CNRS Nantes University US2B US2B
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Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  HIV_apo  ***

elNémo ID: 2602061631263072433

Job options:

ID        	=	 2602061631263072433
JOBID     	=	 HIV_apo
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER HIV_apo

CRYST1   46.416   46.416  101.370  90.00  90.00  90.00 P 41 21 2     1
HETATM    1  O   HOH A   1       5.851   5.385  -0.099  0.50 18.43           O  
ANISOU    1  O   HOH A   1     2309   3264   1429   -227    183    401       O  
HETATM    2  O   HOH A   2      -5.279   8.960 -13.040  1.00  7.16           O  
ANISOU    2  O   HOH A   2      525   1875    320    308    -23     -5       O  
HETATM    3  O   HOH A   3       5.894 -10.829   0.408  1.00 21.65           O  
ANISOU    3  O   HOH A   3     2010   4919   1294   1692    130    181       O  
HETATM    4  O   HOH A   4       0.376  10.111 -11.893  1.00 13.19           O  
ANISOU    4  O   HOH A   4     1921   1916   1171   -190   -379    451       O  
HETATM    5  O   HOH A   5      -8.967   2.762 -15.966  1.00 11.86           O  
ANISOU    5  O   HOH A   5     1474   2058    973     21     30   -260       O  
HETATM    6  O   HOH A   6       5.346  -7.484  -1.671  1.00 18.99           O  
ANISOU    6  O   HOH A   6     2591   2699   1925    228    -11    559       O  
HETATM    7  O   HOH A   7       2.083  11.776 -29.492  1.00 18.30           O  
ANISOU    7  O   HOH A   7     3202   2665   1086    129   -203   -179       O  
HETATM    8  O   HOH A   8      -5.427  10.780 -16.988  1.00 14.74           O  
ANISOU    8  O   HOH A   8     1509   2813   1275   -134    145     97       O  
HETATM    9  O   HOH A   9       4.161  12.800 -26.603  1.00 16.83           O  
ANISOU    9  O   HOH A   9     2006   2944   1441    -13    176    199       O  
HETATM   10  O   HOH A  10       1.500  -8.806   4.341  1.00 17.05           O  
ANISOU   10  O   HOH A  10     2146   2447   1884    213     17    586       O  
HETATM   11  O   HOH A  11      11.530  21.963   2.160  1.00 18.47           O  
ANISOU   11  O   HOH A  11     3221   2361   1435   -662   -497     27       O  
HETATM   12  O   HOH A  12      -7.674   7.644 -14.738  1.00 17.51           O  
ANISOU   12  O   HOH A  12     2257   2592   1802    -62    -81    121       O  
HETATM   13  O   HOH A  13      -1.562   4.660 -23.820  1.00 18.43           O  
ANISOU   13  O   HOH A  13     2496   3156   1347    180    366    -51       O  
HETATM   14  O   HOH A  14      -1.167   8.110  -0.046  1.00 17.30           O  
ANISOU   14  O   HOH A  14     2856   2319   1397    623   -527    -86       O  
HETATM   15  O   HOH A  15       2.639  11.536  -2.698  1.00 25.01           O  
ANISOU   15  O   HOH A  15     4087   2644   2771   -553   -865   -261       O  
HETATM   16  O   HOH A  16       0.653  10.279   0.052  1.00 21.03           O  
ANISOU   16  O   HOH A  16     3528   2455   2006    192    -63   -252       O  
HETATM   17  O   HOH A  17      -1.640  14.041 -21.927  1.00 16.89           O  
ANISOU   17  O   HOH A  17     2272   2806   1336    281    -74    508       O  
HETATM   18  O   HOH A  19      -7.853   7.139 -10.079  1.00 22.59           O  
ANISOU   18  O   HOH A  19     3635   2656   2293   1287  -1556  -1119       O  
HETATM   19  O   HOH A  20       0.912   2.400 -22.843  1.00 18.31           O  
ANISOU   19  O   HOH A  20     2170   3271   1513    -42    151     93       O  
HETATM   20  O   HOH A  21     -10.626   1.127  -6.347  1.00 20.60           O  
ANISOU   20  O   HOH A  21     2320   3100   2406    590   -349   -665       O  
HETATM   21  O   HOH A  22       3.256  22.087 -10.996  1.00 29.23           O  
ANISOU   21  O   HOH A  22     3153   5558   2395   2214   -941  -1192       O  
HETATM   22  O   HOH A  23       1.155   4.816 -24.071  1.00 19.30           O  
ANISOU   22  O   HOH A  23     2481   2897   1953    -82   -220    -96       O  
HETATM   23  O   HOH A  24     -10.243   0.683 -14.566  1.00 24.74           O  
ANISOU   23  O   HOH A  24     3858   3453   2089   -998   -875    640       O  
HETATM   24  O   HOH A  25       8.556  15.313  -1.164  1.00 46.30           O  
ANISOU   24  O   HOH A  25    11995   2870   2724    990  -2422  -2439       O  
HETATM   25  O   HOH A  26       9.666   9.845  -7.034  1.00 26.62           O  
ANISOU   25  O   HOH A  26     3088   4292   2733     42    226   -858       O  
HETATM   26  O   HOH A  27      14.596   9.013 -15.557  1.00 29.28           O  
ANISOU   26  O   HOH A  27     2477   5842   2806    -22   -635    -65       O  
HETATM   27  O   HOH A  28      -2.761   2.228 -25.166  0.50 22.91           O  
ANISOU   27  O   HOH A  28     4054   2902   1748   -854   -817    594       O  
HETATM   28  O   HOH A  29       4.026  -9.017 -11.631  1.00 29.39           O  
ANISOU   28  O   HOH A  29     4798   2536   3831    332    853    -48       O  
HETATM   29  O   HOH A  30       2.375  -1.591 -24.050  1.00 23.41           O  
ANISOU   29  O   HOH A  30     3259   3719   1916   -418   -274     94       O  
HETATM   30  O   HOH A  31      10.396  -7.503  -4.013  1.00 31.16           O  
ANISOU   30  O   HOH A  31     3942   4892   3005   2442   1155   1469       O  
HETATM   31  O   HOH A  32      10.541   4.744 -24.270  1.00 34.12           O  
ANISOU   31  O   HOH A  32     7099   3039   2824   1698   1108     73       O  
HETATM   32  O   HOH A  33       2.848   3.989 -26.389  1.00 15.42           O  
ANISOU   32  O   HOH A  33     2140   2374   1343    139    320    155       O  
HETATM   33  O   HOH A  34       1.779 -13.622   5.941  1.00 10.06           O  
ANISOU   33  O   HOH A  34     1788   1112    922    551    343    -24       O  
HETATM   34  O   HOH A  35       5.607   8.185 -27.806  1.00 17.98           O  
ANISOU   34  O   HOH A  35     2492   3129   1210    708   -365   -386       O  
HETATM   35  O   HOH A  36      -0.940  16.712 -18.954  1.00 20.00           O  
ANISOU   35  O   HOH A  36     2572   2590   2434    532   -357    261       O  
HETATM   36  O   HOH A  37       6.453  13.425 -25.359  1.00 21.88           O  
ANISOU   36  O   HOH A  37     2602   4117   1593   -550    209   -135       O  
HETATM   37  O   HOH A  38      -6.736   3.009 -26.148  1.00 23.29           O  
ANISOU   37  O   HOH A  38     2924   3603   2321     -7    747    271       O  
HETATM   38  O   HOH A  39      15.303  13.398  -8.908  1.00 25.52           O  
ANISOU   38  O   HOH A  39     2065   4305   3325    670    470   1722       O  
HETATM   39  O   HOH A  40       5.823  -9.050  -3.815  1.00 29.09           O  
ANISOU   39  O   HOH A  40     4429   3438   3186    160    699   -360       O  
HETATM   40  O   HOH A  41      -6.009   8.080  -6.136  1.00 24.56           O  
ANISOU   40  O   HOH A  41     3745   3512   2074   -207    302   -495       O  
HETATM   41  O   HOH A  42      -4.131  10.119  -6.213  1.00 23.91           O  
ANISOU   41  O   HOH A  42     2671   3428   2983    439   -419   -701       O  
HETATM   42  O   HOH A  43      12.226  -6.448  -0.573  1.00 31.10           O  
ANISOU   42  O   HOH A  43     2189   4600   5027   1130    252    701       O  
HETATM   43  O   HOH A  44      -1.630  11.801 -10.919  1.00 30.62           O  
ANISOU   43  O   HOH A  44     4213   4853   2568   1905   -835  -1602       O  
HETATM   44  O   HOH A  45      12.199  -1.367 -14.923  1.00 33.72           O  
ANISOU   44  O   HOH A  45     3244   5905   3661   -477    194    187       O  
HETATM   45  O   HOH A  46      -9.729  -5.531  -8.989  1.00 29.70           O  
ANISOU   45  O   HOH A  46     3126   3286   4870   -372  -1377    711       O  
HETATM   46  O   HOH A  47       7.105  12.905  -4.941  1.00 27.00           O  
ANISOU   46  O   HOH A  47     4042   3241   2973   -714    913    102       O  
HETATM   47  O   HOH A  48       3.886   9.480 -29.812  1.00 22.13           O  
ANISOU   47  O   HOH A  48     2313   3930   2164    350   -197    336       O  
HETATM   48  O   HOH A  49      14.639   5.261 -18.477  1.00 28.45           O  
ANISOU   48  O   HOH A  49     2926   4645   3237   1158      2   -386       O  
HETATM   49  O   HOH A  50       5.706   8.603   0.471  0.50 20.75           O  
ANISOU   49  O   HOH A  50     4318   1376   2190    -64   -456   -768       O  
HETATM   50  O   HOH A  51      12.391   3.759 -20.921  1.00 30.05           O  
ANISOU   50  O   HOH A  51     2184   4073   5160    222    640   -743       O  
HETATM   51  O   HOH A  52       1.267  21.403 -22.572  1.00 31.37           O  
ANISOU   51  O   HOH A  52     5765   2766   3385    833  -1066     52       O  
HETATM   52  O   HOH A  53       3.146  18.339 -25.459  1.00 33.20           O  
ANISOU   52  O   HOH A  53     4350   5190   3073  -1221    212   1964       O  
HETATM   53  O   HOH A  54       2.845 -11.875  -2.292  1.00 31.18           O  
ANISOU   53  O   HOH A  54     4034   3543   4268   1761    393   -144       O  
HETATM   54  O   HOH A  55       7.040  10.078  -5.886  1.00 33.41           O  
ANISOU   54  O   HOH A  55     2825   7812   2058   -461   -286  -1453       O  
HETATM   55  O   HOH A  57      -5.094  -9.717   4.109  1.00 22.68           O  
ANISOU   55  O   HOH A  57     3341   2858   2416   -192    401    223       O  
HETATM   56  O   HOH A  58      12.301   9.185 -23.495  1.00 27.98           O  
ANISOU   56  O   HOH A  58     3507   4514   2610    687    704     95       O  
HETATM   57  O   HOH A  59      -7.315 -11.163  -3.433  1.00 31.44           O  
ANISOU   57  O   HOH A  59     4631   2837   4475    152   -484    436       O  
HETATM   58  O   HOH A  60      -8.593  -3.476 -14.587  1.00 32.12           O  
ANISOU   58  O   HOH A  60     4119   4233   3851   -606   1183    810       O  
HETATM   59  O   HOH A  61       7.454   1.186 -27.745  1.00 26.87           O  
ANISOU   59  O   HOH A  61     3585   4283   2340   -387    348    294       O  
HETATM   60  O   HOH A  62       8.862   7.972  -0.219  0.50 28.84           O  
ANISOU   60  O   HOH A  62     2054   5273   3629    -46  -1031   1790       O  
HETATM   61  O   HOH A  63      -8.563  -4.629 -12.325  1.00 31.42           O  
ANISOU   61  O   HOH A  63     3862   4573   3502  -1059   1070  -1024       O  
HETATM   62  O   HOH A  64       4.355  -3.495 -23.190  1.00 29.10           O  
ANISOU   62  O   HOH A  64     4483   4201   2370   -448    321    216       O  
HETATM   63  O   HOH A  65      -7.739  -5.802 -17.394  1.00 35.25           O  
ANISOU   63  O   HOH A  65     4993   2393   6006  -1321  -1321    794       O  
HETATM   64  O   HOH A  66      -1.289  21.178 -21.628  1.00 52.89           O  
ANISOU   64  O   HOH A  66     6665   9264   4164   3818    328    863       O  
HETATM   65  O   HOH A  67       4.946  10.671  -1.726  1.00 36.01           O  
ANISOU   65  O   HOH A  67     6497   3495   3688   -892   -404   -244       O  
HETATM   66  O   HOH A  68      -9.448  10.967 -18.193  1.00 39.81           O  
ANISOU   66  O   HOH A  68     2629   4905   7590   -126   -953   2939       O  
HETATM   67  O   HOH A  69      -1.142  14.595 -11.855  1.00 27.63           O  
ANISOU   67  O   HOH A  69     4635   3325   2538   -102   -126   -254       O  
HETATM   68  O   HOH A  70      10.749  -3.619 -22.635  1.00 40.82           O  
ANISOU   68  O   HOH A  70     2270   9010   4227    754   1738    538       O  
HETATM   69  O   HOH A  71       6.739  23.721 -14.041  1.00 38.64           O  
ANISOU   69  O   HOH A  71     6756   4574   3349    -48  -1212   -286       O  
HETATM   70  O   HOH A  74       3.035  11.551  -5.557  1.00 30.39           O  
ANISOU   70  O   HOH A  74     3296   5546   2701    325   -438  -1190       O  
HETATM   71  O   HOH A  75       4.462   9.949  -6.586  1.00 31.11           O  
ANISOU   71  O   HOH A  75     4484   3513   3822   -952  -1708   -393       O  
HETATM   72  O   HOH A  76      -1.441  18.544 -20.954  1.00 33.31           O  
ANISOU   72  O   HOH A  76     5512   3416   3728   -649  -1661    740       O  
HETATM   73  O   HOH A  77      -4.422  11.539 -11.292  1.00 32.12           O  
ANISOU   73  O   HOH A  77     6253   3611   2341   1243   -461    414       O  
HETATM   74  O   HOH A  78      -7.558   9.140  -8.298  1.00 32.27           O  
ANISOU   74  O   HOH A  78     3299   4792   4167    109   -247  -2593       O  
HETATM   75  O   HOH A  79      10.774  11.987  -7.826  1.00 33.35           O  
ANISOU   75  O   HOH A  79     3856   5199   3617    -69   -732   -195       O  
HETATM   76  O   HOH A  80      -0.098  -1.560 -21.993  1.00 37.44           O  
ANISOU   76  O   HOH A  80     7511   4193   2521   -481   -339   -308       O  
HETATM   77  O   HOH A  81     -11.247  -2.394 -11.273  1.00 33.95           O  
ANISOU   77  O   HOH A  81     3695   4533   4670    540   -767  -1880       O  
HETATM   78  O   HOH A  82       2.426  23.047 -16.328  1.00 34.85           O  
ANISOU   78  O   HOH A  82     5941   4012   3288   1587   -870   -390       O  
HETATM   79  O   HOH A  84       7.185   4.065 -25.936  1.00 31.03           O  
ANISOU   79  O   HOH A  84     3875   3532   4380    465    117    353       O  
HETATM   80  O   HOH A  85       6.524   7.202  -2.053  1.00 28.62           O  
ANISOU   80  O   HOH A  85     4944   4301   1628  -1001   -760    801       O  
HETATM   81  O   HOH A  86       3.670  16.284  -5.099  1.00 35.92           O  
ANISOU   81  O   HOH A  86     2520   7465   3662   -796    707   -660       O  
HETATM   82  O   HOH A  88       9.622  23.881 -17.491  1.00 27.84           O  
ANISOU   82  O   HOH A  88     4907   2913   2758    -47   -918   -674       O  
HETATM   83  O   HOH A  89      11.871  -6.159   3.234  1.00 37.44           O  
ANISOU   83  O   HOH A  89     4878   3199   6145   1329  -2316   -251       O  
HETATM   84  O   HOH A  90       9.420  14.022  -5.833  1.00 36.82           O  
ANISOU   84  O   HOH A  90     3176   5878   4935  -1436   1063  -1202       O  
HETATM   85  O   HOH A  91       4.895  14.324  -4.736  1.00 69.62           O  
ANISOU   85  O   HOH A  91     8446  12260   5743  -2225   -241  -1681       O  
HETATM   86  O   HOH A  92      -5.398  11.020  -8.746  1.00 30.22           O  
ANISOU   86  O   HOH A  92     3480   4969   3032   1235   -478   -831       O  
HETATM   87  O   HOH A  93      -2.196  13.932  -7.231  1.00 41.79           O  
ANISOU   87  O   HOH A  93     5641   6008   4227   2522    299   -920       O  
HETATM   88  O   HOH A  94      -0.372 -14.002  -0.960  1.00 42.56           O  
ANISOU   88  O   HOH A  94     6816   3554   5800   1445  -2283    767       O  
HETATM   89  O   HOH A  95      13.687   6.794 -23.398  1.00 43.40           O  
ANISOU   89  O   HOH A  95     6730   4889   4871   1610   1191   1844       O  
HETATM   90  O   HOH A  96      -9.774  -4.240 -18.315  1.00 41.03           O  
ANISOU   90  O   HOH A  96     7172   5389   3027  -1263    874    529       O  
HETATM   91  O   HOH A  97       5.606  12.386 -28.932  1.00 44.63           O  
ANISOU   91  O   HOH A  97     5229   9344   2383   1808    876    560       O  
HETATM   92  O   HOH A  98       2.518 -14.104  -0.459  1.00 35.39           O  
ANISOU   92  O   HOH A  98     4915   4782   3749   1892   -757   -205       O  
HETATM   93  O   HOH A  99      -2.523 -14.071  -5.397  1.00 62.55           O  
ANISOU   93  O   HOH A  99    14341   3105   6317   4648    378   1918       O  
HETATM   94  O   HOH A 100     -13.931  -1.467 -17.627  1.00 37.65           O  
ANISOU   94  O   HOH A 100     6991   3871   3443   -430   1230   -412       O  
HETATM   95  O   HOH A 105      14.954   8.018 -12.998  1.00 40.92           O  
ANISOU   95  O   HOH A 105     4024   8550   2973   2491    141   1484       O  
HETATM   96  O   HOH A 124       3.660   1.263 -28.149  1.00 29.98           O  
ANISOU   96  O   HOH A 124     3807   4784   2797     44   -996    835       O  
HETATM   97  O   HOH A 127      18.603   5.945  -8.250  1.00 38.76           O  
ANISOU   97  O   HOH A 127     4083   5345   5298  -1121   1766  -1292       O  
HETATM   98  O   HOH A 128     -14.075  -3.071 -20.031  1.00 35.24           O  
ANISOU   98  O   HOH A 128     5140   5184   3065  -1221   1337   -491       O  
HETATM   99  O   HOH A 129     -17.299  -0.865 -18.151  1.00 80.62           O  
ANISOU   99  O   HOH A 129    15117  12894   2621  -7307   2049  -1509       O  
HETATM  100  O   HOH A 131       4.817  20.292 -24.483  1.00 48.62           O  
ANISOU  100  O   HOH A 131     5275   6916   6279   -669    551  -3156       O  
HETATM  101  O   HOH A 132       7.609  22.904 -21.401  1.00 36.70           O  
ANISOU  101  O   HOH A 132     5319   4534   4091   1054    -17    974       O  
HETATM  102  O   HOH A 133      11.499   1.627  -2.499  1.00 37.30           O  
ANISOU  102  O   HOH A 133     4728   6938   2504  -1634    741   -353       O  
HETATM  103  O   HOH A 134      -8.417  10.176  -5.816  1.00 31.11           O  
ANISOU  103  O   HOH A 134     3197   5356   3265    543    162   -407       O  
HETATM  104  O   HOH A 135      -7.481  11.875  -9.747  1.00 44.05           O  
ANISOU  104  O   HOH A 135     4775   7735   4227  -2833   1074   -135       O  
HETATM  105  O   HOH A 136       1.475  -6.599 -16.377  1.00 38.92           O  
HETATM  106  O   HOH A 148       7.921  16.017 -26.420  1.00 42.21           O  
HETATM  107  O   HOH A 153      -0.013  15.205  -4.702  1.00 33.51           O  
HETATM  108  O   HOH A 157     -11.050  -1.793 -14.417  1.00 35.90           O  
HETATM  109  O   HOH A 163      -3.742  17.971 -22.269  1.00 34.46           O  
HETATM  110  O   HOH A 169       9.808  15.314 -24.498  1.00 41.50           O  
HETATM  111  O   HOH A 173       7.602  11.372 -24.904  1.00 35.85           O  
HETATM  112  O   HOH A 174       6.014   9.490  -3.661  1.00 37.61           O  
HETATM  113 MG    MG A 201       7.441   6.653  -0.187  0.50 20.67          MG  
ANISOU  113 MG    MG A 201     3139   3127   1585   -318    -43    517      MG  
HETATM  114  C1  PGR A 907     -10.005  -0.600 -17.874  1.00 21.25           C  
ANISOU  114  C1  PGR A 907     2832   3318   1922   -227   -375    -12       C  
HETATM  115  O1  PGR A 907     -11.155  -1.433 -17.853  1.00 27.89           O  
ANISOU  115  O1  PGR A 907     3955   4007   2634   -313     15    265       O  
HETATM  116  C2  PGR A 907      -9.514  -0.478 -19.305  1.00 22.18           C  
ANISOU  116  C2  PGR A 907     2881   3233   2311      6   -124    240       C  
HETATM  117  O2  PGR A 907      -8.319   0.287 -19.376  1.00 28.42           O  
ANISOU  117  O2  PGR A 907     3884   3943   2972   -497   -578    -38       O  
HETATM  118  C3  PGR A 907     -10.553   0.184 -20.178  1.00 12.13           C  
ANISOU  118  C3  PGR A 907     1415   2288    905    330    -77    -84       C  
ATOM    119  N   PRO A1001      -4.475 -10.469  -7.839  1.00 23.99           N  
ANISOU  119  N   PRO A1001     3081   2999   3032     54    -47    -99       N  
ATOM    120  CA  PRO A1001      -3.664 -11.208  -6.887  1.00 23.50           C  
ANISOU  120  CA  PRO A1001     3061   2870   2998     26    -18    -31       C  
ATOM    121  C   PRO A1001      -3.849 -10.705  -5.464  1.00 22.61           C  
ANISOU  121  C   PRO A1001     2950   2728   2914     78    -26    -46       C  
ATOM    122  O   PRO A1001      -4.385  -9.619  -5.251  1.00 22.30           O  
ANISOU  122  O   PRO A1001     3088   2426   2958     99   -175   -158       O  
ATOM    123  CB  PRO A1001      -2.240 -10.923  -7.356  1.00 23.71           C  
ANISOU  123  CB  PRO A1001     3058   2980   2968     89    -65     44       C  
ATOM    124  CG  PRO A1001      -2.317  -9.576  -7.950  1.00 25.39           C  
ANISOU  124  CG  PRO A1001     3285   3173   3186    -14     64    -10       C  
ATOM    125  CD  PRO A1001      -3.674  -9.494  -8.598  1.00 25.09           C  
ANISOU  125  CD  PRO A1001     3216   3229   3088     48    -50    -79       C  
ATOM    126  N   GLN A1002      -3.406 -11.503  -4.505  1.00 22.47           N  
ANISOU  126  N   GLN A1002     2881   2669   2987     15     46     80       N  
ATOM    127  CA  GLN A1002      -3.196 -11.034  -3.143  1.00 21.24           C  
ANISOU  127  CA  GLN A1002     2691   2524   2853     47     -2     71       C  
ATOM    128  C   GLN A1002      -1.700 -10.981  -2.870  1.00 21.08           C  
ANISOU  128  C   GLN A1002     2600   2390   3018    192    -35     52       C  
ATOM    129  O   GLN A1002      -0.997 -11.984  -3.034  1.00 23.44           O  
ANISOU  129  O   GLN A1002     2727   2349   3828    206   -292    -19       O  
ATOM    130  CB  GLN A1002      -3.887 -11.965  -2.148  1.00 21.87           C  
ANISOU  130  CB  GLN A1002     2875   2443   2991     70    -17     29       C  
ATOM    131  CG  GLN A1002      -3.564 -11.665  -0.701  1.00 23.53           C  
ANISOU  131  CG  GLN A1002     3074   2686   3179     84    140    225       C  
ATOM    132  CD  GLN A1002      -4.561 -12.290   0.258  1.00 24.38           C  
ANISOU  132  CD  GLN A1002     3095   2886   3281     51    238    293       C  
ATOM    133  NE2 GLN A1002      -4.111 -13.281   1.002  1.00 30.58           N  
ANISOU  133  NE2 GLN A1002     3857   3586   4174     64    218    769       N  
ATOM    134  OE1 GLN A1002      -5.726 -11.882   0.326  1.00 29.75           O  
ANISOU  134  OE1 GLN A1002     3919   3514   3869     52    442    650       O  
ATOM    135  N   ILE A1003      -1.219  -9.805  -2.474  1.00 18.01           N  
ANISOU  135  N   ILE A1003     2206   2208   2426    121   -199    115       N  
ATOM    136  CA  ILE A1003       0.209  -9.547  -2.335  1.00 18.20           C  
ANISOU  136  CA  ILE A1003     2329   2217   2368     48     14    127       C  
ATOM    137  C   ILE A1003       0.523  -9.242  -0.873  1.00 17.18           C  
ANISOU  137  C   ILE A1003     2140   2133   2253    110    -80    243       C  
ATOM    138  O   ILE A1003       0.000  -8.281  -0.308  1.00 16.92           O  
ANISOU  138  O   ILE A1003     2142   2097   2189    107    -75    403       O  
ATOM    139  CB  ILE A1003       0.647  -8.366  -3.233  1.00 17.76           C  
ANISOU  139  CB  ILE A1003     2213   2237   2295    192    -40    151       C  
ATOM    140  CG1 ILE A1003       0.376  -8.709  -4.703  1.00 19.95           C  
ANISOU  140  CG1 ILE A1003     2566   2418   2593     47   -135    259       C  
ATOM    141  CG2 ILE A1003       2.124  -8.031  -3.013  1.00 19.19           C  
ANISOU  141  CG2 ILE A1003     2437   2465   2386     71    -66    174       C  
ATOM    142  CD1 ILE A1003       0.575  -7.565  -5.646  1.00 18.33           C  
ANISOU  142  CD1 ILE A1003     2439   2294   2230    -16     -5     40       C  
ATOM    143  N   THR A1004       1.351 -10.083  -0.253  1.00 16.35           N  
ANISOU  143  N   THR A1004     1918   1969   2324    167     -2    269       N  
ATOM    144  CA  THR A1004       1.842  -9.803   1.086  1.00 16.56           C  
ANISOU  144  CA  THR A1004     2061   1972   2258    192     57    253       C  
ATOM    145  C   THR A1004       3.015  -8.832   1.033  1.00 16.56           C  
ANISOU  145  C   THR A1004     2103   2030   2156    103     15    336       C  
ATOM    146  O   THR A1004       3.541  -8.519  -0.041  1.00 17.70           O  
ANISOU  146  O   THR A1004     2096   2409   2219    162    213    194       O  
ATOM    147  CB  THR A1004       2.301 -11.087   1.814  1.00 17.41           C  
ANISOU  147  CB  THR A1004     2220   2098   2295    195    141    322       C  
ATOM    148  CG2 THR A1004       1.140 -12.055   1.967  1.00 17.70           C  
ANISOU  148  CG2 THR A1004     2169   1997   2558    179    -37    129       C  
ATOM    149  OG1 THR A1004       3.365 -11.702   1.083  1.00 19.87           O  
ANISOU  149  OG1 THR A1004     2681   2191   2677    670    301    540       O  
ATOM    150  N   LEU A1005       3.412  -8.343   2.199  1.00 15.13           N  
ANISOU  150  N   LEU A1005     1921   1866   1961    228     -8    360       N  
ATOM    151  CA  LEU A1005       4.276  -7.175   2.271  1.00 15.28           C  
ANISOU  151  CA  LEU A1005     2017   1856   1931     75     47    280       C  
ATOM    152  C   LEU A1005       5.595  -7.446   3.002  1.00 14.84           C  
ANISOU  152  C   LEU A1005     1966   1712   1959     21     11    256       C  
ATOM    153  O   LEU A1005       6.266  -6.529   3.462  1.00 14.75           O  
ANISOU  153  O   LEU A1005     1957   1864   1781    156    170    389       O  
ATOM    154  CB  LEU A1005       3.507  -6.004   2.880  1.00 15.26           C  
ANISOU  154  CB  LEU A1005     2105   1838   1854    235     34    453       C  
ATOM    155  CG  LEU A1005       2.334  -5.535   2.009  1.00 15.05           C  
ANISOU  155  CG  LEU A1005     2022   1702   1991    248     37    356       C  
ATOM    156  CD1 LEU A1005       1.426  -4.579   2.755  1.00 16.45           C  
ANISOU  156  CD1 LEU A1005     2246   1979   2023    440      8    323       C  
ATOM    157  CD2 LEU A1005       2.861  -4.886   0.735  1.00 16.44           C  
ANISOU  157  CD2 LEU A1005     2005   2294   1944     81     42    382       C  
ATOM    158  N   TRP A1006       5.977  -8.719   3.072  1.00 14.92           N  
ANISOU  158  N   TRP A1006     1874   1736   2057     88     56    320       N  
ATOM    159  CA  TRP A1006       7.303  -9.089   3.572  1.00 14.34           C  
ANISOU  159  CA  TRP A1006     1834   1814   1799     79     42    301       C  
ATOM    160  C   TRP A1006       8.423  -8.497   2.739  1.00 15.93           C  
ANISOU  160  C   TRP A1006     2028   2118   1906    -86    -67    267       C  
ATOM    161  O   TRP A1006       9.474  -8.133   3.269  1.00 18.70           O  
ANISOU  161  O   TRP A1006     2168   2717   2220   -257    -78    813       O  
ATOM    162  CB  TRP A1006       7.457 -10.608   3.610  1.00 13.63           C  
ANISOU  162  CB  TRP A1006     2013   1685   1480     -4     94    100       C  
ATOM    163  CG  TRP A1006       6.480 -11.270   4.504  1.00 12.23           C  
ANISOU  163  CG  TRP A1006     2037   1310   1300     36     60    132       C  
ATOM    164  CD1 TRP A1006       5.308 -11.860   4.141  1.00 11.36           C  
ANISOU  164  CD1 TRP A1006     1726   1445   1145    -74    -50    115       C  
ATOM    165  CD2 TRP A1006       6.578 -11.406   5.927  1.00 11.60           C  
ANISOU  165  CD2 TRP A1006     2302    819   1284    -41    -68    -52       C  
ATOM    166  CE2 TRP A1006       5.432 -12.094   6.358  1.00 12.54           C  
ANISOU  166  CE2 TRP A1006     2667   1114    982    -76    175   -140       C  
ATOM    167  CE3 TRP A1006       7.529 -11.020   6.873  1.00 12.57           C  
ANISOU  167  CE3 TRP A1006     2299   1306   1170     75    195   -226       C  
ATOM    168  NE1 TRP A1006       4.668 -12.359   5.251  1.00 11.83           N  
ANISOU  168  NE1 TRP A1006     2140   1157   1196    -12    135    -51       N  
ATOM    169  CZ2 TRP A1006       5.212 -12.405   7.700  1.00 13.66           C  
ANISOU  169  CZ2 TRP A1006     2193   1760   1237   -315      3    -81       C  
ATOM    170  CZ3 TRP A1006       7.306 -11.326   8.197  1.00 13.79           C  
ANISOU  170  CZ3 TRP A1006     2317   1638   1284   -103     24   -140       C  
ATOM    171  CH2 TRP A1006       6.163 -12.016   8.597  1.00 14.40           C  
ANISOU  171  CH2 TRP A1006     2318   1894   1259    -61    175   -241       C  
ATOM    172  N  ALYS A1007       8.212  -8.389   1.431  0.40 15.77           N  
ANISOU  172  N  ALYS A1007     1918   2139   1935    -28    -57    332       N  
ATOM    173  N  BLYS A1007       8.195  -8.458   1.432  0.60 15.74           N  
ANISOU  173  N  BLYS A1007     1882   2150   1949    -23    -85    424       N  
ATOM    174  CA ALYS A1007       9.174  -7.720   0.556  0.40 15.76           C  
ANISOU  174  CA ALYS A1007     2019   2081   1887     14    -18    184       C  
ATOM    175  CA BLYS A1007       9.117  -7.855   0.495  0.60 15.60           C  
ANISOU  175  CA BLYS A1007     2019   2023   1882      9    -43    271       C  
ATOM    176  C  ALYS A1007       8.510  -6.563  -0.178  0.40 15.10           C  
ANISOU  176  C  ALYS A1007     1961   2044   1733     31     -8    177       C  
ATOM    177  C  BLYS A1007       8.474  -6.592  -0.053  0.60 15.21           C  
ANISOU  177  C  BLYS A1007     1973   1974   1830      9    -77    245       C  
ATOM    178  O  ALYS A1007       7.284  -6.475  -0.232  0.40 14.10           O  
ANISOU  178  O  ALYS A1007     1938   2216   1199     26    168    276       O  
ATOM    179  O  BLYS A1007       7.283  -6.339   0.142  0.60 14.20           O  
ANISOU  179  O  BLYS A1007     1910   1937   1546    -71   -162    430       O  
ATOM    180  CB ALYS A1007       9.763  -8.707  -0.451  0.40 16.50           C  
ANISOU  180  CB ALYS A1007     2082   2092   2092     57    -43    181       C  
ATOM    181  CB BLYS A1007       9.410  -8.813  -0.660  0.60 17.48           C  
ANISOU  181  CB BLYS A1007     2242   2107   2292    108    -86    278       C  
ATOM    182  CG ALYS A1007       8.750  -9.304  -1.426  0.40 17.65           C  
ANISOU  182  CG ALYS A1007     2301   2120   2282    101   -142     -2       C  
ATOM    183  CG BLYS A1007       9.583 -10.268  -0.249  0.60 20.42           C  
ANISOU  183  CG BLYS A1007     2695   2464   2599     49     12    249       C  
ATOM    184  CD ALYS A1007       9.448 -10.110  -2.516  0.40 19.10           C  
ANISOU  184  CD ALYS A1007     2368   2467   2422     15    -99     61       C  
ATOM    185  CD BLYS A1007      11.006 -10.571   0.149  0.60 24.50           C  
ANISOU  185  CD BLYS A1007     3143   3066   3099   -180    -80    215       C  
ATOM    186  CE ALYS A1007       8.521 -11.135  -3.140  0.40 20.76           C  
ANISOU  186  CE ALYS A1007     2578   2657   2651    -17    -65    -72       C  
ATOM    187  CE BLYS A1007      11.135 -11.985   0.711  0.60 25.47           C  
ANISOU  187  CE BLYS A1007     3286   3112   3278    -76   -138      9       C  
ATOM    188  NZ ALYS A1007       9.100 -11.714  -4.380  0.40 23.63           N1+
ANISOU  188  NZ ALYS A1007     2905   3043   3030     -7   -253     63       N1+
ATOM    189  NZ BLYS A1007      11.461 -12.985  -0.347  0.60 28.03           N1+
ANISOU  189  NZ BLYS A1007     3540   3247   3861   -227   -147   -301       N1+
ATOM    190  N  AARG A1008       9.316  -5.669  -0.738  0.50 14.52           N  
ANISOU  190  N  AARG A1008     1896   1988   1633     21     64    170       N  
ATOM    191  N  BARG A1008       9.271  -5.793  -0.745  0.50 14.17           N  
ANISOU  191  N  BARG A1008     1868   1887   1628     18      0    242       N  
ATOM    192  CA AARG A1008       8.756  -4.556  -1.489  0.50 15.08           C  
ANISOU  192  CA AARG A1008     2011   1995   1722     56    -17    132       C  
ATOM    193  CA BARG A1008       8.736  -4.639  -1.452  0.50 14.56           C  
ANISOU  193  CA BARG A1008     1960   1926   1644     56    -31    175       C  
ATOM    194  C  AARG A1008       7.825  -5.117  -2.563  0.50 14.60           C  
ANISOU  194  C  AARG A1008     2051   1966   1529     48     48    134       C  
ATOM    195  C  BARG A1008       7.818  -5.134  -2.569  0.50 14.46           C  
ANISOU  195  C  BARG A1008     2041   1944   1509     48     42    152       C  
ATOM    196  O  AARG A1008       8.186  -6.067  -3.262  0.50 14.86           O  
ANISOU  196  O  AARG A1008     2333   1837   1477    108    -51    187       O  
ATOM    197  O  BARG A1008       8.184  -6.052  -3.308  0.50 14.86           O  
ANISOU  197  O  BARG A1008     2339   1837   1468    108    -29    172       O  
ATOM    198  CB AARG A1008       9.864  -3.724  -2.126  0.50 15.41           C  
ANISOU  198  CB AARG A1008     2069   2061   1725    -58     -2     93       C  
ATOM    199  CB BARG A1008       9.870  -3.789  -2.028  0.50 14.91           C  
ANISOU  199  CB BARG A1008     2030   2032   1603    -67     -3    146       C  
ATOM    200  CG AARG A1008      10.740  -2.972  -1.135  0.50 16.53           C  
ANISOU  200  CG AARG A1008     2111   2179   1991   -105      0     85       C  
ATOM    201  CG BARG A1008      10.786  -3.174  -0.976  0.50 14.54           C  
ANISOU  201  CG BARG A1008     1866   1969   1687    -93     -4    157       C  
ATOM    202  CD AARG A1008      11.595  -1.937  -1.855  0.50 19.57           C  
ANISOU  202  CD AARG A1008     2547   2483   2403    -55    129    -11       C  
ATOM    203  CD BARG A1008      11.962  -2.428  -1.603  0.50 16.40           C  
ANISOU  203  CD BARG A1008     2224   2186   1820    -30     99    143       C  
ATOM    204  NE AARG A1008      12.530  -2.571  -2.781  0.50 23.38           N  
ANISOU  204  NE AARG A1008     2927   3043   2913   -248    316     54       N  
ATOM    205  NE BARG A1008      12.689  -1.656  -0.603  0.50 16.26           N  
ANISOU  205  NE BARG A1008     2082   2480   1614   -222    275    243       N  
ATOM    206  CZ AARG A1008      12.918  -2.056  -3.947  0.50 25.15           C  
ANISOU  206  CZ AARG A1008     3202   3197   3156   -160     41     26       C  
ATOM    207  CZ BARG A1008      13.830  -1.012  -0.828  0.50 20.98           C  
ANISOU  207  CZ BARG A1008     2526   3032   2410   -214    280     32       C  
ATOM    208  NH1AARG A1008      12.460  -0.880  -4.369  0.50 25.15           N1+
ANISOU  208  NH1AARG A1008     3294   3225   3033   -429    195     66       N1+
ATOM    209  NH1BARG A1008      14.388  -1.033  -2.031  0.50 22.95           N1+
ANISOU  209  NH1BARG A1008     3038   3338   2344   -119    535    -22       N1+
ATOM    210  NH2AARG A1008      13.774  -2.730  -4.697  0.50 23.88           N  
ANISOU  210  NH2AARG A1008     3295   2985   2790   -145    373    -72       N  
ATOM    211  NH2BARG A1008      14.416  -0.343   0.157  0.50 20.60           N  
ANISOU  211  NH2BARG A1008     2278   3366   2182   -207    565    -53       N  
ATOM    212  N   PRO A1009       6.614  -4.547  -2.683  1.00 14.21           N  
ANISOU  212  N   PRO A1009     2058   1939   1400    105    -18    158       N  
ATOM    213  CA  PRO A1009       5.645  -4.980  -3.684  1.00 15.13           C  
ANISOU  213  CA  PRO A1009     2183   2011   1552     60    -57    175       C  
ATOM    214  C   PRO A1009       5.971  -4.505  -5.103  1.00 15.12           C  
ANISOU  214  C   PRO A1009     2282   1993   1469     62   -216     86       C  
ATOM    215  O   PRO A1009       5.297  -3.646  -5.670  1.00 15.01           O  
ANISOU  215  O   PRO A1009     2370   1899   1433     99   -288     77       O  
ATOM    216  CB  PRO A1009       4.328  -4.417  -3.157  1.00 15.06           C  
ANISOU  216  CB  PRO A1009     2222   2088   1411     15   -218    301       C  
ATOM    217  CG  PRO A1009       4.705  -3.205  -2.403  1.00 15.25           C  
ANISOU  217  CG  PRO A1009     2220   2025   1547    236    -47    124       C  
ATOM    218  CD  PRO A1009       6.060  -3.495  -1.807  1.00 14.60           C  
ANISOU  218  CD  PRO A1009     2099   1991   1456    219   -119    230       C  
ATOM    219  N   LEU A1010       7.028  -5.079  -5.661  1.00 15.10           N  
ANISOU  219  N   LEU A1010     2361   1927   1448    164    -96    217       N  
ATOM    220  CA  LEU A1010       7.432  -4.806  -7.025  1.00 16.62           C  
ANISOU  220  CA  LEU A1010     2494   2071   1750     47    -10    106       C  
ATOM    221  C   LEU A1010       6.667  -5.724  -7.973  1.00 16.97           C  
ANISOU  221  C   LEU A1010     2787   1945   1715    108    -19    152       C  
ATOM    222  O   LEU A1010       6.545  -6.928  -7.741  1.00 20.06           O  
ANISOU  222  O   LEU A1010     3429   2169   2020    182    -70    101       O  
ATOM    223  CB  LEU A1010       8.932  -5.038  -7.168  1.00 17.49           C  
ANISOU  223  CB  LEU A1010     2508   2207   1930    104     40    113       C  
ATOM    224  CG  LEU A1010       9.818  -4.118  -6.331  1.00 18.26           C  
ANISOU  224  CG  LEU A1010     2317   2465   2152   -221    146    245       C  
ATOM    225  CD1 LEU A1010      11.263  -4.599  -6.343  1.00 24.44           C  
ANISOU  225  CD1 LEU A1010     3325   2779   3182   -143   -217    267       C  
ATOM    226  CD2 LEU A1010       9.721  -2.678  -6.821  1.00 24.22           C  
ANISOU  226  CD2 LEU A1010     2985   3187   3028    -78   -145   -205       C  
ATOM    227  N   VAL A1011       6.144  -5.141  -9.043  1.00 17.18           N  
ANISOU  227  N   VAL A1011     2755   1967   1806    152   -144     84       N  
ATOM    228  CA  VAL A1011       5.423  -5.903 -10.042  1.00 18.59           C  
ANISOU  228  CA  VAL A1011     2812   2209   2040     95    -92    -56       C  
ATOM    229  C   VAL A1011       5.916  -5.511 -11.420  1.00 19.35           C  
ANISOU  229  C   VAL A1011     2938   2223   2190     56    -73    -46       C  
ATOM    230  O   VAL A1011       6.546  -4.467 -11.598  1.00 19.43           O  
ANISOU  230  O   VAL A1011     3297   2338   1745    117    -60    -17       O  
ATOM    231  CB  VAL A1011       3.902  -5.676  -9.957  1.00 20.19           C  
ANISOU  231  CB  VAL A1011     2980   2428   2260    -16   -207    -71       C  
ATOM    232  CG1 VAL A1011       3.358  -6.119  -8.599  1.00 22.52           C  
ANISOU  232  CG1 VAL A1011     3102   2823   2630     19     64   -208       C  
ATOM    233  CG2 VAL A1011       3.568  -4.224 -10.226  1.00 21.56           C  
ANISOU  233  CG2 VAL A1011     3287   2536   2367    224   -219   -129       C  
ATOM    234  N   THR A1012       5.634  -6.365 -12.398  1.00 20.00           N  
ANISOU  234  N   THR A1012     3103   2425   2069    102   -132    -69       N  
ATOM    235  CA  THR A1012       5.892  -6.039 -13.786  1.00 20.80           C  
ANISOU  235  CA  THR A1012     2897   2630   2376    158    -41   -130       C  
ATOM    236  C   THR A1012       4.741  -5.225 -14.336  1.00 18.98           C  
ANISOU  236  C   THR A1012     2566   2544   2099     14    -97     34       C  
ATOM    237  O   THR A1012       3.564  -5.528 -14.095  1.00 21.25           O  
ANISOU  237  O   THR A1012     3069   2771   2230   -132   -267     71       O  
ATOM    238  CB  THR A1012       6.073  -7.310 -14.614  1.00 22.83           C  
ANISOU  238  CB  THR A1012     3231   2909   2533    143   -122   -190       C  
ATOM    239  CG2 THR A1012       6.371  -6.966 -16.070  0.50 21.01           C  
ANISOU  239  CG2 THR A1012     3094   2729   2158    187    -37   -138       C  
ATOM    240  OG1 THR A1012       7.155  -8.068 -14.068  1.00 25.66           O  
ANISOU  240  OG1 THR A1012     3727   3205   2817    792    -52   -515       O  
ATOM    241  N   ILE A1013       5.084  -4.159 -15.044  1.00 18.46           N  
ANISOU  241  N   ILE A1013     2408   2649   1956     60    -97     33       N  
ATOM    242  CA  ILE A1013       4.086  -3.379 -15.741  1.00 17.25           C  
ANISOU  242  CA  ILE A1013     2295   2434   1823     18     37    123       C  
ATOM    243  C   ILE A1013       4.395  -3.354 -17.236  1.00 16.90           C  
ANISOU  243  C   ILE A1013     2073   2651   1695    -14    158     79       C  
ATOM    244  O   ILE A1013       5.555  -3.461 -17.652  1.00 18.32           O  
ANISOU  244  O   ILE A1013     2161   3061   1738    132     96     49       O  
ATOM    245  CB  ILE A1013       4.005  -1.953 -15.185  1.00 16.66           C  
ANISOU  245  CB  ILE A1013     2138   2412   1779    108     18    213       C  
ATOM    246  CG1 ILE A1013       5.323  -1.211 -15.418  1.00 18.24           C  
ANISOU  246  CG1 ILE A1013     2551   2212   2164   -105     76    259       C  
ATOM    247  CG2 ILE A1013       3.688  -1.996 -13.699  1.00 18.26           C  
ANISOU  247  CG2 ILE A1013     2528   2559   1848   -109    199     31       C  
ATOM    248  CD1 ILE A1013       5.243   0.264 -15.192  1.00 19.02           C  
ANISOU  248  CD1 ILE A1013     2568   2526   2132      9    120   -140       C  
ATOM    249  N   LYS A1014       3.340  -3.232 -18.029  1.00 14.99           N  
ANISOU  249  N   LYS A1014     2075   2127   1493     -6     88    232       N  
ATOM    250  CA  LYS A1014       3.470  -2.998 -19.458  1.00 16.16           C  
ANISOU  250  CA  LYS A1014     2150   2265   1724    -35     61     76       C  
ATOM    251  C   LYS A1014       2.981  -1.591 -19.728  1.00 15.23           C  
ANISOU  251  C   LYS A1014     2098   2186   1501    -68     33     72       C  
ATOM    252  O   LYS A1014       1.864  -1.245 -19.376  1.00 14.53           O  
ANISOU  252  O   LYS A1014     1805   2159   1554     50     24    200       O  
ATOM    253  CB  LYS A1014       2.577  -3.954 -20.242  1.00 18.09           C  
ANISOU  253  CB  LYS A1014     2430   2433   2009    -96    120     78       C  
ATOM    254  CG  LYS A1014       2.986  -5.400 -20.231  1.00 21.51           C  
ANISOU  254  CG  LYS A1014     2898   2878   2395   -105   -169    -74       C  
ATOM    255  CD  LYS A1014       2.277  -6.126 -21.375  1.00 23.44           C  
ANISOU  255  CD  LYS A1014     3104   2968   2831    -59   -197   -113       C  
ATOM    256  CE  LYS A1014       2.522  -7.605 -21.375  1.00 26.63           C  
ANISOU  256  CE  LYS A1014     3368   3313   3435    -42   -217   -108       C  
ATOM    257  NZ  LYS A1014       1.672  -8.250 -22.412  1.00 26.50           N1+
ANISOU  257  NZ  LYS A1014     3844   3358   2865   -216   -410   -264       N1+
ATOM    258  N   ILE A1015       3.815  -0.791 -20.368  1.00 14.12           N  
ANISOU  258  N   ILE A1015     1901   2024   1440    -36    167     -1       N  
ATOM    259  CA  ILE A1015       3.452   0.576 -20.691  1.00 14.56           C  
ANISOU  259  CA  ILE A1015     1921   2032   1579    -16    136     96       C  
ATOM    260  C   ILE A1015       4.309   1.064 -21.847  1.00 15.29           C  
ANISOU  260  C   ILE A1015     1983   2202   1623     67    147    141       C  
ATOM    261  O   ILE A1015       5.501   0.771 -21.911  1.00 15.76           O  
ANISOU  261  O   ILE A1015     1930   2501   1555    -50    284     26       O  
ATOM    262  CB  ILE A1015       3.643   1.510 -19.462  1.00 14.34           C  
ANISOU  262  CB  ILE A1015     1802   2023   1622    -49     47      0       C  
ATOM    263  CG1 ILE A1015       3.233   2.946 -19.803  1.00 15.26           C  
ANISOU  263  CG1 ILE A1015     2015   2020   1760   -128    168     17       C  
ATOM    264  CG2 ILE A1015       5.083   1.432 -18.943  1.00 15.91           C  
ANISOU  264  CG2 ILE A1015     2228   2090   1726    -49    102    -29       C  
ATOM    265  CD1 ILE A1015       3.267   3.917 -18.639  1.00 17.01           C  
ANISOU  265  CD1 ILE A1015     2267   2245   1950     30     19    152       C  
ATOM    266  N   GLY A1016       3.688   1.805 -22.761  1.00 15.72           N  
ANISOU  266  N   GLY A1016     2035   2332   1604    111    255    231       N  
ATOM    267  CA  GLY A1016       4.419   2.420 -23.866  1.00 16.66           C  
ANISOU  267  CA  GLY A1016     2141   2319   1869    -58    231    171       C  
ATOM    268  C   GLY A1016       5.176   1.420 -24.713  1.00 16.94           C  
ANISOU  268  C   GLY A1016     2202   2326   1907     11    185    113       C  
ATOM    269  O   GLY A1016       6.229   1.742 -25.280  1.00 18.51           O  
ANISOU  269  O   GLY A1016     2435   2708   1887    -83    438    146       O  
ATOM    270  N   GLY A1017       4.659   0.200 -24.806  1.00 16.15           N  
ANISOU  270  N   GLY A1017     2101   2233   1801     73    226     37       N  
ATOM    271  CA  GLY A1017       5.290  -0.818 -25.640  1.00 16.93           C  
ANISOU  271  CA  GLY A1017     2133   2384   1915     98    257      2       C  
ATOM    272  C   GLY A1017       6.505  -1.448 -24.975  1.00 18.07           C  
ANISOU  272  C   GLY A1017     2222   2576   2065    177    219    -58       C  
ATOM    273  O   GLY A1017       7.258  -2.172 -25.623  1.00 20.00           O  
ANISOU  273  O   GLY A1017     2478   2967   2154    315    218   -450       O  
ATOM    274  N   GLN A1018       6.674  -1.193 -23.675  1.00 17.93           N  
ANISOU  274  N   GLN A1018     2178   2596   2036    185    178    -87       N  
ATOM    275  CA  GLN A1018       7.818  -1.665 -22.903  1.00 19.41           C  
ANISOU  275  CA  GLN A1018     2414   2700   2258     36    170    -20       C  
ATOM    276  C   GLN A1018       7.358  -2.451 -21.670  1.00 19.07           C  
ANISOU  276  C   GLN A1018     2389   2623   2232     41    214      9       C  
ATOM    277  O   GLN A1018       6.232  -2.289 -21.220  1.00 19.57           O  
ANISOU  277  O   GLN A1018     2311   2741   2381    262    561    -38       O  
ATOM    278  CB  GLN A1018       8.640  -0.469 -22.409  1.00 20.80           C  
ANISOU  278  CB  GLN A1018     2597   2823   2481    -39    132     52       C  
ATOM    279  CG  GLN A1018       9.195   0.450 -23.485  1.00 24.50           C  
ANISOU  279  CG  GLN A1018     2912   3228   3169     12    -16    -32       C  
ATOM    280  CD  GLN A1018      10.274   1.362 -22.923  0.50 22.43           C  
ANISOU  280  CD  GLN A1018     2636   2846   3040     16    127   -119       C  
ATOM    281  NE2 GLN A1018      11.472   0.816 -22.747  0.50 25.42           N  
ANISOU  281  NE2 GLN A1018     3033   3047   3575    -15    -87   -364       N  
ATOM    282  OE1 GLN A1018      10.029   2.532 -22.628  0.50 23.71           O  
ANISOU  282  OE1 GLN A1018     2727   2602   3678    356    337   -183       O  
ATOM    283  N   LEU A1019       8.256  -3.262 -21.118  1.00 20.32           N  
ANISOU  283  N   LEU A1019     2460   2941   2317    120    221    -35       N  
ATOM    284  CA  LEU A1019       8.079  -3.879 -19.805  1.00 22.09           C  
ANISOU  284  CA  LEU A1019     2641   3077   2673     19    108    -34       C  
ATOM    285  C   LEU A1019       8.977  -3.179 -18.796  1.00 22.15           C  
ANISOU  285  C   LEU A1019     2544   3287   2582     35     57    -47       C  
ATOM    286  O   LEU A1019      10.160  -2.942 -19.061  1.00 23.07           O  
ANISOU  286  O   LEU A1019     2335   3954   2477     30     92      3       O  
ATOM    287  CB  LEU A1019       8.477  -5.355 -19.834  1.00 23.60           C  
ANISOU  287  CB  LEU A1019     2709   3212   3043     36    150      8       C  
ATOM    288  CG  LEU A1019       7.586  -6.359 -20.560  1.00 26.58           C  
ANISOU  288  CG  LEU A1019     3388   3445   3263     56     85   -201       C  
ATOM    289  CD1 LEU A1019       8.309  -7.699 -20.676  1.00 29.63           C  
ANISOU  289  CD1 LEU A1019     3758   3609   3890    128     26    -92       C  
ATOM    290  CD2 LEU A1019       6.261  -6.541 -19.844  1.00 29.56           C  
ANISOU  290  CD2 LEU A1019     3611   3778   3839    -18    144   -244       C  
ATOM    291  N   LYS A1020       8.429  -2.873 -17.629  1.00 20.73           N  
ANISOU  291  N   LYS A1020     2323   3168   2383     -6     15     85       N  
ATOM    292  CA  LYS A1020       9.224  -2.285 -16.567  1.00 21.29           C  
ANISOU  292  CA  LYS A1020     2634   2981   2472     13     76     47       C  
ATOM    293  C   LYS A1020       8.819  -2.899 -15.243  1.00 20.59           C  
ANISOU  293  C   LYS A1020     2546   2836   2441    -35    -11    178       C  
ATOM    294  O   LYS A1020       7.798  -3.580 -15.152  1.00 22.24           O  
ANISOU  294  O   LYS A1020     2724   3255   2469      4    -54    541       O  
ATOM    295  CB  LYS A1020       9.028  -0.772 -16.539  1.00 21.40           C  
ANISOU  295  CB  LYS A1020     2745   2954   2431   -106    -41    178       C  
ATOM    296  CG  LYS A1020       9.439  -0.090 -17.841  1.00 23.85           C  
ANISOU  296  CG  LYS A1020     3171   3247   2642    -44    -90    120       C  
ATOM    297  CD  LYS A1020       9.298   1.410 -17.788  0.50 23.30           C  
ANISOU  297  CD  LYS A1020     2939   3160   2753     14    127     88       C  
ATOM    298  CE  LYS A1020      10.070   2.053 -18.933  0.50 25.28           C  
ANISOU  298  CE  LYS A1020     3260   3260   3083    -21    157    139       C  
ATOM    299  NZ  LYS A1020      11.530   2.068 -18.664  0.50 25.74           N1+
ANISOU  299  NZ  LYS A1020     3111   3529   3139    -89     99    -87       N1+
ATOM    300  N  AGLU A1021       9.647  -2.673 -14.229  0.50 20.18           N  
ANISOU  300  N  AGLU A1021     2601   2711   2352     68     30     36       N  
ATOM    301  N  BGLU A1021       9.630  -2.663 -14.220  0.50 19.91           N  
ANISOU  301  N  BGLU A1021     2558   2695   2312     71     27     19       N  
ATOM    302  CA AGLU A1021       9.323  -3.035 -12.855  0.50 20.11           C  
ANISOU  302  CA AGLU A1021     2628   2654   2359     65      2     53       C  
ATOM    303  CA BGLU A1021       9.285  -3.057 -12.862  0.50 19.90           C  
ANISOU  303  CA BGLU A1021     2593   2632   2334     77     -6     43       C  
ATOM    304  C  AGLU A1021       8.897  -1.768 -12.122  0.50 19.11           C  
ANISOU  304  C  AGLU A1021     2519   2530   2209     94    -25     18       C  
ATOM    305  C  BGLU A1021       8.947  -1.805 -12.063  0.50 19.01           C  
ANISOU  305  C  BGLU A1021     2517   2518   2187     92    -38     28       C  
ATOM    306  O  AGLU A1021       9.467  -0.700 -12.342  0.50 19.31           O  
ANISOU  306  O  AGLU A1021     2572   2650   2115    148     87    -98       O  
ATOM    307  O  BGLU A1021       9.635  -0.791 -12.166  0.50 18.95           O  
ANISOU  307  O  BGLU A1021     2586   2561   2053    102     82     -8       O  
ATOM    308  CB AGLU A1021      10.544  -3.648 -12.166  0.50 20.42           C  
ANISOU  308  CB AGLU A1021     2755   2624   2379     65     -6     37       C  
ATOM    309  CB BGLU A1021      10.452  -3.799 -12.209  0.50 20.84           C  
ANISOU  309  CB BGLU A1021     2800   2687   2431     88    -23     11       C  
ATOM    310  CG AGLU A1021      10.245  -4.265 -10.808  0.50 21.32           C  
ANISOU  310  CG AGLU A1021     2808   2748   2542     82     15    113       C  
ATOM    311  CG BGLU A1021      10.821  -5.098 -12.909  0.50 23.12           C  
ANISOU  311  CG BGLU A1021     2923   2955   2906    191    -95    -17       C  
ATOM    312  CD AGLU A1021      11.399  -5.092 -10.280  0.50 22.95           C  
ANISOU  312  CD AGLU A1021     3065   2911   2743      4    -13    103       C  
ATOM    313  CD BGLU A1021       9.814  -6.207 -12.661  0.50 27.32           C  
ANISOU  313  CD BGLU A1021     3476   3556   3347     87   -113    -53       C  
ATOM    314  OE1AGLU A1021      12.468  -4.512  -9.990  0.50 26.64           O  
ANISOU  314  OE1AGLU A1021     3307   3812   3000     43   -287    128       O  
ATOM    315  OE1BGLU A1021       9.672  -6.637 -11.496  0.50 31.42           O  
ANISOU  315  OE1BGLU A1021     3832   4013   4094    266   -149   -300       O  
ATOM    316  OE2AGLU A1021      11.237  -6.324 -10.161  0.50 27.76           O1-
ANISOU  316  OE2AGLU A1021     4056   3094   3396    166    -33    191       O1-
ATOM    317  OE2BGLU A1021       9.170  -6.656 -13.636  0.50 30.26           O1-
ANISOU  317  OE2BGLU A1021     3703   4045   3748    347   -239    140       O1-
ATOM    318  N   ALA A1022       7.886  -1.882 -11.269  1.00 17.87           N  
ANISOU  318  N   ALA A1022     2562   2362   1864     99   -130    257       N  
ATOM    319  CA  ALA A1022       7.448  -0.749 -10.481  1.00 17.03           C  
ANISOU  319  CA  ALA A1022     2367   2306   1796     59    -38    146       C  
ATOM    320  C   ALA A1022       6.898  -1.193  -9.141  1.00 15.84           C  
ANISOU  320  C   ALA A1022     2487   2054   1477     25     17    153       C  
ATOM    321  O   ALA A1022       6.460  -2.325  -8.980  1.00 16.54           O  
ANISOU  321  O   ALA A1022     2838   2010   1434     68    -66    151       O  
ATOM    322  CB  ALA A1022       6.400   0.050 -11.241  1.00 16.07           C  
ANISOU  322  CB  ALA A1022     2249   2300   1557     43    -62    296       C  
ATOM    323  N   LEU A1023       6.909  -0.260  -8.199  1.00 15.16           N  
ANISOU  323  N   LEU A1023     2356   2018   1387      1    -56    209       N  
ATOM    324  CA  LEU A1023       6.478  -0.498  -6.825  1.00 16.08           C  
ANISOU  324  CA  LEU A1023     2433   2071   1603    -41    -29    155       C  
ATOM    325  C   LEU A1023       5.023  -0.082  -6.629  1.00 14.97           C  
ANISOU  325  C   LEU A1023     2382   1898   1406    -84   -104    315       C  
ATOM    326  O   LEU A1023       4.650   1.054  -6.961  1.00 16.22           O  
ANISOU  326  O   LEU A1023     2598   1955   1607    271   -164    470       O  
ATOM    327  CB  LEU A1023       7.363   0.349  -5.918  1.00 15.47           C  
ANISOU  327  CB  LEU A1023     2309   1954   1613   -127   -108    178       C  
ATOM    328  CG  LEU A1023       7.143   0.237  -4.416  1.00 16.52           C  
ANISOU  328  CG  LEU A1023     2320   2109   1847   -184   -102    127       C  
ATOM    329  CD1 LEU A1023       7.612  -1.099  -3.926  1.00 18.55           C  
ANISOU  329  CD1 LEU A1023     2842   2415   1792    139    -78    -45       C  
ATOM    330  CD2 LEU A1023       7.852   1.367  -3.677  1.00 17.77           C  
ANISOU  330  CD2 LEU A1023     2728   2354   1670   -189   -192    -65       C  
ATOM    331  N   LEU A1024       4.206  -0.970  -6.058  1.00 14.32           N  
ANISOU  331  N   LEU A1024     2341   1756   1342    -12   -133    223       N  
ATOM    332  CA  LEU A1024       2.843  -0.606  -5.685  1.00 14.76           C  
ANISOU  332  CA  LEU A1024     2294   1821   1491      2   -233    198       C  
ATOM    333  C   LEU A1024       2.897   0.184  -4.379  1.00 14.97           C  
ANISOU  333  C   LEU A1024     2368   1855   1464     24   -147     95       C  
ATOM    334  O   LEU A1024       3.166  -0.387  -3.323  1.00 15.92           O  
ANISOU  334  O   LEU A1024     2945   1781   1321    246   -304    312       O  
ATOM    335  CB  LEU A1024       1.963  -1.851  -5.526  1.00 15.01           C  
ANISOU  335  CB  LEU A1024     2312   1887   1500     71   -144    151       C  
ATOM    336  CG  LEU A1024       1.881  -2.785  -6.742  1.00 16.47           C  
ANISOU  336  CG  LEU A1024     2668   1934   1654     19   -251    207       C  
ATOM    337  CD1 LEU A1024       0.939  -3.962  -6.485  1.00 18.26           C  
ANISOU  337  CD1 LEU A1024     2749   2058   2127    -17   -206   -190       C  
ATOM    338  CD2 LEU A1024       1.461  -2.023  -8.003  1.00 18.58           C  
ANISOU  338  CD2 LEU A1024     3066   2335   1658    127   -570    -90       C  
ATOM    339  N   ASP A1025       2.659   1.491  -4.457  1.00 15.07           N  
ANISOU  339  N   ASP A1025     2349   2041   1333    -50   -201    127       N  
ATOM    340  CA  ASP A1025       3.023   2.429  -3.392  1.00 14.72           C  
ANISOU  340  CA  ASP A1025     2248   1816   1528     91   -152    107       C  
ATOM    341  C   ASP A1025       1.796   3.200  -2.880  1.00 13.43           C  
ANISOU  341  C   ASP A1025     1971   1837   1294     82   -216    147       C  
ATOM    342  O   ASP A1025       1.409   4.217  -3.451  1.00 15.51           O  
ANISOU  342  O   ASP A1025     2733   1781   1378    343   -512    160       O  
ATOM    343  CB  ASP A1025       4.069   3.398  -3.941  1.00 15.68           C  
ANISOU  343  CB  ASP A1025     2267   1994   1694     37   -169    -21       C  
ATOM    344  CG  ASP A1025       4.698   4.261  -2.869  1.00 18.00           C  
ANISOU  344  CG  ASP A1025     2678   2205   1955    -46   -136     -8       C  
ATOM    345  OD1 ASP A1025       4.146   4.323  -1.747  1.00 18.43           O  
ANISOU  345  OD1 ASP A1025     2651   2685   1666     88   -312    -44       O  
ATOM    346  OD2 ASP A1025       5.756   4.874  -3.159  1.00 19.59           O1-
ANISOU  346  OD2 ASP A1025     2932   2504   2005    -47     93    225       O1-
ATOM    347  N   THR A1026       1.172   2.709  -1.811  1.00 14.25           N  
ANISOU  347  N   THR A1026     2239   1877   1295    154   -335    171       N  
ATOM    348  CA  THR A1026       0.003   3.377  -1.247  1.00 14.18           C  
ANISOU  348  CA  THR A1026     2135   1957   1295     76   -330    105       C  
ATOM    349  C   THR A1026       0.334   4.692  -0.566  1.00 14.36           C  
ANISOU  349  C   THR A1026     2132   1949   1374    148   -324    130       C  
ATOM    350  O   THR A1026      -0.579   5.458  -0.227  1.00 16.15           O  
ANISOU  350  O   THR A1026     2573   2011   1550    300   -411     -2       O  
ATOM    351  CB  THR A1026      -0.737   2.496  -0.234  1.00 13.63           C  
ANISOU  351  CB  THR A1026     1885   1999   1292    183   -225     25       C  
ATOM    352  CG2 THR A1026      -1.202   1.208  -0.897  1.00 13.82           C  
ANISOU  352  CG2 THR A1026     1855   2164   1229     99   -399    146       C  
ATOM    353  OG1 THR A1026       0.136   2.201   0.864  1.00 15.00           O  
ANISOU  353  OG1 THR A1026     2065   2383   1249    195   -578    210       O  
ATOM    354  N   GLY A1027       1.624   4.956  -0.362  1.00 14.95           N  
ANISOU  354  N   GLY A1027     2321   1918   1438    141   -380    179       N  
ATOM    355  CA  GLY A1027       2.055   6.230   0.191  1.00 15.97           C  
ANISOU  355  CA  GLY A1027     2361   2041   1664     14   -295    112       C  
ATOM    356  C   GLY A1027       2.325   7.303  -0.849  1.00 17.04           C  
ANISOU  356  C   GLY A1027     2718   2031   1724    -52   -348     40       C  
ATOM    357  O   GLY A1027       2.772   8.389  -0.524  1.00 19.08           O  
ANISOU  357  O   GLY A1027     3488   2149   1611    -28   -484     47       O  
ATOM    358  N   ALA A1028       2.076   6.990  -2.115  1.00 16.30           N  
ANISOU  358  N   ALA A1028     2641   2075   1475    -17   -379     65       N  
ATOM    359  CA  ALA A1028       2.308   7.942  -3.202  1.00 15.79           C  
ANISOU  359  CA  ALA A1028     2370   1933   1695    -21   -209     48       C  
ATOM    360  C   ALA A1028       0.978   8.322  -3.836  1.00 14.68           C  
ANISOU  360  C   ALA A1028     2363   1654   1558     24   -281     32       C  
ATOM    361  O   ALA A1028       0.179   7.450  -4.200  1.00 15.18           O  
ANISOU  361  O   ALA A1028     2598   1698   1470   -104   -298     42       O  
ATOM    362  CB  ALA A1028       3.217   7.319  -4.248  1.00 17.08           C  
ANISOU  362  CB  ALA A1028     2495   2164   1828    111   -294     69       C  
ATOM    363  N   ASP A1029       0.734   9.622  -3.987  1.00 14.62           N  
ANISOU  363  N   ASP A1029     2391   1698   1465    -19   -130    -78       N  
ATOM    364  CA  ASP A1029      -0.504  10.079  -4.589  1.00 14.80           C  
ANISOU  364  CA  ASP A1029     2243   1805   1574     74   -113   -117       C  
ATOM    365  C   ASP A1029      -0.494   9.746  -6.080  1.00 14.87           C  
ANISOU  365  C   ASP A1029     2147   1948   1554    -29    -89   -129       C  
ATOM    366  O   ASP A1029      -1.521   9.381  -6.637  1.00 15.75           O  
ANISOU  366  O   ASP A1029     2246   2149   1589     92    -26   -193       O  
ATOM    367  CB  ASP A1029      -0.666  11.596  -4.436  1.00 15.73           C  
ANISOU  367  CB  ASP A1029     2600   1754   1620     18    -51   -145       C  
ATOM    368  CG  ASP A1029      -0.705  12.065  -2.986  1.00 19.46           C  
ANISOU  368  CG  ASP A1029     3269   2260   1864    -64    -49   -326       C  
ATOM    369  OD1 ASP A1029      -1.019  11.276  -2.073  1.00 19.33           O  
ANISOU  369  OD1 ASP A1029     3482   2280   1581    -45     24   -291       O  
ATOM    370  OD2 ASP A1029      -0.427  13.262  -2.774  1.00 25.60           O1-
ANISOU  370  OD2 ASP A1029     4890   2618   2219   -348    472   -528       O1-
ATOM    371  N   ASP A1030       0.673   9.904  -6.711  1.00 14.14           N  
ANISOU  371  N   ASP A1030     2116   1907   1348     66    -93    -74       N  
ATOM    372  CA  ASP A1030       0.808   9.871  -8.169  1.00 14.97           C  
ANISOU  372  CA  ASP A1030     2123   1932   1633      4   -237    -58       C  
ATOM    373  C   ASP A1030       1.749   8.758  -8.604  1.00 14.04           C  
ANISOU  373  C   ASP A1030     1935   1884   1513     33   -273    -22       C  
ATOM    374  O   ASP A1030       2.607   8.301  -7.853  1.00 15.07           O  
ANISOU  374  O   ASP A1030     2223   2027   1474    193   -482     80       O  
ATOM    375  CB  ASP A1030       1.372  11.189  -8.709  1.00 16.07           C  
ANISOU  375  CB  ASP A1030     2345   2077   1684    143   -175    -32       C  
ATOM    376  CG  ASP A1030       0.584  12.390  -8.261  1.00 18.68           C  
ANISOU  376  CG  ASP A1030     2841   2475   1781     -7   -328   -309       C  
ATOM    377  OD1 ASP A1030      -0.642  12.411  -8.455  1.00 22.68           O  
ANISOU  377  OD1 ASP A1030     3263   3196   2156    647   -413    -75       O  
ATOM    378  OD2 ASP A1030       1.192  13.297  -7.664  1.00 27.04           O1-
ANISOU  378  OD2 ASP A1030     3540   2888   3844   -447   -723   -967       O1-
ATOM    379  N   THR A1031       1.574   8.353  -9.851  1.00 14.11           N  
ANISOU  379  N   THR A1031     1981   1879   1500     53   -173    -65       N  
ATOM    380  CA  THR A1031       2.426   7.405 -10.524  1.00 12.60           C  
ANISOU  380  CA  THR A1031     1748   1688   1352    -46    -80    143       C  
ATOM    381  C   THR A1031       3.531   8.148 -11.229  1.00 12.24           C  
ANISOU  381  C   THR A1031     1624   1642   1384     12   -136     66       C  
ATOM    382  O   THR A1031       3.269   9.090 -11.996  1.00 13.79           O  
ANISOU  382  O   THR A1031     2012   1893   1335    -97   -243    318       O  
ATOM    383  CB  THR A1031       1.582   6.601 -11.516  1.00 12.59           C  
ANISOU  383  CB  THR A1031     1797   1623   1360     40    -93    183       C  
ATOM    384  CG2 THR A1031       2.432   5.672 -12.380  1.00 12.92           C  
ANISOU  384  CG2 THR A1031     1819   1740   1349   -110     26     95       C  
ATOM    385  OG1 THR A1031       0.619   5.841 -10.770  1.00 12.89           O  
ANISOU  385  OG1 THR A1031     1698   1954   1245   -150    -67    239       O  
ATOM    386  N  AVAL A1032       4.771   7.763 -10.949  0.70 12.15           N  
ANISOU  386  N  AVAL A1032     1564   1708   1344    -34    -58    271       N  
ATOM    387  N  BVAL A1032       4.760   7.710 -10.956  0.30 12.39           N  
ANISOU  387  N  BVAL A1032     1617   1691   1397    -17    -78    171       N  
ATOM    388  CA AVAL A1032       5.918   8.409 -11.571  0.70 13.09           C  
ANISOU  388  CA AVAL A1032     1800   1729   1443    -87    -66    191       C  
ATOM    389  CA BVAL A1032       5.981   8.344 -11.445  0.30 12.68           C  
ANISOU  389  CA BVAL A1032     1706   1677   1434    -40    -74    107       C  
ATOM    390  C  AVAL A1032       6.925   7.359 -12.010  0.70 12.92           C  
ANISOU  390  C  AVAL A1032     1702   1811   1393   -128   -222    163       C  
ATOM    391  C  BVAL A1032       6.878   7.263 -12.034  0.30 12.96           C  
ANISOU  391  C  BVAL A1032     1688   1769   1465    -66   -135    121       C  
ATOM    392  O  AVAL A1032       7.331   6.496 -11.227  0.70 12.87           O  
ANISOU  392  O  AVAL A1032     1899   1656   1333    103   -292    211       O  
ATOM    393  O  BVAL A1032       7.169   6.269 -11.366  0.30 12.94           O  
ANISOU  393  O  BVAL A1032     1742   1751   1423    -60   -160    109       O  
ATOM    394  CB AVAL A1032       6.548   9.486 -10.647  0.70 14.61           C  
ANISOU  394  CB AVAL A1032     1917   1871   1760   -109     14    161       C  
ATOM    395  CB BVAL A1032       6.747   9.046 -10.296  0.30 12.47           C  
ANISOU  395  CB BVAL A1032     1555   1663   1518    -27    -47    129       C  
ATOM    396  CG1AVAL A1032       6.978   8.900  -9.349  0.70 17.31           C  
ANISOU  396  CG1AVAL A1032     2367   2099   2110     82    -89     39       C  
ATOM    397  CG1BVAL A1032       5.836  10.036  -9.583  0.30  8.66           C  
ANISOU  397  CG1BVAL A1032     1445   1048    794    -77    -27   -189       C  
ATOM    398  CG2AVAL A1032       7.709  10.196 -11.321  0.70 12.28           C  
ANISOU  398  CG2AVAL A1032     1590   1541   1535   -101    -42     48       C  
ATOM    399  CG2BVAL A1032       7.303   8.026  -9.302  0.30 16.38           C  
ANISOU  399  CG2BVAL A1032     2080   1923   2220     -3     51   -100       C  
ATOM    400  N   LEU A1033       7.298   7.439 -13.284  1.00 13.10           N  
ANISOU  400  N   LEU A1033     1770   1819   1387     -7   -197    206       N  
ATOM    401  CA  LEU A1033       8.147   6.461 -13.928  1.00 14.17           C  
ANISOU  401  CA  LEU A1033     1911   1931   1540     30   -136    117       C  
ATOM    402  C   LEU A1033       9.353   7.126 -14.549  1.00 13.00           C  
ANISOU  402  C   LEU A1033     1653   1827   1458     70   -222    -10       C  
ATOM    403  O   LEU A1033       9.308   8.297 -14.932  1.00 13.42           O  
ANISOU  403  O   LEU A1033     1665   1886   1546    142   -153     81       O  
ATOM    404  CB  LEU A1033       7.395   5.688 -15.011  1.00 15.29           C  
ANISOU  404  CB  LEU A1033     1986   1972   1851     42    -95    -20       C  
ATOM    405  CG  LEU A1033       6.117   4.964 -14.588  1.00 16.35           C  
ANISOU  405  CG  LEU A1033     2235   2067   1909   -157   -231     10       C  
ATOM    406  CD1 LEU A1033       5.488   4.344 -15.813  1.00 19.71           C  
ANISOU  406  CD1 LEU A1033     2436   2506   2547   -249   -428     59       C  
ATOM    407  CD2 LEU A1033       6.397   3.916 -13.543  1.00 17.79           C  
ANISOU  407  CD2 LEU A1033     2413   2034   2309   -504    -65   -171       C  
ATOM    408  N   GLU A1034      10.412   6.335 -14.667  1.00 14.91           N  
ANISOU  408  N   GLU A1034     1774   2161   1730    155    -71     97       N  
ATOM    409  CA  GLU A1034      11.649   6.722 -15.305  1.00 16.85           C  
ANISOU  409  CA  GLU A1034     2025   2318   2057     64     26    114       C  
ATOM    410  C   GLU A1034      11.415   7.191 -16.728  1.00 16.41           C  
ANISOU  410  C   GLU A1034     1868   2348   2017     51     16     21       C  
ATOM    411  O   GLU A1034      10.402   6.868 -17.339  1.00 17.10           O  
ANISOU  411  O   GLU A1034     2160   2455   1879     18    164    -63       O  
ATOM    412  CB  GLU A1034      12.580   5.502 -15.338  1.00 17.83           C  
ANISOU  412  CB  GLU A1034     2141   2381   2251    176     18    214       C  
ATOM    413  CG  GLU A1034      12.010   4.347 -16.172  0.50 19.16           C  
ANISOU  413  CG  GLU A1034     2419   2504   2354    173    109    118       C  
ATOM    414  CD  GLU A1034      12.936   3.146 -16.274  0.50 19.80           C  
ANISOU  414  CD  GLU A1034     2427   2671   2424    175    273     84       C  
ATOM    415  OE1 GLU A1034      12.768   2.201 -15.487  0.50 18.67           O  
ANISOU  415  OE1 GLU A1034     2458   2607   2027    335    950    245       O  
ATOM    416  OE2 GLU A1034      13.816   3.133 -17.159  0.50 22.79           O1-
ANISOU  416  OE2 GLU A1034     3029   3057   2573    249    971    132       O1-
ATOM    417  N   GLU A1035      12.382   7.930 -17.253  1.00 16.91           N  
ANISOU  417  N   GLU A1035     1922   2475   2027    -23    117     97       N  
ATOM    418  CA  GLU A1035      12.315   8.448 -18.609  1.00 16.51           C  
ANISOU  418  CA  GLU A1035     1940   2275   2055     23    146     96       C  
ATOM    419  C   GLU A1035      11.880   7.394 -19.622  1.00 17.05           C  
ANISOU  419  C   GLU A1035     2094   2276   2107    135    249     85       C  
ATOM    420  O   GLU A1035      12.416   6.280 -19.669  1.00 17.38           O  
ANISOU  420  O   GLU A1035     2200   2234   2169    344    292    145       O  
ATOM    421  CB  GLU A1035      13.657   9.061 -19.019  1.00 18.17           C  
ANISOU  421  CB  GLU A1035     1989   2481   2432     23    225     35       C  
ATOM    422  CG  GLU A1035      13.614   9.745 -20.373  1.00 19.28           C  
ANISOU  422  CG  GLU A1035     2130   2810   2384    -88    307     -8       C  
ATOM    423  CD  GLU A1035      12.521  10.790 -20.447  1.00 20.88           C  
ANISOU  423  CD  GLU A1035     2598   2834   2500   -156    206    192       C  
ATOM    424  OE1 GLU A1035      12.494  11.678 -19.575  1.00 19.60           O  
ANISOU  424  OE1 GLU A1035     2378   2552   2518   -257    797   -363       O  
ATOM    425  OE2 GLU A1035      11.676  10.723 -21.362  1.00 22.20           O1-
ANISOU  425  OE2 GLU A1035     2263   3511   2659    -55    286    -71       O1-
ATOM    426  N  AMET A1036      10.902   7.766 -20.437  0.50 15.39           N  
ANISOU  426  N  AMET A1036     1943   2118   1784    153    135    -28       N  
ATOM    427  N  BMET A1036      10.890   7.761 -20.426  0.50 15.52           N  
ANISOU  427  N  BMET A1036     1955   2124   1816    166    127    -32       N  
ATOM    428  CA AMET A1036      10.399   6.914 -21.504  0.50 15.77           C  
ANISOU  428  CA AMET A1036     2004   2103   1883     52    109     38       C  
ATOM    429  CA BMET A1036      10.355   6.906 -21.477  0.50 15.82           C  
ANISOU  429  CA BMET A1036     1967   2120   1921     85    114     10       C  
ATOM    430  C  AMET A1036       9.513   7.750 -22.416  0.50 15.62           C  
ANISOU  430  C  AMET A1036     2079   2051   1803     53    154     -2       C  
ATOM    431  C  BMET A1036       9.604   7.791 -22.459  0.50 15.79           C  
ANISOU  431  C  BMET A1036     2072   2072   1853     89    142    -21       C  
ATOM    432  O  AMET A1036       9.081   8.840 -22.043  0.50 15.37           O  
ANISOU  432  O  AMET A1036     2255   2012   1572    164    268    127       O  
ATOM    433  O  BMET A1036       9.378   8.970 -22.186  0.50 16.48           O  
ANISOU  433  O  BMET A1036     2287   2177   1798    278    212      8       O  
ATOM    434  CB AMET A1036       9.602   5.748 -20.924  0.50 14.90           C  
ANISOU  434  CB AMET A1036     1953   2093   1615      7    139    -40       C  
ATOM    435  CB BMET A1036       9.413   5.858 -20.888  0.50 15.17           C  
ANISOU  435  CB BMET A1036     1997   2069   1696     65    113    -63       C  
ATOM    436  CG AMET A1036       8.306   6.157 -20.244  0.50 14.19           C  
ANISOU  436  CG AMET A1036     1753   2026   1612     50     76     27       C  
ATOM    437  CG BMET A1036       8.222   6.442 -20.145  0.50 14.78           C  
ANISOU  437  CG BMET A1036     1695   2230   1691    124     81     92       C  
ATOM    438  SD AMET A1036       7.331   4.743 -19.705  0.50 17.44           S  
ANISOU  438  SD AMET A1036     2237   2328   2060    -75    -52    191       S  
ATOM    439  SD BMET A1036       7.078   5.191 -19.521  0.50 16.00           S  
ANISOU  439  SD BMET A1036     1778   2284   2014     80     72    -28       S  
ATOM    440  CE AMET A1036       6.954   3.994 -21.288  0.50 18.73           C  
ANISOU  440  CE AMET A1036     2282   2393   2441   -157     52    128       C  
ATOM    441  CE BMET A1036       8.130   4.289 -18.388  0.50 18.31           C  
ANISOU  441  CE BMET A1036     1867   2685   2405     65     91   -121       C  
ATOM    442  N   ASN A1037       9.225   7.224 -23.600  1.00 15.55           N  
ANISOU  442  N   ASN A1037     2082   2093   1731    114    245    -48       N  
ATOM    443  CA  ASN A1037       8.412   7.929 -24.570  1.00 15.44           C  
ANISOU  443  CA  ASN A1037     1989   2060   1817    133    201   -103       C  
ATOM    444  C   ASN A1037       6.945   7.554 -24.397  1.00 15.31           C  
ANISOU  444  C   ASN A1037     1938   1927   1949     97    289    -70       C  
ATOM    445  O   ASN A1037       6.594   6.369 -24.430  1.00 17.25           O  
ANISOU  445  O   ASN A1037     2054   1896   2601    139    535   -118       O  
ATOM    446  CB  ASN A1037       8.862   7.575 -25.987  1.00 16.89           C  
ANISOU  446  CB  ASN A1037     2271   2219   1927     -8    205   -142       C  
ATOM    447  CG  ASN A1037      10.246   8.069 -26.297  1.00 20.61           C  
ANISOU  447  CG  ASN A1037     2582   2919   2329    103    562   -313       C  
ATOM    448  ND2 ASN A1037      10.948   7.347 -27.165  1.00 28.24           N  
ANISOU  448  ND2 ASN A1037     3638   3687   3405   -123   1217   -417       N  
ATOM    449  OD1 ASN A1037      10.691   9.088 -25.763  1.00 22.41           O  
ANISOU  449  OD1 ASN A1037     2635   3404   2473   -544    751   -190       O  
ATOM    450  N   LEU A1038       6.097   8.560 -24.204  1.00 13.89           N  
ANISOU  450  N   LEU A1038     1945   1916   1417    167     98     19       N  
ATOM    451  CA  LEU A1038       4.661   8.358 -24.159  1.00 14.04           C  
ANISOU  451  CA  LEU A1038     2034   1825   1475    157     34     41       C  
ATOM    452  C   LEU A1038       3.963   9.306 -25.121  1.00 13.84           C  
ANISOU  452  C   LEU A1038     1984   1867   1406    166    -28      9       C  
ATOM    453  O   LEU A1038       4.466  10.394 -25.399  1.00 14.86           O  
ANISOU  453  O   LEU A1038     2164   2040   1440    136     51     56       O  
ATOM    454  CB  LEU A1038       4.131   8.592 -22.746  1.00 13.06           C  
ANISOU  454  CB  LEU A1038     1762   1795   1406    135     48   -181       C  
ATOM    455  CG  LEU A1038       4.577   7.597 -21.678  1.00 12.27           C  
ANISOU  455  CG  LEU A1038     1531   1689   1441     41     -7    -71       C  
ATOM    456  CD1 LEU A1038       3.971   8.010 -20.349  1.00 13.35           C  
ANISOU  456  CD1 LEU A1038     1649   2050   1372      3    -56   -136       C  
ATOM    457  CD2 LEU A1038       4.179   6.188 -22.024  1.00 14.19           C  
ANISOU  457  CD2 LEU A1038     1927   1984   1478    187    175    120       C  
ATOM    458  N   PRO A1039       2.794   8.886 -25.616  1.00 14.62           N  
ANISOU  458  N   PRO A1039     2069   1915   1567    227   -103     80       N  
ATOM    459  CA  PRO A1039       2.040   9.687 -26.562  1.00 14.78           C  
ANISOU  459  CA  PRO A1039     2077   1972   1567    209    -80     67       C  
ATOM    460  C   PRO A1039       1.252  10.817 -25.930  1.00 13.75           C  
ANISOU  460  C   PRO A1039     2053   1834   1334    229   -115    114       C  
ATOM    461  O   PRO A1039       0.868  10.741 -24.754  1.00 14.73           O  
ANISOU  461  O   PRO A1039     2182   2035   1378    167    -96     39       O  
ATOM    462  CB  PRO A1039       1.097   8.666 -27.185  1.00 15.80           C  
ANISOU  462  CB  PRO A1039     2042   2179   1781    204   -114     27       C  
ATOM    463  CG  PRO A1039       0.832   7.707 -26.094  1.00 16.13           C  
ANISOU  463  CG  PRO A1039     2306   1718   2104     17   -196   -131       C  
ATOM    464  CD  PRO A1039       2.129   7.603 -25.339  1.00 15.67           C  
ANISOU  464  CD  PRO A1039     2145   2002   1806    127   -186     -7       C  
ATOM    465  N   GLY A1040       0.978  11.845 -26.734  1.00 13.77           N  
ANISOU  465  N   GLY A1040     2002   1839   1391    164   -107     24       N  
ATOM    466  CA  GLY A1040       0.050  12.885 -26.335  1.00 14.59           C  
ANISOU  466  CA  GLY A1040     2034   1927   1581     31   -134      8       C  
ATOM    467  C   GLY A1040       0.749  14.143 -25.860  1.00 14.67           C  
ANISOU  467  C   GLY A1040     2114   1993   1464    -44   -181     15       C  
ATOM    468  O   GLY A1040       1.984  14.262 -25.887  1.00 15.96           O  
ANISOU  468  O   GLY A1040     2412   2097   1555     51   -130   -191       O  
ATOM    469  N   ARG A1041      -0.074  15.078 -25.424  1.00 14.99           N  
ANISOU  469  N   ARG A1041     1982   2143   1567     70   -260    -94       N  
ATOM    470  CA  ARG A1041       0.386  16.367 -24.942  1.00 15.46           C  
ANISOU  470  CA  ARG A1041     2081   2241   1551   -107   -209    -50       C  
ATOM    471  C   ARG A1041       0.778  16.225 -23.490  1.00 16.10           C  
ANISOU  471  C   ARG A1041     2151   2532   1431   -461   -107     95       C  
ATOM    472  O   ARG A1041       0.031  15.689 -22.699  1.00 21.70           O  
ANISOU  472  O   ARG A1041     2699   4093   1452  -1055   -101   -119       O  
ATOM    473  CB  ARG A1041      -0.741  17.394 -25.071  1.00 17.13           C  
ANISOU  473  CB  ARG A1041     2233   2465   1809    -36   -260   -124       C  
ATOM    474  CG  ARG A1041      -0.325  18.819 -24.765  1.00 20.09           C  
ANISOU  474  CG  ARG A1041     2661   2594   2377    126   -204   -266       C  
ATOM    475  CD  ARG A1041      -1.514  19.768 -24.795  1.00 23.32           C  
ANISOU  475  CD  ARG A1041     3046   2972   2841    110   -162   -266       C  
ATOM    476  NE  ARG A1041      -2.229  19.735 -26.069  0.75 28.06           N  
ANISOU  476  NE  ARG A1041     3491   3359   3811    374    -80   -207       N  
ATOM    477  CZ  ARG A1041      -3.393  19.121 -26.279  0.75 26.08           C  
ANISOU  477  CZ  ARG A1041     3350   3052   3507    144     -3   -187       C  
ATOM    478  NH1 ARG A1041      -4.023  18.470 -25.300  0.75 28.15           N1+
ANISOU  478  NH1 ARG A1041     3471   3273   3951    145   -398   -257       N1+
ATOM    479  NH2 ARG A1041      -3.936  19.168 -27.480  0.75 28.99           N  
ANISOU  479  NH2 ARG A1041     3930   3221   3864    159     78    -89       N  
ATOM    480  N   TRP A1042       1.949  16.696 -23.141  1.00 15.19           N  
ANISOU  480  N   TRP A1042     2126   2329   1313   -249    -16     11       N  
ATOM    481  CA  TRP A1042       2.333  16.695 -21.750  1.00 14.01           C  
ANISOU  481  CA  TRP A1042     1878   2045   1400   -231   -139     38       C  
ATOM    482  C   TRP A1042       2.488  18.129 -21.286  1.00 14.54           C  
ANISOU  482  C   TRP A1042     2107   1937   1478    -53   -135     92       C  
ATOM    483  O   TRP A1042       2.566  19.068 -22.100  1.00 14.57           O  
ANISOU  483  O   TRP A1042     2287   1791   1456   -125   -143    114       O  
ATOM    484  CB  TRP A1042       3.633  15.924 -21.538  1.00 14.55           C  
ANISOU  484  CB  TRP A1042     1975   1959   1591   -157    -71     72       C  
ATOM    485  CG  TRP A1042       4.771  16.444 -22.359  1.00 15.07           C  
ANISOU  485  CG  TRP A1042     2079   2034   1612    -94   -127    -74       C  
ATOM    486  CD1 TRP A1042       5.108  16.051 -23.613  1.00 17.13           C  
ANISOU  486  CD1 TRP A1042     2282   2476   1750   -245   -113   -109       C  
ATOM    487  CD2 TRP A1042       5.719  17.448 -21.983  1.00 14.60           C  
ANISOU  487  CD2 TRP A1042     1812   2030   1705   -120    110    114       C  
ATOM    488  CE2 TRP A1042       6.612  17.604 -23.062  1.00 16.37           C  
ANISOU  488  CE2 TRP A1042     1995   2273   1950   -459     59     43       C  
ATOM    489  CE3 TRP A1042       5.920  18.212 -20.827  1.00 14.81           C  
ANISOU  489  CE3 TRP A1042     1975   1897   1756    -66   -140    -96       C  
ATOM    490  NE1 TRP A1042       6.209  16.748 -24.049  1.00 18.65           N  
ANISOU  490  NE1 TRP A1042     2532   2610   1944   -286    139    -99       N  
ATOM    491  CZ2 TRP A1042       7.670  18.506 -23.035  1.00 16.81           C  
ANISOU  491  CZ2 TRP A1042     2174   2385   1828   -297     68    208       C  
ATOM    492  CZ3 TRP A1042       6.971  19.108 -20.802  1.00 17.08           C  
ANISOU  492  CZ3 TRP A1042     2187   2358   1944   -178     70   -109       C  
ATOM    493  CH2 TRP A1042       7.834  19.246 -21.902  1.00 16.90           C  
ANISOU  493  CH2 TRP A1042     2300   2020   2099   -402    -58    -28       C  
ATOM    494  N   LYS A1043       2.543  18.293 -19.971  1.00 13.87           N  
ANISOU  494  N   LYS A1043     2127   1863   1280    -29   -214    132       N  
ATOM    495  CA  LYS A1043       2.879  19.580 -19.388  1.00 15.27           C  
ANISOU  495  CA  LYS A1043     2146   2049   1606    -61    -85     45       C  
ATOM    496  C   LYS A1043       3.778  19.325 -18.198  1.00 15.23           C  
ANISOU  496  C   LYS A1043     2247   2054   1483    -99   -205    -43       C  
ATOM    497  O   LYS A1043       3.681  18.277 -17.578  1.00 14.15           O  
ANISOU  497  O   LYS A1043     2096   1764   1514   -160   -220    -45       O  
ATOM    498  CB  LYS A1043       1.615  20.329 -18.959  1.00 17.09           C  
ANISOU  498  CB  LYS A1043     2378   2239   1873    -13   -182     64       C  
ATOM    499  CG  LYS A1043       0.786  19.613 -17.919  1.00 19.15           C  
ANISOU  499  CG  LYS A1043     2400   2535   2341     93    -34    -53       C  
ATOM    500  CD  LYS A1043      -0.476  20.383 -17.574  1.00 21.58           C  
ANISOU  500  CD  LYS A1043     2796   2812   2590    149     -4    -11       C  
ATOM    501  CE  LYS A1043      -1.401  19.555 -16.688  1.00 24.21           C  
ANISOU  501  CE  LYS A1043     3064   3094   3041    355    266     15       C  
ATOM    502  NZ  LYS A1043      -2.628  20.302 -16.291  1.00 27.18           N1+
ANISOU  502  NZ  LYS A1043     3234   3529   3562    205    505   -217       N1+
ATOM    503  N   PRO A1044       4.672  20.271 -17.889  1.00 15.32           N  
ANISOU  503  N   PRO A1044     2250   1908   1661    -15   -228    129       N  
ATOM    504  CA  PRO A1044       5.520  20.056 -16.725  1.00 15.44           C  
ANISOU  504  CA  PRO A1044     2119   2109   1637      1   -191    -58       C  
ATOM    505  C   PRO A1044       4.709  20.127 -15.432  1.00 17.59           C  
ANISOU  505  C   PRO A1044     2346   2431   1906    156   -124   -279       C  
ATOM    506  O   PRO A1044       3.715  20.847 -15.351  1.00 19.24           O  
ANISOU  506  O   PRO A1044     2629   2765   1916    358   -559   -394       O  
ATOM    507  CB  PRO A1044       6.537  21.196 -16.816  1.00 17.63           C  
ANISOU  507  CB  PRO A1044     2332   2272   2092    -64   -252   -143       C  
ATOM    508  CG  PRO A1044       5.915  22.215 -17.652  1.00 17.69           C  
ANISOU  508  CG  PRO A1044     2558   2143   2018   -277    -89   -187       C  
ATOM    509  CD  PRO A1044       4.986  21.529 -18.585  1.00 16.48           C  
ANISOU  509  CD  PRO A1044     2356   2021   1885    -68   -182     68       C  
ATOM    510  N   LYS A1045       5.139  19.365 -14.437  1.00 16.40           N  
ANISOU  510  N   LYS A1045     2112   2341   1776    159   -172   -123       N  
ATOM    511  CA  LYS A1045       4.500  19.346 -13.113  1.00 16.50           C  
ANISOU  511  CA  LYS A1045     2121   2365   1782    128    -77   -178       C  
ATOM    512  C   LYS A1045       5.614  19.304 -12.076  1.00 15.64           C  
ANISOU  512  C   LYS A1045     1997   2277   1668    168   -143   -222       C  
ATOM    513  O   LYS A1045       6.574  18.572 -12.245  1.00 15.12           O  
ANISOU  513  O   LYS A1045     1780   2529   1434    110    -65   -510       O  
ATOM    514  CB  LYS A1045       3.606  18.111 -12.944  1.00 17.25           C  
ANISOU  514  CB  LYS A1045     2124   2565   1863    263   -167   -164       C  
ATOM    515  CG  LYS A1045       2.801  18.073 -11.635  1.00 18.22           C  
ANISOU  515  CG  LYS A1045     2372   2417   2132    -99   -144    -65       C  
ATOM    516  CD  LYS A1045       2.038  16.738 -11.453  1.00 21.10           C  
ANISOU  516  CD  LYS A1045     2590   2847   2578      2     90   -134       C  
ATOM    517  CE  LYS A1045       1.155  16.730 -10.209  1.00 24.19           C  
ANISOU  517  CE  LYS A1045     3158   3261   2772    190   -139     -3       C  
ATOM    518  NZ  LYS A1045       0.267  17.921 -10.141  1.00 31.39           N1+
ANISOU  518  NZ  LYS A1045     3530   4435   3962    137     88   -146       N1+
ATOM    519  N   MET A1046       5.490  20.101 -11.018  1.00 16.00           N  
ANISOU  519  N   MET A1046     2011   2479   1587    247   -241   -331       N  
ATOM    520  CA  MET A1046       6.432  20.051  -9.906  1.00 15.48           C  
ANISOU  520  CA  MET A1046     1851   2272   1758    189    -60   -204       C  
ATOM    521  C   MET A1046       5.869  19.141  -8.841  1.00 14.46           C  
ANISOU  521  C   MET A1046     1651   2280   1560    261    -36   -274       C  
ATOM    522  O   MET A1046       4.739  19.329  -8.377  1.00 19.42           O  
ANISOU  522  O   MET A1046     1787   3334   2255    477    251    -98       O  
ATOM    523  CB  MET A1046       6.674  21.450  -9.338  1.00 16.31           C  
ANISOU  523  CB  MET A1046     1963   2329   1902    227   -243   -385       C  
ATOM    524  CG  MET A1046       7.174  22.467 -10.346  1.00 17.75           C  
ANISOU  524  CG  MET A1046     2421   2363   1958    314   -175   -424       C  
ATOM    525  SD  MET A1046       8.662  21.994 -11.261  1.00 19.69           S  
ANISOU  525  SD  MET A1046     3267   2441   1773     65   -186   -269       S  
ATOM    526  CE  MET A1046       9.848  21.836  -9.945  1.00 19.17           C  
ANISOU  526  CE  MET A1046     3129   2489   1664    139     63   -199       C  
ATOM    527  N   ILE A1047       6.632  18.122  -8.482  1.00 14.00           N  
ANISOU  527  N   ILE A1047     1604   2339   1374    155     93   -313       N  
ATOM    528  CA  ILE A1047       6.203  17.189  -7.459  1.00 14.40           C  
ANISOU  528  CA  ILE A1047     1816   2233   1421    -19    123   -197       C  
ATOM    529  C   ILE A1047       7.178  17.149  -6.303  1.00 13.96           C  
ANISOU  529  C   ILE A1047     1789   2203   1313   -147    183   -253       C  
ATOM    530  O   ILE A1047       8.275  17.663  -6.372  1.00 14.63           O  
ANISOU  530  O   ILE A1047     1891   2625   1042    -59    314   -330       O  
ATOM    531  CB  ILE A1047       5.971  15.766  -8.008  1.00 14.32           C  
ANISOU  531  CB  ILE A1047     1843   2207   1389   -217     17   -173       C  
ATOM    532  CG1 ILE A1047       7.255  15.159  -8.559  1.00 15.43           C  
ANISOU  532  CG1 ILE A1047     2175   2311   1377   -118     81   -305       C  
ATOM    533  CG2 ILE A1047       4.853  15.769  -9.049  1.00 18.08           C  
ANISOU  533  CG2 ILE A1047     2020   2876   1972    -55     70   -342       C  
ATOM    534  CD1 ILE A1047       7.143  13.683  -8.920  1.00 16.46           C  
ANISOU  534  CD1 ILE A1047     2298   2561   1392   -153    133   -174       C  
ATOM    535  N   GLY A1048       6.749  16.529  -5.219  1.00 14.44           N  
ANISOU  535  N   GLY A1048     1873   2306   1306   -241    233      6       N  
ATOM    536  CA  GLY A1048       7.570  16.455  -4.033  1.00 15.18           C  
ANISOU  536  CA  GLY A1048     2145   2119   1501    -86     92   -168       C  
ATOM    537  C   GLY A1048       7.185  17.573  -3.093  1.00 15.22           C  
ANISOU  537  C   GLY A1048     2137   2002   1642    -90    196   -146       C  
ATOM    538  O   GLY A1048       6.028  17.670  -2.691  1.00 19.87           O  
ANISOU  538  O   GLY A1048     2638   2704   2205   -144    395   -836       O  
ATOM    539  N   GLY A1049       8.156  18.405  -2.740  1.00 14.62           N  
ANISOU  539  N   GLY A1049     2023   1997   1534    -28    -33   -140       N  
ATOM    540  CA  GLY A1049       7.912  19.557  -1.879  1.00 14.81           C  
ANISOU  540  CA  GLY A1049     2169   1860   1596     79   -135    -65       C  
ATOM    541  C   GLY A1049       8.655  19.467  -0.557  1.00 15.07           C  
ANISOU  541  C   GLY A1049     2339   1904   1482     79   -245    -93       C  
ATOM    542  O   GLY A1049       8.983  20.482   0.047  1.00 16.24           O  
ANISOU  542  O   GLY A1049     2645   1769   1753    179   -486   -325       O  
ATOM    543  N   ILE A1050       8.909  18.248  -0.092  1.00 15.58           N  
ANISOU  543  N   ILE A1050     2534   1826   1558     46   -245   -207       N  
ATOM    544  CA  ILE A1050       9.597  18.059   1.187  1.00 16.35           C  
ANISOU  544  CA  ILE A1050     2370   2042   1800      0   -144    -43       C  
ATOM    545  C   ILE A1050      11.097  18.109   0.934  1.00 16.38           C  
ANISOU  545  C   ILE A1050     2496   2026   1701     46   -130    -20       C  
ATOM    546  O   ILE A1050      11.712  17.124   0.520  1.00 19.61           O  
ANISOU  546  O   ILE A1050     2860   2227   2361     68     50   -124       O  
ATOM    547  CB  ILE A1050       9.215  16.716   1.845  1.00 18.50           C  
ANISOU  547  CB  ILE A1050     2636   2343   2048      7    -77   -126       C  
ATOM    548  CG1 ILE A1050       7.698  16.580   1.962  1.00 20.74           C  
ANISOU  548  CG1 ILE A1050     2924   2384   2572     12    -75     84       C  
ATOM    549  CG2 ILE A1050       9.850  16.591   3.211  1.00 18.00           C  
ANISOU  549  CG2 ILE A1050     2790   2145   1901     48   -156    224       C  
ATOM    550  CD1 ILE A1050       7.245  15.252   2.578  0.50 19.57           C  
ANISOU  550  CD1 ILE A1050     2735   2321   2377    -25    -18    165       C  
ATOM    551  N   GLY A1051      11.677  19.279   1.144  1.00 15.03           N  
ANISOU  551  N   GLY A1051     2286   1880   1544     66   -177    135       N  
ATOM    552  CA  GLY A1051      13.079  19.505   0.826  1.00 14.65           C  
ANISOU  552  CA  GLY A1051     1961   1893   1712      1    -94    -13       C  
ATOM    553  C   GLY A1051      13.293  20.217  -0.497  1.00 13.25           C  
ANISOU  553  C   GLY A1051     1783   1631   1619    127   -191   -144       C  
ATOM    554  O   GLY A1051      14.395  20.653  -0.810  1.00 14.34           O  
ANISOU  554  O   GLY A1051     1810   1919   1717    211   -341    -91       O  
ATOM    555  N   GLY A1052      12.235  20.332  -1.287  1.00 12.12           N  
ANISOU  555  N   GLY A1052     1635   1775   1193    211   -154   -146       N  
ATOM    556  CA  GLY A1052      12.365  20.865  -2.636  1.00 12.53           C  
ANISOU  556  CA  GLY A1052     1758   1630   1370     95    -81    -68       C  
ATOM    557  C   GLY A1052      11.437  20.145  -3.582  1.00 11.85           C  
ANISOU  557  C   GLY A1052     1475   1730   1297     50    -11   -127       C  
ATOM    558  O   GLY A1052      10.749  19.208  -3.186  1.00 13.34           O  
ANISOU  558  O   GLY A1052     1966   1787   1314    124   -193   -155       O  
ATOM    559  N   PHE A1053      11.402  20.600  -4.830  1.00 12.06           N  
ANISOU  559  N   PHE A1053     1492   1895   1194    -10     76   -289       N  
ATOM    560  CA  PHE A1053      10.529  20.013  -5.840  1.00 11.96           C  
ANISOU  560  CA  PHE A1053     1537   1832   1176     44    104    -99       C  
ATOM    561  C   PHE A1053      11.335  19.443  -6.977  1.00 11.96           C  
ANISOU  561  C   PHE A1053     1439   1820   1286     70     79   -178       C  
ATOM    562  O   PHE A1053      12.431  19.902  -7.269  1.00 12.05           O  
ANISOU  562  O   PHE A1053     1594   1868   1116    -60     68   -320       O  
ATOM    563  CB  PHE A1053       9.575  21.051  -6.420  1.00 12.90           C  
ANISOU  563  CB  PHE A1053     1643   2040   1217    214     96   -204       C  
ATOM    564  CG  PHE A1053       8.561  21.565  -5.443  1.00 15.25           C  
ANISOU  564  CG  PHE A1053     1827   2485   1480    490   -225     22       C  
ATOM    565  CD1 PHE A1053       8.793  22.727  -4.738  1.00 15.40           C  
ANISOU  565  CD1 PHE A1053     1777   2436   1639    554    -39   -246       C  
ATOM    566  CD2 PHE A1053       7.367  20.897  -5.258  1.00 15.02           C  
ANISOU  566  CD2 PHE A1053     1869   2322   1515    607    458   -177       C  
ATOM    567  CE1 PHE A1053       7.847  23.214  -3.847  1.00 16.34           C  
ANISOU  567  CE1 PHE A1053     2018   2530   1659    617    -91   -322       C  
ATOM    568  CE2 PHE A1053       6.419  21.381  -4.370  1.00 17.08           C  
ANISOU  568  CE2 PHE A1053     1856   2609   2025    585    144    178       C  
ATOM    569  CZ  PHE A1053       6.670  22.531  -3.667  1.00 16.25           C  
ANISOU  569  CZ  PHE A1053     1956   2533   1682    855    186     88       C  
ATOM    570  N   ILE A1054      10.729  18.491  -7.666  1.00 12.40           N  
ANISOU  570  N   ILE A1054     1579   1935   1194     -9    130   -251       N  
ATOM    571  CA  ILE A1054      11.303  17.850  -8.840  1.00 12.20           C  
ANISOU  571  CA  ILE A1054     1479   1914   1240     21     31   -166       C  
ATOM    572  C   ILE A1054      10.316  18.107  -9.989  1.00 11.71           C  
ANISOU  572  C   ILE A1054     1367   1865   1214    -35     78   -233       C  
ATOM    573  O   ILE A1054       9.167  18.005  -9.833  1.00 12.09           O  
ANISOU  573  O   ILE A1054     1309   2167   1117    141      9   -326       O  
ATOM    574  CB  ILE A1054      11.412  16.333  -8.609  1.00 14.16           C  
ANISOU  574  CB  ILE A1054     1636   2170   1573     44   -114   -138       C  
ATOM    575  CG1 ILE A1054      12.186  15.991  -7.339  1.00 14.38           C  
ANISOU  575  CG1 ILE A1054     1739   1992   1729    -53    119   -147       C  
ATOM    576  CG2 ILE A1054      11.968  15.639  -9.774  1.00 14.52           C  
ANISOU  576  CG2 ILE A1054     1782   2134   1598      3    -51   -193       C  
ATOM    577  CD1 ILE A1054      13.410  16.353  -7.443  1.00 16.41           C  
ANISOU  577  CD1 ILE A1054     2061   2197   1973    -54     -9   -148       C  
ATOM    578  N   LYS A1055      10.857  18.461 -11.137  1.00 12.26           N  
ANISOU  578  N   LYS A1055     1406   2095   1157   -152     14   -211       N  
ATOM    579  CA  LYS A1055      10.032  18.636 -12.325  1.00 12.62           C  
ANISOU  579  CA  LYS A1055     1583   1995   1215    -98     65   -206       C  
ATOM    580  C   LYS A1055       9.918  17.326 -13.089  1.00 11.83           C  
ANISOU  580  C   LYS A1055     1381   1928   1183   -196    142   -242       C  
ATOM    581  O   LYS A1055      10.911  16.623 -13.309  1.00 13.01           O  
ANISOU  581  O   LYS A1055     1462   2295   1186   -237    208   -403       O  
ATOM    582  CB  LYS A1055      10.621  19.724 -13.227  1.00 13.82           C  
ANISOU  582  CB  LYS A1055     1931   2000   1319   -183     33   -208       C  
ATOM    583  CG  LYS A1055       9.733  20.151 -14.370  1.00 13.71           C  
ANISOU  583  CG  LYS A1055     1680   2220   1309   -284    -16     -5       C  
ATOM    584  CD  LYS A1055      10.423  21.145 -15.319  1.00 14.79           C  
ANISOU  584  CD  LYS A1055     2282   1948   1388   -348   -107    -34       C  
ATOM    585  CE  LYS A1055      10.721  22.474 -14.651  1.00 18.80           C  
ANISOU  585  CE  LYS A1055     2584   2667   1889   -490    -41     -7       C  
ATOM    586  NZ  LYS A1055      11.497  23.344 -15.579  1.00 22.34           N1+
ANISOU  586  NZ  LYS A1055     2704   3008   2776   -329    582    419       N1+
ATOM    587  N   VAL A1056       8.685  17.013 -13.480  1.00 11.76           N  
ANISOU  587  N   VAL A1056     1299   1975   1194   -128    100   -227       N  
ATOM    588  CA  VAL A1056       8.383  15.821 -14.264  1.00 11.17           C  
ANISOU  588  CA  VAL A1056     1361   1795   1088   -266    117   -166       C  
ATOM    589  C   VAL A1056       7.428  16.233 -15.390  1.00 12.18           C  
ANISOU  589  C   VAL A1056     1530   1909   1188   -192    175    -82       C  
ATOM    590  O   VAL A1056       6.913  17.349 -15.392  1.00 12.49           O  
ANISOU  590  O   VAL A1056     1610   2004   1129   -166     24   -125       O  
ATOM    591  CB  VAL A1056       7.743  14.694 -13.388  1.00 12.04           C  
ANISOU  591  CB  VAL A1056     1472   1860   1240   -164     45   -155       C  
ATOM    592  CG1 VAL A1056       8.715  14.250 -12.332  1.00 14.73           C  
ANISOU  592  CG1 VAL A1056     2008   2425   1160   -169   -120      6       C  
ATOM    593  CG2 VAL A1056       6.431  15.151 -12.765  1.00 13.74           C  
ANISOU  593  CG2 VAL A1056     1787   2129   1305   -324    140    -98       C  
ATOM    594  N   ARG A1057       7.203  15.342 -16.351  1.00 11.01           N  
ANISOU  594  N   ARG A1057     1447   1624   1109    -71     98    -54       N  
ATOM    595  CA  ARG A1057       6.234  15.593 -17.411  1.00 11.27           C  
ANISOU  595  CA  ARG A1057     1431   1677   1174   -120     95    -34       C  
ATOM    596  C   ARG A1057       4.957  14.818 -17.125  1.00 11.28           C  
ANISOU  596  C   ARG A1057     1434   1729   1123    -92     66    -69       C  
ATOM    597  O   ARG A1057       5.007  13.615 -16.876  1.00 11.56           O  
ANISOU  597  O   ARG A1057     1491   1607   1292    -66    190     72       O  
ATOM    598  CB  ARG A1057       6.799  15.111 -18.737  1.00 11.64           C  
ANISOU  598  CB  ARG A1057     1632   1778   1013     -7     27   -145       C  
ATOM    599  CG  ARG A1057       8.116  15.750 -19.105  1.00 12.94           C  
ANISOU  599  CG  ARG A1057     1817   1977   1123    110    234   -183       C  
ATOM    600  CD  ARG A1057       8.470  15.592 -20.575  1.00 13.76           C  
ANISOU  600  CD  ARG A1057     1695   2006   1526   -160    213   -120       C  
ATOM    601  NE  ARG A1057       8.387  14.228 -21.076  1.00 14.22           N  
ANISOU  601  NE  ARG A1057     1755   2315   1332   -114    468     82       N  
ATOM    602  CZ  ARG A1057       9.286  13.280 -20.848  1.00 14.78           C  
ANISOU  602  CZ  ARG A1057     1760   2122   1732   -245    342   -349       C  
ATOM    603  NH1 ARG A1057      10.325  13.526 -20.074  1.00 15.12           N1+
ANISOU  603  NH1 ARG A1057     1568   2304   1872   -402    118    232       N1+
ATOM    604  NH2 ARG A1057       9.137  12.075 -21.383  1.00 17.44           N  
ANISOU  604  NH2 ARG A1057     2154   2296   2173     16    256   -148       N  
ATOM    605  N   GLN A1058       3.825  15.507 -17.165  1.00 10.96           N  
ANISOU  605  N   GLN A1058     1438   1468   1256    -71    114      9       N  
ATOM    606  CA  GLN A1058       2.539  14.883 -16.918  1.00 11.38           C  
ANISOU  606  CA  GLN A1058     1408   1699   1216    -54    -76     17       C  
ATOM    607  C   GLN A1058       1.849  14.474 -18.221  1.00 11.18           C  
ANISOU  607  C   GLN A1058     1280   1828   1137   -139     78    -32       C  
ATOM    608  O   GLN A1058       1.522  15.328 -19.050  1.00 12.31           O  
ANISOU  608  O   GLN A1058     1593   1771   1310   -136   -125    130       O  
ATOM    609  CB  GLN A1058       1.633  15.848 -16.168  1.00 11.63           C  
ANISOU  609  CB  GLN A1058     1501   1747   1170   -114    -46   -104       C  
ATOM    610  CG  GLN A1058       0.277  15.265 -15.866  1.00 12.36           C  
ANISOU  610  CG  GLN A1058     1614   1703   1376     17    200     52       C  
ATOM    611  CD  GLN A1058      -0.622  16.192 -15.119  1.00 14.07           C  
ANISOU  611  CD  GLN A1058     1639   2203   1503    -26     29   -254       C  
ATOM    612  NE2 GLN A1058      -1.922  16.026 -15.319  1.00 16.66           N  
ANISOU  612  NE2 GLN A1058     1805   2555   1967    101     10    -45       N  
ATOM    613  OE1 GLN A1058      -0.167  17.042 -14.353  1.00 19.04           O  
ANISOU  613  OE1 GLN A1058     2200   3069   1964    114   -181   -912       O  
ATOM    614  N   TYR A1059       1.610  13.176 -18.373  1.00 10.85           N  
ANISOU  614  N   TYR A1059     1334   1651   1135   -103   -106     59       N  
ATOM    615  CA  TYR A1059       0.851  12.622 -19.496  1.00 11.16           C  
ANISOU  615  CA  TYR A1059     1429   1648   1163   -136     12     21       C  
ATOM    616  C   TYR A1059      -0.450  12.067 -18.956  1.00 11.05           C  
ANISOU  616  C   TYR A1059     1362   1742   1095    -83    -26     28       C  
ATOM    617  O   TYR A1059      -0.442  11.263 -18.025  1.00 12.44           O  
ANISOU  617  O   TYR A1059     1464   2023   1238    -79    -20    305       O  
ATOM    618  CB  TYR A1059       1.605  11.472 -20.160  1.00 11.37           C  
ANISOU  618  CB  TYR A1059     1465   1762   1093    -94    -63     62       C  
ATOM    619  CG  TYR A1059       2.896  11.853 -20.846  1.00 11.90           C  
ANISOU  619  CG  TYR A1059     1469   1855   1195   -241    117    -69       C  
ATOM    620  CD1 TYR A1059       4.085  11.929 -20.130  1.00 11.20           C  
ANISOU  620  CD1 TYR A1059     1393   1802   1058   -300    112      4       C  
ATOM    621  CD2 TYR A1059       2.927  12.136 -22.198  1.00 11.51           C  
ANISOU  621  CD2 TYR A1059     1317   1939   1115   -121     -9   -151       C  
ATOM    622  CE1 TYR A1059       5.268  12.259 -20.758  1.00 12.46           C  
ANISOU  622  CE1 TYR A1059     1469   1981   1284   -104   -112   -222       C  
ATOM    623  CE2 TYR A1059       4.110  12.469 -22.834  1.00 12.53           C  
ANISOU  623  CE2 TYR A1059     1648   2098   1014   -301     23   -234       C  
ATOM    624  CZ  TYR A1059       5.276  12.539 -22.102  1.00 11.70           C  
ANISOU  624  CZ  TYR A1059     1295   1945   1203   -274    130     21       C  
ATOM    625  OH  TYR A1059       6.464  12.863 -22.716  1.00 14.88           O  
ANISOU  625  OH  TYR A1059     1450   2629   1574   -299    238   -165       O  
ATOM    626  N   ASP A1060      -1.565  12.466 -19.560  1.00 11.77           N  
ANISOU  626  N   ASP A1060     1316   1982   1172    -76     44    259       N  
ATOM    627  CA  ASP A1060      -2.867  11.968 -19.152  1.00 12.56           C  
ANISOU  627  CA  ASP A1060     1548   1822   1400     14     77    101       C  
ATOM    628  C   ASP A1060      -3.354  10.823 -20.037  1.00 13.24           C  
ANISOU  628  C   ASP A1060     1558   1987   1485     38     97     88       C  
ATOM    629  O   ASP A1060      -2.886  10.637 -21.169  1.00 13.26           O  
ANISOU  629  O   ASP A1060     1587   2064   1387     27    137    122       O  
ATOM    630  CB  ASP A1060      -3.885  13.110 -19.135  1.00 13.30           C  
ANISOU  630  CB  ASP A1060     1764   1916   1373    -68    -13     56       C  
ATOM    631  CG  ASP A1060      -3.501  14.211 -18.146  1.00 15.58           C  
ANISOU  631  CG  ASP A1060     2248   1942   1730    -56   -171     19       C  
ATOM    632  OD1 ASP A1060      -3.050  13.880 -17.030  1.00 16.05           O  
ANISOU  632  OD1 ASP A1060     2262   2080   1753    121    -80    -18       O  
ATOM    633  OD2 ASP A1060      -3.608  15.395 -18.509  1.00 24.28           O1-
ANISOU  633  OD2 ASP A1060     4320   2211   2692     47   -623    180       O1-
ATOM    634  N   GLN A1061      -4.268  10.039 -19.471  1.00 12.94           N  
ANISOU  634  N   GLN A1061     1435   1881   1598    -41    108    -23       N  
ATOM    635  CA  GLN A1061      -4.958   8.976 -20.180  1.00 14.64           C  
ANISOU  635  CA  GLN A1061     1812   1988   1761     -2     27    -64       C  
ATOM    636  C   GLN A1061      -4.016   8.017 -20.918  1.00 12.97           C  
ANISOU  636  C   GLN A1061     1477   1962   1489    -33    162    -95       C  
ATOM    637  O   GLN A1061      -4.184   7.706 -22.099  1.00 14.67           O  
ANISOU  637  O   GLN A1061     1831   2060   1682   -109   -131   -111       O  
ATOM    638  CB  GLN A1061      -6.028   9.560 -21.095  1.00 16.87           C  
ANISOU  638  CB  GLN A1061     1910   2370   2127     52    -26   -227       C  
ATOM    639  CG  GLN A1061      -7.173  10.190 -20.308  1.00 20.90           C  
ANISOU  639  CG  GLN A1061     2472   2750   2719    104    -28   -216       C  
ATOM    640  CD  GLN A1061      -8.406  10.500 -21.154  0.50 17.19           C  
ANISOU  640  CD  GLN A1061     1962   2533   2037    211    -73    -22       C  
ATOM    641  NE2 GLN A1061      -9.280  11.341 -20.627  0.50 20.78           N  
ANISOU  641  NE2 GLN A1061     2310   3142   2443   -271    293    573       N  
ATOM    642  OE1 GLN A1061      -8.559  10.000 -22.266  0.50 23.74           O  
ANISOU  642  OE1 GLN A1061     2062   3368   3589    536   -739    -65       O  
ATOM    643  N   ILE A1062      -3.047   7.519 -20.158  1.00 12.00           N  
ANISOU  643  N   ILE A1062     1487   1832   1240     52      8    -11       N  
ATOM    644  CA  ILE A1062      -2.108   6.503 -20.620  1.00 12.03           C  
ANISOU  644  CA  ILE A1062     1606   1587   1377    -90     42    -36       C  
ATOM    645  C   ILE A1062      -2.554   5.120 -20.155  1.00 12.28           C  
ANISOU  645  C   ILE A1062     1659   1701   1304   -147    123   -129       C  
ATOM    646  O   ILE A1062      -2.961   4.929 -18.997  1.00 13.82           O  
ANISOU  646  O   ILE A1062     1902   1912   1436    -93    335    -59       O  
ATOM    647  CB  ILE A1062      -0.698   6.802 -20.055  1.00 11.69           C  
ANISOU  647  CB  ILE A1062     1597   1634   1208     62     93     80       C  
ATOM    648  CG1 ILE A1062      -0.227   8.178 -20.540  1.00 12.25           C  
ANISOU  648  CG1 ILE A1062     1458   1793   1401   -114    -19     29       C  
ATOM    649  CG2 ILE A1062       0.264   5.690 -20.404  1.00 12.93           C  
ANISOU  649  CG2 ILE A1062     1545   1891   1475    -24     86     62       C  
ATOM    650  CD1 ILE A1062      -0.075   8.290 -22.044  1.00 12.95           C  
ANISOU  650  CD1 ILE A1062     1519   1609   1789    -38     19    -44       C  
ATOM    651  N   LEU A1063      -2.497   4.159 -21.073  1.00 13.26           N  
ANISOU  651  N   LEU A1063     1724   1880   1433    -93    130   -203       N  
ATOM    652  CA  LEU A1063      -2.857   2.785 -20.769  1.00 14.87           C  
ANISOU  652  CA  LEU A1063     1836   2106   1706     29    213   -138       C  
ATOM    653  C   LEU A1063      -1.657   2.060 -20.147  1.00 14.60           C  
ANISOU  653  C   LEU A1063     1847   2013   1684    -48    163   -132       C  
ATOM    654  O   LEU A1063      -0.529   2.116 -20.665  1.00 16.87           O  
ANISOU  654  O   LEU A1063     1922   2569   1919     17    459    -70       O  
ATOM    655  CB  LEU A1063      -3.321   2.085 -22.056  1.00 17.14           C  
ANISOU  655  CB  LEU A1063     2071   2243   2198    -86    109   -295       C  
ATOM    656  CG  LEU A1063      -3.933   0.688 -22.029  1.00 19.40           C  
ANISOU  656  CG  LEU A1063     2460   2392   2517    208    112   -221       C  
ATOM    657  CD1 LEU A1063      -5.311   0.693 -21.449  1.00 21.65           C  
ANISOU  657  CD1 LEU A1063     2574   2808   2844   -384    408    270       C  
ATOM    658  CD2 LEU A1063      -3.998   0.143 -23.448  0.50 17.75           C  
ANISOU  658  CD2 LEU A1063     2324   2384   2035   -152    102   -239       C  
ATOM    659  N  AILE A1064      -1.927   1.329 -19.076  0.70 14.47           N  
ANISOU  659  N  AILE A1064     1783   1959   1753     53    359   -118       N  
ATOM    660  N  BILE A1064      -1.898   1.411 -19.015  0.30 15.35           N  
ANISOU  660  N  BILE A1064     1905   2071   1855    -24    197    -86       N  
ATOM    661  CA AILE A1064      -0.921   0.569 -18.369  0.70 15.22           C  
ANISOU  661  CA AILE A1064     1861   2163   1758    -35    259    -88       C  
ATOM    662  CA BILE A1064      -0.919   0.521 -18.419  0.30 15.58           C  
ANISOU  662  CA BILE A1064     1946   2110   1861    -22    154    -48       C  
ATOM    663  C  AILE A1064      -1.519  -0.796 -18.000  0.70 14.65           C  
ANISOU  663  C  AILE A1064     1847   2054   1665    129    226     26       C  
ATOM    664  C  BILE A1064      -1.548  -0.844 -18.186  0.30 15.02           C  
ANISOU  664  C  BILE A1064     1907   2026   1772     47    175    -22       C  
ATOM    665  O  AILE A1064      -2.712  -0.901 -17.725  0.70 17.03           O  
ANISOU  665  O  AILE A1064     1950   2340   2181    -58    481    178       O  
ATOM    666  O  BILE A1064      -2.770  -0.999 -18.227  0.30 15.26           O  
ANISOU  666  O  BILE A1064     1995   2002   1797    -45    306    -21       O  
ATOM    667  CB AILE A1064      -0.484   1.335 -17.109  0.70 16.15           C  
ANISOU  667  CB AILE A1064     1979   2099   2058     12    238   -214       C  
ATOM    668  CB BILE A1064      -0.367   1.086 -17.094  0.30 15.79           C  
ANISOU  668  CB BILE A1064     1931   2062   2006     -5    139   -109       C  
ATOM    669  CG1AILE A1064       0.821   0.778 -16.546  0.70 16.04           C  
ANISOU  669  CG1AILE A1064     2245   2122   1727    -61    258    -18       C  
ATOM    670  CG1BILE A1064       0.195   2.487 -17.327  0.30 14.89           C  
ANISOU  670  CG1BILE A1064     1905   1832   1921    -22    206    -17       C  
ATOM    671  CG2AILE A1064      -1.604   1.303 -16.065  0.70 15.72           C  
ANISOU  671  CG2AILE A1064     1935   2245   1793     -2    379   -575       C  
ATOM    672  CG2BILE A1064       0.708   0.170 -16.517  0.30 16.84           C  
ANISOU  672  CG2BILE A1064     2133   2262   2003    -61    119   -115       C  
ATOM    673  CD1AILE A1064       1.462   1.651 -15.484  0.70 15.99           C  
ANISOU  673  CD1AILE A1064     1938   2294   1840     68    195    -87       C  
ATOM    674  CD1BILE A1064       0.795   3.121 -16.104  0.30 17.83           C  
ANISOU  674  CD1BILE A1064     2240   2335   2200    -32     97     39       C  
ATOM    675  N   GLU A1065      -0.698  -1.840 -17.996  1.00 13.85           N  
ANISOU  675  N   GLU A1065     1765   1911   1585     65    304    -61       N  
ATOM    676  CA  GLU A1065      -1.129  -3.128 -17.514  1.00 16.55           C  
ANISOU  676  CA  GLU A1065     2119   2292   1875    113     56     46       C  
ATOM    677  C   GLU A1065      -0.258  -3.439 -16.313  1.00 18.86           C  
ANISOU  677  C   GLU A1065     2324   2853   1986    100    112    158       C  
ATOM    678  O   GLU A1065       0.951  -3.552 -16.431  1.00 19.32           O  
ANISOU  678  O   GLU A1065     2322   3313   1705    194    -38    733       O  
ATOM    679  CB  GLU A1065      -0.984  -4.161 -18.630  1.00 16.66           C  
ANISOU  679  CB  GLU A1065     2177   2165   1986      5    215     -8       C  
ATOM    680  CG  GLU A1065      -1.677  -5.467 -18.365  1.00 19.86           C  
ANISOU  680  CG  GLU A1065     2540   2463   2542    129     -4     35       C  
ATOM    681  CD  GLU A1065      -1.482  -6.436 -19.508  0.75 21.44           C  
ANISOU  681  CD  GLU A1065     3020   2632   2492    201    -21    -53       C  
ATOM    682  OE1 GLU A1065      -1.771  -6.059 -20.666  0.75 26.74           O  
ANISOU  682  OE1 GLU A1065     4306   2641   3213    464   -317   -525       O  
ATOM    683  OE2 GLU A1065      -1.020  -7.562 -19.254  0.75 30.25           O1-
ANISOU  683  OE2 GLU A1065     4050   3581   3863    356    112   -265       O1-
ATOM    684  N   ILE A1066      -0.889  -3.506 -15.144  1.00 20.07           N  
ANISOU  684  N   ILE A1066     2374   3201   2049    103      6    273       N  
ATOM    685  CA  ILE A1066      -0.178  -3.558 -13.869  1.00 21.68           C  
ANISOU  685  CA  ILE A1066     2604   3047   2584    183     45    135       C  
ATOM    686  C   ILE A1066      -0.468  -4.962 -13.415  1.00 24.54           C  
ANISOU  686  C   ILE A1066     2867   3518   2937    150     28    375       C  
ATOM    687  O   ILE A1066      -1.607  -5.319 -13.075  1.00 24.83           O  
ANISOU  687  O   ILE A1066     2977   3873   2581    313     89    806       O  
ATOM    688  CB  ILE A1066      -0.694  -2.511 -12.852  1.00 21.95           C  
ANISOU  688  CB  ILE A1066     2853   3013   2471    108    -72    183       C  
ATOM    689  CG1 ILE A1066      -0.428  -1.088 -13.352  1.00 23.22           C  
ANISOU  689  CG1 ILE A1066     2994   3040   2788     26    128    120       C  
ATOM    690  CG2 ILE A1066      -0.045  -2.705 -11.486  0.50 19.95           C  
ANISOU  690  CG2 ILE A1066     2473   2965   2140    128   -116    -48       C  
ATOM    691  CD1 ILE A1066      -1.312  -0.039 -12.702  0.50 19.07           C  
ANISOU  691  CD1 ILE A1066     2487   2615   2143     23      0    -28       C  
ATOM    692  N   CYS A1067       0.552  -5.796 -13.500  1.00 28.68           N  
ANISOU  692  N   CYS A1067     3483   3681   3730     79     84    199       N  
ATOM    693  CA  CYS A1067       0.430  -7.143 -13.029  1.00 28.56           C  
ANISOU  693  CA  CYS A1067     3522   3634   3693     16     75    203       C  
ATOM    694  C   CYS A1067      -0.797  -7.830 -13.635  1.00 28.82           C  
ANISOU  694  C   CYS A1067     3580   3685   3684    -68     56    148       C  
ATOM    695  O   CYS A1067      -1.537  -8.514 -12.921  1.00 30.49           O  
ANISOU  695  O   CYS A1067     3791   3522   4271   -388    149    341       O  
ATOM    696  CB  CYS A1067       0.311  -7.108 -11.509  1.00 29.81           C  
ANISOU  696  CB  CYS A1067     3608   3674   4044     42     36    101       C  
ATOM    697  SG  CYS A1067       0.464  -8.700 -10.818  1.00 31.82           S  
ANISOU  697  SG  CYS A1067     4036   3869   4184    219   -161    584       S  
ATOM    698  N   GLY A1068      -1.031  -7.630 -14.933  1.00 28.06           N  
ANISOU  698  N   GLY A1068     3507   3468   3686     22     85    202       N  
ATOM    699  CA  GLY A1068      -2.100  -8.344 -15.663  1.00 25.62           C  
ANISOU  699  CA  GLY A1068     3195   3248   3291     21     29    133       C  
ATOM    700  C   GLY A1068      -3.427  -7.588 -15.808  1.00 25.71           C  
ANISOU  700  C   GLY A1068     3299   3200   3269     -1     12    102       C  
ATOM    701  O   GLY A1068      -4.319  -8.002 -16.553  1.00 27.29           O  
ANISOU  701  O   GLY A1068     3301   3487   3581    122    112     77       O  
ATOM    702  N   HIS A1069      -3.566  -6.482 -15.094  1.00 23.21           N  
ANISOU  702  N   HIS A1069     2998   3047   2771     82    127    263       N  
ATOM    703  CA  HIS A1069      -4.829  -5.753 -15.054  1.00 21.22           C  
ANISOU  703  CA  HIS A1069     2758   2745   2557     -6    107    196       C  
ATOM    704  C   HIS A1069      -4.627  -4.424 -15.753  1.00 19.08           C  
ANISOU  704  C   HIS A1069     2497   2483   2269   -109     80    199       C  
ATOM    705  O   HIS A1069      -3.708  -3.678 -15.424  1.00 21.20           O  
ANISOU  705  O   HIS A1069     2488   3184   2384   -218     23    633       O  
ATOM    706  CB  HIS A1069      -5.248  -5.507 -13.605  1.00 21.53           C  
ANISOU  706  CB  HIS A1069     2898   2741   2539   -101    149    238       C  
ATOM    707  CG  HIS A1069      -5.662  -6.745 -12.873  1.00 23.57           C  
ANISOU  707  CG  HIS A1069     3281   2879   2794   -105    239    338       C  
ATOM    708  CD2 HIS A1069      -4.981  -7.876 -12.568  1.00 24.65           C  
ANISOU  708  CD2 HIS A1069     3600   3287   2476   -240    747    513       C  
ATOM    709  ND1 HIS A1069      -6.925  -6.906 -12.348  1.00 25.75           N  
ANISOU  709  ND1 HIS A1069     3716   3159   2906   -488    470    478       N  
ATOM    710  CE1 HIS A1069      -7.005  -8.084 -11.752  1.00 24.77           C  
ANISOU  710  CE1 HIS A1069     3779   2772   2858   -290    418    639       C  
ATOM    711  NE2 HIS A1069      -5.839  -8.694 -11.873  1.00 25.95           N  
ANISOU  711  NE2 HIS A1069     3947   3241   2673   -355    406    526       N  
ATOM    712  N   LYS A1070      -5.498  -4.096 -16.694  1.00 15.24           N  
ANISOU  712  N   LYS A1070     1968   1964   1859     26    196    -28       N  
ATOM    713  CA  LYS A1070      -5.336  -2.859 -17.428  1.00 16.26           C  
ANISOU  713  CA  LYS A1070     2159   2080   1940      2     96    -76       C  
ATOM    714  C   LYS A1070      -5.996  -1.677 -16.718  1.00 14.32           C  
ANISOU  714  C   LYS A1070     1836   1826   1776    -25    237    -79       C  
ATOM    715  O   LYS A1070      -7.005  -1.818 -16.039  1.00 16.02           O  
ANISOU  715  O   LYS A1070     2187   1890   2006    -66    303    -31       O  
ATOM    716  CB  LYS A1070      -5.877  -3.009 -18.844  1.00 16.60           C  
ANISOU  716  CB  LYS A1070     2248   2014   2044    117    116    -49       C  
ATOM    717  CG  LYS A1070      -5.066  -3.988 -19.676  1.00 18.89           C  
ANISOU  717  CG  LYS A1070     2559   2441   2177     15    111   -188       C  
ATOM    718  CD  LYS A1070      -5.535  -4.039 -21.101  1.00 19.06           C  
ANISOU  718  CD  LYS A1070     2520   2415   2305    122    100   -253       C  
ATOM    719  CE  LYS A1070      -4.875  -5.209 -21.834  1.00 21.03           C  
ANISOU  719  CE  LYS A1070     2696   2631   2660    371    -39   -205       C  
ATOM    720  NZ  LYS A1070      -5.310  -5.302 -23.256  1.00 21.98           N1+
ANISOU  720  NZ  LYS A1070     2888   2906   2555    412    156   -397       N1+
ATOM    721  N   ALA A1071      -5.417  -0.501 -16.909  1.00 13.54           N  
ANISOU  721  N   ALA A1071     1784   1693   1666    -43    258    -59       N  
ATOM    722  CA  ALA A1071      -5.963   0.737 -16.361  1.00 13.80           C  
ANISOU  722  CA  ALA A1071     1739   1738   1765    -55    123    -20       C  
ATOM    723  C   ALA A1071      -5.522   1.879 -17.243  1.00 12.73           C  
ANISOU  723  C   ALA A1071     1558   1739   1540    -97    247    -68       C  
ATOM    724  O   ALA A1071      -4.520   1.781 -17.937  1.00 15.09           O  
ANISOU  724  O   ALA A1071     1561   2158   2012     78    575   -198       O  
ATOM    725  CB  ALA A1071      -5.481   0.969 -14.934  1.00 15.00           C  
ANISOU  725  CB  ALA A1071     1826   1934   1936    -31    280     34       C  
ATOM    726  N   ILE A1072      -6.267   2.969 -17.190  1.00 12.92           N  
ANISOU  726  N   ILE A1072     1647   1662   1596    -71    311    -92       N  
ATOM    727  CA  ILE A1072      -5.900   4.202 -17.860  1.00 13.03           C  
ANISOU  727  CA  ILE A1072     1573   1778   1600   -140    108    -56       C  
ATOM    728  C   ILE A1072      -5.805   5.303 -16.827  1.00 11.98           C  
ANISOU  728  C   ILE A1072     1437   1552   1563    -82     18      3       C  
ATOM    729  O   ILE A1072      -6.649   5.419 -15.960  1.00 13.24           O  
ANISOU  729  O   ILE A1072     1602   1803   1625   -177     89     -6       O  
ATOM    730  CB  ILE A1072      -6.945   4.563 -18.908  1.00 14.51           C  
ANISOU  730  CB  ILE A1072     1835   1862   1816   -193    240     25       C  
ATOM    731  CG1 ILE A1072      -6.862   3.542 -20.038  1.00 15.92           C  
ANISOU  731  CG1 ILE A1072     1889   2321   1839   -300    122   -162       C  
ATOM    732  CG2 ILE A1072      -6.716   5.964 -19.427  1.00 15.60           C  
ANISOU  732  CG2 ILE A1072     2150   2091   1686   -177   -215    148       C  
ATOM    733  CD1 ILE A1072      -7.993   3.613 -21.007  1.00 18.55           C  
ANISOU  733  CD1 ILE A1072     2117   2517   2415   -182   -100    -70       C  
ATOM    734  N   GLY A1073      -4.761   6.104 -16.913  1.00 11.71           N  
ANISOU  734  N   GLY A1073     1422   1607   1420     -9     50    -17       N  
ATOM    735  CA  GLY A1073      -4.660   7.245 -16.049  1.00 11.88           C  
ANISOU  735  CA  GLY A1073     1550   1633   1329   -140      4    -49       C  
ATOM    736  C   GLY A1073      -3.418   8.053 -16.299  1.00 11.17           C  
ANISOU  736  C   GLY A1073     1390   1664   1190    -90     56    -74       C  
ATOM    737  O   GLY A1073      -2.693   7.856 -17.284  1.00 12.40           O  
ANISOU  737  O   GLY A1073     1735   1744   1231   -148    150    -72       O  
ATOM    738  N   THR A1074      -3.172   8.979 -15.384  1.00 11.30           N  
ANISOU  738  N   THR A1074     1560   1613   1117   -131     18   -109       N  
ATOM    739  CA  THR A1074      -2.084   9.911 -15.529  1.00 11.11           C  
ANISOU  739  CA  THR A1074     1500   1634   1087   -120     49     25       C  
ATOM    740  C   THR A1074      -0.769   9.270 -15.096  1.00 10.89           C  
ANISOU  740  C   THR A1074     1323   1735   1080   -247     44     89       C  
ATOM    741  O   THR A1074      -0.680   8.613 -14.045  1.00 11.91           O  
ANISOU  741  O   THR A1074     1569   1913   1041   -229    105    283       O  
ATOM    742  CB  THR A1074      -2.372  11.157 -14.699  1.00 11.92           C  
ANISOU  742  CB  THR A1074     1687   1581   1260    -61     13    -65       C  
ATOM    743  CG2 THR A1074      -1.193  12.105 -14.694  1.00 12.78           C  
ANISOU  743  CG2 THR A1074     1853   1673   1330   -201    -25    -82       C  
ATOM    744  OG1 THR A1074      -3.538  11.818 -15.234  1.00 13.62           O  
ANISOU  744  OG1 THR A1074     1628   1890   1654    194    -32    -66       O  
ATOM    745  N   VAL A1075       0.250   9.458 -15.928  1.00 11.51           N  
ANISOU  745  N   VAL A1075     1535   1733   1103   -111     68    216       N  
ATOM    746  CA  VAL A1075       1.585   8.971 -15.655  1.00 11.76           C  
ANISOU  746  CA  VAL A1075     1593   1679   1196    -68    -72    113       C  
ATOM    747  C   VAL A1075       2.532  10.146 -15.728  1.00 12.66           C  
ANISOU  747  C   VAL A1075     1505   2025   1278    -61      9    211       C  
ATOM    748  O   VAL A1075       2.561  10.871 -16.725  1.00 13.43           O  
ANISOU  748  O   VAL A1075     1724   2173   1203   -248   -135    300       O  
ATOM    749  CB  VAL A1075       2.007   7.894 -16.673  1.00 12.51           C  
ANISOU  749  CB  VAL A1075     1737   1788   1228    -17    -25    199       C  
ATOM    750  CG1 VAL A1075       3.468   7.468 -16.461  1.00 13.54           C  
ANISOU  750  CG1 VAL A1075     1882   1911   1350     29     44     35       C  
ATOM    751  CG2 VAL A1075       1.043   6.699 -16.571  1.00 14.01           C  
ANISOU  751  CG2 VAL A1075     1915   1890   1518    -44    -46    -72       C  
ATOM    752  N   LEU A1076       3.290  10.338 -14.655  1.00 12.19           N  
ANISOU  752  N   LEU A1076     1412   2011   1208   -173   -117    195       N  
ATOM    753  CA  LEU A1076       4.335  11.341 -14.632  1.00 12.27           C  
ANISOU  753  CA  LEU A1076     1488   1789   1384     16    -44    199       C  
ATOM    754  C   LEU A1076       5.635  10.666 -15.029  1.00 12.20           C  
ANISOU  754  C   LEU A1076     1407   1807   1419      4    100    154       C  
ATOM    755  O   LEU A1076       5.924   9.544 -14.594  1.00 14.48           O  
ANISOU  755  O   LEU A1076     1706   2008   1785    252    195    363       O  
ATOM    756  CB  LEU A1076       4.456  11.973 -13.244  1.00 11.90           C  
ANISOU  756  CB  LEU A1076     1411   1717   1391    -98   -142    108       C  
ATOM    757  CG  LEU A1076       3.150  12.454 -12.630  1.00 13.14           C  
ANISOU  757  CG  LEU A1076     1789   1914   1287   -109    -33     75       C  
ATOM    758  CD1 LEU A1076       3.416  13.013 -11.236  1.00 13.43           C  
ANISOU  758  CD1 LEU A1076     1771   1773   1556   -297     71    -71       C  
ATOM    759  CD2 LEU A1076       2.471  13.495 -13.519  1.00 14.08           C  
ANISOU  759  CD2 LEU A1076     1662   2251   1434    131    195    194       C  
ATOM    760  N   VAL A1077       6.416  11.342 -15.860  1.00 11.31           N  
ANISOU  760  N   VAL A1077     1371   1718   1208    -79    -24    252       N  
ATOM    761  CA  VAL A1077       7.665  10.790 -16.354  1.00 13.00           C  
ANISOU  761  CA  VAL A1077     1631   1820   1487   -100    -74     35       C  
ATOM    762  C   VAL A1077       8.787  11.758 -15.996  1.00 12.76           C  
ANISOU  762  C   VAL A1077     1518   1911   1417   -123    -70     74       C  
ATOM    763  O   VAL A1077       8.715  12.962 -16.280  1.00 13.24           O  
ANISOU  763  O   VAL A1077     1448   2039   1543   -177   -165     29       O  
ATOM    764  CB  VAL A1077       7.627  10.590 -17.878  1.00 12.93           C  
ANISOU  764  CB  VAL A1077     1686   1838   1388   -114     -1     48       C  
ATOM    765  CG1 VAL A1077       8.960  10.111 -18.397  1.00 14.31           C  
ANISOU  765  CG1 VAL A1077     1946   1954   1536    -56     24    -15       C  
ATOM    766  CG2 VAL A1077       6.530   9.616 -18.252  1.00 14.31           C  
ANISOU  766  CG2 VAL A1077     1899   2102   1434     44    -81   -110       C  
ATOM    767  N   GLY A1078       9.828  11.230 -15.367  1.00 14.68           N  
ANISOU  767  N   GLY A1078     1625   2008   1942   -177   -259     46       N  
ATOM    768  CA  GLY A1078      10.950  12.058 -14.957  1.00 16.36           C  
ANISOU  768  CA  GLY A1078     1860   2225   2131    -65   -289     92       C  
ATOM    769  C   GLY A1078      11.874  11.307 -14.030  1.00 17.83           C  
ANISOU  769  C   GLY A1078     1987   2399   2389    -58   -377    139       C  
ATOM    770  O   GLY A1078      11.794  10.088 -13.902  1.00 18.00           O  
ANISOU  770  O   GLY A1078     1763   2550   2525    -86   -625    346       O  
ATOM    771  N   PRO A1079      12.782  12.043 -13.399  1.00 19.61           N  
ANISOU  771  N   PRO A1079     2216   2644   2588   -187   -451    106       N  
ATOM    772  CA  PRO A1079      13.901  11.435 -12.673  1.00 20.90           C  
ANISOU  772  CA  PRO A1079     2437   2745   2758   -147   -444     53       C  
ATOM    773  C   PRO A1079      13.615  10.912 -11.260  1.00 24.27           C  
ANISOU  773  C   PRO A1079     2992   3079   3150   -307   -401   -106       C  
ATOM    774  O   PRO A1079      14.194  11.384 -10.275  1.00 26.57           O  
ANISOU  774  O   PRO A1079     3250   3795   3048   -286   -908     29       O  
ATOM    775  CB  PRO A1079      14.952  12.549 -12.660  1.00 23.76           C  
ANISOU  775  CB  PRO A1079     2822   2876   3327   -255   -419      8       C  
ATOM    776  CG  PRO A1079      14.172  13.819 -12.748  1.00 18.42           C  
ANISOU  776  CG  PRO A1079     1885   2571   2539     -2   -481    -62       C  
ATOM    777  CD  PRO A1079      12.854  13.512 -13.423  1.00 18.80           C  
ANISOU  777  CD  PRO A1079     1905   2721   2515     47   -608     25       C  
ATOM    778  N   THR A1080      12.778   9.892 -11.187  1.00 22.85           N  
ANISOU  778  N   THR A1080     2693   3005   2982   -314   -148    -38       N  
ATOM    779  CA  THR A1080      12.422   9.234  -9.937  1.00 21.42           C  
ANISOU  779  CA  THR A1080     2654   2833   2650    -96   -263    -13       C  
ATOM    780  C   THR A1080      13.409   8.106  -9.611  1.00 22.11           C  
ANISOU  780  C   THR A1080     2641   2951   2809   -169   -221     14       C  
ATOM    781  O   THR A1080      13.869   7.398 -10.507  1.00 22.46           O  
ANISOU  781  O   THR A1080     2451   3042   3038   -233     26     72       O  
ATOM    782  CB  THR A1080      10.990   8.662 -10.061  1.00 19.38           C  
ANISOU  782  CB  THR A1080     2349   2615   2400   -148   -193    -17       C  
ATOM    783  CG2 THR A1080      10.892   7.660 -11.215  1.00 18.49           C  
ANISOU  783  CG2 THR A1080     2489   2603   1933    -41   -178    112       C  
ATOM    784  OG1 THR A1080      10.590   8.043  -8.831  1.00 19.47           O  
ANISOU  784  OG1 THR A1080     2626   3007   1762   -167   -188    125       O  
ATOM    785  N   PRO A1081      13.756   7.941  -8.328  1.00 24.85           N  
ANISOU  785  N   PRO A1081     3006   3218   3216     41   -144    -58       N  
ATOM    786  CA  PRO A1081      14.714   6.887  -7.982  1.00 23.76           C  
ANISOU  786  CA  PRO A1081     2839   3165   3021     44   -189     23       C  
ATOM    787  C   PRO A1081      14.136   5.484  -8.111  1.00 22.99           C  
ANISOU  787  C   PRO A1081     2770   3049   2915    100    -81     42       C  
ATOM    788  O   PRO A1081      14.873   4.518  -8.283  1.00 24.41           O  
ANISOU  788  O   PRO A1081     2599   3433   3239    171   -373    132       O  
ATOM    789  CB  PRO A1081      15.065   7.185  -6.521  1.00 25.11           C  
ANISOU  789  CB  PRO A1081     3030   3304   3204    119   -186   -108       C  
ATOM    790  CG  PRO A1081      14.433   8.508  -6.200  1.00 27.62           C  
ANISOU  790  CG  PRO A1081     3521   3501   3468    106   -377   -106       C  
ATOM    791  CD  PRO A1081      13.310   8.693  -7.147  1.00 25.15           C  
ANISOU  791  CD  PRO A1081     2956   3322   3277    128   -338    -55       C  
ATOM    792  N   VAL A1082      12.816   5.379  -8.020  1.00 22.12           N  
ANISOU  792  N   VAL A1082     2671   2997   2735    -31   -292     80       N  
ATOM    793  CA  VAL A1082      12.129   4.101  -8.126  1.00 22.02           C  
ANISOU  793  CA  VAL A1082     2743   2951   2672     -7   -135    151       C  
ATOM    794  C   VAL A1082      10.894   4.361  -8.979  1.00 19.49           C  
ANISOU  794  C   VAL A1082     2338   2662   2401    -27   -170    208       C  
ATOM    795  O   VAL A1082      10.275   5.413  -8.858  1.00 19.69           O  
ANISOU  795  O   VAL A1082     2178   2909   2392    -63   -288    139       O  
ATOM    796  CB  VAL A1082      11.689   3.593  -6.729  1.00 23.52           C  
ANISOU  796  CB  VAL A1082     3054   3086   2794    -32   -369    208       C  
ATOM    797  CG1 VAL A1082      10.998   4.681  -5.980  1.00 27.05           C  
ANISOU  797  CG1 VAL A1082     3448   3785   3045    109   -276    121       C  
ATOM    798  CG2 VAL A1082      10.802   2.384  -6.830  1.00 25.29           C  
ANISOU  798  CG2 VAL A1082     3207   3416   2984   -169   -237    279       C  
ATOM    799  N   ASN A1083      10.556   3.424  -9.851  1.00 18.15           N  
ANISOU  799  N   ASN A1083     2265   2421   2207     86    -57    350       N  
ATOM    800  CA  ASN A1083       9.293   3.495 -10.575  1.00 16.82           C  
ANISOU  800  CA  ASN A1083     2158   2210   2020     57    -39    258       C  
ATOM    801  C   ASN A1083       8.166   3.225  -9.607  1.00 15.93           C  
ANISOU  801  C   ASN A1083     2046   2075   1930     70     30    268       C  
ATOM    802  O   ASN A1083       8.169   2.199  -8.920  1.00 17.39           O  
ANISOU  802  O   ASN A1083     2419   2119   2067    256      8    693       O  
ATOM    803  CB  ASN A1083       9.248   2.454 -11.685  1.00 17.34           C  
ANISOU  803  CB  ASN A1083     2242   2258   2088    251     56    319       C  
ATOM    804  CG  ASN A1083      10.169   2.789 -12.827  1.00 18.49           C  
ANISOU  804  CG  ASN A1083     2110   2536   2376    255    148    382       C  
ATOM    805  ND2 ASN A1083      10.619   1.764 -13.543  1.00 19.31           N  
ANISOU  805  ND2 ASN A1083     2366   2391   2580    374    346    257       N  
ATOM    806  OD1 ASN A1083      10.477   3.957 -13.067  1.00 21.87           O  
ANISOU  806  OD1 ASN A1083     2520   2754   3034    313    634    673       O  
ATOM    807  N  AILE A1084       7.210   4.147  -9.549  0.50 14.66           N  
ANISOU  807  N  AILE A1084     1914   1961   1694     50    -92    211       N  
ATOM    808  N  BILE A1084       7.203   4.139  -9.565  0.50 14.92           N  
ANISOU  808  N  BILE A1084     1929   1992   1746     60    -91    217       N  
ATOM    809  CA AILE A1084       6.167   4.133  -8.530  0.50 14.63           C  
ANISOU  809  CA AILE A1084     1913   1916   1727     31   -107    154       C  
ATOM    810  CA BILE A1084       6.164   4.139  -8.544  0.50 14.86           C  
ANISOU  810  CA BILE A1084     1929   1968   1749     67   -106    173       C  
ATOM    811  C  AILE A1084       4.786   4.072  -9.187  0.50 14.15           C  
ANISOU  811  C  AILE A1084     1862   1887   1624     16   -168    157       C  
ATOM    812  C  BILE A1084       4.782   4.073  -9.193  0.50 14.32           C  
ANISOU  812  C  BILE A1084     1880   1914   1645     27   -167    162       C  
ATOM    813  O  AILE A1084       4.453   4.926 -10.006  0.50 14.25           O  
ANISOU  813  O  AILE A1084     1924   1849   1639    -43   -139    303       O  
ATOM    814  O  BILE A1084       4.443   4.924 -10.013  0.50 14.37           O  
ANISOU  814  O  BILE A1084     1949   1864   1646    -31   -138    308       O  
ATOM    815  CB AILE A1084       6.252   5.403  -7.665  0.50 14.57           C  
ANISOU  815  CB AILE A1084     1866   1984   1682     98   -134    139       C  
ATOM    816  CB BILE A1084       6.247   5.424  -7.709  0.50 15.25           C  
ANISOU  816  CB BILE A1084     1933   2092   1766    112   -125    138       C  
ATOM    817  CG1AILE A1084       7.448   5.318  -6.711  0.50 15.54           C  
ANISOU  817  CG1AILE A1084     2077   1863   1962      2    -15     -8       C  
ATOM    818  CG1BILE A1084       7.603   5.507  -7.004  0.50 17.90           C  
ANISOU  818  CG1BILE A1084     2355   2293   2153     70     52     26       C  
ATOM    819  CG2AILE A1084       4.959   5.633  -6.897  0.50 15.50           C  
ANISOU  819  CG2AILE A1084     2092   2105   1692      4    -98    184       C  
ATOM    820  CG2BILE A1084       5.106   5.499  -6.712  0.50 16.08           C  
ANISOU  820  CG2BILE A1084     2070   2136   1901     13   -118    196       C  
ATOM    821  CD1AILE A1084       7.929   6.682  -6.220  0.50 15.66           C  
ANISOU  821  CD1AILE A1084     2120   1871   1958   -238    -75      0       C  
ATOM    822  CD1BILE A1084       7.820   4.431  -5.975  0.50 20.78           C  
ANISOU  822  CD1BILE A1084     2709   2696   2490    112     61      4       C  
ATOM    823  N   ILE A1085       3.993   3.066  -8.819  1.00 14.02           N  
ANISOU  823  N   ILE A1085     1924   1803   1600     85   -185    187       N  
ATOM    824  CA  ILE A1085       2.564   3.050  -9.117  1.00 13.46           C  
ANISOU  824  CA  ILE A1085     1947   1719   1448    -11   -204    146       C  
ATOM    825  C   ILE A1085       1.844   3.613  -7.903  1.00 12.75           C  
ANISOU  825  C   ILE A1085     1860   1644   1340     46   -297    192       C  
ATOM    826  O   ILE A1085       1.816   2.989  -6.843  1.00 14.86           O  
ANISOU  826  O   ILE A1085     2266   2018   1363    -76   -168    290       O  
ATOM    827  CB  ILE A1085       2.028   1.627  -9.412  1.00 13.38           C  
ANISOU  827  CB  ILE A1085     2018   1753   1313     -7   -228    168       C  
ATOM    828  CG1 ILE A1085       2.862   0.931 -10.501  1.00 15.16           C  
ANISOU  828  CG1 ILE A1085     2179   1828   1750   -164   -275    139       C  
ATOM    829  CG2 ILE A1085       0.560   1.683  -9.802  1.00 15.68           C  
ANISOU  829  CG2 ILE A1085     2311   1969   1676    -51   -230     17       C  
ATOM    830  CD1 ILE A1085       2.999   1.722 -11.789  1.00 17.73           C  
ANISOU  830  CD1 ILE A1085     2661   2107   1966   -237    258    116       C  
ATOM    831  N   GLY A1086       1.311   4.818  -8.050  1.00 13.45           N  
ANISOU  831  N   GLY A1086     1980   1758   1371    121   -137    150       N  
ATOM    832  CA  GLY A1086       0.679   5.513  -6.955  1.00 13.18           C  
ANISOU  832  CA  GLY A1086     2003   1675   1327    139   -159    256       C  
ATOM    833  C   GLY A1086      -0.817   5.269  -6.905  1.00 13.25           C  
ANISOU  833  C   GLY A1086     1971   1802   1260     -2    -20     63       C  
ATOM    834  O   GLY A1086      -1.394   4.533  -7.723  1.00 13.12           O  
ANISOU  834  O   GLY A1086     2090   1732   1163   -223     54     40       O  
ATOM    835  N   ARG A1087      -1.466   5.925  -5.952  1.00 13.81           N  
ANISOU  835  N   ARG A1087     2250   1761   1237      0    -61   -145       N  
ATOM    836  CA  ARG A1087      -2.856   5.669  -5.691  1.00 13.85           C  
ANISOU  836  CA  ARG A1087     2074   1801   1387     78     33     16       C  
ATOM    837  C   ARG A1087      -3.733   5.955  -6.892  1.00 13.21           C  
ANISOU  837  C   ARG A1087     2024   1733   1260   -111    101     -6       C  
ATOM    838  O   ARG A1087      -4.774   5.336  -7.057  1.00 15.47           O  
ANISOU  838  O   ARG A1087     2522   2164   1189   -230    199   -102       O  
ATOM    839  CB  ARG A1087      -3.334   6.478  -4.488  1.00 13.71           C  
ANISOU  839  CB  ARG A1087     2158   1761   1287    105    -30    -71       C  
ATOM    840  CG  ARG A1087      -2.739   6.008  -3.170  1.00 14.34           C  
ANISOU  840  CG  ARG A1087     2366   1926   1155    122   -108     79       C  
ATOM    841  CD  ARG A1087      -3.424   6.703  -1.987  1.00 15.33           C  
ANISOU  841  CD  ARG A1087     2387   2089   1347    345    -35    -29       C  
ATOM    842  NE  ARG A1087      -3.165   8.148  -1.975  1.00 15.89           N  
ANISOU  842  NE  ARG A1087     2444   2358   1236    445    -48    -62       N  
ATOM    843  CZ  ARG A1087      -4.015   9.077  -2.414  1.00 16.60           C  
ANISOU  843  CZ  ARG A1087     2677   2143   1484    158   -215    -98       C  
ATOM    844  NH1 ARG A1087      -5.223   8.750  -2.872  1.00 16.97           N1+
ANISOU  844  NH1 ARG A1087     2839   2081   1527    343   -453   -267       N1+
ATOM    845  NH2 ARG A1087      -3.657  10.353  -2.376  1.00 18.06           N  
ANISOU  845  NH2 ARG A1087     3010   1958   1891    489   -447   -186       N  
ATOM    846  N   ASN A1088      -3.335   6.901  -7.740  1.00 12.88           N  
ANISOU  846  N   ASN A1088     1797   1897   1199   -222     -7     32       N  
ATOM    847  CA  ASN A1088      -4.185   7.214  -8.883  1.00 12.93           C  
ANISOU  847  CA  ASN A1088     1773   1859   1279     29      6    -92       C  
ATOM    848  C   ASN A1088      -4.444   5.985  -9.756  1.00 13.15           C  
ANISOU  848  C   ASN A1088     1816   1981   1196   -171    -12   -114       C  
ATOM    849  O   ASN A1088      -5.540   5.812 -10.273  1.00 15.83           O  
ANISOU  849  O   ASN A1088     1795   2498   1718   -237    289   -695       O  
ATOM    850  CB  ASN A1088      -3.632   8.381  -9.707  1.00 11.97           C  
ANISOU  850  CB  ASN A1088     1560   1786   1200     96    -52    -92       C  
ATOM    851  CG  ASN A1088      -2.421   8.004 -10.532  1.00 12.75           C  
ANISOU  851  CG  ASN A1088     1518   2028   1295     76    -12     -9       C  
ATOM    852  ND2 ASN A1088      -2.503   8.240 -11.855  1.00 12.70           N  
ANISOU  852  ND2 ASN A1088     1617   1878   1328     13    281    135       N  
ATOM    853  OD1 ASN A1088      -1.415   7.536  -9.987  1.00 12.76           O  
ANISOU  853  OD1 ASN A1088     1788   1761   1297     63   -207     11       O  
ATOM    854  N   LEU A1089      -3.432   5.158  -9.956  1.00 13.27           N  
ANISOU  854  N   LEU A1089     2025   1684   1331   -190   -224    -21       N  
ATOM    855  CA  LEU A1089      -3.599   3.957 -10.765  1.00 13.08           C  
ANISOU  855  CA  LEU A1089     1885   1706   1375    -46   -167    -52       C  
ATOM    856  C   LEU A1089      -3.981   2.741  -9.952  1.00 13.86           C  
ANISOU  856  C   LEU A1089     2086   1919   1260   -125   -244     27       C  
ATOM    857  O   LEU A1089      -4.666   1.850 -10.456  1.00 14.95           O  
ANISOU  857  O   LEU A1089     2203   2127   1351    -79   -500    -33       O  
ATOM    858  CB  LEU A1089      -2.351   3.670 -11.590  1.00 14.51           C  
ANISOU  858  CB  LEU A1089     2111   1765   1633    -19   -232   -152       C  
ATOM    859  CG  LEU A1089      -2.167   4.609 -12.774  1.00 15.99           C  
ANISOU  859  CG  LEU A1089     2150   2127   1796    -85    307   -252       C  
ATOM    860  CD1 LEU A1089      -0.848   4.354 -13.486  1.00 20.35           C  
ANISOU  860  CD1 LEU A1089     2534   2649   2548   -392    -20   -418       C  
ATOM    861  CD2 LEU A1089      -3.319   4.454 -13.724  1.00 19.01           C  
ANISOU  861  CD2 LEU A1089     2224   3062   1937    181    260    425       C  
ATOM    862  N   LEU A1090      -3.551   2.691  -8.692  1.00 14.32           N  
ANISOU  862  N   LEU A1090     2246   1863   1333   -159   -335      1       N  
ATOM    863  CA  LEU A1090      -4.019   1.621  -7.815  1.00 14.11           C  
ANISOU  863  CA  LEU A1090     2076   1816   1470    -56   -173     11       C  
ATOM    864  C   LEU A1090      -5.539   1.623  -7.740  1.00 14.58           C  
ANISOU  864  C   LEU A1090     2190   1853   1496     23   -162     66       C  
ATOM    865  O   LEU A1090      -6.171   0.563  -7.755  1.00 15.08           O  
ANISOU  865  O   LEU A1090     2183   2051   1492    -38   -247    110       O  
ATOM    866  CB  LEU A1090      -3.406   1.753  -6.417  1.00 14.85           C  
ANISOU  866  CB  LEU A1090     2412   1718   1512   -133   -132    232       C  
ATOM    867  CG  LEU A1090      -1.895   1.566  -6.374  1.00 15.82           C  
ANISOU  867  CG  LEU A1090     2346   2027   1637   -218   -262    238       C  
ATOM    868  CD1 LEU A1090      -1.374   1.803  -4.965  1.00 17.12           C  
ANISOU  868  CD1 LEU A1090     2402   2423   1680   -139   -485    149       C  
ATOM    869  CD2 LEU A1090      -1.474   0.188  -6.877  1.00 16.31           C  
ANISOU  869  CD2 LEU A1090     2137   2308   1750    -42   -208     53       C  
ATOM    870  N  ATHR A1091      -6.157   2.807  -7.641  0.33 13.75           N  
ANISOU  870  N  ATHR A1091     2037   1795   1389     33    -77      5       N  
ATOM    871  N  BTHR A1091      -6.143   2.804  -7.661  0.33 14.61           N  
ANISOU  871  N  BTHR A1091     2126   1889   1537     26    -98     10       N  
ATOM    872  N  CTHR A1091      -6.084   2.824  -7.696  0.33 13.67           N  
ANISOU  872  N  CTHR A1091     2041   1758   1395     -1    -73     26       N  
ATOM    873  CA ATHR A1091      -7.628   2.872  -7.607  0.33 14.04           C  
ANISOU  873  CA ATHR A1091     2001   1887   1444    105   -114    -27       C  
ATOM    874  CA BTHR A1091      -7.594   2.871  -7.601  0.33 15.37           C  
ANISOU  874  CA BTHR A1091     2130   2027   1681     90   -162    -31       C  
ATOM    875  CA CTHR A1091      -7.499   3.041  -7.612  0.33 13.58           C  
ANISOU  875  CA CTHR A1091     1939   1809   1409     13    -98    -16       C  
ATOM    876  C  ATHR A1091      -8.217   2.380  -8.924  0.33 14.56           C  
ANISOU  876  C  ATHR A1091     2007   1990   1534    103   -138    -29       C  
ATOM    877  C  BTHR A1091      -8.232   2.423  -8.917  0.33 15.39           C  
ANISOU  877  C  BTHR A1091     2088   2087   1670     93   -155    -32       C  
ATOM    878  C  CTHR A1091      -8.232   2.552  -8.884  0.33 14.59           C  
ANISOU  878  C  CTHR A1091     2003   1992   1546     60   -108    -23       C  
ATOM    879  O  ATHR A1091      -9.206   1.643  -8.930  0.33 15.47           O  
ANISOU  879  O  ATHR A1091     2288   2120   1467    183   -342    -63       O  
ATOM    880  O  BTHR A1091      -9.272   1.760  -8.913  0.33 16.02           O  
ANISOU  880  O  BTHR A1091     2290   2199   1595    186   -322    -90       O  
ATOM    881  O  CTHR A1091      -9.326   1.988  -8.807  0.33 15.01           O  
ANISOU  881  O  CTHR A1091     2086   2056   1561    189   -196   -169       O  
ATOM    882  CB ATHR A1091      -8.218   4.290  -7.313  0.33 13.82           C  
ANISOU  882  CB ATHR A1091     1965   1846   1438     86    -62    -23       C  
ATOM    883  CB BTHR A1091      -8.117   4.269  -7.226  0.33 16.12           C  
ANISOU  883  CB BTHR A1091     2237   2080   1807     36   -119    -29       C  
ATOM    884  CB CTHR A1091      -7.724   4.535  -7.353  0.33 13.66           C  
ANISOU  884  CB CTHR A1091     2050   1757   1383   -123    -22     15       C  
ATOM    885  CG2ATHR A1091      -8.116   4.633  -5.832  0.33 11.34           C  
ANISOU  885  CG2ATHR A1091     1800   1730    776    -13     65    -62       C  
ATOM    886  CG2BTHR A1091      -7.913   5.249  -8.352  0.33 14.98           C  
ANISOU  886  CG2BTHR A1091     1830   2101   1757     61   -162    -66       C  
ATOM    887  CG2CTHR A1091      -9.181   4.862  -7.355  0.33 12.08           C  
ANISOU  887  CG2CTHR A1091     1748   1606   1234   -307    139    126       C  
ATOM    888  OG1ATHR A1091      -7.548   5.284  -8.093  0.33 13.66           O  
ANISOU  888  OG1ATHR A1091     1739   2035   1412    225    165    -20       O  
ATOM    889  OG1BTHR A1091      -9.510   4.176  -6.927  0.33 20.23           O  
ANISOU  889  OG1BTHR A1091     2699   2548   2439    105   -324    -84       O  
ATOM    890  OG1CTHR A1091      -7.124   4.885  -6.088  0.33 10.22           O  
ANISOU  890  OG1CTHR A1091     1570   1569    741   -362   -122   -135       O  
ATOM    891  N   GLN A1092      -7.613   2.778 -10.038  1.00 15.15           N  
ANISOU  891  N   GLN A1092     2034   2242   1479    215   -194   -154       N  
ATOM    892  CA  GLN A1092      -8.163   2.391 -11.336  1.00 15.30           C  
ANISOU  892  CA  GLN A1092     1941   2223   1646     96   -195   -115       C  
ATOM    893  C   GLN A1092      -8.206   0.879 -11.488  1.00 16.33           C  
ANISOU  893  C   GLN A1092     2097   2343   1765    195   -269    -55       C  
ATOM    894  O   GLN A1092      -9.155   0.368 -12.067  1.00 18.02           O  
ANISOU  894  O   GLN A1092     2347   2498   1998    145   -380   -157       O  
ATOM    895  CB  GLN A1092      -7.362   3.003 -12.479  1.00 14.90           C  
ANISOU  895  CB  GLN A1092     1566   2585   1508     51   -163   -242       C  
ATOM    896  CG  GLN A1092      -7.510   4.508 -12.618  1.00 13.28           C  
ANISOU  896  CG  GLN A1092     1391   2397   1255    108   -130   -224       C  
ATOM    897  CD  GLN A1092      -8.943   4.964 -12.819  1.00 12.90           C  
ANISOU  897  CD  GLN A1092     1679   2437    782    311    122   -427       C  
ATOM    898  NE2 GLN A1092      -9.580   4.425 -13.829  1.00 10.55           N  
ANISOU  898  NE2 GLN A1092     1166   2105    736    269     82   -372       N  
ATOM    899  OE1 GLN A1092      -9.480   5.795 -12.041  1.00 17.70           O  
ANISOU  899  OE1 GLN A1092     2030   3135   1557    611     -1   -916       O  
ATOM    900  N   ILE A1093      -7.196   0.155 -10.980  1.00 17.32           N  
ANISOU  900  N   ILE A1093     2292   2453   1833    302   -425   -137       N  
ATOM    901  CA  ILE A1093      -7.227  -1.330 -11.046  1.00 18.15           C  
ANISOU  901  CA  ILE A1093     2195   2524   2174    137   -419   -161       C  
ATOM    902  C   ILE A1093      -7.996  -2.002  -9.915  1.00 18.94           C  
ANISOU  902  C   ILE A1093     2213   2456   2525    211   -594    -67       C  
ATOM    903  O   ILE A1093      -8.085  -3.235  -9.852  1.00 21.58           O  
ANISOU  903  O   ILE A1093     2533   2620   3043     -2   -793   -323       O  
ATOM    904  CB  ILE A1093      -5.825  -1.985 -11.101  1.00 19.25           C  
ANISOU  904  CB  ILE A1093     2407   2592   2315    252   -256   -148       C  
ATOM    905  CG1 ILE A1093      -5.022  -1.685  -9.843  1.00 17.66           C  
ANISOU  905  CG1 ILE A1093     2349   2525   1836    128   -407     46       C  
ATOM    906  CG2 ILE A1093      -5.086  -1.576 -12.326  1.00 19.46           C  
ANISOU  906  CG2 ILE A1093     2259   2928   2205    271   -290    313       C  
ATOM    907  CD1 ILE A1093      -3.682  -2.353  -9.808  1.00 19.72           C  
ANISOU  907  CD1 ILE A1093     2618   2651   2221     76   -104   -209       C  
ATOM    908  N   GLY A1094      -8.549  -1.214  -9.006  1.00 17.90           N  
ANISOU  908  N   GLY A1094     2316   2331   2151     59   -486   -237       N  
ATOM    909  CA  GLY A1094      -9.354  -1.774  -7.928  1.00 18.72           C  
ANISOU  909  CA  GLY A1094     2291   2386   2433    -19   -444     43       C  
ATOM    910  C   GLY A1094      -8.520  -2.406  -6.829  1.00 19.04           C  
ANISOU  910  C   GLY A1094     2402   2372   2457    -28   -434     95       C  
ATOM    911  O   GLY A1094      -8.977  -3.319  -6.136  1.00 20.90           O  
ANISOU  911  O   GLY A1094     2450   2744   2745   -304   -844    357       O  
ATOM    912  N   CYS A1095      -7.310  -1.894  -6.648  1.00 17.57           N  
ANISOU  912  N   CYS A1095     2284   2143   2250     14   -511    238       N  
ATOM    913  CA  CYS A1095      -6.424  -2.381  -5.600  1.00 17.20           C  
ANISOU  913  CA  CYS A1095     2243   2126   2164    106   -353     51       C  
ATOM    914  C   CYS A1095      -6.829  -1.790  -4.252  1.00 18.32           C  
ANISOU  914  C   CYS A1095     2475   2209   2275     79   -376    121       C  
ATOM    915  O   CYS A1095      -6.988  -0.571  -4.120  1.00 19.93           O  
ANISOU  915  O   CYS A1095     3120   2174   2277    248   -714    155       O  
ATOM    916  CB  CYS A1095      -4.989  -2.000  -5.939  1.00 18.04           C  
ANISOU  916  CB  CYS A1095     2270   2325   2260    120   -542     98       C  
ATOM    917  SG  CYS A1095      -3.779  -2.607  -4.760  1.00 18.68           S  
ANISOU  917  SG  CYS A1095     2375   2447   2274   -152   -699    435       S  
ATOM    918  N   THR A1096      -7.002  -2.664  -3.260  1.00 16.88           N  
ANISOU  918  N   THR A1096     2321   2203   1889     11   -304    116       N  
ATOM    919  CA  THR A1096      -7.359  -2.249  -1.921  1.00 17.22           C  
ANISOU  919  CA  THR A1096     2187   2175   2179    123   -279      0       C  
ATOM    920  C   THR A1096      -6.344  -2.805  -0.938  1.00 16.69           C  
ANISOU  920  C   THR A1096     2072   2243   2026    116   -207     75       C  
ATOM    921  O   THR A1096      -5.633  -3.772  -1.229  1.00 16.87           O  
ANISOU  921  O   THR A1096     2177   2146   2085     -4   -351     14       O  
ATOM    922  CB  THR A1096      -8.768  -2.749  -1.514  1.00 18.82           C  
ANISOU  922  CB  THR A1096     2498   2426   2224     67   -294    -40       C  
ATOM    923  CG2 THR A1096      -9.840  -2.069  -2.356  1.00 19.75           C  
ANISOU  923  CG2 THR A1096     2441   2674   2389    224   -448   -142       C  
ATOM    924  OG1 THR A1096      -8.861  -4.166  -1.693  1.00 19.18           O  
ANISOU  924  OG1 THR A1096     2162   2517   2609     66   -134    -88       O  
ATOM    925  N   LEU A1097      -6.279  -2.171   0.225  1.00 15.86           N  
ANISOU  925  N   LEU A1097     1954   2068   2003    180   -231    -27       N  
ATOM    926  CA  LEU A1097      -5.613  -2.759   1.379  1.00 15.51           C  
ANISOU  926  CA  LEU A1097     2004   2024   1863    143   -134     52       C  
ATOM    927  C   LEU A1097      -6.624  -3.542   2.207  1.00 15.64           C  
ANISOU  927  C   LEU A1097     1828   2064   2050    119   -135     61       C  
ATOM    928  O   LEU A1097      -7.742  -3.074   2.428  1.00 17.58           O  
ANISOU  928  O   LEU A1097     1832   2432   2413    242     24    223       O  
ATOM    929  CB  LEU A1097      -5.012  -1.662   2.248  1.00 15.32           C  
ANISOU  929  CB  LEU A1097     2043   1937   1838    204   -222    -43       C  
ATOM    930  CG  LEU A1097      -3.828  -0.906   1.655  1.00 15.84           C  
ANISOU  930  CG  LEU A1097     2078   2107   1832    104   -265     76       C  
ATOM    931  CD1 LEU A1097      -3.637   0.434   2.356  1.00 17.38           C  
ANISOU  931  CD1 LEU A1097     2327   2238   2037   -197    -42    195       C  
ATOM    932  CD2 LEU A1097      -2.555  -1.744   1.719  1.00 17.07           C  
ANISOU  932  CD2 LEU A1097     2147   2404   1932     16    -87    204       C  
ATOM    933  N   ASN A1098      -6.215  -4.713   2.686  1.00 16.05           N  
ANISOU  933  N   ASN A1098     1785   2191   2122     48    -76    114       N  
ATOM    934  CA  ASN A1098      -7.119  -5.596   3.407  1.00 16.53           C  
ANISOU  934  CA  ASN A1098     1980   2198   2100    128    -35     90       C  
ATOM    935  C   ASN A1098      -6.421  -6.230   4.585  1.00 17.53           C  
ANISOU  935  C   ASN A1098     2078   2414   2166     44    -60    193       C  
ATOM    936  O   ASN A1098      -5.308  -6.745   4.462  1.00 17.14           O  
ANISOU  936  O   ASN A1098     1854   2382   2276   -128    -37    221       O  
ATOM    937  CB  ASN A1098      -7.633  -6.704   2.498  1.00 18.36           C  
ANISOU  937  CB  ASN A1098     2097   2526   2350   -117     11    133       C  
ATOM    938  CG  ASN A1098      -8.450  -6.178   1.363  1.00 18.91           C  
ANISOU  938  CG  ASN A1098     1888   2634   2663   -114   -192     26       C  
ATOM    939  ND2 ASN A1098      -7.777  -5.759   0.306  1.00 19.37           N  
ANISOU  939  ND2 ASN A1098     2282   2400   2678   -357   -430    249       N  
ATOM    940  OD1 ASN A1098      -9.682  -6.133   1.435  1.00 25.39           O  
ANISOU  940  OD1 ASN A1098     2360   3956   3330   -163   -139    272       O  
ATOM    941  N   PHE A1099      -7.093  -6.215   5.723  1.00 19.17           N  
ANISOU  941  N   PHE A1099     2150   2741   2392     56     29    199       N  
ATOM    942  CA  PHE A1099      -6.632  -6.993   6.858  1.00 18.99           C  
ANISOU  942  CA  PHE A1099     2296   2513   2404     33     88    240       C  
ATOM    943  C   PHE A1099      -7.774  -7.277   7.811  1.00 20.91           C  
ANISOU  943  C   PHE A1099     2402   2881   2660      0     96    152       C  
ATOM    944  O   PHE A1099      -8.876  -6.779   7.604  1.00 22.34           O  
ANISOU  944  O   PHE A1099     2409   3208   2870    -25    319    365       O  
ATOM    945  CB  PHE A1099      -5.464  -6.313   7.582  1.00 20.46           C  
ANISOU  945  CB  PHE A1099     2519   2663   2588    -32     34    197       C  
ATOM    946  CG  PHE A1099      -5.734  -4.904   8.021  1.00 19.94           C  
ANISOU  946  CG  PHE A1099     2172   2904   2497    -95    159    292       C  
ATOM    947  CD1 PHE A1099      -6.044  -4.622   9.344  1.00 23.34           C  
ANISOU  947  CD1 PHE A1099     2557   2924   3386    -74     36     51       C  
ATOM    948  CD2 PHE A1099      -5.640  -3.856   7.123  1.00 21.72           C  
ANISOU  948  CD2 PHE A1099     2777   2794   2679      7   -248    202       C  
ATOM    949  CE1 PHE A1099      -6.275  -3.324   9.757  1.00 23.87           C  
ANISOU  949  CE1 PHE A1099     2869   3040   3157   -120    300     77       C  
ATOM    950  CE2 PHE A1099      -5.862  -2.562   7.529  1.00 23.66           C  
ANISOU  950  CE2 PHE A1099     2968   2894   3128    -12   -124    355       C  
ATOM    951  CZ  PHE A1099      -6.190  -2.289   8.845  1.00 24.81           C  
ANISOU  951  CZ  PHE A1099     3166   3069   3190    133     17    135       C  
ATOM    952  OXT PHE A1099      -7.589  -8.044   8.756  1.00 22.48           O1-
TER   
HETATM  953  O   HOH B   1       5.385   5.851   0.099  0.50 18.43      F000 O  
ANISOU  953  O   HOH B   1     2309   3264   1429   -227    183    401  F000 O  
HETATM  954  O   HOH B   2       8.960  -5.279  13.040  1.00  7.16      F000 O  
ANISOU  954  O   HOH B   2      525   1875    320    308    -23     -5  F000 O  
HETATM  955  O   HOH B   3     -10.829   5.894  -0.408  1.00 21.65      F000 O  
ANISOU  955  O   HOH B   3     2010   4919   1294   1692    130    181  F000 O  
HETATM  956  O   HOH B   4      10.111   0.376  11.893  1.00 13.19      F000 O  
ANISOU  956  O   HOH B   4     1921   1916   1171   -190   -379    451  F000 O  
HETATM  957  O   HOH B   5       2.762  -8.967  15.966  1.00 11.86      F000 O  
ANISOU  957  O   HOH B   5     1474   2058    973     21     30   -260  F000 O  
HETATM  958  O   HOH B   6      -7.484   5.346   1.671  1.00 18.99      F000 O  
ANISOU  958  O   HOH B   6     2591   2699   1925    228    -11    559  F000 O  
HETATM  959  O   HOH B   7      11.776   2.083  29.492  1.00 18.30      F000 O  
ANISOU  959  O   HOH B   7     3202   2665   1086    129   -203   -179  F000 O  
HETATM  960  O   HOH B   8      10.780  -5.427  16.988  1.00 14.74      F000 O  
ANISOU  960  O   HOH B   8     1509   2813   1275   -134    145     97  F000 O  
HETATM  961  O   HOH B   9      12.800   4.161  26.603  1.00 16.83      F000 O  
ANISOU  961  O   HOH B   9     2006   2944   1441    -13    176    199  F000 O  
HETATM  962  O   HOH B  10      -8.806   1.500  -4.341  1.00 17.05      F000 O  
ANISOU  962  O   HOH B  10     2146   2447   1884    213     17    586  F000 O  
HETATM  963  O   HOH B  11      21.963  11.530  -2.160  1.00 18.47      F000 O  
ANISOU  963  O   HOH B  11     3221   2361   1435   -662   -497     27  F000 O  
HETATM  964  O   HOH B  12       7.644  -7.674  14.738  1.00 17.51      F000 O  
ANISOU  964  O   HOH B  12     2257   2592   1802    -62    -81    121  F000 O  
HETATM  965  O   HOH B  13       4.660  -1.562  23.820  1.00 18.43      F000 O  
ANISOU  965  O   HOH B  13     2496   3156   1347    180    366    -51  F000 O  
HETATM  966  O   HOH B  14       8.110  -1.167   0.046  1.00 17.30      F000 O  
ANISOU  966  O   HOH B  14     2856   2319   1397    623   -527    -86  F000 O  
HETATM  967  O   HOH B  15      11.536   2.639   2.698  1.00 25.01      F000 O  
ANISOU  967  O   HOH B  15     4087   2644   2771   -553   -865   -261  F000 O  
HETATM  968  O   HOH B  16      10.279   0.653  -0.052  1.00 21.03      F000 O  
ANISOU  968  O   HOH B  16     3528   2455   2006    192    -63   -252  F000 O  
HETATM  969  O   HOH B  17      14.041  -1.640  21.927  1.00 16.89      F000 O  
ANISOU  969  O   HOH B  17     2272   2806   1336    281    -74    508  F000 O  
HETATM  970  O   HOH B  19       7.139  -7.853  10.079  1.00 22.59      F000 O  
ANISOU  970  O   HOH B  19     3635   2656   2293   1287  -1556  -1119  F000 O  
HETATM  971  O   HOH B  20       2.400   0.912  22.843  1.00 18.31      F000 O  
ANISOU  971  O   HOH B  20     2170   3271   1513    -42    151     93  F000 O  
HETATM  972  O   HOH B  21       1.127 -10.626   6.347  1.00 20.60      F000 O  
ANISOU  972  O   HOH B  21     2320   3100   2406    590   -349   -665  F000 O  
HETATM  973  O   HOH B  22      22.087   3.256  10.996  1.00 29.23      F000 O  
ANISOU  973  O   HOH B  22     3153   5558   2395   2214   -941  -1192  F000 O  
HETATM  974  O   HOH B  23       4.816   1.155  24.071  1.00 19.30      F000 O  
ANISOU  974  O   HOH B  23     2481   2897   1953    -82   -220    -96  F000 O  
HETATM  975  O   HOH B  24       0.683 -10.243  14.566  1.00 24.74      F000 O  
ANISOU  975  O   HOH B  24     3858   3453   2089   -998   -875    640  F000 O  
HETATM  976  O   HOH B  25      15.313   8.556   1.164  1.00 46.30      F000 O  
ANISOU  976  O   HOH B  25    11995   2870   2724    990  -2422  -2439  F000 O  
HETATM  977  O   HOH B  26       9.845   9.666   7.034  1.00 26.62      F000 O  
ANISOU  977  O   HOH B  26     3088   4292   2733     42    226   -858  F000 O  
HETATM  978  O   HOH B  27       9.013  14.596  15.557  1.00 29.28      F000 O  
ANISOU  978  O   HOH B  27     2477   5842   2806    -22   -635    -65  F000 O  
HETATM  979  O   HOH B  28       2.228  -2.761  25.166  0.50 22.91      F000 O  
ANISOU  979  O   HOH B  28     4054   2902   1748   -854   -817    594  F000 O  
HETATM  980  O   HOH B  29      -9.017   4.026  11.631  1.00 29.39      F000 O  
ANISOU  980  O   HOH B  29     4798   2536   3831    332    853    -48  F000 O  
HETATM  981  O   HOH B  30      -1.591   2.375  24.050  1.00 23.41      F000 O  
ANISOU  981  O   HOH B  30     3259   3719   1916   -418   -274     94  F000 O  
HETATM  982  O   HOH B  31      -7.503  10.396   4.013  1.00 31.16      F000 O  
ANISOU  982  O   HOH B  31     3942   4892   3005   2442   1155   1469  F000 O  
HETATM  983  O   HOH B  32       4.744  10.541  24.270  1.00 34.12      F000 O  
ANISOU  983  O   HOH B  32     7099   3039   2824   1698   1108     73  F000 O  
HETATM  984  O   HOH B  33       3.989   2.848  26.389  1.00 15.42      F000 O  
ANISOU  984  O   HOH B  33     2140   2374   1343    139    320    155  F000 O  
HETATM  985  O   HOH B  34     -13.622   1.779  -5.941  1.00 10.06      F000 O  
ANISOU  985  O   HOH B  34     1788   1112    922    551    343    -24  F000 O  
HETATM  986  O   HOH B  35       8.185   5.607  27.806  1.00 17.98      F000 O  
ANISOU  986  O   HOH B  35     2492   3129   1210    708   -365   -386  F000 O  
HETATM  987  O   HOH B  36      16.712  -0.940  18.954  1.00 20.00      F000 O  
ANISOU  987  O   HOH B  36     2572   2590   2434    532   -357    261  F000 O  
HETATM  988  O   HOH B  37      13.425   6.453  25.359  1.00 21.88      F000 O  
ANISOU  988  O   HOH B  37     2602   4117   1593   -550    209   -135  F000 O  
HETATM  989  O   HOH B  38       3.009  -6.736  26.148  1.00 23.29      F000 O  
ANISOU  989  O   HOH B  38     2924   3603   2321     -7    747    271  F000 O  
HETATM  990  O   HOH B  39      13.398  15.303   8.908  1.00 25.52      F000 O  
ANISOU  990  O   HOH B  39     2065   4305   3325    670    470   1722  F000 O  
HETATM  991  O   HOH B  40      -9.050   5.823   3.815  1.00 29.09      F000 O  
ANISOU  991  O   HOH B  40     4429   3438   3186    160    699   -360  F000 O  
HETATM  992  O   HOH B  41       8.080  -6.009   6.136  1.00 24.56      F000 O  
ANISOU  992  O   HOH B  41     3745   3512   2074   -207    302   -495  F000 O  
HETATM  993  O   HOH B  42      10.119  -4.131   6.213  1.00 23.91      F000 O  
ANISOU  993  O   HOH B  42     2671   3428   2983    439   -419   -701  F000 O  
HETATM  994  O   HOH B  43      -6.448  12.226   0.573  1.00 31.10      F000 O  
ANISOU  994  O   HOH B  43     2189   4600   5027   1130    252    701  F000 O  
HETATM  995  O   HOH B  44      11.801  -1.630  10.919  1.00 30.62      F000 O  
ANISOU  995  O   HOH B  44     4213   4853   2568   1905   -835  -1602  F000 O  
HETATM  996  O   HOH B  45      -1.367  12.199  14.923  1.00 33.72      F000 O  
ANISOU  996  O   HOH B  45     3244   5905   3661   -477    194    187  F000 O  
HETATM  997  O   HOH B  46      -5.531  -9.729   8.989  1.00 29.70      F000 O  
ANISOU  997  O   HOH B  46     3126   3286   4870   -372  -1377    711  F000 O  
HETATM  998  O   HOH B  47      12.905   7.105   4.941  1.00 27.00      F000 O  
ANISOU  998  O   HOH B  47     4042   3241   2973   -714    913    102  F000 O  
HETATM  999  O   HOH B  48       9.480   3.886  29.812  1.00 22.13      F000 O  
ANISOU  999  O   HOH B  48     2313   3930   2164    350   -197    336  F000 O  
HETATM 1000  O   HOH B  49       5.261  14.639  18.477  1.00 28.45      F000 O  
ANISOU 1000  O   HOH B  49     2926   4645   3237   1158      2   -386  F000 O  
HETATM 1001  O   HOH B  50       8.603   5.706  -0.471  0.50 20.75      F000 O  
ANISOU 1001  O   HOH B  50     4318   1376   2190    -64   -456   -768  F000 O  
HETATM 1002  O   HOH B  51       3.759  12.391  20.921  1.00 30.05      F000 O  
ANISOU 1002  O   HOH B  51     2184   4073   5160    222    640   -743  F000 O  
HETATM 1003  O   HOH B  52      21.403   1.267  22.572  1.00 31.37      F000 O  
ANISOU 1003  O   HOH B  52     5765   2766   3385    833  -1066     52  F000 O  
HETATM 1004  O   HOH B  53      18.339   3.146  25.459  1.00 33.20      F000 O  
ANISOU 1004  O   HOH B  53     4350   5190   3073  -1221    212   1964  F000 O  
HETATM 1005  O   HOH B  54     -11.875   2.845   2.292  1.00 31.18      F000 O  
ANISOU 1005  O   HOH B  54     4034   3543   4268   1761    393   -144  F000 O  
HETATM 1006  O   HOH B  55      10.078   7.040   5.886  1.00 33.41      F000 O  
ANISOU 1006  O   HOH B  55     2825   7812   2058   -461   -286  -1453  F000 O  
HETATM 1007  O   HOH B  57      -9.717  -5.094  -4.109  1.00 22.68      F000 O  
ANISOU 1007  O   HOH B  57     3341   2858   2416   -192    401    223  F000 O  
HETATM 1008  O   HOH B  58       9.185  12.301  23.495  1.00 27.98      F000 O  
ANISOU 1008  O   HOH B  58     3507   4514   2610    687    704     95  F000 O  
HETATM 1009  O   HOH B  59     -11.163  -7.315   3.433  1.00 31.44      F000 O  
ANISOU 1009  O   HOH B  59     4631   2837   4475    152   -484    436  F000 O  
HETATM 1010  O   HOH B  60      -3.476  -8.593  14.587  1.00 32.12      F000 O  
ANISOU 1010  O   HOH B  60     4119   4233   3851   -606   1183    810  F000 O  
HETATM 1011  O   HOH B  61       1.186   7.454  27.745  1.00 26.87      F000 O  
ANISOU 1011  O   HOH B  61     3585   4283   2340   -387    348    294  F000 O  
HETATM 1012  O   HOH B  62       7.972   8.862   0.219  0.50 28.84      F000 O  
ANISOU 1012  O   HOH B  62     2054   5273   3629    -46  -1031   1790  F000 O  
HETATM 1013  O   HOH B  63      -4.629  -8.563  12.325  1.00 31.42      F000 O  
ANISOU 1013  O   HOH B  63     3862   4573   3502  -1059   1070  -1024  F000 O  
HETATM 1014  O   HOH B  64      -3.495   4.355  23.190  1.00 29.10      F000 O  
ANISOU 1014  O   HOH B  64     4483   4201   2370   -448    321    216  F000 O  
HETATM 1015  O   HOH B  65      -5.802  -7.739  17.394  1.00 35.25      F000 O  
ANISOU 1015  O   HOH B  65     4993   2393   6006  -1321  -1321    794  F000 O  
HETATM 1016  O   HOH B  66      21.178  -1.289  21.628  1.00 52.89      F000 O  
ANISOU 1016  O   HOH B  66     6665   9264   4164   3818    328    863  F000 O  
HETATM 1017  O   HOH B  67      10.671   4.946   1.726  1.00 36.01      F000 O  
ANISOU 1017  O   HOH B  67     6497   3495   3688   -892   -404   -244  F000 O  
HETATM 1018  O   HOH B  68      10.967  -9.448  18.193  1.00 39.81      F000 O  
ANISOU 1018  O   HOH B  68     2629   4905   7590   -126   -953   2939  F000 O  
HETATM 1019  O   HOH B  69      14.595  -1.142  11.855  1.00 27.63      F000 O  
ANISOU 1019  O   HOH B  69     4635   3325   2538   -102   -126   -254  F000 O  
HETATM 1020  O   HOH B  70      -3.619  10.749  22.635  1.00 40.82      F000 O  
ANISOU 1020  O   HOH B  70     2270   9010   4227    754   1738    538  F000 O  
HETATM 1021  O   HOH B  71      23.721   6.739  14.041  1.00 38.64      F000 O  
ANISOU 1021  O   HOH B  71     6756   4574   3349    -48  -1212   -286  F000 O  
HETATM 1022  O   HOH B  74      11.551   3.035   5.557  1.00 30.39      F000 O  
ANISOU 1022  O   HOH B  74     3296   5546   2701    325   -438  -1190  F000 O  
HETATM 1023  O   HOH B  75       9.949   4.462   6.586  1.00 31.11      F000 O  
ANISOU 1023  O   HOH B  75     4484   3513   3822   -952  -1708   -393  F000 O  
HETATM 1024  O   HOH B  76      18.544  -1.441  20.954  1.00 33.31      F000 O  
ANISOU 1024  O   HOH B  76     5512   3416   3728   -649  -1661    740  F000 O  
HETATM 1025  O   HOH B  77      11.539  -4.422  11.292  1.00 32.12      F000 O  
ANISOU 1025  O   HOH B  77     6253   3611   2341   1243   -461    414  F000 O  
HETATM 1026  O   HOH B  78       9.140  -7.558   8.298  1.00 32.27      F000 O  
ANISOU 1026  O   HOH B  78     3299   4792   4167    109   -247  -2593  F000 O  
HETATM 1027  O   HOH B  79      11.987  10.774   7.826  1.00 33.35      F000 O  
ANISOU 1027  O   HOH B  79     3856   5199   3617    -69   -732   -195  F000 O  
HETATM 1028  O   HOH B  80      -1.560  -0.098  21.993  1.00 37.44      F000 O  
ANISOU 1028  O   HOH B  80     7511   4193   2521   -481   -339   -308  F000 O  
HETATM 1029  O   HOH B  81      -2.394 -11.247  11.273  1.00 33.95      F000 O  
ANISOU 1029  O   HOH B  81     3695   4533   4670    540   -767  -1880  F000 O  
HETATM 1030  O   HOH B  82      23.047   2.426  16.328  1.00 34.85      F000 O  
ANISOU 1030  O   HOH B  82     5941   4012   3288   1587   -870   -390  F000 O  
HETATM 1031  O   HOH B  84       4.065   7.185  25.936  1.00 31.03      F000 O  
ANISOU 1031  O   HOH B  84     3875   3532   4380    465    117    353  F000 O  
HETATM 1032  O   HOH B  85       7.202   6.524   2.053  1.00 28.62      F000 O  
ANISOU 1032  O   HOH B  85     4944   4301   1628  -1001   -760    801  F000 O  
HETATM 1033  O   HOH B  86      16.284   3.670   5.099  1.00 35.92      F000 O  
ANISOU 1033  O   HOH B  86     2520   7465   3662   -796    707   -660  F000 O  
HETATM 1034  O   HOH B  88      23.881   9.622  17.491  1.00 27.84      F000 O  
ANISOU 1034  O   HOH B  88     4907   2913   2758    -47   -918   -674  F000 O  
HETATM 1035  O   HOH B  89      -6.159  11.871  -3.234  1.00 37.44      F000 O  
ANISOU 1035  O   HOH B  89     4878   3199   6145   1329  -2316   -251  F000 O  
HETATM 1036  O   HOH B  90      14.022   9.420   5.833  1.00 36.82      F000 O  
ANISOU 1036  O   HOH B  90     3176   5878   4935  -1436   1063  -1202  F000 O  
HETATM 1037  O   HOH B  91      14.324   4.895   4.736  1.00 69.62      F000 O  
ANISOU 1037  O   HOH B  91     8446  12260   5743  -2225   -241  -1681  F000 O  
HETATM 1038  O   HOH B  92      11.020  -5.398   8.746  1.00 30.22      F000 O  
ANISOU 1038  O   HOH B  92     3480   4969   3032   1235   -478   -831  F000 O  
HETATM 1039  O   HOH B  93      13.932  -2.196   7.231  1.00 41.79      F000 O  
ANISOU 1039  O   HOH B  93     5641   6008   4227   2522    299   -920  F000 O  
HETATM 1040  O   HOH B  94     -14.002  -0.372   0.960  1.00 42.56      F000 O  
ANISOU 1040  O   HOH B  94     6816   3554   5800   1445  -2283    767  F000 O  
HETATM 1041  O   HOH B  95       6.794  13.687  23.398  1.00 43.40      F000 O  
ANISOU 1041  O   HOH B  95     6730   4889   4871   1610   1191   1844  F000 O  
HETATM 1042  O   HOH B  96      -4.240  -9.774  18.315  1.00 41.03      F000 O  
ANISOU 1042  O   HOH B  96     7172   5389   3027  -1263    874    529  F000 O  
HETATM 1043  O   HOH B  97      12.386   5.606  28.932  1.00 44.63      F000 O  
ANISOU 1043  O   HOH B  97     5229   9344   2383   1808    876    560  F000 O  
HETATM 1044  O   HOH B  98     -14.104   2.518   0.459  1.00 35.39      F000 O  
ANISOU 1044  O   HOH B  98     4915   4782   3749   1892   -757   -205  F000 O  
HETATM 1045  O   HOH B  99     -14.071  -2.523   5.397  1.00 62.55      F000 O  
ANISOU 1045  O   HOH B  99    14341   3105   6317   4648    378   1918  F000 O  
HETATM 1046  O   HOH B 100      -1.467 -13.931  17.627  1.00 37.65      F000 O  
ANISOU 1046  O   HOH B 100     6991   3871   3443   -430   1230   -412  F000 O  
HETATM 1047  O   HOH B 105       8.018  14.954  12.998  1.00 40.92      F000 O  
ANISOU 1047  O   HOH B 105     4024   8550   2973   2491    141   1484  F000 O  
HETATM 1048  O   HOH B 124       1.263   3.660  28.149  1.00 29.98      F000 O  
ANISOU 1048  O   HOH B 124     3807   4784   2797     44   -996    835  F000 O  
HETATM 1049  O   HOH B 127       5.945  18.603   8.250  1.00 38.76      F000 O  
ANISOU 1049  O   HOH B 127     4083   5345   5298  -1121   1766  -1292  F000 O  
HETATM 1050  O   HOH B 128      -3.071 -14.075  20.031  1.00 35.24      F000 O  
ANISOU 1050  O   HOH B 128     5140   5184   3065  -1221   1337   -491  F000 O  
HETATM 1051  O   HOH B 129      -0.865 -17.299  18.151  1.00 80.62      F000 O  
ANISOU 1051  O   HOH B 129    15117  12894   2621  -7307   2049  -1509  F000 O  
HETATM 1052  O   HOH B 131      20.292   4.817  24.483  1.00 48.62      F000 O  
ANISOU 1052  O   HOH B 131     5275   6916   6279   -669    551  -3156  F000 O  
HETATM 1053  O   HOH B 132      22.904   7.609  21.401  1.00 36.70      F000 O  
ANISOU 1053  O   HOH B 132     5319   4534   4091   1054    -17    974  F000 O  
HETATM 1054  O   HOH B 133       1.627  11.499   2.499  1.00 37.30      F000 O  
ANISOU 1054  O   HOH B 133     4728   6938   2504  -1634    741   -353  F000 O  
HETATM 1055  O   HOH B 134      10.176  -8.417   5.816  1.00 31.11      F000 O  
ANISOU 1055  O   HOH B 134     3197   5356   3265    543    162   -407  F000 O  
HETATM 1056  O   HOH B 135      11.875  -7.481   9.747  1.00 44.05      F000 O  
ANISOU 1056  O   HOH B 135     4775   7735   4227  -2833   1074   -135  F000 O  
HETATM 1057  O   HOH B 136      -6.599   1.475  16.377  1.00 38.92      F000 O  
HETATM 1058  O   HOH B 148      16.017   7.921  26.420  1.00 42.21      F000 O  
HETATM 1059  O   HOH B 153      15.205  -0.013   4.702  1.00 33.51      F000 O  
HETATM 1060  O   HOH B 157      -1.793 -11.050  14.417  1.00 35.90      F000 O  
HETATM 1061  O   HOH B 163      17.971  -3.742  22.269  1.00 34.46      F000 O  
HETATM 1062  O   HOH B 169      15.314   9.808  24.498  1.00 41.50      F000 O  
HETATM 1063  O   HOH B 173      11.372   7.602  24.904  1.00 35.85      F000 O  
HETATM 1064  O   HOH B 174       9.490   6.014   3.661  1.00 37.61      F000 O  
HETATM 1065 MG    MG B 201       6.653   7.441   0.187  0.50 20.67      F000MG  
ANISOU 1065 MG    MG B 201     3139   3127   1585   -318    -43    517  F000MG  
HETATM 1066  C1  PGR B 907      -0.600 -10.005  17.874  1.00 21.25      F000 C  
ANISOU 1066  C1  PGR B 907     2832   3318   1922   -227   -375    -12  F000 C  
HETATM 1067  O1  PGR B 907      -1.433 -11.155  17.853  1.00 27.89      F000 O  
ANISOU 1067  O1  PGR B 907     3955   4007   2634   -313     15    265  F000 O  
HETATM 1068  C2  PGR B 907      -0.478  -9.514  19.305  1.00 22.18      F000 C  
ANISOU 1068  C2  PGR B 907     2881   3233   2311      6   -124    240  F000 C  
HETATM 1069  O2  PGR B 907       0.287  -8.319  19.376  1.00 28.42      F000 O  
ANISOU 1069  O2  PGR B 907     3884   3943   2972   -497   -578    -38  F000 O  
HETATM 1070  C3  PGR B 907       0.184 -10.553  20.178  1.00 12.13      F000 C  
ANISOU 1070  C3  PGR B 907     1415   2288    905    330    -77    -84  F000 C  
ATOM   1071  N   PRO B1001     -10.469  -4.475   7.839  1.00 23.99      F000 N  
ANISOU 1071  N   PRO B1001     3081   2999   3032     54    -47    -99  F000 N  
ATOM   1072  CA  PRO B1001     -11.208  -3.664   6.887  1.00 23.50      F000 C  
ANISOU 1072  CA  PRO B1001     3061   2870   2998     26    -18    -31  F000 C  
ATOM   1073  C   PRO B1001     -10.705  -3.849   5.464  1.00 22.61      F000 C  
ANISOU 1073  C   PRO B1001     2950   2728   2914     78    -26    -46  F000 C  
ATOM   1074  O   PRO B1001      -9.619  -4.385   5.251  1.00 22.30      F000 O  
ANISOU 1074  O   PRO B1001     3088   2426   2958     99   -175   -158  F000 O  
ATOM   1075  CB  PRO B1001     -10.923  -2.240   7.356  1.00 23.71      F000 C  
ANISOU 1075  CB  PRO B1001     3058   2980   2968     89    -65     44  F000 C  
ATOM   1076  CG  PRO B1001      -9.576  -2.317   7.950  1.00 25.39      F000 C  
ANISOU 1076  CG  PRO B1001     3285   3173   3186    -14     64    -10  F000 C  
ATOM   1077  CD  PRO B1001      -9.494  -3.674   8.598  1.00 25.09      F000 C  
ANISOU 1077  CD  PRO B1001     3216   3229   3088     48    -50    -79  F000 C  
ATOM   1078  N   GLN B1002     -11.503  -3.406   4.505  1.00 22.47      F000 N  
ANISOU 1078  N   GLN B1002     2881   2669   2987     15     46     80  F000 N  
ATOM   1079  CA  GLN B1002     -11.034  -3.196   3.143  1.00 21.24      F000 C  
ANISOU 1079  CA  GLN B1002     2691   2524   2853     47     -2     71  F000 C  
ATOM   1080  C   GLN B1002     -10.981  -1.700   2.870  1.00 21.08      F000 C  
ANISOU 1080  C   GLN B1002     2600   2390   3018    192    -35     52  F000 C  
ATOM   1081  O   GLN B1002     -11.984  -0.997   3.034  1.00 23.44      F000 O  
ANISOU 1081  O   GLN B1002     2727   2349   3828    206   -292    -19  F000 O  
ATOM   1082  CB  GLN B1002     -11.965  -3.887   2.148  1.00 21.87      F000 C  
ANISOU 1082  CB  GLN B1002     2875   2443   2991     70    -17     29  F000 C  
ATOM   1083  CG  GLN B1002     -11.665  -3.564   0.701  1.00 23.53      F000 C  
ANISOU 1083  CG  GLN B1002     3074   2686   3179     84    140    225  F000 C  
ATOM   1084  CD  GLN B1002     -12.290  -4.561  -0.258  1.00 24.38      F000 C  
ANISOU 1084  CD  GLN B1002     3095   2886   3281     51    238    293  F000 C  
ATOM   1085  NE2 GLN B1002     -13.281  -4.111  -1.002  1.00 30.58      F000 N  
ANISOU 1085  NE2 GLN B1002     3857   3586   4174     64    218    769  F000 N  
ATOM   1086  OE1 GLN B1002     -11.882  -5.726  -0.326  1.00 29.75      F000 O  
ANISOU 1086  OE1 GLN B1002     3919   3514   3869     52    442    650  F000 O  
ATOM   1087  N   ILE B1003      -9.805  -1.219   2.474  1.00 18.01      F000 N  
ANISOU 1087  N   ILE B1003     2206   2208   2426    121   -199    115  F000 N  
ATOM   1088  CA  ILE B1003      -9.547   0.209   2.335  1.00 18.20      F000 C  
ANISOU 1088  CA  ILE B1003     2329   2217   2368     48     14    127  F000 C  
ATOM   1089  C   ILE B1003      -9.242   0.523   0.873  1.00 17.18      F000 C  
ANISOU 1089  C   ILE B1003     2140   2133   2253    110    -80    243  F000 C  
ATOM   1090  O   ILE B1003      -8.281   0.000   0.308  1.00 16.92      F000 O  
ANISOU 1090  O   ILE B1003     2142   2097   2189    107    -75    403  F000 O  
ATOM   1091  CB  ILE B1003      -8.366   0.647   3.233  1.00 17.76      F000 C  
ANISOU 1091  CB  ILE B1003     2213   2237   2295    192    -40    151  F000 C  
ATOM   1092  CG1 ILE B1003      -8.709   0.376   4.703  1.00 19.95      F000 C  
ANISOU 1092  CG1 ILE B1003     2566   2418   2593     47   -135    259  F000 C  
ATOM   1093  CG2 ILE B1003      -8.031   2.124   3.013  1.00 19.19      F000 C  
ANISOU 1093  CG2 ILE B1003     2437   2465   2386     71    -66    174  F000 C  
ATOM   1094  CD1 ILE B1003      -7.565   0.575   5.646  1.00 18.33      F000 C  
ANISOU 1094  CD1 ILE B1003     2439   2294   2230    -16     -5     40  F000 C  
ATOM   1095  N   THR B1004     -10.083   1.351   0.253  1.00 16.35      F000 N  
ANISOU 1095  N   THR B1004     1918   1969   2324    167     -2    269  F000 N  
ATOM   1096  CA  THR B1004      -9.803   1.842  -1.086  1.00 16.56      F000 C  
ANISOU 1096  CA  THR B1004     2061   1972   2258    192     57    253  F000 C  
ATOM   1097  C   THR B1004      -8.832   3.015  -1.033  1.00 16.56      F000 C  
ANISOU 1097  C   THR B1004     2103   2030   2156    103     15    336  F000 C  
ATOM   1098  O   THR B1004      -8.519   3.541   0.041  1.00 17.70      F000 O  
ANISOU 1098  O   THR B1004     2096   2409   2219    162    213    194  F000 O  
ATOM   1099  CB  THR B1004     -11.087   2.301  -1.814  1.00 17.41      F000 C  
ANISOU 1099  CB  THR B1004     2220   2098   2295    195    141    322  F000 C  
ATOM   1100  CG2 THR B1004     -12.055   1.140  -1.967  1.00 17.70      F000 C  
ANISOU 1100  CG2 THR B1004     2169   1997   2558    179    -37    129  F000 C  
ATOM   1101  OG1 THR B1004     -11.702   3.365  -1.083  1.00 19.87      F000 O  
ANISOU 1101  OG1 THR B1004     2681   2191   2677    670    301    540  F000 O  
ATOM   1102  N   LEU B1005      -8.343   3.412  -2.199  1.00 15.13      F000 N  
ANISOU 1102  N   LEU B1005     1921   1866   1961    228     -8    360  F000 N  
ATOM   1103  CA  LEU B1005      -7.175   4.276  -2.271  1.00 15.28      F000 C  
ANISOU 1103  CA  LEU B1005     2017   1856   1931     75     47    280  F000 C  
ATOM   1104  C   LEU B1005      -7.446   5.595  -3.002  1.00 14.84      F000 C  
ANISOU 1104  C   LEU B1005     1966   1712   1959     21     11    256  F000 C  
ATOM   1105  O   LEU B1005      -6.529   6.266  -3.462  1.00 14.75      F000 O  
ANISOU 1105  O   LEU B1005     1957   1864   1781    156    170    389  F000 O  
ATOM   1106  CB  LEU B1005      -6.004   3.507  -2.880  1.00 15.26      F000 C  
ANISOU 1106  CB  LEU B1005     2105   1838   1854    235     34    453  F000 C  
ATOM   1107  CG  LEU B1005      -5.535   2.334  -2.009  1.00 15.05      F000 C  
ANISOU 1107  CG  LEU B1005     2022   1702   1991    248     37    356  F000 C  
ATOM   1108  CD1 LEU B1005      -4.579   1.426  -2.755  1.00 16.45      F000 C  
ANISOU 1108  CD1 LEU B1005     2246   1979   2023    440      8    323  F000 C  
ATOM   1109  CD2 LEU B1005      -4.886   2.861  -0.735  1.00 16.44      F000 C  
ANISOU 1109  CD2 LEU B1005     2005   2294   1944     81     42    382  F000 C  
ATOM   1110  N   TRP B1006      -8.719   5.977  -3.072  1.00 14.92      F000 N  
ANISOU 1110  N   TRP B1006     1874   1736   2057     88     56    320  F000 N  
ATOM   1111  CA  TRP B1006      -9.089   7.303  -3.572  1.00 14.34      F000 C  
ANISOU 1111  CA  TRP B1006     1834   1814   1799     79     42    301  F000 C  
ATOM   1112  C   TRP B1006      -8.497   8.423  -2.739  1.00 15.93      F000 C  
ANISOU 1112  C   TRP B1006     2028   2118   1906    -86    -67    267  F000 C  
ATOM   1113  O   TRP B1006      -8.133   9.474  -3.269  1.00 18.70      F000 O  
ANISOU 1113  O   TRP B1006     2168   2717   2220   -257    -78    813  F000 O  
ATOM   1114  CB  TRP B1006     -10.608   7.457  -3.610  1.00 13.63      F000 C  
ANISOU 1114  CB  TRP B1006     2013   1685   1480     -4     94    100  F000 C  
ATOM   1115  CG  TRP B1006     -11.270   6.480  -4.504  1.00 12.23      F000 C  
ANISOU 1115  CG  TRP B1006     2037   1310   1300     36     60    132  F000 C  
ATOM   1116  CD1 TRP B1006     -11.860   5.308  -4.141  1.00 11.36      F000 C  
ANISOU 1116  CD1 TRP B1006     1726   1445   1145    -74    -50    115  F000 C  
ATOM   1117  CD2 TRP B1006     -11.406   6.578  -5.927  1.00 11.60      F000 C  
ANISOU 1117  CD2 TRP B1006     2302    819   1284    -41    -68    -52  F000 C  
ATOM   1118  CE2 TRP B1006     -12.094   5.432  -6.358  1.00 12.54      F000 C  
ANISOU 1118  CE2 TRP B1006     2667   1114    982    -76    175   -140  F000 C  
ATOM   1119  CE3 TRP B1006     -11.020   7.529  -6.873  1.00 12.57      F000 C  
ANISOU 1119  CE3 TRP B1006     2299   1306   1170     75    195   -226  F000 C  
ATOM   1120  NE1 TRP B1006     -12.359   4.668  -5.251  1.00 11.83      F000 N  
ANISOU 1120  NE1 TRP B1006     2140   1157   1196    -12    135    -51  F000 N  
ATOM   1121  CZ2 TRP B1006     -12.405   5.212  -7.700  1.00 13.66      F000 C  
ANISOU 1121  CZ2 TRP B1006     2193   1760   1237   -315      3    -81  F000 C  
ATOM   1122  CZ3 TRP B1006     -11.326   7.306  -8.197  1.00 13.79      F000 C  
ANISOU 1122  CZ3 TRP B1006     2317   1638   1284   -103     24   -140  F000 C  
ATOM   1123  CH2 TRP B1006     -12.016   6.163  -8.597  1.00 14.40      F000 C  
ANISOU 1123  CH2 TRP B1006     2318   1894   1259    -61    175   -241  F000 C  
ATOM   1124  N  ALYS B1007      -8.389   8.212  -1.431  0.40 15.77      F000 N  
ANISOU 1124  N  ALYS B1007     1918   2139   1935    -28    -57    332  F000 N  
ATOM   1125  N  BLYS B1007      -8.458   8.195  -1.432  0.60 15.74      F000 N  
ANISOU 1125  N  BLYS B1007     1882   2150   1949    -23    -85    424  F000 N  
ATOM   1126  CA ALYS B1007      -7.720   9.174  -0.556  0.40 15.76      F000 C  
ANISOU 1126  CA ALYS B1007     2019   2081   1887     14    -18    184  F000 C  
ATOM   1127  CA BLYS B1007      -7.855   9.117  -0.495  0.60 15.60      F000 C  
ANISOU 1127  CA BLYS B1007     2019   2023   1882      9    -43    271  F000 C  
ATOM   1128  C  ALYS B1007      -6.563   8.510   0.178  0.40 15.10      F000 C  
ANISOU 1128  C  ALYS B1007     1961   2044   1733     31     -8    177  F000 C  
ATOM   1129  C  BLYS B1007      -6.592   8.474   0.053  0.60 15.21      F000 C  
ANISOU 1129  C  BLYS B1007     1973   1974   1830      9    -77    245  F000 C  
ATOM   1130  O  ALYS B1007      -6.475   7.284   0.232  0.40 14.10      F000 O  
ANISOU 1130  O  ALYS B1007     1938   2216   1199     26    168    276  F000 O  
ATOM   1131  O  BLYS B1007      -6.339   7.283  -0.142  0.60 14.20      F000 O  
ANISOU 1131  O  BLYS B1007     1910   1937   1546    -71   -162    430  F000 O  
ATOM   1132  CB ALYS B1007      -8.707   9.763   0.451  0.40 16.50      F000 C  
ANISOU 1132  CB ALYS B1007     2082   2092   2092     57    -43    181  F000 C  
ATOM   1133  CB BLYS B1007      -8.813   9.410   0.660  0.60 17.48      F000 C  
ANISOU 1133  CB BLYS B1007     2242   2107   2292    108    -86    278  F000 C  
ATOM   1134  CG ALYS B1007      -9.304   8.750   1.426  0.40 17.65      F000 C  
ANISOU 1134  CG ALYS B1007     2301   2120   2282    101   -142     -2  F000 C  
ATOM   1135  CG BLYS B1007     -10.268   9.583   0.249  0.60 20.42      F000 C  
ANISOU 1135  CG BLYS B1007     2695   2464   2599     49     12    249  F000 C  
ATOM   1136  CD ALYS B1007     -10.110   9.448   2.516  0.40 19.10      F000 C  
ANISOU 1136  CD ALYS B1007     2368   2467   2422     15    -99     61  F000 C  
ATOM   1137  CD BLYS B1007     -10.571  11.006  -0.149  0.60 24.50      F000 C  
ANISOU 1137  CD BLYS B1007     3143   3066   3099   -180    -80    215  F000 C  
ATOM   1138  CE ALYS B1007     -11.135   8.521   3.140  0.40 20.76      F000 C  
ANISOU 1138  CE ALYS B1007     2578   2657   2651    -17    -65    -72  F000 C  
ATOM   1139  CE BLYS B1007     -11.985  11.135  -0.711  0.60 25.47      F000 C  
ANISOU 1139  CE BLYS B1007     3286   3112   3278    -76   -138      9  F000 C  
ATOM   1140  NZ ALYS B1007     -11.714   9.100   4.380  0.40 23.63      F000 N1+
ANISOU 1140  NZ ALYS B1007     2905   3043   3030     -7   -253     63  F000 N1+
ATOM   1141  NZ BLYS B1007     -12.985  11.461   0.347  0.60 28.03      F000 N1+
ANISOU 1141  NZ BLYS B1007     3540   3247   3861   -227   -147   -301  F000 N1+
ATOM   1142  N  AARG B1008      -5.669   9.316   0.738  0.50 14.52      F000 N  
ANISOU 1142  N  AARG B1008     1896   1988   1633     21     64    170  F000 N  
ATOM   1143  N  BARG B1008      -5.793   9.271   0.745  0.50 14.17      F000 N  
ANISOU 1143  N  BARG B1008     1868   1887   1628     18      0    242  F000 N  
ATOM   1144  CA AARG B1008      -4.556   8.756   1.489  0.50 15.08      F000 C  
ANISOU 1144  CA AARG B1008     2011   1995   1722     56    -17    132  F000 C  
ATOM   1145  CA BARG B1008      -4.639   8.736   1.452  0.50 14.56      F000 C  
ANISOU 1145  CA BARG B1008     1960   1926   1644     56    -31    175  F000 C  
ATOM   1146  C  AARG B1008      -5.117   7.825   2.563  0.50 14.60      F000 C  
ANISOU 1146  C  AARG B1008     2051   1966   1529     48     48    134  F000 C  
ATOM   1147  C  BARG B1008      -5.134   7.818   2.569  0.50 14.46      F000 C  
ANISOU 1147  C  BARG B1008     2041   1944   1509     48     42    152  F000 C  
ATOM   1148  O  AARG B1008      -6.067   8.186   3.262  0.50 14.86      F000 O  
ANISOU 1148  O  AARG B1008     2333   1837   1477    108    -51    187  F000 O  
ATOM   1149  O  BARG B1008      -6.052   8.184   3.308  0.50 14.86      F000 O  
ANISOU 1149  O  BARG B1008     2339   1837   1468    108    -29    172  F000 O  
ATOM   1150  CB AARG B1008      -3.724   9.864   2.126  0.50 15.41      F000 C  
ANISOU 1150  CB AARG B1008     2069   2061   1725    -58     -2     93  F000 C  
ATOM   1151  CB BARG B1008      -3.789   9.870   2.028  0.50 14.91      F000 C  
ANISOU 1151  CB BARG B1008     2030   2032   1603    -67     -3    146  F000 C  
ATOM   1152  CG AARG B1008      -2.972  10.740   1.135  0.50 16.53      F000 C  
ANISOU 1152  CG AARG B1008     2111   2179   1991   -105      0     85  F000 C  
ATOM   1153  CG BARG B1008      -3.174  10.786   0.976  0.50 14.54      F000 C  
ANISOU 1153  CG BARG B1008     1866   1969   1687    -93     -4    157  F000 C  
ATOM   1154  CD AARG B1008      -1.937  11.595   1.855  0.50 19.57      F000 C  
ANISOU 1154  CD AARG B1008     2547   2483   2403    -55    129    -11  F000 C  
ATOM   1155  CD BARG B1008      -2.428  11.962   1.603  0.50 16.40      F000 C  
ANISOU 1155  CD BARG B1008     2224   2186   1820    -30     99    143  F000 C  
ATOM   1156  NE AARG B1008      -2.571  12.530   2.781  0.50 23.38      F000 N  
ANISOU 1156  NE AARG B1008     2927   3043   2913   -248    316     54  F000 N  
ATOM   1157  NE BARG B1008      -1.656  12.689   0.603  0.50 16.26      F000 N  
ANISOU 1157  NE BARG B1008     2082   2480   1614   -222    275    243  F000 N  
ATOM   1158  CZ AARG B1008      -2.056  12.918   3.947  0.50 25.15      F000 C  
ANISOU 1158  CZ AARG B1008     3202   3197   3156   -160     41     26  F000 C  
ATOM   1159  CZ BARG B1008      -1.012  13.830   0.828  0.50 20.98      F000 C  
ANISOU 1159  CZ BARG B1008     2526   3032   2410   -214    280     32  F000 C  
ATOM   1160  NH1AARG B1008      -0.880  12.460   4.369  0.50 25.15      F000 N1+
ANISOU 1160  NH1AARG B1008     3294   3225   3033   -429    195     66  F000 N1+
ATOM   1161  NH1BARG B1008      -1.033  14.388   2.031  0.50 22.95      F000 N1+
ANISOU 1161  NH1BARG B1008     3038   3338   2344   -119    535    -22  F000 N1+
ATOM   1162  NH2AARG B1008      -2.730  13.774   4.697  0.50 23.88      F000 N  
ANISOU 1162  NH2AARG B1008     3295   2985   2790   -145    373    -72  F000 N  
ATOM   1163  NH2BARG B1008      -0.343  14.416  -0.157  0.50 20.60      F000 N  
ANISOU 1163  NH2BARG B1008     2278   3366   2182   -207    565    -53  F000 N  
ATOM   1164  N   PRO B1009      -4.547   6.614   2.683  1.00 14.21      F000 N  
ANISOU 1164  N   PRO B1009     2058   1939   1400    105    -18    158  F000 N  
ATOM   1165  CA  PRO B1009      -4.980   5.645   3.684  1.00 15.13      F000 C  
ANISOU 1165  CA  PRO B1009     2183   2011   1552     60    -57    175  F000 C  
ATOM   1166  C   PRO B1009      -4.505   5.971   5.103  1.00 15.12      F000 C  
ANISOU 1166  C   PRO B1009     2282   1993   1469     62   -216     86  F000 C  
ATOM   1167  O   PRO B1009      -3.646   5.297   5.670  1.00 15.01      F000 O  
ANISOU 1167  O   PRO B1009     2370   1899   1433     99   -288     77  F000 O  
ATOM   1168  CB  PRO B1009      -4.417   4.328   3.157  1.00 15.06      F000 C  
ANISOU 1168  CB  PRO B1009     2222   2088   1411     15   -218    301  F000 C  
ATOM   1169  CG  PRO B1009      -3.205   4.705   2.403  1.00 15.25      F000 C  
ANISOU 1169  CG  PRO B1009     2220   2025   1547    236    -47    124  F000 C  
ATOM   1170  CD  PRO B1009      -3.495   6.060   1.807  1.00 14.60      F000 C  
ANISOU 1170  CD  PRO B1009     2099   1991   1456    219   -119    230  F000 C  
ATOM   1171  N   LEU B1010      -5.079   7.028   5.661  1.00 15.10      F000 N  
ANISOU 1171  N   LEU B1010     2361   1927   1448    164    -96    217  F000 N  
ATOM   1172  CA  LEU B1010      -4.806   7.432   7.025  1.00 16.62      F000 C  
ANISOU 1172  CA  LEU B1010     2494   2071   1750     47    -10    106  F000 C  
ATOM   1173  C   LEU B1010      -5.724   6.667   7.973  1.00 16.97      F000 C  
ANISOU 1173  C   LEU B1010     2787   1945   1715    108    -19    152  F000 C  
ATOM   1174  O   LEU B1010      -6.928   6.545   7.741  1.00 20.06      F000 O  
ANISOU 1174  O   LEU B1010     3429   2169   2020    182    -70    101  F000 O  
ATOM   1175  CB  LEU B1010      -5.038   8.932   7.168  1.00 17.49      F000 C  
ANISOU 1175  CB  LEU B1010     2508   2207   1930    104     40    113  F000 C  
ATOM   1176  CG  LEU B1010      -4.118   9.818   6.331  1.00 18.26      F000 C  
ANISOU 1176  CG  LEU B1010     2317   2465   2152   -221    146    245  F000 C  
ATOM   1177  CD1 LEU B1010      -4.599  11.263   6.343  1.00 24.44      F000 C  
ANISOU 1177  CD1 LEU B1010     3325   2779   3182   -143   -217    267  F000 C  
ATOM   1178  CD2 LEU B1010      -2.678   9.721   6.821  1.00 24.22      F000 C  
ANISOU 1178  CD2 LEU B1010     2985   3187   3028    -78   -145   -205  F000 C  
ATOM   1179  N   VAL B1011      -5.141   6.144   9.043  1.00 17.18      F000 N  
ANISOU 1179  N   VAL B1011     2755   1967   1806    152   -144     84  F000 N  
ATOM   1180  CA  VAL B1011      -5.903   5.423  10.042  1.00 18.59      F000 C  
ANISOU 1180  CA  VAL B1011     2812   2209   2040     95    -92    -56  F000 C  
ATOM   1181  C   VAL B1011      -5.511   5.916  11.420  1.00 19.35      F000 C  
ANISOU 1181  C   VAL B1011     2938   2223   2190     56    -73    -46  F000 C  
ATOM   1182  O   VAL B1011      -4.467   6.546  11.598  1.00 19.43      F000 O  
ANISOU 1182  O   VAL B1011     3297   2338   1745    117    -60    -17  F000 O  
ATOM   1183  CB  VAL B1011      -5.676   3.902   9.957  1.00 20.19      F000 C  
ANISOU 1183  CB  VAL B1011     2980   2428   2260    -16   -207    -71  F000 C  
ATOM   1184  CG1 VAL B1011      -6.119   3.358   8.599  1.00 22.52      F000 C  
ANISOU 1184  CG1 VAL B1011     3102   2823   2630     19     64   -208  F000 C  
ATOM   1185  CG2 VAL B1011      -4.224   3.568  10.226  1.00 21.56      F000 C  
ANISOU 1185  CG2 VAL B1011     3287   2536   2367    224   -219   -129  F000 C  
ATOM   1186  N   THR B1012      -6.365   5.634  12.398  1.00 20.00      F000 N  
ANISOU 1186  N   THR B1012     3103   2425   2069    102   -132    -69  F000 N  
ATOM   1187  CA  THR B1012      -6.039   5.892  13.786  1.00 20.80      F000 C  
ANISOU 1187  CA  THR B1012     2897   2630   2376    158    -41   -130  F000 C  
ATOM   1188  C   THR B1012      -5.225   4.741  14.336  1.00 18.98      F000 C  
ANISOU 1188  C   THR B1012     2566   2544   2099     14    -97     34  F000 C  
ATOM   1189  O   THR B1012      -5.528   3.564  14.095  1.00 21.25      F000 O  
ANISOU 1189  O   THR B1012     3069   2771   2230   -132   -267     71  F000 O  
ATOM   1190  CB  THR B1012      -7.310   6.073  14.614  1.00 22.83      F000 C  
ANISOU 1190  CB  THR B1012     3231   2909   2533    143   -122   -190  F000 C  
ATOM   1191  CG2 THR B1012      -6.966   6.371  16.070  0.50 21.01      F000 C  
ANISOU 1191  CG2 THR B1012     3094   2729   2158    187    -37   -138  F000 C  
ATOM   1192  OG1 THR B1012      -8.068   7.155  14.068  1.00 25.66      F000 O  
ANISOU 1192  OG1 THR B1012     3727   3205   2817    792    -52   -515  F000 O  
ATOM   1193  N   ILE B1013      -4.159   5.084  15.044  1.00 18.46      F000 N  
ANISOU 1193  N   ILE B1013     2408   2649   1956     60    -97     33  F000 N  
ATOM   1194  CA  ILE B1013      -3.379   4.086  15.741  1.00 17.25      F000 C  
ANISOU 1194  CA  ILE B1013     2295   2434   1823     18     37    123  F000 C  
ATOM   1195  C   ILE B1013      -3.354   4.395  17.236  1.00 16.90      F000 C  
ANISOU 1195  C   ILE B1013     2073   2651   1695    -14    158     79  F000 C  
ATOM   1196  O   ILE B1013      -3.461   5.555  17.652  1.00 18.32      F000 O  
ANISOU 1196  O   ILE B1013     2161   3061   1738    132     96     49  F000 O  
ATOM   1197  CB  ILE B1013      -1.953   4.005  15.185  1.00 16.66      F000 C  
ANISOU 1197  CB  ILE B1013     2138   2412   1779    108     18    213  F000 C  
ATOM   1198  CG1 ILE B1013      -1.211   5.323  15.418  1.00 18.24      F000 C  
ANISOU 1198  CG1 ILE B1013     2551   2212   2164   -105     76    259  F000 C  
ATOM   1199  CG2 ILE B1013      -1.996   3.688  13.699  1.00 18.26      F000 C  
ANISOU 1199  CG2 ILE B1013     2528   2559   1848   -109    199     31  F000 C  
ATOM   1200  CD1 ILE B1013       0.264   5.243  15.192  1.00 19.02      F000 C  
ANISOU 1200  CD1 ILE B1013     2568   2526   2132      9    120   -140  F000 C  
ATOM   1201  N   LYS B1014      -3.232   3.340  18.029  1.00 14.99      F000 N  
ANISOU 1201  N   LYS B1014     2075   2127   1493     -6     88    232  F000 N  
ATOM   1202  CA  LYS B1014      -2.998   3.470  19.458  1.00 16.16      F000 C  
ANISOU 1202  CA  LYS B1014     2150   2265   1724    -35     61     76  F000 C  
ATOM   1203  C   LYS B1014      -1.591   2.981  19.728  1.00 15.23      F000 C  
ANISOU 1203  C   LYS B1014     2098   2186   1501    -68     33     72  F000 C  
ATOM   1204  O   LYS B1014      -1.245   1.864  19.376  1.00 14.53      F000 O  
ANISOU 1204  O   LYS B1014     1805   2159   1554     50     24    200  F000 O  
ATOM   1205  CB  LYS B1014      -3.954   2.577  20.242  1.00 18.09      F000 C  
ANISOU 1205  CB  LYS B1014     2430   2433   2009    -96    120     78  F000 C  
ATOM   1206  CG  LYS B1014      -5.400   2.986  20.231  1.00 21.51      F000 C  
ANISOU 1206  CG  LYS B1014     2898   2878   2395   -105   -169    -74  F000 C  
ATOM   1207  CD  LYS B1014      -6.126   2.277  21.375  1.00 23.44      F000 C  
ANISOU 1207  CD  LYS B1014     3104   2968   2831    -59   -197   -113  F000 C  
ATOM   1208  CE  LYS B1014      -7.605   2.522  21.375  1.00 26.63      F000 C  
ANISOU 1208  CE  LYS B1014     3368   3313   3435    -42   -217   -108  F000 C  
ATOM   1209  NZ  LYS B1014      -8.250   1.672  22.412  1.00 26.50      F000 N1+
ANISOU 1209  NZ  LYS B1014     3844   3358   2865   -216   -410   -264  F000 N1+
ATOM   1210  N   ILE B1015      -0.791   3.815  20.368  1.00 14.12      F000 N  
ANISOU 1210  N   ILE B1015     1901   2024   1440    -36    167     -1  F000 N  
ATOM   1211  CA  ILE B1015       0.576   3.452  20.691  1.00 14.56      F000 C  
ANISOU 1211  CA  ILE B1015     1921   2032   1579    -16    136     96  F000 C  
ATOM   1212  C   ILE B1015       1.064   4.309  21.847  1.00 15.29      F000 C  
ANISOU 1212  C   ILE B1015     1983   2202   1623     67    147    141  F000 C  
ATOM   1213  O   ILE B1015       0.771   5.501  21.911  1.00 15.76      F000 O  
ANISOU 1213  O   ILE B1015     1930   2501   1555    -50    284     26  F000 O  
ATOM   1214  CB  ILE B1015       1.510   3.643  19.462  1.00 14.34      F000 C  
ANISOU 1214  CB  ILE B1015     1802   2023   1622    -49     47      0  F000 C  
ATOM   1215  CG1 ILE B1015       2.946   3.233  19.803  1.00 15.26      F000 C  
ANISOU 1215  CG1 ILE B1015     2015   2020   1760   -128    168     17  F000 C  
ATOM   1216  CG2 ILE B1015       1.432   5.083  18.943  1.00 15.91      F000 C  
ANISOU 1216  CG2 ILE B1015     2228   2090   1726    -49    102    -29  F000 C  
ATOM   1217  CD1 ILE B1015       3.917   3.267  18.639  1.00 17.01      F000 C  
ANISOU 1217  CD1 ILE B1015     2267   2245   1950     30     19    152  F000 C  
ATOM   1218  N   GLY B1016       1.805   3.688  22.761  1.00 15.72      F000 N  
ANISOU 1218  N   GLY B1016     2035   2332   1604    111    255    231  F000 N  
ATOM   1219  CA  GLY B1016       2.420   4.419  23.866  1.00 16.66      F000 C  
ANISOU 1219  CA  GLY B1016     2141   2319   1869    -58    231    171  F000 C  
ATOM   1220  C   GLY B1016       1.420   5.176  24.713  1.00 16.94      F000 C  
ANISOU 1220  C   GLY B1016     2202   2326   1907     11    185    113  F000 C  
ATOM   1221  O   GLY B1016       1.742   6.229  25.280  1.00 18.51      F000 O  
ANISOU 1221  O   GLY B1016     2435   2708   1887    -83    438    146  F000 O  
ATOM   1222  N   GLY B1017       0.200   4.659  24.806  1.00 16.15      F000 N  
ANISOU 1222  N   GLY B1017     2101   2233   1801     73    226     37  F000 N  
ATOM   1223  CA  GLY B1017      -0.818   5.290  25.640  1.00 16.93      F000 C  
ANISOU 1223  CA  GLY B1017     2133   2384   1915     98    257      2  F000 C  
ATOM   1224  C   GLY B1017      -1.448   6.505  24.975  1.00 18.07      F000 C  
ANISOU 1224  C   GLY B1017     2222   2576   2065    177    219    -58  F000 C  
ATOM   1225  O   GLY B1017      -2.172   7.258  25.623  1.00 20.00      F000 O  
ANISOU 1225  O   GLY B1017     2478   2967   2154    315    218   -450  F000 O  
ATOM   1226  N   GLN B1018      -1.193   6.674  23.675  1.00 17.93      F000 N  
ANISOU 1226  N   GLN B1018     2178   2596   2036    185    178    -87  F000 N  
ATOM   1227  CA  GLN B1018      -1.665   7.818  22.903  1.00 19.41      F000 C  
ANISOU 1227  CA  GLN B1018     2414   2700   2258     36    170    -20  F000 C  
ATOM   1228  C   GLN B1018      -2.451   7.358  21.670  1.00 19.07      F000 C  
ANISOU 1228  C   GLN B1018     2389   2623   2232     41    214      9  F000 C  
ATOM   1229  O   GLN B1018      -2.289   6.232  21.220  1.00 19.57      F000 O  
ANISOU 1229  O   GLN B1018     2311   2741   2381    262    561    -38  F000 O  
ATOM   1230  CB  GLN B1018      -0.469   8.640  22.409  1.00 20.80      F000 C  
ANISOU 1230  CB  GLN B1018     2597   2823   2481    -39    132     52  F000 C  
ATOM   1231  CG  GLN B1018       0.450   9.195  23.485  1.00 24.50      F000 C  
ANISOU 1231  CG  GLN B1018     2912   3228   3169     12    -16    -32  F000 C  
ATOM   1232  CD  GLN B1018       1.362  10.274  22.923  0.50 22.43      F000 C  
ANISOU 1232  CD  GLN B1018     2636   2846   3040     16    127   -119  F000 C  
ATOM   1233  NE2 GLN B1018       0.816  11.472  22.747  0.50 25.42      F000 N  
ANISOU 1233  NE2 GLN B1018     3033   3047   3575    -15    -87   -364  F000 N  
ATOM   1234  OE1 GLN B1018       2.532  10.029  22.628  0.50 23.71      F000 O  
ANISOU 1234  OE1 GLN B1018     2727   2602   3678    356    337   -183  F000 O  
ATOM   1235  N   LEU B1019      -3.262   8.256  21.118  1.00 20.32      F000 N  
ANISOU 1235  N   LEU B1019     2460   2941   2317    120    221    -35  F000 N  
ATOM   1236  CA  LEU B1019      -3.879   8.079  19.805  1.00 22.09      F000 C  
ANISOU 1236  CA  LEU B1019     2641   3077   2673     19    108    -34  F000 C  
ATOM   1237  C   LEU B1019      -3.179   8.977  18.796  1.00 22.15      F000 C  
ANISOU 1237  C   LEU B1019     2544   3287   2582     35     57    -47  F000 C  
ATOM   1238  O   LEU B1019      -2.942  10.160  19.061  1.00 23.07      F000 O  
ANISOU 1238  O   LEU B1019     2335   3954   2477     30     92      3  F000 O  
ATOM   1239  CB  LEU B1019      -5.355   8.477  19.834  1.00 23.60      F000 C  
ANISOU 1239  CB  LEU B1019     2709   3212   3043     36    150      8  F000 C  
ATOM   1240  CG  LEU B1019      -6.359   7.586  20.560  1.00 26.58      F000 C  
ANISOU 1240  CG  LEU B1019     3388   3445   3263     56     85   -201  F000 C  
ATOM   1241  CD1 LEU B1019      -7.699   8.309  20.676  1.00 29.63      F000 C  
ANISOU 1241  CD1 LEU B1019     3758   3609   3890    128     26    -92  F000 C  
ATOM   1242  CD2 LEU B1019      -6.541   6.261  19.844  1.00 29.56      F000 C  
ANISOU 1242  CD2 LEU B1019     3611   3778   3839    -18    144   -244  F000 C  
ATOM   1243  N   LYS B1020      -2.873   8.429  17.629  1.00 20.73      F000 N  
ANISOU 1243  N   LYS B1020     2323   3168   2383     -6     15     85  F000 N  
ATOM   1244  CA  LYS B1020      -2.285   9.224  16.567  1.00 21.29      F000 C  
ANISOU 1244  CA  LYS B1020     2634   2981   2472     13     76     47  F000 C  
ATOM   1245  C   LYS B1020      -2.899   8.819  15.243  1.00 20.59      F000 C  
ANISOU 1245  C   LYS B1020     2546   2836   2441    -35    -11    178  F000 C  
ATOM   1246  O   LYS B1020      -3.580   7.798  15.152  1.00 22.24      F000 O  
ANISOU 1246  O   LYS B1020     2724   3255   2469      4    -54    541  F000 O  
ATOM   1247  CB  LYS B1020      -0.772   9.028  16.539  1.00 21.40      F000 C  
ANISOU 1247  CB  LYS B1020     2745   2954   2431   -106    -41    178  F000 C  
ATOM   1248  CG  LYS B1020      -0.090   9.439  17.841  1.00 23.85      F000 C  
ANISOU 1248  CG  LYS B1020     3171   3247   2642    -44    -90    120  F000 C  
ATOM   1249  CD  LYS B1020       1.410   9.298  17.788  0.50 23.30      F000 C  
ANISOU 1249  CD  LYS B1020     2939   3160   2753     14    127     88  F000 C  
ATOM   1250  CE  LYS B1020       2.053  10.070  18.933  0.50 25.28      F000 C  
ANISOU 1250  CE  LYS B1020     3260   3260   3083    -21    157    139  F000 C  
ATOM   1251  NZ  LYS B1020       2.068  11.530  18.664  0.50 25.74      F000 N1+
ANISOU 1251  NZ  LYS B1020     3111   3529   3139    -89     99    -87  F000 N1+
ATOM   1252  N  AGLU B1021      -2.673   9.647  14.229  0.50 20.18      F000 N  
ANISOU 1252  N  AGLU B1021     2601   2711   2352     68     30     36  F000 N  
ATOM   1253  N  BGLU B1021      -2.663   9.630  14.220  0.50 19.91      F000 N  
ANISOU 1253  N  BGLU B1021     2558   2695   2312     71     27     19  F000 N  
ATOM   1254  CA AGLU B1021      -3.035   9.323  12.855  0.50 20.11      F000 C  
ANISOU 1254  CA AGLU B1021     2628   2654   2359     65      2     53  F000 C  
ATOM   1255  CA BGLU B1021      -3.057   9.285  12.862  0.50 19.90      F000 C  
ANISOU 1255  CA BGLU B1021     2593   2632   2334     77     -6     43  F000 C  
ATOM   1256  C  AGLU B1021      -1.768   8.897  12.122  0.50 19.11      F000 C  
ANISOU 1256  C  AGLU B1021     2519   2530   2209     94    -25     18  F000 C  
ATOM   1257  C  BGLU B1021      -1.805   8.947  12.063  0.50 19.01      F000 C  
ANISOU 1257  C  BGLU B1021     2517   2518   2187     92    -38     28  F000 C  
ATOM   1258  O  AGLU B1021      -0.700   9.467  12.342  0.50 19.31      F000 O  
ANISOU 1258  O  AGLU B1021     2572   2650   2115    148     87    -98  F000 O  
ATOM   1259  O  BGLU B1021      -0.791   9.635  12.166  0.50 18.95      F000 O  
ANISOU 1259  O  BGLU B1021     2586   2561   2053    102     82     -8  F000 O  
ATOM   1260  CB AGLU B1021      -3.648  10.544  12.166  0.50 20.42      F000 C  
ANISOU 1260  CB AGLU B1021     2755   2624   2379     65     -6     37  F000 C  
ATOM   1261  CB BGLU B1021      -3.799  10.452  12.209  0.50 20.84      F000 C  
ANISOU 1261  CB BGLU B1021     2800   2687   2431     88    -23     11  F000 C  
ATOM   1262  CG AGLU B1021      -4.265  10.245  10.808  0.50 21.32      F000 C  
ANISOU 1262  CG AGLU B1021     2808   2748   2542     82     15    113  F000 C  
ATOM   1263  CG BGLU B1021      -5.098  10.821  12.909  0.50 23.12      F000 C  
ANISOU 1263  CG BGLU B1021     2923   2955   2906    191    -95    -17  F000 C  
ATOM   1264  CD AGLU B1021      -5.092  11.399  10.280  0.50 22.95      F000 C  
ANISOU 1264  CD AGLU B1021     3065   2911   2743      4    -13    103  F000 C  
ATOM   1265  CD BGLU B1021      -6.207   9.814  12.661  0.50 27.32      F000 C  
ANISOU 1265  CD BGLU B1021     3476   3556   3347     87   -113    -53  F000 C  
ATOM   1266  OE1AGLU B1021      -4.512  12.468   9.990  0.50 26.64      F000 O  
ANISOU 1266  OE1AGLU B1021     3307   3812   3000     43   -287    128  F000 O  
ATOM   1267  OE1BGLU B1021      -6.637   9.672  11.496  0.50 31.42      F000 O  
ANISOU 1267  OE1BGLU B1021     3832   4013   4094    266   -149   -300  F000 O  
ATOM   1268  OE2AGLU B1021      -6.324  11.237  10.161  0.50 27.76      F000 O1-
ANISOU 1268  OE2AGLU B1021     4056   3094   3396    166    -33    191  F000 O1-
ATOM   1269  OE2BGLU B1021      -6.656   9.170  13.636  0.50 30.26      F000 O1-
ANISOU 1269  OE2BGLU B1021     3703   4045   3748    347   -239    140  F000 O1-
ATOM   1270  N   ALA B1022      -1.882   7.886  11.269  1.00 17.87      F000 N  
ANISOU 1270  N   ALA B1022     2562   2362   1864     99   -130    257  F000 N  
ATOM   1271  CA  ALA B1022      -0.749   7.448  10.481  1.00 17.03      F000 C  
ANISOU 1271  CA  ALA B1022     2367   2306   1796     59    -38    146  F000 C  
ATOM   1272  C   ALA B1022      -1.193   6.898   9.141  1.00 15.84      F000 C  
ANISOU 1272  C   ALA B1022     2487   2054   1477     25     17    153  F000 C  
ATOM   1273  O   ALA B1022      -2.325   6.460   8.980  1.00 16.54      F000 O  
ANISOU 1273  O   ALA B1022     2838   2010   1434     68    -66    151  F000 O  
ATOM   1274  CB  ALA B1022       0.050   6.400  11.241  1.00 16.07      F000 C  
ANISOU 1274  CB  ALA B1022     2249   2300   1557     43    -62    296  F000 C  
ATOM   1275  N   LEU B1023      -0.260   6.909   8.199  1.00 15.16      F000 N  
ANISOU 1275  N   LEU B1023     2356   2018   1387      1    -56    209  F000 N  
ATOM   1276  CA  LEU B1023      -0.498   6.478   6.825  1.00 16.08      F000 C  
ANISOU 1276  CA  LEU B1023     2433   2071   1603    -41    -29    155  F000 C  
ATOM   1277  C   LEU B1023      -0.082   5.023   6.629  1.00 14.97      F000 C  
ANISOU 1277  C   LEU B1023     2382   1898   1406    -84   -104    315  F000 C  
ATOM   1278  O   LEU B1023       1.054   4.650   6.961  1.00 16.22      F000 O  
ANISOU 1278  O   LEU B1023     2598   1955   1607    271   -164    470  F000 O  
ATOM   1279  CB  LEU B1023       0.349   7.363   5.918  1.00 15.47      F000 C  
ANISOU 1279  CB  LEU B1023     2309   1954   1613   -127   -108    178  F000 C  
ATOM   1280  CG  LEU B1023       0.237   7.143   4.416  1.00 16.52      F000 C  
ANISOU 1280  CG  LEU B1023     2320   2109   1847   -184   -102    127  F000 C  
ATOM   1281  CD1 LEU B1023      -1.099   7.612   3.926  1.00 18.55      F000 C  
ANISOU 1281  CD1 LEU B1023     2842   2415   1792    139    -78    -45  F000 C  
ATOM   1282  CD2 LEU B1023       1.367   7.852   3.677  1.00 17.77      F000 C  
ANISOU 1282  CD2 LEU B1023     2728   2354   1670   -189   -192    -65  F000 C  
ATOM   1283  N   LEU B1024      -0.970   4.206   6.058  1.00 14.32      F000 N  
ANISOU 1283  N   LEU B1024     2341   1756   1342    -12   -133    223  F000 N  
ATOM   1284  CA  LEU B1024      -0.606   2.843   5.685  1.00 14.76      F000 C  
ANISOU 1284  CA  LEU B1024     2294   1821   1491      2   -233    198  F000 C  
ATOM   1285  C   LEU B1024       0.184   2.897   4.379  1.00 14.97      F000 C  
ANISOU 1285  C   LEU B1024     2368   1855   1464     24   -147     95  F000 C  
ATOM   1286  O   LEU B1024      -0.387   3.166   3.323  1.00 15.92      F000 O  
ANISOU 1286  O   LEU B1024     2945   1781   1321    246   -304    312  F000 O  
ATOM   1287  CB  LEU B1024      -1.851   1.963   5.526  1.00 15.01      F000 C  
ANISOU 1287  CB  LEU B1024     2312   1887   1500     71   -144    151  F000 C  
ATOM   1288  CG  LEU B1024      -2.785   1.881   6.742  1.00 16.47      F000 C  
ANISOU 1288  CG  LEU B1024     2668   1934   1654     19   -251    207  F000 C  
ATOM   1289  CD1 LEU B1024      -3.962   0.939   6.485  1.00 18.26      F000 C  
ANISOU 1289  CD1 LEU B1024     2749   2058   2127    -17   -206   -190  F000 C  
ATOM   1290  CD2 LEU B1024      -2.023   1.461   8.003  1.00 18.58      F000 C  
ANISOU 1290  CD2 LEU B1024     3066   2335   1658    127   -570    -90  F000 C  
ATOM   1291  N   ASP B1025       1.491   2.659   4.457  1.00 15.07      F000 N  
ANISOU 1291  N   ASP B1025     2349   2041   1333    -50   -201    127  F000 N  
ATOM   1292  CA  ASP B1025       2.429   3.023   3.392  1.00 14.72      F000 C  
ANISOU 1292  CA  ASP B1025     2248   1816   1528     91   -152    107  F000 C  
ATOM   1293  C   ASP B1025       3.200   1.796   2.880  1.00 13.43      F000 C  
ANISOU 1293  C   ASP B1025     1971   1837   1294     82   -216    147  F000 C  
ATOM   1294  O   ASP B1025       4.217   1.409   3.451  1.00 15.51      F000 O  
ANISOU 1294  O   ASP B1025     2733   1781   1378    343   -512    160  F000 O  
ATOM   1295  CB  ASP B1025       3.398   4.069   3.941  1.00 15.68      F000 C  
ANISOU 1295  CB  ASP B1025     2267   1994   1694     37   -169    -21  F000 C  
ATOM   1296  CG  ASP B1025       4.261   4.698   2.869  1.00 18.00      F000 C  
ANISOU 1296  CG  ASP B1025     2678   2205   1955    -46   -136     -8  F000 C  
ATOM   1297  OD1 ASP B1025       4.323   4.146   1.747  1.00 18.43      F000 O  
ANISOU 1297  OD1 ASP B1025     2651   2685   1666     88   -312    -44  F000 O  
ATOM   1298  OD2 ASP B1025       4.874   5.756   3.159  1.00 19.59      F000 O1-
ANISOU 1298  OD2 ASP B1025     2932   2504   2005    -47     93    225  F000 O1-
ATOM   1299  N   THR B1026       2.709   1.172   1.811  1.00 14.25      F000 N  
ANISOU 1299  N   THR B1026     2239   1877   1295    154   -335    171  F000 N  
ATOM   1300  CA  THR B1026       3.377   0.003   1.247  1.00 14.18      F000 C  
ANISOU 1300  CA  THR B1026     2135   1957   1295     76   -330    105  F000 C  
ATOM   1301  C   THR B1026       4.692   0.334   0.566  1.00 14.36      F000 C  
ANISOU 1301  C   THR B1026     2132   1949   1374    148   -324    130  F000 C  
ATOM   1302  O   THR B1026       5.458  -0.579   0.227  1.00 16.15      F000 O  
ANISOU 1302  O   THR B1026     2573   2011   1550    300   -411     -2  F000 O  
ATOM   1303  CB  THR B1026       2.496  -0.737   0.234  1.00 13.63      F000 C  
ANISOU 1303  CB  THR B1026     1885   1999   1292    183   -225     25  F000 C  
ATOM   1304  CG2 THR B1026       1.208  -1.202   0.897  1.00 13.82      F000 C  
ANISOU 1304  CG2 THR B1026     1855   2164   1229     99   -399    146  F000 C  
ATOM   1305  OG1 THR B1026       2.201   0.136  -0.864  1.00 15.00      F000 O  
ANISOU 1305  OG1 THR B1026     2065   2383   1249    195   -578    210  F000 O  
ATOM   1306  N   GLY B1027       4.956   1.624   0.362  1.00 14.95      F000 N  
ANISOU 1306  N   GLY B1027     2321   1918   1438    141   -380    179  F000 N  
ATOM   1307  CA  GLY B1027       6.230   2.055  -0.191  1.00 15.97      F000 C  
ANISOU 1307  CA  GLY B1027     2361   2041   1664     14   -295    112  F000 C  
ATOM   1308  C   GLY B1027       7.303   2.325   0.849  1.00 17.04      F000 C  
ANISOU 1308  C   GLY B1027     2718   2031   1724    -52   -348     40  F000 C  
ATOM   1309  O   GLY B1027       8.389   2.772   0.524  1.00 19.08      F000 O  
ANISOU 1309  O   GLY B1027     3488   2149   1611    -28   -484     47  F000 O  
ATOM   1310  N   ALA B1028       6.990   2.076   2.115  1.00 16.30      F000 N  
ANISOU 1310  N   ALA B1028     2641   2075   1475    -17   -379     65  F000 N  
ATOM   1311  CA  ALA B1028       7.942   2.308   3.202  1.00 15.79      F000 C  
ANISOU 1311  CA  ALA B1028     2370   1933   1695    -21   -209     48  F000 C  
ATOM   1312  C   ALA B1028       8.322   0.978   3.836  1.00 14.68      F000 C  
ANISOU 1312  C   ALA B1028     2363   1654   1558     24   -281     32  F000 C  
ATOM   1313  O   ALA B1028       7.450   0.179   4.200  1.00 15.18      F000 O  
ANISOU 1313  O   ALA B1028     2598   1698   1470   -104   -298     42  F000 O  
ATOM   1314  CB  ALA B1028       7.319   3.217   4.248  1.00 17.08      F000 C  
ANISOU 1314  CB  ALA B1028     2495   2164   1828    111   -294     69  F000 C  
ATOM   1315  N   ASP B1029       9.622   0.734   3.987  1.00 14.62      F000 N  
ANISOU 1315  N   ASP B1029     2391   1698   1465    -19   -130    -78  F000 N  
ATOM   1316  CA  ASP B1029      10.079  -0.504   4.589  1.00 14.80      F000 C  
ANISOU 1316  CA  ASP B1029     2243   1805   1574     74   -113   -117  F000 C  
ATOM   1317  C   ASP B1029       9.746  -0.494   6.080  1.00 14.87      F000 C  
ANISOU 1317  C   ASP B1029     2147   1948   1554    -29    -89   -129  F000 C  
ATOM   1318  O   ASP B1029       9.381  -1.521   6.637  1.00 15.75      F000 O  
ANISOU 1318  O   ASP B1029     2246   2149   1589     92    -26   -193  F000 O  
ATOM   1319  CB  ASP B1029      11.596  -0.666   4.436  1.00 15.73      F000 C  
ANISOU 1319  CB  ASP B1029     2600   1754   1620     18    -51   -145  F000 C  
ATOM   1320  CG  ASP B1029      12.065  -0.705   2.986  1.00 19.46      F000 C  
ANISOU 1320  CG  ASP B1029     3269   2260   1864    -64    -49   -326  F000 C  
ATOM   1321  OD1 ASP B1029      11.276  -1.019   2.073  1.00 19.33      F000 O  
ANISOU 1321  OD1 ASP B1029     3482   2280   1581    -45     24   -291  F000 O  
ATOM   1322  OD2 ASP B1029      13.262  -0.427   2.774  1.00 25.60      F000 O1-
ANISOU 1322  OD2 ASP B1029     4890   2618   2219   -348    472   -528  F000 O1-
ATOM   1323  N   ASP B1030       9.904   0.673   6.711  1.00 14.14      F000 N  
ANISOU 1323  N   ASP B1030     2116   1907   1348     66    -93    -74  F000 N  
ATOM   1324  CA  ASP B1030       9.871   0.808   8.169  1.00 14.97      F000 C  
ANISOU 1324  CA  ASP B1030     2123   1932   1633      4   -237    -58  F000 C  
ATOM   1325  C   ASP B1030       8.758   1.749   8.604  1.00 14.04      F000 C  
ANISOU 1325  C   ASP B1030     1935   1884   1513     33   -273    -22  F000 C  
ATOM   1326  O   ASP B1030       8.301   2.607   7.853  1.00 15.07      F000 O  
ANISOU 1326  O   ASP B1030     2223   2027   1474    193   -482     80  F000 O  
ATOM   1327  CB  ASP B1030      11.189   1.372   8.709  1.00 16.07      F000 C  
ANISOU 1327  CB  ASP B1030     2345   2077   1684    143   -175    -32  F000 C  
ATOM   1328  CG  ASP B1030      12.390   0.584   8.261  1.00 18.68      F000 C  
ANISOU 1328  CG  ASP B1030     2841   2475   1781     -7   -328   -309  F000 C  
ATOM   1329  OD1 ASP B1030      12.411  -0.642   8.455  1.00 22.68      F000 O  
ANISOU 1329  OD1 ASP B1030     3263   3196   2156    647   -413    -75  F000 O  
ATOM   1330  OD2 ASP B1030      13.297   1.192   7.664  1.00 27.04      F000 O1-
ANISOU 1330  OD2 ASP B1030     3540   2888   3844   -447   -723   -967  F000 O1-
ATOM   1331  N   THR B1031       8.353   1.574   9.851  1.00 14.11      F000 N  
ANISOU 1331  N   THR B1031     1981   1879   1500     53   -173    -65  F000 N  
ATOM   1332  CA  THR B1031       7.405   2.426  10.524  1.00 12.60      F000 C  
ANISOU 1332  CA  THR B1031     1748   1688   1352    -46    -80    143  F000 C  
ATOM   1333  C   THR B1031       8.148   3.531  11.229  1.00 12.24      F000 C  
ANISOU 1333  C   THR B1031     1624   1642   1384     12   -136     66  F000 C  
ATOM   1334  O   THR B1031       9.090   3.269  11.996  1.00 13.79      F000 O  
ANISOU 1334  O   THR B1031     2012   1893   1335    -97   -243    318  F000 O  
ATOM   1335  CB  THR B1031       6.601   1.582  11.516  1.00 12.59      F000 C  
ANISOU 1335  CB  THR B1031     1797   1623   1360     40    -93    183  F000 C  
ATOM   1336  CG2 THR B1031       5.672   2.432  12.380  1.00 12.92      F000 C  
ANISOU 1336  CG2 THR B1031     1819   1740   1349   -110     26     95  F000 C  
ATOM   1337  OG1 THR B1031       5.841   0.619  10.770  1.00 12.89      F000 O  
ANISOU 1337  OG1 THR B1031     1698   1954   1245   -150    -67    239  F000 O  
ATOM   1338  N  AVAL B1032       7.763   4.771  10.949  0.70 12.15      F000 N  
ANISOU 1338  N  AVAL B1032     1564   1708   1344    -34    -58    271  F000 N  
ATOM   1339  N  BVAL B1032       7.710   4.760  10.956  0.30 12.39      F000 N  
ANISOU 1339  N  BVAL B1032     1617   1691   1397    -17    -78    171  F000 N  
ATOM   1340  CA AVAL B1032       8.409   5.918  11.571  0.70 13.09      F000 C  
ANISOU 1340  CA AVAL B1032     1800   1729   1443    -87    -66    191  F000 C  
ATOM   1341  CA BVAL B1032       8.344   5.981  11.445  0.30 12.68      F000 C  
ANISOU 1341  CA BVAL B1032     1706   1677   1434    -40    -74    107  F000 C  
ATOM   1342  C  AVAL B1032       7.359   6.925  12.010  0.70 12.92      F000 C  
ANISOU 1342  C  AVAL B1032     1702   1811   1393   -128   -222    163  F000 C  
ATOM   1343  C  BVAL B1032       7.263   6.878  12.034  0.30 12.96      F000 C  
ANISOU 1343  C  BVAL B1032     1688   1769   1465    -66   -135    121  F000 C  
ATOM   1344  O  AVAL B1032       6.496   7.331  11.227  0.70 12.87      F000 O  
ANISOU 1344  O  AVAL B1032     1899   1656   1333    103   -292    211  F000 O  
ATOM   1345  O  BVAL B1032       6.269   7.169  11.366  0.30 12.94      F000 O  
ANISOU 1345  O  BVAL B1032     1742   1751   1423    -60   -160    109  F000 O  
ATOM   1346  CB AVAL B1032       9.486   6.548  10.647  0.70 14.61      F000 C  
ANISOU 1346  CB AVAL B1032     1917   1871   1760   -109     14    161  F000 C  
ATOM   1347  CB BVAL B1032       9.046   6.747  10.296  0.30 12.47      F000 C  
ANISOU 1347  CB BVAL B1032     1555   1663   1518    -27    -47    129  F000 C  
ATOM   1348  CG1AVAL B1032       8.900   6.978   9.349  0.70 17.31      F000 C  
ANISOU 1348  CG1AVAL B1032     2367   2099   2110     82    -89     39  F000 C  
ATOM   1349  CG1BVAL B1032      10.036   5.836   9.583  0.30  8.66      F000 C  
ANISOU 1349  CG1BVAL B1032     1445   1048    794    -77    -27   -189  F000 C  
ATOM   1350  CG2AVAL B1032      10.196   7.709  11.321  0.70 12.28      F000 C  
ANISOU 1350  CG2AVAL B1032     1590   1541   1535   -101    -42     48  F000 C  
ATOM   1351  CG2BVAL B1032       8.026   7.303   9.302  0.30 16.38      F000 C  
ANISOU 1351  CG2BVAL B1032     2080   1923   2220     -3     51   -100  F000 C  
ATOM   1352  N   LEU B1033       7.439   7.298  13.284  1.00 13.10      F000 N  
ANISOU 1352  N   LEU B1033     1770   1819   1387     -7   -197    206  F000 N  
ATOM   1353  CA  LEU B1033       6.461   8.147  13.928  1.00 14.17      F000 C  
ANISOU 1353  CA  LEU B1033     1911   1931   1540     30   -136    117  F000 C  
ATOM   1354  C   LEU B1033       7.126   9.353  14.549  1.00 13.00      F000 C  
ANISOU 1354  C   LEU B1033     1653   1827   1458     70   -222    -10  F000 C  
ATOM   1355  O   LEU B1033       8.297   9.308  14.932  1.00 13.42      F000 O  
ANISOU 1355  O   LEU B1033     1665   1886   1546    142   -153     81  F000 O  
ATOM   1356  CB  LEU B1033       5.688   7.395  15.011  1.00 15.29      F000 C  
ANISOU 1356  CB  LEU B1033     1986   1972   1851     42    -95    -20  F000 C  
ATOM   1357  CG  LEU B1033       4.964   6.117  14.588  1.00 16.35      F000 C  
ANISOU 1357  CG  LEU B1033     2235   2067   1909   -157   -231     10  F000 C  
ATOM   1358  CD1 LEU B1033       4.344   5.488  15.813  1.00 19.71      F000 C  
ANISOU 1358  CD1 LEU B1033     2436   2506   2547   -249   -428     59  F000 C  
ATOM   1359  CD2 LEU B1033       3.916   6.397  13.543  1.00 17.79      F000 C  
ANISOU 1359  CD2 LEU B1033     2413   2034   2309   -504    -65   -171  F000 C  
ATOM   1360  N   GLU B1034       6.335  10.412  14.667  1.00 14.91      F000 N  
ANISOU 1360  N   GLU B1034     1774   2161   1730    155    -71     97  F000 N  
ATOM   1361  CA  GLU B1034       6.722  11.649  15.305  1.00 16.85      F000 C  
ANISOU 1361  CA  GLU B1034     2025   2318   2057     64     26    114  F000 C  
ATOM   1362  C   GLU B1034       7.191  11.415  16.728  1.00 16.41      F000 C  
ANISOU 1362  C   GLU B1034     1868   2348   2017     51     16     21  F000 C  
ATOM   1363  O   GLU B1034       6.868  10.402  17.339  1.00 17.10      F000 O  
ANISOU 1363  O   GLU B1034     2160   2455   1879     18    164    -63  F000 O  
ATOM   1364  CB  GLU B1034       5.502  12.580  15.338  1.00 17.83      F000 C  
ANISOU 1364  CB  GLU B1034     2141   2381   2251    176     18    214  F000 C  
ATOM   1365  CG  GLU B1034       4.347  12.010  16.172  0.50 19.16      F000 C  
ANISOU 1365  CG  GLU B1034     2419   2504   2354    173    109    118  F000 C  
ATOM   1366  CD  GLU B1034       3.146  12.936  16.274  0.50 19.80      F000 C  
ANISOU 1366  CD  GLU B1034     2427   2671   2424    175    273     84  F000 C  
ATOM   1367  OE1 GLU B1034       2.201  12.768  15.487  0.50 18.67      F000 O  
ANISOU 1367  OE1 GLU B1034     2458   2607   2027    335    950    245  F000 O  
ATOM   1368  OE2 GLU B1034       3.133  13.816  17.159  0.50 22.79      F000 O1-
ANISOU 1368  OE2 GLU B1034     3029   3057   2573    249    971    132  F000 O1-
ATOM   1369  N   GLU B1035       7.930  12.382  17.253  1.00 16.91      F000 N  
ANISOU 1369  N   GLU B1035     1922   2475   2027    -23    117     97  F000 N  
ATOM   1370  CA  GLU B1035       8.448  12.315  18.609  1.00 16.51      F000 C  
ANISOU 1370  CA  GLU B1035     1940   2275   2055     23    146     96  F000 C  
ATOM   1371  C   GLU B1035       7.394  11.880  19.622  1.00 17.05      F000 C  
ANISOU 1371  C   GLU B1035     2094   2276   2107    135    249     85  F000 C  
ATOM   1372  O   GLU B1035       6.280  12.416  19.669  1.00 17.38      F000 O  
ANISOU 1372  O   GLU B1035     2200   2234   2169    344    292    145  F000 O  
ATOM   1373  CB  GLU B1035       9.061  13.657  19.019  1.00 18.17      F000 C  
ANISOU 1373  CB  GLU B1035     1989   2481   2432     23    225     35  F000 C  
ATOM   1374  CG  GLU B1035       9.745  13.614  20.373  1.00 19.28      F000 C  
ANISOU 1374  CG  GLU B1035     2130   2810   2384    -88    307     -8  F000 C  
ATOM   1375  CD  GLU B1035      10.790  12.521  20.447  1.00 20.88      F000 C  
ANISOU 1375  CD  GLU B1035     2598   2834   2500   -156    206    192  F000 C  
ATOM   1376  OE1 GLU B1035      11.678  12.494  19.575  1.00 19.60      F000 O  
ANISOU 1376  OE1 GLU B1035     2378   2552   2518   -257    797   -363  F000 O  
ATOM   1377  OE2 GLU B1035      10.723  11.676  21.362  1.00 22.20      F000 O1-
ANISOU 1377  OE2 GLU B1035     2263   3511   2659    -55    286    -71  F000 O1-
ATOM   1378  N  AMET B1036       7.766  10.902  20.437  0.50 15.39      F000 N  
ANISOU 1378  N  AMET B1036     1943   2118   1784    153    135    -28  F000 N  
ATOM   1379  N  BMET B1036       7.761  10.890  20.426  0.50 15.52      F000 N  
ANISOU 1379  N  BMET B1036     1955   2124   1816    166    127    -32  F000 N  
ATOM   1380  CA AMET B1036       6.914  10.399  21.504  0.50 15.77      F000 C  
ANISOU 1380  CA AMET B1036     2004   2103   1883     52    109     38  F000 C  
ATOM   1381  CA BMET B1036       6.906  10.355  21.477  0.50 15.82      F000 C  
ANISOU 1381  CA BMET B1036     1967   2120   1921     85    114     10  F000 C  
ATOM   1382  C  AMET B1036       7.750   9.513  22.416  0.50 15.62      F000 C  
ANISOU 1382  C  AMET B1036     2079   2051   1803     53    154     -2  F000 C  
ATOM   1383  C  BMET B1036       7.791   9.604  22.459  0.50 15.79      F000 C  
ANISOU 1383  C  BMET B1036     2072   2072   1853     89    142    -21  F000 C  
ATOM   1384  O  AMET B1036       8.840   9.081  22.043  0.50 15.37      F000 O  
ANISOU 1384  O  AMET B1036     2255   2012   1572    164    268    127  F000 O  
ATOM   1385  O  BMET B1036       8.970   9.378  22.186  0.50 16.48      F000 O  
ANISOU 1385  O  BMET B1036     2287   2177   1798    278    212      8  F000 O  
ATOM   1386  CB AMET B1036       5.748   9.602  20.924  0.50 14.90      F000 C  
ANISOU 1386  CB AMET B1036     1953   2093   1615      7    139    -40  F000 C  
ATOM   1387  CB BMET B1036       5.858   9.413  20.888  0.50 15.17      F000 C  
ANISOU 1387  CB BMET B1036     1997   2069   1696     65    113    -63  F000 C  
ATOM   1388  CG AMET B1036       6.157   8.306  20.244  0.50 14.19      F000 C  
ANISOU 1388  CG AMET B1036     1753   2026   1612     50     76     27  F000 C  
ATOM   1389  CG BMET B1036       6.442   8.222  20.145  0.50 14.78      F000 C  
ANISOU 1389  CG BMET B1036     1695   2230   1691    124     81     92  F000 C  
ATOM   1390  SD AMET B1036       4.743   7.331  19.705  0.50 17.44      F000 S  
ANISOU 1390  SD AMET B1036     2237   2328   2060    -75    -52    191  F000 S  
ATOM   1391  SD BMET B1036       5.191   7.078  19.521  0.50 16.00      F000 S  
ANISOU 1391  SD BMET B1036     1778   2284   2014     80     72    -28  F000 S  
ATOM   1392  CE AMET B1036       3.994   6.954  21.288  0.50 18.73      F000 C  
ANISOU 1392  CE AMET B1036     2282   2393   2441   -157     52    128  F000 C  
ATOM   1393  CE BMET B1036       4.289   8.130  18.388  0.50 18.31      F000 C  
ANISOU 1393  CE BMET B1036     1867   2685   2405     65     91   -121  F000 C  
ATOM   1394  N   ASN B1037       7.224   9.225  23.600  1.00 15.55      F000 N  
ANISOU 1394  N   ASN B1037     2082   2093   1731    114    245    -48  F000 N  
ATOM   1395  CA  ASN B1037       7.929   8.412  24.570  1.00 15.44      F000 C  
ANISOU 1395  CA  ASN B1037     1989   2060   1817    133    201   -103  F000 C  
ATOM   1396  C   ASN B1037       7.554   6.945  24.397  1.00 15.31      F000 C  
ANISOU 1396  C   ASN B1037     1938   1927   1949     97    289    -70  F000 C  
ATOM   1397  O   ASN B1037       6.369   6.594  24.430  1.00 17.25      F000 O  
ANISOU 1397  O   ASN B1037     2054   1896   2601    139    535   -118  F000 O  
ATOM   1398  CB  ASN B1037       7.575   8.862  25.987  1.00 16.89      F000 C  
ANISOU 1398  CB  ASN B1037     2271   2219   1927     -8    205   -142  F000 C  
ATOM   1399  CG  ASN B1037       8.069  10.246  26.297  1.00 20.61      F000 C  
ANISOU 1399  CG  ASN B1037     2582   2919   2329    103    562   -313  F000 C  
ATOM   1400  ND2 ASN B1037       7.347  10.948  27.165  1.00 28.24      F000 N  
ANISOU 1400  ND2 ASN B1037     3638   3687   3405   -123   1217   -417  F000 N  
ATOM   1401  OD1 ASN B1037       9.088  10.691  25.763  1.00 22.41      F000 O  
ANISOU 1401  OD1 ASN B1037     2635   3404   2473   -544    751   -190  F000 O  
ATOM   1402  N   LEU B1038       8.560   6.097  24.204  1.00 13.89      F000 N  
ANISOU 1402  N   LEU B1038     1945   1916   1417    167     98     19  F000 N  
ATOM   1403  CA  LEU B1038       8.358   4.661  24.159  1.00 14.04      F000 C  
ANISOU 1403  CA  LEU B1038     2034   1825   1475    157     34     41  F000 C  
ATOM   1404  C   LEU B1038       9.306   3.963  25.121  1.00 13.84      F000 C  
ANISOU 1404  C   LEU B1038     1984   1867   1406    166    -28      9  F000 C  
ATOM   1405  O   LEU B1038      10.394   4.466  25.399  1.00 14.86      F000 O  
ANISOU 1405  O   LEU B1038     2164   2040   1440    136     51     56  F000 O  
ATOM   1406  CB  LEU B1038       8.592   4.131  22.746  1.00 13.06      F000 C  
ANISOU 1406  CB  LEU B1038     1762   1795   1406    135     48   -181  F000 C  
ATOM   1407  CG  LEU B1038       7.597   4.577  21.678  1.00 12.27      F000 C  
ANISOU 1407  CG  LEU B1038     1531   1689   1441     41     -7    -71  F000 C  
ATOM   1408  CD1 LEU B1038       8.010   3.971  20.349  1.00 13.35      F000 C  
ANISOU 1408  CD1 LEU B1038     1649   2050   1372      3    -56   -136  F000 C  
ATOM   1409  CD2 LEU B1038       6.188   4.179  22.024  1.00 14.19      F000 C  
ANISOU 1409  CD2 LEU B1038     1927   1984   1478    187    175    120  F000 C  
ATOM   1410  N   PRO B1039       8.886   2.794  25.616  1.00 14.62      F000 N  
ANISOU 1410  N   PRO B1039     2069   1915   1567    227   -103     80  F000 N  
ATOM   1411  CA  PRO B1039       9.687   2.040  26.562  1.00 14.78      F000 C  
ANISOU 1411  CA  PRO B1039     2077   1972   1567    209    -80     67  F000 C  
ATOM   1412  C   PRO B1039      10.817   1.252  25.930  1.00 13.75      F000 C  
ANISOU 1412  C   PRO B1039     2053   1834   1334    229   -115    114  F000 C  
ATOM   1413  O   PRO B1039      10.741   0.868  24.754  1.00 14.73      F000 O  
ANISOU 1413  O   PRO B1039     2182   2035   1378    167    -96     39  F000 O  
ATOM   1414  CB  PRO B1039       8.666   1.097  27.185  1.00 15.80      F000 C  
ANISOU 1414  CB  PRO B1039     2042   2179   1781    204   -114     27  F000 C  
ATOM   1415  CG  PRO B1039       7.707   0.832  26.094  1.00 16.13      F000 C  
ANISOU 1415  CG  PRO B1039     2306   1718   2104     17   -196   -131  F000 C  
ATOM   1416  CD  PRO B1039       7.603   2.129  25.339  1.00 15.67      F000 C  
ANISOU 1416  CD  PRO B1039     2145   2002   1806    127   -186     -7  F000 C  
ATOM   1417  N   GLY B1040      11.845   0.978  26.734  1.00 13.77      F000 N  
ANISOU 1417  N   GLY B1040     2002   1839   1391    164   -107     24  F000 N  
ATOM   1418  CA  GLY B1040      12.885   0.050  26.335  1.00 14.59      F000 C  
ANISOU 1418  CA  GLY B1040     2034   1927   1581     31   -134      8  F000 C  
ATOM   1419  C   GLY B1040      14.143   0.749  25.860  1.00 14.67      F000 C  
ANISOU 1419  C   GLY B1040     2114   1993   1464    -44   -181     15  F000 C  
ATOM   1420  O   GLY B1040      14.262   1.984  25.887  1.00 15.96      F000 O  
ANISOU 1420  O   GLY B1040     2412   2097   1555     51   -130   -191  F000 O  
ATOM   1421  N   ARG B1041      15.078  -0.074  25.424  1.00 14.99      F000 N  
ANISOU 1421  N   ARG B1041     1982   2143   1567     70   -260    -94  F000 N  
ATOM   1422  CA  ARG B1041      16.367   0.386  24.942  1.00 15.46      F000 C  
ANISOU 1422  CA  ARG B1041     2081   2241   1551   -107   -209    -50  F000 C  
ATOM   1423  C   ARG B1041      16.225   0.778  23.490  1.00 16.10      F000 C  
ANISOU 1423  C   ARG B1041     2151   2532   1431   -461   -107     95  F000 C  
ATOM   1424  O   ARG B1041      15.689   0.031  22.699  1.00 21.70      F000 O  
ANISOU 1424  O   ARG B1041     2699   4093   1452  -1055   -101   -119  F000 O  
ATOM   1425  CB  ARG B1041      17.394  -0.741  25.071  1.00 17.13      F000 C  
ANISOU 1425  CB  ARG B1041     2233   2465   1809    -36   -260   -124  F000 C  
ATOM   1426  CG  ARG B1041      18.819  -0.325  24.765  1.00 20.09      F000 C  
ANISOU 1426  CG  ARG B1041     2661   2594   2377    126   -204   -266  F000 C  
ATOM   1427  CD  ARG B1041      19.768  -1.514  24.795  1.00 23.32      F000 C  
ANISOU 1427  CD  ARG B1041     3046   2972   2841    110   -162   -266  F000 C  
ATOM   1428  NE  ARG B1041      19.735  -2.229  26.069  0.75 28.06      F000 N  
ANISOU 1428  NE  ARG B1041     3491   3359   3811    374    -80   -207  F000 N  
ATOM   1429  CZ  ARG B1041      19.121  -3.393  26.279  0.75 26.08      F000 C  
ANISOU 1429  CZ  ARG B1041     3350   3052   3507    144     -3   -187  F000 C  
ATOM   1430  NH1 ARG B1041      18.470  -4.023  25.300  0.75 28.15      F000 N1+
ANISOU 1430  NH1 ARG B1041     3471   3273   3951    145   -398   -257  F000 N1+
ATOM   1431  NH2 ARG B1041      19.168  -3.936  27.480  0.75 28.99      F000 N  
ANISOU 1431  NH2 ARG B1041     3930   3221   3864    159     78    -89  F000 N  
ATOM   1432  N   TRP B1042      16.696   1.949  23.141  1.00 15.19      F000 N  
ANISOU 1432  N   TRP B1042     2126   2329   1313   -249    -16     11  F000 N  
ATOM   1433  CA  TRP B1042      16.695   2.333  21.750  1.00 14.01      F000 C  
ANISOU 1433  CA  TRP B1042     1878   2045   1400   -231   -139     38  F000 C  
ATOM   1434  C   TRP B1042      18.129   2.488  21.286  1.00 14.54      F000 C  
ANISOU 1434  C   TRP B1042     2107   1937   1478    -53   -135     92  F000 C  
ATOM   1435  O   TRP B1042      19.068   2.566  22.100  1.00 14.57      F000 O  
ANISOU 1435  O   TRP B1042     2287   1791   1456   -125   -143    114  F000 O  
ATOM   1436  CB  TRP B1042      15.924   3.633  21.538  1.00 14.55      F000 C  
ANISOU 1436  CB  TRP B1042     1975   1959   1591   -157    -71     72  F000 C  
ATOM   1437  CG  TRP B1042      16.444   4.771  22.359  1.00 15.07      F000 C  
ANISOU 1437  CG  TRP B1042     2079   2034   1612    -94   -127    -74  F000 C  
ATOM   1438  CD1 TRP B1042      16.051   5.108  23.613  1.00 17.13      F000 C  
ANISOU 1438  CD1 TRP B1042     2282   2476   1750   -245   -113   -109  F000 C  
ATOM   1439  CD2 TRP B1042      17.448   5.719  21.983  1.00 14.60      F000 C  
ANISOU 1439  CD2 TRP B1042     1812   2030   1705   -120    110    114  F000 C  
ATOM   1440  CE2 TRP B1042      17.604   6.612  23.062  1.00 16.37      F000 C  
ANISOU 1440  CE2 TRP B1042     1995   2273   1950   -459     59     43  F000 C  
ATOM   1441  CE3 TRP B1042      18.212   5.920  20.827  1.00 14.81      F000 C  
ANISOU 1441  CE3 TRP B1042     1975   1897   1756    -66   -140    -96  F000 C  
ATOM   1442  NE1 TRP B1042      16.748   6.209  24.049  1.00 18.65      F000 N  
ANISOU 1442  NE1 TRP B1042     2532   2610   1944   -286    139    -99  F000 N  
ATOM   1443  CZ2 TRP B1042      18.506   7.670  23.035  1.00 16.81      F000 C  
ANISOU 1443  CZ2 TRP B1042     2174   2385   1828   -297     68    208  F000 C  
ATOM   1444  CZ3 TRP B1042      19.108   6.971  20.802  1.00 17.08      F000 C  
ANISOU 1444  CZ3 TRP B1042     2187   2358   1944   -178     70   -109  F000 C  
ATOM   1445  CH2 TRP B1042      19.246   7.834  21.902  1.00 16.90      F000 C  
ANISOU 1445  CH2 TRP B1042     2300   2020   2099   -402    -58    -28  F000 C  
ATOM   1446  N   LYS B1043      18.293   2.543  19.971  1.00 13.87      F000 N  
ANISOU 1446  N   LYS B1043     2127   1863   1280    -29   -214    132  F000 N  
ATOM   1447  CA  LYS B1043      19.580   2.879  19.388  1.00 15.27      F000 C  
ANISOU 1447  CA  LYS B1043     2146   2049   1606    -61    -85     45  F000 C  
ATOM   1448  C   LYS B1043      19.325   3.778  18.198  1.00 15.23      F000 C  
ANISOU 1448  C   LYS B1043     2247   2054   1483    -99   -205    -43  F000 C  
ATOM   1449  O   LYS B1043      18.277   3.681  17.578  1.00 14.15      F000 O  
ANISOU 1449  O   LYS B1043     2096   1764   1514   -160   -220    -45  F000 O  
ATOM   1450  CB  LYS B1043      20.329   1.615  18.959  1.00 17.09      F000 C  
ANISOU 1450  CB  LYS B1043     2378   2239   1873    -13   -182     64  F000 C  
ATOM   1451  CG  LYS B1043      19.613   0.786  17.919  1.00 19.15      F000 C  
ANISOU 1451  CG  LYS B1043     2400   2535   2341     93    -34    -53  F000 C  
ATOM   1452  CD  LYS B1043      20.383  -0.476  17.574  1.00 21.58      F000 C  
ANISOU 1452  CD  LYS B1043     2796   2812   2590    149     -4    -11  F000 C  
ATOM   1453  CE  LYS B1043      19.555  -1.401  16.688  1.00 24.21      F000 C  
ANISOU 1453  CE  LYS B1043     3064   3094   3041    355    266     15  F000 C  
ATOM   1454  NZ  LYS B1043      20.302  -2.628  16.291  1.00 27.18      F000 N1+
ANISOU 1454  NZ  LYS B1043     3234   3529   3562    205    505   -217  F000 N1+
ATOM   1455  N   PRO B1044      20.271   4.672  17.889  1.00 15.32      F000 N  
ANISOU 1455  N   PRO B1044     2250   1908   1661    -15   -228    129  F000 N  
ATOM   1456  CA  PRO B1044      20.056   5.520  16.725  1.00 15.44      F000 C  
ANISOU 1456  CA  PRO B1044     2119   2109   1637      1   -191    -58  F000 C  
ATOM   1457  C   PRO B1044      20.127   4.709  15.432  1.00 17.59      F000 C  
ANISOU 1457  C   PRO B1044     2346   2431   1906    156   -124   -279  F000 C  
ATOM   1458  O   PRO B1044      20.847   3.715  15.351  1.00 19.24      F000 O  
ANISOU 1458  O   PRO B1044     2629   2765   1916    358   -559   -394  F000 O  
ATOM   1459  CB  PRO B1044      21.196   6.537  16.816  1.00 17.63      F000 C  
ANISOU 1459  CB  PRO B1044     2332   2272   2092    -64   -252   -143  F000 C  
ATOM   1460  CG  PRO B1044      22.215   5.915  17.652  1.00 17.69      F000 C  
ANISOU 1460  CG  PRO B1044     2558   2143   2018   -277    -89   -187  F000 C  
ATOM   1461  CD  PRO B1044      21.529   4.986  18.585  1.00 16.48      F000 C  
ANISOU 1461  CD  PRO B1044     2356   2021   1885    -68   -182     68  F000 C  
ATOM   1462  N   LYS B1045      19.365   5.139  14.437  1.00 16.40      F000 N  
ANISOU 1462  N   LYS B1045     2112   2341   1776    159   -172   -123  F000 N  
ATOM   1463  CA  LYS B1045      19.346   4.500  13.113  1.00 16.50      F000 C  
ANISOU 1463  CA  LYS B1045     2121   2365   1782    128    -77   -178  F000 C  
ATOM   1464  C   LYS B1045      19.304   5.614  12.076  1.00 15.64      F000 C  
ANISOU 1464  C   LYS B1045     1997   2277   1668    168   -143   -222  F000 C  
ATOM   1465  O   LYS B1045      18.572   6.574  12.245  1.00 15.12      F000 O  
ANISOU 1465  O   LYS B1045     1780   2529   1434    110    -65   -510  F000 O  
ATOM   1466  CB  LYS B1045      18.111   3.606  12.944  1.00 17.25      F000 C  
ANISOU 1466  CB  LYS B1045     2124   2565   1863    263   -167   -164  F000 C  
ATOM   1467  CG  LYS B1045      18.073   2.801  11.635  1.00 18.22      F000 C  
ANISOU 1467  CG  LYS B1045     2372   2417   2132    -99   -144    -65  F000 C  
ATOM   1468  CD  LYS B1045      16.738   2.038  11.453  1.00 21.10      F000 C  
ANISOU 1468  CD  LYS B1045     2590   2847   2578      2     90   -134  F000 C  
ATOM   1469  CE  LYS B1045      16.730   1.155  10.209  1.00 24.19      F000 C  
ANISOU 1469  CE  LYS B1045     3158   3261   2772    190   -139     -3  F000 C  
ATOM   1470  NZ  LYS B1045      17.921   0.267  10.141  1.00 31.39      F000 N1+
ANISOU 1470  NZ  LYS B1045     3530   4435   3962    137     88   -146  F000 N1+
ATOM   1471  N   MET B1046      20.101   5.490  11.018  1.00 16.00      F000 N  
ANISOU 1471  N   MET B1046     2011   2479   1587    247   -241   -331  F000 N  
ATOM   1472  CA  MET B1046      20.051   6.432   9.906  1.00 15.48      F000 C  
ANISOU 1472  CA  MET B1046     1851   2272   1758    189    -60   -204  F000 C  
ATOM   1473  C   MET B1046      19.141   5.869   8.841  1.00 14.46      F000 C  
ANISOU 1473  C   MET B1046     1651   2280   1560    261    -36   -274  F000 C  
ATOM   1474  O   MET B1046      19.329   4.739   8.377  1.00 19.42      F000 O  
ANISOU 1474  O   MET B1046     1787   3334   2255    477    251    -98  F000 O  
ATOM   1475  CB  MET B1046      21.450   6.674   9.338  1.00 16.31      F000 C  
ANISOU 1475  CB  MET B1046     1963   2329   1902    227   -243   -385  F000 C  
ATOM   1476  CG  MET B1046      22.467   7.174  10.346  1.00 17.75      F000 C  
ANISOU 1476  CG  MET B1046     2421   2363   1958    314   -175   -424  F000 C  
ATOM   1477  SD  MET B1046      21.994   8.662  11.261  1.00 19.69      F000 S  
ANISOU 1477  SD  MET B1046     3267   2441   1773     65   -186   -269  F000 S  
ATOM   1478  CE  MET B1046      21.836   9.848   9.945  1.00 19.17      F000 C  
ANISOU 1478  CE  MET B1046     3129   2489   1664    139     63   -199  F000 C  
ATOM   1479  N   ILE B1047      18.122   6.632   8.482  1.00 14.00      F000 N  
ANISOU 1479  N   ILE B1047     1604   2339   1374    155     93   -313  F000 N  
ATOM   1480  CA  ILE B1047      17.189   6.203   7.459  1.00 14.40      F000 C  
ANISOU 1480  CA  ILE B1047     1816   2233   1421    -19    123   -197  F000 C  
ATOM   1481  C   ILE B1047      17.149   7.178   6.303  1.00 13.96      F000 C  
ANISOU 1481  C   ILE B1047     1789   2203   1313   -147    183   -253  F000 C  
ATOM   1482  O   ILE B1047      17.663   8.275   6.372  1.00 14.63      F000 O  
ANISOU 1482  O   ILE B1047     1891   2625   1042    -59    314   -330  F000 O  
ATOM   1483  CB  ILE B1047      15.766   5.971   8.008  1.00 14.32      F000 C  
ANISOU 1483  CB  ILE B1047     1843   2207   1389   -217     17   -173  F000 C  
ATOM   1484  CG1 ILE B1047      15.159   7.255   8.559  1.00 15.43      F000 C  
ANISOU 1484  CG1 ILE B1047     2175   2311   1377   -118     81   -305  F000 C  
ATOM   1485  CG2 ILE B1047      15.769   4.853   9.049  1.00 18.08      F000 C  
ANISOU 1485  CG2 ILE B1047     2020   2876   1972    -55     70   -342  F000 C  
ATOM   1486  CD1 ILE B1047      13.683   7.143   8.920  1.00 16.46      F000 C  
ANISOU 1486  CD1 ILE B1047     2298   2561   1392   -153    133   -174  F000 C  
ATOM   1487  N   GLY B1048      16.529   6.749   5.219  1.00 14.44      F000 N  
ANISOU 1487  N   GLY B1048     1873   2306   1306   -241    233      6  F000 N  
ATOM   1488  CA  GLY B1048      16.455   7.570   4.033  1.00 15.18      F000 C  
ANISOU 1488  CA  GLY B1048     2145   2119   1501    -86     92   -168  F000 C  
ATOM   1489  C   GLY B1048      17.573   7.185   3.093  1.00 15.22      F000 C  
ANISOU 1489  C   GLY B1048     2137   2002   1642    -90    196   -146  F000 C  
ATOM   1490  O   GLY B1048      17.670   6.028   2.691  1.00 19.87      F000 O  
ANISOU 1490  O   GLY B1048     2638   2704   2205   -144    395   -836  F000 O  
ATOM   1491  N   GLY B1049      18.405   8.156   2.740  1.00 14.62      F000 N  
ANISOU 1491  N   GLY B1049     2023   1997   1534    -28    -33   -140  F000 N  
ATOM   1492  CA  GLY B1049      19.557   7.912   1.879  1.00 14.81      F000 C  
ANISOU 1492  CA  GLY B1049     2169   1860   1596     79   -135    -65  F000 C  
ATOM   1493  C   GLY B1049      19.467   8.655   0.557  1.00 15.07      F000 C  
ANISOU 1493  C   GLY B1049     2339   1904   1482     79   -245    -93  F000 C  
ATOM   1494  O   GLY B1049      20.482   8.983  -0.047  1.00 16.24      F000 O  
ANISOU 1494  O   GLY B1049     2645   1769   1753    179   -486   -325  F000 O  
ATOM   1495  N   ILE B1050      18.248   8.909   0.092  1.00 15.58      F000 N  
ANISOU 1495  N   ILE B1050     2534   1826   1558     46   -245   -207  F000 N  
ATOM   1496  CA  ILE B1050      18.059   9.597  -1.187  1.00 16.35      F000 C  
ANISOU 1496  CA  ILE B1050     2370   2042   1800      0   -144    -43  F000 C  
ATOM   1497  C   ILE B1050      18.109  11.097  -0.934  1.00 16.38      F000 C  
ANISOU 1497  C   ILE B1050     2496   2026   1701     46   -130    -20  F000 C  
ATOM   1498  O   ILE B1050      17.124  11.712  -0.520  1.00 19.61      F000 O  
ANISOU 1498  O   ILE B1050     2860   2227   2361     68     50   -124  F000 O  
ATOM   1499  CB  ILE B1050      16.716   9.215  -1.845  1.00 18.50      F000 C  
ANISOU 1499  CB  ILE B1050     2636   2343   2048      7    -77   -126  F000 C  
ATOM   1500  CG1 ILE B1050      16.580   7.698  -1.962  1.00 20.74      F000 C  
ANISOU 1500  CG1 ILE B1050     2924   2384   2572     12    -75     84  F000 C  
ATOM   1501  CG2 ILE B1050      16.591   9.850  -3.211  1.00 18.00      F000 C  
ANISOU 1501  CG2 ILE B1050     2790   2145   1901     48   -156    224  F000 C  
ATOM   1502  CD1 ILE B1050      15.252   7.245  -2.578  0.50 19.57      F000 C  
ANISOU 1502  CD1 ILE B1050     2735   2321   2377    -25    -18    165  F000 C  
ATOM   1503  N   GLY B1051      19.279  11.677  -1.144  1.00 15.03      F000 N  
ANISOU 1503  N   GLY B1051     2286   1880   1544     66   -177    135  F000 N  
ATOM   1504  CA  GLY B1051      19.505  13.079  -0.826  1.00 14.65      F000 C  
ANISOU 1504  CA  GLY B1051     1961   1893   1712      1    -94    -13  F000 C  
ATOM   1505  C   GLY B1051      20.217  13.293   0.497  1.00 13.25      F000 C  
ANISOU 1505  C   GLY B1051     1783   1631   1619    127   -191   -144  F000 C  
ATOM   1506  O   GLY B1051      20.653  14.395   0.810  1.00 14.34      F000 O  
ANISOU 1506  O   GLY B1051     1810   1919   1717    211   -341    -91  F000 O  
ATOM   1507  N   GLY B1052      20.332  12.235   1.287  1.00 12.12      F000 N  
ANISOU 1507  N   GLY B1052     1635   1775   1193    211   -154   -146  F000 N  
ATOM   1508  CA  GLY B1052      20.865  12.365   2.636  1.00 12.53      F000 C  
ANISOU 1508  CA  GLY B1052     1758   1630   1370     95    -81    -68  F000 C  
ATOM   1509  C   GLY B1052      20.145  11.437   3.582  1.00 11.85      F000 C  
ANISOU 1509  C   GLY B1052     1475   1730   1297     50    -11   -127  F000 C  
ATOM   1510  O   GLY B1052      19.208  10.749   3.186  1.00 13.34      F000 O  
ANISOU 1510  O   GLY B1052     1966   1787   1314    124   -193   -155  F000 O  
ATOM   1511  N   PHE B1053      20.600  11.402   4.830  1.00 12.06      F000 N  
ANISOU 1511  N   PHE B1053     1492   1895   1194    -10     76   -289  F000 N  
ATOM   1512  CA  PHE B1053      20.013  10.529   5.840  1.00 11.96      F000 C  
ANISOU 1512  CA  PHE B1053     1537   1832   1176     44    104    -99  F000 C  
ATOM   1513  C   PHE B1053      19.443  11.335   6.977  1.00 11.96      F000 C  
ANISOU 1513  C   PHE B1053     1439   1820   1286     70     79   -178  F000 C  
ATOM   1514  O   PHE B1053      19.902  12.431   7.269  1.00 12.05      F000 O  
ANISOU 1514  O   PHE B1053     1594   1868   1116    -60     68   -320  F000 O  
ATOM   1515  CB  PHE B1053      21.051   9.575   6.420  1.00 12.90      F000 C  
ANISOU 1515  CB  PHE B1053     1643   2040   1217    214     96   -204  F000 C  
ATOM   1516  CG  PHE B1053      21.565   8.561   5.443  1.00 15.25      F000 C  
ANISOU 1516  CG  PHE B1053     1827   2485   1480    490   -225     22  F000 C  
ATOM   1517  CD1 PHE B1053      22.727   8.793   4.738  1.00 15.40      F000 C  
ANISOU 1517  CD1 PHE B1053     1777   2436   1639    554    -39   -246  F000 C  
ATOM   1518  CD2 PHE B1053      20.897   7.367   5.258  1.00 15.02      F000 C  
ANISOU 1518  CD2 PHE B1053     1869   2322   1515    607    458   -177  F000 C  
ATOM   1519  CE1 PHE B1053      23.214   7.847   3.847  1.00 16.34      F000 C  
ANISOU 1519  CE1 PHE B1053     2018   2530   1659    617    -91   -322  F000 C  
ATOM   1520  CE2 PHE B1053      21.381   6.419   4.370  1.00 17.08      F000 C  
ANISOU 1520  CE2 PHE B1053     1856   2609   2025    585    144    178  F000 C  
ATOM   1521  CZ  PHE B1053      22.531   6.670   3.667  1.00 16.25      F000 C  
ANISOU 1521  CZ  PHE B1053     1956   2533   1682    855    186     88  F000 C  
ATOM   1522  N   ILE B1054      18.491  10.729   7.666  1.00 12.40      F000 N  
ANISOU 1522  N   ILE B1054     1579   1935   1194     -9    130   -251  F000 N  
ATOM   1523  CA  ILE B1054      17.850  11.303   8.840  1.00 12.20      F000 C  
ANISOU 1523  CA  ILE B1054     1479   1914   1240     21     31   -166  F000 C  
ATOM   1524  C   ILE B1054      18.107  10.316   9.989  1.00 11.71      F000 C  
ANISOU 1524  C   ILE B1054     1367   1865   1214    -35     78   -233  F000 C  
ATOM   1525  O   ILE B1054      18.005   9.167   9.833  1.00 12.09      F000 O  
ANISOU 1525  O   ILE B1054     1309   2167   1117    141      9   -326  F000 O  
ATOM   1526  CB  ILE B1054      16.333  11.412   8.609  1.00 14.16      F000 C  
ANISOU 1526  CB  ILE B1054     1636   2170   1573     44   -114   -138  F000 C  
ATOM   1527  CG1 ILE B1054      15.991  12.186   7.339  1.00 14.38      F000 C  
ANISOU 1527  CG1 ILE B1054     1739   1992   1729    -53    119   -147  F000 C  
ATOM   1528  CG2 ILE B1054      15.639  11.968   9.774  1.00 14.52      F000 C  
ANISOU 1528  CG2 ILE B1054     1782   2134   1598      3    -51   -193  F000 C  
ATOM   1529  CD1 ILE B1054      16.353  13.410   7.443  1.00 16.41      F000 C  
ANISOU 1529  CD1 ILE B1054     2061   2197   1973    -54     -9   -148  F000 C  
ATOM   1530  N   LYS B1055      18.461  10.857  11.137  1.00 12.26      F000 N  
ANISOU 1530  N   LYS B1055     1406   2095   1157   -152     14   -211  F000 N  
ATOM   1531  CA  LYS B1055      18.636  10.032  12.325  1.00 12.62      F000 C  
ANISOU 1531  CA  LYS B1055     1583   1995   1215    -98     65   -206  F000 C  
ATOM   1532  C   LYS B1055      17.326   9.918  13.089  1.00 11.83      F000 C  
ANISOU 1532  C   LYS B1055     1381   1928   1183   -196    142   -242  F000 C  
ATOM   1533  O   LYS B1055      16.623  10.911  13.309  1.00 13.01      F000 O  
ANISOU 1533  O   LYS B1055     1462   2295   1186   -237    208   -403  F000 O  
ATOM   1534  CB  LYS B1055      19.724  10.621  13.227  1.00 13.82      F000 C  
ANISOU 1534  CB  LYS B1055     1931   2000   1319   -183     33   -208  F000 C  
ATOM   1535  CG  LYS B1055      20.151   9.733  14.370  1.00 13.71      F000 C  
ANISOU 1535  CG  LYS B1055     1680   2220   1309   -284    -16     -5  F000 C  
ATOM   1536  CD  LYS B1055      21.145  10.423  15.319  1.00 14.79      F000 C  
ANISOU 1536  CD  LYS B1055     2282   1948   1388   -348   -107    -34  F000 C  
ATOM   1537  CE  LYS B1055      22.474  10.721  14.651  1.00 18.80      F000 C  
ANISOU 1537  CE  LYS B1055     2584   2667   1889   -490    -41     -7  F000 C  
ATOM   1538  NZ  LYS B1055      23.344  11.497  15.579  1.00 22.34      F000 N1+
ANISOU 1538  NZ  LYS B1055     2704   3008   2776   -329    582    419  F000 N1+
ATOM   1539  N   VAL B1056      17.013   8.685  13.480  1.00 11.76      F000 N  
ANISOU 1539  N   VAL B1056     1299   1975   1194   -128    100   -227  F000 N  
ATOM   1540  CA  VAL B1056      15.821   8.383  14.264  1.00 11.17      F000 C  
ANISOU 1540  CA  VAL B1056     1361   1795   1088   -266    117   -166  F000 C  
ATOM   1541  C   VAL B1056      16.233   7.428  15.390  1.00 12.18      F000 C  
ANISOU 1541  C   VAL B1056     1530   1909   1188   -192    175    -82  F000 C  
ATOM   1542  O   VAL B1056      17.349   6.913  15.392  1.00 12.49      F000 O  
ANISOU 1542  O   VAL B1056     1610   2004   1129   -166     24   -125  F000 O  
ATOM   1543  CB  VAL B1056      14.694   7.743  13.388  1.00 12.04      F000 C  
ANISOU 1543  CB  VAL B1056     1472   1860   1240   -164     45   -155  F000 C  
ATOM   1544  CG1 VAL B1056      14.250   8.715  12.332  1.00 14.73      F000 C  
ANISOU 1544  CG1 VAL B1056     2008   2425   1160   -169   -120      6  F000 C  
ATOM   1545  CG2 VAL B1056      15.151   6.431  12.765  1.00 13.74      F000 C  
ANISOU 1545  CG2 VAL B1056     1787   2129   1305   -324    140    -98  F000 C  
ATOM   1546  N   ARG B1057      15.342   7.203  16.351  1.00 11.01      F000 N  
ANISOU 1546  N   ARG B1057     1447   1624   1109    -71     98    -54  F000 N  
ATOM   1547  CA  ARG B1057      15.593   6.234  17.411  1.00 11.27      F000 C  
ANISOU 1547  CA  ARG B1057     1431   1677   1174   -120     95    -34  F000 C  
ATOM   1548  C   ARG B1057      14.818   4.957  17.125  1.00 11.28      F000 C  
ANISOU 1548  C   ARG B1057     1434   1729   1123    -92     66    -69  F000 C  
ATOM   1549  O   ARG B1057      13.615   5.007  16.876  1.00 11.56      F000 O  
ANISOU 1549  O   ARG B1057     1491   1607   1292    -66    190     72  F000 O  
ATOM   1550  CB  ARG B1057      15.111   6.799  18.737  1.00 11.64      F000 C  
ANISOU 1550  CB  ARG B1057     1632   1778   1013     -7     27   -145  F000 C  
ATOM   1551  CG  ARG B1057      15.750   8.116  19.105  1.00 12.94      F000 C  
ANISOU 1551  CG  ARG B1057     1817   1977   1123    110    234   -183  F000 C  
ATOM   1552  CD  ARG B1057      15.592   8.470  20.575  1.00 13.76      F000 C  
ANISOU 1552  CD  ARG B1057     1695   2006   1526   -160    213   -120  F000 C  
ATOM   1553  NE  ARG B1057      14.228   8.387  21.076  1.00 14.22      F000 N  
ANISOU 1553  NE  ARG B1057     1755   2315   1332   -114    468     82  F000 N  
ATOM   1554  CZ  ARG B1057      13.280   9.286  20.848  1.00 14.78      F000 C  
ANISOU 1554  CZ  ARG B1057     1760   2122   1732   -245    342   -349  F000 C  
ATOM   1555  NH1 ARG B1057      13.526  10.325  20.074  1.00 15.12      F000 N1+
ANISOU 1555  NH1 ARG B1057     1568   2304   1872   -402    118    232  F000 N1+
ATOM   1556  NH2 ARG B1057      12.075   9.137  21.383  1.00 17.44      F000 N  
ANISOU 1556  NH2 ARG B1057     2154   2296   2173     16    256   -148  F000 N  
ATOM   1557  N   GLN B1058      15.507   3.825  17.165  1.00 10.96      F000 N  
ANISOU 1557  N   GLN B1058     1438   1468   1256    -71    114      9  F000 N  
ATOM   1558  CA  GLN B1058      14.883   2.539  16.918  1.00 11.38      F000 C  
ANISOU 1558  CA  GLN B1058     1408   1699   1216    -54    -76     17  F000 C  
ATOM   1559  C   GLN B1058      14.474   1.849  18.221  1.00 11.18      F000 C  
ANISOU 1559  C   GLN B1058     1280   1828   1137   -139     78    -32  F000 C  
ATOM   1560  O   GLN B1058      15.328   1.522  19.050  1.00 12.31      F000 O  
ANISOU 1560  O   GLN B1058     1593   1771   1310   -136   -125    130  F000 O  
ATOM   1561  CB  GLN B1058      15.848   1.633  16.168  1.00 11.63      F000 C  
ANISOU 1561  CB  GLN B1058     1501   1747   1170   -114    -46   -104  F000 C  
ATOM   1562  CG  GLN B1058      15.265   0.277  15.866  1.00 12.36      F000 C  
ANISOU 1562  CG  GLN B1058     1614   1703   1376     17    200     52  F000 C  
ATOM   1563  CD  GLN B1058      16.192  -0.622  15.119  1.00 14.07      F000 C  
ANISOU 1563  CD  GLN B1058     1639   2203   1503    -26     29   -254  F000 C  
ATOM   1564  NE2 GLN B1058      16.026  -1.922  15.319  1.00 16.66      F000 N  
ANISOU 1564  NE2 GLN B1058     1805   2555   1967    101     10    -45  F000 N  
ATOM   1565  OE1 GLN B1058      17.042  -0.167  14.353  1.00 19.04      F000 O  
ANISOU 1565  OE1 GLN B1058     2200   3069   1964    114   -181   -912  F000 O  
ATOM   1566  N   TYR B1059      13.176   1.610  18.373  1.00 10.85      F000 N  
ANISOU 1566  N   TYR B1059     1334   1651   1135   -103   -106     59  F000 N  
ATOM   1567  CA  TYR B1059      12.622   0.851  19.496  1.00 11.16      F000 C  
ANISOU 1567  CA  TYR B1059     1429   1648   1163   -136     12     21  F000 C  
ATOM   1568  C   TYR B1059      12.067  -0.450  18.956  1.00 11.05      F000 C  
ANISOU 1568  C   TYR B1059     1362   1742   1095    -83    -26     28  F000 C  
ATOM   1569  O   TYR B1059      11.263  -0.442  18.025  1.00 12.44      F000 O  
ANISOU 1569  O   TYR B1059     1464   2023   1238    -79    -20    305  F000 O  
ATOM   1570  CB  TYR B1059      11.472   1.605  20.160  1.00 11.37      F000 C  
ANISOU 1570  CB  TYR B1059     1465   1762   1093    -94    -63     62  F000 C  
ATOM   1571  CG  TYR B1059      11.853   2.896  20.846  1.00 11.90      F000 C  
ANISOU 1571  CG  TYR B1059     1469   1855   1195   -241    117    -69  F000 C  
ATOM   1572  CD1 TYR B1059      11.929   4.085  20.130  1.00 11.20      F000 C  
ANISOU 1572  CD1 TYR B1059     1393   1802   1058   -300    112      4  F000 C  
ATOM   1573  CD2 TYR B1059      12.136   2.927  22.198  1.00 11.51      F000 C  
ANISOU 1573  CD2 TYR B1059     1317   1939   1115   -121     -9   -151  F000 C  
ATOM   1574  CE1 TYR B1059      12.259   5.268  20.758  1.00 12.46      F000 C  
ANISOU 1574  CE1 TYR B1059     1469   1981   1284   -104   -112   -222  F000 C  
ATOM   1575  CE2 TYR B1059      12.469   4.110  22.834  1.00 12.53      F000 C  
ANISOU 1575  CE2 TYR B1059     1648   2098   1014   -301     23   -234  F000 C  
ATOM   1576  CZ  TYR B1059      12.539   5.276  22.102  1.00 11.70      F000 C  
ANISOU 1576  CZ  TYR B1059     1295   1945   1203   -274    130     21  F000 C  
ATOM   1577  OH  TYR B1059      12.863   6.464  22.716  1.00 14.88      F000 O  
ANISOU 1577  OH  TYR B1059     1450   2629   1574   -299    238   -165  F000 O  
ATOM   1578  N   ASP B1060      12.466  -1.565  19.560  1.00 11.77      F000 N  
ANISOU 1578  N   ASP B1060     1316   1982   1172    -76     44    259  F000 N  
ATOM   1579  CA  ASP B1060      11.968  -2.867  19.152  1.00 12.56      F000 C  
ANISOU 1579  CA  ASP B1060     1548   1822   1400     14     77    101  F000 C  
ATOM   1580  C   ASP B1060      10.823  -3.354  20.037  1.00 13.24      F000 C  
ANISOU 1580  C   ASP B1060     1558   1987   1485     38     97     88  F000 C  
ATOM   1581  O   ASP B1060      10.637  -2.886  21.169  1.00 13.26      F000 O  
ANISOU 1581  O   ASP B1060     1587   2064   1387     27    137    122  F000 O  
ATOM   1582  CB  ASP B1060      13.110  -3.885  19.135  1.00 13.30      F000 C  
ANISOU 1582  CB  ASP B1060     1764   1916   1373    -68    -13     56  F000 C  
ATOM   1583  CG  ASP B1060      14.211  -3.501  18.146  1.00 15.58      F000 C  
ANISOU 1583  CG  ASP B1060     2248   1942   1730    -56   -171     19  F000 C  
ATOM   1584  OD1 ASP B1060      13.880  -3.050  17.030  1.00 16.05      F000 O  
ANISOU 1584  OD1 ASP B1060     2262   2080   1753    121    -80    -18  F000 O  
ATOM   1585  OD2 ASP B1060      15.395  -3.608  18.509  1.00 24.28      F000 O1-
ANISOU 1585  OD2 ASP B1060     4320   2211   2692     47   -623    180  F000 O1-
ATOM   1586  N   GLN B1061      10.039  -4.268  19.471  1.00 12.94      F000 N  
ANISOU 1586  N   GLN B1061     1435   1881   1598    -41    108    -23  F000 N  
ATOM   1587  CA  GLN B1061       8.976  -4.958  20.180  1.00 14.64      F000 C  
ANISOU 1587  CA  GLN B1061     1812   1988   1761     -2     27    -64  F000 C  
ATOM   1588  C   GLN B1061       8.017  -4.016  20.918  1.00 12.97      F000 C  
ANISOU 1588  C   GLN B1061     1477   1962   1489    -33    162    -95  F000 C  
ATOM   1589  O   GLN B1061       7.706  -4.184  22.099  1.00 14.67      F000 O  
ANISOU 1589  O   GLN B1061     1831   2060   1682   -109   -131   -111  F000 O  
ATOM   1590  CB  GLN B1061       9.560  -6.028  21.095  1.00 16.87      F000 C  
ANISOU 1590  CB  GLN B1061     1910   2370   2127     52    -26   -227  F000 C  
ATOM   1591  CG  GLN B1061      10.190  -7.173  20.308  1.00 20.90      F000 C  
ANISOU 1591  CG  GLN B1061     2472   2750   2719    104    -28   -216  F000 C  
ATOM   1592  CD  GLN B1061      10.500  -8.406  21.154  0.50 17.19      F000 C  
ANISOU 1592  CD  GLN B1061     1962   2533   2037    211    -73    -22  F000 C  
ATOM   1593  NE2 GLN B1061      11.341  -9.280  20.627  0.50 20.78      F000 N  
ANISOU 1593  NE2 GLN B1061     2310   3142   2443   -271    293    573  F000 N  
ATOM   1594  OE1 GLN B1061      10.000  -8.559  22.266  0.50 23.74      F000 O  
ANISOU 1594  OE1 GLN B1061     2062   3368   3589    536   -739    -65  F000 O  
ATOM   1595  N   ILE B1062       7.519  -3.047  20.158  1.00 12.00      F000 N  
ANISOU 1595  N   ILE B1062     1487   1832   1240     52      8    -11  F000 N  
ATOM   1596  CA  ILE B1062       6.503  -2.108  20.620  1.00 12.03      F000 C  
ANISOU 1596  CA  ILE B1062     1606   1587   1377    -90     42    -36  F000 C  
ATOM   1597  C   ILE B1062       5.120  -2.554  20.155  1.00 12.28      F000 C  
ANISOU 1597  C   ILE B1062     1659   1701   1304   -147    123   -129  F000 C  
ATOM   1598  O   ILE B1062       4.929  -2.961  18.997  1.00 13.82      F000 O  
ANISOU 1598  O   ILE B1062     1902   1912   1436    -93    335    -59  F000 O  
ATOM   1599  CB  ILE B1062       6.802  -0.698  20.055  1.00 11.69      F000 C  
ANISOU 1599  CB  ILE B1062     1597   1634   1208     62     93     80  F000 C  
ATOM   1600  CG1 ILE B1062       8.178  -0.227  20.540  1.00 12.25      F000 C  
ANISOU 1600  CG1 ILE B1062     1458   1793   1401   -114    -19     29  F000 C  
ATOM   1601  CG2 ILE B1062       5.690   0.264  20.404  1.00 12.93      F000 C  
ANISOU 1601  CG2 ILE B1062     1545   1891   1475    -24     86     62  F000 C  
ATOM   1602  CD1 ILE B1062       8.290  -0.075  22.044  1.00 12.95      F000 C  
ANISOU 1602  CD1 ILE B1062     1519   1609   1789    -38     19    -44  F000 C  
ATOM   1603  N   LEU B1063       4.159  -2.497  21.073  1.00 13.26      F000 N  
ANISOU 1603  N   LEU B1063     1724   1880   1433    -93    130   -203  F000 N  
ATOM   1604  CA  LEU B1063       2.785  -2.857  20.769  1.00 14.87      F000 C  
ANISOU 1604  CA  LEU B1063     1836   2106   1706     29    213   -138  F000 C  
ATOM   1605  C   LEU B1063       2.060  -1.657  20.147  1.00 14.60      F000 C  
ANISOU 1605  C   LEU B1063     1847   2013   1684    -48    163   -132  F000 C  
ATOM   1606  O   LEU B1063       2.116  -0.529  20.665  1.00 16.87      F000 O  
ANISOU 1606  O   LEU B1063     1922   2569   1919     17    459    -70  F000 O  
ATOM   1607  CB  LEU B1063       2.085  -3.321  22.056  1.00 17.14      F000 C  
ANISOU 1607  CB  LEU B1063     2071   2243   2198    -86    109   -295  F000 C  
ATOM   1608  CG  LEU B1063       0.688  -3.933  22.029  1.00 19.40      F000 C  
ANISOU 1608  CG  LEU B1063     2460   2392   2517    208    112   -221  F000 C  
ATOM   1609  CD1 LEU B1063       0.693  -5.311  21.449  1.00 21.65      F000 C  
ANISOU 1609  CD1 LEU B1063     2574   2808   2844   -384    408    270  F000 C  
ATOM   1610  CD2 LEU B1063       0.143  -3.998  23.448  0.50 17.75      F000 C  
ANISOU 1610  CD2 LEU B1063     2324   2384   2035   -152    102   -239  F000 C  
ATOM   1611  N  AILE B1064       1.329  -1.927  19.076  0.70 14.47      F000 N  
ANISOU 1611  N  AILE B1064     1783   1959   1753     53    359   -118  F000 N  
ATOM   1612  N  BILE B1064       1.411  -1.898  19.015  0.30 15.35      F000 N  
ANISOU 1612  N  BILE B1064     1905   2071   1855    -24    197    -86  F000 N  
ATOM   1613  CA AILE B1064       0.569  -0.921  18.369  0.70 15.22      F000 C  
ANISOU 1613  CA AILE B1064     1861   2163   1758    -35    259    -88  F000 C  
ATOM   1614  CA BILE B1064       0.521  -0.919  18.419  0.30 15.58      F000 C  
ANISOU 1614  CA BILE B1064     1946   2110   1861    -22    154    -48  F000 C  
ATOM   1615  C  AILE B1064      -0.796  -1.519  18.000  0.70 14.65      F000 C  
ANISOU 1615  C  AILE B1064     1847   2054   1665    129    226     26  F000 C  
ATOM   1616  C  BILE B1064      -0.844  -1.548  18.186  0.30 15.02      F000 C  
ANISOU 1616  C  BILE B1064     1907   2026   1772     47    175    -22  F000 C  
ATOM   1617  O  AILE B1064      -0.901  -2.712  17.725  0.70 17.03      F000 O  
ANISOU 1617  O  AILE B1064     1950   2340   2181    -58    481    178  F000 O  
ATOM   1618  O  BILE B1064      -0.999  -2.770  18.227  0.30 15.26      F000 O  
ANISOU 1618  O  BILE B1064     1995   2002   1797    -45    306    -21  F000 O  
ATOM   1619  CB AILE B1064       1.335  -0.484  17.109  0.70 16.15      F000 C  
ANISOU 1619  CB AILE B1064     1979   2099   2058     12    238   -214  F000 C  
ATOM   1620  CB BILE B1064       1.086  -0.367  17.094  0.30 15.79      F000 C  
ANISOU 1620  CB BILE B1064     1931   2062   2006     -5    139   -109  F000 C  
ATOM   1621  CG1AILE B1064       0.778   0.821  16.546  0.70 16.04      F000 C  
ANISOU 1621  CG1AILE B1064     2245   2122   1727    -61    258    -18  F000 C  
ATOM   1622  CG1BILE B1064       2.487   0.195  17.327  0.30 14.89      F000 C  
ANISOU 1622  CG1BILE B1064     1905   1832   1921    -22    206    -17  F000 C  
ATOM   1623  CG2AILE B1064       1.303  -1.604  16.065  0.70 15.72      F000 C  
ANISOU 1623  CG2AILE B1064     1935   2245   1793     -2    379   -575  F000 C  
ATOM   1624  CG2BILE B1064       0.170   0.708  16.517  0.30 16.84      F000 C  
ANISOU 1624  CG2BILE B1064     2133   2262   2003    -61    119   -115  F000 C  
ATOM   1625  CD1AILE B1064       1.651   1.462  15.484  0.70 15.99      F000 C  
ANISOU 1625  CD1AILE B1064     1938   2294   1840     68    195    -87  F000 C  
ATOM   1626  CD1BILE B1064       3.121   0.795  16.104  0.30 17.83      F000 C  
ANISOU 1626  CD1BILE B1064     2240   2335   2200    -32     97     39  F000 C  
ATOM   1627  N   GLU B1065      -1.840  -0.698  17.996  1.00 13.85      F000 N  
ANISOU 1627  N   GLU B1065     1765   1911   1585     65    304    -61  F000 N  
ATOM   1628  CA  GLU B1065      -3.128  -1.129  17.514  1.00 16.55      F000 C  
ANISOU 1628  CA  GLU B1065     2119   2292   1875    113     56     46  F000 C  
ATOM   1629  C   GLU B1065      -3.439  -0.258  16.313  1.00 18.86      F000 C  
ANISOU 1629  C   GLU B1065     2324   2853   1986    100    112    158  F000 C  
ATOM   1630  O   GLU B1065      -3.552   0.951  16.431  1.00 19.32      F000 O  
ANISOU 1630  O   GLU B1065     2322   3313   1705    194    -38    733  F000 O  
ATOM   1631  CB  GLU B1065      -4.161  -0.984  18.630  1.00 16.66      F000 C  
ANISOU 1631  CB  GLU B1065     2177   2165   1986      5    215     -8  F000 C  
ATOM   1632  CG  GLU B1065      -5.467  -1.677  18.365  1.00 19.86      F000 C  
ANISOU 1632  CG  GLU B1065     2540   2463   2542    129     -4     35  F000 C  
ATOM   1633  CD  GLU B1065      -6.436  -1.482  19.508  0.75 21.44      F000 C  
ANISOU 1633  CD  GLU B1065     3020   2632   2492    201    -21    -53  F000 C  
ATOM   1634  OE1 GLU B1065      -6.059  -1.771  20.666  0.75 26.74      F000 O  
ANISOU 1634  OE1 GLU B1065     4306   2641   3213    464   -317   -525  F000 O  
ATOM   1635  OE2 GLU B1065      -7.562  -1.020  19.254  0.75 30.25      F000 O1-
ANISOU 1635  OE2 GLU B1065     4050   3581   3863    356    112   -265  F000 O1-
ATOM   1636  N   ILE B1066      -3.506  -0.889  15.144  1.00 20.07      F000 N  
ANISOU 1636  N   ILE B1066     2374   3201   2049    103      6    273  F000 N  
ATOM   1637  CA  ILE B1066      -3.558  -0.178  13.869  1.00 21.68      F000 C  
ANISOU 1637  CA  ILE B1066     2604   3047   2584    183     45    135  F000 C  
ATOM   1638  C   ILE B1066      -4.962  -0.468  13.415  1.00 24.54      F000 C  
ANISOU 1638  C   ILE B1066     2867   3518   2937    150     28    375  F000 C  
ATOM   1639  O   ILE B1066      -5.319  -1.607  13.075  1.00 24.83      F000 O  
ANISOU 1639  O   ILE B1066     2977   3873   2581    313     89    806  F000 O  
ATOM   1640  CB  ILE B1066      -2.511  -0.694  12.852  1.00 21.95      F000 C  
ANISOU 1640  CB  ILE B1066     2853   3013   2471    108    -72    183  F000 C  
ATOM   1641  CG1 ILE B1066      -1.088  -0.428  13.352  1.00 23.22      F000 C  
ANISOU 1641  CG1 ILE B1066     2994   3040   2788     26    128    120  F000 C  
ATOM   1642  CG2 ILE B1066      -2.705  -0.045  11.486  0.50 19.95      F000 C  
ANISOU 1642  CG2 ILE B1066     2473   2965   2140    128   -116    -48  F000 C  
ATOM   1643  CD1 ILE B1066      -0.039  -1.312  12.702  0.50 19.07      F000 C  
ANISOU 1643  CD1 ILE B1066     2487   2615   2143     23      0    -28  F000 C  
ATOM   1644  N   CYS B1067      -5.796   0.552  13.500  1.00 28.68      F000 N  
ANISOU 1644  N   CYS B1067     3483   3681   3730     79     84    199  F000 N  
ATOM   1645  CA  CYS B1067      -7.143   0.430  13.029  1.00 28.56      F000 C  
ANISOU 1645  CA  CYS B1067     3522   3634   3693     16     75    203  F000 C  
ATOM   1646  C   CYS B1067      -7.830  -0.797  13.635  1.00 28.82      F000 C  
ANISOU 1646  C   CYS B1067     3580   3685   3684    -68     56    148  F000 C  
ATOM   1647  O   CYS B1067      -8.514  -1.537  12.921  1.00 30.49      F000 O  
ANISOU 1647  O   CYS B1067     3791   3522   4271   -388    149    341  F000 O  
ATOM   1648  CB  CYS B1067      -7.108   0.311  11.509  1.00 29.81      F000 C  
ANISOU 1648  CB  CYS B1067     3608   3674   4044     42     36    101  F000 C  
ATOM   1649  SG  CYS B1067      -8.700   0.464  10.818  1.00 31.82      F000 S  
ANISOU 1649  SG  CYS B1067     4036   3869   4184    219   -161    584  F000 S  
ATOM   1650  N   GLY B1068      -7.630  -1.031  14.933  1.00 28.06      F000 N  
ANISOU 1650  N   GLY B1068     3507   3468   3686     22     85    202  F000 N  
ATOM   1651  CA  GLY B1068      -8.344  -2.100  15.663  1.00 25.62      F000 C  
ANISOU 1651  CA  GLY B1068     3195   3248   3291     21     29    133  F000 C  
ATOM   1652  C   GLY B1068      -7.588  -3.427  15.808  1.00 25.71      F000 C  
ANISOU 1652  C   GLY B1068     3299   3200   3269     -1     12    102  F000 C  
ATOM   1653  O   GLY B1068      -8.002  -4.319  16.553  1.00 27.29      F000 O  
ANISOU 1653  O   GLY B1068     3301   3487   3581    122    112     77  F000 O  
ATOM   1654  N   HIS B1069      -6.482  -3.566  15.094  1.00 23.21      F000 N  
ANISOU 1654  N   HIS B1069     2998   3047   2771     82    127    263  F000 N  
ATOM   1655  CA  HIS B1069      -5.753  -4.829  15.054  1.00 21.22      F000 C  
ANISOU 1655  CA  HIS B1069     2758   2745   2557     -6    107    196  F000 C  
ATOM   1656  C   HIS B1069      -4.424  -4.627  15.753  1.00 19.08      F000 C  
ANISOU 1656  C   HIS B1069     2497   2483   2269   -109     80    199  F000 C  
ATOM   1657  O   HIS B1069      -3.678  -3.708  15.424  1.00 21.20      F000 O  
ANISOU 1657  O   HIS B1069     2488   3184   2384   -218     23    633  F000 O  
ATOM   1658  CB  HIS B1069      -5.507  -5.248  13.605  1.00 21.53      F000 C  
ANISOU 1658  CB  HIS B1069     2898   2741   2539   -101    149    238  F000 C  
ATOM   1659  CG  HIS B1069      -6.745  -5.662  12.873  1.00 23.57      F000 C  
ANISOU 1659  CG  HIS B1069     3281   2879   2794   -105    239    338  F000 C  
ATOM   1660  CD2 HIS B1069      -7.876  -4.981  12.568  1.00 24.65      F000 C  
ANISOU 1660  CD2 HIS B1069     3600   3287   2476   -240    747    513  F000 C  
ATOM   1661  ND1 HIS B1069      -6.906  -6.925  12.348  1.00 25.75      F000 N  
ANISOU 1661  ND1 HIS B1069     3716   3159   2906   -488    470    478  F000 N  
ATOM   1662  CE1 HIS B1069      -8.084  -7.005  11.752  1.00 24.77      F000 C  
ANISOU 1662  CE1 HIS B1069     3779   2772   2858   -290    418    639  F000 C  
ATOM   1663  NE2 HIS B1069      -8.694  -5.839  11.873  1.00 25.95      F000 N  
ANISOU 1663  NE2 HIS B1069     3947   3241   2673   -355    406    526  F000 N  
ATOM   1664  N   LYS B1070      -4.096  -5.498  16.694  1.00 15.24      F000 N  
ANISOU 1664  N   LYS B1070     1968   1964   1859     26    196    -28  F000 N  
ATOM   1665  CA  LYS B1070      -2.859  -5.336  17.428  1.00 16.26      F000 C  
ANISOU 1665  CA  LYS B1070     2159   2080   1940      2     96    -76  F000 C  
ATOM   1666  C   LYS B1070      -1.677  -5.996  16.718  1.00 14.32      F000 C  
ANISOU 1666  C   LYS B1070     1836   1826   1776    -25    237    -79  F000 C  
ATOM   1667  O   LYS B1070      -1.818  -7.005  16.039  1.00 16.02      F000 O  
ANISOU 1667  O   LYS B1070     2187   1890   2006    -66    303    -31  F000 O  
ATOM   1668  CB  LYS B1070      -3.009  -5.877  18.844  1.00 16.60      F000 C  
ANISOU 1668  CB  LYS B1070     2248   2014   2044    117    116    -49  F000 C  
ATOM   1669  CG  LYS B1070      -3.988  -5.066  19.676  1.00 18.89      F000 C  
ANISOU 1669  CG  LYS B1070     2559   2441   2177     15    111   -188  F000 C  
ATOM   1670  CD  LYS B1070      -4.039  -5.535  21.101  1.00 19.06      F000 C  
ANISOU 1670  CD  LYS B1070     2520   2415   2305    122    100   -253  F000 C  
ATOM   1671  CE  LYS B1070      -5.209  -4.875  21.834  1.00 21.03      F000 C  
ANISOU 1671  CE  LYS B1070     2696   2631   2660    371    -39   -205  F000 C  
ATOM   1672  NZ  LYS B1070      -5.302  -5.310  23.256  1.00 21.98      F000 N1+
ANISOU 1672  NZ  LYS B1070     2888   2906   2555    412    156   -397  F000 N1+
ATOM   1673  N   ALA B1071      -0.501  -5.417  16.909  1.00 13.54      F000 N  
ANISOU 1673  N   ALA B1071     1784   1693   1666    -43    258    -59  F000 N  
ATOM   1674  CA  ALA B1071       0.737  -5.963  16.361  1.00 13.80      F000 C  
ANISOU 1674  CA  ALA B1071     1739   1738   1765    -55    123    -20  F000 C  
ATOM   1675  C   ALA B1071       1.879  -5.522  17.243  1.00 12.73      F000 C  
ANISOU 1675  C   ALA B1071     1558   1739   1540    -97    247    -68  F000 C  
ATOM   1676  O   ALA B1071       1.781  -4.520  17.937  1.00 15.09      F000 O  
ANISOU 1676  O   ALA B1071     1561   2158   2012     78    575   -198  F000 O  
ATOM   1677  CB  ALA B1071       0.969  -5.481  14.934  1.00 15.00      F000 C  
ANISOU 1677  CB  ALA B1071     1826   1934   1936    -31    280     34  F000 C  
ATOM   1678  N   ILE B1072       2.969  -6.267  17.190  1.00 12.92      F000 N  
ANISOU 1678  N   ILE B1072     1647   1662   1596    -71    311    -92  F000 N  
ATOM   1679  CA  ILE B1072       4.202  -5.900  17.860  1.00 13.03      F000 C  
ANISOU 1679  CA  ILE B1072     1573   1778   1600   -140    108    -56  F000 C  
ATOM   1680  C   ILE B1072       5.303  -5.805  16.827  1.00 11.98      F000 C  
ANISOU 1680  C   ILE B1072     1437   1552   1563    -82     18      3  F000 C  
ATOM   1681  O   ILE B1072       5.419  -6.649  15.960  1.00 13.24      F000 O  
ANISOU 1681  O   ILE B1072     1602   1803   1625   -177     89     -6  F000 O  
ATOM   1682  CB  ILE B1072       4.563  -6.945  18.908  1.00 14.51      F000 C  
ANISOU 1682  CB  ILE B1072     1835   1862   1816   -193    240     25  F000 C  
ATOM   1683  CG1 ILE B1072       3.542  -6.862  20.038  1.00 15.92      F000 C  
ANISOU 1683  CG1 ILE B1072     1889   2321   1839   -300    122   -162  F000 C  
ATOM   1684  CG2 ILE B1072       5.964  -6.716  19.427  1.00 15.60      F000 C  
ANISOU 1684  CG2 ILE B1072     2150   2091   1686   -177   -215    148  F000 C  
ATOM   1685  CD1 ILE B1072       3.613  -7.993  21.007  1.00 18.55      F000 C  
ANISOU 1685  CD1 ILE B1072     2117   2517   2415   -182   -100    -70  F000 C  
ATOM   1686  N   GLY B1073       6.104  -4.761  16.913  1.00 11.71      F000 N  
ANISOU 1686  N   GLY B1073     1422   1607   1420     -9     50    -17  F000 N  
ATOM   1687  CA  GLY B1073       7.245  -4.660  16.049  1.00 11.88      F000 C  
ANISOU 1687  CA  GLY B1073     1550   1633   1329   -140      4    -49  F000 C  
ATOM   1688  C   GLY B1073       8.053  -3.418  16.299  1.00 11.17      F000 C  
ANISOU 1688  C   GLY B1073     1390   1664   1190    -90     56    -74  F000 C  
ATOM   1689  O   GLY B1073       7.856  -2.693  17.284  1.00 12.40      F000 O  
ANISOU 1689  O   GLY B1073     1735   1744   1231   -148    150    -72  F000 O  
ATOM   1690  N   THR B1074       8.979  -3.172  15.384  1.00 11.30      F000 N  
ANISOU 1690  N   THR B1074     1560   1613   1117   -131     18   -109  F000 N  
ATOM   1691  CA  THR B1074       9.911  -2.084  15.529  1.00 11.11      F000 C  
ANISOU 1691  CA  THR B1074     1500   1634   1087   -120     49     25  F000 C  
ATOM   1692  C   THR B1074       9.270  -0.769  15.096  1.00 10.89      F000 C  
ANISOU 1692  C   THR B1074     1323   1735   1080   -247     44     89  F000 C  
ATOM   1693  O   THR B1074       8.613  -0.680  14.045  1.00 11.91      F000 O  
ANISOU 1693  O   THR B1074     1569   1913   1041   -229    105    283  F000 O  
ATOM   1694  CB  THR B1074      11.157  -2.372  14.699  1.00 11.92      F000 C  
ANISOU 1694  CB  THR B1074     1687   1581   1260    -61     13    -65  F000 C  
ATOM   1695  CG2 THR B1074      12.105  -1.193  14.694  1.00 12.78      F000 C  
ANISOU 1695  CG2 THR B1074     1853   1673   1330   -201    -25    -82  F000 C  
ATOM   1696  OG1 THR B1074      11.818  -3.538  15.234  1.00 13.62      F000 O  
ANISOU 1696  OG1 THR B1074     1628   1890   1654    194    -32    -66  F000 O  
ATOM   1697  N   VAL B1075       9.458   0.250  15.928  1.00 11.51      F000 N  
ANISOU 1697  N   VAL B1075     1535   1733   1103   -111     68    216  F000 N  
ATOM   1698  CA  VAL B1075       8.971   1.585  15.655  1.00 11.76      F000 C  
ANISOU 1698  CA  VAL B1075     1593   1679   1196    -68    -72    113  F000 C  
ATOM   1699  C   VAL B1075      10.146   2.532  15.728  1.00 12.66      F000 C  
ANISOU 1699  C   VAL B1075     1505   2025   1278    -61      9    211  F000 C  
ATOM   1700  O   VAL B1075      10.871   2.561  16.725  1.00 13.43      F000 O  
ANISOU 1700  O   VAL B1075     1724   2173   1203   -248   -135    300  F000 O  
ATOM   1701  CB  VAL B1075       7.894   2.007  16.673  1.00 12.51      F000 C  
ANISOU 1701  CB  VAL B1075     1737   1788   1228    -17    -25    199  F000 C  
ATOM   1702  CG1 VAL B1075       7.468   3.468  16.461  1.00 13.54      F000 C  
ANISOU 1702  CG1 VAL B1075     1882   1911   1350     29     44     35  F000 C  
ATOM   1703  CG2 VAL B1075       6.699   1.043  16.571  1.00 14.01      F000 C  
ANISOU 1703  CG2 VAL B1075     1915   1890   1518    -44    -46    -72  F000 C  
ATOM   1704  N   LEU B1076      10.338   3.290  14.655  1.00 12.19      F000 N  
ANISOU 1704  N   LEU B1076     1412   2011   1208   -173   -117    195  F000 N  
ATOM   1705  CA  LEU B1076      11.341   4.335  14.632  1.00 12.27      F000 C  
ANISOU 1705  CA  LEU B1076     1488   1789   1384     16    -44    199  F000 C  
ATOM   1706  C   LEU B1076      10.666   5.635  15.029  1.00 12.20      F000 C  
ANISOU 1706  C   LEU B1076     1407   1807   1419      4    100    154  F000 C  
ATOM   1707  O   LEU B1076       9.544   5.924  14.594  1.00 14.48      F000 O  
ANISOU 1707  O   LEU B1076     1706   2008   1785    252    195    363  F000 O  
ATOM   1708  CB  LEU B1076      11.973   4.456  13.244  1.00 11.90      F000 C  
ANISOU 1708  CB  LEU B1076     1411   1717   1391    -98   -142    108  F000 C  
ATOM   1709  CG  LEU B1076      12.454   3.150  12.630  1.00 13.14      F000 C  
ANISOU 1709  CG  LEU B1076     1789   1914   1287   -109    -33     75  F000 C  
ATOM   1710  CD1 LEU B1076      13.013   3.416  11.236  1.00 13.43      F000 C  
ANISOU 1710  CD1 LEU B1076     1771   1773   1556   -297     71    -71  F000 C  
ATOM   1711  CD2 LEU B1076      13.495   2.471  13.519  1.00 14.08      F000 C  
ANISOU 1711  CD2 LEU B1076     1662   2251   1434    131    195    194  F000 C  
ATOM   1712  N   VAL B1077      11.342   6.416  15.860  1.00 11.31      F000 N  
ANISOU 1712  N   VAL B1077     1371   1718   1208    -79    -24    252  F000 N  
ATOM   1713  CA  VAL B1077      10.790   7.665  16.354  1.00 13.00      F000 C  
ANISOU 1713  CA  VAL B1077     1631   1820   1487   -100    -74     35  F000 C  
ATOM   1714  C   VAL B1077      11.758   8.787  15.996  1.00 12.76      F000 C  
ANISOU 1714  C   VAL B1077     1518   1911   1417   -123    -70     74  F000 C  
ATOM   1715  O   VAL B1077      12.962   8.715  16.280  1.00 13.24      F000 O  
ANISOU 1715  O   VAL B1077     1448   2039   1543   -177   -165     29  F000 O  
ATOM   1716  CB  VAL B1077      10.590   7.627  17.878  1.00 12.93      F000 C  
ANISOU 1716  CB  VAL B1077     1686   1838   1388   -114     -1     48  F000 C  
ATOM   1717  CG1 VAL B1077      10.111   8.960  18.397  1.00 14.31      F000 C  
ANISOU 1717  CG1 VAL B1077     1946   1954   1536    -56     24    -15  F000 C  
ATOM   1718  CG2 VAL B1077       9.616   6.530  18.252  1.00 14.31      F000 C  
ANISOU 1718  CG2 VAL B1077     1899   2102   1434     44    -81   -110  F000 C  
ATOM   1719  N   GLY B1078      11.230   9.828  15.367  1.00 14.68      F000 N  
ANISOU 1719  N   GLY B1078     1625   2008   1942   -177   -259     46  F000 N  
ATOM   1720  CA  GLY B1078      12.058  10.950  14.957  1.00 16.36      F000 C  
ANISOU 1720  CA  GLY B1078     1860   2225   2131    -65   -289     92  F000 C  
ATOM   1721  C   GLY B1078      11.307  11.874  14.030  1.00 17.83      F000 C  
ANISOU 1721  C   GLY B1078     1987   2399   2389    -58   -377    139  F000 C  
ATOM   1722  O   GLY B1078      10.088  11.794  13.902  1.00 18.00      F000 O  
ANISOU 1722  O   GLY B1078     1763   2550   2525    -86   -625    346  F000 O  
ATOM   1723  N   PRO B1079      12.043  12.782  13.399  1.00 19.61      F000 N  
ANISOU 1723  N   PRO B1079     2216   2644   2588   -187   -451    106  F000 N  
ATOM   1724  CA  PRO B1079      11.435  13.901  12.673  1.00 20.90      F000 C  
ANISOU 1724  CA  PRO B1079     2437   2745   2758   -147   -444     53  F000 C  
ATOM   1725  C   PRO B1079      10.912  13.615  11.260  1.00 24.27      F000 C  
ANISOU 1725  C   PRO B1079     2992   3079   3150   -307   -401   -106  F000 C  
ATOM   1726  O   PRO B1079      11.384  14.194  10.275  1.00 26.57      F000 O  
ANISOU 1726  O   PRO B1079     3250   3795   3048   -286   -908     29  F000 O  
ATOM   1727  CB  PRO B1079      12.549  14.952  12.660  1.00 23.76      F000 C  
ANISOU 1727  CB  PRO B1079     2822   2876   3327   -255   -419      8  F000 C  
ATOM   1728  CG  PRO B1079      13.819  14.172  12.748  1.00 18.42      F000 C  
ANISOU 1728  CG  PRO B1079     1885   2571   2539     -2   -481    -62  F000 C  
ATOM   1729  CD  PRO B1079      13.512  12.854  13.423  1.00 18.80      F000 C  
ANISOU 1729  CD  PRO B1079     1905   2721   2515     47   -608     25  F000 C  
ATOM   1730  N   THR B1080       9.892  12.778  11.187  1.00 22.85      F000 N  
ANISOU 1730  N   THR B1080     2693   3005   2982   -314   -148    -38  F000 N  
ATOM   1731  CA  THR B1080       9.234  12.422   9.937  1.00 21.42      F000 C  
ANISOU 1731  CA  THR B1080     2654   2833   2650    -96   -263    -13  F000 C  
ATOM   1732  C   THR B1080       8.106  13.409   9.611  1.00 22.11      F000 C  
ANISOU 1732  C   THR B1080     2641   2951   2809   -169   -221     14  F000 C  
ATOM   1733  O   THR B1080       7.398  13.869  10.507  1.00 22.46      F000 O  
ANISOU 1733  O   THR B1080     2451   3042   3038   -233     26     72  F000 O  
ATOM   1734  CB  THR B1080       8.662  10.990  10.061  1.00 19.38      F000 C  
ANISOU 1734  CB  THR B1080     2349   2615   2400   -148   -193    -17  F000 C  
ATOM   1735  CG2 THR B1080       7.660  10.892  11.215  1.00 18.49      F000 C  
ANISOU 1735  CG2 THR B1080     2489   2603   1933    -41   -178    112  F000 C  
ATOM   1736  OG1 THR B1080       8.043  10.590   8.831  1.00 19.47      F000 O  
ANISOU 1736  OG1 THR B1080     2626   3007   1762   -167   -188    125  F000 O  
ATOM   1737  N   PRO B1081       7.941  13.756   8.328  1.00 24.85      F000 N  
ANISOU 1737  N   PRO B1081     3006   3218   3216     41   -144    -58  F000 N  
ATOM   1738  CA  PRO B1081       6.887  14.714   7.982  1.00 23.76      F000 C  
ANISOU 1738  CA  PRO B1081     2839   3165   3021     44   -189     23  F000 C  
ATOM   1739  C   PRO B1081       5.484  14.136   8.111  1.00 22.99      F000 C  
ANISOU 1739  C   PRO B1081     2770   3049   2915    100    -81     42  F000 C  
ATOM   1740  O   PRO B1081       4.518  14.873   8.283  1.00 24.41      F000 O  
ANISOU 1740  O   PRO B1081     2599   3433   3239    171   -373    132  F000 O  
ATOM   1741  CB  PRO B1081       7.185  15.065   6.521  1.00 25.11      F000 C  
ANISOU 1741  CB  PRO B1081     3030   3304   3204    119   -186   -108  F000 C  
ATOM   1742  CG  PRO B1081       8.508  14.433   6.200  1.00 27.62      F000 C  
ANISOU 1742  CG  PRO B1081     3521   3501   3468    106   -377   -106  F000 C  
ATOM   1743  CD  PRO B1081       8.693  13.310   7.147  1.00 25.15      F000 C  
ANISOU 1743  CD  PRO B1081     2956   3322   3277    128   -338    -55  F000 C  
ATOM   1744  N   VAL B1082       5.379  12.816   8.020  1.00 22.12      F000 N  
ANISOU 1744  N   VAL B1082     2671   2997   2735    -31   -292     80  F000 N  
ATOM   1745  CA  VAL B1082       4.101  12.129   8.126  1.00 22.02      F000 C  
ANISOU 1745  CA  VAL B1082     2743   2951   2672     -7   -135    151  F000 C  
ATOM   1746  C   VAL B1082       4.361  10.894   8.979  1.00 19.49      F000 C  
ANISOU 1746  C   VAL B1082     2338   2662   2401    -27   -170    208  F000 C  
ATOM   1747  O   VAL B1082       5.413  10.275   8.858  1.00 19.69      F000 O  
ANISOU 1747  O   VAL B1082     2178   2909   2392    -63   -288    139  F000 O  
ATOM   1748  CB  VAL B1082       3.593  11.689   6.729  1.00 23.52      F000 C  
ANISOU 1748  CB  VAL B1082     3054   3086   2794    -32   -369    208  F000 C  
ATOM   1749  CG1 VAL B1082       4.681  10.998   5.980  1.00 27.05      F000 C  
ANISOU 1749  CG1 VAL B1082     3448   3785   3045    109   -276    121  F000 C  
ATOM   1750  CG2 VAL B1082       2.384  10.802   6.830  1.00 25.29      F000 C  
ANISOU 1750  CG2 VAL B1082     3207   3416   2984   -169   -237    279  F000 C  
ATOM   1751  N   ASN B1083       3.424  10.556   9.851  1.00 18.15      F000 N  
ANISOU 1751  N   ASN B1083     2265   2421   2207     86    -57    350  F000 N  
ATOM   1752  CA  ASN B1083       3.495   9.293  10.575  1.00 16.82      F000 C  
ANISOU 1752  CA  ASN B1083     2158   2210   2020     57    -39    258  F000 C  
ATOM   1753  C   ASN B1083       3.225   8.166   9.607  1.00 15.93      F000 C  
ANISOU 1753  C   ASN B1083     2046   2075   1930     70     30    268  F000 C  
ATOM   1754  O   ASN B1083       2.199   8.169   8.920  1.00 17.39      F000 O  
ANISOU 1754  O   ASN B1083     2419   2119   2067    256      8    693  F000 O  
ATOM   1755  CB  ASN B1083       2.454   9.248  11.685  1.00 17.34      F000 C  
ANISOU 1755  CB  ASN B1083     2242   2258   2088    251     56    319  F000 C  
ATOM   1756  CG  ASN B1083       2.789  10.169  12.827  1.00 18.49      F000 C  
ANISOU 1756  CG  ASN B1083     2110   2536   2376    255    148    382  F000 C  
ATOM   1757  ND2 ASN B1083       1.764  10.619  13.543  1.00 19.31      F000 N  
ANISOU 1757  ND2 ASN B1083     2366   2391   2580    374    346    257  F000 N  
ATOM   1758  OD1 ASN B1083       3.957  10.477  13.067  1.00 21.87      F000 O  
ANISOU 1758  OD1 ASN B1083     2520   2754   3034    313    634    673  F000 O  
ATOM   1759  N  AILE B1084       4.147   7.210   9.549  0.50 14.66      F000 N  
ANISOU 1759  N  AILE B1084     1914   1961   1694     50    -92    211  F000 N  
ATOM   1760  N  BILE B1084       4.139   7.203   9.565  0.50 14.92      F000 N  
ANISOU 1760  N  BILE B1084     1929   1992   1746     60    -91    217  F000 N  
ATOM   1761  CA AILE B1084       4.133   6.167   8.530  0.50 14.63      F000 C  
ANISOU 1761  CA AILE B1084     1913   1916   1727     31   -107    154  F000 C  
ATOM   1762  CA BILE B1084       4.139   6.164   8.544  0.50 14.86      F000 C  
ANISOU 1762  CA BILE B1084     1929   1968   1749     67   -106    173  F000 C  
ATOM   1763  C  AILE B1084       4.072   4.786   9.187  0.50 14.15      F000 C  
ANISOU 1763  C  AILE B1084     1862   1887   1624     16   -168    157  F000 C  
ATOM   1764  C  BILE B1084       4.073   4.782   9.193  0.50 14.32      F000 C  
ANISOU 1764  C  BILE B1084     1880   1914   1645     27   -167    162  F000 C  
ATOM   1765  O  AILE B1084       4.926   4.453  10.006  0.50 14.25      F000 O  
ANISOU 1765  O  AILE B1084     1924   1849   1639    -43   -139    303  F000 O  
ATOM   1766  O  BILE B1084       4.924   4.443  10.013  0.50 14.37      F000 O  
ANISOU 1766  O  BILE B1084     1949   1864   1646    -31   -138    308  F000 O  
ATOM   1767  CB AILE B1084       5.403   6.252   7.665  0.50 14.57      F000 C  
ANISOU 1767  CB AILE B1084     1866   1984   1682     98   -134    139  F000 C  
ATOM   1768  CB BILE B1084       5.424   6.247   7.709  0.50 15.25      F000 C  
ANISOU 1768  CB BILE B1084     1933   2092   1766    112   -125    138  F000 C  
ATOM   1769  CG1AILE B1084       5.318   7.448   6.711  0.50 15.54      F000 C  
ANISOU 1769  CG1AILE B1084     2077   1863   1962      2    -15     -8  F000 C  
ATOM   1770  CG1BILE B1084       5.507   7.603   7.004  0.50 17.90      F000 C  
ANISOU 1770  CG1BILE B1084     2355   2293   2153     70     52     26  F000 C  
ATOM   1771  CG2AILE B1084       5.633   4.959   6.897  0.50 15.50      F000 C  
ANISOU 1771  CG2AILE B1084     2092   2105   1692      4    -98    184  F000 C  
ATOM   1772  CG2BILE B1084       5.499   5.106   6.712  0.50 16.08      F000 C  
ANISOU 1772  CG2BILE B1084     2070   2136   1901     13   -118    196  F000 C  
ATOM   1773  CD1AILE B1084       6.682   7.929   6.220  0.50 15.66      F000 C  
ANISOU 1773  CD1AILE B1084     2120   1871   1958   -238    -75      0  F000 C  
ATOM   1774  CD1BILE B1084       4.431   7.820   5.975  0.50 20.78      F000 C  
ANISOU 1774  CD1BILE B1084     2709   2696   2490    112     61      4  F000 C  
ATOM   1775  N   ILE B1085       3.066   3.993   8.819  1.00 14.02      F000 N  
ANISOU 1775  N   ILE B1085     1924   1803   1600     85   -185    187  F000 N  
ATOM   1776  CA  ILE B1085       3.050   2.564   9.117  1.00 13.46      F000 C  
ANISOU 1776  CA  ILE B1085     1947   1719   1448    -11   -204    146  F000 C  
ATOM   1777  C   ILE B1085       3.613   1.844   7.903  1.00 12.75      F000 C  
ANISOU 1777  C   ILE B1085     1860   1644   1340     46   -297    192  F000 C  
ATOM   1778  O   ILE B1085       2.989   1.816   6.843  1.00 14.86      F000 O  
ANISOU 1778  O   ILE B1085     2266   2018   1363    -76   -168    290  F000 O  
ATOM   1779  CB  ILE B1085       1.627   2.028   9.412  1.00 13.38      F000 C  
ANISOU 1779  CB  ILE B1085     2018   1753   1313     -7   -228    168  F000 C  
ATOM   1780  CG1 ILE B1085       0.931   2.862  10.501  1.00 15.16      F000 C  
ANISOU 1780  CG1 ILE B1085     2179   1828   1750   -164   -275    139  F000 C  
ATOM   1781  CG2 ILE B1085       1.683   0.560   9.802  1.00 15.68      F000 C  
ANISOU 1781  CG2 ILE B1085     2311   1969   1676    -51   -230     17  F000 C  
ATOM   1782  CD1 ILE B1085       1.722   2.999  11.789  1.00 17.73      F000 C  
ANISOU 1782  CD1 ILE B1085     2661   2107   1966   -237    258    116  F000 C  
ATOM   1783  N   GLY B1086       4.818   1.311   8.050  1.00 13.45      F000 N  
ANISOU 1783  N   GLY B1086     1980   1758   1371    121   -137    150  F000 N  
ATOM   1784  CA  GLY B1086       5.513   0.679   6.955  1.00 13.18      F000 C  
ANISOU 1784  CA  GLY B1086     2003   1675   1327    139   -159    256  F000 C  
ATOM   1785  C   GLY B1086       5.269  -0.817   6.905  1.00 13.25      F000 C  
ANISOU 1785  C   GLY B1086     1971   1802   1260     -2    -20     63  F000 C  
ATOM   1786  O   GLY B1086       4.533  -1.394   7.723  1.00 13.12      F000 O  
ANISOU 1786  O   GLY B1086     2090   1732   1163   -223     54     40  F000 O  
ATOM   1787  N   ARG B1087       5.925  -1.466   5.952  1.00 13.81      F000 N  
ANISOU 1787  N   ARG B1087     2250   1761   1237      0    -61   -145  F000 N  
ATOM   1788  CA  ARG B1087       5.669  -2.856   5.691  1.00 13.85      F000 C  
ANISOU 1788  CA  ARG B1087     2074   1801   1387     78     33     16  F000 C  
ATOM   1789  C   ARG B1087       5.955  -3.733   6.892  1.00 13.21      F000 C  
ANISOU 1789  C   ARG B1087     2024   1733   1260   -111    101     -6  F000 C  
ATOM   1790  O   ARG B1087       5.336  -4.774   7.057  1.00 15.47      F000 O  
ANISOU 1790  O   ARG B1087     2522   2164   1189   -230    199   -102  F000 O  
ATOM   1791  CB  ARG B1087       6.478  -3.334   4.488  1.00 13.71      F000 C  
ANISOU 1791  CB  ARG B1087     2158   1761   1287    105    -30    -71  F000 C  
ATOM   1792  CG  ARG B1087       6.008  -2.739   3.170  1.00 14.34      F000 C  
ANISOU 1792  CG  ARG B1087     2366   1926   1155    122   -108     79  F000 C  
ATOM   1793  CD  ARG B1087       6.703  -3.424   1.987  1.00 15.33      F000 C  
ANISOU 1793  CD  ARG B1087     2387   2089   1347    345    -35    -29  F000 C  
ATOM   1794  NE  ARG B1087       8.148  -3.165   1.975  1.00 15.89      F000 N  
ANISOU 1794  NE  ARG B1087     2444   2358   1236    445    -48    -62  F000 N  
ATOM   1795  CZ  ARG B1087       9.077  -4.015   2.414  1.00 16.60      F000 C  
ANISOU 1795  CZ  ARG B1087     2677   2143   1484    158   -215    -98  F000 C  
ATOM   1796  NH1 ARG B1087       8.750  -5.223   2.872  1.00 16.97      F000 N1+
ANISOU 1796  NH1 ARG B1087     2839   2081   1527    343   -453   -267  F000 N1+
ATOM   1797  NH2 ARG B1087      10.353  -3.657   2.376  1.00 18.06      F000 N  
ANISOU 1797  NH2 ARG B1087     3010   1958   1891    489   -447   -186  F000 N  
ATOM   1798  N   ASN B1088       6.901  -3.335   7.740  1.00 12.88      F000 N  
ANISOU 1798  N   ASN B1088     1797   1897   1199   -222     -7     32  F000 N  
ATOM   1799  CA  ASN B1088       7.214  -4.185   8.883  1.00 12.93      F000 C  
ANISOU 1799  CA  ASN B1088     1773   1859   1279     29      6    -92  F000 C  
ATOM   1800  C   ASN B1088       5.985  -4.444   9.756  1.00 13.15      F000 C  
ANISOU 1800  C   ASN B1088     1816   1981   1196   -171    -12   -114  F000 C  
ATOM   1801  O   ASN B1088       5.812  -5.540  10.273  1.00 15.83      F000 O  
ANISOU 1801  O   ASN B1088     1795   2498   1718   -237    289   -695  F000 O  
ATOM   1802  CB  ASN B1088       8.381  -3.632   9.707  1.00 11.97      F000 C  
ANISOU 1802  CB  ASN B1088     1560   1786   1200     96    -52    -92  F000 C  
ATOM   1803  CG  ASN B1088       8.004  -2.421  10.532  1.00 12.75      F000 C  
ANISOU 1803  CG  ASN B1088     1518   2028   1295     76    -12     -9  F000 C  
ATOM   1804  ND2 ASN B1088       8.240  -2.503  11.855  1.00 12.70      F000 N  
ANISOU 1804  ND2 ASN B1088     1617   1878   1328     13    281    135  F000 N  
ATOM   1805  OD1 ASN B1088       7.536  -1.415   9.987  1.00 12.76      F000 O  
ANISOU 1805  OD1 ASN B1088     1788   1761   1297     63   -207     11  F000 O  
ATOM   1806  N   LEU B1089       5.158  -3.432   9.956  1.00 13.27      F000 N  
ANISOU 1806  N   LEU B1089     2025   1684   1331   -190   -224    -21  F000 N  
ATOM   1807  CA  LEU B1089       3.957  -3.599  10.765  1.00 13.08      F000 C  
ANISOU 1807  CA  LEU B1089     1885   1706   1375    -46   -167    -52  F000 C  
ATOM   1808  C   LEU B1089       2.741  -3.981   9.952  1.00 13.86      F000 C  
ANISOU 1808  C   LEU B1089     2086   1919   1260   -125   -244     27  F000 C  
ATOM   1809  O   LEU B1089       1.850  -4.666  10.456  1.00 14.95      F000 O  
ANISOU 1809  O   LEU B1089     2203   2127   1351    -79   -500    -33  F000 O  
ATOM   1810  CB  LEU B1089       3.670  -2.351  11.590  1.00 14.51      F000 C  
ANISOU 1810  CB  LEU B1089     2111   1765   1633    -19   -232   -152  F000 C  
ATOM   1811  CG  LEU B1089       4.609  -2.167  12.774  1.00 15.99      F000 C  
ANISOU 1811  CG  LEU B1089     2150   2127   1796    -85    307   -252  F000 C  
ATOM   1812  CD1 LEU B1089       4.354  -0.848  13.486  1.00 20.35      F000 C  
ANISOU 1812  CD1 LEU B1089     2534   2649   2548   -392    -20   -418  F000 C  
ATOM   1813  CD2 LEU B1089       4.454  -3.319  13.724  1.00 19.01      F000 C  
ANISOU 1813  CD2 LEU B1089     2224   3062   1937    181    260    425  F000 C  
ATOM   1814  N   LEU B1090       2.691  -3.551   8.692  1.00 14.32      F000 N  
ANISOU 1814  N   LEU B1090     2246   1863   1333   -159   -335      1  F000 N  
ATOM   1815  CA  LEU B1090       1.621  -4.019   7.815  1.00 14.11      F000 C  
ANISOU 1815  CA  LEU B1090     2076   1816   1470    -56   -173     11  F000 C  
ATOM   1816  C   LEU B1090       1.623  -5.539   7.740  1.00 14.58      F000 C  
ANISOU 1816  C   LEU B1090     2190   1853   1496     23   -162     66  F000 C  
ATOM   1817  O   LEU B1090       0.563  -6.171   7.755  1.00 15.08      F000 O  
ANISOU 1817  O   LEU B1090     2183   2051   1492    -38   -247    110  F000 O  
ATOM   1818  CB  LEU B1090       1.753  -3.406   6.417  1.00 14.85      F000 C  
ANISOU 1818  CB  LEU B1090     2412   1718   1512   -133   -132    232  F000 C  
ATOM   1819  CG  LEU B1090       1.566  -1.895   6.374  1.00 15.82      F000 C  
ANISOU 1819  CG  LEU B1090     2346   2027   1637   -218   -262    238  F000 C  
ATOM   1820  CD1 LEU B1090       1.803  -1.374   4.965  1.00 17.12      F000 C  
ANISOU 1820  CD1 LEU B1090     2402   2423   1680   -139   -485    149  F000 C  
ATOM   1821  CD2 LEU B1090       0.188  -1.474   6.877  1.00 16.31      F000 C  
ANISOU 1821  CD2 LEU B1090     2137   2308   1750    -42   -208     53  F000 C  
ATOM   1822  N  ATHR B1091       2.807  -6.157   7.641  0.33 13.75      F000 N  
ANISOU 1822  N  ATHR B1091     2037   1795   1389     33    -77      5  F000 N  
ATOM   1823  N  BTHR B1091       2.804  -6.143   7.661  0.33 14.61      F000 N  
ANISOU 1823  N  BTHR B1091     2126   1889   1537     26    -98     10  F000 N  
ATOM   1824  N  CTHR B1091       2.824  -6.084   7.696  0.33 13.67      F000 N  
ANISOU 1824  N  CTHR B1091     2041   1758   1395     -1    -73     26  F000 N  
ATOM   1825  CA ATHR B1091       2.872  -7.628   7.607  0.33 14.04      F000 C  
ANISOU 1825  CA ATHR B1091     2001   1887   1444    105   -114    -27  F000 C  
ATOM   1826  CA BTHR B1091       2.871  -7.594   7.601  0.33 15.37      F000 C  
ANISOU 1826  CA BTHR B1091     2130   2027   1681     90   -162    -31  F000 C  
ATOM   1827  CA CTHR B1091       3.041  -7.499   7.612  0.33 13.58      F000 C  
ANISOU 1827  CA CTHR B1091     1939   1809   1409     13    -98    -16  F000 C  
ATOM   1828  C  ATHR B1091       2.380  -8.217   8.924  0.33 14.56      F000 C  
ANISOU 1828  C  ATHR B1091     2007   1990   1534    103   -138    -29  F000 C  
ATOM   1829  C  BTHR B1091       2.423  -8.232   8.917  0.33 15.39      F000 C  
ANISOU 1829  C  BTHR B1091     2088   2087   1670     93   -155    -32  F000 C  
ATOM   1830  C  CTHR B1091       2.552  -8.232   8.884  0.33 14.59      F000 C  
ANISOU 1830  C  CTHR B1091     2003   1992   1546     60   -108    -23  F000 C  
ATOM   1831  O  ATHR B1091       1.643  -9.206   8.930  0.33 15.47      F000 O  
ANISOU 1831  O  ATHR B1091     2288   2120   1467    183   -342    -63  F000 O  
ATOM   1832  O  BTHR B1091       1.760  -9.272   8.913  0.33 16.02      F000 O  
ANISOU 1832  O  BTHR B1091     2290   2199   1595    186   -322    -90  F000 O  
ATOM   1833  O  CTHR B1091       1.988  -9.326   8.807  0.33 15.01      F000 O  
ANISOU 1833  O  CTHR B1091     2086   2056   1561    189   -196   -169  F000 O  
ATOM   1834  CB ATHR B1091       4.290  -8.218   7.313  0.33 13.82      F000 C  
ANISOU 1834  CB ATHR B1091     1965   1846   1438     86    -62    -23  F000 C  
ATOM   1835  CB BTHR B1091       4.269  -8.117   7.226  0.33 16.12      F000 C  
ANISOU 1835  CB BTHR B1091     2237   2080   1807     36   -119    -29  F000 C  
ATOM   1836  CB CTHR B1091       4.535  -7.724   7.353  0.33 13.66      F000 C  
ANISOU 1836  CB CTHR B1091     2050   1757   1383   -123    -22     15  F000 C  
ATOM   1837  CG2ATHR B1091       4.633  -8.116   5.832  0.33 11.34      F000 C  
ANISOU 1837  CG2ATHR B1091     1800   1730    776    -13     65    -62  F000 C  
ATOM   1838  CG2BTHR B1091       5.249  -7.913   8.352  0.33 14.98      F000 C  
ANISOU 1838  CG2BTHR B1091     1830   2101   1757     61   -162    -66  F000 C  
ATOM   1839  CG2CTHR B1091       4.862  -9.181   7.355  0.33 12.08      F000 C  
ANISOU 1839  CG2CTHR B1091     1748   1606   1234   -307    139    126  F000 C  
ATOM   1840  OG1ATHR B1091       5.284  -7.548   8.093  0.33 13.66      F000 O  
ANISOU 1840  OG1ATHR B1091     1739   2035   1412    225    165    -20  F000 O  
ATOM   1841  OG1BTHR B1091       4.176  -9.510   6.927  0.33 20.23      F000 O  
ANISOU 1841  OG1BTHR B1091     2699   2548   2439    105   -324    -84  F000 O  
ATOM   1842  OG1CTHR B1091       4.885  -7.124   6.088  0.33 10.22      F000 O  
ANISOU 1842  OG1CTHR B1091     1570   1569    741   -362   -122   -135  F000 O  
ATOM   1843  N   GLN B1092       2.778  -7.613  10.038  1.00 15.15      F000 N  
ANISOU 1843  N   GLN B1092     2034   2242   1479    215   -194   -154  F000 N  
ATOM   1844  CA  GLN B1092       2.391  -8.163  11.336  1.00 15.30      F000 C  
ANISOU 1844  CA  GLN B1092     1941   2223   1646     96   -195   -115  F000 C  
ATOM   1845  C   GLN B1092       0.879  -8.206  11.488  1.00 16.33      F000 C  
ANISOU 1845  C   GLN B1092     2097   2343   1765    195   -269    -55  F000 C  
ATOM   1846  O   GLN B1092       0.368  -9.155  12.067  1.00 18.02      F000 O  
ANISOU 1846  O   GLN B1092     2347   2498   1998    145   -380   -157  F000 O  
ATOM   1847  CB  GLN B1092       3.003  -7.362  12.479  1.00 14.90      F000 C  
ANISOU 1847  CB  GLN B1092     1566   2585   1508     51   -163   -242  F000 C  
ATOM   1848  CG  GLN B1092       4.508  -7.510  12.618  1.00 13.28      F000 C  
ANISOU 1848  CG  GLN B1092     1391   2397   1255    108   -130   -224  F000 C  
ATOM   1849  CD  GLN B1092       4.964  -8.943  12.819  1.00 12.90      F000 C  
ANISOU 1849  CD  GLN B1092     1679   2437    782    311    122   -427  F000 C  
ATOM   1850  NE2 GLN B1092       4.425  -9.580  13.829  1.00 10.55      F000 N  
ANISOU 1850  NE2 GLN B1092     1166   2105    736    269     82   -372  F000 N  
ATOM   1851  OE1 GLN B1092       5.795  -9.480  12.041  1.00 17.70      F000 O  
ANISOU 1851  OE1 GLN B1092     2030   3135   1557    611     -1   -916  F000 O  
ATOM   1852  N   ILE B1093       0.155  -7.196  10.980  1.00 17.32      F000 N  
ANISOU 1852  N   ILE B1093     2292   2453   1833    302   -425   -137  F000 N  
ATOM   1853  CA  ILE B1093      -1.330  -7.227  11.046  1.00 18.15      F000 C  
ANISOU 1853  CA  ILE B1093     2195   2524   2174    137   -419   -161  F000 C  
ATOM   1854  C   ILE B1093      -2.002  -7.996   9.915  1.00 18.94      F000 C  
ANISOU 1854  C   ILE B1093     2213   2456   2525    211   -594    -67  F000 C  
ATOM   1855  O   ILE B1093      -3.235  -8.085   9.852  1.00 21.58      F000 O  
ANISOU 1855  O   ILE B1093     2533   2620   3043     -2   -793   -323  F000 O  
ATOM   1856  CB  ILE B1093      -1.985  -5.825  11.101  1.00 19.25      F000 C  
ANISOU 1856  CB  ILE B1093     2407   2592   2315    252   -256   -148  F000 C  
ATOM   1857  CG1 ILE B1093      -1.685  -5.022   9.843  1.00 17.66      F000 C  
ANISOU 1857  CG1 ILE B1093     2349   2525   1836    128   -407     46  F000 C  
ATOM   1858  CG2 ILE B1093      -1.576  -5.086  12.326  1.00 19.46      F000 C  
ANISOU 1858  CG2 ILE B1093     2259   2928   2205    271   -290    313  F000 C  
ATOM   1859  CD1 ILE B1093      -2.353  -3.682   9.808  1.00 19.72      F000 C  
ANISOU 1859  CD1 ILE B1093     2618   2651   2221     76   -104   -209  F000 C  
ATOM   1860  N   GLY B1094      -1.214  -8.549   9.006  1.00 17.90      F000 N  
ANISOU 1860  N   GLY B1094     2316   2331   2151     59   -486   -237  F000 N  
ATOM   1861  CA  GLY B1094      -1.774  -9.354   7.928  1.00 18.72      F000 C  
ANISOU 1861  CA  GLY B1094     2291   2386   2433    -19   -444     43  F000 C  
ATOM   1862  C   GLY B1094      -2.406  -8.520   6.829  1.00 19.04      F000 C  
ANISOU 1862  C   GLY B1094     2402   2372   2457    -28   -434     95  F000 C  
ATOM   1863  O   GLY B1094      -3.319  -8.977   6.136  1.00 20.90      F000 O  
ANISOU 1863  O   GLY B1094     2450   2744   2745   -304   -844    357  F000 O  
ATOM   1864  N   CYS B1095      -1.894  -7.310   6.648  1.00 17.57      F000 N  
ANISOU 1864  N   CYS B1095     2284   2143   2250     14   -511    238  F000 N  
ATOM   1865  CA  CYS B1095      -2.381  -6.424   5.600  1.00 17.20      F000 C  
ANISOU 1865  CA  CYS B1095     2243   2126   2164    106   -353     51  F000 C  
ATOM   1866  C   CYS B1095      -1.790  -6.829   4.252  1.00 18.32      F000 C  
ANISOU 1866  C   CYS B1095     2475   2209   2275     79   -376    121  F000 C  
ATOM   1867  O   CYS B1095      -0.571  -6.988   4.120  1.00 19.93      F000 O  
ANISOU 1867  O   CYS B1095     3120   2174   2277    248   -714    155  F000 O  
ATOM   1868  CB  CYS B1095      -2.000  -4.989   5.939  1.00 18.04      F000 C  
ANISOU 1868  CB  CYS B1095     2270   2325   2260    120   -542     98  F000 C  
ATOM   1869  SG  CYS B1095      -2.607  -3.779   4.760  1.00 18.68      F000 S  
ANISOU 1869  SG  CYS B1095     2375   2447   2274   -152   -699    435  F000 S  
ATOM   1870  N   THR B1096      -2.664  -7.002   3.260  1.00 16.88      F000 N  
ANISOU 1870  N   THR B1096     2321   2203   1889     11   -304    116  F000 N  
ATOM   1871  CA  THR B1096      -2.249  -7.359   1.921  1.00 17.22      F000 C  
ANISOU 1871  CA  THR B1096     2187   2175   2179    123   -279      0  F000 C  
ATOM   1872  C   THR B1096      -2.805  -6.344   0.938  1.00 16.69      F000 C  
ANISOU 1872  C   THR B1096     2072   2243   2026    116   -207     75  F000 C  
ATOM   1873  O   THR B1096      -3.772  -5.633   1.229  1.00 16.87      F000 O  
ANISOU 1873  O   THR B1096     2177   2146   2085     -4   -351     14  F000 O  
ATOM   1874  CB  THR B1096      -2.749  -8.768   1.514  1.00 18.82      F000 C  
ANISOU 1874  CB  THR B1096     2498   2426   2224     67   -294    -40  F000 C  
ATOM   1875  CG2 THR B1096      -2.069  -9.840   2.356  1.00 19.75      F000 C  
ANISOU 1875  CG2 THR B1096     2441   2674   2389    224   -448   -142  F000 C  
ATOM   1876  OG1 THR B1096      -4.166  -8.861   1.693  1.00 19.18      F000 O  
ANISOU 1876  OG1 THR B1096     2162   2517   2609     66   -134    -88  F000 O  
ATOM   1877  N   LEU B1097      -2.171  -6.279  -0.225  1.00 15.86      F000 N  
ANISOU 1877  N   LEU B1097     1954   2068   2003    180   -231    -27  F000 N  
ATOM   1878  CA  LEU B1097      -2.759  -5.613  -1.379  1.00 15.51      F000 C  
ANISOU 1878  CA  LEU B1097     2004   2024   1863    143   -134     52  F000 C  
ATOM   1879  C   LEU B1097      -3.542  -6.624  -2.207  1.00 15.64      F000 C  
ANISOU 1879  C   LEU B1097     1828   2064   2050    119   -135     61  F000 C  
ATOM   1880  O   LEU B1097      -3.074  -7.742  -2.428  1.00 17.58      F000 O  
ANISOU 1880  O   LEU B1097     1832   2432   2413    242     24    223  F000 O  
ATOM   1881  CB  LEU B1097      -1.662  -5.012  -2.248  1.00 15.32      F000 C  
ANISOU 1881  CB  LEU B1097     2043   1937   1838    204   -222    -43  F000 C  
ATOM   1882  CG  LEU B1097      -0.906  -3.828  -1.655  1.00 15.84      F000 C  
ANISOU 1882  CG  LEU B1097     2078   2107   1832    104   -265     76  F000 C  
ATOM   1883  CD1 LEU B1097       0.434  -3.637  -2.356  1.00 17.38      F000 C  
ANISOU 1883  CD1 LEU B1097     2327   2238   2037   -197    -42    195  F000 C  
ATOM   1884  CD2 LEU B1097      -1.744  -2.555  -1.719  1.00 17.07      F000 C  
ANISOU 1884  CD2 LEU B1097     2147   2404   1932     16    -87    204  F000 C  
ATOM   1885  N   ASN B1098      -4.713  -6.215  -2.686  1.00 16.05      F000 N  
ANISOU 1885  N   ASN B1098     1785   2191   2122     48    -76    114  F000 N  
ATOM   1886  CA  ASN B1098      -5.596  -7.119  -3.407  1.00 16.53      F000 C  
ANISOU 1886  CA  ASN B1098     1980   2198   2100    128    -35     90  F000 C  
ATOM   1887  C   ASN B1098      -6.230  -6.421  -4.585  1.00 17.53      F000 C  
ANISOU 1887  C   ASN B1098     2078   2414   2166     44    -60    193  F000 C  
ATOM   1888  O   ASN B1098      -6.745  -5.308  -4.462  1.00 17.14      F000 O  
ANISOU 1888  O   ASN B1098     1854   2382   2276   -128    -37    221  F000 O  
ATOM   1889  CB  ASN B1098      -6.704  -7.633  -2.498  1.00 18.36      F000 C  
ANISOU 1889  CB  ASN B1098     2097   2526   2350   -117     11    133  F000 C  
ATOM   1890  CG  ASN B1098      -6.178  -8.450  -1.363  1.00 18.91      F000 C  
ANISOU 1890  CG  ASN B1098     1888   2634   2663   -114   -192     26  F000 C  
ATOM   1891  ND2 ASN B1098      -5.759  -7.777  -0.306  1.00 19.37      F000 N  
ANISOU 1891  ND2 ASN B1098     2282   2400   2678   -357   -430    249  F000 N  
ATOM   1892  OD1 ASN B1098      -6.133  -9.682  -1.435  1.00 25.39      F000 O  
ANISOU 1892  OD1 ASN B1098     2360   3956   3330   -163   -139    272  F000 O  
ATOM   1893  N   PHE B1099      -6.215  -7.093  -5.723  1.00 19.17      F000 N  
ANISOU 1893  N   PHE B1099     2150   2741   2392     56     29    199  F000 N  
ATOM   1894  CA  PHE B1099      -6.993  -6.632  -6.858  1.00 18.99      F000 C  
ANISOU 1894  CA  PHE B1099     2296   2513   2404     33     88    240  F000 C  
ATOM   1895  C   PHE B1099      -7.277  -7.774  -7.811  1.00 20.91      F000 C  
ANISOU 1895  C   PHE B1099     2402   2881   2660      0     96    152  F000 C  
ATOM   1896  O   PHE B1099      -6.779  -8.876  -7.604  1.00 22.34      F000 O  
ANISOU 1896  O   PHE B1099     2409   3208   2870    -25    319    365  F000 O  
ATOM   1897  CB  PHE B1099      -6.313  -5.464  -7.582  1.00 20.46      F000 C  
ANISOU 1897  CB  PHE B1099     2519   2663   2588    -32     34    197  F000 C  
ATOM   1898  CG  PHE B1099      -4.904  -5.734  -8.021  1.00 19.94      F000 C  
ANISOU 1898  CG  PHE B1099     2172   2904   2497    -95    159    292  F000 C  
ATOM   1899  CD1 PHE B1099      -4.622  -6.044  -9.344  1.00 23.34      F000 C  
ANISOU 1899  CD1 PHE B1099     2557   2924   3386    -74     36     51  F000 C  
ATOM   1900  CD2 PHE B1099      -3.856  -5.640  -7.123  1.00 21.72      F000 C  
ANISOU 1900  CD2 PHE B1099     2777   2794   2679      7   -248    202  F000 C  
ATOM   1901  CE1 PHE B1099      -3.324  -6.275  -9.757  1.00 23.87      F000 C  
ANISOU 1901  CE1 PHE B1099     2869   3040   3157   -120    300     77  F000 C  
ATOM   1902  CE2 PHE B1099      -2.562  -5.862  -7.529  1.00 23.66      F000 C  
ANISOU 1902  CE2 PHE B1099     2968   2894   3128    -12   -124    355  F000 C  
ATOM   1903  CZ  PHE B1099      -2.289  -6.190  -8.845  1.00 24.81      F000 C  
ANISOU 1903  CZ  PHE B1099     3166   3069   3190    133     17    135  F000 C  
ATOM   1904  OXT PHE B1099      -8.044  -7.589  -8.756  1.00 22.48      F000 O1-
TER   
CONECT  114  115  116
CONECT  115  114
CONECT  116  114  117  118
CONECT  117  116
CONECT  118  116
CONECT 1066 1067 1068
CONECT 1067 1066
CONECT 1068 1066 1069 1070
CONECT 1069 1068
CONECT 1070 1068
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.