  1.00 26.13      I    O  
HETATM 1922  O   HOH A2062      13.202 -32.891 -37.313  1.00 33.05      I    O  
HETATM 1923  O   HOH A2063      12.310 -36.726 -35.434  1.00 40.54      I    O  
HETATM 1924  O   HOH A2064       8.795 -39.132 -32.748  1.00 59.98      I    O  
HETATM 1925  O   HOH A2065      16.879 -46.564 -43.933  1.00 56.17      I    O  
HETATM 1926  O   HOH A2066      10.887 -39.552 -50.256  1.00 34.62      I    O  
HETATM 1927  O   HOH A2067      10.992 -45.627 -47.812  1.00 44.48      I    O  
HETATM 1928  O   HOH A2068      16.983 -38.231 -51.790  1.00 38.66      I    O  
HETATM 1929  O   HOH A2069      12.209 -38.434 -52.279  1.00 41.70      I    O  
HETATM 1930  O   HOH A2070      11.768 -33.672 -52.804  1.00 36.08      I    O  
HETATM 1931  O   HOH A2071      20.726 -32.652 -51.128  1.00 33.06      I    O  
HETATM 1932  O   HOH A2072      21.403 -28.246 -52.988  1.00 44.32      I    O  
HETATM 1933  O   HOH A2073      27.394 -31.683 -43.715  1.00 34.32      I    O  
HETATM 1934  O   HOH A2074       9.097 -41.314 -34.397  1.00 47.45      I    O  
HETATM 1935  O   HOH A2075      17.430 -44.403 -27.293  1.00 54.26      I    O  
HETATM 1936  O   HOH A2076      14.147 -49.037 -33.567  1.00 43.92      I    O  
HETATM 1937  O   HOH A2077      15.932 -47.456 -41.200  1.00 47.97      I    O  
HETATM 1938  O   HOH A2078      25.006 -48.283 -30.778  1.00 37.23      I    O  
HETATM 1939  O   HOH A2079      19.762 -48.448 -44.568  1.00 44.09      I    O  
HETATM 1940  O   HOH A2080      12.669 -44.203 -49.144  1.00 29.33      I    O  
HETATM 1941  O   HOH A2081      22.906 -38.578 -48.697  1.00 35.67      I    O  
HETATM 1942  O   HOH A2082      26.268 -37.978 -46.372  1.00 37.41      I    O  
HETATM 1943  O   HOH A2083      28.668 -38.897 -45.381  1.00 41.10      I    O  
HETATM 1944  O   HOH A2084      28.295 -42.184 -42.728  1.00 43.85      I    O  
HETATM 1945  O   HOH A2085      26.079 -36.700 -38.414  1.00 22.33      I    O  
HETATM 1946  O   HOH A2086      32.374 -32.571 -40.988  1.00 52.48      I    O  
HETATM 1947  O   HOH A2087      15.734 -34.174 -28.295  1.00 43.71      I    O  
HETATM 1948  O   HOH A2088      18.147 -29.564 -30.683  1.00 41.76      I    O  
HETATM 1949  O   HOH A2089      18.476 -26.881 -18.905  1.00 48.67      I    O  
HETATM 1950  O   HOH A2090      18.739 -37.638 -13.438  1.00 47.09      I    O  
HETATM 1951  O   HOH A2091      25.456 -34.690 -16.867  1.00 34.89      I    O  
HETATM 1952  O   HOH A2092      25.548 -31.249 -16.604  1.00 58.86      I    O  
HETATM 1953  O   HOH A2093      23.533 -38.680 -14.552  1.00 33.10      I    O  
HETATM 1954  O   HOH A2094      24.161 -36.329 -18.475  1.00 22.73      I    O  
HETATM 1955  O   HOH A2095      29.140 -34.381 -21.724  1.00 38.27      I    O  
HETATM 1956  O   HOH A2096       7.926 -28.938 -14.859  1.00 46.63      I    O  
HETATM 1957  O   HOH A2097      29.462 -36.780 -19.272  1.00 38.35      I    O  
HETATM 1958  O   HOH A2098      19.992 -45.320 -26.807  1.00 40.13      I    O  
HETATM 1959  O   HOH A2099      29.575 -45.558 -28.334  1.00 24.20      I    O  
HETATM 1960  O   HOH A2100      32.960 -42.685 -27.080  1.00 31.83      I    O  
HETATM 1961  O   HOH A2101      32.312 -42.096 -23.287  1.00 30.04      I    O  
HETATM 1962  O   HOH A2102      32.352 -38.196 -35.654  1.00 43.21      I    O  
HETATM 1963  O   HOH A2103      27.583 -29.723 -36.908  1.00 25.77      I    O  
HETATM 1964  O   HOH A2104      20.749 -23.678 -18.668  1.00 45.00      I    O  
HETATM 1965  O   HOH A2105      13.246 -21.516 -23.566  1.00 43.17      I    O  
HETATM 1966  O   HOH A2106      17.561 -16.334 -27.614  1.00 37.27      I    O  
HETATM 1967  O   HOH A2107      22.199 -11.700 -23.393  1.00 31.04      I    O  
HETATM 1968  O   HOH A2108      26.427 -17.238 -25.094  1.00 31.67      I    O  
HETATM 1969  O   HOH A2109      25.631 -17.266 -21.241  1.00 40.10      I    O  
HETATM 1970  O   HOH A2110      23.860 -20.851 -30.023  1.00 29.33      I    O  
HETATM 1971  O   HOH A2111      22.191 -22.703 -25.061  1.00 38.27      I    O  
HETATM 1972  O   HOH A2112      27.507 -21.085 -18.646  1.00 44.12      I    O  
HETATM 1973  O   HOH A2113      32.028 -26.662 -18.558  1.00 42.43      I    O  
HETATM 1974  O   HOH A2114      35.412 -27.381 -24.747  1.00 35.13      I    O  
HETATM 1975  O   HOH A2115      34.286 -32.253 -20.853  1.00 29.70      I    O  
HETATM 1976  O   HOH A2116      31.165 -34.690 -19.533  1.00 40.07      I    O  
HETATM 1977  O   HOH A2117      33.522 -31.166 -30.117  1.00 28.55      I    O  
HETATM 1978  O   HOH A2118      39.035 -32.939 -25.619  1.00 41.98      I    O  
HETATM 1979  O   HOH A2119      36.181 -33.940 -21.465  1.00 35.65      I    O  
HETATM 1980  O   HOH A2120      37.425 -36.342 -24.323  1.00 32.68      I    O  
HETATM 1981  O   HOH A2121      34.666 -31.050 -33.744  1.00 54.41      I    O  
HETATM 1982  O   HOH A2122      33.910 -42.228 -31.859  1.00 34.41      I    O  
HETATM 1983  O   HOH A2123      32.172 -29.109 -31.710  1.00 28.28      I    O  
HETATM 1984  O   HOH A2124      20.783 -19.125 -30.049  1.00 29.46      I    O  
HETATM 1985  O   HOH A2125      18.855 -15.383 -30.821  1.00 28.83      I    O  
HETATM 1986  O   HOH A2126      25.769 -10.743 -23.015  1.00 49.01      I    O  
HETATM 1987  O   HOH A2127      24.770  -6.935 -29.566  1.00 41.99      I    O  
HETATM 1988  O   HOH A2128      26.814 -15.784 -22.946  1.00 45.49      I    O  
HETATM 1989  O   HOH A2129      32.859 -17.517 -22.127  1.00 48.50      I    O  
HETATM 1990  O   HOH A2130      34.850 -22.711 -30.520  1.00 56.07      I    O  
HETATM 1991  O   HOH A2131      35.613 -28.785 -31.377  1.00 54.97      I    O  
HETATM 1992  O   HOH A2132      20.003  -8.783 -37.887  1.00 36.85      I    O  
HETATM 1993  O   HOH A2133      13.762  -8.359 -27.101  1.00 38.23      I    O  
HETATM 1994  O   HOH A2134      21.437  -4.815 -36.219  1.00 48.70      I    O  
HETATM 1995  O   HOH A2135      26.861  -5.340 -40.550  1.00 47.51      I    O  
HETATM 1996  O   HOH A2136      31.228  -7.707 -34.433  1.00 37.68      I    O  
HETATM 1997  O   HOH A2137      23.956  -3.807 -35.106  1.00 56.24      I    O  
HETATM 1998  O   HOH A2138      32.158  -6.094 -36.504  1.00 53.71      I    O  
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.