CNRS Nantes University UFIP UFIP
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***  jyjang_2  ***

elNémo ID: 21060108063138685

Job options:

ID        	=	 21060108063138685
JOBID     	=	 jyjang_2
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 jyjang_2

HETATM    1  N   MSE A   1      56.669 -29.384 -25.083  1.00 31.03           N  
ANISOU    1  N   MSE A   1     4691   3810   3288   1443     43     99       N  
HETATM    2  CA  MSE A   1      56.173 -30.364 -26.058  1.00 28.20           C  
ANISOU    2  CA  MSE A   1     4352   3450   2911   1447     37    100       C  
HETATM    3  C   MSE A   1      55.006 -31.168 -25.502  1.00 26.08           C  
ANISOU    3  C   MSE A   1     4077   3189   2643   1442     21     91       C  
HETATM    4  O   MSE A   1      54.015 -31.387 -26.193  1.00 29.52           O  
ANISOU    4  O   MSE A   1     4524   3619   3075   1444     10     88       O  
HETATM    5  CB  MSE A   1      57.275 -31.323 -26.524  1.00 43.77           C  
ANISOU    5  CB  MSE A   1     6338   5427   4864   1450     49    107       C  
HETATM    6  CG  MSE A   1      56.769 -32.519 -27.376  1.00 24.93           C  
ANISOU    6  CG  MSE A   1     3972   3043   2459   1453     42    106       C  
HETATM    7  CE  MSE A   1      55.590 -33.606 -29.843  1.00 27.00           C  
ANISOU    7  CE  MSE A   1     4276   3291   2691   1464     29    107       C  
HETATM    8 SE   MSE A   1      56.882 -32.259 -29.327  1.00139.81          SE  
ANISOU    8 SE   MSE A   1    18551  17576  16992   1464     46    114      SE  
ATOM      9  N   LYS A   2      55.118 -31.631 -24.261  1.00 25.29           N  
ANISOU    9  N   LYS A   2     3959   3101   2549   1435     21     86       N  
ATOM     10  CA  LYS A   2      53.953 -32.217 -23.605  1.00 26.49           C  
ANISOU   10  CA  LYS A   2     4100   3259   2705   1430      6     77       C  
ATOM     11  C   LYS A   2      53.511 -31.408 -22.378  1.00 30.06           C  
ANISOU   11  C   LYS A   2     4527   3714   3179   1423      1     70       C  
ATOM     12  O   LYS A   2      54.299 -31.065 -21.499  1.00 17.01           O  
ANISOU   12  O   LYS A   2     2860   2067   1535   1420     10     71       O  
ATOM     13  CB  LYS A   2      54.137 -33.696 -23.288  1.00 29.60           C  
ANISOU   13  CB  LYS A   2     4496   3664   3085   1428      6     76       C  
ATOM     14  CG  LYS A   2      52.813 -34.390 -23.040  1.00 36.48           C  
ANISOU   14  CG  LYS A   2     5364   4539   3957   1424    -11     67       C  
ATOM     15  CD  LYS A   2      52.916 -35.890 -23.299  1.00 45.82           C  
ANISOU   15  CD  LYS A   2     6559   5730   5122   1424    -11     67       C  
ATOM     16  CE  LYS A   2      51.603 -36.558 -22.947  1.00 46.87           C  
ANISOU   16  CE  LYS A   2     6687   5867   5257   1420    -27     59       C  
ATOM     17  NZ  LYS A   2      51.500 -37.897 -23.551  1.00 45.44           N1+
ANISOU   17  NZ  LYS A   2     6521   5688   5057   1422    -30     59       N1+
ATOM     18  N   LEU A   3      52.227 -31.103 -22.348  1.00 28.55           N  
ANISOU   18  N   LEU A   3     4333   3519   2997   1422    -13     64       N  
ATOM     19  CA  LEU A   3      51.714 -30.110 -21.449  1.00 28.43           C  
ANISOU   19  CA  LEU A   3     4298   3503   3003   1417    -19     58       C  
ATOM     20  C   LEU A   3      50.409 -30.610 -20.825  1.00 32.36           C  
ANISOU   20  C   LEU A   3     4785   4006   3505   1412    -34     49       C  
ATOM     21  O   LEU A   3      49.525 -31.149 -21.532  1.00 22.97           O  
ANISOU   21  O   LEU A   3     3608   2812   2306   1414    -45     47       O  
ATOM     22  CB  LEU A   3      51.513 -28.828 -22.236  1.00 30.45           C  
ANISOU   22  CB  LEU A   3     4560   3744   3265   1422    -19     61       C  
ATOM     23  CG  LEU A   3      51.449 -27.492 -21.517  1.00 37.34           C  
ANISOU   23  CG  LEU A   3     5414   4613   4159   1419    -18     58       C  
ATOM     24  CD1 LEU A   3      52.324 -26.456 -22.212  1.00 29.87           C  
ANISOU   24  CD1 LEU A   3     4476   3657   3216   1424     -6     66       C  
ATOM     25  CD2 LEU A   3      49.998 -27.059 -21.502  1.00 40.68           C  
ANISOU   25  CD2 LEU A   3     5833   5032   4593   1417    -34     51       C  
ATOM     26  N   SER A   4      50.314 -30.468 -19.493  1.00 29.54           N  
ANISOU   26  N   SER A   4     4406   3658   3162   1405    -36     43       N  
ATOM     27  CA  SER A   4      49.160 -30.957 -18.742  1.00 18.18           C  
ANISOU   27  CA  SER A   4     2955   2225   1729   1399    -50     34       C  
ATOM     28  C   SER A   4      48.544 -29.832 -17.963  1.00 20.36           C  
ANISOU   28  C   SER A   4     3211   2499   2026   1395    -55     28       C  
ATOM     29  O   SER A   4      49.215 -29.232 -17.134  1.00 27.92           O  
ANISOU   29  O   SER A   4     4153   3459   2994   1392    -47     28       O  
ATOM     30  CB  SER A   4      49.561 -32.078 -17.788  1.00 20.06           C  
ANISOU   30  CB  SER A   4     3182   2478   1962   1394    -47     32       C  
ATOM     31  OG  SER A   4      48.429 -32.624 -17.121  1.00 22.19           O  
ANISOU   31  OG  SER A   4     3442   2754   2236   1389    -60     24       O  
ATOM     32  N   ILE A   5      47.270 -29.550 -18.234  1.00 16.86           N  
ANISOU   32  N   ILE A   5     2770   2049   1588   1395    -69     24       N  
ATOM     33  CA  ILE A   5      46.526 -28.477 -17.559  1.00 16.87           C  
ANISOU   33  CA  ILE A   5     2753   2047   1609   1391    -76     18       C  
ATOM     34  C   ILE A   5      45.612 -29.049 -16.509  1.00 25.99           C  
ANISOU   34  C   ILE A   5     3892   3212   2771   1384    -87      9       C  
ATOM     35  O   ILE A   5      44.705 -29.802 -16.821  1.00 28.17           O  
ANISOU   35  O   ILE A   5     4175   3488   3039   1384    -98      6       O  
ATOM     36  CB  ILE A   5      45.597 -27.726 -18.526  1.00 16.99           C  
ANISOU   36  CB  ILE A   5     2779   2049   1627   1396    -85     18       C  
ATOM     37  CG1 ILE A   5      46.395 -27.034 -19.632  1.00 30.44           C  
ANISOU   37  CG1 ILE A   5     4500   3741   3326   1403    -75     26       C  
ATOM     38  CG2 ILE A   5      44.799 -26.713 -17.788  1.00 16.99           C  
ANISOU   38  CG2 ILE A   5     2761   2047   1647   1392    -93     11       C  
ATOM     39  CD1 ILE A   5      45.608 -26.852 -20.923  1.00 29.61           C  
ANISOU   39  CD1 ILE A   5     4413   3624   3213   1409    -84     28       C  
ATOM     40  N   ILE A   6      45.831 -28.684 -15.256  1.00 29.32           N  
ANISOU   40  N   ILE A   6     4292   3642   3207   1378    -84      4       N  
ATOM     41  CA  ILE A   6      45.025 -29.238 -14.182  1.00 24.08           C  
ANISOU   41  CA  ILE A   6     3611   2988   2549   1371    -93     -4       C  
ATOM     42  C   ILE A   6      44.033 -28.169 -13.776  1.00 22.97           C  
ANISOU   42  C   ILE A   6     3458   2842   2427   1369   -102    -10       C  
ATOM     43  O   ILE A   6      44.435 -27.057 -13.473  1.00 25.60           O  
ANISOU   43  O   ILE A   6     3782   3172   2773   1369    -96    -10       O  
ATOM     44  CB  ILE A   6      45.919 -29.726 -13.001  1.00 16.47           C  
ANISOU   44  CB  ILE A   6     2632   2038   1587   1366    -84     -5       C  
ATOM     45  CG1 ILE A   6      46.889 -30.804 -13.505  1.00 16.44           C  
ANISOU   45  CG1 ILE A   6     2644   2039   1565   1369    -75      1       C  
ATOM     46  CG2 ILE A   6      45.067 -30.285 -11.870  1.00 16.36           C  
ANISOU   46  CG2 ILE A   6     2601   2035   1581   1358    -93    -14       C  
ATOM     47  CD1 ILE A   6      47.868 -31.319 -12.487  1.00 23.38           C  
ANISOU   47  CD1 ILE A   6     3509   2930   2442   1364    -65      1       C  
ATOM     48  N   LEU A   7      42.739 -28.487 -13.831  1.00 16.62           N  
ANISOU   48  N   LEU A   7     2654   2037   1623   1367   -116    -15       N  
ATOM     49  CA  LEU A   7      41.697 -27.529 -13.447  1.00 23.01           C  
ANISOU   49  CA  LEU A   7     3452   2842   2450   1365   -126    -21       C  
ATOM     50  C   LEU A   7      40.526 -28.178 -12.720  1.00 27.22           C  
ANISOU   50  C   LEU A   7     3973   3382   2986   1359   -139    -29       C  
ATOM     51  O   LEU A   7      40.270 -29.361 -12.900  1.00 31.01           O  
ANISOU   51  O   LEU A   7     4461   3866   3454   1359   -143    -29       O  
ATOM     52  CB  LEU A   7      41.182 -26.736 -14.656  1.00 18.91           C  
ANISOU   52  CB  LEU A   7     2947   2307   1930   1371   -131    -18       C  
ATOM     53  CG  LEU A   7      40.620 -27.493 -15.854  1.00 19.35           C  
ANISOU   53  CG  LEU A   7     3025   2357   1970   1376   -139    -15       C  
ATOM     54  CD1 LEU A   7      39.204 -27.979 -15.609  1.00 21.05           C  
ANISOU   54  CD1 LEU A   7     3236   2574   2188   1373   -155    -22       C  
ATOM     55  CD2 LEU A   7      40.688 -26.605 -17.076  1.00 16.97           C  
ANISOU   55  CD2 LEU A   7     2740   2041   1667   1383   -138    -10       C  
ATOM     56  N   GLY A   8      39.807 -27.392 -11.918  1.00 21.20           N  
ANISOU   56  N   GLY A   8     3193   2619   2241   1355   -145    -35       N  
ATOM     57  CA  GLY A   8      38.699 -27.917 -11.149  1.00 20.98           C  
ANISOU   57  CA  GLY A   8     3154   2600   2220   1349   -157    -43       C  
ATOM     58  C   GLY A   8      37.491 -27.011 -11.002  1.00 33.29           C  
ANISOU   58  C   GLY A   8     4704   4152   3793   1348   -168    -48       C  
ATOM     59  O   GLY A   8      36.496 -27.391 -10.382  1.00 42.69           O  
ANISOU   59  O   GLY A   8     5885   5348   4989   1343   -178    -54       O  
ATOM     60  N   THR A   9      37.559 -25.809 -11.563  1.00 32.98           N  
ANISOU   60  N   THR A   9     4669   4101   3761   1352   -166    -46       N  
ATOM     61  CA  THR A   9      36.437 -24.880 -11.470  1.00 30.89           C  
ANISOU   61  CA  THR A   9     4397   3830   3511   1351   -177    -51       C  
ATOM     62  C   THR A   9      36.158 -24.159 -12.776  1.00 32.61           C  
ANISOU   62  C   THR A   9     4633   4033   3726   1358   -180    -46       C  
ATOM     63  O   THR A   9      36.971 -24.187 -13.682  1.00 35.23           O  
ANISOU   63  O   THR A   9     4980   4359   4047   1363   -172    -39       O  
ATOM     64  CB  THR A   9      36.667 -23.818 -10.393  1.00 29.20           C  
ANISOU   64  CB  THR A   9     4162   3619   3315   1346   -172    -55       C  
ATOM     65  CG2 THR A   9      36.847 -24.477  -9.061  1.00 18.01           C  
ANISOU   65  CG2 THR A   9     2726   2216   1901   1339   -170    -60       C  
ATOM     66  OG1 THR A   9      37.818 -23.021 -10.721  1.00 34.17           O  
ANISOU   66  OG1 THR A   9     4795   4243   3946   1350   -159    -50       O  
ATOM     67  N   ARG A  10      35.011 -23.493 -12.854  1.00 30.94           N  
ANISOU   67  N   ARG A  10     4417   3814   3523   1357   -191    -50       N  
ATOM     68  CA  ARG A  10      34.671 -22.720 -14.042  1.00 26.23           C  
ANISOU   68  CA  ARG A  10     3836   3204   2927   1364   -195    -46       C  
ATOM     69  C   ARG A  10      35.438 -21.408 -14.177  1.00 23.71           C  
ANISOU   69  C   ARG A  10     3515   2877   2617   1366   -185    -43       C  
ATOM     70  O   ARG A  10      35.800 -21.027 -15.279  1.00 26.37           O  
ANISOU   70  O   ARG A  10     3869   3203   2947   1373   -182    -37       O  
ATOM     71  CB  ARG A  10      33.167 -22.451 -14.119  1.00 22.54           C  
ANISOU   71  CB  ARG A  10     3366   2731   2466   1362   -210    -52       C  
ATOM     72  CG  ARG A  10      32.343 -23.663 -14.435  1.00 21.31           C  
ANISOU   72  CG  ARG A  10     3219   2578   2299   1362   -221    -53       C  
ATOM     73  CD  ARG A  10      30.883 -23.325 -14.507  1.00 27.11           C  
ANISOU   73  CD  ARG A  10     3950   3307   3042   1360   -236    -58       C  
ATOM     74  NE  ARG A  10      30.105 -24.511 -14.828  1.00 40.57           N  
ANISOU   74  NE  ARG A  10     5663   5014   4736   1360   -246    -60       N  
ATOM     75  CZ  ARG A  10      28.811 -24.512 -15.104  1.00 50.69           C  
ANISOU   75  CZ  ARG A  10     6947   6292   6021   1359   -260    -63       C  
ATOM     76  NH1 ARG A  10      28.125 -23.374 -15.099  1.00 57.53           N1+
ANISOU   76  NH1 ARG A  10     7808   7151   6901   1359   -265    -66       N1+
ATOM     77  NH2 ARG A  10      28.211 -25.659 -15.382  1.00 49.56           N  
ANISOU   77  NH2 ARG A  10     6811   6151   5868   1358   -268    -64       N  
ATOM     78  N   PRO A  11      35.657 -20.687 -13.067  1.00 24.14           N  
ANISOU   78  N   PRO A  11     3549   2937   2688   1362   -181    -48       N  
ATOM     79  CA  PRO A  11      36.458 -19.489 -13.300  1.00 19.09           C  
ANISOU   79  CA  PRO A  11     2909   2289   2056   1365   -171    -44       C  
ATOM     80  C   PRO A  11      37.836 -19.870 -13.832  1.00 19.87           C  
ANISOU   80  C   PRO A  11     3020   2387   2141   1369   -157    -36       C  
ATOM     81  O   PRO A  11      38.420 -19.133 -14.643  1.00 23.25           O  
ANISOU   81  O   PRO A  11     3459   2806   2569   1374   -151    -30       O  
ATOM     82  CB  PRO A  11      36.526 -18.848 -11.901  1.00 18.66           C  
ANISOU   82  CB  PRO A  11     2828   2241   2019   1358   -168    -51       C  
ATOM     83  CG  PRO A  11      35.293 -19.279 -11.251  1.00 16.96           C  
ANISOU   83  CG  PRO A  11     2603   2032   1809   1353   -181    -58       C  
ATOM     84  CD  PRO A  11      35.062 -20.681 -11.714  1.00 24.50           C  
ANISOU   84  CD  PRO A  11     3572   2992   2746   1354   -186    -56       C  
ATOM     85  N   GLU A  12      38.311 -21.039 -13.402  1.00 19.26           N  
ANISOU   85  N   GLU A  12     2941   2322   2054   1366   -154    -36       N  
ATOM     86  CA  GLU A  12      39.541 -21.645 -13.927  1.00 21.02           C  
ANISOU   86  CA  GLU A  12     3177   2546   2262   1370   -142    -29       C  
ATOM     87  C   GLU A  12      39.452 -21.943 -15.423  1.00 22.75           C  
ANISOU   87  C   GLU A  12     3422   2755   2466   1377   -144    -22       C  
ATOM     88  O   GLU A  12      40.317 -21.530 -16.197  1.00 30.34           O  
ANISOU   88  O   GLU A  12     4396   3710   3423   1382   -134    -15       O  
ATOM     89  CB  GLU A  12      39.923 -22.903 -13.122  1.00 16.87           C  
ANISOU   89  CB  GLU A  12     2645   2036   1729   1365   -139    -31       C  
ATOM     90  CG  GLU A  12      40.889 -22.576 -11.996  1.00 16.80           C  
ANISOU   90  CG  GLU A  12     2617   2035   1730   1360   -128    -32       C  
ATOM     91  CD  GLU A  12      40.984 -23.617 -10.876  1.00 23.89           C  
ANISOU   91  CD  GLU A  12     3502   2948   2626   1354   -127    -37       C  
ATOM     92  OE1 GLU A  12      41.333 -23.197  -9.747  1.00 20.14           O  
ANISOU   92  OE1 GLU A  12     3007   2480   2164   1348   -122    -41       O  
ATOM     93  OE2 GLU A  12      40.756 -24.832 -11.113  1.00 21.27           O1-
ANISOU   93  OE2 GLU A  12     3179   2621   2280   1354   -131    -36       O1-
ATOM     94  N   ILE A  13      38.398 -22.646 -15.824  1.00 21.96           N  
ANISOU   94  N   ILE A  13     3330   2654   2358   1377   -156    -24       N  
ATOM     95  CA  ILE A  13      38.211 -22.997 -17.222  1.00 23.04           C  
ANISOU   95  CA  ILE A  13     3491   2782   2480   1384   -160    -19       C  
ATOM     96  C   ILE A  13      38.216 -21.748 -18.093  1.00 22.98           C  
ANISOU   96  C   ILE A  13     3493   2761   2478   1389   -158    -15       C  
ATOM     97  O   ILE A  13      38.939 -21.698 -19.086  1.00 24.29           O  
ANISOU   97  O   ILE A  13     3676   2920   2633   1395   -151     -7       O  
ATOM     98  CB  ILE A  13      36.930 -23.816 -17.468  1.00 25.63           C  
ANISOU   98  CB  ILE A  13     3824   3111   2802   1383   -175    -23       C  
ATOM     99  CG1 ILE A  13      36.973 -25.136 -16.683  1.00 25.94           C  
ANISOU   99  CG1 ILE A  13     3856   3164   2835   1378   -176    -26       C  
ATOM    100  CG2 ILE A  13      36.763 -24.083 -18.966  1.00 21.56           C  
ANISOU  100  CG2 ILE A  13     3335   2586   2272   1389   -178    -17       C  
ATOM    101  CD1 ILE A  13      35.692 -25.905 -16.683  1.00 17.03           C  
ANISOU  101  CD1 ILE A  13     2729   2037   1704   1375   -190    -31       C  
ATOM    102  N   ILE A  14      37.441 -20.739 -17.705  1.00 19.18           N  
ANISOU  102  N   ILE A  14     3000   2276   2014   1387   -165    -20       N  
ATOM    103  CA  ILE A  14      37.436 -19.456 -18.410  1.00 18.99           C  
ANISOU  103  CA  ILE A  14     2982   2238   1997   1392   -164    -17       C  
ATOM    104  C   ILE A  14      38.835 -18.847 -18.544  1.00 23.64           C  
ANISOU  104  C   ILE A  14     3571   2824   2586   1395   -148    -10       C  
ATOM    105  O   ILE A  14      39.310 -18.608 -19.649  1.00 29.13           O  
ANISOU  105  O   ILE A  14     4285   3510   3272   1401   -142     -3       O  
ATOM    106  CB  ILE A  14      36.473 -18.448 -17.750  1.00 17.47           C  
ANISOU  106  CB  ILE A  14     2772   2043   1823   1388   -172    -23       C  
ATOM    107  CG1 ILE A  14      35.040 -18.969 -17.828  1.00 18.01           C  
ANISOU  107  CG1 ILE A  14     2842   2111   1890   1386   -189    -29       C  
ATOM    108  CG2 ILE A  14      36.582 -17.094 -18.392  1.00 17.59           C  
ANISOU  108  CG2 ILE A  14     2792   2045   1847   1393   -170    -20       C  
ATOM    109  CD1 ILE A  14      34.116 -18.245 -16.970  1.00 17.45           C  
ANISOU  109  CD1 ILE A  14     2751   2041   1836   1382   -197    -36       C  
ATOM    110  N   LYS A  15      39.520 -18.626 -17.433  1.00 23.08           N  
ANISOU  110  N   LYS A  15     3483   2762   2526   1390   -139    -13       N  
ATOM    111  CA  LYS A  15      40.816 -17.959 -17.523  1.00 20.35           C  
ANISOU  111  CA  LYS A  15     3137   2413   2182   1393   -124     -7       C  
ATOM    112  C   LYS A  15      41.844 -18.789 -18.307  1.00 22.29           C  
ANISOU  112  C   LYS A  15     3400   2659   2409   1397   -114      1       C  
ATOM    113  O   LYS A  15      42.856 -18.251 -18.776  1.00 20.65           O  
ANISOU  113  O   LYS A  15     3200   2446   2200   1401   -102      7       O  
ATOM    114  CB  LYS A  15      41.338 -17.629 -16.130  1.00 17.36           C  
ANISOU  114  CB  LYS A  15     2734   2043   1818   1386   -118    -12       C  
ATOM    115  CG  LYS A  15      40.349 -16.872 -15.296  1.00 26.56           C  
ANISOU  115  CG  LYS A  15     3881   3209   3002   1381   -127    -21       C  
ATOM    116  CD  LYS A  15      41.035 -15.728 -14.643  1.00 28.78           C  
ANISOU  116  CD  LYS A  15     4148   3489   3300   1379   -118    -22       C  
ATOM    117  CE  LYS A  15      40.290 -15.247 -13.437  1.00 30.55           C  
ANISOU  117  CE  LYS A  15     4348   3717   3541   1373   -124    -31       C  
ATOM    118  NZ  LYS A  15      41.238 -14.416 -12.701  1.00 17.28           N1+
ANISOU  118  NZ  LYS A  15     2653   2038   1874   1370   -113    -32       N1+
ATOM    119  N   LEU A  16      41.573 -20.089 -18.459  1.00 23.70           N  
ANISOU  119  N   LEU A  16     3587   2844   2572   1396   -119      1       N  
ATOM    120  CA  LEU A  16      42.501 -20.985 -19.149  1.00 17.40           C  
ANISOU  120  CA  LEU A  16     2807   2049   1757   1400   -110      8       C  
ATOM    121  C   LEU A  16      42.143 -21.199 -20.613  1.00 31.53           C  
ANISOU  121  C   LEU A  16     4620   3827   3531   1407   -115     13       C  
ATOM    122  O   LEU A  16      42.992 -21.595 -21.408  1.00 31.34           O  
ANISOU  122  O   LEU A  16     4613   3802   3494   1412   -106     20       O  
ATOM    123  CB  LEU A  16      42.630 -22.326 -18.414  1.00 17.28           C  
ANISOU  123  CB  LEU A  16     2785   2047   1732   1396   -111      5       C  
ATOM    124  CG  LEU A  16      43.621 -22.323 -17.240  1.00 19.76           C  
ANISOU  124  CG  LEU A  16     3081   2372   2054   1391   -100      3       C  
ATOM    125  CD1 LEU A  16      43.527 -23.607 -16.429  1.00 17.05           C  
ANISOU  125  CD1 LEU A  16     2731   2044   1705   1386   -102     -1       C  
ATOM    126  CD2 LEU A  16      45.032 -22.062 -17.740  1.00 17.23           C  
ANISOU  126  CD2 LEU A  16     2769   2048   1727   1395    -84     12       C  
ATOM    127  N   SER A  17      40.896 -20.910 -20.973  1.00 25.30           N  
ANISOU  127  N   SER A  17     3834   3032   2746   1408   -129      9       N  
ATOM    128  CA  SER A  17      40.464 -21.061 -22.354  1.00 23.22           C  
ANISOU  128  CA  SER A  17     3594   2759   2471   1414   -134     14       C  
ATOM    129  C   SER A  17      41.328 -20.313 -23.375  1.00 20.68           C  
ANISOU  129  C   SER A  17     3288   2427   2145   1421   -123     22       C  
ATOM    130  O   SER A  17      41.496 -20.785 -24.475  1.00 22.56           O  
ANISOU  130  O   SER A  17     3545   2659   2367   1426   -122     28       O  
ATOM    131  CB  SER A  17      38.994 -20.701 -22.518  1.00 23.92           C  
ANISOU  131  CB  SER A  17     3681   2841   2566   1413   -150      8       C  
ATOM    132  OG  SER A  17      38.780 -19.351 -22.193  1.00 28.54           O  
ANISOU  132  OG  SER A  17     4255   3421   3169   1412   -150      6       O  
ATOM    133  N   PRO A  18      41.874 -19.144 -23.023  1.00 26.05           N  
ANISOU  133  N   PRO A  18     3956   3102   2838   1421   -115     23       N  
ATOM    134  CA  PRO A  18      42.770 -18.594 -24.049  1.00 24.75           C  
ANISOU  134  CA  PRO A  18     3808   2928   2667   1427   -104     32       C  
ATOM    135  C   PRO A  18      44.059 -19.384 -24.201  1.00 29.15           C  
ANISOU  135  C   PRO A  18     4373   3491   3211   1429    -90     39       C  
ATOM    136  O   PRO A  18      44.700 -19.346 -25.254  1.00 28.92           O  
ANISOU  136  O   PRO A  18     4362   3455   3170   1435    -83     46       O  
ATOM    137  CB  PRO A  18      43.078 -17.167 -23.543  1.00 19.11           C  
ANISOU  137  CB  PRO A  18     3080   2209   1973   1426    -98     32       C  
ATOM    138  CG  PRO A  18      42.504 -17.061 -22.200  1.00 26.82           C  
ANISOU  138  CG  PRO A  18     4032   3194   2965   1419   -105     23       C  
ATOM    139  CD  PRO A  18      41.461 -18.118 -22.046  1.00 29.23           C  
ANISOU  139  CD  PRO A  18     4339   3506   3263   1416   -118     17       C  
ATOM    140  N   ILE A  19      44.448 -20.081 -23.144  1.00 30.21           N  
ANISOU  140  N   ILE A  19     4494   3639   3346   1424    -87     35       N  
ATOM    141  CA  ILE A  19      45.649 -20.898 -23.205  1.00 30.17           C  
ANISOU  141  CA  ILE A  19     4495   3640   3327   1425    -75     41       C  
ATOM    142  C   ILE A  19      45.338 -22.156 -24.036  1.00 26.80           C  
ANISOU  142  C   ILE A  19     4087   3215   2880   1428    -80     43       C  
ATOM    143  O   ILE A  19      46.131 -22.590 -24.873  1.00 26.05           O  
ANISOU  143  O   ILE A  19     4009   3118   2770   1433    -71     50       O  
ATOM    144  CB  ILE A  19      46.189 -21.181 -21.789  1.00 17.58           C  
ANISOU  144  CB  ILE A  19     2880   2059   1742   1418    -69     36       C  
ATOM    145  CG1 ILE A  19      46.701 -19.873 -21.180  1.00 17.60           C  
ANISOU  145  CG1 ILE A  19     2866   2058   1763   1416    -61     36       C  
ATOM    146  CG2 ILE A  19      47.281 -22.251 -21.807  1.00 17.52           C  
ANISOU  146  CG2 ILE A  19     2879   2060   1719   1419    -58     41       C  
ATOM    147  CD1 ILE A  19      47.376 -20.025 -19.860  1.00 18.08           C  
ANISOU  147  CD1 ILE A  19     2907   2131   1833   1410    -54     32       C  
ATOM    148  N   ILE A  20      44.138 -22.681 -23.850  1.00 20.96           N  
ANISOU  148  N   ILE A  20     3345   2477   2140   1425    -95     36       N  
ATOM    149  CA  ILE A  20      43.680 -23.825 -24.611  1.00 23.81           C  
ANISOU  149  CA  ILE A  20     3723   2839   2484   1427   -102     37       C  
ATOM    150  C   ILE A  20      43.513 -23.498 -26.094  1.00 32.31           C  
ANISOU  150  C   ILE A  20     4822   3903   3552   1434   -103     42       C  
ATOM    151  O   ILE A  20      43.877 -24.276 -26.963  1.00 36.27           O  
ANISOU  151  O   ILE A  20     5342   4403   4035   1438   -100     47       O  
ATOM    152  CB  ILE A  20      42.387 -24.378 -24.018  1.00 27.36           C  
ANISOU  152  CB  ILE A  20     4163   3294   2938   1422   -117     28       C  
ATOM    153  CG1 ILE A  20      42.637 -24.812 -22.573  1.00 29.64           C  
ANISOU  153  CG1 ILE A  20     4431   3597   3235   1415   -115     23       C  
ATOM    154  CG2 ILE A  20      41.885 -25.554 -24.823  1.00 32.40           C  
ANISOU  154  CG2 ILE A  20     4819   3933   3559   1424   -125     28       C  
ATOM    155  CD1 ILE A  20      41.421 -25.334 -21.872  1.00 27.03           C  
ANISOU  155  CD1 ILE A  20     4088   3272   2909   1409   -129     14       C  
ATOM    156  N   ARG A  21      42.995 -22.322 -26.384  1.00 37.66           N  
ANISOU  156  N   ARG A  21     5499   4570   4241   1436   -107     42       N  
ATOM    157  CA  ARG A  21      42.764 -21.939 -27.762  1.00 33.41           C  
ANISOU  157  CA  ARG A  21     4981   4018   3694   1443   -109     47       C  
ATOM    158  C   ARG A  21      44.046 -21.670 -28.516  1.00 32.54           C  
ANISOU  158  C   ARG A  21     4885   3904   3576   1449    -93     56       C  
ATOM    159  O   ARG A  21      44.143 -21.955 -29.712  1.00 39.00           O  
ANISOU  159  O   ARG A  21     5724   4716   4380   1454    -92     62       O  
ATOM    160  CB  ARG A  21      41.843 -20.743 -27.811  1.00 18.12           C  
ANISOU  160  CB  ARG A  21     3038   2073   1773   1443   -118     44       C  
ATOM    161  CG  ARG A  21      40.455 -21.151 -27.531  1.00 18.08           C  
ANISOU  161  CG  ARG A  21     3029   2070   1772   1439   -135     36       C  
ATOM    162  CD  ARG A  21      39.592 -19.993 -27.345  1.00 18.13           C  
ANISOU  162  CD  ARG A  21     3025   2069   1795   1438   -143     32       C  
ATOM    163  NE  ARG A  21      38.325 -20.427 -26.803  1.00 32.44           N  
ANISOU  163  NE  ARG A  21     4829   3886   3612   1433   -158     24       N  
ATOM    164  CZ  ARG A  21      37.683 -19.786 -25.841  1.00 32.10           C  
ANISOU  164  CZ  ARG A  21     4765   3844   3586   1428   -164     17       C  
ATOM    165  NH1 ARG A  21      38.204 -18.682 -25.334  1.00 35.51           N1+
ANISOU  165  NH1 ARG A  21     5185   4274   4032   1427   -157     18       N1+
ATOM    166  NH2 ARG A  21      36.528 -20.250 -25.393  1.00 17.98           N  
ANISOU  166  NH2 ARG A  21     2970   2061   1802   1424   -178     10       N  
ATOM    167  N   ALA A  22      45.031 -21.125 -27.821  1.00 29.08           N  
ANISOU  167  N   ALA A  22     4433   3469   3146   1447    -81     59       N  
ATOM    168  CA  ALA A  22      46.335 -20.939 -28.418  1.00 29.94           C  
ANISOU  168  CA  ALA A  22     4554   3575   3247   1452    -65     68       C  
ATOM    169  C   ALA A  22      46.941 -22.323 -28.693  1.00 43.87           C  
ANISOU  169  C   ALA A  22     6330   5347   4992   1453    -60     71       C  
ATOM    170  O   ALA A  22      47.475 -22.582 -29.777  1.00 47.59           O  
ANISOU  170  O   ALA A  22     6821   5813   5448   1459    -53     78       O  
ATOM    171  CB  ALA A  22      47.219 -20.143 -27.496  1.00 21.88           C  
ANISOU  171  CB  ALA A  22     3515   2557   2241   1449    -54     68       C  
ATOM    172  N   LEU A  23      46.827 -23.217 -27.714  1.00 40.57           N  
ANISOU  172  N   LEU A  23     5900   4942   4574   1447    -63     65       N  
ATOM    173  CA  LEU A  23      47.382 -24.564 -27.827  1.00 32.16           C  
ANISOU  173  CA  LEU A  23     4843   3885   3491   1448    -59     67       C  
ATOM    174  C   LEU A  23      46.926 -25.342 -29.075  1.00 29.58           C  
ANISOU  174  C   LEU A  23     4540   3554   3146   1453    -65     69       C  
ATOM    175  O   LEU A  23      47.689 -26.128 -29.637  1.00 24.12           O  
ANISOU  175  O   LEU A  23     3862   2865   2439   1456    -56     75       O  
ATOM    176  CB  LEU A  23      47.108 -25.359 -26.541  1.00 21.23           C  
ANISOU  176  CB  LEU A  23     3441   2515   2111   1440    -63     60       C  
ATOM    177  CG  LEU A  23      48.070 -24.969 -25.419  1.00 22.04           C  
ANISOU  177  CG  LEU A  23     3524   2624   2225   1436    -52     60       C  
ATOM    178  CD1 LEU A  23      47.819 -25.761 -24.146  1.00 17.52           C  
ANISOU  178  CD1 LEU A  23     2935   2067   1657   1429    -56     53       C  
ATOM    179  CD2 LEU A  23      49.508 -25.117 -25.899  1.00 17.69           C  
ANISOU  179  CD2 LEU A  23     2985   2074   1664   1440    -35     69       C  
ATOM    180  N   GLU A  24      45.687 -25.117 -29.502  1.00 27.57           N  
ANISOU  180  N   GLU A  24     4289   3292   2894   1453    -79     65       N  
ATOM    181  CA  GLU A  24      45.160 -25.743 -30.708  1.00 26.82           C  
ANISOU  181  CA  GLU A  24     4215   3191   2784   1457    -86     67       C  
ATOM    182  C   GLU A  24      45.795 -25.197 -31.980  1.00 31.24           C  
ANISOU  182  C   GLU A  24     4795   3740   3335   1465    -77     75       C  
ATOM    183  O   GLU A  24      45.602 -25.752 -33.048  1.00 37.48           O  
ANISOU  183  O   GLU A  24     5604   4526   4110   1470    -80     77       O  
ATOM    184  CB  GLU A  24      43.647 -25.558 -30.795  1.00 24.07           C  
ANISOU  184  CB  GLU A  24     3864   2838   2442   1456   -104     60       C  
ATOM    185  CG  GLU A  24      42.875 -26.075 -29.606  1.00 23.30           C  
ANISOU  185  CG  GLU A  24     3748   2750   2354   1448   -114     51       C  
ATOM    186  CD  GLU A  24      41.387 -25.818 -29.729  1.00 31.72           C  
ANISOU  186  CD  GLU A  24     4812   3811   3427   1447   -131     45       C  
ATOM    187  OE1 GLU A  24      40.995 -24.669 -30.007  1.00 42.98           O  
ANISOU  187  OE1 GLU A  24     6237   5227   4864   1448   -134     45       O  
ATOM    188  OE2 GLU A  24      40.599 -26.759 -29.551  1.00 38.06           O1-
ANISOU  188  OE2 GLU A  24     5615   4619   4226   1444   -142     39       O1-
ATOM    189  N   LYS A  25      46.531 -24.099 -31.862  1.00 33.97           N  
ANISOU  189  N   LYS A  25     5136   4082   3691   1467    -66     80       N  
ATOM    190  CA  LYS A  25      47.261 -23.525 -32.986  1.00 26.93           C  
ANISOU  190  CA  LYS A  25     4261   3180   2792   1474    -56     89       C  
ATOM    191  C   LYS A  25      48.772 -23.618 -32.750  1.00 31.55           C  
ANISOU  191  C   LYS A  25     4845   3770   3373   1475    -38     95       C  
ATOM    192  O   LYS A  25      49.526 -22.697 -33.076  1.00 33.57           O  
ANISOU  192  O   LYS A  25     5103   4019   3632   1478    -27    102       O  
ATOM    193  CB  LYS A  25      46.830 -22.072 -33.201  1.00 26.93           C  
ANISOU  193  CB  LYS A  25     4257   3168   2807   1475    -59     89       C  
ATOM    194  CG  LYS A  25      45.344 -21.903 -33.530  1.00 35.18           C  
ANISOU  194  CG  LYS A  25     5304   4207   3856   1475    -76     83       C  
ATOM    195  CD  LYS A  25      44.993 -20.449 -33.894  1.00 46.88           C  
ANISOU  195  CD  LYS A  25     6786   5677   5351   1477    -78     85       C  
ATOM    196  CE  LYS A  25      43.498 -20.302 -34.229  1.00 57.48           C  
ANISOU  196  CE  LYS A  25     8130   7013   6697   1477    -96     79       C  
ATOM    197  NZ  LYS A  25      43.039 -18.903 -34.544  1.00 58.09           N1+
ANISOU  197  NZ  LYS A  25     8206   7079   6787   1479    -99     80       N1+
ATOM    198  N   THR A  26      49.191 -24.730 -32.144  1.00 30.49           N  
ANISOU  198  N   THR A  26     4706   3647   3230   1472    -35     94       N  
ATOM    199  CA  THR A  26      50.597 -25.077 -31.953  1.00 25.93           C  
ANISOU  199  CA  THR A  26     4129   3076   2646   1473    -18    100       C  
ATOM    200  C   THR A  26      50.687 -26.582 -32.107  1.00 30.06           C  
ANISOU  200  C   THR A  26     4663   3609   3152   1472    -19     99       C  
ATOM    201  O   THR A  26      49.671 -27.281 -32.046  1.00 23.91           O  
ANISOU  201  O   THR A  26     3883   2831   2369   1470    -33     92       O  
ATOM    202  CB  THR A  26      51.084 -24.772 -30.542  1.00 29.78           C  
ANISOU  202  CB  THR A  26     4593   3573   3149   1466    -13     97       C  
ATOM    203  CG2 THR A  26      51.249 -23.280 -30.325  1.00 26.53           C  
ANISOU  203  CG2 THR A  26     4172   3154   2756   1467     -8     98       C  
ATOM    204  OG1 THR A  26      50.137 -25.297 -29.605  1.00 37.09           O  
ANISOU  204  OG1 THR A  26     5505   4507   4081   1460    -26     88       O  
ATOM    205  N   ASN A  27      51.901 -27.093 -32.287  1.00 40.29           N  
ANISOU  205  N   ASN A  27     5964   4908   4435   1475     -5    105       N  
ATOM    206  CA  ASN A  27      52.082 -28.540 -32.415  1.00 41.19           C  
ANISOU  206  CA  ASN A  27     6087   5031   4532   1475     -5    105       C  
ATOM    207  C   ASN A  27      52.358 -29.256 -31.080  1.00 49.49           C  
ANISOU  207  C   ASN A  27     7121   6096   5587   1468     -3    100       C  
ATOM    208  O   ASN A  27      52.555 -30.478 -31.053  1.00 55.46           O  
ANISOU  208  O   ASN A  27     7882   6861   6330   1467     -3     99       O  
ATOM    209  CB  ASN A  27      53.143 -28.875 -33.469  1.00 24.65           C  
ANISOU  209  CB  ASN A  27     4013   2933   2420   1481      9    114       C  
ATOM    210  CG  ASN A  27      54.415 -28.114 -33.263  1.00 27.26           C  
ANISOU  210  CG  ASN A  27     4339   3262   2755   1483     26    121       C  
ATOM    211  ND2 ASN A  27      55.181 -27.953 -34.328  1.00 28.05           N  
ANISOU  211  ND2 ASN A  27     4457   3356   2844   1490     37    129       N  
ATOM    212  OD1 ASN A  27      54.708 -27.658 -32.156  1.00 34.41           O  
ANISOU  212  OD1 ASN A  27     5225   4174   3676   1478     29    119       O  
ATOM    213  N   ILE A  28      52.356 -28.486 -29.989  1.00 43.30           N  
ANISOU  213  N   ILE A  28     6315   5315   4821   1463     -3     97       N  
ATOM    214  CA  ILE A  28      52.459 -29.020 -28.634  1.00 38.74           C  
ANISOU  214  CA  ILE A  28     5718   4750   4250   1456     -4     92       C  
ATOM    215  C   ILE A  28      51.384 -30.087 -28.337  1.00 36.63           C  
ANISOU  215  C   ILE A  28     5448   4490   3978   1452    -18     84       C  
ATOM    216  O   ILE A  28      50.210 -29.933 -28.695  1.00 28.66           O  
ANISOU  216  O   ILE A  28     4443   3475   2973   1452    -32     79       O  
ATOM    217  CB  ILE A  28      52.379 -27.885 -27.579  1.00 33.83           C  
ANISOU  217  CB  ILE A  28     5074   4130   3652   1451     -4     88       C  
ATOM    218  CG1 ILE A  28      53.572 -26.937 -27.710  1.00 38.01           C  
ANISOU  218  CG1 ILE A  28     5602   4654   4186   1454     12     96       C  
ATOM    219  CG2 ILE A  28      52.326 -28.444 -26.164  1.00 30.16           C  
ANISOU  219  CG2 ILE A  28     4588   3678   3194   1443     -6     82       C  
ATOM    220  CD1 ILE A  28      53.624 -25.847 -26.635  1.00 37.44           C  
ANISOU  220  CD1 ILE A  28     5508   4583   4136   1449     13     93       C  
ATOM    221  N   ASP A  29      51.815 -31.175 -27.698  1.00 32.90           N  
ANISOU  221  N   ASP A  29     4971   4030   3499   1449    -15     83       N  
ATOM    222  CA  ASP A  29      50.943 -32.267 -27.301  1.00 33.27           C  
ANISOU  222  CA  ASP A  29     5015   4084   3542   1444    -27     75       C  
ATOM    223  C   ASP A  29      50.452 -31.937 -25.896  1.00 41.25           C  
ANISOU  223  C   ASP A  29     6000   5102   4570   1437    -33     68       C  
ATOM    224  O   ASP A  29      51.253 -31.776 -24.978  1.00 44.45           O  
ANISOU  224  O   ASP A  29     6392   5515   4983   1434    -24     69       O  
ATOM    225  CB  ASP A  29      51.744 -33.571 -27.302  1.00 40.65           C  
ANISOU  225  CB  ASP A  29     5957   5029   4460   1445    -19     78       C  
ATOM    226  CG  ASP A  29      50.869 -34.805 -27.332  1.00 50.53           C  
ANISOU  226  CG  ASP A  29     7213   6285   5702   1443    -32     72       C  
ATOM    227  OD1 ASP A  29      49.673 -34.686 -27.667  1.00 61.96           O  
ANISOU  227  OD1 ASP A  29     8663   7727   7154   1443    -45     67       O  
ATOM    228  OD2 ASP A  29      51.386 -35.900 -27.027  1.00 48.36           O1-
ANISOU  228  OD2 ASP A  29     6938   6020   5417   1441    -27     72       O1-
ATOM    229  N   TRP A  30      49.142 -31.820 -25.720  1.00 37.29           N  
ANISOU  229  N   TRP A  30     5493   4598   4077   1434    -49     61       N  
ATOM    230  CA  TRP A  30      48.628 -31.314 -24.461  1.00 24.58           C  
ANISOU  230  CA  TRP A  30     3860   2994   2486   1427    -55     54       C  
ATOM    231  C   TRP A  30      47.320 -31.984 -24.072  1.00 26.27           C  
ANISOU  231  C   TRP A  30     4068   3212   2703   1423    -71     46       C  
ATOM    232  O   TRP A  30      46.641 -32.582 -24.909  1.00 30.82           O  
ANISOU  232  O   TRP A  30     4659   3784   3268   1426    -79     45       O  
ATOM    233  CB  TRP A  30      48.419 -29.806 -24.560  1.00 25.47           C  
ANISOU  233  CB  TRP A  30     3967   3096   2614   1429    -55     55       C  
ATOM    234  CG  TRP A  30      47.388 -29.421 -25.601  1.00 28.14           C  
ANISOU  234  CG  TRP A  30     4318   3422   2951   1433    -66     54       C  
ATOM    235  CD1 TRP A  30      47.628 -29.115 -26.909  1.00 28.38           C  
ANISOU  235  CD1 TRP A  30     4369   3442   2972   1440    -63     61       C  
ATOM    236  CD2 TRP A  30      45.964 -29.322 -25.419  1.00 20.37           C  
ANISOU  236  CD2 TRP A  30     3328   2435   1975   1430    -83     47       C  
ATOM    237  CE2 TRP A  30      45.414 -28.946 -26.659  1.00 21.30           C  
ANISOU  237  CE2 TRP A  30     3464   2541   2088   1435    -89     49       C  
ATOM    238  CE3 TRP A  30      45.106 -29.512 -24.332  1.00 26.98           C  
ANISOU  238  CE3 TRP A  30     4147   3281   2825   1423    -93     38       C  
ATOM    239  NE1 TRP A  30      46.450 -28.828 -27.547  1.00 27.61           N  
ANISOU  239  NE1 TRP A  30     4279   3335   2876   1441    -76     57       N  
ATOM    240  CZ2 TRP A  30      44.037 -28.743 -26.841  1.00 17.62           C  
ANISOU  240  CZ2 TRP A  30     2997   2069   1628   1434   -104     43       C  
ATOM    241  CZ3 TRP A  30      43.733 -29.318 -24.518  1.00 31.20           C  
ANISOU  241  CZ3 TRP A  30     4681   3809   3364   1422   -109     33       C  
ATOM    242  CH2 TRP A  30      43.217 -28.935 -25.763  1.00 17.53           C  
ANISOU  242  CH2 TRP A  30     2967   2065   1627   1428   -114     35       C  
ATOM    243  N   HIS A  31      46.965 -31.874 -22.795  1.00 22.55           N  
ANISOU  243  N   HIS A  31     3574   2749   2245   1416    -75     39       N  
ATOM    244  CA  HIS A  31      45.732 -32.485 -22.298  1.00 25.86           C  
ANISOU  244  CA  HIS A  31     3986   3172   2668   1411    -90     31       C  
ATOM    245  C   HIS A  31      45.239 -31.756 -21.049  1.00 25.33           C  
ANISOU  245  C   HIS A  31     3894   3109   2621   1405    -95     25       C  
ATOM    246  O   HIS A  31      45.963 -30.948 -20.459  1.00 21.38           O  
ANISOU  246  O   HIS A  31     3382   2611   2131   1404    -85     26       O  
ATOM    247  CB  HIS A  31      45.937 -33.985 -21.996  1.00 26.79           C  
ANISOU  247  CB  HIS A  31     4105   3301   2772   1409    -89     30       C  
ATOM    248  CG  HIS A  31      46.962 -34.253 -20.936  1.00 32.01           C  
ANISOU  248  CG  HIS A  31     4753   3975   3436   1405    -78     31       C  
ATOM    249  CD2 HIS A  31      46.853 -34.336 -19.588  1.00 30.08           C  
ANISOU  249  CD2 HIS A  31     4486   3740   3202   1398    -80     25       C  
ATOM    250  ND1 HIS A  31      48.301 -34.439 -21.222  1.00 35.65           N  
ANISOU  250  ND1 HIS A  31     5222   4438   3887   1408    -63     38       N  
ATOM    251  CE1 HIS A  31      48.966 -34.633 -20.098  1.00 34.04           C  
ANISOU  251  CE1 HIS A  31     5001   4245   3688   1403    -56     37       C  
ATOM    252  NE2 HIS A  31      48.111 -34.576 -19.092  1.00 32.18           N  
ANISOU  252  NE2 HIS A  31     4747   4014   3465   1397    -66     29       N  
ATOM    253  N   ILE A  32      44.006 -32.053 -20.654  1.00 24.51           N  
ANISOU  253  N   ILE A  32     3782   3007   2522   1401   -109     17       N  
ATOM    254  CA  ILE A  32      43.408 -31.459 -19.467  1.00 26.95           C  
ANISOU  254  CA  ILE A  32     4068   3320   2850   1395   -115     10       C  
ATOM    255  C   ILE A  32      43.016 -32.532 -18.449  1.00 33.70           C  
ANISOU  255  C   ILE A  32     4910   4188   3705   1388   -120      4       C  
ATOM    256  O   ILE A  32      42.395 -33.537 -18.806  1.00 34.22           O  
ANISOU  256  O   ILE A  32     4985   4256   3761   1388   -128      2       O  
ATOM    257  CB  ILE A  32      42.135 -30.665 -19.824  1.00 22.61           C  
ANISOU  257  CB  ILE A  32     3519   2761   2311   1395   -128      7       C  
ATOM    258  CG1 ILE A  32      42.451 -29.524 -20.780  1.00 20.52           C  
ANISOU  258  CG1 ILE A  32     3266   2483   2048   1402   -123     12       C  
ATOM    259  CG2 ILE A  32      41.481 -30.097 -18.596  1.00 22.33           C  
ANISOU  259  CG2 ILE A  32     3460   2731   2295   1389   -134     -1       C  
ATOM    260  CD1 ILE A  32      41.222 -28.858 -21.253  1.00 18.92           C  
ANISOU  260  CD1 ILE A  32     3065   2270   1853   1403   -136      9       C  
ATOM    261  N   ILE A  33      43.386 -32.304 -17.189  1.00 25.59           N  
ANISOU  261  N   ILE A  33     3863   3171   2690   1383   -115      1       N  
ATOM    262  CA  ILE A  33      42.874 -33.072 -16.079  1.00 27.02           C  
ANISOU  262  CA  ILE A  33     4029   3364   2875   1376   -121     -6       C  
ATOM    263  C   ILE A  33      41.848 -32.213 -15.361  1.00 31.23           C  
ANISOU  263  C   ILE A  33     4543   3895   3426   1371   -131    -13       C  
ATOM    264  O   ILE A  33      42.200 -31.205 -14.739  1.00 37.01           O  
ANISOU  264  O   ILE A  33     5262   4627   4173   1369   -126    -13       O  
ATOM    265  CB  ILE A  33      43.991 -33.455 -15.084  1.00 29.18           C  
ANISOU  265  CB  ILE A  33     4289   3649   3147   1372   -109     -5       C  
ATOM    266  CG1 ILE A  33      45.232 -33.955 -15.826  1.00 29.10           C  
ANISOU  266  CG1 ILE A  33     4296   3639   3121   1377    -97      3       C  
ATOM    267  CG2 ILE A  33      43.488 -34.488 -14.084  1.00 20.48           C  
ANISOU  267  CG2 ILE A  33     3175   2560   2046   1365   -116    -11       C  
ATOM    268  CD1 ILE A  33      46.342 -34.394 -14.914  1.00 16.38           C  
ANISOU  268  CD1 ILE A  33     2673   2040   1509   1373    -85      5       C  
ATOM    269  N   HIS A  34      40.579 -32.599 -15.469  1.00 24.88           N  
ANISOU  269  N   HIS A  34     3740   3089   2623   1370   -145    -18       N  
ATOM    270  CA  HIS A  34      39.482 -31.904 -14.788  1.00 26.82           C  
ANISOU  270  CA  HIS A  34     3971   3335   2887   1365   -156    -25       C  
ATOM    271  C   HIS A  34      39.123 -32.622 -13.478  1.00 23.51           C  
ANISOU  271  C   HIS A  34     3532   2929   2473   1358   -159    -31       C  
ATOM    272  O   HIS A  34      39.047 -33.837 -13.441  1.00 25.22           O  
ANISOU  272  O   HIS A  34     3753   3152   2679   1356   -162    -32       O  
ATOM    273  CB  HIS A  34      38.259 -31.796 -15.712  1.00 16.65           C  
ANISOU  273  CB  HIS A  34     2694   2035   1596   1368   -169    -26       C  
ATOM    274  CG  HIS A  34      37.077 -31.130 -15.082  1.00 40.31           C  
ANISOU  274  CG  HIS A  34     5675   5030   4610   1364   -181    -33       C  
ATOM    275  CD2 HIS A  34      36.992 -30.122 -14.181  1.00 44.21           C  
ANISOU  275  CD2 HIS A  34     6151   5526   5122   1361   -180    -37       C  
ATOM    276  ND1 HIS A  34      35.777 -31.496 -15.367  1.00 45.26           N  
ANISOU  276  ND1 HIS A  34     6305   5653   5236   1363   -195    -37       N  
ATOM    277  CE1 HIS A  34      34.944 -30.739 -14.674  1.00 47.10           C  
ANISOU  277  CE1 HIS A  34     6522   5886   5486   1360   -202    -43       C  
ATOM    278  NE2 HIS A  34      35.656 -29.895 -13.946  1.00 49.40           N  
ANISOU  278  NE2 HIS A  34     6800   6181   5788   1358   -193    -43       N  
ATOM    279  N   THR A  35      38.924 -31.875 -12.400  1.00 20.94           N  
ANISOU  279  N   THR A  35     3186   2607   2164   1353   -160    -36       N  
ATOM    280  CA  THR A  35      38.521 -32.488 -11.140  1.00 30.16           C  
ANISOU  280  CA  THR A  35     4334   3786   3337   1345   -164    -43       C  
ATOM    281  C   THR A  35      37.115 -32.007 -10.789  1.00 40.72           C  
ANISOU  281  C   THR A  35     5663   5122   4689   1342   -177    -49       C  
ATOM    282  O   THR A  35      36.688 -30.946 -11.253  1.00 34.84           O  
ANISOU  282  O   THR A  35     4919   4366   3952   1345   -181    -49       O  
ATOM    283  CB  THR A  35      39.514 -32.194 -10.000  1.00 30.17           C  
ANISOU  283  CB  THR A  35     4319   3798   3347   1341   -152    -43       C  
ATOM    284  CG2 THR A  35      40.891 -32.719 -10.354  1.00 26.30           C  
ANISOU  284  CG2 THR A  35     3839   3310   2843   1344   -139    -36       C  
ATOM    285  OG1 THR A  35      39.608 -30.780  -9.790  1.00 34.90           O  
ANISOU  285  OG1 THR A  35     4908   4391   3961   1341   -149    -44       O  
ATOM    286  N   ASN A  36      36.388 -32.804 -10.007  1.00 47.17           N  
ANISOU  286  N   ASN A  36     6468   5947   5507   1336   -185    -55       N  
ATOM    287  CA  ASN A  36      35.046 -32.437  -9.569  1.00 52.02           C  
ANISOU  287  CA  ASN A  36     7071   6559   6134   1333   -198    -62       C  
ATOM    288  C   ASN A  36      34.905 -32.537  -8.054  1.00 50.74           C  
ANISOU  288  C   ASN A  36     6885   6410   5984   1325   -197    -68       C  
ATOM    289  O   ASN A  36      33.832 -32.799  -7.529  1.00 50.45           O  
ANISOU  289  O   ASN A  36     6839   6376   5954   1320   -208    -74       O  
ATOM    290  CB  ASN A  36      34.009 -33.312 -10.263  1.00 61.01           C  
ANISOU  290  CB  ASN A  36     8222   7695   7265   1334   -210    -63       C  
ATOM    291  CG  ASN A  36      34.337 -33.550 -11.724  1.00 75.47           C  
ANISOU  291  CG  ASN A  36    10078   9516   9081   1341   -209    -56       C  
ATOM    292  ND2 ASN A  36      34.158 -34.785 -12.192  1.00 82.65           N  
ANISOU  292  ND2 ASN A  36    11000  10428   9977   1342   -212    -55       N  
ATOM    293  OD1 ASN A  36      34.768 -32.643 -12.417  1.00 79.96           O  
ANISOU  293  OD1 ASN A  36    10655  10075   9650   1346   -204    -52       O  
ATOM    294  N   ASN A  42      27.751 -31.292 -11.300  1.00 97.67           N  
ANISOU  294  N   ASN A  42    12859  12303  11946   1332   -273    -81       N  
ATOM    295  CA  ASN A  42      27.692 -31.529 -12.736  1.00 99.57           C  
ANISOU  295  CA  ASN A  42    13124  12534  12175   1338   -276    -76       C  
ATOM    296  C   ASN A  42      29.063 -31.939 -13.241  1.00 97.71           C  
ANISOU  296  C   ASN A  42    12901  12300  11925   1343   -263    -70       C  
ATOM    297  O   ASN A  42      30.073 -31.374 -12.820  1.00100.66           O  
ANISOU  297  O   ASN A  42    13268  12676  12301   1343   -251    -68       O  
ATOM    298  CB  ASN A  42      27.194 -30.265 -13.467  1.00100.74           C  
ANISOU  298  CB  ASN A  42    13278  12669  12331   1343   -281    -75       C  
ATOM    299  CG  ASN A  42      27.340 -30.350 -14.996  1.00101.35           C  
ANISOU  299  CG  ASN A  42    13380  12735  12394   1350   -282    -70       C  
ATOM    300  ND2 ASN A  42      26.489 -31.151 -15.635  1.00103.90           N  
ANISOU  300  ND2 ASN A  42    13714  13055  12710   1351   -292    -71       N  
ATOM    301  OD1 ASN A  42      28.197 -29.690 -15.587  1.00 97.34           O  
ANISOU  301  OD1 ASN A  42    12881  12221  11883   1355   -273    -64       O  
HETATM  302  N   MSE A  43      29.107 -32.942 -14.113  1.00 91.03           N  
ANISOU  302  N   MSE A  43    12073  11452  11064   1346   -265    -67       N  
HETATM  303  CA  MSE A  43      30.322 -33.195 -14.875  1.00 85.72           C  
ANISOU  303  CA  MSE A  43    11416  10777  10377   1351   -254    -60       C  
HETATM  304  C   MSE A  43      30.330 -32.241 -16.065  1.00 80.71           C  
ANISOU  304  C   MSE A  43    10796  10128   9740   1358   -254    -56       C  
HETATM  305  O   MSE A  43      29.584 -32.428 -17.033  1.00 79.47           O  
ANISOU  305  O   MSE A  43    10654   9963   9578   1361   -264    -55       O  
HETATM  306  CB  MSE A  43      30.415 -34.647 -15.321  1.00 87.13           C  
ANISOU  306  CB  MSE A  43    11607  10959  10539   1351   -255    -59       C  
HETATM  307  CG  MSE A  43      31.573 -35.390 -14.679  1.00 86.50           C  
ANISOU  307  CG  MSE A  43    11522  10891  10452   1350   -243    -57       C  
HETATM  308  CE  MSE A  43      32.651 -35.580 -17.441  1.00 82.75           C  
ANISOU  308  CE  MSE A  43    11096  10399   9948   1364   -235    -44       C  
HETATM  309 SE   MSE A  43      32.375 -36.712 -15.875  1.00185.59          SE  
ANISOU  309 SE   MSE A  43    24098  23440  22977   1355   -237    -51      SE  
ATOM    310  N   ASP A  44      31.209 -31.240 -15.968  1.00 75.88           N  
ANISOU  310  N   ASP A  44    10182   9515   9134   1360   -244    -52       N  
ATOM    311  CA  ASP A  44      31.151 -29.950 -16.688  1.00 66.88           C  
ANISOU  311  CA  ASP A  44     9048   8362   7999   1364   -244    -50       C  
ATOM    312  C   ASP A  44      31.148 -29.938 -18.208  1.00 58.31           C  
ANISOU  312  C   ASP A  44     7988   7265   6902   1372   -246    -44       C  
ATOM    313  O   ASP A  44      31.497 -28.921 -18.805  1.00 49.31           O  
ANISOU  313  O   ASP A  44     6855   6117   5765   1376   -241    -40       O  
ATOM    314  CB  ASP A  44      32.323 -29.076 -16.241  1.00 68.64           C  
ANISOU  314  CB  ASP A  44     9263   8587   8228   1365   -230    -47       C  
ATOM    315  CG  ASP A  44      31.932 -28.086 -15.178  1.00 66.66           C  
ANISOU  315  CG  ASP A  44     8991   8339   7997   1360   -231    -52       C  
ATOM    316  OD1 ASP A  44      30.830 -27.506 -15.307  1.00 67.54           O  
ANISOU  316  OD1 ASP A  44     9101   8444   8118   1360   -242    -55       O  
ATOM    317  OD2 ASP A  44      32.727 -27.896 -14.226  1.00 58.31           O1-
ANISOU  317  OD2 ASP A  44     7920   7290   6946   1357   -222    -53       O1-
ATOM    318  N   LYS A  45      30.760 -31.051 -18.822  1.00 60.00           N  
ANISOU  318  N   LYS A  45     8215   7479   7103   1373   -252    -44       N  
ATOM    319  CA  LYS A  45      30.807 -31.217 -20.265  1.00 56.58           C  
ANISOU  319  CA  LYS A  45     7806   7036   6657   1379   -253    -39       C  
ATOM    320  C   LYS A  45      30.144 -30.040 -20.996  1.00 54.68           C  
ANISOU  320  C   LYS A  45     7570   6781   6423   1383   -260    -39       C  
ATOM    321  O   LYS A  45      30.775 -29.361 -21.828  1.00 53.80           O  
ANISOU  321  O   LYS A  45     7471   6662   6307   1388   -253    -33       O  
ATOM    322  CB  LYS A  45      30.131 -32.539 -20.638  1.00 64.22           C  
ANISOU  322  CB  LYS A  45     8782   8005   7613   1378   -262    -42       C  
ATOM    323  CG  LYS A  45      30.639 -33.165 -21.928  1.00 72.34           C  
ANISOU  323  CG  LYS A  45     9835   9028   8624   1384   -259    -36       C  
ATOM    324  CD  LYS A  45      29.516 -33.819 -22.723  1.00 74.60           C  
ANISOU  324  CD  LYS A  45    10133   9308   8904   1385   -273    -39       C  
ATOM    325  CE  LYS A  45      28.378 -32.830 -22.956  1.00 72.28           C  
ANISOU  325  CE  LYS A  45     9837   9005   8623   1385   -285    -42       C  
ATOM    326  NZ  LYS A  45      27.364 -33.300 -23.937  1.00 69.43           N1+
ANISOU  326  NZ  LYS A  45     9490   8636   8255   1387   -297    -43       N1+
ATOM    327  N   ILE A  46      28.883 -29.786 -20.651  1.00 53.67           N  
ANISOU  327  N   ILE A  46     7434   6653   6307   1379   -272    -45       N  
ATOM    328  CA  ILE A  46      28.090 -28.751 -21.313  1.00 49.32           C  
ANISOU  328  CA  ILE A  46     6887   6089   5763   1382   -281    -45       C  
ATOM    329  C   ILE A  46      28.795 -27.393 -21.354  1.00 44.09           C  
ANISOU  329  C   ILE A  46     6223   5422   5109   1385   -271    -41       C  
ATOM    330  O   ILE A  46      28.709 -26.671 -22.365  1.00 36.18           O  
ANISOU  330  O   ILE A  46     5234   4408   4104   1391   -272    -38       O  
ATOM    331  CB  ILE A  46      26.713 -28.581 -20.659  1.00 40.23           C  
ANISOU  331  CB  ILE A  46     5722   4940   4626   1377   -294    -52       C  
ATOM    332  CG1 ILE A  46      25.962 -29.912 -20.637  1.00 42.67           C  
ANISOU  332  CG1 ILE A  46     6033   5253   4927   1374   -304    -56       C  
ATOM    333  CG2 ILE A  46      25.914 -27.561 -21.417  1.00 35.20           C  
ANISOU  333  CG2 ILE A  46     5091   4289   3994   1380   -302    -52       C  
ATOM    334  CD1 ILE A  46      24.695 -29.878 -19.794  1.00 45.09           C  
ANISOU  334  CD1 ILE A  46     6323   5563   5248   1368   -316    -63       C  
ATOM    335  N   PHE A  47      29.498 -27.065 -20.265  1.00 37.94           N  
ANISOU  335  N   PHE A  47     5426   4650   4337   1382   -262    -42       N  
ATOM    336  CA  PHE A  47      30.206 -25.786 -20.156  1.00 33.88           C  
ANISOU  336  CA  PHE A  47     4908   4133   3834   1384   -252    -39       C  
ATOM    337  C   PHE A  47      31.363 -25.755 -21.134  1.00 35.52           C  
ANISOU  337  C   PHE A  47     5133   4335   4028   1390   -241    -31       C  
ATOM    338  O   PHE A  47      31.528 -24.792 -21.885  1.00 34.22           O  
ANISOU  338  O   PHE A  47     4977   4160   3865   1395   -238    -27       O  
ATOM    339  CB  PHE A  47      30.691 -25.527 -18.720  1.00 34.02           C  
ANISOU  339  CB  PHE A  47     4902   4161   3863   1378   -245    -43       C  
ATOM    340  CG  PHE A  47      31.287 -24.151 -18.505  1.00 37.68           C  
ANISOU  340  CG  PHE A  47     5358   4621   4339   1379   -237    -41       C  
ATOM    341  CD1 PHE A  47      30.487 -23.026 -18.491  1.00 34.74           C  
ANISOU  341  CD1 PHE A  47     4980   4241   3981   1379   -244    -44       C  
ATOM    342  CD2 PHE A  47      32.654 -23.992 -18.300  1.00 42.11           C  
ANISOU  342  CD2 PHE A  47     5918   5185   4897   1381   -222    -36       C  
ATOM    343  CE1 PHE A  47      31.043 -21.771 -18.296  1.00 36.13           C  
ANISOU  343  CE1 PHE A  47     5149   4412   4168   1381   -236    -42       C  
ATOM    344  CE2 PHE A  47      33.209 -22.737 -18.101  1.00 38.13           C  
ANISOU  344  CE2 PHE A  47     5407   4676   4405   1382   -214    -35       C  
ATOM    345  CZ  PHE A  47      32.404 -21.631 -18.098  1.00 35.51           C  
ANISOU  345  CZ  PHE A  47     5069   4337   4087   1382   -221    -38       C  
ATOM    346  N   PHE A  48      32.149 -26.825 -21.144  1.00 36.96           N  
ANISOU  346  N   PHE A  48     5321   4525   4197   1390   -234    -28       N  
ATOM    347  CA  PHE A  48      33.265 -26.925 -22.073  1.00 38.97           C  
ANISOU  347  CA  PHE A  48     5593   4775   4437   1396   -222    -21       C  
ATOM    348  C   PHE A  48      32.772 -26.783 -23.505  1.00 44.14           C  
ANISOU  348  C   PHE A  48     6271   5418   5084   1402   -229    -17       C  
ATOM    349  O   PHE A  48      33.496 -26.304 -24.381  1.00 45.64           O  
ANISOU  349  O   PHE A  48     6474   5599   5267   1408   -221    -11       O  
ATOM    350  CB  PHE A  48      33.981 -28.261 -21.908  1.00 35.58           C  
ANISOU  350  CB  PHE A  48     5169   4356   3994   1395   -216    -19       C  
ATOM    351  CG  PHE A  48      35.012 -28.276 -20.823  1.00 37.79           C  
ANISOU  351  CG  PHE A  48     5433   4646   4279   1392   -204    -19       C  
ATOM    352  CD1 PHE A  48      36.274 -27.739 -21.043  1.00 38.50           C  
ANISOU  352  CD1 PHE A  48     5527   4734   4366   1395   -190    -12       C  
ATOM    353  CD2 PHE A  48      34.739 -28.860 -19.594  1.00 38.85           C  
ANISOU  353  CD2 PHE A  48     5550   4793   4420   1385   -207    -25       C  
ATOM    354  CE1 PHE A  48      37.247 -27.771 -20.055  1.00 33.19           C  
ANISOU  354  CE1 PHE A  48     4841   4072   3698   1392   -178    -12       C  
ATOM    355  CE2 PHE A  48      35.707 -28.899 -18.596  1.00 37.79           C  
ANISOU  355  CE2 PHE A  48     5401   4669   4289   1382   -196    -25       C  
ATOM    356  CZ  PHE A  48      36.962 -28.350 -18.829  1.00 34.68           C  
ANISOU  356  CZ  PHE A  48     5012   4273   3893   1385   -181    -18       C  
ATOM    357  N   GLU A  49      31.529 -27.191 -23.742  1.00 42.45           N  
ANISOU  357  N   GLU A  49     6058   5200   4869   1401   -243    -22       N  
ATOM    358  CA  GLU A  49      30.988 -27.089 -25.089  1.00 41.28           C  
ANISOU  358  CA  GLU A  49     5931   5041   4714   1406   -250    -19       C  
ATOM    359  C   GLU A  49      30.433 -25.709 -25.451  1.00 39.09           C  
ANISOU  359  C   GLU A  49     5652   4752   4447   1409   -255    -19       C  
ATOM    360  O   GLU A  49      30.612 -25.254 -26.574  1.00 46.35           O  
ANISOU  360  O   GLU A  49     6589   5661   5360   1415   -253    -14       O  
ATOM    361  CB  GLU A  49      29.999 -28.216 -25.368  1.00 45.45           C  
ANISOU  361  CB  GLU A  49     6465   5571   5234   1405   -263    -23       C  
ATOM    362  CG  GLU A  49      30.702 -29.522 -25.695  1.00 56.31           C  
ANISOU  362  CG  GLU A  49     7852   6952   6592   1406   -258    -21       C  
ATOM    363  CD  GLU A  49      29.821 -30.718 -25.437  1.00 68.14           C  
ANISOU  363  CD  GLU A  49     9349   8456   8087   1402   -269    -26       C  
ATOM    364  OE1 GLU A  49      28.728 -30.504 -24.866  1.00 73.42           O  
ANISOU  364  OE1 GLU A  49    10004   9125   8768   1397   -280    -32       O  
ATOM    365  OE2 GLU A  49      30.215 -31.853 -25.798  1.00 67.08           O1-
ANISOU  365  OE2 GLU A  49     9224   8325   7938   1403   -266    -25       O1-
ATOM    366  N   GLU A  50      29.786 -25.033 -24.512  1.00 38.51           N  
ANISOU  366  N   GLU A  50     5560   4680   4391   1404   -260    -25       N  
ATOM    367  CA  GLU A  50      29.384 -23.638 -24.731  1.00 36.06           C  
ANISOU  367  CA  GLU A  50     5248   4361   4093   1406   -263    -25       C  
ATOM    368  C   GLU A  50      30.560 -22.757 -25.139  1.00 36.22           C  
ANISOU  368  C   GLU A  50     5273   4375   4112   1411   -249    -18       C  
ATOM    369  O   GLU A  50      30.382 -21.797 -25.867  1.00 48.95           O  
ANISOU  369  O   GLU A  50     6893   5976   5728   1415   -250    -15       O  
ATOM    370  CB  GLU A  50      28.740 -23.041 -23.477  1.00 40.38           C  
ANISOU  370  CB  GLU A  50     5771   4913   4659   1400   -268    -31       C  
ATOM    371  CG  GLU A  50      27.360 -23.570 -23.151  1.00 50.65           C  
ANISOU  371  CG  GLU A  50     7065   6216   5964   1396   -284    -38       C  
ATOM    372  CD  GLU A  50      26.922 -23.209 -21.741  1.00 64.00           C  
ANISOU  372  CD  GLU A  50     8731   7915   7672   1389   -286    -45       C  
ATOM    373  OE1 GLU A  50      27.721 -22.598 -20.982  1.00 60.66           O  
ANISOU  373  OE1 GLU A  50     8295   7496   7257   1387   -276    -44       O  
ATOM    374  OE2 GLU A  50      25.768 -23.545 -21.395  1.00 71.58           O1-
ANISOU  374  OE2 GLU A  50     9684   8876   8636   1385   -299    -51       O1-
ATOM    375  N   LEU A  51      31.756 -23.077 -24.661  1.00 30.76           N  
ANISOU  375  N   LEU A  51     4579   3692   3418   1410   -236    -15       N  
ATOM    376  CA  LEU A  51      32.935 -22.269 -24.929  1.00 26.76           C  
ANISOU  376  CA  LEU A  51     4076   3181   2912   1414   -222     -8       C  
ATOM    377  C   LEU A  51      33.766 -22.814 -26.076  1.00 28.03           C  
ANISOU  377  C   LEU A  51     4258   3338   3053   1420   -214     -1       C  
ATOM    378  O   LEU A  51      34.924 -22.426 -26.234  1.00 28.90           O  
ANISOU  378  O   LEU A  51     4373   3447   3162   1423   -200      5       O  
ATOM    379  CB  LEU A  51      33.818 -22.185 -23.687  1.00 30.27           C  
ANISOU  379  CB  LEU A  51     4501   3636   3364   1410   -211     -9       C  
ATOM    380  CG  LEU A  51      33.335 -21.426 -22.450  1.00 29.36           C  
ANISOU  380  CG  LEU A  51     4361   3525   3269   1404   -214    -16       C  
ATOM    381  CD1 LEU A  51      34.498 -21.233 -21.485  1.00 23.05           C  
ANISOU  381  CD1 LEU A  51     3548   2734   2476   1401   -200    -15       C  
ATOM    382  CD2 LEU A  51      32.740 -20.101 -22.862  1.00 30.99           C  
ANISOU  382  CD2 LEU A  51     4569   3720   3487   1406   -219    -16       C  
ATOM    383  N   ASN A  52      33.177 -23.715 -26.864  1.00 30.71           N  
ANISOU  383  N   ASN A  52     4613   3675   3380   1422   -222     -1       N  
ATOM    384  CA  ASN A  52      33.853 -24.333 -28.008  1.00 33.41           C  
ANISOU  384  CA  ASN A  52     4977   4013   3703   1428   -216      6       C  
ATOM    385  C   ASN A  52      35.164 -24.989 -27.624  1.00 37.45           C  
ANISOU  385  C   ASN A  52     5488   4534   4206   1427   -202      9       C  
ATOM    386  O   ASN A  52      36.147 -24.930 -28.383  1.00 37.26           O  
ANISOU  386  O   ASN A  52     5478   4507   4172   1433   -191     16       O  
ATOM    387  CB  ASN A  52      34.114 -23.307 -29.109  1.00 38.34           C  
ANISOU  387  CB  ASN A  52     5616   4625   4326   1434   -212     12       C  
ATOM    388  CG  ASN A  52      32.839 -22.813 -29.757  1.00 46.23           C  
ANISOU  388  CG  ASN A  52     6622   5615   5330   1436   -226      9       C  
ATOM    389  ND2 ASN A  52      32.937 -21.711 -30.510  1.00 45.15           N  
ANISOU  389  ND2 ASN A  52     6492   5466   5196   1441   -224     13       N  
ATOM    390  OD1 ASN A  52      31.775 -23.417 -29.588  1.00 44.41           O  
ANISOU  390  OD1 ASN A  52     6388   5386   5100   1433   -239      3       O  
ATOM    391  N   LEU A  53      35.174 -25.594 -26.435  1.00 33.02           N  
ANISOU  391  N   LEU A  53     4911   3986   3651   1421   -202      4       N  
ATOM    392  CA  LEU A  53      36.391 -26.184 -25.870  1.00 30.83           C  
ANISOU  392  CA  LEU A  53     4628   3718   3367   1420   -189      7       C  
ATOM    393  C   LEU A  53      36.362 -27.709 -25.921  1.00 32.12           C  
ANISOU  393  C   LEU A  53     4798   3889   3516   1419   -191      6       C  
ATOM    394  O   LEU A  53      35.331 -28.340 -25.652  1.00 39.05           O  
ANISOU  394  O   LEU A  53     5672   4771   4395   1415   -204      0       O  
ATOM    395  CB  LEU A  53      36.613 -25.708 -24.437  1.00 28.75           C  
ANISOU  395  CB  LEU A  53     4340   3463   3120   1414   -185      3       C  
ATOM    396  CG  LEU A  53      37.009 -24.250 -24.275  1.00 26.18           C  
ANISOU  396  CG  LEU A  53     4007   3132   2808   1415   -178      5       C  
ATOM    397  CD1 LEU A  53      37.075 -23.915 -22.798  1.00 26.37           C  
ANISOU  397  CD1 LEU A  53     4005   3165   2848   1409   -176      0       C  
ATOM    398  CD2 LEU A  53      38.332 -23.936 -24.988  1.00 20.53           C  
ANISOU  398  CD2 LEU A  53     3304   2411   2084   1421   -163     14       C  
ATOM    399  N   PRO A  54      37.494 -28.310 -26.291  1.00 26.75           N  
ANISOU  399  N   PRO A  54     4129   3212   2821   1422   -179     12       N  
ATOM    400  CA  PRO A  54      37.513 -29.769 -26.410  1.00 27.45           C  
ANISOU  400  CA  PRO A  54     4225   3308   2895   1421   -181     11       C  
ATOM    401  C   PRO A  54      37.320 -30.383 -25.037  1.00 33.25           C  
ANISOU  401  C   PRO A  54     4940   4057   3638   1413   -184      4       C  
ATOM    402  O   PRO A  54      37.761 -29.775 -24.059  1.00 36.86           O  
ANISOU  402  O   PRO A  54     5380   4519   4107   1410   -177      4       O  
ATOM    403  CB  PRO A  54      38.906 -30.061 -26.973  1.00 22.02           C  
ANISOU  403  CB  PRO A  54     3551   2621   2194   1425   -166     18       C  
ATOM    404  CG  PRO A  54      39.709 -28.857 -26.701  1.00 27.93           C  
ANISOU  404  CG  PRO A  54     4293   3368   2953   1427   -155     22       C  
ATOM    405  CD  PRO A  54      38.772 -27.693 -26.675  1.00 30.23           C  
ANISOU  405  CD  PRO A  54     4577   3650   3260   1426   -164     19       C  
ATOM    406  N   ASN A  55      36.639 -31.521 -24.946  1.00 32.15           N  
ANISOU  406  N   ASN A  55     4802   3922   3492   1410   -193      0       N  
ATOM    407  CA  ASN A  55      36.429 -32.138 -23.640  1.00 36.02           C  
ANISOU  407  CA  ASN A  55     5273   4425   3989   1403   -195     -6       C  
ATOM    408  C   ASN A  55      37.753 -32.576 -23.022  1.00 35.65           C  
ANISOU  408  C   ASN A  55     5220   4388   3937   1402   -181     -3       C  
ATOM    409  O   ASN A  55      38.677 -32.987 -23.732  1.00 32.16           O  
ANISOU  409  O   ASN A  55     4794   3945   3481   1407   -171      3       O  
ATOM    410  CB  ASN A  55      35.453 -33.315 -23.711  1.00 42.62           C  
ANISOU  410  CB  ASN A  55     6112   5264   4819   1401   -208    -11       C  
ATOM    411  CG  ASN A  55      34.004 -32.878 -23.681  1.00 56.40           C  
ANISOU  411  CG  ASN A  55     7851   7002   6575   1399   -223    -17       C  
ATOM    412  ND2 ASN A  55      33.768 -31.571 -23.703  1.00 63.36           N  
ANISOU  412  ND2 ASN A  55     8727   7877   7468   1400   -224    -16       N  
ATOM    413  OD1 ASN A  55      33.106 -33.708 -23.645  1.00 60.58           O  
ANISOU  413  OD1 ASN A  55     8380   7534   7102   1396   -234    -21       O  
ATOM    414  N   PRO A  56      37.868 -32.432 -21.695  1.00 36.38           N  
ANISOU  414  N   PRO A  56     5292   4490   4042   1396   -178     -6       N  
ATOM    415  CA  PRO A  56      39.020 -32.946 -20.948  1.00 38.40           C  
ANISOU  415  CA  PRO A  56     5539   4757   4293   1394   -166     -4       C  
ATOM    416  C   PRO A  56      39.191 -34.443 -21.127  1.00 33.32           C  
ANISOU  416  C   PRO A  56     4905   4120   3634   1394   -166     -4       C  
ATOM    417  O   PRO A  56      38.260 -35.194 -20.840  1.00 35.26           O  
ANISOU  417  O   PRO A  56     5147   4370   3880   1390   -177    -10       O  
ATOM    418  CB  PRO A  56      38.647 -32.647 -19.492  1.00 36.56           C  
ANISOU  418  CB  PRO A  56     5281   4533   4077   1387   -169    -11       C  
ATOM    419  CG  PRO A  56      37.814 -31.454 -19.574  1.00 33.73           C  
ANISOU  419  CG  PRO A  56     4917   4165   3733   1387   -176    -13       C  
ATOM    420  CD  PRO A  56      37.048 -31.528 -20.873  1.00 32.01           C  
ANISOU  420  CD  PRO A  56     4719   3936   3507   1392   -186    -12       C  
ATOM    421  N   LYS A  57      40.363 -34.851 -21.602  1.00 30.16           N  
ANISOU  421  N   LYS A  57     4517   3722   3220   1398   -153      2       N  
ATOM    422  CA  LYS A  57      40.742 -36.261 -21.672  1.00 35.10           C  
ANISOU  422  CA  LYS A  57     5150   4356   3831   1397   -151      3       C  
ATOM    423  C   LYS A  57      40.464 -37.028 -20.376  1.00 37.25           C  
ANISOU  423  C   LYS A  57     5404   4641   4108   1390   -154     -3       C  
ATOM    424  O   LYS A  57      39.873 -38.103 -20.413  1.00 38.74           O  
ANISOU  424  O   LYS A  57     5595   4833   4290   1388   -162     -7       O  
ATOM    425  CB  LYS A  57      42.223 -36.365 -22.015  1.00 36.26           C  
ANISOU  425  CB  LYS A  57     5307   4504   3966   1401   -134     10       C  
ATOM    426  CG  LYS A  57      42.753 -37.768 -22.102  1.00 35.36           C  
ANISOU  426  CG  LYS A  57     5201   4399   3837   1401   -130     12       C  
ATOM    427  CD  LYS A  57      44.138 -37.723 -22.719  1.00 34.13           C  
ANISOU  427  CD  LYS A  57     5058   4241   3668   1407   -114     20       C  
ATOM    428  CE  LYS A  57      44.742 -39.099 -22.873  1.00 30.41           C  
ANISOU  428  CE  LYS A  57     4596   3778   3180   1407   -109     22       C  
ATOM    429  NZ  LYS A  57      46.183 -38.929 -23.216  1.00 34.46           N1+
ANISOU  429  NZ  LYS A  57     5117   4291   3685   1411    -92     30       N1+
ATOM    430  N   TYR A  58      40.883 -36.453 -19.245  1.00 38.45           N  
ANISOU  430  N   TYR A  58     5536   4800   4272   1386   -148     -5       N  
ATOM    431  CA  TYR A  58      40.699 -37.029 -17.903  1.00 32.87           C  
ANISOU  431  CA  TYR A  58     4810   4106   3572   1378   -150    -10       C  
ATOM    432  C   TYR A  58      39.742 -36.271 -17.003  1.00 37.54           C  
ANISOU  432  C   TYR A  58     5382   4699   4184   1373   -159    -17       C  
ATOM    433  O   TYR A  58      40.026 -35.151 -16.593  1.00 34.74           O  
ANISOU  433  O   TYR A  58     5017   4342   3841   1372   -155    -17       O  
ATOM    434  CB  TYR A  58      42.024 -37.052 -17.162  1.00 19.58           C  
ANISOU  434  CB  TYR A  58     3118   2432   1888   1377   -135     -7       C  
ATOM    435  CG  TYR A  58      43.063 -37.841 -17.866  1.00 22.10           C  
ANISOU  435  CG  TYR A  58     3454   2753   2190   1381   -125     -1       C  
ATOM    436  CD1 TYR A  58      43.069 -39.226 -17.792  1.00 23.36           C  
ANISOU  436  CD1 TYR A  58     3618   2920   2337   1379   -127     -2       C  
ATOM    437  CD2 TYR A  58      44.036 -37.215 -18.607  1.00 16.55           C  
ANISOU  437  CD2 TYR A  58     2763   2043   1482   1387   -114      7       C  
ATOM    438  CE1 TYR A  58      44.017 -39.966 -18.437  1.00 25.30           C  
ANISOU  438  CE1 TYR A  58     3880   3168   2566   1383   -117      4       C  
ATOM    439  CE2 TYR A  58      44.997 -37.940 -19.256  1.00 25.35           C  
ANISOU  439  CE2 TYR A  58     3893   3160   2580   1391   -104     13       C  
ATOM    440  CZ  TYR A  58      44.980 -39.323 -19.180  1.00 28.79           C  
ANISOU  440  CZ  TYR A  58     4333   3603   3002   1389   -106     11       C  
ATOM    441  OH  TYR A  58      45.938 -40.067 -19.833  1.00 33.29           O  
ANISOU  441  OH  TYR A  58     4918   4174   3555   1393    -96     17       O  
ATOM    442  N   ASN A  59      38.633 -36.899 -16.649  1.00 42.63           N  
ANISOU  442  N   ASN A  59     6020   5346   4830   1369   -172    -23       N  
ATOM    443  CA  ASN A  59      37.833 -36.391 -15.553  1.00 44.34           C  
ANISOU  443  CA  ASN A  59     6216   5567   5065   1363   -179    -30       C  
ATOM    444  C   ASN A  59      38.023 -37.257 -14.320  1.00 46.41           C  
ANISOU  444  C   ASN A  59     6462   5843   5328   1356   -177    -34       C  
ATOM    445  O   ASN A  59      37.846 -38.473 -14.371  1.00 52.86           O  
ANISOU  445  O   ASN A  59     7284   6666   6135   1355   -180    -35       O  
ATOM    446  CB  ASN A  59      36.366 -36.326 -15.937  1.00 46.07           C  
ANISOU  446  CB  ASN A  59     6438   5779   5289   1362   -195    -35       C  
ATOM    447  CG  ASN A  59      36.101 -35.305 -16.998  1.00 51.94           C  
ANISOU  447  CG  ASN A  59     7193   6507   6033   1368   -197    -32       C  
ATOM    448  ND2 ASN A  59      36.050 -35.754 -18.246  1.00 59.39           N  
ANISOU  448  ND2 ASN A  59     8159   7444   6964   1373   -200    -28       N  
ATOM    449  OD1 ASN A  59      35.941 -34.118 -16.708  1.00 50.42           O  
ANISOU  449  OD1 ASN A  59     6991   6311   5855   1368   -198    -33       O  
ATOM    450  N   LEU A  60      38.401 -36.624 -13.218  1.00 40.55           N  
ANISOU  450  N   LEU A  60     5701   5108   4599   1352   -171    -36       N  
ATOM    451  CA  LEU A  60      38.586 -37.317 -11.957  1.00 40.84           C  
ANISOU  451  CA  LEU A  60     5720   5158   4638   1345   -169    -40       C  
ATOM    452  C   LEU A  60      37.532 -36.842 -10.997  1.00 41.74           C  
ANISOU  452  C   LEU A  60     5815   5275   4769   1339   -178    -47       C  
ATOM    453  O   LEU A  60      37.504 -35.673 -10.646  1.00 51.24           O  
ANISOU  453  O   LEU A  60     7008   6475   5986   1338   -177    -48       O  
ATOM    454  CB  LEU A  60      39.955 -36.996 -11.363  1.00 39.87           C  
ANISOU  454  CB  LEU A  60     5590   5043   4517   1344   -154    -36       C  
ATOM    455  CG  LEU A  60      41.149 -37.090 -12.308  1.00 33.01           C  
ANISOU  455  CG  LEU A  60     4739   4170   3634   1351   -142    -28       C  
ATOM    456  CD1 LEU A  60      42.419 -36.751 -11.553  1.00 35.27           C  
ANISOU  456  CD1 LEU A  60     5014   4463   3923   1349   -128    -25       C  
ATOM    457  CD2 LEU A  60      41.219 -38.474 -12.927  1.00 25.10           C  
ANISOU  457  CD2 LEU A  60     3752   3170   2613   1353   -143    -26       C  
ATOM    458  N   ASN A  61      36.651 -37.734 -10.577  1.00 46.48           N  
ANISOU  458  N   ASN A  61     6410   5881   5369   1335   -188    -52       N  
ATOM    459  CA  ASN A  61      35.743 -37.400  -9.502  1.00 52.20           C  
ANISOU  459  CA  ASN A  61     7114   6611   6110   1329   -195    -59       C  
ATOM    460  C   ASN A  61      36.509 -37.537  -8.202  1.00 58.44           C  
ANISOU  460  C   ASN A  61     7886   7413   6905   1323   -186    -61       C  
ATOM    461  O   ASN A  61      37.022 -38.605  -7.879  1.00 62.11           O  
ANISOU  461  O   ASN A  61     8351   7888   7361   1321   -182    -60       O  
ATOM    462  CB  ASN A  61      34.521 -38.308  -9.520  1.00 54.64           C  
ANISOU  462  CB  ASN A  61     7424   6920   6418   1326   -208    -64       C  
ATOM    463  CG  ASN A  61      33.680 -38.112 -10.754  1.00 64.87           C  
ANISOU  463  CG  ASN A  61     8736   8202   7709   1331   -218    -63       C  
ATOM    464  ND2 ASN A  61      32.534 -37.454 -10.595  1.00 69.18           N  
ANISOU  464  ND2 ASN A  61     9274   8743   8268   1329   -229    -67       N  
ATOM    465  OD1 ASN A  61      34.057 -38.539 -11.846  1.00 71.94           O  
ANISOU  465  OD1 ASN A  61     9651   9092   8591   1337   -216    -58       O  
ATOM    466  N   ILE A  62      36.626 -36.437  -7.476  1.00 57.35           N  
ANISOU  466  N   ILE A  62     7733   7276   6782   1320   -183    -63       N  
ATOM    467  CA  ILE A  62      37.293 -36.467  -6.193  1.00 56.41           C  
ANISOU  467  CA  ILE A  62     7595   7169   6670   1314   -175    -65       C  
ATOM    468  C   ILE A  62      36.225 -36.785  -5.153  1.00 62.46           C  
ANISOU  468  C   ILE A  62     8343   7943   7446   1307   -185    -73       C  
ATOM    469  O   ILE A  62      36.507 -37.245  -4.037  1.00 65.27           O  
ANISOU  469  O   ILE A  62     8684   8311   7805   1301   -181    -76       O  
ATOM    470  CB  ILE A  62      37.986 -35.123  -5.927  1.00 51.20           C  
ANISOU  470  CB  ILE A  62     6926   6506   6021   1315   -167    -64       C  
ATOM    471  CG1 ILE A  62      39.087 -34.900  -6.970  1.00 55.26           C  
ANISOU  471  CG1 ILE A  62     7458   7013   6524   1322   -157    -56       C  
ATOM    472  CG2 ILE A  62      38.570 -35.070  -4.541  1.00 49.95           C  
ANISOU  472  CG2 ILE A  62     6747   6361   5872   1308   -159    -67       C  
ATOM    473  CD1 ILE A  62      40.002 -36.109  -7.208  1.00 53.64           C  
ANISOU  473  CD1 ILE A  62     7264   6816   6302   1323   -149    -51       C  
ATOM    474  N   GLY A  63      34.979 -36.566  -5.560  1.00 62.24           N  
ANISOU  474  N   GLY A  63     8318   7907   7423   1308   -197    -76       N  
ATOM    475  CA  GLY A  63      33.843 -36.713  -4.680  1.00 62.03           C  
ANISOU  475  CA  GLY A  63     8276   7886   7407   1302   -207    -83       C  
ATOM    476  C   GLY A  63      33.968 -35.661  -3.609  1.00 64.80           C  
ANISOU  476  C   GLY A  63     8606   8240   7774   1297   -203    -87       C  
ATOM    477  O   GLY A  63      34.869 -34.829  -3.659  1.00 66.82           O  
ANISOU  477  O   GLY A  63     8862   8494   8034   1299   -194    -84       O  
ATOM    478  N   SER A  64      33.064 -35.676  -2.641  1.00 64.82           N  
ANISOU  478  N   SER A  64     8591   8248   7788   1291   -210    -93       N  
ATOM    479  CA  SER A  64      33.252 -34.828  -1.483  1.00 60.59           C  
ANISOU  479  CA  SER A  64     8035   7718   7268   1286   -206    -97       C  
ATOM    480  C   SER A  64      33.798 -35.667  -0.335  1.00 60.98           C  
ANISOU  480  C   SER A  64     8071   7783   7316   1280   -200    -99       C  
ATOM    481  O   SER A  64      33.899 -36.896  -0.431  1.00 65.29           O  
ANISOU  481  O   SER A  64     8624   8334   7849   1279   -200    -98       O  
ATOM    482  CB  SER A  64      31.968 -34.085  -1.106  1.00 63.73           C  
ANISOU  482  CB  SER A  64     8421   8112   7681   1283   -217   -103       C  
ATOM    483  OG  SER A  64      31.938 -32.796  -1.714  1.00 64.31           O  
ANISOU  483  OG  SER A  64     8499   8174   7761   1288   -217   -102       O  
ATOM    484  N   GLY A  65      34.161 -34.980   0.740  1.00 55.04           N  
ANISOU  484  N   GLY A  65     7301   7037   6576   1275   -194   -103       N  
ATOM    485  CA  GLY A  65      34.837 -35.568   1.876  1.00 50.73           C  
ANISOU  485  CA  GLY A  65     6741   6504   6030   1268   -186   -104       C  
ATOM    486  C   GLY A  65      35.596 -34.399   2.458  1.00 47.93           C  
ANISOU  486  C   GLY A  65     6374   6151   5688   1267   -178   -105       C  
ATOM    487  O   GLY A  65      35.407 -33.267   2.001  1.00 45.37           O  
ANISOU  487  O   GLY A  65     6052   5817   5371   1270   -179   -105       O  
ATOM    488  N   THR A  66      36.457 -34.653   3.437  1.00 47.39           N  
ANISOU  488  N   THR A  66     6293   6093   5620   1262   -168   -106       N  
ATOM    489  CA  THR A  66      37.176 -33.572   4.122  1.00 51.02           C  
ANISOU  489  CA  THR A  66     6739   6554   6093   1259   -160   -108       C  
ATOM    490  C   THR A  66      38.249 -32.866   3.287  1.00 49.76           C  
ANISOU  490  C   THR A  66     6590   6386   5929   1265   -151   -102       C  
ATOM    491  O   THR A  66      38.760 -33.434   2.325  1.00 56.48           O  
ANISOU  491  O   THR A  66     7460   7234   6766   1271   -148    -96       O  
ATOM    492  CB  THR A  66      37.863 -34.100   5.366  1.00 54.46           C  
ANISOU  492  CB  THR A  66     7160   7005   6530   1251   -152   -110       C  
ATOM    493  CG2 THR A  66      37.554 -33.207   6.538  1.00 58.82           C  
ANISOU  493  CG2 THR A  66     7689   7559   7099   1245   -153   -117       C  
ATOM    494  OG1 THR A  66      37.410 -35.431   5.635  1.00 52.38           O  
ANISOU  494  OG1 THR A  66     6897   6749   6257   1249   -157   -111       O  
ATOM    495  N   HIS A  67      38.594 -31.636   3.672  1.00 41.41           N  
ANISOU  495  N   HIS A  67     5523   5326   4886   1264   -146   -104       N  
ATOM    496  CA  HIS A  67      39.709 -30.895   3.062  1.00 47.95           C  
ANISOU  496  CA  HIS A  67     6359   6147   5713   1269   -136    -99       C  
ATOM    497  C   HIS A  67      40.955 -31.762   2.825  1.00 51.65           C  
ANISOU  497  C   HIS A  67     6836   6621   6167   1270   -125    -93       C  
ATOM    498  O   HIS A  67      41.486 -31.856   1.696  1.00 54.92           O  
ANISOU  498  O   HIS A  67     7269   7028   6570   1277   -121    -86       O  
ATOM    499  CB  HIS A  67      40.091 -29.722   3.953  1.00 53.62           C  
ANISOU  499  CB  HIS A  67     7058   6866   6449   1264   -130   -103       C  
ATOM    500  CG  HIS A  67      39.387 -28.450   3.613  1.00 65.46           C  
ANISOU  500  CG  HIS A  67     8557   8355   7961   1267   -135   -105       C  
ATOM    501  CD2 HIS A  67      38.804 -27.514   4.401  1.00 64.67           C  
ANISOU  501  CD2 HIS A  67     8439   8254   7877   1262   -139   -112       C  
ATOM    502  ND1 HIS A  67      39.228 -28.013   2.314  1.00 75.58           N  
ANISOU  502  ND1 HIS A  67     9856   9623   9238   1275   -138   -100       N  
ATOM    503  CE1 HIS A  67      38.578 -26.862   2.317  1.00 77.17           C  
ANISOU  503  CE1 HIS A  67    10051   9816   9453   1275   -143   -104       C  
ATOM    504  NE2 HIS A  67      38.309 -26.538   3.571  1.00 71.45           N  
ANISOU  504  NE2 HIS A  67     9306   9100   8742   1268   -143   -111       N  
ATOM    505  N   GLY A  68      41.405 -32.383   3.911  1.00 45.63           N  
ANISOU  505  N   GLY A  68     6060   5871   5405   1263   -120    -95       N  
ATOM    506  CA  GLY A  68      42.451 -33.383   3.887  1.00 40.48           C  
ANISOU  506  CA  GLY A  68     5415   5227   4739   1263   -112    -91       C  
ATOM    507  C   GLY A  68      42.226 -34.469   2.862  1.00 43.41           C  
ANISOU  507  C   GLY A  68     5806   5596   5092   1269   -116    -86       C  
ATOM    508  O   GLY A  68      43.098 -34.683   2.029  1.00 55.46           O  
ANISOU  508  O   GLY A  68     7347   7118   6606   1274   -109    -79       O  
ATOM    509  N   GLU A  69      41.082 -35.155   2.891  1.00 35.88           N  
ANISOU  509  N   GLU A  69     4854   4644   4136   1268   -127    -89       N  
ATOM    510  CA  GLU A  69      40.874 -36.219   1.900  1.00 32.13           C  
ANISOU  510  CA  GLU A  69     4398   4166   3643   1273   -131    -84       C  
ATOM    511  C   GLU A  69      40.670 -35.707   0.487  1.00 30.37           C  
ANISOU  511  C   GLU A  69     4194   3928   3415   1281   -134    -80       C  
ATOM    512  O   GLU A  69      40.931 -36.426  -0.468  1.00 31.75           O  
ANISOU  512  O   GLU A  69     4388   4100   3575   1287   -133    -74       O  
ATOM    513  CB  GLU A  69      39.738 -37.181   2.249  1.00 33.78           C  
ANISOU  513  CB  GLU A  69     4604   4381   3850   1269   -142    -89       C  
ATOM    514  CG  GLU A  69      39.080 -36.958   3.567  1.00 48.25           C  
ANISOU  514  CG  GLU A  69     6414   6221   5697   1261   -146    -96       C  
ATOM    515  CD  GLU A  69      37.956 -37.951   3.805  1.00 57.97           C  
ANISOU  515  CD  GLU A  69     7644   7457   6925   1258   -157   -100       C  
ATOM    516  OE1 GLU A  69      38.263 -39.118   4.162  1.00 59.82           O  
ANISOU  516  OE1 GLU A  69     7878   7700   7150   1256   -154    -99       O  
ATOM    517  OE2 GLU A  69      36.775 -37.561   3.626  1.00 57.43           O1-
ANISOU  517  OE2 GLU A  69     7574   7381   6864   1259   -168   -103       O1-
ATOM    518  N   GLN A  70      40.182 -34.485   0.334  1.00 35.64           N  
ANISOU  518  N   GLN A  70     4858   4587   4096   1283   -138    -82       N  
ATOM    519  CA  GLN A  70      40.010 -33.968  -1.012  1.00 45.55           C  
ANISOU  519  CA  GLN A  70     6132   5829   5347   1291   -140    -77       C  
ATOM    520  C   GLN A  70      41.386 -33.853  -1.608  1.00 46.84           C  
ANISOU  520  C   GLN A  70     6307   5990   5501   1295   -128    -70       C  
ATOM    521  O   GLN A  70      41.686 -34.470  -2.634  1.00 50.72           O  
ANISOU  521  O   GLN A  70     6817   6476   5977   1301   -126    -64       O  
ATOM    522  CB  GLN A  70      39.280 -32.625  -1.015  1.00 54.36           C  
ANISOU  522  CB  GLN A  70     7241   6936   6479   1291   -146    -81       C  
ATOM    523  CG  GLN A  70      37.826 -32.721  -0.565  1.00 60.65           C  
ANISOU  523  CG  GLN A  70     8028   7733   7283   1287   -159    -88       C  
ATOM    524  CD  GLN A  70      37.054 -33.847  -1.250  1.00 64.77           C  
ANISOU  524  CD  GLN A  70     8564   8254   7792   1289   -169    -86       C  
ATOM    525  NE2 GLN A  70      36.219 -33.473  -2.208  1.00 63.33           N  
ANISOU  525  NE2 GLN A  70     8394   8060   7609   1294   -178    -86       N  
ATOM    526  OE1 GLN A  70      37.198 -35.035  -0.917  1.00 67.01           O  
ANISOU  526  OE1 GLN A  70     8848   8547   8066   1287   -168    -86       O  
ATOM    527  N   THR A  71      42.241 -33.125  -0.898  1.00 44.68           N  
ANISOU  527  N   THR A  71     6020   5719   5237   1292   -118    -71       N  
ATOM    528  CA  THR A  71      43.619 -32.935  -1.322  1.00 34.70           C  
ANISOU  528  CA  THR A  71     4764   4453   3967   1296   -105    -64       C  
ATOM    529  C   THR A  71      44.387 -34.245  -1.522  1.00 31.16           C  
ANISOU  529  C   THR A  71     4325   4012   3501   1297    -99    -59       C  
ATOM    530  O   THR A  71      45.097 -34.407  -2.507  1.00 36.94           O  
ANISOU  530  O   THR A  71     5075   4739   4221   1303    -93    -52       O  
ATOM    531  CB  THR A  71      44.345 -32.011  -0.363  1.00 28.67           C  
ANISOU  531  CB  THR A  71     3982   3694   3219   1291    -96    -67       C  
ATOM    532  CG2 THR A  71      45.806 -31.911  -0.739  1.00 19.75           C  
ANISOU  532  CG2 THR A  71     2859   2562   2082   1294    -82    -60       C  
ATOM    533  OG1 THR A  71      43.740 -30.709  -0.437  1.00 31.11           O  
ANISOU  533  OG1 THR A  71     4285   3993   3543   1292   -101    -70       O  
ATOM    534  N   GLY A  72      44.213 -35.186  -0.609  1.00 26.04           N  
ANISOU  534  N   GLY A  72     3667   3376   2851   1291   -101    -63       N  
ATOM    535  CA  GLY A  72      44.860 -36.480  -0.706  1.00 21.13           C  
ANISOU  535  CA  GLY A  72     3053   2762   2212   1291    -96    -59       C  
ATOM    536  C   GLY A  72      44.402 -37.310  -1.886  1.00 24.48           C  
ANISOU  536  C   GLY A  72     3499   3181   2620   1297   -102    -55       C  
ATOM    537  O   GLY A  72      45.239 -37.858  -2.610  1.00 32.35           O  
ANISOU  537  O   GLY A  72     4512   4178   3603   1302    -95    -49       O  
ATOM    538  N   LYS A  73      43.087 -37.431  -2.079  1.00 18.08           N  
ANISOU  538  N   LYS A  73     2690   2367   1813   1297   -115    -59       N  
ATOM    539  CA  LYS A  73      42.567 -38.177  -3.221  1.00 21.84           C  
ANISOU  539  CA  LYS A  73     3186   2837   2274   1303   -122    -56       C  
ATOM    540  C   LYS A  73      43.064 -37.561  -4.542  1.00 28.12           C  
ANISOU  540  C   LYS A  73     4001   3619   3063   1311   -117    -49       C  
ATOM    541  O   LYS A  73      43.489 -38.288  -5.448  1.00 27.56           O  
ANISOU  541  O   LYS A  73     3949   3547   2977   1316   -115    -44       O  
ATOM    542  CB  LYS A  73      41.042 -38.276  -3.194  1.00 33.10           C  
ANISOU  542  CB  LYS A  73     4611   4261   3707   1301   -137    -62       C  
ATOM    543  CG  LYS A  73      40.478 -39.167  -2.085  1.00 51.13           C  
ANISOU  543  CG  LYS A  73     6878   6555   5992   1294   -142    -68       C  
ATOM    544  CD  LYS A  73      38.941 -39.047  -1.969  1.00 64.42           C  
ANISOU  544  CD  LYS A  73     8556   8235   7685   1291   -156    -74       C  
ATOM    545  CE  LYS A  73      38.388 -39.766  -0.721  1.00 66.12           C  
ANISOU  545  CE  LYS A  73     8754   8463   7906   1283   -160    -80       C  
ATOM    546  NZ  LYS A  73      37.024 -39.289  -0.307  1.00 63.55           N1+
ANISOU  546  NZ  LYS A  73     8417   8135   7594   1280   -172    -86       N1+
HETATM  547  N   MSE A  74      43.071 -36.234  -4.666  1.00 26.89           N  
ANISOU  547  N   MSE A  74     3841   3455   2920   1313   -116    -50       N  
HETATM  548  CA  MSE A  74      43.665 -35.727  -5.901  1.00 28.55           C  
ANISOU  548  CA  MSE A  74     4070   3654   3123   1320   -111    -43       C  
HETATM  549  C   MSE A  74      45.164 -35.910  -6.011  1.00 26.14           C  
ANISOU  549  C   MSE A  74     3771   3353   2809   1322    -96    -36       C  
HETATM  550  O   MSE A  74      45.654 -36.109  -7.104  1.00 32.68           O  
ANISOU  550  O   MSE A  74     4618   4174   3624   1329    -92    -29       O  
HETATM  551  CB  MSE A  74      43.277 -34.292  -6.268  1.00 29.66           C  
ANISOU  551  CB  MSE A  74     4210   3784   3277   1323   -113    -43       C  
HETATM  552  CG  MSE A  74      42.312 -33.639  -5.344  1.00 35.76           C  
ANISOU  552  CG  MSE A  74     4963   4557   4067   1317   -122    -51       C  
HETATM  553  CE  MSE A  74      41.738 -30.985  -4.430  1.00 15.84           C  
ANISOU  553  CE  MSE A  74     2412   2025   1580   1314   -124    -59       C  
HETATM  554 SE   MSE A  74      41.549 -31.985  -6.054  1.00 65.30          SE  
ANISOU  554 SE   MSE A  74     8707   8282   7822   1322   -128    -52      SE  
ATOM    555  N   LEU A  75      45.900 -35.810  -4.909  1.00 21.58           N  
ANISOU  555  N   LEU A  75     3176   2785   2239   1317    -88    -38       N  
ATOM    556  CA  LEU A  75      47.329 -36.137  -4.934  1.00 18.91           C  
ANISOU  556  CA  LEU A  75     2842   2452   1892   1318    -74    -32       C  
ATOM    557  C   LEU A  75      47.564 -37.536  -5.545  1.00 29.63           C  
ANISOU  557  C   LEU A  75     4216   3813   3229   1321    -73    -27       C  
ATOM    558  O   LEU A  75      48.339 -37.707  -6.496  1.00 34.55           O  
ANISOU  558  O   LEU A  75     4856   4431   3839   1327    -66    -20       O  
ATOM    559  CB  LEU A  75      47.898 -36.070  -3.533  1.00 15.47           C  
ANISOU  559  CB  LEU A  75     2384   2027   1466   1310    -68    -35       C  
ATOM    560  CG  LEU A  75      48.898 -34.959  -3.265  1.00 20.05           C  
ANISOU  560  CG  LEU A  75     2956   2605   2057   1310    -57    -34       C  
ATOM    561  CD1 LEU A  75      48.530 -33.748  -4.051  1.00 28.91           C  
ANISOU  561  CD1 LEU A  75     4084   3713   3187   1315    -59    -33       C  
ATOM    562  CD2 LEU A  75      48.905 -34.613  -1.788  1.00 17.37           C  
ANISOU  562  CD2 LEU A  75     2591   2275   1734   1301    -56    -41       C  
ATOM    563  N   ILE A  76      46.850 -38.524  -5.021  1.00 30.81           N  
ANISOU  563  N   ILE A  76     4361   3971   3375   1317    -81    -32       N  
ATOM    564  CA  ILE A  76      46.911 -39.879  -5.553  1.00 29.58           C  
ANISOU  564  CA  ILE A  76     4219   3818   3201   1319    -82    -29       C  
ATOM    565  C   ILE A  76      46.509 -39.976  -7.046  1.00 31.00           C  
ANISOU  565  C   ILE A  76     4423   3986   3369   1327    -87    -25       C  
ATOM    566  O   ILE A  76      47.287 -40.494  -7.874  1.00 33.54           O  
ANISOU  566  O   ILE A  76     4762   4306   3676   1332    -80    -18       O  
ATOM    567  CB  ILE A  76      46.076 -40.830  -4.659  1.00 26.81           C  
ANISOU  567  CB  ILE A  76     3857   3478   2851   1312    -91    -35       C  
ATOM    568  CG1 ILE A  76      46.821 -41.079  -3.342  1.00 32.67           C  
ANISOU  568  CG1 ILE A  76     4580   4233   3598   1305    -83    -37       C  
ATOM    569  CG2 ILE A  76      45.777 -42.141  -5.375  1.00 19.79           C  
ANISOU  569  CG2 ILE A  76     2985   2590   1945   1315    -95    -34       C  
ATOM    570  CD1 ILE A  76      46.022 -40.827  -2.067  1.00 15.16           C  
ANISOU  570  CD1 ILE A  76     2340   2023   1397   1297    -90    -46       C  
ATOM    571  N   GLU A  77      45.324 -39.452  -7.388  1.00 29.75           N  
ANISOU  571  N   GLU A  77     4266   3819   3219   1328    -98    -29       N  
ATOM    572  CA  GLU A  77      44.758 -39.592  -8.744  1.00 34.85           C  
ANISOU  572  CA  GLU A  77     4933   4454   3855   1335   -105    -26       C  
ATOM    573  C   GLU A  77      45.519 -38.816  -9.830  1.00 33.97           C  
ANISOU  573  C   GLU A  77     4837   4331   3739   1342    -97    -19       C  
ATOM    574  O   GLU A  77      45.919 -39.380 -10.880  1.00 35.94           O  
ANISOU  574  O   GLU A  77     5107   4577   3972   1348    -94    -13       O  
ATOM    575  CB  GLU A  77      43.280 -39.197  -8.758  1.00 38.47           C  
ANISOU  575  CB  GLU A  77     5387   4907   4324   1333   -120    -32       C  
ATOM    576  CG  GLU A  77      42.373 -40.159  -8.021  1.00 49.13           C  
ANISOU  576  CG  GLU A  77     6728   6265   5675   1327   -129    -38       C  
ATOM    577  CD  GLU A  77      42.508 -41.583  -8.528  1.00 65.02           C  
ANISOU  577  CD  GLU A  77     8754   8281   7669   1329   -129    -36       C  
ATOM    578  OE1 GLU A  77      42.527 -41.773  -9.765  1.00 71.46           O  
ANISOU  578  OE1 GLU A  77     9591   9088   8474   1336   -130    -32       O  
ATOM    579  OE2 GLU A  77      42.610 -42.513  -7.694  1.00 68.73           O1-
ANISOU  579  OE2 GLU A  77     9214   8762   8136   1324   -129    -39       O1-
ATOM    580  N   ILE A  78      45.706 -37.523  -9.573  1.00 25.90           N  
ANISOU  580  N   ILE A  78     3805   3304   2731   1342    -94    -19       N  
ATOM    581  CA  ILE A  78      46.557 -36.688 -10.408  1.00 26.49           C  
ANISOU  581  CA  ILE A  78     3891   3369   2803   1348    -84    -12       C  
ATOM    582  C   ILE A  78      47.907 -37.342 -10.579  1.00 27.99           C  
ANISOU  582  C   ILE A  78     4089   3565   2979   1350    -71     -5       C  
ATOM    583  O   ILE A  78      48.460 -37.323 -11.677  1.00 31.72           O  
ANISOU  583  O   ILE A  78     4580   4030   3440   1356    -65      1       O  
ATOM    584  CB  ILE A  78      46.721 -35.257  -9.855  1.00 25.42           C  
ANISOU  584  CB  ILE A  78     3741   3231   2687   1346    -81    -14       C  
ATOM    585  CG1 ILE A  78      45.387 -34.511  -9.952  1.00 16.01           C  
ANISOU  585  CG1 ILE A  78     2546   2032   1507   1345    -94    -19       C  
ATOM    586  CG2 ILE A  78      47.803 -34.492 -10.620  1.00 16.04           C  
ANISOU  586  CG2 ILE A  78     2564   2035   1496   1352    -69     -6       C  
ATOM    587  CD1 ILE A  78      45.346 -33.234  -9.174  1.00 16.02           C  
ANISOU  587  CD1 ILE A  78     2528   2031   1528   1342    -93    -23       C  
ATOM    588  N   GLU A  79      48.426 -37.956  -9.518  1.00 29.82           N  
ANISOU  588  N   GLU A  79     4308   3810   3212   1344    -66     -7       N  
ATOM    589  CA  GLU A  79      49.688 -38.688  -9.667  1.00 33.03           C  
ANISOU  589  CA  GLU A  79     4723   4223   3605   1346    -54     -1       C  
ATOM    590  C   GLU A  79      49.633 -39.861 -10.650  1.00 30.89           C  
ANISOU  590  C   GLU A  79     4473   3951   3313   1350    -55      3       C  
ATOM    591  O   GLU A  79      50.579 -40.077 -11.412  1.00 30.81           O  
ANISOU  591  O   GLU A  79     4477   3938   3290   1356    -46     10       O  
ATOM    592  CB  GLU A  79      50.221 -39.186  -8.335  1.00 31.36           C  
ANISOU  592  CB  GLU A  79     4493   4026   3398   1338    -49     -4       C  
ATOM    593  CG  GLU A  79      51.588 -39.778  -8.461  1.00 30.16           C  
ANISOU  593  CG  GLU A  79     4348   3880   3233   1340    -35      3       C  
ATOM    594  CD  GLU A  79      52.031 -40.408  -7.190  1.00 32.76           C  
ANISOU  594  CD  GLU A  79     4660   4224   3564   1333    -31      0       C  
ATOM    595  OE1 GLU A  79      51.341 -41.347  -6.727  1.00 39.13           O  
ANISOU  595  OE1 GLU A  79     5462   5038   4367   1329    -39     -4       O  
ATOM    596  OE2 GLU A  79      53.053 -39.943  -6.651  1.00 27.34           O1-
ANISOU  596  OE2 GLU A  79     3964   3540   2883   1331    -21      3       O1-
ATOM    597  N   LYS A  80      48.550 -40.631 -10.624  1.00 23.77           N  
ANISOU  597  N   LYS A  80     3572   3051   2409   1349    -67     -2       N  
ATOM    598  CA  LYS A  80      48.455 -41.752 -11.555  1.00 22.51           C  
ANISOU  598  CA  LYS A  80     3432   2889   2230   1353    -70      0       C  
ATOM    599  C   LYS A  80      48.429 -41.238 -12.999  1.00 26.97           C  
ANISOU  599  C   LYS A  80     4018   3441   2789   1361    -69      5       C  
ATOM    600  O   LYS A  80      49.108 -41.785 -13.903  1.00 28.35           O  
ANISOU  600  O   LYS A  80     4212   3613   2948   1366    -63     11       O  
ATOM    601  CB  LYS A  80      47.245 -42.624 -11.242  1.00 33.72           C  
ANISOU  601  CB  LYS A  80     4848   4314   3650   1349    -83     -6       C  
ATOM    602  CG  LYS A  80      47.482 -43.624 -10.125  1.00 44.99           C  
ANISOU  602  CG  LYS A  80     6262   5756   5076   1343    -81     -9       C  
ATOM    603  CD  LYS A  80      46.212 -43.868  -9.321  1.00 57.17           C  
ANISOU  603  CD  LYS A  80     7790   7302   6629   1337    -94    -18       C  
ATOM    604  CE  LYS A  80      46.401 -45.058  -8.386  1.00 65.73           C  
ANISOU  604  CE  LYS A  80     8865   8401   7708   1331    -93    -20       C  
ATOM    605  NZ  LYS A  80      47.784 -45.097  -7.807  1.00 67.57           N1+
ANISOU  605  NZ  LYS A  80     9092   8643   7939   1329    -78    -16       N1+
ATOM    606  N   VAL A  81      47.690 -40.153 -13.222  1.00 30.30           N  
ANISOU  606  N   VAL A  81     4437   3853   3223   1362    -76      3       N  
ATOM    607  CA  VAL A  81      47.739 -39.551 -14.555  1.00 26.88           C  
ANISOU  607  CA  VAL A  81     4023   3406   2784   1369    -75      8       C  
ATOM    608  C   VAL A  81      49.137 -39.036 -14.933  1.00 25.60           C  
ANISOU  608  C   VAL A  81     3868   3242   2618   1374    -60     16       C  
ATOM    609  O   VAL A  81      49.627 -39.343 -15.991  1.00 19.64           O  
ANISOU  609  O   VAL A  81     3133   2482   1849   1380    -55     22       O  
ATOM    610  CB  VAL A  81      46.706 -38.430 -14.761  1.00 27.37           C  
ANISOU  610  CB  VAL A  81     4082   3458   2860   1370    -85      5       C  
ATOM    611  CG1 VAL A  81      46.936 -37.777 -16.111  1.00 29.58           C  
ANISOU  611  CG1 VAL A  81     4381   3723   3134   1378    -82     11       C  
ATOM    612  CG2 VAL A  81      45.291 -38.962 -14.670  1.00 26.14           C  
ANISOU  612  CG2 VAL A  81     3924   3302   2707   1367   -101     -2       C  
ATOM    613  N   LEU A  82      49.790 -38.261 -14.080  1.00 25.20           N  
ANISOU  613  N   LEU A  82     3801   3195   2579   1370    -52     17       N  
ATOM    614  CA  LEU A  82      51.059 -37.681 -14.500  1.00 29.91           C  
ANISOU  614  CA  LEU A  82     4404   3787   3173   1374    -38     24       C  
ATOM    615  C   LEU A  82      52.158 -38.730 -14.658  1.00 34.76           C  
ANISOU  615  C   LEU A  82     5027   4409   3770   1376    -27     30       C  
ATOM    616  O   LEU A  82      53.106 -38.544 -15.422  1.00 35.86           O  
ANISOU  616  O   LEU A  82     5181   4544   3901   1381    -16     38       O  
ATOM    617  CB  LEU A  82      51.495 -36.539 -13.579  1.00 30.08           C  
ANISOU  617  CB  LEU A  82     4406   3811   3213   1371    -32     23       C  
ATOM    618  CG  LEU A  82      50.559 -35.325 -13.520  1.00 26.94           C  
ANISOU  618  CG  LEU A  82     4000   3404   2832   1370    -41     18       C  
ATOM    619  CD1 LEU A  82      51.292 -34.131 -12.943  1.00 27.79           C  
ANISOU  619  CD1 LEU A  82     4094   3510   2955   1368    -31     19       C  
ATOM    620  CD2 LEU A  82      49.981 -34.989 -14.879  1.00 24.43           C  
ANISOU  620  CD2 LEU A  82     3702   3072   2508   1377    -46     21       C  
ATOM    621  N   LEU A  83      52.033 -39.837 -13.938  1.00 39.62           N  
ANISOU  621  N   LEU A  83     5636   5036   4380   1371    -29     26       N  
ATOM    622  CA  LEU A  83      52.932 -40.966 -14.168  1.00 32.53           C  
ANISOU  622  CA  LEU A  83     4749   4146   3466   1373    -21     31       C  
ATOM    623  C   LEU A  83      52.680 -41.552 -15.544  1.00 30.99           C  
ANISOU  623  C   LEU A  83     4579   3943   3254   1380    -24     35       C  
ATOM    624  O   LEU A  83      53.625 -41.804 -16.280  1.00 30.23           O  
ANISOU  624  O   LEU A  83     4497   3844   3144   1385    -13     42       O  
ATOM    625  CB  LEU A  83      52.766 -42.053 -13.114  1.00 23.84           C  
ANISOU  625  CB  LEU A  83     3636   3059   2363   1366    -24     26       C  
ATOM    626  CG  LEU A  83      53.306 -41.732 -11.737  1.00 20.42           C  
ANISOU  626  CG  LEU A  83     3180   2637   1944   1359    -19     24       C  
ATOM    627  CD1 LEU A  83      53.155 -42.950 -10.882  1.00 19.09           C  
ANISOU  627  CD1 LEU A  83     3002   2480   1769   1354    -22     20       C  
ATOM    628  CD2 LEU A  83      54.737 -41.294 -11.821  1.00 15.74           C  
ANISOU  628  CD2 LEU A  83     2589   2044   1349   1361     -3     32       C  
ATOM    629  N   LYS A  84      51.413 -41.773 -15.893  1.00 27.15           N  
ANISOU  629  N   LYS A  84     4096   3451   2767   1380    -38     29       N  
ATOM    630  CA  LYS A  84      51.092 -42.215 -17.261  1.00 28.04           C  
ANISOU  630  CA  LYS A  84     4232   3555   2866   1386    -41     32       C  
ATOM    631  C   LYS A  84      51.493 -41.219 -18.387  1.00 36.37           C  
ANISOU  631  C   LYS A  84     5302   4597   3919   1393    -35     38       C  
ATOM    632  O   LYS A  84      52.152 -41.602 -19.345  1.00 33.78           O  
ANISOU  632  O   LYS A  84     4993   4266   3577   1399    -28     44       O  
ATOM    633  CB  LYS A  84      49.606 -42.561 -17.352  1.00 28.91           C  
ANISOU  633  CB  LYS A  84     4342   3663   2979   1384    -58     25       C  
ATOM    634  CG  LYS A  84      49.142 -43.185 -18.652  1.00 32.73           C  
ANISOU  634  CG  LYS A  84     4848   4138   3449   1390    -63     26       C  
ATOM    635  CD  LYS A  84      47.641 -43.495 -18.561  1.00 43.56           C  
ANISOU  635  CD  LYS A  84     6216   5508   4826   1387    -80     18       C  
ATOM    636  CE  LYS A  84      47.297 -44.198 -17.226  1.00 47.66           C  
ANISOU  636  CE  LYS A  84     6717   6041   5352   1379    -85     12       C  
ATOM    637  NZ  LYS A  84      45.848 -44.545 -17.094  1.00 50.24           N1+
ANISOU  637  NZ  LYS A  84     7039   6366   5685   1376   -101      4       N1+
ATOM    638  N   GLU A  85      51.112 -39.947 -18.259  1.00 37.62           N  
ANISOU  638  N   GLU A  85     5452   4749   4094   1393    -38     37       N  
ATOM    639  CA  GLU A  85      51.280 -38.948 -19.322  1.00 36.99           C  
ANISOU  639  CA  GLU A  85     5386   4655   4014   1400    -35     42       C  
ATOM    640  C   GLU A  85      52.676 -38.372 -19.450  1.00 35.64           C  
ANISOU  640  C   GLU A  85     5217   4483   3841   1402    -19     50       C  
ATOM    641  O   GLU A  85      53.076 -37.977 -20.539  1.00 43.78           O  
ANISOU  641  O   GLU A  85     6265   5505   4865   1409    -13     56       O  
ATOM    642  CB  GLU A  85      50.310 -37.782 -19.139  1.00 34.16           C  
ANISOU  642  CB  GLU A  85     5017   4289   3673   1398    -45     38       C  
ATOM    643  CG  GLU A  85      48.858 -38.146 -19.267  1.00 33.13           C  
ANISOU  643  CG  GLU A  85     4888   4156   3544   1396    -61     31       C  
ATOM    644  CD  GLU A  85      48.407 -38.285 -20.690  1.00 36.27           C  
ANISOU  644  CD  GLU A  85     5308   4543   3931   1403    -66     33       C  
ATOM    645  OE1 GLU A  85      49.213 -38.053 -21.620  1.00 41.32           O  
ANISOU  645  OE1 GLU A  85     5963   5176   4561   1409    -57     41       O  
ATOM    646  OE2 GLU A  85      47.232 -38.626 -20.879  1.00 16.63           O1-
ANISOU  646  OE2 GLU A  85     2822   2052   1444   1402    -80     28       O1-
ATOM    647  N   LYS A  86      53.393 -38.305 -18.338  1.00 27.60           N  
ANISOU  647  N   LYS A  86     4181   3475   2830   1398    -11     50       N  
ATOM    648  CA  LYS A  86      54.753 -37.772 -18.311  1.00 32.90           C  
ANISOU  648  CA  LYS A  86     4852   4146   3502   1399      5     57       C  
ATOM    649  C   LYS A  86      54.940 -36.482 -19.119  1.00 32.96           C  
ANISOU  649  C   LYS A  86     4867   4140   3515   1405      9     62       C  
ATOM    650  O   LYS A  86      55.683 -36.470 -20.096  1.00 36.13           O  
ANISOU  650  O   LYS A  86     5286   4536   3905   1411     18     70       O  
ATOM    651  CB  LYS A  86      55.763 -38.822 -18.800  1.00 34.17           C  
ANISOU  651  CB  LYS A  86     5027   4312   3643   1403     15     64       C  
ATOM    652  CG  LYS A  86      55.566 -40.220 -18.257  1.00 38.40           C  
ANISOU  652  CG  LYS A  86     5561   4860   4170   1399     11     60       C  
ATOM    653  CD  LYS A  86      55.183 -41.227 -19.362  1.00 50.34           C  
ANISOU  653  CD  LYS A  86     7095   6369   5664   1404      7     61       C  
ATOM    654  CE  LYS A  86      55.196 -42.685 -18.830  1.00 97.13           C  
ANISOU  654  CE  LYS A  86    13019  12308  11579   1400      5     58       C  
ATOM    655  NZ  LYS A  86      54.629 -43.731 -19.748  1.00 92.31           N1+
ANISOU  655  NZ  LYS A  86    12426  11694  10953   1403     -2     56       N1+
ATOM    656  N   PRO A  87      54.270 -35.393 -18.721  1.00 31.98           N  
ANISOU  656  N   PRO A  87     4731   4011   3410   1402      2     57       N  
ATOM    657  CA  PRO A  87      54.483 -34.135 -19.444  1.00 29.40           C  
ANISOU  657  CA  PRO A  87     4411   3672   3090   1407      7     62       C  
ATOM    658  C   PRO A  87      55.741 -33.399 -18.983  1.00 32.02           C  
ANISOU  658  C   PRO A  87     4733   4005   3429   1407     22     67       C  
ATOM    659  O   PRO A  87      56.411 -33.833 -18.044  1.00 42.14           O  
ANISOU  659  O   PRO A  87     6002   5297   4712   1402     28     66       O  
ATOM    660  CB  PRO A  87      53.255 -33.322 -19.058  1.00 28.19           C  
ANISOU  660  CB  PRO A  87     4245   3514   2953   1404     -6     55       C  
ATOM    661  CG  PRO A  87      52.962 -33.784 -17.663  1.00 25.33           C  
ANISOU  661  CG  PRO A  87     3861   3163   2599   1396    -11     47       C  
ATOM    662  CD  PRO A  87      53.244 -35.257 -17.667  1.00 29.23           C  
ANISOU  662  CD  PRO A  87     4362   3667   3075   1396    -10     48       C  
ATOM    663  N   ASP A  88      56.043 -32.286 -19.643  1.00 24.14           N  
ANISOU  663  N   ASP A  88     3740   2995   2436   1411     27     71       N  
ATOM    664  CA  ASP A  88      57.180 -31.446 -19.298  1.00 24.56           C  
ANISOU  664  CA  ASP A  88     3786   3048   2499   1411     41     76       C  
ATOM    665  C   ASP A  88      56.716 -30.285 -18.436  1.00 28.19           C  
ANISOU  665  C   ASP A  88     4225   3505   2981   1406     36     70       C  
ATOM    666  O   ASP A  88      57.416 -29.857 -17.522  1.00 36.98           O  
ANISOU  666  O   ASP A  88     5321   4624   4106   1402     44     69       O  
ATOM    667  CB  ASP A  88      57.844 -30.891 -20.560  1.00 33.95           C  
ANISOU  667  CB  ASP A  88     4994   4225   3680   1419     50     85       C  
ATOM    668  CG  ASP A  88      57.963 -31.929 -21.667  1.00 43.41           C  
ANISOU  668  CG  ASP A  88     6216   5422   4855   1424     51     90       C  
ATOM    669  OD1 ASP A  88      58.930 -32.719 -21.620  1.00 42.94           O  
ANISOU  669  OD1 ASP A  88     6161   5370   4784   1425     62     95       O  
ATOM    670  OD2 ASP A  88      57.098 -31.949 -22.582  1.00 42.25           O1-
ANISOU  670  OD2 ASP A  88     6084   5268   4703   1428     42     90       O1-
ATOM    671  N   VAL A  89      55.535 -29.761 -18.738  1.00 24.47           N  
ANISOU  671  N   VAL A  89     3755   3027   2517   1407     24     65       N  
ATOM    672  CA  VAL A  89      54.966 -28.705 -17.922  1.00 29.38           C  
ANISOU  672  CA  VAL A  89     4356   3646   3160   1402     18     59       C  
ATOM    673  C   VAL A  89      53.573 -29.059 -17.434  1.00 28.06           C  
ANISOU  673  C   VAL A  89     4182   3483   2998   1398      2     50       C  
ATOM    674  O   VAL A  89      52.754 -29.609 -18.186  1.00 23.15           O  
ANISOU  674  O   VAL A  89     3574   2858   2366   1401     -8     49       O  
ATOM    675  CB  VAL A  89      54.859 -27.354 -18.669  1.00 30.20           C  
ANISOU  675  CB  VAL A  89     4466   3735   3273   1407     19     62       C  
ATOM    676  CG1 VAL A  89      54.976 -26.212 -17.668  1.00 27.76           C  
ANISOU  676  CG1 VAL A  89     4135   3427   2987   1402     22     57       C  
ATOM    677  CG2 VAL A  89      55.917 -27.232 -19.720  1.00 29.98           C  
ANISOU  677  CG2 VAL A  89     4457   3701   3234   1414     33     72       C  
ATOM    678  N   VAL A  90      53.310 -28.717 -16.173  1.00 25.65           N  
ANISOU  678  N   VAL A  90     3854   3185   2709   1391     -1     42       N  
ATOM    679  CA  VAL A  90      51.958 -28.718 -15.641  1.00 16.68           C  
ANISOU  679  CA  VAL A  90     2707   2050   1582   1387    -17     34       C  
ATOM    680  C   VAL A  90      51.523 -27.286 -15.431  1.00 29.95           C  
ANISOU  680  C   VAL A  90     4376   3721   3282   1386    -20     30       C  
ATOM    681  O   VAL A  90      52.165 -26.526 -14.717  1.00 36.10           O  
ANISOU  681  O   VAL A  90     5140   4502   4074   1383    -12     29       O  
ATOM    682  CB  VAL A  90      51.870 -29.495 -14.334  1.00 20.93           C  
ANISOU  682  CB  VAL A  90     3226   2602   2123   1379    -19     27       C  
ATOM    683  CG1 VAL A  90      50.632 -29.094 -13.539  1.00 16.51           C  
ANISOU  683  CG1 VAL A  90     2650   2044   1579   1374    -32     18       C  
ATOM    684  CG2 VAL A  90      51.884 -30.995 -14.620  1.00 17.07           C  
ANISOU  684  CG2 VAL A  90     2749   2121   1615   1380    -21     29       C  
ATOM    685  N   VAL A  91      50.431 -26.916 -16.075  1.00 16.82           N  
ANISOU  685  N   VAL A  91     2720   2049   1620   1389    -31     28       N  
ATOM    686  CA  VAL A  91      49.891 -25.578 -15.962  1.00 26.15           C  
ANISOU  686  CA  VAL A  91     3893   3222   2820   1388    -35     25       C  
ATOM    687  C   VAL A  91      48.617 -25.560 -15.119  1.00 25.85           C  
ANISOU  687  C   VAL A  91     3840   3189   2794   1383    -49     15       C  
ATOM    688  O   VAL A  91      47.699 -26.350 -15.357  1.00 18.15           O  
ANISOU  688  O   VAL A  91     2871   2215   1810   1383    -60     13       O  
ATOM    689  CB  VAL A  91      49.557 -25.031 -17.344  1.00 27.26           C  
ANISOU  689  CB  VAL A  91     4054   3349   2956   1396    -38     30       C  
ATOM    690  CG1 VAL A  91      49.072 -23.592 -17.252  1.00 18.87           C  
ANISOU  690  CG1 VAL A  91     2983   2277   1912   1396    -41     27       C  
ATOM    691  CG2 VAL A  91      50.765 -25.152 -18.237  1.00 30.14           C  
ANISOU  691  CG2 VAL A  91     4436   3710   3307   1402    -24     40       C  
ATOM    692  N   VAL A  92      48.572 -24.643 -14.149  1.00 16.80           N  
ANISOU  692  N   VAL A  92     2673   2044   1666   1378    -49     10       N  
ATOM    693  CA  VAL A  92      47.423 -24.455 -13.271  1.00 16.75           C  
ANISOU  693  CA  VAL A  92     2650   2041   1673   1372    -61      1       C  
ATOM    694  C   VAL A  92      47.055 -22.970 -13.217  1.00 23.91           C  
ANISOU  694  C   VAL A  92     3548   2938   2598   1372    -63     -2       C  
ATOM    695  O   VAL A  92      47.917 -22.117 -13.364  1.00 27.30           O  
ANISOU  695  O   VAL A  92     3976   3362   3034   1374    -52      2       O  
ATOM    696  CB  VAL A  92      47.717 -25.006 -11.829  1.00 23.46           C  
ANISOU  696  CB  VAL A  92     3478   2906   2529   1364    -58     -5       C  
ATOM    697  CG1 VAL A  92      47.619 -26.520 -11.808  1.00 16.53           C  
ANISOU  697  CG1 VAL A  92     2608   2039   1635   1363    -61     -5       C  
ATOM    698  CG2 VAL A  92      49.087 -24.567 -11.329  1.00 16.59           C  
ANISOU  698  CG2 VAL A  92     2600   2040   1665   1363    -43     -2       C  
ATOM    699  N   GLN A  93      45.779 -22.645 -13.045  1.00 20.31           N  
ANISOU  699  N   GLN A  93     3087   2480   2152   1371    -76     -8       N  
ATOM    700  CA  GLN A  93      45.433 -21.247 -12.776  1.00 21.14           C  
ANISOU  700  CA  GLN A  93     3180   2578   2276   1370    -78    -12       C  
ATOM    701  C   GLN A  93      44.615 -21.154 -11.505  1.00 29.83           C  
ANISOU  701  C   GLN A  93     4258   3686   3390   1362    -86    -21       C  
ATOM    702  O   GLN A  93      43.748 -21.985 -11.269  1.00 36.62           O  
ANISOU  702  O   GLN A  93     5117   4552   4245   1359    -96    -25       O  
ATOM    703  CB  GLN A  93      44.676 -20.570 -13.927  1.00 17.02           C  
ANISOU  703  CB  GLN A  93     2673   2041   1753   1376    -85     -9       C  
ATOM    704  CG  GLN A  93      44.334 -19.118 -13.635  1.00 17.08           C  
ANISOU  704  CG  GLN A  93     2668   2041   1780   1375    -87    -13       C  
ATOM    705  CD  GLN A  93      42.977 -18.928 -12.938  1.00 25.75           C  
ANISOU  705  CD  GLN A  93     3753   3142   2890   1370   -101    -22       C  
ATOM    706  NE2 GLN A  93      42.845 -17.865 -12.155  1.00 17.04           N  
ANISOU  706  NE2 GLN A  93     2632   2038   1807   1366   -100    -27       N  
ATOM    707  OE1 GLN A  93      42.072 -19.729 -13.107  1.00 26.27           O  
ANISOU  707  OE1 GLN A  93     3823   3209   2948   1369   -112    -24       O  
ATOM    708  N   GLY A  94      44.903 -20.150 -10.681  1.00 27.66           N  
ANISOU  708  N   GLY A  94     3965   3411   3133   1358    -81    -25       N  
ATOM    709  CA  GLY A  94      44.063 -19.878  -9.545  1.00 27.68           C  
ANISOU  709  CA  GLY A  94     3947   3420   3151   1352    -89    -35       C  
ATOM    710  C   GLY A  94      44.590 -20.475  -8.271  1.00 27.53           C  
ANISOU  710  C   GLY A  94     3910   3415   3134   1344    -84    -39       C  
ATOM    711  O   GLY A  94      45.797 -20.701  -8.134  1.00 23.36           O  
ANISOU  711  O   GLY A  94     3381   2891   2602   1344    -72    -35       O  
ATOM    712  N   ASP A  95      43.675 -20.736  -7.342  1.00 26.48           N  
ANISOU  712  N   ASP A  95     3762   3290   3008   1338    -94    -47       N  
ATOM    713  CA  ASP A  95      44.066 -21.064  -5.987  1.00 24.24           C  
ANISOU  713  CA  ASP A  95     3458   3019   2731   1331    -89    -52       C  
ATOM    714  C   ASP A  95      43.126 -22.013  -5.235  1.00 23.86           C  
ANISOU  714  C   ASP A  95     3402   2983   2682   1325   -100    -58       C  
ATOM    715  O   ASP A  95      42.956 -21.881  -4.024  1.00 23.35           O  
ANISOU  715  O   ASP A  95     3317   2926   2628   1318   -101    -65       O  
ATOM    716  CB  ASP A  95      44.290 -19.772  -5.192  1.00 25.01           C  
ANISOU  716  CB  ASP A  95     3537   3116   2850   1327    -85    -57       C  
ATOM    717  CG  ASP A  95      43.065 -18.884  -5.152  1.00 30.98           C  
ANISOU  717  CG  ASP A  95     4288   3865   3619   1327    -96    -62       C  
ATOM    718  OD1 ASP A  95      41.935 -19.398  -5.060  1.00 34.50           O  
ANISOU  718  OD1 ASP A  95     4733   4313   4062   1325   -108    -66       O  
ATOM    719  OD2 ASP A  95      43.233 -17.654  -5.202  1.00 36.97           O1-
ANISOU  719  OD2 ASP A  95     5040   4615   4390   1328    -93    -63       O1-
ATOM    720  N   THR A  96      42.533 -22.974  -5.937  1.00 21.44           N  
ANISOU  720  N   THR A  96     3111   2676   2360   1328   -107    -56       N  
ATOM    721  CA  THR A  96      41.708 -23.974  -5.273  1.00 21.38           C  
ANISOU  721  CA  THR A  96     3096   2678   2349   1323   -117    -61       C  
ATOM    722  C   THR A  96      42.582 -25.092  -4.754  1.00 24.90           C  
ANISOU  722  C   THR A  96     3540   3137   2785   1320   -109    -59       C  
ATOM    723  O   THR A  96      43.790 -25.065  -4.922  1.00 25.80           O  
ANISOU  723  O   THR A  96     3657   3250   2894   1322    -97    -54       O  
ATOM    724  CB  THR A  96      40.675 -24.576  -6.216  1.00 26.76           C  
ANISOU  724  CB  THR A  96     3794   3354   3019   1327   -128    -60       C  
ATOM    725  CG2 THR A  96      39.619 -23.550  -6.581  1.00 24.96           C  
ANISOU  725  CG2 THR A  96     3566   3115   2802   1329   -138    -62       C  
ATOM    726  OG1 THR A  96      41.330 -25.015  -7.405  1.00 29.67           O  
ANISOU  726  OG1 THR A  96     4184   3717   3371   1334   -123    -51       O  
ATOM    727  N   ASN A  97      41.967 -26.080  -4.118  1.00 33.13           N  
ANISOU  727  N   ASN A  97     4576   4189   3823   1315   -116    -64       N  
ATOM    728  CA  ASN A  97      42.710 -27.234  -3.628  1.00 25.09           C  
ANISOU  728  CA  ASN A  97     3556   3183   2795   1312   -109    -62       C  
ATOM    729  C   ASN A  97      43.274 -28.074  -4.795  1.00 29.08           C  
ANISOU  729  C   ASN A  97     4084   3684   3279   1319   -106    -54       C  
ATOM    730  O   ASN A  97      44.346 -28.662  -4.698  1.00 27.06           O  
ANISOU  730  O   ASN A  97     3831   3435   3016   1319    -95    -50       O  
ATOM    731  CB  ASN A  97      41.855 -28.050  -2.646  1.00 18.80           C  
ANISOU  731  CB  ASN A  97     2746   2397   1999   1305   -118    -69       C  
ATOM    732  CG  ASN A  97      41.804 -27.420  -1.234  1.00 45.53           C  
ANISOU  732  CG  ASN A  97     6107   5791   5404   1298   -116    -77       C  
ATOM    733  ND2 ASN A  97      40.911 -27.932  -0.380  1.00 51.56           N  
ANISOU  733  ND2 ASN A  97     6858   6562   6171   1292   -125    -83       N  
ATOM    734  OD1 ASN A  97      42.568 -26.497  -0.920  1.00 52.34           O  
ANISOU  734  OD1 ASN A  97     6960   6650   6276   1297   -108    -77       O  
ATOM    735  N   THR A  98      42.557 -28.096  -5.910  1.00 32.59           N  
ANISOU  735  N   THR A  98     4546   4120   3718   1325   -113    -51       N  
ATOM    736  CA  THR A  98      43.040 -28.748  -7.123  1.00 33.79           C  
ANISOU  736  CA  THR A  98     4721   4266   3851   1331   -110    -44       C  
ATOM    737  C   THR A  98      44.384 -28.184  -7.561  1.00 32.56           C  
ANISOU  737  C   THR A  98     4572   4106   3693   1335    -96    -37       C  
ATOM    738  O   THR A  98      45.323 -28.932  -7.817  1.00 40.53           O  
ANISOU  738  O   THR A  98     5591   5121   4690   1337    -87    -32       O  
ATOM    739  CB  THR A  98      42.025 -28.592  -8.301  1.00 31.94           C  
ANISOU  739  CB  THR A  98     4503   4020   3611   1337   -121    -42       C  
ATOM    740  CG2 THR A  98      42.604 -29.116  -9.594  1.00 27.17           C  
ANISOU  740  CG2 THR A  98     3924   3410   2990   1344   -116    -34       C  
ATOM    741  OG1 THR A  98      40.829 -29.319  -8.016  1.00 34.91           O  
ANISOU  741  OG1 THR A  98     4877   4400   3987   1334   -134    -48       O  
ATOM    742  N   VAL A  99      44.460 -26.863  -7.656  1.00 24.72           N  
ANISOU  742  N   VAL A  99     3574   3105   2713   1337    -94    -37       N  
ATOM    743  CA  VAL A  99      45.671 -26.182  -8.079  1.00 24.46           C  
ANISOU  743  CA  VAL A  99     3547   3066   2681   1341    -81    -31       C  
ATOM    744  C   VAL A  99      46.875 -26.567  -7.227  1.00 28.79           C  
ANISOU  744  C   VAL A  99     4085   3626   3229   1336    -68    -30       C  
ATOM    745  O   VAL A  99      47.928 -26.922  -7.764  1.00 29.19           O  
ANISOU  745  O   VAL A  99     4147   3676   3268   1340    -58    -23       O  
ATOM    746  CB  VAL A  99      45.493 -24.666  -8.047  1.00 25.14           C  
ANISOU  746  CB  VAL A  99     3625   3143   2785   1341    -80    -33       C  
ATOM    747  CG1 VAL A  99      46.788 -23.967  -8.394  1.00 29.27           C  
ANISOU  747  CG1 VAL A  99     4152   3660   3309   1345    -66    -27       C  
ATOM    748  CG2 VAL A  99      44.389 -24.256  -8.992  1.00 18.71           C  
ANISOU  748  CG2 VAL A  99     2823   2317   1970   1346    -92    -33       C  
ATOM    749  N   LEU A 100      46.718 -26.527  -5.905  1.00 29.10           N  
ANISOU  749  N   LEU A 100     4102   3675   3281   1329    -69    -37       N  
ATOM    750  CA  LEU A 100      47.826 -26.866  -5.008  1.00 24.79           C  
ANISOU  750  CA  LEU A 100     3544   3140   2735   1324    -58    -37       C  
ATOM    751  C   LEU A 100      48.160 -28.330  -5.103  1.00 25.87           C  
ANISOU  751  C   LEU A 100     3690   3286   2854   1324    -57    -34       C  
ATOM    752  O   LEU A 100      49.329 -28.684  -5.115  1.00 28.12           O  
ANISOU  752  O   LEU A 100     3978   3575   3131   1324    -45    -29       O  
ATOM    753  CB  LEU A 100      47.515 -26.510  -3.569  1.00 15.96           C  
ANISOU  753  CB  LEU A 100     2400   2029   1633   1315    -61    -46       C  
ATOM    754  CG  LEU A 100      48.507 -26.983  -2.496  1.00 25.32           C  
ANISOU  754  CG  LEU A 100     3572   3228   2820   1309    -51    -48       C  
ATOM    755  CD1 LEU A 100      49.907 -26.413  -2.739  1.00 19.16           C  
ANISOU  755  CD1 LEU A 100     2794   2444   2041   1311    -36    -42       C  
ATOM    756  CD2 LEU A 100      47.989 -26.656  -1.084  1.00 15.78           C  
ANISOU  756  CD2 LEU A 100     2339   2028   1629   1300    -55    -57       C  
ATOM    757  N   ALA A 101      47.140 -29.181  -5.177  1.00 27.09           N  
ANISOU  757  N   ALA A 101     3848   3443   3001   1323    -68    -37       N  
ATOM    758  CA  ALA A 101      47.364 -30.624  -5.323  1.00 28.62           C  
ANISOU  758  CA  ALA A 101     4052   3645   3177   1323    -68    -34       C  
ATOM    759  C   ALA A 101      48.178 -30.955  -6.575  1.00 30.53           C  
ANISOU  759  C   ALA A 101     4317   3881   3402   1331    -60    -25       C  
ATOM    760  O   ALA A 101      49.226 -31.598  -6.482  1.00 28.18           O  
ANISOU  760  O   ALA A 101     4022   3589   3095   1331    -50    -20       O  
ATOM    761  CB  ALA A 101      46.039 -31.398  -5.323  1.00 21.68           C  
ANISOU  761  CB  ALA A 101     3175   2768   2294   1322    -82    -39       C  
ATOM    762  N   GLY A 102      47.691 -30.511  -7.734  1.00 26.24           N  
ANISOU  762  N   GLY A 102     3790   3325   2856   1338    -65    -21       N  
ATOM    763  CA  GLY A 102      48.402 -30.674  -8.986  1.00 22.78           C  
ANISOU  763  CA  GLY A 102     3374   2879   2403   1345    -58    -13       C  
ATOM    764  C   GLY A 102      49.816 -30.141  -8.941  1.00 18.68           C  
ANISOU  764  C   GLY A 102     2853   2360   1886   1346    -43     -7       C  
ATOM    765  O   GLY A 102      50.736 -30.808  -9.385  1.00 24.61           O  
ANISOU  765  O   GLY A 102     3615   3113   2622   1349    -34     -1       O  
ATOM    766  N   ALA A 103      49.998 -28.946  -8.385  1.00 16.64           N  
ANISOU  766  N   ALA A 103     2580   2098   1645   1344    -39    -10       N  
ATOM    767  CA  ALA A 103      51.329 -28.351  -8.328  1.00 16.17           C  
ANISOU  767  CA  ALA A 103     2517   2037   1588   1345    -25     -5       C  
ATOM    768  C   ALA A 103      52.253 -29.184  -7.440  1.00 21.50           C  
ANISOU  768  C   ALA A 103     3184   2727   2260   1340    -16     -5       C  
ATOM    769  O   ALA A 103      53.407 -29.402  -7.778  1.00 29.54           O  
ANISOU  769  O   ALA A 103     4210   3745   3270   1342     -4      1       O  
ATOM    770  CB  ALA A 103      51.262 -26.915  -7.849  1.00 16.21           C  
ANISOU  770  CB  ALA A 103     2508   2037   1615   1343    -23     -9       C  
ATOM    771  N   LEU A 104      51.725 -29.661  -6.316  1.00 19.47           N  
ANISOU  771  N   LEU A 104     2910   2480   2009   1332    -22    -13       N  
ATOM    772  CA  LEU A 104      52.453 -30.531  -5.394  1.00 18.10           C  
ANISOU  772  CA  LEU A 104     2726   2321   1831   1327    -16    -13       C  
ATOM    773  C   LEU A 104      52.909 -31.834  -6.045  1.00 15.82           C  
ANISOU  773  C   LEU A 104     2454   2035   1520   1330    -13     -7       C  
ATOM    774  O   LEU A 104      54.098 -32.120  -6.072  1.00 35.37           O  
ANISOU  774  O   LEU A 104     4935   4516   3990   1331     -1     -2       O  
ATOM    775  CB  LEU A 104      51.600 -30.823  -4.161  1.00 18.73           C  
ANISOU  775  CB  LEU A 104     2787   2411   1921   1319    -25    -23       C  
ATOM    776  CG  LEU A 104      52.259 -30.650  -2.795  1.00 23.21           C  
ANISOU  776  CG  LEU A 104     3331   2987   2499   1310    -18    -27       C  
ATOM    777  CD1 LEU A 104      52.883 -29.302  -2.701  1.00 30.61           C  
ANISOU  777  CD1 LEU A 104     4261   3918   3452   1311    -10    -27       C  
ATOM    778  CD2 LEU A 104      51.222 -30.793  -1.722  1.00 24.04           C  
ANISOU  778  CD2 LEU A 104     3419   3101   2615   1303    -29    -37       C  
ATOM    779  N   VAL A 105      51.972 -32.615  -6.571  1.00 15.82           N  
ANISOU  779  N   VAL A 105     2466   2035   1509   1333    -23     -8       N  
ATOM    780  CA  VAL A 105      52.331 -33.777  -7.392  1.00 26.35           C  
ANISOU  780  CA  VAL A 105     3820   3370   2822   1337    -21     -1       C  
ATOM    781  C   VAL A 105      53.386 -33.493  -8.480  1.00 27.14           C  
ANISOU  781  C   VAL A 105     3938   3462   2913   1345    -10      8       C  
ATOM    782  O   VAL A 105      54.401 -34.203  -8.583  1.00 19.90           O  
ANISOU  782  O   VAL A 105     3027   2551   1983   1346      0     14       O  
ATOM    783  CB  VAL A 105      51.135 -34.372  -8.110  1.00 20.41           C  
ANISOU  783  CB  VAL A 105     3080   2613   2060   1340    -34     -3       C  
ATOM    784  CG1 VAL A 105      51.496 -35.749  -8.635  1.00 20.79           C  
ANISOU  784  CG1 VAL A 105     3145   2667   2088   1343    -32      2       C  
ATOM    785  CG2 VAL A 105      49.987 -34.469  -7.182  1.00 24.14           C  
ANISOU  785  CG2 VAL A 105     3537   3092   2544   1334    -46    -12       C  
ATOM    786  N   ALA A 106      53.148 -32.479  -9.303  1.00 22.52           N  
ANISOU  786  N   ALA A 106     3360   2864   2332   1350    -11     10       N  
ATOM    787  CA  ALA A 106      54.083 -32.237 -10.383  1.00 31.47           C  
ANISOU  787  CA  ALA A 106     4512   3989   3455   1357      0     20       C  
ATOM    788  C   ALA A 106      55.463 -31.983  -9.796  1.00 33.67           C  
ANISOU  788  C   ALA A 106     4782   4274   3739   1354     14     23       C  
ATOM    789  O   ALA A 106      56.458 -32.532 -10.253  1.00 28.73           O  
ANISOU  789  O   ALA A 106     4167   3649   3100   1358     25     30       O  
ATOM    790  CB  ALA A 106      53.636 -31.078 -11.233  1.00 30.05           C  
ANISOU  790  CB  ALA A 106     4340   3795   3283   1362     -3     21       C  
ATOM    791  N   SER A 107      55.502 -31.171  -8.754  1.00 31.82           N  
ANISOU  791  N   SER A 107     4525   4041   3523   1349     15     17       N  
ATOM    792  CA  SER A 107      56.750 -30.816  -8.110  1.00 27.98           C  
ANISOU  792  CA  SER A 107     4028   3560   3044   1345     29     19       C  
ATOM    793  C   SER A 107      57.474 -32.048  -7.567  1.00 39.60           C  
ANISOU  793  C   SER A 107     5497   5044   4504   1342     34     21       C  
ATOM    794  O   SER A 107      58.698 -32.131  -7.608  1.00 37.51           O  
ANISOU  794  O   SER A 107     5235   4782   4235   1343     47     27       O  
ATOM    795  CB  SER A 107      56.466 -29.855  -6.969  1.00 22.02           C  
ANISOU  795  CB  SER A 107     3248   2806   2311   1339     26     11       C  
ATOM    796  OG  SER A 107      57.601 -29.647  -6.170  1.00 24.78           O  
ANISOU  796  OG  SER A 107     3585   3162   2668   1334     38     11       O  
ATOM    797  N   LYS A 108      56.729 -33.012  -7.052  1.00 43.47           N  
ANISOU  797  N   LYS A 108     5983   5543   4989   1338     25     16       N  
ATOM    798  CA  LYS A 108      57.386 -34.188  -6.512  1.00 36.23           C  
ANISOU  798  CA  LYS A 108     5065   4640   4062   1334     30     17       C  
ATOM    799  C   LYS A 108      57.818 -35.166  -7.602  1.00 36.33           C  
ANISOU  799  C   LYS A 108     5101   4652   4053   1341     34     26       C  
ATOM    800  O   LYS A 108      58.770 -35.923  -7.407  1.00 41.74           O  
ANISOU  800  O   LYS A 108     5787   5344   4727   1340     42     30       O  
ATOM    801  CB  LYS A 108      56.526 -34.855  -5.446  1.00 32.08           C  
ANISOU  801  CB  LYS A 108     4524   4125   3541   1327     20      9       C  
ATOM    802  CG  LYS A 108      56.643 -34.150  -4.106  1.00 34.98           C  
ANISOU  802  CG  LYS A 108     4866   4499   3928   1319     21      2       C  
ATOM    803  CD  LYS A 108      55.567 -34.621  -3.117  1.00 32.46           C  
ANISOU  803  CD  LYS A 108     4531   4188   3614   1312     10     -7       C  
ATOM    804  CE  LYS A 108      55.869 -34.129  -1.704  1.00 24.12           C  
ANISOU  804  CE  LYS A 108     3450   3140   2576   1303     13    -14       C  
ATOM    805  NZ  LYS A 108      55.013 -34.884  -0.785  1.00 25.57           N1+
ANISOU  805  NZ  LYS A 108     3621   3333   2760   1297      3    -21       N1+
ATOM    806  N   LEU A 109      57.137 -35.132  -8.748  1.00 29.33           N  
ANISOU  806  N   LEU A 109     4232   3755   3158   1348     27     28       N  
ATOM    807  CA  LEU A 109      57.533 -35.923  -9.919  1.00 20.85           C  
ANISOU  807  CA  LEU A 109     3181   2677   2062   1355     31     36       C  
ATOM    808  C   LEU A 109      58.601 -35.209 -10.753  1.00 25.31           C  
ANISOU  808  C   LEU A 109     3759   3234   2625   1361     44     44       C  
ATOM    809  O   LEU A 109      58.969 -35.656 -11.833  1.00 29.52           O  
ANISOU  809  O   LEU A 109     4312   3762   3142   1367     48     52       O  
ATOM    810  CB  LEU A 109      56.327 -36.236 -10.792  1.00 18.52           C  
ANISOU  810  CB  LEU A 109     2901   2375   1759   1359     19     34       C  
ATOM    811  CG  LEU A 109      55.340 -37.193 -10.164  1.00 19.41           C  
ANISOU  811  CG  LEU A 109     3007   2497   1870   1354      7     27       C  
ATOM    812  CD1 LEU A 109      54.330 -37.659 -11.186  1.00 25.84           C  
ANISOU  812  CD1 LEU A 109     3839   3304   2674   1359     -4     27       C  
ATOM    813  CD2 LEU A 109      56.127 -38.330  -9.644  1.00 17.79           C  
ANISOU  813  CD2 LEU A 109     2800   2305   1654   1351     14     29       C  
ATOM    814  N   LYS A 110      59.075 -34.086 -10.235  1.00 29.21           N  
ANISOU  814  N   LYS A 110     4239   3725   3136   1358     50     43       N  
ATOM    815  CA  LYS A 110      60.155 -33.312 -10.829  1.00 31.97           C  
ANISOU  815  CA  LYS A 110     4595   4066   3486   1363     63     51       C  
ATOM    816  C   LYS A 110      59.739 -32.642 -12.131  1.00 31.98           C  
ANISOU  816  C   LYS A 110     4614   4053   3484   1371     61     55       C  
ATOM    817  O   LYS A 110      60.583 -32.265 -12.923  1.00 37.29           O  
ANISOU  817  O   LYS A 110     5298   4718   4151   1376     71     63       O  
ATOM    818  CB  LYS A 110      61.431 -34.153 -10.971  1.00 44.05           C  
ANISOU  818  CB  LYS A 110     6133   5603   5002   1364     76     59       C  
ATOM    819  CG  LYS A 110      61.769 -34.951  -9.702  1.00 57.59           C  
ANISOU  819  CG  LYS A 110     7831   7333   6718   1356     77     55       C  
ATOM    820  CD  LYS A 110      63.163 -35.577  -9.705  1.00 67.39           C  
ANISOU  820  CD  LYS A 110     9077   8581   7948   1356     91     62       C  
ATOM    821  CE  LYS A 110      64.136 -34.743  -8.875  1.00 73.97           C  
ANISOU  821  CE  LYS A 110     9892   9416   8798   1352    101     62       C  
ATOM    822  NZ  LYS A 110      65.299 -35.536  -8.372  1.00 77.91           N1+
ANISOU  822  NZ  LYS A 110    10387   9925   9288   1348    111     66       N1+
ATOM    823  N   ILE A 111      58.429 -32.463 -12.310  1.00 31.67           N  
ANISOU  823  N   ILE A 111     4575   4009   3449   1371     47     49       N  
ATOM    824  CA  ILE A 111      57.844 -31.746 -13.451  1.00 26.49           C  
ANISOU  824  CA  ILE A 111     3934   3338   2792   1378     43     52       C  
ATOM    825  C   ILE A 111      57.760 -30.233 -13.181  1.00 26.23           C  
ANISOU  825  C   ILE A 111     3888   3297   2779   1377     44     49       C  
ATOM    826  O   ILE A 111      57.293 -29.809 -12.134  1.00 38.65           O  
ANISOU  826  O   ILE A 111     5442   4875   4369   1370     38     41       O  
ATOM    827  CB  ILE A 111      56.418 -32.304 -13.772  1.00 18.71           C  
ANISOU  827  CB  ILE A 111     2956   2353   1802   1378     27     47       C  
ATOM    828  CG1 ILE A 111      56.412 -33.836 -13.781  1.00 17.17           C  
ANISOU  828  CG1 ILE A 111     2768   2167   1588   1378     25     47       C  
ATOM    829  CG2 ILE A 111      55.875 -31.785 -15.092  1.00 16.46           C  
ANISOU  829  CG2 ILE A 111     2690   2053   1512   1386     22     50       C  
ATOM    830  CD1 ILE A 111      55.021 -34.430 -13.809  1.00 18.30           C  
ANISOU  830  CD1 ILE A 111     2913   2311   1729   1376      9     41       C  
ATOM    831  N   ASP A 112      58.230 -29.429 -14.123  1.00 21.27           N  
ANISOU  831  N   ASP A 112     3273   2658   2152   1383     51     56       N  
ATOM    832  CA  ASP A 112      58.079 -27.984 -14.072  1.00 20.62           C  
ANISOU  832  CA  ASP A 112     3182   2566   2087   1383     51     54       C  
ATOM    833  C   ASP A 112      56.608 -27.591 -14.021  1.00 26.44           C  
ANISOU  833  C   ASP A 112     3915   3298   2833   1382     35     47       C  
ATOM    834  O   ASP A 112      55.777 -28.146 -14.742  1.00 31.71           O  
ANISOU  834  O   ASP A 112     4597   3963   3489   1385     26     47       O  
ATOM    835  CB  ASP A 112      58.705 -27.358 -15.314  1.00 29.42           C  
ANISOU  835  CB  ASP A 112     4315   3667   3196   1391     60     63       C  
ATOM    836  CG  ASP A 112      60.205 -27.158 -15.187  1.00 37.87           C  
ANISOU  836  CG  ASP A 112     5384   4740   4267   1392     77     70       C  
ATOM    837  OD1 ASP A 112      60.802 -27.557 -14.152  1.00 34.94           O  
ANISOU  837  OD1 ASP A 112     4998   4380   3900   1386     82     67       O  
ATOM    838  OD2 ASP A 112      60.790 -26.590 -16.138  1.00 41.06           O1-
ANISOU  838  OD2 ASP A 112     5801   5134   4668   1398     85     77       O1-
ATOM    839  N   VAL A 113      56.299 -26.617 -13.169  1.00 27.36           N  
ANISOU  839  N   VAL A 113     4012   3414   2970   1377     33     40       N  
ATOM    840  CA  VAL A 113      54.938 -26.121 -12.982  1.00 22.90           C  
ANISOU  840  CA  VAL A 113     3439   2844   2415   1376     18     33       C  
ATOM    841  C   VAL A 113      54.834 -24.659 -13.410  1.00 27.18           C  
ANISOU  841  C   VAL A 113     3982   3374   2972   1379     20     33       C  
ATOM    842  O   VAL A 113      55.723 -23.851 -13.127  1.00 33.74           O  
ANISOU  842  O   VAL A 113     4804   4202   3813   1378     30     35       O  
ATOM    843  CB  VAL A 113      54.512 -26.256 -11.500  1.00 23.06           C  
ANISOU  843  CB  VAL A 113     3436   2877   2450   1367     13     23       C  
ATOM    844  CG1 VAL A 113      53.092 -25.690 -11.252  1.00 16.87           C  
ANISOU  844  CG1 VAL A 113     2644   2089   1678   1364     -2     15       C  
ATOM    845  CG2 VAL A 113      54.600 -27.692 -11.083  1.00 16.39           C  
ANISOU  845  CG2 VAL A 113     2591   2045   1591   1363     12     22       C  
ATOM    846  N   ALA A 114      53.749 -24.320 -14.095  1.00 22.87           N  
ANISOU  846  N   ALA A 114     3445   2819   2427   1382      9     32       N  
ATOM    847  CA  ALA A 114      53.474 -22.926 -14.442  1.00 24.97           C  
ANISOU  847  CA  ALA A 114     3709   3072   2706   1384      8     32       C  
ATOM    848  C   ALA A 114      52.201 -22.388 -13.773  1.00 22.02           C  
ANISOU  848  C   ALA A 114     3321   2698   2348   1380     -6     22       C  
ATOM    849  O   ALA A 114      51.135 -23.007 -13.850  1.00 21.14           O  
ANISOU  849  O   ALA A 114     3213   2589   2232   1379    -18     19       O  
ATOM    850  CB  ALA A 114      53.382 -22.774 -15.945  1.00 34.15           C  
ANISOU  850  CB  ALA A 114     4896   4222   3857   1393      8     39       C  
ATOM    851  N   HIS A 115      52.305 -21.238 -13.112  1.00 22.26           N  
ANISOU  851  N   HIS A 115     3334   2726   2398   1377     -3     18       N  
ATOM    852  CA  HIS A 115      51.125 -20.651 -12.468  1.00 16.88           C  
ANISOU  852  CA  HIS A 115     2638   2044   1732   1373    -16      9       C  
ATOM    853  C   HIS A 115      50.626 -19.466 -13.262  1.00 18.25           C  
ANISOU  853  C   HIS A 115     2819   2203   1914   1378    -19     11       C  
ATOM    854  O   HIS A 115      51.341 -18.474 -13.423  1.00 20.42           O  
ANISOU  854  O   HIS A 115     3092   2471   2198   1379    -10     14       O  
ATOM    855  CB  HIS A 115      51.406 -20.220 -11.024  1.00 26.24           C  
ANISOU  855  CB  HIS A 115     3797   3237   2935   1365    -12      2       C  
ATOM    856  CG  HIS A 115      50.174 -20.121 -10.173  1.00 27.39           C  
ANISOU  856  CG  HIS A 115     3927   3387   3092   1359    -25     -8       C  
ATOM    857  CD2 HIS A 115      48.958 -20.708 -10.293  1.00 27.95           C  
ANISOU  857  CD2 HIS A 115     4002   3460   3158   1359    -39    -11       C  
ATOM    858  ND1 HIS A 115      50.121 -19.359  -9.027  1.00 23.11           N  
ANISOU  858  ND1 HIS A 115     3362   2850   2570   1353    -25    -15       N  
ATOM    859  CE1 HIS A 115      48.926 -19.486  -8.473  1.00 21.03           C  
ANISOU  859  CE1 HIS A 115     3089   2589   2312   1349    -38    -23       C  
ATOM    860  NE2 HIS A 115      48.202 -20.297  -9.222  1.00 23.28           N  
ANISOU  860  NE2 HIS A 115     3390   2873   2582   1352    -47    -20       N  
ATOM    861  N   VAL A 116      49.400 -19.588 -13.759  1.00 19.12           N  
ANISOU  861  N   VAL A 116     2936   2308   2020   1379    -32      9       N  
ATOM    862  CA  VAL A 116      48.762 -18.565 -14.571  1.00 22.67           C  
ANISOU  862  CA  VAL A 116     3394   2744   2477   1384    -38     10       C  
ATOM    863  C   VAL A 116      48.048 -17.578 -13.669  1.00 26.63           C  
ANISOU  863  C   VAL A 116     3875   3245   2999   1379    -44      1       C  
ATOM    864  O   VAL A 116      47.252 -17.981 -12.823  1.00 38.69           O  
ANISOU  864  O   VAL A 116     5390   4781   4531   1373    -53     -6       O  
ATOM    865  CB  VAL A 116      47.752 -19.213 -15.560  1.00 29.41           C  
ANISOU  865  CB  VAL A 116     4266   3593   3315   1388    -50     11       C  
ATOM    866  CG1 VAL A 116      46.998 -18.164 -16.376  1.00 17.32           C  
ANISOU  866  CG1 VAL A 116     2743   2048   1791   1393    -56     12       C  
ATOM    867  CG2 VAL A 116      48.485 -20.169 -16.457  1.00 17.21           C  
ANISOU  867  CG2 VAL A 116     2742   2049   1750   1393    -43     20       C  
ATOM    868  N   GLU A 117      48.349 -16.293 -13.859  1.00 23.29           N  
ANISOU  868  N   GLU A 117     3448   2811   2589   1381    -39      3       N  
ATOM    869  CA  GLU A 117      47.845 -15.199 -13.020  1.00 22.92           C  
ANISOU  869  CA  GLU A 117     3382   2763   2564   1377    -43     -5       C  
ATOM    870  C   GLU A 117      48.474 -15.297 -11.635  1.00 20.71           C  
ANISOU  870  C   GLU A 117     3079   2495   2294   1369    -36    -11       C  
ATOM    871  O   GLU A 117      47.769 -15.379 -10.638  1.00 19.42           O  
ANISOU  871  O   GLU A 117     2900   2339   2140   1363    -44    -19       O  
ATOM    872  CB  GLU A 117      46.307 -15.179 -12.944  1.00 17.23           C  
ANISOU  872  CB  GLU A 117     2659   2042   1847   1375    -60    -11       C  
ATOM    873  CG  GLU A 117      45.721 -13.891 -12.384  1.00 35.85           C  
ANISOU  873  CG  GLU A 117     5001   4395   4227   1372    -64    -18       C  
ATOM    874  CD  GLU A 117      44.240 -13.990 -12.031  1.00 38.29           C  
ANISOU  874  CD  GLU A 117     5304   4706   4540   1369    -80    -25       C  
ATOM    875  OE1 GLU A 117      43.777 -15.085 -11.679  1.00 45.35           O  
ANISOU  875  OE1 GLU A 117     6197   5609   5426   1366    -86    -28       O  
ATOM    876  OE2 GLU A 117      43.528 -12.969 -12.103  1.00 42.95           O1-
ANISOU  876  OE2 GLU A 117     5889   5287   5142   1370    -86    -28       O1-
ATOM    877  N   ALA A 118      49.809 -15.304 -11.595  1.00 20.90           N  
ANISOU  877  N   ALA A 118     3104   2521   2316   1370    -22     -6       N  
ATOM    878  CA  ALA A 118      50.573 -15.440 -10.352  1.00 19.02           C  
ANISOU  878  CA  ALA A 118     2846   2294   2086   1363    -14    -10       C  
ATOM    879  C   ALA A 118      50.905 -14.100  -9.694  1.00 31.83           C  
ANISOU  879  C   ALA A 118     4452   3913   3731   1360     -9    -15       C  
ATOM    880  O   ALA A 118      51.065 -13.074 -10.365  1.00 37.64           O  
ANISOU  880  O   ALA A 118     5192   4635   4472   1364     -6    -11       O  
ATOM    881  CB  ALA A 118      51.854 -16.214 -10.609  1.00 21.04           C  
ANISOU  881  CB  ALA A 118     3112   2555   2329   1365     -2     -3       C  
ATOM    882  N   GLY A 119      51.014 -14.103  -8.371  1.00 36.49           N  
ANISOU  882  N   GLY A 119     5019   4513   4333   1352     -8    -22       N  
ATOM    883  CA  GLY A 119      51.448 -12.909  -7.677  1.00 39.13           C  
ANISOU  883  CA  GLY A 119     5336   4845   4688   1349     -2    -27       C  
ATOM    884  C   GLY A 119      50.398 -12.107  -6.933  1.00 43.21           C  
ANISOU  884  C   GLY A 119     5836   5360   5222   1344    -12    -36       C  
ATOM    885  O   GLY A 119      50.764 -11.269  -6.123  1.00 50.22           O  
ANISOU  885  O   GLY A 119     6706   6248   6127   1340     -7    -41       O  
ATOM    886  N   LEU A 120      49.114 -12.334  -7.199  1.00 43.88           N  
ANISOU  886  N   LEU A 120     5926   5444   5303   1345    -26    -38       N  
ATOM    887  CA  LEU A 120      48.053 -11.726  -6.379  1.00 49.47           C  
ANISOU  887  CA  LEU A 120     6616   6152   6026   1340    -36    -48       C  
ATOM    888  C   LEU A 120      48.140 -12.120  -4.894  1.00 55.60           C  
ANISOU  888  C   LEU A 120     7370   6943   6811   1331    -35    -56       C  
ATOM    889  O   LEU A 120      48.418 -13.277  -4.557  1.00 53.61           O  
ANISOU  889  O   LEU A 120     7119   6703   6547   1328    -34    -55       O  
ATOM    890  CB  LEU A 120      46.671 -12.116  -6.890  1.00 39.50           C  
ANISOU  890  CB  LEU A 120     5364   4888   4757   1343    -51    -49       C  
ATOM    891  CG  LEU A 120      46.525 -12.031  -8.387  1.00 39.11           C  
ANISOU  891  CG  LEU A 120     5339   4827   4696   1351    -52    -40       C  
ATOM    892  CD1 LEU A 120      45.302 -12.846  -8.751  1.00 45.21           C  
ANISOU  892  CD1 LEU A 120     6120   5600   5456   1352    -66    -41       C  
ATOM    893  CD2 LEU A 120      46.402 -10.583  -8.807  1.00 17.20           C  
ANISOU  893  CD2 LEU A 120     2563   2038   1935   1354    -51    -40       C  
ATOM    894  N   ARG A 121      47.889 -11.150  -4.016  1.00 62.61           N  
ANISOU  894  N   ARG A 121     8239   7831   7718   1326    -36    -64       N  
ATOM    895  CA  ARG A 121      47.943 -11.360  -2.566  1.00 68.97           C  
ANISOU  895  CA  ARG A 121     9022   8650   8534   1317    -35    -72       C  
ATOM    896  C   ARG A 121      46.845 -10.559  -1.877  1.00 79.73           C  
ANISOU  896  C   ARG A 121    10369  10011   9913   1313    -45    -81       C  
ATOM    897  O   ARG A 121      46.599  -9.400  -2.224  1.00 83.20           O  
ANISOU  897  O   ARG A 121    10808  10439  10363   1316    -46    -81       O  
ATOM    898  CB  ARG A 121      49.302 -10.923  -1.989  1.00 62.45           C  
ANISOU  898  CB  ARG A 121     8185   7827   7717   1314    -21    -72       C  
ATOM    899  CG  ARG A 121      50.531 -11.640  -2.551  1.00 58.71           C  
ANISOU  899  CG  ARG A 121     7725   7355   7229   1317    -10    -64       C  
ATOM    900  CD  ARG A 121      50.616 -13.082  -2.060  1.00 55.43           C  
ANISOU  900  CD  ARG A 121     7308   6953   6799   1313    -11    -64       C  
ATOM    901  NE  ARG A 121      51.836 -13.756  -2.495  1.00 51.54           N  
ANISOU  901  NE  ARG A 121     6826   6462   6293   1316      0    -57       N  
ATOM    902  CZ  ARG A 121      51.881 -14.657  -3.468  1.00 45.52           C  
ANISOU  902  CZ  ARG A 121     6084   5699   5511   1322     -1    -49       C  
ATOM    903  NH1 ARG A 121      50.762 -14.985  -4.096  1.00 45.23           N1+
ANISOU  903  NH1 ARG A 121     6060   5659   5466   1325    -12    -48       N1+
ATOM    904  NH2 ARG A 121      53.037 -15.228  -3.803  1.00 38.81           N  
ANISOU  904  NH2 ARG A 121     5244   4852   4651   1324     10    -42       N  
ATOM    905  N   SER A 122      46.184 -11.173  -0.902  1.00 84.96           N  
ANISOU  905  N   SER A 122    11019  10685  10576   1307    -52    -87       N  
ATOM    906  CA  SER A 122      45.277 -10.431  -0.032  1.00 89.26           C  
ANISOU  906  CA  SER A 122    11545  11231  11137   1302    -60    -96       C  
ATOM    907  C   SER A 122      45.988 -10.102   1.281  1.00 95.37           C  
ANISOU  907  C   SER A 122    12298  12014  11926   1294    -52   -103       C  
ATOM    908  O   SER A 122      45.467  -9.355   2.111  1.00100.71           O  
ANISOU  908  O   SER A 122    12957  12691  12618   1289    -55   -110       O  
ATOM    909  CB  SER A 122      43.982 -11.212   0.232  1.00 87.67           C  
ANISOU  909  CB  SER A 122    11344  11037  10930   1299    -73   -100       C  
ATOM    910  OG  SER A 122      44.201 -12.347   1.054  1.00 85.19           O  
ANISOU  910  OG  SER A 122    11023  10737  10609   1294    -72   -102       O  
ATOM    911  N   PHE A 123      47.186 -10.667   1.445  1.00 95.72           N  
ANISOU  911  N   PHE A 123    12342  12064  11964   1292    -41   -100       N  
ATOM    912  CA  PHE A 123      47.987 -10.558   2.673  1.00 94.28           C  
ANISOU  912  CA  PHE A 123    12140  11891  11792   1284    -32   -105       C  
ATOM    913  C   PHE A 123      47.209 -10.939   3.952  1.00 97.51           C  
ANISOU  913  C   PHE A 123    12531  12312  12206   1276    -40   -114       C  
ATOM    914  O   PHE A 123      47.592 -10.571   5.068  1.00 94.51           O  
ANISOU  914  O   PHE A 123    12132  11939  11840   1269    -35   -120       O  
ATOM    915  CB  PHE A 123      48.662  -9.181   2.790  1.00 87.74           C  
ANISOU  915  CB  PHE A 123    11303  11054  10981   1284    -24   -107       C  
ATOM    916  CG  PHE A 123      49.671  -8.899   1.701  1.00 80.65           C  
ANISOU  916  CG  PHE A 123    10420  10145  10077   1291    -14    -98       C  
ATOM    917  CD1 PHE A 123      50.900  -9.542   1.691  1.00 76.52           C  
ANISOU  917  CD1 PHE A 123     9901   9628   9546   1291     -3    -94       C  
ATOM    918  CD2 PHE A 123      49.390  -7.975   0.692  1.00 79.25           C  
ANISOU  918  CD2 PHE A 123    10254   9953   9903   1298    -15    -94       C  
ATOM    919  CE1 PHE A 123      51.827  -9.281   0.689  1.00 78.75           C  
ANISOU  919  CE1 PHE A 123    10197   9901   9823   1298      7    -85       C  
ATOM    920  CE2 PHE A 123      50.314  -7.703  -0.317  1.00 77.00           C  
ANISOU  920  CE2 PHE A 123     9984   9659   9614   1305     -6    -86       C  
ATOM    921  CZ  PHE A 123      51.532  -8.357  -0.319  1.00 78.30           C  
ANISOU  921  CZ  PHE A 123    10152   9829   9770   1305      5    -81       C  
ATOM    922  N   ASP A 124      46.121 -11.687   3.754  1.00100.39           N  
ANISOU  922  N   ASP A 124    12903  12681  12562   1277    -51   -114       N  
ATOM    923  CA  ASP A 124      45.312 -12.268   4.824  1.00 97.11           C  
ANISOU  923  CA  ASP A 124    12473  12277  12147   1270    -59   -121       C  
ATOM    924  C   ASP A 124      45.544 -13.779   4.821  1.00 91.77           C  
ANISOU  924  C   ASP A 124    11805  11611  11453   1269    -59   -118       C  
ATOM    925  O   ASP A 124      44.770 -14.539   4.231  1.00 84.70           O  
ANISOU  925  O   ASP A 124    10922  10715  10545   1272    -67   -115       O  
ATOM    926  CB  ASP A 124      43.825 -11.950   4.600  1.00 96.95           C  
ANISOU  926  CB  ASP A 124    12455  12251  12130   1271    -73   -124       C  
ATOM    927  CG  ASP A 124      42.912 -12.586   5.645  1.00 97.47           C  
ANISOU  927  CG  ASP A 124    12508  12329  12197   1264    -81   -131       C  
ATOM    928  OD1 ASP A 124      43.403 -12.952   6.735  1.00100.48           O  
ANISOU  928  OD1 ASP A 124    12874  12722  12582   1257    -76   -135       O  
ATOM    929  OD2 ASP A 124      41.696 -12.710   5.377  1.00 93.56           O1-
ANISOU  929  OD2 ASP A 124    12016  11832  11699   1266    -93   -132       O1-
ATOM    930  N   ARG A 125      46.619 -14.206   5.480  1.00 92.79           N  
ANISOU  930  N   ARG A 125    11926  11749  11581   1264    -49   -118       N  
ATOM    931  CA  ARG A 125      47.021 -15.608   5.491  1.00 97.41           C  
ANISOU  931  CA  ARG A 125    12518  12343  12149   1263    -47   -114       C  
ATOM    932  C   ARG A 125      46.123 -16.438   6.412  1.00104.21           C  
ANISOU  932  C   ARG A 125    13369  13217  13009   1257    -56   -120       C  
ATOM    933  O   ARG A 125      46.603 -17.298   7.154  1.00104.26           O  
ANISOU  933  O   ARG A 125    13369  13235  13010   1252    -52   -121       O  
ATOM    934  CB  ARG A 125      48.497 -15.737   5.899  1.00 96.94           C  
ANISOU  934  CB  ARG A 125    12454  12290  12091   1260    -33   -113       C  
ATOM    935  CG  ARG A 125      49.211 -16.983   5.357  1.00 94.15           C  
ANISOU  935  CG  ARG A 125    12114  11940  11717   1263    -28   -105       C  
ATOM    936  CD  ARG A 125      50.645 -17.089   5.884  1.00 89.15           C  
ANISOU  936  CD  ARG A 125    11474  11313  11086   1259    -15   -104       C  
ATOM    937  NE  ARG A 125      50.719 -16.823   7.319  1.00 85.38           N  
ANISOU  937  NE  ARG A 125    10973  10845  10623   1250    -13   -113       N  
ATOM    938  CZ  ARG A 125      50.451 -17.719   8.264  1.00 81.24           C  
ANISOU  938  CZ  ARG A 125    10440  10334  10095   1243    -16   -117       C  
ATOM    939  NH1 ARG A 125      50.092 -18.953   7.931  1.00 81.95           N1+
ANISOU  939  NH1 ARG A 125    10540  10428  10167   1245    -21   -113       N1+
ATOM    940  NH2 ARG A 125      50.538 -17.380   9.545  1.00 78.38           N  
ANISOU  940  NH2 ARG A 125    10056   9979   9747   1234    -14   -125       N  
ATOM    941  N   ASN A 126      44.819 -16.162   6.361  1.00109.54           N  
ANISOU  941  N   ASN A 126    14044  13889  13688   1258    -68   -124       N  
ATOM    942  CA  ASN A 126      43.812 -16.939   7.086  1.00110.00           C  
ANISOU  942  CA  ASN A 126    14095  13957  13744   1253    -77   -129       C  
ATOM    943  C   ASN A 126      42.918 -17.746   6.147  1.00106.37           C  
ANISOU  943  C   ASN A 126    13653  13495  13269   1258    -87   -124       C  
ATOM    944  O   ASN A 126      42.733 -18.950   6.346  1.00106.22           O  
ANISOU  944  O   ASN A 126    13635  13484  13238   1256    -90   -124       O  
ATOM    945  CB  ASN A 126      42.961 -16.046   7.997  1.00111.09           C  
ANISOU  945  CB  ASN A 126    14213  14095  13899   1247    -83   -137       C  
ATOM    946  CG  ASN A 126      43.491 -15.990   9.419  1.00113.56           C  
ANISOU  946  CG  ASN A 126    14506  14420  14223   1238    -77   -143       C  
ATOM    947  ND2 ASN A 126      43.019 -15.014  10.187  1.00116.17           N  
ANISOU  947  ND2 ASN A 126    14820  14749  14570   1234    -79   -150       N  
ATOM    948  OD1 ASN A 126      44.309 -16.818   9.826  1.00112.08           O  
ANISOU  948  OD1 ASN A 126    14316  14241  14028   1235    -70   -142       O  
HETATM  949  N   MSE A 127      42.358 -17.086   5.132  1.00 99.80           N  
ANISOU  949  N   MSE A 127    12832  12649  12437   1265    -93   -122       N  
HETATM  950  CA  MSE A 127      41.631 -17.804   4.092  1.00 89.05           C  
ANISOU  950  CA  MSE A 127    11489  11283  11061   1271   -102   -117       C  
HETATM  951  C   MSE A 127      42.608 -18.777   3.444  1.00 83.40           C  
ANISOU  951  C   MSE A 127    10789  10570  10328   1275    -94   -109       C  
HETATM  952  O   MSE A 127      43.738 -18.404   3.115  1.00 81.03           O  
ANISOU  952  O   MSE A 127    10493  10266  10028   1277    -83   -105       O  
HETATM  953  CB  MSE A 127      41.001 -16.849   3.066  1.00 84.52           C  
ANISOU  953  CB  MSE A 127    10927  10696  10492   1278   -107   -115       C  
HETATM  954  CG  MSE A 127      41.978 -15.937   2.360  1.00 84.20           C  
ANISOU  954  CG  MSE A 127    10893  10644  10454   1283    -97   -110       C  
HETATM  955  CE  MSE A 127      40.998 -13.134   2.202  1.00 41.03           C  
ANISOU  955  CE  MSE A 127     5414   5156   5019   1286   -103   -116       C  
HETATM  956 SE   MSE A 127      41.119 -14.729   1.091  1.00214.73          SE  
ANISOU  956 SE   MSE A 127    27439  27157  26992   1291   -105   -107      SE  
ATOM    957  N   PRO A 128      42.184 -20.042   3.286  1.00 79.45           N  
ANISOU  957  N   PRO A 128    10297  10077   9814   1275   -100   -108       N  
ATOM    958  CA  PRO A 128      43.049 -21.139   2.828  1.00 71.34           C  
ANISOU  958  CA  PRO A 128     9283   9054   8769   1277    -93   -101       C  
ATOM    959  C   PRO A 128      43.563 -20.884   1.416  1.00 56.69           C  
ANISOU  959  C   PRO A 128     7449   7187   6905   1286    -89    -93       C  
ATOM    960  O   PRO A 128      44.613 -21.397   1.015  1.00 57.68           O  
ANISOU  960  O   PRO A 128     7584   7313   7019   1289    -80    -87       O  
ATOM    961  CB  PRO A 128      42.109 -22.344   2.836  1.00 73.78           C  
ANISOU  961  CB  PRO A 128     9597   9370   9067   1276   -104   -102       C  
ATOM    962  CG  PRO A 128      40.759 -21.758   2.614  1.00 76.10           C  
ANISOU  962  CG  PRO A 128     9890   9656   9368   1277   -116   -106       C  
ATOM    963  CD  PRO A 128      40.769 -20.445   3.348  1.00 76.72           C  
ANISOU  963  CD  PRO A 128     9951   9732   9467   1274   -114   -111       C  
ATOM    964  N   GLU A 129      42.813 -20.066   0.687  1.00 44.62           N  
ANISOU  964  N   GLU A 129     5927   5646   5381   1291    -96    -92       N  
ATOM    965  CA  GLU A 129      43.140 -19.695  -0.673  1.00 44.26           C  
ANISOU  965  CA  GLU A 129     5902   5588   5329   1300    -94    -85       C  
ATOM    966  C   GLU A 129      44.396 -18.831  -0.798  1.00 40.10           C  
ANISOU  966  C   GLU A 129     5373   5055   4807   1301    -80    -81       C  
ATOM    967  O   GLU A 129      45.180 -19.027  -1.722  1.00 45.06           O  
ANISOU  967  O   GLU A 129     6017   5678   5424   1307    -73    -74       O  
ATOM    968  CB  GLU A 129      41.927 -19.050  -1.344  1.00 52.79           C  
ANISOU  968  CB  GLU A 129     6988   6657   6413   1303   -105    -86       C  
ATOM    969  CG  GLU A 129      40.828 -20.051  -1.723  1.00 56.80           C  
ANISOU  969  CG  GLU A 129     7506   7167   6909   1305   -118    -86       C  
ATOM    970  CD  GLU A 129      39.484 -19.391  -1.888  1.00 64.27           C  
ANISOU  970  CD  GLU A 129     8450   8105   7863   1305   -130    -90       C  
ATOM    971  OE1 GLU A 129      38.936 -19.395  -3.017  1.00 70.97           O  
ANISOU  971  OE1 GLU A 129     9316   8944   8705   1311   -136    -86       O  
ATOM    972  OE2 GLU A 129      38.982 -18.859  -0.875  1.00 63.70           O1-
ANISOU  972  OE2 GLU A 129     8359   8038   7807   1299   -133    -97       O1-
ATOM    973  N   GLU A 130      44.608 -17.893   0.121  1.00 32.89           N  
ANISOU  973  N   GLU A 130     4441   4143   3912   1296    -76    -87       N  
ATOM    974  CA  GLU A 130      45.870 -17.142   0.131  1.00 39.62           C  
ANISOU  974  CA  GLU A 130     5290   4992   4772   1297    -63    -85       C  
ATOM    975  C   GLU A 130      47.090 -18.062   0.282  1.00 40.84           C  
ANISOU  975  C   GLU A 130     5447   5155   4914   1296    -52    -80       C  
ATOM    976  O   GLU A 130      48.109 -17.895  -0.395  1.00 47.50           O  
ANISOU  976  O   GLU A 130     6302   5993   5753   1300    -42    -74       O  
ATOM    977  CB  GLU A 130      45.885 -16.101   1.247  1.00 46.58           C  
ANISOU  977  CB  GLU A 130     6149   5875   5674   1290    -61    -93       C  
ATOM    978  CG  GLU A 130      47.218 -15.366   1.397  1.00 50.03           C  
ANISOU  978  CG  GLU A 130     6580   6310   6120   1290    -47    -91       C  
ATOM    979  CD  GLU A 130      47.534 -14.430   0.227  1.00 58.96           C  
ANISOU  979  CD  GLU A 130     7725   7425   7251   1298    -43    -85       C  
ATOM    980  OE1 GLU A 130      46.651 -14.162  -0.615  1.00 57.40           O  
ANISOU  980  OE1 GLU A 130     7540   7219   7052   1303    -52    -83       O  
ATOM    981  OE2 GLU A 130      48.678 -13.945   0.157  1.00 66.98           O1-
ANISOU  981  OE2 GLU A 130     8739   8437   8272   1299    -31    -82       O1-
ATOM    982  N   ILE A 131      46.977 -19.026   1.185  1.00 31.49           N  
ANISOU  982  N   ILE A 131     4254   3984   3727   1289    -54    -84       N  
ATOM    983  CA  ILE A 131      48.013 -20.013   1.413  1.00 20.75           C  
ANISOU  983  CA  ILE A 131     2896   2634   2356   1288    -45    -81       C  
ATOM    984  C   ILE A 131      48.255 -20.762   0.123  1.00 33.16           C  
ANISOU  984  C   ILE A 131     4492   4200   3907   1295    -45    -71       C  
ATOM    985  O   ILE A 131      49.389 -20.828  -0.343  1.00 36.50           O  
ANISOU  985  O   ILE A 131     4923   4622   4324   1299    -34    -65       O  
ATOM    986  CB  ILE A 131      47.555 -20.995   2.488  1.00 27.65           C  
ANISOU  986  CB  ILE A 131     3757   3522   3227   1280    -51    -86       C  
ATOM    987  CG1 ILE A 131      47.002 -20.223   3.684  1.00 41.34           C  
ANISOU  987  CG1 ILE A 131     5468   5259   4980   1273    -54    -96       C  
ATOM    988  CG2 ILE A 131      48.670 -21.928   2.912  1.00 26.52           C  
ANISOU  988  CG2 ILE A 131     3613   3390   3075   1277    -41    -84       C  
ATOM    989  CD1 ILE A 131      46.165 -21.083   4.603  1.00 51.37           C  
ANISOU  989  CD1 ILE A 131     6728   6541   6249   1266    -63   -102       C  
ATOM    990  N   ASN A 132      47.180 -21.321  -0.447  1.00 36.79           N  
ANISOU  990  N   ASN A 132     4962   4658   4357   1299    -56    -71       N  
ATOM    991  CA  ASN A 132      47.221 -21.987  -1.755  1.00 27.43           C  
ANISOU  991  CA  ASN A 132     3801   3467   3154   1306    -57    -63       C  
ATOM    992  C   ASN A 132      48.020 -21.210  -2.795  1.00 26.20           C  
ANISOU  992  C   ASN A 132     3659   3299   2996   1313    -48    -55       C  
ATOM    993  O   ASN A 132      48.930 -21.734  -3.432  1.00 19.87           O  
ANISOU  993  O   ASN A 132     2870   2496   2181   1317    -40    -48       O  
ATOM    994  CB  ASN A 132      45.809 -22.161  -2.277  1.00 19.28           C  
ANISOU  994  CB  ASN A 132     2777   2430   2118   1309    -72    -64       C  
ATOM    995  CG  ASN A 132      45.130 -23.362  -1.704  1.00 29.16           C  
ANISOU  995  CG  ASN A 132     4025   3693   3362   1304    -79    -68       C  
ATOM    996  ND2 ASN A 132      43.804 -23.417  -1.832  1.00 26.51           N  
ANISOU  996  ND2 ASN A 132     3691   3355   3028   1305    -93    -72       N  
ATOM    997  OD1 ASN A 132      45.784 -24.254  -1.169  1.00 33.99           O  
ANISOU  997  OD1 ASN A 132     4632   4315   3966   1301    -74    -67       O  
ATOM    998  N   ARG A 133      47.654 -19.950  -2.957  1.00 16.27           N  
ANISOU  998  N   ARG A 133     2397   2031   1753   1315    -50    -57       N  
ATOM    999  CA  ARG A 133      48.382 -19.019  -3.792  1.00 27.74           C  
ANISOU  999  CA  ARG A 133     3859   3472   3209   1321    -42    -52       C  
ATOM   1000  C   ARG A 133      49.889 -19.010  -3.469  1.00 37.11           C  
ANISOU 1000  C   ARG A 133     5042   4663   4396   1319    -27    -48       C  
ATOM   1001  O   ARG A 133      50.739 -19.145  -4.358  1.00 44.46           O  
ANISOU 1001  O   ARG A 133     5988   5589   5316   1325    -18    -40       O  
ATOM   1002  CB  ARG A 133      47.779 -17.633  -3.575  1.00 27.61           C  
ANISOU 1002  CB  ARG A 133     3832   3447   3212   1320    -46    -57       C  
ATOM   1003  CG  ARG A 133      47.979 -16.641  -4.677  1.00 37.78           C  
ANISOU 1003  CG  ARG A 133     5133   4720   4502   1327    -43    -51       C  
ATOM   1004  CD  ARG A 133      46.673 -15.888  -4.927  1.00 51.38           C  
ANISOU 1004  CD  ARG A 133     6856   6434   6233   1329    -55    -55       C  
ATOM   1005  NE  ARG A 133      45.924 -15.627  -3.696  1.00 55.70           N  
ANISOU 1005  NE  ARG A 133     7380   6988   6794   1321    -62    -65       N  
ATOM   1006  CZ  ARG A 133      44.797 -14.914  -3.623  1.00 53.70           C  
ANISOU 1006  CZ  ARG A 133     7123   6730   6552   1321    -73    -70       C  
ATOM   1007  NH1 ARG A 133      44.269 -14.368  -4.717  1.00 54.89           N1+
ANISOU 1007  NH1 ARG A 133     7287   6868   6701   1327    -78    -66       N1+
ATOM   1008  NH2 ARG A 133      44.200 -14.740  -2.446  1.00 49.66           N  
ANISOU 1008  NH2 ARG A 133     6590   6225   6053   1314    -78    -79       N  
ATOM   1009  N   VAL A 134      50.222 -18.864  -2.192  1.00 35.64           N  
ANISOU 1009  N   VAL A 134     4834   4485   4221   1311    -23    -55       N  
ATOM   1010  CA  VAL A 134      51.622 -18.716  -1.802  1.00 34.97           C  
ANISOU 1010  CA  VAL A 134     4742   4404   4139   1309     -9    -53       C  
ATOM   1011  C   VAL A 134      52.433 -19.987  -2.059  1.00 30.54           C  
ANISOU 1011  C   VAL A 134     4193   3851   3561   1310     -3    -47       C  
ATOM   1012  O   VAL A 134      53.520 -19.932  -2.641  1.00 31.48           O  
ANISOU 1012  O   VAL A 134     4322   3967   3674   1314      9    -40       O  
ATOM   1013  CB  VAL A 134      51.755 -18.243  -0.327  1.00 27.62           C  
ANISOU 1013  CB  VAL A 134     3786   3482   3227   1300     -7    -62       C  
ATOM   1014  CG1 VAL A 134      53.196 -18.292   0.140  1.00 27.11           C  
ANISOU 1014  CG1 VAL A 134     3714   3422   3164   1297      7    -60       C  
ATOM   1015  CG2 VAL A 134      51.224 -16.843  -0.192  1.00 23.08           C  
ANISOU 1015  CG2 VAL A 134     3201   2898   2671   1300    -10    -67       C  
ATOM   1016  N   LEU A 135      51.894 -21.128  -1.639  1.00 27.20           N  
ANISOU 1016  N   LEU A 135     3769   3438   3128   1307     -9    -49       N  
ATOM   1017  CA  LEU A 135      52.551 -22.410  -1.847  1.00 30.19           C  
ANISOU 1017  CA  LEU A 135     4158   3825   3489   1308     -5    -43       C  
ATOM   1018  C   LEU A 135      52.752 -22.676  -3.332  1.00 28.51           C  
ANISOU 1018  C   LEU A 135     3971   3603   3259   1317     -3    -34       C  
ATOM   1019  O   LEU A 135      53.886 -22.915  -3.770  1.00 30.06           O  
ANISOU 1019  O   LEU A 135     4176   3799   3447   1320      8    -27       O  
ATOM   1020  CB  LEU A 135      51.747 -23.541  -1.201  1.00 39.66           C  
ANISOU 1020  CB  LEU A 135     5352   5036   4681   1303    -14    -48       C  
ATOM   1021  CG  LEU A 135      51.589 -23.453   0.319  1.00 36.41           C  
ANISOU 1021  CG  LEU A 135     4916   4635   4284   1293    -15    -57       C  
ATOM   1022  CD1 LEU A 135      51.058 -24.763   0.882  1.00 31.11           C  
ANISOU 1022  CD1 LEU A 135     4242   3976   3602   1289    -22    -60       C  
ATOM   1023  CD2 LEU A 135      52.912 -23.105   0.929  1.00 34.60           C  
ANISOU 1023  CD2 LEU A 135     4675   4410   4062   1290     -2    -57       C  
ATOM   1024  N   THR A 136      51.656 -22.616  -4.094  1.00 23.38           N  
ANISOU 1024  N   THR A 136     3332   2945   2605   1322    -14    -33       N  
ATOM   1025  CA  THR A 136      51.690 -22.831  -5.538  1.00 23.03           C  
ANISOU 1025  CA  THR A 136     3313   2892   2546   1331    -14    -25       C  
ATOM   1026  C   THR A 136      52.732 -21.934  -6.228  1.00 28.03           C  
ANISOU 1026  C   THR A 136     3954   3515   3182   1336     -2    -18       C  
ATOM   1027  O   THR A 136      53.534 -22.411  -7.033  1.00 29.46           O  
ANISOU 1027  O   THR A 136     4151   3693   3348   1341      6    -10       O  
ATOM   1028  CB  THR A 136      50.300 -22.630  -6.164  1.00 23.03           C  
ANISOU 1028  CB  THR A 136     3322   2884   2546   1334    -28    -27       C  
ATOM   1029  CG2 THR A 136      50.342 -22.797  -7.685  1.00 16.42           C  
ANISOU 1029  CG2 THR A 136     2511   2036   1693   1343    -28    -18       C  
ATOM   1030  OG1 THR A 136      49.386 -23.583  -5.610  1.00 21.98           O  
ANISOU 1030  OG1 THR A 136     3183   2760   2408   1330    -38    -32       O  
ATOM   1031  N   ASP A 137      52.736 -20.644  -5.903  1.00 24.28           N  
ANISOU 1031  N   ASP A 137     3467   3034   2726   1334      0    -22       N  
ATOM   1032  CA  ASP A 137      53.770 -19.758  -6.432  1.00 21.36           C  
ANISOU 1032  CA  ASP A 137     3102   2654   2360   1338     12    -16       C  
ATOM   1033  C   ASP A 137      55.178 -20.217  -6.087  1.00 26.30           C  
ANISOU 1033  C   ASP A 137     3724   3287   2981   1336     26    -12       C  
ATOM   1034  O   ASP A 137      56.049 -20.239  -6.951  1.00 34.98           O  
ANISOU 1034  O   ASP A 137     4839   4381   4071   1342     35     -4       O  
ATOM   1035  CB  ASP A 137      53.558 -18.318  -5.979  1.00 16.55           C  
ANISOU 1035  CB  ASP A 137     2477   2038   1773   1336     12    -22       C  
ATOM   1036  CG  ASP A 137      52.394 -17.665  -6.678  1.00 24.41           C  
ANISOU 1036  CG  ASP A 137     3480   3023   2772   1340      1    -23       C  
ATOM   1037  OD1 ASP A 137      51.922 -18.200  -7.703  1.00 26.88           O  
ANISOU 1037  OD1 ASP A 137     3812   3330   3069   1346     -5    -18       O  
ATOM   1038  OD2 ASP A 137      51.947 -16.605  -6.215  1.00 21.65           O1-
ANISOU 1038  OD2 ASP A 137     3118   2669   2441   1338     -2    -29       O1-
ATOM   1039  N   HIS A 138      55.402 -20.598  -4.830  1.00 23.16           N  
ANISOU 1039  N   HIS A 138     3308   2902   2590   1328     27    -19       N  
ATOM   1040  CA  HIS A 138      56.729 -21.059  -4.433  1.00 22.90           C  
ANISOU 1040  CA  HIS A 138     3271   2876   2552   1326     40    -15       C  
ATOM   1041  C   HIS A 138      57.138 -22.438  -4.937  1.00 27.76           C  
ANISOU 1041  C   HIS A 138     3902   3498   3146   1328     43     -9       C  
ATOM   1042  O   HIS A 138      58.293 -22.814  -4.789  1.00 32.55           O  
ANISOU 1042  O   HIS A 138     4509   4110   3748   1328     54     -4       O  
ATOM   1043  CB  HIS A 138      56.963 -20.945  -2.925  1.00 20.37           C  
ANISOU 1043  CB  HIS A 138     2925   2566   2247   1316     42    -24       C  
ATOM   1044  CG  HIS A 138      57.276 -19.556  -2.479  1.00 22.64           C  
ANISOU 1044  CG  HIS A 138     3198   2848   2556   1313     47    -28       C  
ATOM   1045  CD2 HIS A 138      58.428 -18.847  -2.517  1.00 27.90           C  
ANISOU 1045  CD2 HIS A 138     3861   3510   3229   1314     60    -25       C  
ATOM   1046  ND1 HIS A 138      56.323 -18.712  -1.956  1.00 27.87           N  
ANISOU 1046  ND1 HIS A 138     3847   3508   3234   1310     38    -36       N  
ATOM   1047  CE1 HIS A 138      56.879 -17.549  -1.672  1.00 36.60           C  
ANISOU 1047  CE1 HIS A 138     4942   4607   4357   1309     45    -39       C  
ATOM   1048  NE2 HIS A 138      58.156 -17.606  -2.005  1.00 38.50           N  
ANISOU 1048  NE2 HIS A 138     5188   4847   4592   1311     58    -32       N  
ATOM   1049  N   ILE A 139      56.227 -23.200  -5.533  1.00 27.50           N  
ANISOU 1049  N   ILE A 139     3884   3466   3100   1332     32     -7       N  
ATOM   1050  CA  ILE A 139      56.686 -24.436  -6.161  1.00 23.26           C  
ANISOU 1050  CA  ILE A 139     3363   2932   2541   1336     36      0       C  
ATOM   1051  C   ILE A 139      56.740 -24.375  -7.665  1.00 22.90           C  
ANISOU 1051  C   ILE A 139     3342   2875   2482   1345     37      9       C  
ATOM   1052  O   ILE A 139      56.916 -25.396  -8.303  1.00 36.94           O  
ANISOU 1052  O   ILE A 139     5137   4656   4241   1349     38     15       O  
ATOM   1053  CB  ILE A 139      55.940 -25.709  -5.668  1.00 49.31           C  
ANISOU 1053  CB  ILE A 139     6662   6244   5831   1332     26     -4       C  
ATOM   1054  CG1 ILE A 139      54.530 -25.827  -6.205  1.00 46.05           C  
ANISOU 1054  CG1 ILE A 139     6257   5826   5415   1335     11     -6       C  
ATOM   1055  CG2 ILE A 139      55.861 -25.724  -4.162  1.00 55.44           C  
ANISOU 1055  CG2 ILE A 139     7413   7032   6621   1322     25    -13       C  
ATOM   1056  CD1 ILE A 139      53.657 -26.706  -5.272  1.00 33.22           C  
ANISOU 1056  CD1 ILE A 139     4621   4213   3789   1328      1    -14       C  
ATOM   1057  N   SER A 140      56.659 -23.165  -8.215  1.00 19.86           N  
ANISOU 1057  N   SER A 140     2961   2478   2107   1349     38     10       N  
ATOM   1058  CA  SER A 140      56.434 -22.949  -9.638  1.00 16.54           C  
ANISOU 1058  CA  SER A 140     2563   2045   1677   1358     37     17       C  
ATOM   1059  C   SER A 140      57.698 -22.555 -10.373  1.00 30.86           C  
ANISOU 1059  C   SER A 140     4388   3852   3486   1363     52     27       C  
ATOM   1060  O   SER A 140      58.541 -21.841  -9.836  1.00 29.87           O  
ANISOU 1060  O   SER A 140     4249   3725   3373   1360     61     26       O  
ATOM   1061  CB  SER A 140      55.375 -21.867  -9.830  1.00 22.51           C  
ANISOU 1061  CB  SER A 140     3316   2791   2446   1359     27     13       C  
ATOM   1062  OG  SER A 140      54.087 -22.437  -9.920  1.00 24.81           O  
ANISOU 1062  OG  SER A 140     3611   3084   2733   1359     13      9       O  
ATOM   1063  N   SER A 141      57.818 -23.011 -11.619  1.00 29.88           N  
ANISOU 1063  N   SER A 141     4288   3722   3345   1370     53     35       N  
ATOM   1064  CA  SER A 141      59.006 -22.754 -12.427  1.00 24.34           C  
ANISOU 1064  CA  SER A 141     3599   3014   2637   1376     67     45       C  
ATOM   1065  C   SER A 141      58.742 -21.555 -13.283  1.00 25.54           C  
ANISOU 1065  C   SER A 141     3759   3151   2796   1381     67     47       C  
ATOM   1066  O   SER A 141      59.627 -20.716 -13.484  1.00 29.33           O  
ANISOU 1066  O   SER A 141     4238   3623   3283   1383     78     52       O  
ATOM   1067  CB  SER A 141      59.324 -23.949 -13.329  1.00 24.35           C  
ANISOU 1067  CB  SER A 141     3621   3017   2613   1381     70     53       C  
ATOM   1068  OG  SER A 141      59.446 -25.136 -12.581  1.00 32.11           O  
ANISOU 1068  OG  SER A 141     4599   4014   3589   1376     69     50       O  
ATOM   1069  N   TYR A 142      57.515 -21.487 -13.799  1.00 24.95           N  
ANISOU 1069  N   TYR A 142     3691   3070   2719   1384     54     45       N  
ATOM   1070  CA  TYR A 142      57.060 -20.332 -14.575  1.00 27.19           C  
ANISOU 1070  CA  TYR A 142     3982   3339   3011   1389     51     46       C  
ATOM   1071  C   TYR A 142      55.956 -19.568 -13.824  1.00 32.29           C  
ANISOU 1071  C   TYR A 142     4610   3984   3675   1384     40     36       C  
ATOM   1072  O   TYR A 142      54.879 -20.108 -13.533  1.00 36.18           O  
ANISOU 1072  O   TYR A 142     5100   4481   4165   1381     27     31       O  
ATOM   1073  CB  TYR A 142      56.563 -20.763 -15.963  1.00 33.25           C  
ANISOU 1073  CB  TYR A 142     4775   4099   3760   1396     46     53       C  
ATOM   1074  CG  TYR A 142      57.536 -21.615 -16.762  1.00 33.40           C  
ANISOU 1074  CG  TYR A 142     4813   4119   3759   1401     57     62       C  
ATOM   1075  CD1 TYR A 142      58.483 -21.035 -17.592  1.00 33.18           C  
ANISOU 1075  CD1 TYR A 142     4797   4082   3729   1407     69     71       C  
ATOM   1076  CD2 TYR A 142      57.492 -22.993 -16.693  1.00 35.12           C  
ANISOU 1076  CD2 TYR A 142     5037   4347   3961   1400     54     62       C  
ATOM   1077  CE1 TYR A 142      59.356 -21.798 -18.325  1.00 40.24           C  
ANISOU 1077  CE1 TYR A 142     5708   4977   4604   1411     79     80       C  
ATOM   1078  CE2 TYR A 142      58.372 -23.767 -17.417  1.00 45.02           C  
ANISOU 1078  CE2 TYR A 142     6308   5602   5196   1405     63     71       C  
ATOM   1079  CZ  TYR A 142      59.301 -23.165 -18.237  1.00 47.26           C  
ANISOU 1079  CZ  TYR A 142     6602   5877   5477   1410     76     80       C  
ATOM   1080  OH  TYR A 142      60.180 -23.943 -18.961  1.00 48.92           O  
ANISOU 1080  OH  TYR A 142     6829   6088   5668   1415     86     88       O  
ATOM   1081  N   LEU A 143      56.233 -18.313 -13.499  1.00 30.78           N  
ANISOU 1081  N   LEU A 143     4407   3786   3503   1383     44     34       N  
ATOM   1082  CA  LEU A 143      55.242 -17.475 -12.848  1.00 30.34           C  
ANISOU 1082  CA  LEU A 143     4336   3729   3465   1379     34     25       C  
ATOM   1083  C   LEU A 143      54.727 -16.411 -13.781  1.00 27.49           C  
ANISOU 1083  C   LEU A 143     3984   3352   3109   1385     31     28       C  
ATOM   1084  O   LEU A 143      55.369 -15.382 -13.949  1.00 30.06           O  
ANISOU 1084  O   LEU A 143     4307   3669   3444   1386     39     31       O  
ATOM   1085  CB  LEU A 143      55.839 -16.818 -11.607  1.00 33.48           C  
ANISOU 1085  CB  LEU A 143     4708   4130   3881   1372     41     20       C  
ATOM   1086  CG  LEU A 143      55.892 -17.793 -10.442  1.00 26.73           C  
ANISOU 1086  CG  LEU A 143     3839   3291   3025   1365     39     14       C  
ATOM   1087  CD1 LEU A 143      57.288 -17.888  -9.904  1.00 20.62           C  
ANISOU 1087  CD1 LEU A 143     3057   2524   2253   1362     54     16       C  
ATOM   1088  CD2 LEU A 143      54.923 -17.309  -9.404  1.00 23.00           C  
ANISOU 1088  CD2 LEU A 143     3347   2823   2570   1358     29      3       C  
ATOM   1089  N   PHE A 144      53.564 -16.652 -14.374  1.00 31.11           N  
ANISOU 1089  N   PHE A 144     4454   3807   3561   1387     18     27       N  
ATOM   1090  CA  PHE A 144      52.959 -15.699 -15.309  1.00 27.39           C  
ANISOU 1090  CA  PHE A 144     3993   3321   3094   1393     13     29       C  
ATOM   1091  C   PHE A 144      52.150 -14.663 -14.570  1.00 27.72           C  
ANISOU 1091  C   PHE A 144     4017   3360   3157   1389      5     21       C  
ATOM   1092  O   PHE A 144      50.946 -14.822 -14.376  1.00 32.39           O  
ANISOU 1092  O   PHE A 144     4604   3952   3749   1387     -8     15       O  
ATOM   1093  CB  PHE A 144      52.109 -16.427 -16.349  1.00 28.23           C  
ANISOU 1093  CB  PHE A 144     4120   3424   3183   1398      3     32       C  
ATOM   1094  CG  PHE A 144      52.907 -17.355 -17.210  1.00 32.74           C  
ANISOU 1094  CG  PHE A 144     4711   3997   3733   1403     11     41       C  
ATOM   1095  CD1 PHE A 144      53.876 -16.851 -18.071  1.00 34.56           C  
ANISOU 1095  CD1 PHE A 144     4954   4217   3959   1408     23     50       C  
ATOM   1096  CD2 PHE A 144      52.717 -18.726 -17.139  1.00 30.56           C  
ANISOU 1096  CD2 PHE A 144     4441   3730   3441   1401      7     41       C  
ATOM   1097  CE1 PHE A 144      54.635 -17.697 -18.852  1.00 39.27           C  
ANISOU 1097  CE1 PHE A 144     5569   4816   4537   1413     31     59       C  
ATOM   1098  CE2 PHE A 144      53.470 -19.580 -17.918  1.00 33.48           C  
ANISOU 1098  CE2 PHE A 144     4829   4101   3792   1406     15     49       C  
ATOM   1099  CZ  PHE A 144      54.427 -19.070 -18.778  1.00 40.79           C  
ANISOU 1099  CZ  PHE A 144     5766   5017   4713   1412     27     58       C  
ATOM   1100  N   ALA A 145      52.843 -13.611 -14.141  1.00 27.01           N  
ANISOU 1100  N   ALA A 145     3914   3266   3083   1387     14     20       N  
ATOM   1101  CA  ALA A 145      52.259 -12.537 -13.339  1.00 23.43           C  
ANISOU 1101  CA  ALA A 145     3441   2811   2651   1383      9     11       C  
ATOM   1102  C   ALA A 145      51.569 -11.559 -14.260  1.00 29.25           C  
ANISOU 1102  C   ALA A 145     4188   3533   3393   1388      4     13       C  
ATOM   1103  O   ALA A 145      52.104 -11.246 -15.324  1.00 31.37           O  
ANISOU 1103  O   ALA A 145     4474   3792   3655   1395     10     22       O  
ATOM   1104  CB  ALA A 145      53.331 -11.836 -12.561  1.00 19.32           C  
ANISOU 1104  CB  ALA A 145     2904   2292   2146   1379     22     10       C  
ATOM   1105  N   PRO A 146      50.368 -11.093 -13.872  1.00 30.29           N  
ANISOU 1105  N   PRO A 146     4311   3664   3536   1385     -9      6       N  
ATOM   1106  CA  PRO A 146      49.563 -10.199 -14.723  1.00 32.41           C  
ANISOU 1106  CA  PRO A 146     4588   3918   3808   1390    -16      7       C  
ATOM   1107  C   PRO A 146      50.082  -8.759 -14.808  1.00 36.56           C  
ANISOU 1107  C   PRO A 146     5108   4433   4350   1392     -8      8       C  
ATOM   1108  O   PRO A 146      49.966  -8.124 -15.864  1.00 38.46           O  
ANISOU 1108  O   PRO A 146     5364   4661   4590   1398     -8     14       O  
ATOM   1109  CB  PRO A 146      48.175 -10.231 -14.068  1.00 25.09           C  
ANISOU 1109  CB  PRO A 146     3649   2995   2889   1386    -32     -2       C  
ATOM   1110  CG  PRO A 146      48.391 -10.704 -12.688  1.00 17.47           C  
ANISOU 1110  CG  PRO A 146     2664   2044   1930   1378    -30     -9       C  
ATOM   1111  CD  PRO A 146      49.648 -11.512 -12.657  1.00 26.47           C  
ANISOU 1111  CD  PRO A 146     3807   3191   3058   1378    -18     -4       C  
ATOM   1112  N   THR A 147      50.652  -8.266 -13.713  1.00 34.84           N  
ANISOU 1112  N   THR A 147     4869   4220   4148   1386     -2      3       N  
ATOM   1113  CA  THR A 147      51.046  -6.870 -13.597  1.00 39.34           C  
ANISOU 1113  CA  THR A 147     5430   4781   4737   1386      5      2       C  
ATOM   1114  C   THR A 147      52.432  -6.780 -12.998  1.00 47.93           C  
ANISOU 1114  C   THR A 147     6508   5874   5831   1384     20      3       C  
ATOM   1115  O   THR A 147      52.900  -7.729 -12.375  1.00 50.57           O  
ANISOU 1115  O   THR A 147     6836   6220   6158   1380     23      2       O  
ATOM   1116  CB  THR A 147      50.101  -6.114 -12.644  1.00 37.69           C  
ANISOU 1116  CB  THR A 147     5200   4573   4547   1381     -5     -9       C  
ATOM   1117  CG2 THR A 147      48.666  -6.219 -13.116  1.00 33.49           C  
ANISOU 1117  CG2 THR A 147     4677   4037   4011   1383    -20    -10       C  
ATOM   1118  OG1 THR A 147      50.191  -6.683 -11.327  1.00 44.21           O  
ANISOU 1118  OG1 THR A 147     6008   5414   5378   1373     -5    -16       O  
ATOM   1119  N   GLU A 148      53.080  -5.630 -13.162  1.00 52.29           N  
ANISOU 1119  N   GLU A 148     7056   6416   6395   1385     29      5       N  
ATOM   1120  CA  GLU A 148      54.345  -5.370 -12.475  1.00 45.39           C  
ANISOU 1120  CA  GLU A 148     6169   5545   5530   1382     42      4       C  
ATOM   1121  C   GLU A 148      54.206  -5.495 -10.954  1.00 40.53           C  
ANISOU 1121  C   GLU A 148     5529   4943   4928   1373     40     -6       C  
ATOM   1122  O   GLU A 148      55.051  -6.111 -10.315  1.00 45.14           O  
ANISOU 1122  O   GLU A 148     6105   5537   5509   1369     48     -7       O  
ATOM   1123  CB  GLU A 148      54.929  -4.007 -12.869  1.00 40.23           C  
ANISOU 1123  CB  GLU A 148     5515   4879   4891   1385     51      7       C  
ATOM   1124  CG  GLU A 148      55.796  -4.044 -14.122  1.00 44.18           C  
ANISOU 1124  CG  GLU A 148     6036   5370   5379   1393     62     20       C  
ATOM   1125  CD  GLU A 148      57.166  -4.679 -13.873  1.00 51.47           C  
ANISOU 1125  CD  GLU A 148     6960   6302   6296   1392     76     24       C  
ATOM   1126  OE1 GLU A 148      57.686  -4.597 -12.728  1.00 49.71           O  
ANISOU 1126  OE1 GLU A 148     6717   6087   6085   1385     80     17       O  
ATOM   1127  OE2 GLU A 148      57.721  -5.267 -14.830  1.00 52.02           O1-
ANISOU 1127  OE2 GLU A 148     7049   6368   6348   1397     82     34       O1-
ATOM   1128  N   ILE A 149      53.141  -4.922 -10.392  1.00 30.28           N  
ANISOU 1128  N   ILE A 149     4217   3644   3643   1369     29    -15       N  
ATOM   1129  CA  ILE A 149      52.858  -5.011  -8.966  1.00 27.47           C  
ANISOU 1129  CA  ILE A 149     3839   3300   3300   1361     25    -25       C  
ATOM   1130  C   ILE A 149      52.909  -6.470  -8.492  1.00 39.90           C  
ANISOU 1130  C   ILE A 149     5413   4889   4859   1357     23    -26       C  
ATOM   1131  O   ILE A 149      53.513  -6.792  -7.448  1.00 44.37           O  
ANISOU 1131  O   ILE A 149     5963   5466   5430   1351     29    -31       O  
ATOM   1132  CB  ILE A 149      51.456  -4.436  -8.639  1.00 49.37           C  
ANISOU 1132  CB  ILE A 149     6603   6070   6083   1359     11    -33       C  
ATOM   1133  CG1 ILE A 149      51.072  -3.304  -9.606  1.00 45.04           C  
ANISOU 1133  CG1 ILE A 149     6066   5507   5542   1365      9    -30       C  
ATOM   1134  CG2 ILE A 149      51.387  -3.971  -7.188  1.00 52.73           C  
ANISOU 1134  CG2 ILE A 149     7002   6504   6529   1350     11    -44       C  
ATOM   1135  CD1 ILE A 149      51.819  -2.021  -9.397  1.00 43.14           C  
ANISOU 1135  CD1 ILE A 149     5814   5258   5320   1365     19    -31       C  
ATOM   1136  N   ALA A 150      52.289  -7.349  -9.283  1.00 41.43           N  
ANISOU 1136  N   ALA A 150     5624   5083   5034   1361     16    -22       N  
ATOM   1137  CA  ALA A 150      52.293  -8.793  -9.025  1.00 34.66           C  
ANISOU 1137  CA  ALA A 150     4771   4239   4161   1359     13    -21       C  
ATOM   1138  C   ALA A 150      53.714  -9.348  -8.966  1.00 35.18           C  
ANISOU 1138  C   ALA A 150     4838   4309   4219   1359     28    -16       C  
ATOM   1139  O   ALA A 150      54.071 -10.130  -8.067  1.00 41.64           O  
ANISOU 1139  O   ALA A 150     5645   5140   5034   1353     30    -19       O  
ATOM   1140  CB  ALA A 150      51.500  -9.504 -10.096  1.00 27.87           C  
ANISOU 1140  CB  ALA A 150     3932   3374   3282   1365      4    -16       C  
ATOM   1141  N   LYS A 151      54.516  -8.932  -9.940  1.00 29.44           N  
ANISOU 1141  N   LYS A 151     4125   3572   3487   1365     37     -7       N  
ATOM   1142  CA  LYS A 151      55.913  -9.306 -10.012  1.00 28.27           C  
ANISOU 1142  CA  LYS A 151     3981   3428   3334   1366     52     -1       C  
ATOM   1143  C   LYS A 151      56.658  -8.866  -8.756  1.00 25.03           C  
ANISOU 1143  C   LYS A 151     3547   3024   2940   1358     60     -8       C  
ATOM   1144  O   LYS A 151      57.433  -9.625  -8.193  1.00 26.93           O  
ANISOU 1144  O   LYS A 151     3782   3274   3175   1354     66     -8       O  
ATOM   1145  CB  LYS A 151      56.546  -8.702 -11.269  1.00 31.70           C  
ANISOU 1145  CB  LYS A 151     4434   3848   3764   1374     60      9       C  
ATOM   1146  CG  LYS A 151      58.006  -9.049 -11.482  1.00 30.70           C  
ANISOU 1146  CG  LYS A 151     4312   3723   3629   1375     76     16       C  
ATOM   1147  CD  LYS A 151      58.474  -8.493 -12.809  1.00 36.91           C  
ANISOU 1147  CD  LYS A 151     5118   4495   4410   1384     83     27       C  
ATOM   1148  CE  LYS A 151      59.460  -7.354 -12.621  1.00 43.58           C  
ANISOU 1148  CE  LYS A 151     5954   5334   5272   1383     96     27       C  
ATOM   1149  NZ  LYS A 151      60.849  -7.762 -12.983  1.00 42.75           N1+
ANISOU 1149  NZ  LYS A 151     5856   5229   5157   1386    111     36       N1+
ATOM   1150  N   ASN A 152      56.402  -7.648  -8.305  1.00 27.93           N  
ANISOU 1150  N   ASN A 152     3899   3385   3327   1356     58    -14       N  
ATOM   1151  CA  ASN A 152      57.031  -7.139  -7.090  1.00 34.41           C  
ANISOU 1151  CA  ASN A 152     4697   4211   4166   1349     65    -21       C  
ATOM   1152  C   ASN A 152      56.647  -7.939  -5.854  1.00 33.72           C  
ANISOU 1152  C   ASN A 152     4593   4139   4080   1340     59    -30       C  
ATOM   1153  O   ASN A 152      57.471  -8.128  -4.953  1.00 37.67           O  
ANISOU 1153  O   ASN A 152     5080   4648   4586   1334     67    -33       O  
ATOM   1154  CB  ASN A 152      56.721  -5.651  -6.883  1.00 33.63           C  
ANISOU 1154  CB  ASN A 152     4586   4102   4089   1348     64    -27       C  
ATOM   1155  CG  ASN A 152      57.326  -4.778  -7.962  1.00 36.49           C  
ANISOU 1155  CG  ASN A 152     4961   4449   4453   1355     72    -18       C  
ATOM   1156  ND2 ASN A 152      56.728  -3.615  -8.191  1.00 37.36           N  
ANISOU 1156  ND2 ASN A 152     5070   4549   4578   1357     68    -21       N  
ATOM   1157  OD1 ASN A 152      58.317  -5.150  -8.589  1.00 41.73           O  
ANISOU 1157  OD1 ASN A 152     5638   5112   5106   1359     83    -10       O  
ATOM   1158  N   ASN A 153      55.403  -8.406  -5.812  1.00 32.72           N  
ANISOU 1158  N   ASN A 153     4469   4016   3948   1340     45    -33       N  
ATOM   1159  CA  ASN A 153      54.992  -9.331  -4.756  1.00 40.05           C  
ANISOU 1159  CA  ASN A 153     5385   4960   4874   1333     39    -40       C  
ATOM   1160  C   ASN A 153      55.821 -10.599  -4.759  1.00 43.53           C  
ANISOU 1160  C   ASN A 153     5832   5409   5297   1332     46    -35       C  
ATOM   1161  O   ASN A 153      56.401 -10.986  -3.727  1.00 46.03           O  
ANISOU 1161  O   ASN A 153     6133   5737   5617   1325     51    -39       O  
ATOM   1162  CB  ASN A 153      53.524  -9.700  -4.901  1.00 47.76           C  
ANISOU 1162  CB  ASN A 153     6365   5936   5844   1333     24    -43       C  
ATOM   1163  CG  ASN A 153      52.620  -8.554  -4.580  1.00 57.96           C  
ANISOU 1163  CG  ASN A 153     7646   7222   7154   1332     16    -50       C  
ATOM   1164  ND2 ASN A 153      51.427  -8.858  -4.101  1.00 60.14           N  
ANISOU 1164  ND2 ASN A 153     7915   7503   7431   1328      3    -56       N  
ATOM   1165  OD1 ASN A 153      52.996  -7.394  -4.745  1.00 66.29           O  
ANISOU 1165  OD1 ASN A 153     8698   8267   8223   1333     22    -50       O  
ATOM   1166  N   LEU A 154      55.873 -11.236  -5.932  1.00 37.44           N  
ANISOU 1166  N   LEU A 154     5085   4635   4507   1339     46    -26       N  
ATOM   1167  CA  LEU A 154      56.607 -12.478  -6.102  1.00 30.23           C  
ANISOU 1167  CA  LEU A 154     4180   3729   3575   1340     52    -20       C  
ATOM   1168  C   LEU A 154      58.046 -12.251  -5.755  1.00 36.67           C  
ANISOU 1168  C   LEU A 154     4989   4547   4396   1338     67    -18       C  
ATOM   1169  O   LEU A 154      58.727 -13.157  -5.293  1.00 50.41           O  
ANISOU 1169  O   LEU A 154     6727   6298   6129   1334     73    -17       O  
ATOM   1170  CB  LEU A 154      56.518 -12.938  -7.547  1.00 30.61           C  
ANISOU 1170  CB  LEU A 154     4256   3770   3605   1349     51    -10       C  
ATOM   1171  CG  LEU A 154      55.116 -13.225  -8.077  1.00 27.86           C  
ANISOU 1171  CG  LEU A 154     3918   3419   3249   1352     36    -11       C  
ATOM   1172  CD1 LEU A 154      55.129 -13.412  -9.596  1.00 23.63           C  
ANISOU 1172  CD1 LEU A 154     3408   2873   2697   1361     37     -1       C  
ATOM   1173  CD2 LEU A 154      54.576 -14.448  -7.362  1.00 23.04           C  
ANISOU 1173  CD2 LEU A 154     3301   2822   2630   1347     29    -15       C  
ATOM   1174  N   LEU A 155      58.501 -11.027  -5.988  1.00 35.82           N  
ANISOU 1174  N   LEU A 155     4879   4429   4303   1340     74    -17       N  
ATOM   1175  CA  LEU A 155      59.877 -10.611  -5.729  1.00 42.15           C  
ANISOU 1175  CA  LEU A 155     5673   5229   5111   1338     89    -15       C  
ATOM   1176  C   LEU A 155      60.214 -10.385  -4.243  1.00 38.63           C  
ANISOU 1176  C   LEU A 155     5201   4793   4682   1328     91    -25       C  
ATOM   1177  O   LEU A 155      61.293 -10.775  -3.779  1.00 34.69           O  
ANISOU 1177  O   LEU A 155     4696   4301   4182   1325    102    -24       O  
ATOM   1178  CB  LEU A 155      60.211  -9.363  -6.553  1.00 38.13           C  
ANISOU 1178  CB  LEU A 155     5171   4705   4612   1344     95    -10       C  
ATOM   1179  CG  LEU A 155      60.557  -9.636  -8.011  1.00 35.89           C  
ANISOU 1179  CG  LEU A 155     4913   4412   4311   1354     99      2       C  
ATOM   1180  CD1 LEU A 155      60.818  -8.332  -8.737  1.00 37.25           C  
ANISOU 1180  CD1 LEU A 155     5091   4569   4494   1359    105      6       C  
ATOM   1181  CD2 LEU A 155      61.749 -10.582  -8.126  1.00 32.57           C  
ANISOU 1181  CD2 LEU A 155     4500   3999   3876   1354    111      9       C  
ATOM   1182  N   ARG A 156      59.305  -9.764  -3.497  1.00 37.93           N  
ANISOU 1182  N   ARG A 156     5096   4705   4609   1324     82    -34       N  
ATOM   1183  CA  ARG A 156      59.518  -9.629  -2.060  1.00 52.98           C  
ANISOU 1183  CA  ARG A 156     6978   6621   6530   1314     84    -44       C  
ATOM   1184  C   ARG A 156      59.513 -10.986  -1.372  1.00 56.21           C  
ANISOU 1184  C   ARG A 156     7383   7046   6927   1309     81    -46       C  
ATOM   1185  O   ARG A 156      59.803 -11.078  -0.187  1.00 60.34           O  
ANISOU 1185  O   ARG A 156     7888   7579   7460   1301     83    -53       O  
ATOM   1186  CB  ARG A 156      58.428  -8.798  -1.395  1.00 60.96           C  
ANISOU 1186  CB  ARG A 156     7974   7631   7559   1310     74    -54       C  
ATOM   1187  CG  ARG A 156      58.200  -7.386  -1.884  1.00 67.10           C  
ANISOU 1187  CG  ARG A 156     8751   8393   8350   1314     74    -54       C  
ATOM   1188  CD  ARG A 156      56.815  -6.991  -1.408  1.00 72.43           C  
ANISOU 1188  CD  ARG A 156     9417   9069   9035   1312     60    -62       C  
ATOM   1189  NE  ARG A 156      55.959  -8.182  -1.392  1.00 80.53           N  
ANISOU 1189  NE  ARG A 156    10450  10104  10045   1311     50    -62       N  
ATOM   1190  CZ  ARG A 156      55.438  -8.749  -0.301  1.00 80.54           C  
ANISOU 1190  CZ  ARG A 156    10436  10117  10048   1304     43    -70       C  
ATOM   1191  NH1 ARG A 156      55.662  -8.225   0.901  1.00 79.61           N1+
ANISOU 1191  NH1 ARG A 156    10297  10005   9948   1296     46    -79       N1+
ATOM   1192  NH2 ARG A 156      54.693  -9.849  -0.421  1.00 75.35           N  
ANISOU 1192  NH2 ARG A 156     9787   9467   9376   1304     34    -69       N  
ATOM   1193  N   GLU A 157      59.140 -12.030  -2.101  1.00 59.07           N  
ANISOU 1193  N   GLU A 157     7764   7411   7270   1314     76    -40       N  
ATOM   1194  CA  GLU A 157      59.120 -13.384  -1.556  1.00 52.45           C  
ANISOU 1194  CA  GLU A 157     6925   6587   6419   1309     74    -41       C  
ATOM   1195  C   GLU A 157      60.290 -14.196  -2.046  1.00 46.33           C  
ANISOU 1195  C   GLU A 157     6161   5814   5627   1312     85    -32       C  
ATOM   1196  O   GLU A 157      60.226 -15.411  -2.091  1.00 47.33           O  
ANISOU 1196  O   GLU A 157     6296   5950   5738   1312     83    -29       O  
ATOM   1197  CB  GLU A 157      57.850 -14.107  -1.952  1.00 49.79           C  
ANISOU 1197  CB  GLU A 157     6598   6251   6068   1312     60    -41       C  
ATOM   1198  CG  GLU A 157      56.604 -13.419  -1.516  1.00 54.49           C  
ANISOU 1198  CG  GLU A 157     7183   6845   6678   1310     49    -49       C  
ATOM   1199  CD  GLU A 157      55.490 -14.401  -1.374  1.00 55.74           C  
ANISOU 1199  CD  GLU A 157     7344   7010   6825   1308     36    -51       C  
ATOM   1200  OE1 GLU A 157      55.545 -15.197  -0.414  1.00 55.01           O  
ANISOU 1200  OE1 GLU A 157     7241   6931   6731   1302     35    -56       O  
ATOM   1201  OE2 GLU A 157      54.594 -14.412  -2.241  1.00 54.51           O1-
ANISOU 1201  OE2 GLU A 157     7202   6847   6661   1314     27    -48       O1-
ATOM   1202  N   GLY A 158      61.351 -13.516  -2.437  1.00 50.41           N  
ANISOU 1202  N   GLY A 158     6681   6324   6150   1315     97    -27       N  
ATOM   1203  CA  GLY A 158      62.579 -14.187  -2.801  1.00 52.55           C  
ANISOU 1203  CA  GLY A 158     6960   6597   6407   1317    109    -19       C  
ATOM   1204  C   GLY A 158      62.461 -15.050  -4.035  1.00 52.38           C  
ANISOU 1204  C   GLY A 158     6965   6573   6363   1325    108     -9       C  
ATOM   1205  O   GLY A 158      63.350 -15.843  -4.305  1.00 54.67           O  
ANISOU 1205  O   GLY A 158     7264   6868   6640   1326    116     -2       O  
ATOM   1206  N   ILE A 159      61.377 -14.912  -4.790  1.00 53.03           N  
ANISOU 1206  N   ILE A 159     7059   6648   6440   1330     97     -8       N  
ATOM   1207  CA  ILE A 159      61.226 -15.729  -5.994  1.00 49.30           C  
ANISOU 1207  CA  ILE A 159     6613   6174   5947   1338     96      2       C  
ATOM   1208  C   ILE A 159      62.096 -15.190  -7.122  1.00 49.54           C  
ANISOU 1208  C   ILE A 159     6658   6191   5973   1346    107     12       C  
ATOM   1209  O   ILE A 159      62.004 -14.015  -7.478  1.00 51.28           O  
ANISOU 1209  O   ILE A 159     6879   6401   6206   1348    108     12       O  
ATOM   1210  CB  ILE A 159      59.759 -15.871  -6.441  1.00 36.54           C  
ANISOU 1210  CB  ILE A 159     5004   4553   4325   1341     80      0       C  
ATOM   1211  CG1 ILE A 159      58.974 -16.666  -5.393  1.00 34.05           C  
ANISOU 1211  CG1 ILE A 159     4676   4252   4010   1334     70     -9       C  
ATOM   1212  CG2 ILE A 159      59.699 -16.569  -7.767  1.00 27.36           C  
ANISOU 1212  CG2 ILE A 159     3868   3386   3141   1349     80      9       C  
ATOM   1213  CD1 ILE A 159      57.541 -16.877  -5.735  1.00 34.91           C  
ANISOU 1213  CD1 ILE A 159     4792   4358   4114   1336     55    -11       C  
ATOM   1214  N   GLU A 160      62.946 -16.059  -7.661  1.00 47.29           N  
ANISOU 1214  N   GLU A 160     6387   5910   5671   1349    115     20       N  
ATOM   1215  CA  GLU A 160      63.934 -15.686  -8.669  1.00 47.32           C  
ANISOU 1215  CA  GLU A 160     6406   5904   5669   1356    127     30       C  
ATOM   1216  C   GLU A 160      63.325 -14.930  -9.860  1.00 48.42           C  
ANISOU 1216  C   GLU A 160     6562   6028   5808   1364    123     35       C  
ATOM   1217  O   GLU A 160      62.410 -15.419 -10.517  1.00 49.54           O  
ANISOU 1217  O   GLU A 160     6718   6168   5937   1368    113     37       O  
ATOM   1218  CB  GLU A 160      64.706 -16.934  -9.107  1.00 55.68           C  
ANISOU 1218  CB  GLU A 160     7479   6969   6707   1358    134     39       C  
ATOM   1219  CG  GLU A 160      65.522 -16.779 -10.374  1.00 75.29           C  
ANISOU 1219  CG  GLU A 160     9985   9444   9180   1366    145     51       C  
ATOM   1220  CD  GLU A 160      66.699 -15.821 -10.240  1.00 89.94           C  
ANISOU 1220  CD  GLU A 160    11832  11293  11049   1366    159     53       C  
ATOM   1221  OE1 GLU A 160      67.621 -16.106  -9.439  1.00 94.35           O  
ANISOU 1221  OE1 GLU A 160    12378  11860  11611   1360    167     51       O  
ATOM   1222  OE2 GLU A 160      66.707 -14.789 -10.954  1.00 91.93           O1-
ANISOU 1222  OE2 GLU A 160    12090  11532  11308   1371    162     56       O1-
ATOM   1223  N   GLU A 161      63.830 -13.724 -10.107  1.00 51.46           N  
ANISOU 1223  N   GLU A 161     6944   6402   6206   1366    131     37       N  
ATOM   1224  CA  GLU A 161      63.320 -12.834 -11.153  1.00 55.74           C  
ANISOU 1224  CA  GLU A 161     7499   6930   6750   1373    128     41       C  
ATOM   1225  C   GLU A 161      63.168 -13.467 -12.542  1.00 60.97           C  
ANISOU 1225  C   GLU A 161     8189   7586   7390   1381    127     51       C  
ATOM   1226  O   GLU A 161      62.261 -13.103 -13.290  1.00 69.21           O  
ANISOU 1226  O   GLU A 161     9243   8621   8432   1386    119     52       O  
ATOM   1227  CB  GLU A 161      64.196 -11.585 -11.251  1.00 59.88           C  
ANISOU 1227  CB  GLU A 161     8017   7443   7290   1374    140     43       C  
ATOM   1228  CG  GLU A 161      63.825 -10.623 -12.367  1.00 67.49           C  
ANISOU 1228  CG  GLU A 161     8996   8392   8257   1381    139     48       C  
ATOM   1229  CD  GLU A 161      64.000  -9.163 -11.958  1.00 79.19           C  
ANISOU 1229  CD  GLU A 161    10462   9866   9763   1379    142     43       C  
ATOM   1230  OE1 GLU A 161      64.587  -8.912 -10.880  1.00 81.99           O  
ANISOU 1230  OE1 GLU A 161    10796  10226  10131   1372    147     37       O  
ATOM   1231  OE2 GLU A 161      63.543  -8.267 -12.707  1.00 81.45           O1-
ANISOU 1231  OE2 GLU A 161    10755  10138  10053   1384    140     45       O1-
ATOM   1232  N   ASN A 162      64.037 -14.410 -12.893  1.00 55.52           N  
ANISOU 1232  N   ASN A 162     7510   6901   6683   1383    136     58       N  
ATOM   1233  CA  ASN A 162      63.953 -15.034 -14.218  1.00 51.95           C  
ANISOU 1233  CA  ASN A 162     7084   6444   6210   1391    136     68       C  
ATOM   1234  C   ASN A 162      62.832 -16.060 -14.349  1.00 46.80           C  
ANISOU 1234  C   ASN A 162     6440   5798   5543   1392    122     66       C  
ATOM   1235  O   ASN A 162      62.570 -16.567 -15.437  1.00 48.85           O  
ANISOU 1235  O   ASN A 162     6721   6053   5786   1398    120     72       O  
ATOM   1236  CB  ASN A 162      65.305 -15.616 -14.673  1.00 57.07           C  
ANISOU 1236  CB  ASN A 162     7744   7095   6845   1394    151     78       C  
ATOM   1237  CG  ASN A 162      65.794 -16.759 -13.790  1.00 62.55           C  
ANISOU 1237  CG  ASN A 162     8430   7805   7533   1389    153     76       C  
ATOM   1238  ND2 ASN A 162      67.104 -16.826 -13.592  1.00 65.99           N  
ANISOU 1238  ND2 ASN A 162     8862   8243   7968   1388    167     80       N  
ATOM   1239  OD1 ASN A 162      65.010 -17.572 -13.298  1.00 61.41           O  
ANISOU 1239  OD1 ASN A 162     8281   7669   7382   1385    142     70       O  
ATOM   1240  N   LYS A 163      62.176 -16.363 -13.236  1.00 42.57           N  
ANISOU 1240  N   LYS A 163     5887   5272   5015   1384    113     56       N  
ATOM   1241  CA  LYS A 163      61.005 -17.227 -13.266  1.00 38.74           C  
ANISOU 1241  CA  LYS A 163     5406   4792   4519   1384     98     52       C  
ATOM   1242  C   LYS A 163      59.734 -16.423 -13.500  1.00 37.65           C  
ANISOU 1242  C   LYS A 163     5268   4645   4391   1385     86     47       C  
ATOM   1243  O   LYS A 163      58.695 -17.000 -13.835  1.00 39.99           O  
ANISOU 1243  O   LYS A 163     5573   4943   4678   1387     74     46       O  
ATOM   1244  CB  LYS A 163      60.869 -18.029 -11.973  1.00 34.73           C  
ANISOU 1244  CB  LYS A 163     4881   4300   4014   1376     94     44       C  
ATOM   1245  CG  LYS A 163      61.921 -19.094 -11.796  1.00 30.35           C  
ANISOU 1245  CG  LYS A 163     4330   3756   3447   1374    104     49       C  
ATOM   1246  CD  LYS A 163      61.550 -20.030 -10.689  1.00 29.49           C  
ANISOU 1246  CD  LYS A 163     4207   3661   3336   1367     97     41       C  
ATOM   1247  CE  LYS A 163      62.726 -20.884 -10.285  1.00 34.90           C  
ANISOU 1247  CE  LYS A 163     4891   4357   4013   1364    108     45       C  
ATOM   1248  NZ  LYS A 163      63.610 -20.168  -9.334  1.00 41.52           N1+
ANISOU 1248  NZ  LYS A 163     5708   5197   4869   1359    118     41       N1+
ATOM   1249  N   ILE A 164      59.824 -15.102 -13.332  1.00 31.38           N  
ANISOU 1249  N   ILE A 164     4464   3843   3617   1385     89     45       N  
ATOM   1250  CA  ILE A 164      58.655 -14.228 -13.449  1.00 32.21           C  
ANISOU 1250  CA  ILE A 164     4566   3940   3733   1385     77     40       C  
ATOM   1251  C   ILE A 164      58.448 -13.622 -14.828  1.00 33.62           C  
ANISOU 1251  C   ILE A 164     4765   4103   3906   1394     77     47       C  
ATOM   1252  O   ILE A 164      59.347 -13.015 -15.387  1.00 40.10           O  
ANISOU 1252  O   ILE A 164     5592   4916   4729   1398     89     54       O  
ATOM   1253  CB  ILE A 164      58.699 -13.065 -12.457  1.00 28.80           C  
ANISOU 1253  CB  ILE A 164     4110   3506   3325   1380     78     32       C  
ATOM   1254  CG1 ILE A 164      59.130 -13.552 -11.072  1.00 32.50           C  
ANISOU 1254  CG1 ILE A 164     4558   3989   3801   1371     81     25       C  
ATOM   1255  CG2 ILE A 164      57.335 -12.409 -12.397  1.00 20.15           C  
ANISOU 1255  CG2 ILE A 164     3010   2405   2240   1379     64     25       C  
ATOM   1256  CD1 ILE A 164      59.083 -12.471 -10.007  1.00 32.36           C  
ANISOU 1256  CD1 ILE A 164     4517   3972   3808   1365     81     16       C  
ATOM   1257  N   PHE A 165      57.240 -13.763 -15.353  1.00 31.60           N  
ANISOU 1257  N   PHE A 165     4518   3844   3645   1396     64     46       N  
ATOM   1258  CA  PHE A 165      56.897 -13.218 -16.655  1.00 29.28           C  
ANISOU 1258  CA  PHE A 165     4243   3535   3345   1404     62     52       C  
ATOM   1259  C   PHE A 165      55.621 -12.409 -16.573  1.00 35.86           C  
ANISOU 1259  C   PHE A 165     5071   4363   4192   1403     49     45       C  
ATOM   1260  O   PHE A 165      54.532 -12.968 -16.424  1.00 39.86           O  
ANISOU 1260  O   PHE A 165     5578   4874   4695   1401     36     40       O  
ATOM   1261  CB  PHE A 165      56.675 -14.332 -17.655  1.00 22.03           C  
ANISOU 1261  CB  PHE A 165     3349   2618   2404   1409     59     58       C  
ATOM   1262  CG  PHE A 165      57.879 -15.168 -17.904  1.00 34.87           C  
ANISOU 1262  CG  PHE A 165     4984   4250   4015   1411     71     66       C  
ATOM   1263  CD1 PHE A 165      58.211 -16.210 -17.040  1.00 38.13           C  
ANISOU 1263  CD1 PHE A 165     5388   4677   4423   1406     73     63       C  
ATOM   1264  CD2 PHE A 165      58.675 -14.939 -19.024  1.00 36.29           C  
ANISOU 1264  CD2 PHE A 165     5182   4421   4186   1418     82     76       C  
ATOM   1265  CE1 PHE A 165      59.329 -17.001 -17.277  1.00 36.60           C  
ANISOU 1265  CE1 PHE A 165     5203   4489   4215   1407     84     70       C  
ATOM   1266  CE2 PHE A 165      59.796 -15.730 -19.279  1.00 33.07           C  
ANISOU 1266  CE2 PHE A 165     4784   4018   3764   1420     94     84       C  
ATOM   1267  CZ  PHE A 165      60.126 -16.759 -18.401  1.00 34.90           C  
ANISOU 1267  CZ  PHE A 165     5006   4264   3990   1415     95     80       C  
ATOM   1268  N   VAL A 166      55.758 -11.093 -16.672  1.00 34.52           N  
ANISOU 1268  N   VAL A 166     4896   4183   4038   1404     52     45       N  
ATOM   1269  CA  VAL A 166      54.600 -10.212 -16.718  1.00 32.39           C  
ANISOU 1269  CA  VAL A 166     4622   3905   3781   1405     41     40       C  
ATOM   1270  C   VAL A 166      53.966 -10.238 -18.110  1.00 33.31           C  
ANISOU 1270  C   VAL A 166     4762   4011   3884   1412     35     46       C  
ATOM   1271  O   VAL A 166      54.562  -9.770 -19.065  1.00 38.15           O  
ANISOU 1271  O   VAL A 166     5389   4614   4493   1418     43     54       O  
ATOM   1272  CB  VAL A 166      54.978  -8.780 -16.332  1.00 17.87           C  
ANISOU 1272  CB  VAL A 166     2768   2058   1963   1403     47     37       C  
ATOM   1273  CG1 VAL A 166      53.757  -7.895 -16.353  1.00 17.92           C  
ANISOU 1273  CG1 VAL A 166     2770   2057   1982   1403     35     32       C  
ATOM   1274  CG2 VAL A 166      55.599  -8.767 -14.961  1.00 19.64           C  
ANISOU 1274  CG2 VAL A 166     2969   2293   2200   1396     53     31       C  
ATOM   1275  N   VAL A 167      52.766 -10.802 -18.216  1.00 30.25           N  
ANISOU 1275  N   VAL A 167     4378   3625   3489   1412     20     42       N  
ATOM   1276  CA  VAL A 167      52.172 -11.128 -19.516  1.00 26.53           C  
ANISOU 1276  CA  VAL A 167     3931   3147   3003   1418     14     48       C  
ATOM   1277  C   VAL A 167      50.710 -10.738 -19.557  1.00 28.70           C  
ANISOU 1277  C   VAL A 167     4204   3417   3285   1417     -2     42       C  
ATOM   1278  O   VAL A 167      49.983 -11.120 -20.480  1.00 27.24           O  
ANISOU 1278  O   VAL A 167     4035   3227   3087   1422    -11     44       O  
ATOM   1279  CB  VAL A 167      52.234 -12.647 -19.814  1.00 22.01           C  
ANISOU 1279  CB  VAL A 167     3372   2583   2409   1419     12     51       C  
ATOM   1280  CG1 VAL A 167      53.678 -13.167 -19.706  1.00 18.68           C  
ANISOU 1280  CG1 VAL A 167     2952   2168   1979   1419     28     57       C  
ATOM   1281  CG2 VAL A 167      51.313 -13.411 -18.870  1.00 19.40           C  
ANISOU 1281  CG2 VAL A 167     3028   2264   2079   1413      0     42       C  
ATOM   1282  N   GLY A 168      50.288  -9.981 -18.546  1.00 28.34           N  
ANISOU 1282  N   GLY A 168     4137   3373   3259   1412     -6     33       N  
ATOM   1283  CA  GLY A 168      48.923  -9.515 -18.444  1.00 22.37           C  
ANISOU 1283  CA  GLY A 168     3376   2613   2511   1411    -21     27       C  
ATOM   1284  C   GLY A 168      47.996 -10.622 -18.018  1.00 26.18           C  
ANISOU 1284  C   GLY A 168     3856   3106   2986   1407    -33     21       C  
ATOM   1285  O   GLY A 168      48.435 -11.736 -17.815  1.00 34.64           O  
ANISOU 1285  O   GLY A 168     4930   4188   4045   1406    -30     23       O  
ATOM   1286  N   ASN A 169      46.711 -10.319 -17.892  1.00 25.03           N  
ANISOU 1286  N   ASN A 169     3706   2958   2847   1405    -47     15       N  
ATOM   1287  CA  ASN A 169      45.740 -11.302 -17.465  1.00 17.79           C  
ANISOU 1287  CA  ASN A 169     2786   2051   1924   1402    -60      9       C  
ATOM   1288  C   ASN A 169      44.999 -11.925 -18.630  1.00 24.88           C  
ANISOU 1288  C   ASN A 169     3706   2943   2805   1407    -69     13       C  
ATOM   1289  O   ASN A 169      44.638 -11.252 -19.592  1.00 32.25           O  
ANISOU 1289  O   ASN A 169     4652   3864   3738   1412    -72     17       O  
ATOM   1290  CB  ASN A 169      44.749 -10.675 -16.502  1.00 17.76           C  
ANISOU 1290  CB  ASN A 169     2761   2048   1938   1396    -70      0       C  
ATOM   1291  CG  ASN A 169      44.055 -11.691 -15.639  1.00 18.85           C  
ANISOU 1291  CG  ASN A 169     2890   2200   2073   1390    -79     -7       C  
ATOM   1292  ND2 ASN A 169      44.285 -11.607 -14.350  1.00 21.81           N  
ANISOU 1292  ND2 ASN A 169     3243   2584   2460   1384    -76    -14       N  
ATOM   1293  OD1 ASN A 169      43.310 -12.535 -16.123  1.00 23.74           O  
ANISOU 1293  OD1 ASN A 169     3520   2820   2679   1392    -88     -7       O  
ATOM   1294  N   THR A 170      44.772 -13.227 -18.536  1.00 21.71           N  
ANISOU 1294  N   THR A 170     3666   2689   1895   1552    213    158       N  
ATOM   1295  CA  THR A 170      44.104 -13.959 -19.598  1.00 20.05           C  
ANISOU 1295  CA  THR A 170     3432   2476   1708   1553    196    152       C  
ATOM   1296  C   THR A 170      42.605 -13.768 -19.506  1.00 23.53           C  
ANISOU 1296  C   THR A 170     3849   2897   2195   1557    208    162       C  
ATOM   1297  O   THR A 170      41.876 -14.248 -20.372  1.00 22.02           O  
ANISOU 1297  O   THR A 170     3637   2701   2029   1559    196    160       O  
ATOM   1298  CB  THR A 170      44.435 -15.464 -19.557  1.00 20.59           C  
ANISOU 1298  CB  THR A 170     3502   2552   1769   1550    181    143       C  
ATOM   1299  CG2 THR A 170      45.915 -15.671 -19.359  1.00 18.71           C  
ANISOU 1299  CG2 THR A 170     3290   2333   1485   1545    173    134       C  
ATOM   1300  OG1 THR A 170      43.714 -16.099 -18.496  1.00 31.41           O  
ANISOU 1300  OG1 THR A 170     4866   3907   3160   1549    194    151       O  
ATOM   1301  N   ILE A 171      42.141 -13.075 -18.464  1.00 18.49           N  
ANISOU 1301  N   ILE A 171     3213   2245   1568   1558    231    174       N  
ATOM   1302  CA  ILE A 171      40.719 -12.749 -18.357  1.00 18.72           C  
ANISOU 1302  CA  ILE A 171     3219   2253   1639   1562    244    184       C  
ATOM   1303  C   ILE A 171      40.295 -11.804 -19.479  1.00 42.86           C  
ANISOU 1303  C   ILE A 171     6264   5310   4711   1566    239    185       C  
ATOM   1304  O   ILE A 171      39.132 -11.807 -19.878  1.00 38.65           O  
ANISOU 1304  O   ILE A 171     5708   4764   4215   1569    240    189       O  
ATOM   1305  CB  ILE A 171      40.327 -12.146 -16.973  1.00 24.07           C  
ANISOU 1305  CB  ILE A 171     3904   2917   2324   1562    271    195       C  
ATOM   1306  CG1 ILE A 171      38.814 -12.165 -16.774  1.00 19.04           C  
ANISOU 1306  CG1 ILE A 171     3243   2259   1733   1566    282    204       C  
ATOM   1307  CG2 ILE A 171      40.878 -10.751 -16.824  1.00 18.77           C  
ANISOU 1307  CG2 ILE A 171     3249   2250   1634   1563    283    199       C  
ATOM   1308  CD1 ILE A 171      38.209 -13.513 -16.900  1.00 19.09           C  
ANISOU 1308  CD1 ILE A 171     3232   2260   1760   1565    271    201       C  
ATOM   1309  N   VAL A 172      41.241 -11.023 -20.005  1.00 18.68           N  
ANISOU 1309  N   VAL A 172     3216   2262   1619   1566    234    180       N  
ATOM   1310  CA  VAL A 172      40.941 -10.146 -21.121  1.00 23.59           C  
ANISOU 1310  CA  VAL A 172     3826   2884   2252   1569    229    180       C  
ATOM   1311  C   VAL A 172      40.685 -10.957 -22.387  1.00 21.62           C  
ANISOU 1311  C   VAL A 172     3560   2640   2015   1570    205    172       C  
ATOM   1312  O   VAL A 172      39.602 -10.841 -22.985  1.00 25.40           O  
ANISOU 1312  O   VAL A 172     4015   3107   2528   1573    204    176       O  
ATOM   1313  CB  VAL A 172      42.046  -9.104 -21.394  1.00 29.98           C  
ANISOU 1313  CB  VAL A 172     4656   3708   3027   1569    229    177       C  
ATOM   1314  CG1 VAL A 172      41.609  -8.192 -22.525  1.00 27.65           C  
ANISOU 1314  CG1 VAL A 172     4347   3412   2747   1573    224    178       C  
ATOM   1315  CG2 VAL A 172      42.350  -8.272 -20.155  1.00 24.52           C  
ANISOU 1315  CG2 VAL A 172     3982   3012   2322   1568    251    186       C  
ATOM   1316  N   ASP A 173      41.685 -11.759 -22.782  1.00 20.91           N  
ANISOU 1316  N   ASP A 173     3482   2567   1896   1566    187    160       N  
ATOM   1317  CA  ASP A 173      41.572 -12.715 -23.879  1.00 18.55           C  
ANISOU 1317  CA  ASP A 173     3170   2274   1605   1566    164    151       C  
ATOM   1318  C   ASP A 173      40.246 -13.423 -23.713  1.00 18.73           C  
ANISOU 1318  C   ASP A 173     3169   2279   1670   1568    166    157       C  
ATOM   1319  O   ASP A 173      39.432 -13.445 -24.617  1.00 18.85           O  
ANISOU 1319  O   ASP A 173     3162   2288   1712   1570    157    158       O  
ATOM   1320  CB  ASP A 173      42.625 -13.836 -23.818  1.00 36.21           C  
ANISOU 1320  CB  ASP A 173     5421   4526   3811   1561    149    139       C  
ATOM   1321  CG  ASP A 173      44.079 -13.354 -23.766  1.00 40.84           C  
ANISOU 1321  CG  ASP A 173     6035   5132   4351   1559    147    131       C  
ATOM   1322  OD1 ASP A 173      44.401 -12.373 -23.072  1.00 44.14           O  
ANISOU 1322  OD1 ASP A 173     6466   5548   4756   1559    163    138       O  
ATOM   1323  OD2 ASP A 173      44.933 -14.026 -24.392  1.00 48.08           O1-
ANISOU 1323  OD2 ASP A 173     6960   6065   5244   1556    128    118       O1-
ATOM   1324  N   ALA A 174      40.051 -14.026 -22.543  1.00 20.19           N  
ANISOU 1324  N   ALA A 174     3358   2456   1859   1566    177    161       N  
ATOM   1325  CA  ALA A 174      38.906 -14.897 -22.275  1.00 22.59           C  
ANISOU 1325  CA  ALA A 174     3641   2744   2199   1567    178    166       C  
ATOM   1326  C   ALA A 174      37.586 -14.183 -22.472  1.00 24.42           C  
ANISOU 1326  C   ALA A 174     3850   2957   2470   1571    189    177       C  
ATOM   1327  O   ALA A 174      36.681 -14.717 -23.089  1.00 31.34           O  
ANISOU 1327  O   ALA A 174     4704   3826   3377   1573    179    178       O  
ATOM   1328  CB  ALA A 174      38.980 -15.449 -20.859  1.00 18.88           C  
ANISOU 1328  CB  ALA A 174     3181   2268   1724   1564    193    170       C  
ATOM   1329  N   THR A 175      37.477 -12.978 -21.925  1.00 21.89           N  
ANISOU 1329  N   THR A 175     3536   2631   2150   1573    209    185       N  
ATOM   1330  CA  THR A 175      36.220 -12.258 -21.965  1.00 22.62           C  
ANISOU 1330  CA  THR A 175     3608   2705   2280   1578    221    195       C  
ATOM   1331  C   THR A 175      35.889 -11.844 -23.398  1.00 29.01           C  
ANISOU 1331  C   THR A 175     4402   3517   3102   1581    206    193       C  
ATOM   1332  O   THR A 175      34.754 -11.989 -23.847  1.00 34.41           O  
ANISOU 1332  O   THR A 175     5062   4188   3823   1584    203    198       O  
ATOM   1333  CB  THR A 175      36.211 -11.087 -20.967  1.00 22.19           C  
ANISOU 1333  CB  THR A 175     3566   2644   2221   1579    246    204       C  
ATOM   1334  CG2 THR A 175      35.045 -10.153 -21.231  1.00 19.63           C  
ANISOU 1334  CG2 THR A 175     3223   2305   1932   1584    257    213       C  
ATOM   1335  OG1 THR A 175      36.074 -11.622 -19.642  1.00 34.83           O  
ANISOU 1335  OG1 THR A 175     5174   4237   3824   1577    261    208       O  
ATOM   1336  N   LEU A 176      36.902 -11.382 -24.121  1.00 19.30           N  
ANISOU 1336  N   LEU A 176     3185   2304   1842   1580    195    186       N  
ATOM   1337  CA  LEU A 176      36.755 -11.071 -25.536  1.00 19.32           C  
ANISOU 1337  CA  LEU A 176     3176   2312   1853   1582    179    182       C  
ATOM   1338  C   LEU A 176      36.317 -12.271 -26.412  1.00 26.93           C  
ANISOU 1338  C   LEU A 176     4122   3277   2835   1582    157    177       C  
ATOM   1339  O   LEU A 176      35.259 -12.225 -27.077  1.00 34.99           O  
ANISOU 1339  O   LEU A 176     5119   4286   3890   1585    153    181       O  
ATOM   1340  CB  LEU A 176      38.036 -10.402 -26.059  1.00 19.15           C  
ANISOU 1340  CB  LEU A 176     3174   2309   1792   1581    173    174       C  
ATOM   1341  CG  LEU A 176      38.119  -8.867 -25.944  1.00 19.67           C  
ANISOU 1341  CG  LEU A 176     3247   2373   1853   1584    188    181       C  
ATOM   1342  CD1 LEU A 176      36.904  -8.224 -25.245  1.00 19.39           C  
ANISOU 1342  CD1 LEU A 176     3198   2317   1852   1587    210    194       C  
ATOM   1343  CD2 LEU A 176      39.374  -8.456 -25.268  1.00 19.01           C  
ANISOU 1343  CD2 LEU A 176     3191   2302   1728   1581    196    177       C  
ATOM   1344  N   GLN A 177      37.124 -13.332 -26.396  1.00 24.91           N  
ANISOU 1344  N   GLN A 177     3876   3032   2555   1578    144    167       N  
ATOM   1345  CA  GLN A 177      36.813 -14.583 -27.083  1.00 19.21           C  
ANISOU 1345  CA  GLN A 177     3140   2312   1847   1576    124    161       C  
ATOM   1346  C   GLN A 177      35.442 -15.144 -26.719  1.00 31.52           C  
ANISOU 1346  C   GLN A 177     4677   3851   3449   1578    129    170       C  
ATOM   1347  O   GLN A 177      34.638 -15.415 -27.595  1.00 36.09           O  
ANISOU 1347  O   GLN A 177     5234   4423   4056   1580    117    171       O  
ATOM   1348  CB  GLN A 177      37.881 -15.628 -26.800  1.00 19.02           C  
ANISOU 1348  CB  GLN A 177     3134   2302   1791   1571    113    150       C  
ATOM   1349  CG  GLN A 177      39.295 -15.154 -27.050  1.00 18.82           C  
ANISOU 1349  CG  GLN A 177     3133   2297   1722   1569    108    140       C  
ATOM   1350  CD  GLN A 177      40.348 -16.212 -26.703  1.00 30.38           C  
ANISOU 1350  CD  GLN A 177     4614   3775   3154   1564     99    129       C  
ATOM   1351  NE2 GLN A 177      41.611 -15.918 -27.002  1.00 26.13           N  
ANISOU 1351  NE2 GLN A 177     4097   3255   2577   1562     92    119       N  
ATOM   1352  OE1 GLN A 177      40.022 -17.278 -26.173  1.00 28.01           O  
ANISOU 1352  OE1 GLN A 177     4309   3468   2864   1563     97    130       O  
ATOM   1353  N   ASN A 178      35.169 -15.325 -25.436  1.00 19.44           N  
ANISOU 1353  N   ASN A 178     3151   2311   1925   1577    147    176       N  
ATOM   1354  CA  ASN A 178      33.885 -15.861 -25.022  1.00 27.64           C  
ANISOU 1354  CA  ASN A 178     4169   3330   3003   1579    153    185       C  
ATOM   1355  C   ASN A 178      32.716 -14.977 -25.433  1.00 29.30           C  
ANISOU 1355  C   ASN A 178     4358   3526   3249   1584    160    194       C  
ATOM   1356  O   ASN A 178      31.616 -15.480 -25.646  1.00 31.05           O  
ANISOU 1356  O   ASN A 178     4557   3734   3506   1586    156    199       O  
ATOM   1357  CB  ASN A 178      33.844 -16.108 -23.511  1.00 27.23           C  
ANISOU 1357  CB  ASN A 178     4127   3271   2949   1577    172    189       C  
ATOM   1358  CG  ASN A 178      34.812 -17.174 -23.074  1.00 32.31           C  
ANISOU 1358  CG  ASN A 178     4787   3926   3563   1573    164    181       C  
ATOM   1359  ND2 ASN A 178      35.004 -17.314 -21.763  1.00 32.46           N  
ANISOU 1359  ND2 ASN A 178     4820   3942   3574   1571    181    184       N  
ATOM   1360  OD1 ASN A 178      35.386 -17.869 -23.909  1.00 34.96           O  
ANISOU 1360  OD1 ASN A 178     5124   4274   3885   1570    143    171       O  
ATOM   1361  N   LEU A 179      32.944 -13.666 -25.523  1.00 29.76           N  
ANISOU 1361  N   LEU A 179     4424   3586   3298   1586    170    197       N  
ATOM   1362  CA  LEU A 179      31.907 -12.763 -26.022  1.00 36.28           C  
ANISOU 1362  CA  LEU A 179     5231   4399   4155   1591    176    206       C  
ATOM   1363  C   LEU A 179      31.592 -13.105 -27.476  1.00 38.29           C  
ANISOU 1363  C   LEU A 179     5467   4657   4424   1592    153    202       C  
ATOM   1364  O   LEU A 179      30.418 -13.271 -27.846  1.00 37.12           O  
ANISOU 1364  O   LEU A 179     5295   4495   4314   1595    150    208       O  
ATOM   1365  CB  LEU A 179      32.330 -11.285 -25.931  1.00 37.08           C  
ANISOU 1365  CB  LEU A 179     5345   4504   4241   1593    190    209       C  
ATOM   1366  CG  LEU A 179      31.475 -10.339 -26.796  1.00 37.65           C  
ANISOU 1366  CG  LEU A 179     5398   4567   4339   1598    190    215       C  
ATOM   1367  CD1 LEU A 179      30.040 -10.272 -26.275  1.00 31.93           C  
ANISOU 1367  CD1 LEU A 179     4653   3820   3657   1601    204    226       C  
ATOM   1368  CD2 LEU A 179      32.095  -8.950 -26.953  1.00 40.74           C  
ANISOU 1368  CD2 LEU A 179     5803   4966   4710   1599    199    216       C  
ATOM   1369  N   LYS A 180      32.645 -13.190 -28.295  1.00 32.79           N  
ANISOU 1369  N   LYS A 180     4783   3980   3698   1590    136    192       N  
ATOM   1370  CA  LYS A 180      32.473 -13.543 -29.706  1.00 29.46           C  
ANISOU 1370  CA  LYS A 180     4346   3563   3285   1590    113    187       C  
ATOM   1371  C   LYS A 180      31.712 -14.868 -29.820  1.00 32.99           C  
ANISOU 1371  C   LYS A 180     4775   4001   3759   1589    101    187       C  
ATOM   1372  O   LYS A 180      30.786 -14.994 -30.622  1.00 38.02           O  
ANISOU 1372  O   LYS A 180     5389   4630   4427   1592     92    191       O  
ATOM   1373  CB  LYS A 180      33.818 -13.582 -30.431  1.00 19.70           C  
ANISOU 1373  CB  LYS A 180     3128   2348   2009   1588     98    174       C  
ATOM   1374  CG  LYS A 180      33.760 -13.335 -31.912  1.00 85.68           C  
ANISOU 1374  CG  LYS A 180    11473  10711  10370   1589     80    170       C  
ATOM   1375  CD  LYS A 180      35.106 -12.826 -32.414  1.00 85.67           C  
ANISOU 1375  CD  LYS A 180    11493  10730  10327   1588     73    160       C  
ATOM   1376  CE  LYS A 180      35.151 -12.830 -33.939  1.00 84.33           C  
ANISOU 1376  CE  LYS A 180    11313  10568  10159   1589     52    154       C  
ATOM   1377  NZ  LYS A 180      35.094 -14.210 -34.524  1.00 81.65           N1+
ANISOU 1377  NZ  LYS A 180    10965  10233   9826   1586     31    147       N1+
ATOM   1378  N   ILE A 181      32.066 -15.831 -28.975  1.00 33.75           N  
ANISOU 1378  N   ILE A 181     4881   4099   3844   1586    103    184       N  
ATOM   1379  CA  ILE A 181      31.380 -17.121 -28.951  1.00 35.54           C  
ANISOU 1379  CA  ILE A 181     5091   4317   4094   1585     93    184       C  
ATOM   1380  C   ILE A 181      29.901 -16.985 -28.563  1.00 39.13           C  
ANISOU 1380  C   ILE A 181     5524   4750   4594   1588    105    197       C  
ATOM   1381  O   ILE A 181      29.046 -17.642 -29.143  1.00 42.27           O  
ANISOU 1381  O   ILE A 181     5900   5139   5021   1589     93    199       O  
ATOM   1382  CB  ILE A 181      32.144 -18.153 -28.046  1.00 44.40           C  
ANISOU 1382  CB  ILE A 181     6230   5446   5193   1580     94    178       C  
ATOM   1383  CG1 ILE A 181      33.507 -18.471 -28.663  1.00 36.98           C  
ANISOU 1383  CG1 ILE A 181     5310   4530   4213   1576     77    164       C  
ATOM   1384  CG2 ILE A 181      31.366 -19.459 -27.864  1.00 19.92           C  
ANISOU 1384  CG2 ILE A 181     3114   2336   2119   1579     86    180       C  
ATOM   1385  CD1 ILE A 181      34.470 -19.084 -27.717  1.00 31.35           C  
ANISOU 1385  CD1 ILE A 181     4618   3825   3468   1572     81    158       C  
ATOM   1386  N   ALA A 182      29.602 -16.117 -27.599  1.00 47.18           N  
ANISOU 1386  N   ALA A 182     6548   5759   5618   1590    129    205       N  
ATOM   1387  CA  ALA A 182      28.222 -15.892 -27.141  1.00 42.09           C  
ANISOU 1387  CA  ALA A 182     5884   5094   5015   1594    142    216       C  
ATOM   1388  C   ALA A 182      27.380 -15.229 -28.227  1.00 42.82           C  
ANISOU 1388  C   ALA A 182     5955   5179   5135   1598    135    221       C  
ATOM   1389  O   ALA A 182      26.157 -15.377 -28.285  1.00 39.96           O  
ANISOU 1389  O   ALA A 182     5571   4801   4811   1600    137    229       O  
ATOM   1390  CB  ALA A 182      28.207 -15.036 -25.863  1.00 25.07           C  
ANISOU 1390  CB  ALA A 182     3740   2930   2854   1595    169    223       C  
ATOM   1391  N   GLU A 183      28.049 -14.478 -29.085  1.00 43.77           N  
ANISOU 1391  N   GLU A 183     6083   5312   5236   1598    128    217       N  
ATOM   1392  CA  GLU A 183      27.341 -13.778 -30.135  1.00 53.39           C  
ANISOU 1392  CA  GLU A 183     7284   6526   6478   1602    122    221       C  
ATOM   1393  C   GLU A 183      26.824 -14.768 -31.179  1.00 60.27           C  
ANISOU 1393  C   GLU A 183     8134   7395   7369   1602     98    219       C  
ATOM   1394  O   GLU A 183      25.727 -14.599 -31.708  1.00 70.24           O  
ANISOU 1394  O   GLU A 183     9375   8646   8667   1605     95    226       O  
ATOM   1395  CB  GLU A 183      28.232 -12.686 -30.762  1.00 51.15           C  
ANISOU 1395  CB  GLU A 183     7014   6256   6166   1603    120    217       C  
ATOM   1396  CG  GLU A 183      28.234 -11.369 -29.982  1.00 44.86           C  
ANISOU 1396  CG  GLU A 183     6228   5454   5364   1605    145    224       C  
ATOM   1397  CD  GLU A 183      29.242 -10.380 -30.510  1.00 45.83           C  
ANISOU 1397  CD  GLU A 183     6367   5592   5455   1605    143    219       C  
ATOM   1398  OE1 GLU A 183      30.242 -10.841 -31.121  1.00 39.74           O  
ANISOU 1398  OE1 GLU A 183     5607   4838   4655   1602    127    208       O  
ATOM   1399  OE2 GLU A 183      29.030  -9.154 -30.318  1.00 43.98           O1-
ANISOU 1399  OE2 GLU A 183     6134   5353   5225   1609    159    225       O1-
ATOM   1400  N   LYS A 184      27.607 -15.805 -31.463  1.00 53.14           N  
ANISOU 1400  N   LYS A 184     7240   6506   6446   1597     82    209       N  
ATOM   1401  CA  LYS A 184      27.246 -16.762 -32.509  1.00 41.18           C  
ANISOU 1401  CA  LYS A 184     5708   4992   4946   1596     58    206       C  
ATOM   1402  C   LYS A 184      26.350 -17.882 -31.986  1.00 33.00           C  
ANISOU 1402  C   LYS A 184     4657   3943   3940   1596     57    211       C  
ATOM   1403  O   LYS A 184      26.223 -18.920 -32.623  1.00 40.03           O  
ANISOU 1403  O   LYS A 184     5536   4834   4838   1594     38    207       O  
ATOM   1404  CB  LYS A 184      28.498 -17.377 -33.167  1.00 38.20           C  
ANISOU 1404  CB  LYS A 184     5346   4635   4532   1592     39    193       C  
ATOM   1405  CG  LYS A 184      29.677 -16.423 -33.393  1.00 35.56           C  
ANISOU 1405  CG  LYS A 184     5034   4318   4160   1592     42    186       C  
ATOM   1406  CD  LYS A 184      30.888 -17.129 -34.050  1.00 34.31           C  
ANISOU 1406  CD  LYS A 184     4890   4180   3966   1588     22    172       C  
ATOM   1407  CE  LYS A 184      31.309 -18.441 -33.332  1.00 67.73           C  
ANISOU 1407  CE  LYS A 184     9131   8416   8186   1584     19    166       C  
ATOM   1408  NZ  LYS A 184      32.311 -18.281 -32.221  1.00 62.55           N1+
ANISOU 1408  NZ  LYS A 184     8502   7769   7497   1581     33    162       N1+
ATOM   1409  N   ASN A 185      25.735 -17.681 -30.830  1.00 33.96           N  
ANISOU 1409  N   ASN A 185     4776   4049   4077   1597     78    219       N  
ATOM   1410  CA  ASN A 185      24.948 -18.743 -30.203  1.00 46.98           C  
ANISOU 1410  CA  ASN A 185     6413   5685   5752   1596     79    222       C  
ATOM   1411  C   ASN A 185      23.453 -18.407 -30.233  1.00 65.55           C  
ANISOU 1411  C   ASN A 185     8740   8017   8150   1601     85    234       C  
ATOM   1412  O   ASN A 185      22.940 -17.728 -29.346  1.00 68.15           O  
ANISOU 1412  O   ASN A 185     9069   8334   8491   1603    106    241       O  
ATOM   1413  CB  ASN A 185      25.466 -19.017 -28.777  1.00 42.87           C  
ANISOU 1413  CB  ASN A 185     5911   5165   5212   1594     95    221       C  
ATOM   1414  CG  ASN A 185      24.713 -20.145 -28.055  1.00 45.66           C  
ANISOU 1414  CG  ASN A 185     6254   5506   5590   1593     97    225       C  
ATOM   1415  ND2 ASN A 185      25.444 -20.957 -27.289  1.00 35.89           N  
ANISOU 1415  ND2 ASN A 185     5031   4275   4329   1589     98    219       N  
ATOM   1416  OD1 ASN A 185      23.499 -20.262 -28.158  1.00 54.55           O  
ANISOU 1416  OD1 ASN A 185     7356   6615   6754   1595     98    233       O  
ATOM   1417  N   GLU A 186      22.762 -18.906 -31.256  1.00 78.34           N  
ANISOU 1417  N   GLU A 186    10338   9632   9795   1601     67    235       N  
ATOM   1418  CA  GLU A 186      21.359 -18.570 -31.488  1.00 88.93           C  
ANISOU 1418  CA  GLU A 186    11655  10955  11181   1606     70    245       C  
ATOM   1419  C   GLU A 186      20.436 -18.956 -30.333  1.00 88.70           C  
ANISOU 1419  C   GLU A 186    11616  10907  11177   1607     85    252       C  
ATOM   1420  O   GLU A 186      19.364 -18.375 -30.173  1.00 95.35           O  
ANISOU 1420  O   GLU A 186    12443  11734  12051   1611     95    261       O  
ATOM   1421  CB  GLU A 186      20.865 -19.179 -32.808  1.00 97.59           C  
ANISOU 1421  CB  GLU A 186    12731  12052  12298   1605     45    245       C  
ATOM   1422  CG  GLU A 186      21.163 -18.326 -34.054  1.00103.42           C  
ANISOU 1422  CG  GLU A 186    13468  12800  13028   1607     35    243       C  
ATOM   1423  CD  GLU A 186      20.064 -17.310 -34.371  1.00107.15           C  
ANISOU 1423  CD  GLU A 186    13922  13257  13532   1612     42    253       C  
ATOM   1424  OE1 GLU A 186      19.687 -17.188 -35.560  1.00110.67           O  
ANISOU 1424  OE1 GLU A 186    14352  13703  13993   1614     26    254       O  
ATOM   1425  OE2 GLU A 186      19.580 -16.631 -33.439  1.00105.45           O1-
ANISOU 1425  OE2 GLU A 186    13707  13031  13328   1615     63    259       O1-
ATOM   1426  N   ASN A 187      20.852 -19.927 -29.532  1.00 82.29           N  
ANISOU 1426  N   ASN A 187    10815  10098  10353   1603     87    249       N  
ATOM   1427  CA  ASN A 187      20.093 -20.320 -28.352  1.00 82.24           C  
ANISOU 1427  CA  ASN A 187    10803  10077  10368   1604    102    255       C  
ATOM   1428  C   ASN A 187      20.093 -19.208 -27.300  1.00 83.70           C  
ANISOU 1428  C   ASN A 187    11000  10256  10546   1606    129    259       C  
ATOM   1429  O   ASN A 187      19.107 -19.015 -26.581  1.00 82.20           O  
ANISOU 1429  O   ASN A 187    10800  10050  10384   1609    144    267       O  
ATOM   1430  CB  ASN A 187      20.661 -21.627 -27.782  1.00 82.90           C  
ANISOU 1430  CB  ASN A 187    10896  10166  10437   1599     96    249       C  
ATOM   1431  CG  ASN A 187      19.983 -22.059 -26.500  1.00 81.52           C  
ANISOU 1431  CG  ASN A 187    10718   9976  10280   1599    113    254       C  
ATOM   1432  ND2 ASN A 187      20.746 -22.698 -25.620  1.00 77.46           N  
ANISOU 1432  ND2 ASN A 187    10221   9469   9741   1596    118    249       N  
ATOM   1433  OD1 ASN A 187      18.791 -21.827 -26.300  1.00 85.81           O  
ANISOU 1433  OD1 ASN A 187    11242  10502  10858   1603    121    262       O  
ATOM   1434  N   VAL A 188      21.200 -18.466 -27.230  1.00 84.38           N  
ANISOU 1434  N   VAL A 188    11108  10357  10596   1605    135    254       N  
ATOM   1435  CA  VAL A 188      21.341 -17.377 -26.263  1.00 79.27           C  
ANISOU 1435  CA  VAL A 188    10475   9706   9938   1607    160    258       C  
ATOM   1436  C   VAL A 188      21.052 -16.017 -26.882  1.00 72.59           C  
ANISOU 1436  C   VAL A 188     9624   8858   9099   1611    165    262       C  
ATOM   1437  O   VAL A 188      20.697 -15.082 -26.180  1.00 69.27           O  
ANISOU 1437  O   VAL A 188     9207   8429   8685   1614    186    268       O  
ATOM   1438  CB  VAL A 188      22.743 -17.344 -25.599  1.00 80.89           C  
ANISOU 1438  CB  VAL A 188    10710   9927  10098   1603    167    251       C  
ATOM   1439  CG1 VAL A 188      23.237 -18.757 -25.318  1.00 81.02           C  
ANISOU 1439  CG1 VAL A 188    10732   9950  10102   1598    156    244       C  
ATOM   1440  CG2 VAL A 188      23.742 -16.565 -26.452  1.00 77.49           C  
ANISOU 1440  CG2 VAL A 188    10292   9513   9637   1603    159    245       C  
ATOM   1441  N   ARG A 189      21.219 -15.911 -28.196  1.00 73.91           N  
ANISOU 1441  N   ARG A 189     9783   9033   9264   1611    146    259       N  
ATOM   1442  CA  ARG A 189      20.829 -14.712 -28.920  1.00 75.10           C  
ANISOU 1442  CA  ARG A 189     9926   9181   9426   1615    148    264       C  
ATOM   1443  C   ARG A 189      19.298 -14.658 -28.892  1.00 78.54           C  
ANISOU 1443  C   ARG A 189    10337   9597   9909   1619    152    273       C  
ATOM   1444  O   ARG A 189      18.691 -13.578 -28.859  1.00 78.67           O  
ANISOU 1444  O   ARG A 189    10346   9603   9941   1623    165    280       O  
ATOM   1445  CB  ARG A 189      21.381 -14.756 -30.351  1.00 73.72           C  
ANISOU 1445  CB  ARG A 189     9750   9021   9240   1614    125    258       C  
ATOM   1446  CG  ARG A 189      21.456 -13.400 -31.047  1.00 77.09           C  
ANISOU 1446  CG  ARG A 189    10177   9451   9663   1618    127    260       C  
ATOM   1447  CD  ARG A 189      22.591 -13.339 -32.079  1.00 81.37           C  
ANISOU 1447  CD  ARG A 189    10730  10012  10172   1615    110    251       C  
ATOM   1448  NE  ARG A 189      22.386 -14.242 -33.212  1.00 89.33           N  
ANISOU 1448  NE  ARG A 189    11724  11024  11192   1614     85    247       N  
ATOM   1449  CZ  ARG A 189      23.081 -14.199 -34.349  1.00 93.75           C  
ANISOU 1449  CZ  ARG A 189    12288  11599  11734   1613     67    240       C  
ATOM   1450  NH1 ARG A 189      24.032 -13.290 -34.522  1.00 95.07           N1+
ANISOU 1450  NH1 ARG A 189    12473  11780  11870   1613     71    236       N1+
ATOM   1451  NH2 ARG A 189      22.821 -15.064 -35.321  1.00 93.10           N  
ANISOU 1451  NH2 ARG A 189    12191  11519  11664   1612     45    238       N  
ATOM   1452  N   ALA A 190      18.692 -15.844 -28.881  1.00 80.34           N  
ANISOU 1452  N   ALA A 190    10549   9816  10158   1618    142    274       N  
ATOM   1453  CA  ALA A 190      17.264 -15.995 -28.640  1.00 78.59           C  
ANISOU 1453  CA  ALA A 190    10305   9575   9980   1621    147    282       C  
ATOM   1454  C   ALA A 190      16.910 -15.277 -27.365  1.00 81.91           C  
ANISOU 1454  C   ALA A 190    10733   9985  10405   1624    174    288       C  
ATOM   1455  O   ALA A 190      16.101 -14.356 -27.372  1.00 90.98           O  
ANISOU 1455  O   ALA A 190    11871  11122  11574   1628    185    294       O  
ATOM   1456  CB  ALA A 190      16.892 -17.461 -28.515  1.00 77.77           C  
ANISOU 1456  CB  ALA A 190    10190   9466   9891   1619    134    281       C  
ATOM   1457  N   PHE A 191      17.530 -15.694 -26.269  1.00 79.54           N  
ANISOU 1457  N   PHE A 191    10450   9688  10083   1621    186    285       N  
ATOM   1458  CA  PHE A 191      17.244 -15.100 -24.971  1.00 76.39           C  
ANISOU 1458  CA  PHE A 191    10060   9280   9686   1622    213    290       C  
ATOM   1459  C   PHE A 191      17.527 -13.596 -24.922  1.00 71.95           C  
ANISOU 1459  C   PHE A 191     9507   8719   9110   1625    229    292       C  
ATOM   1460  O   PHE A 191      16.703 -12.825 -24.437  1.00 74.78           O  
ANISOU 1460  O   PHE A 191     9859   9065   9488   1629    246    299       O  
ATOM   1461  CB  PHE A 191      18.012 -15.807 -23.858  1.00 75.81           C  
ANISOU 1461  CB  PHE A 191    10005   9211   9587   1618    222    285       C  
ATOM   1462  CG  PHE A 191      17.889 -15.124 -22.537  1.00 72.46           C  
ANISOU 1462  CG  PHE A 191     9593   8780   9159   1620    250    290       C  
ATOM   1463  CD1 PHE A 191      16.695 -15.162 -21.842  1.00 72.01           C  
ANISOU 1463  CD1 PHE A 191     9522   8705   9135   1622    263    297       C  
ATOM   1464  CD2 PHE A 191      18.953 -14.421 -22.004  1.00 70.46           C  
ANISOU 1464  CD2 PHE A 191     9364   8537   8869   1618    263    287       C  
ATOM   1465  CE1 PHE A 191      16.563 -14.526 -20.629  1.00 71.25           C  
ANISOU 1465  CE1 PHE A 191     9436   8600   9035   1624    290    301       C  
ATOM   1466  CE2 PHE A 191      18.830 -13.784 -20.798  1.00 71.17           C  
ANISOU 1466  CE2 PHE A 191     9465   8619   8956   1619    289    292       C  
ATOM   1467  CZ  PHE A 191      17.628 -13.835 -20.107  1.00 72.21           C  
ANISOU 1467  CZ  PHE A 191     9583   8734   9121   1622    303    299       C  
ATOM   1468  N   PHE A 192      18.690 -13.185 -25.417  1.00 65.11           N  
ANISOU 1468  N   PHE A 192     8659   7871   8210   1623    222    286       N  
ATOM   1469  CA  PHE A 192      19.066 -11.778 -25.403  1.00 64.70           C  
ANISOU 1469  CA  PHE A 192     8618   7822   8142   1625    236    288       C  
ATOM   1470  C   PHE A 192      17.994 -10.946 -26.067  1.00 72.50           C  
ANISOU 1470  C   PHE A 192     9586   8799   9163   1630    237    295       C  
ATOM   1471  O   PHE A 192      17.480 -10.002 -25.469  1.00 77.88           O  
ANISOU 1471  O   PHE A 192    10267   9469   9854   1634    257    301       O  
ATOM   1472  CB  PHE A 192      20.404 -11.544 -26.105  1.00 62.87           C  
ANISOU 1472  CB  PHE A 192     8404   7611   7873   1622    224    280       C  
ATOM   1473  CG  PHE A 192      20.792 -10.088 -26.209  1.00 62.67           C  
ANISOU 1473  CG  PHE A 192     8390   7591   7833   1625    236    281       C  
ATOM   1474  CD1 PHE A 192      21.289  -9.408 -25.111  1.00 62.15           C  
ANISOU 1474  CD1 PHE A 192     8344   7525   7745   1624    259    283       C  
ATOM   1475  CD2 PHE A 192      20.667  -9.403 -27.409  1.00 59.73           C  
ANISOU 1475  CD2 PHE A 192     8008   7221   7466   1627    225    282       C  
ATOM   1476  CE1 PHE A 192      21.654  -8.075 -25.208  1.00 60.00           C  
ANISOU 1476  CE1 PHE A 192     8081   7256   7460   1626    270    284       C  
ATOM   1477  CE2 PHE A 192      21.028  -8.072 -27.507  1.00 53.33           C  
ANISOU 1477  CE2 PHE A 192     7207   6414   6642   1629    236    284       C  
ATOM   1478  CZ  PHE A 192      21.524  -7.410 -26.409  1.00 53.66           C  
ANISOU 1478  CZ  PHE A 192     7268   6456   6663   1629    258    285       C  
ATOM   1479  N   ASN A 193      17.641 -11.307 -27.298  1.00 73.85           N  
ANISOU 1479  N   ASN A 193     9739   8971   9350   1631    214    294       N  
ATOM   1480  CA  ASN A 193      16.615 -10.561 -28.017  1.00 73.47           C  
ANISOU 1480  CA  ASN A 193     9671   8912   9334   1636    213    300       C  
ATOM   1481  C   ASN A 193      15.236 -10.600 -27.342  1.00 72.01           C  
ANISOU 1481  C   ASN A 193     9468   8706   9186   1639    226    308       C  
ATOM   1482  O   ASN A 193      14.392  -9.737 -27.593  1.00 75.22           O  
ANISOU 1482  O   ASN A 193     9862   9101   9615   1644    232    314       O  
ATOM   1483  CB  ASN A 193      16.552 -10.997 -29.479  1.00 73.96           C  
ANISOU 1483  CB  ASN A 193     9718   8979   9403   1636    186    298       C  
ATOM   1484  CG  ASN A 193      17.636 -10.339 -30.322  1.00 79.11           C  
ANISOU 1484  CG  ASN A 193    10384   9649  10025   1635    177    292       C  
ATOM   1485  ND2 ASN A 193      18.216 -11.100 -31.241  1.00 81.31           N  
ANISOU 1485  ND2 ASN A 193    10663   9941  10291   1631    154    285       N  
ATOM   1486  OD1 ASN A 193      17.952  -9.159 -30.141  1.00 79.74           O  
ANISOU 1486  OD1 ASN A 193    10474   9731  10091   1636    191    294       O  
ATOM   1487  N   SER A 194      15.037 -11.571 -26.453  1.00 63.18           N  
ANISOU 1487  N   SER A 194     8350   7582   8073   1637    230    308       N  
ATOM   1488  CA  SER A 194      13.765 -11.743 -25.762  1.00 58.29           C  
ANISOU 1488  CA  SER A 194     7715   6943   7488   1640    242    315       C  
ATOM   1489  C   SER A 194      13.719 -11.013 -24.425  1.00 63.62           C  
ANISOU 1489  C   SER A 194     8404   7612   8156   1642    271    319       C  
ATOM   1490  O   SER A 194      12.878 -11.319 -23.575  1.00 57.62           O  
ANISOU 1490  O   SER A 194     7637   6839   7419   1643    283    323       O  
ATOM   1491  CB  SER A 194      13.492 -13.225 -25.521  1.00 55.50           C  
ANISOU 1491  CB  SER A 194     7354   6587   7147   1638    231    313       C  
ATOM   1492  OG  SER A 194      13.994 -13.643 -24.260  1.00 55.89           O  
ANISOU 1492  OG  SER A 194     7421   6637   7178   1635    246    311       O  
ATOM   1493  N   VAL A 195      14.637 -10.073 -24.223  1.00 71.44           N  
ANISOU 1493  N   VAL A 195     9415   8613   9117   1641    282    317       N  
ATOM   1494  CA  VAL A 195      14.633  -9.247 -23.018  1.00 71.14           C  
ANISOU 1494  CA  VAL A 195     9391   8569   9071   1642    311    321       C  
ATOM   1495  C   VAL A 195      14.914  -7.802 -23.386  1.00 82.37           C  
ANISOU 1495  C   VAL A 195    10819   9994  10482   1645    319    323       C  
ATOM   1496  O   VAL A 195      14.270  -6.884 -22.874  1.00 91.08           O  
ANISOU 1496  O   VAL A 195    11921  11088  11599   1648    339    329       O  
ATOM   1497  CB  VAL A 195      15.670  -9.706 -21.978  1.00 61.61           C  
ANISOU 1497  CB  VAL A 195     8208   7371   7831   1637    320    316       C  
ATOM   1498  CG1 VAL A 195      15.727  -8.722 -20.825  1.00 55.79           C  
ANISOU 1498  CG1 VAL A 195     7486   6629   7084   1639    349    320       C  
ATOM   1499  CG2 VAL A 195      15.335 -11.096 -21.464  1.00 63.36           C  
ANISOU 1499  CG2 VAL A 195     8423   7588   8064   1635    315    315       C  
ATOM   1500  N   VAL A 196      15.872  -7.598 -24.282  1.00 83.93           N  
ANISOU 1500  N   VAL A 196    11026  10208  10656   1643    305    317       N  
ATOM   1501  CA  VAL A 196      16.214  -6.247 -24.697  1.00 90.38           C  
ANISOU 1501  CA  VAL A 196    11849  11030  11460   1645    311    318       C  
ATOM   1502  C   VAL A 196      15.226  -5.707 -25.721  1.00 92.25           C  
ANISOU 1502  C   VAL A 196    12064  11258  11729   1650    303    323       C  
ATOM   1503  O   VAL A 196      14.935  -6.346 -26.734  1.00 90.69           O  
ANISOU 1503  O   VAL A 196    11851  11063  11547   1650    280    322       O  
ATOM   1504  CB  VAL A 196      17.659  -6.136 -25.220  1.00 95.11           C  
ANISOU 1504  CB  VAL A 196    12468  11649  12019   1641    300    311       C  
ATOM   1505  CG1 VAL A 196      18.634  -6.507 -24.119  1.00 93.54           C  
ANISOU 1505  CG1 VAL A 196    12294  11459  11789   1637    311    307       C  
ATOM   1506  CG2 VAL A 196      17.868  -7.012 -26.450  1.00 98.58           C  
ANISOU 1506  CG2 VAL A 196    12897  12097  12460   1640    271    305       C  
ATOM   1507  N   ILE A 197      14.700  -4.525 -25.421  1.00 96.50           N  
ANISOU 1507  N   ILE A 197    12600  11788  12278   1654    321    329       N  
ATOM   1508  CA  ILE A 197      13.726  -3.860 -26.270  1.00 98.86           C  
ANISOU 1508  CA  ILE A 197    12878  12077  12607   1659    316    335       C  
ATOM   1509  C   ILE A 197      14.406  -2.714 -27.006  1.00100.17           C  
ANISOU 1509  C   ILE A 197    13054  12254  12754   1660    315    334       C  
ATOM   1510  O   ILE A 197      14.549  -2.737 -28.232  1.00 98.34           O  
ANISOU 1510  O   ILE A 197    12813  12029  12523   1660    294    331       O  
ATOM   1511  CB  ILE A 197      12.560  -3.300 -25.428  1.00 99.13           C  
ANISOU 1511  CB  ILE A 197    12904  12093  12669   1663    338    343       C  
ATOM   1512  CG1 ILE A 197      11.835  -4.435 -24.687  1.00 96.68           C  
ANISOU 1512  CG1 ILE A 197    12584  11772  12379   1662    340    344       C  
ATOM   1513  CG2 ILE A 197      11.612  -2.463 -26.290  1.00 99.12           C  
ANISOU 1513  CG2 ILE A 197    12883  12083  12696   1669    335    348       C  
ATOM   1514  CD1 ILE A 197      11.371  -5.577 -25.580  1.00 92.71           C  
ANISOU 1514  CD1 ILE A 197    12062  11268  11897   1662    314    342       C  
ATOM   1515  N   ASP A 198      14.845  -1.722 -26.238  1.00100.65           N  
ANISOU 1515  N   ASP A 198    13131  12315  12795   1660    337    335       N  
ATOM   1516  CA  ASP A 198      15.459  -0.530 -26.800  1.00 99.48           C  
ANISOU 1516  CA  ASP A 198    12992  12176  12629   1661    338    335       C  
ATOM   1517  C   ASP A 198      16.959  -0.716 -27.006  1.00 93.79           C  
ANISOU 1517  C   ASP A 198    12294  11476  11868   1657    330    327       C  
ATOM   1518  O   ASP A 198      17.620  -1.413 -26.233  1.00 85.81           O  
ANISOU 1518  O   ASP A 198    11298  10470  10835   1653    333    323       O  
ATOM   1519  CB  ASP A 198      15.200   0.670 -25.887  1.00100.59           C  
ANISOU 1519  CB  ASP A 198    13141  12308  12771   1664    366    341       C  
ATOM   1520  CG  ASP A 198      14.900   1.936 -26.662  1.00102.79           C  
ANISOU 1520  CG  ASP A 198    13412  12585  13058   1668    368    345       C  
ATOM   1521  OD1 ASP A 198      15.367   2.047 -27.815  1.00104.47           O  
ANISOU 1521  OD1 ASP A 198    13623  12809  13263   1668    349    341       O  
ATOM   1522  OD2 ASP A 198      14.192   2.814 -26.121  1.00102.43           O1-
ANISOU 1522  OD2 ASP A 198    13363  12527  13028   1672    388    351       O1-
ATOM   1523  N   ASP A 199      17.499  -0.068 -28.036  1.00 95.60           N  
ANISOU 1523  N   ASP A 199    12525  11715  12083   1657    318    325       N  
ATOM   1524  CA  ASP A 199      18.937  -0.101 -28.302  1.00 94.35           C  
ANISOU 1524  CA  ASP A 199    12388  11577  11885   1653    310    317       C  
ATOM   1525  C   ASP A 199      19.742   0.525 -27.158  1.00 89.36           C  
ANISOU 1525  C   ASP A 199    11782  10949  11224   1651    332    317       C  
ATOM   1526  O   ASP A 199      20.970   0.609 -27.234  1.00 96.67           O  
ANISOU 1526  O   ASP A 199    12727  11890  12113   1648    328    311       O  
ATOM   1527  CB  ASP A 199      19.276   0.628 -29.610  1.00 94.06           C  
ANISOU 1527  CB  ASP A 199    12349  11550  11842   1655    296    315       C  
ATOM   1528  CG  ASP A 199      18.376   0.229 -30.755  1.00 94.32           C  
ANISOU 1528  CG  ASP A 199    12356  11577  11906   1657    276    317       C  
ATOM   1529  OD1 ASP A 199      17.143   0.150 -30.552  1.00 92.55           O  
ANISOU 1529  OD1 ASP A 199    12112  11335  11717   1660    282    324       O  
ATOM   1530  OD2 ASP A 199      18.910   0.007 -31.864  1.00 95.50           O1-
ANISOU 1530  OD2 ASP A 199    12504  11738  12044   1656    255    312       O1-
ATOM   1531  N   ASP A 200      19.050   0.978 -26.115  1.00 72.43           N  
ANISOU 1531  N   ASP A 200     9636   8790   9094   1653    356    323       N  
ATOM   1532  CA  ASP A 200      19.696   1.583 -24.964  1.00 58.21           C  
ANISOU 1532  CA  ASP A 200     7858   6991   7268   1652    378    324       C  
ATOM   1533  C   ASP A 200      19.153   1.010 -23.671  1.00 54.98           C  
ANISOU 1533  C   ASP A 200     7449   6569   6870   1651    395    327       C  
ATOM   1534  O   ASP A 200      17.954   1.056 -23.420  1.00 58.35           O  
ANISOU 1534  O   ASP A 200     7858   6980   7330   1654    403    333       O  
ATOM   1535  CB  ASP A 200      19.498   3.090 -24.969  1.00 53.95           C  
ANISOU 1535  CB  ASP A 200     7320   6447   6732   1655    394    329       C  
ATOM   1536  CG  ASP A 200      20.624   3.821 -25.666  1.00 54.80           C  
ANISOU 1536  CG  ASP A 200     7443   6571   6809   1654    387    325       C  
ATOM   1537  OD1 ASP A 200      21.240   3.237 -26.585  1.00 39.38           O  
ANISOU 1537  OD1 ASP A 200     5490   4631   4842   1652    365    319       O  
ATOM   1538  OD2 ASP A 200      20.894   4.988 -25.300  1.00 65.96           O1-
ANISOU 1538  OD2 ASP A 200     8867   7983   8210   1655    404    328       O1-
ATOM   1539  N   TYR A 201      20.042   0.455 -22.857  1.00 52.36           N  
ANISOU 1539  N   TYR A 201     7137   6246   6511   1646    399    323       N  
ATOM   1540  CA  TYR A 201      19.685  -0.003 -21.518  1.00 46.34           C  
ANISOU 1540  CA  TYR A 201     6379   5473   5753   1645    417    325       C  
ATOM   1541  C   TYR A 201      20.878   0.114 -20.590  1.00 42.35           C  
ANISOU 1541  C   TYR A 201     5902   4979   5210   1641    429    322       C  
ATOM   1542  O   TYR A 201      22.021   0.129 -21.037  1.00 49.22           O  
ANISOU 1542  O   TYR A 201     6787   5865   6049   1638    418    316       O  
ATOM   1543  CB  TYR A 201      19.155  -1.451 -21.527  1.00 46.72           C  
ANISOU 1543  CB  TYR A 201     6414   5517   5821   1644    404    323       C  
ATOM   1544  CG  TYR A 201      20.161  -2.515 -21.938  1.00 40.48           C  
ANISOU 1544  CG  TYR A 201     5632   4743   5006   1639    383    315       C  
ATOM   1545  CD1 TYR A 201      21.014  -3.099 -21.009  1.00 40.71           C  
ANISOU 1545  CD1 TYR A 201     5682   4780   5007   1635    389    311       C  
ATOM   1546  CD2 TYR A 201      20.238  -2.950 -23.251  1.00 41.93           C  
ANISOU 1546  CD2 TYR A 201     5804   4934   5193   1639    357    311       C  
ATOM   1547  CE1 TYR A 201      21.920  -4.068 -21.377  1.00 36.32           C  
ANISOU 1547  CE1 TYR A 201     5134   4238   4429   1631    370    303       C  
ATOM   1548  CE2 TYR A 201      21.146  -3.920 -23.629  1.00 43.56           C  
ANISOU 1548  CE2 TYR A 201     6018   5155   5376   1635    338    302       C  
ATOM   1549  CZ  TYR A 201      21.985  -4.474 -22.686  1.00 38.83           C  
ANISOU 1549  CZ  TYR A 201     5439   4563   4750   1631    345    298       C  
ATOM   1550  OH  TYR A 201      22.893  -5.431 -23.066  1.00 37.86           O  
ANISOU 1550  OH  TYR A 201     5325   4455   4604   1627    326    290       O  
ATOM   1551  N   PHE A 202      20.602   0.225 -19.300  1.00 35.46           N  
ANISOU 1551  N   PHE A 202     5037   4097   4340   1640    452    326       N  
ATOM   1552  CA  PHE A 202      21.631   0.087 -18.293  1.00 35.16           C  
ANISOU 1552  CA  PHE A 202     5025   4067   4268   1636    463    324       C  
ATOM   1553  C   PHE A 202      21.446  -1.301 -17.706  1.00 39.23           C  
ANISOU 1553  C   PHE A 202     5537   4579   4789   1633    459    321       C  
ATOM   1554  O   PHE A 202      20.326  -1.702 -17.417  1.00 41.89           O  
ANISOU 1554  O   PHE A 202     5857   4901   5158   1636    463    326       O  
ATOM   1555  CB  PHE A 202      21.465   1.120 -17.177  1.00 36.69           C  
ANISOU 1555  CB  PHE A 202     5230   4252   4461   1637    492    330       C  
ATOM   1556  CG  PHE A 202      21.555   2.568 -17.628  1.00 39.14           C  
ANISOU 1556  CG  PHE A 202     5543   4563   4768   1640    499    333       C  
ATOM   1557  CD1 PHE A 202      21.943   2.909 -18.913  1.00 36.61           C  
ANISOU 1557  CD1 PHE A 202     5218   4253   4441   1641    480    330       C  
ATOM   1558  CD2 PHE A 202      21.260   3.595 -16.732  1.00 39.55           C  
ANISOU 1558  CD2 PHE A 202     5601   4604   4821   1641    525    340       C  
ATOM   1559  CE1 PHE A 202      22.019   4.245 -19.303  1.00 33.09           C  
ANISOU 1559  CE1 PHE A 202     4775   3807   3992   1644    488    333       C  
ATOM   1560  CE2 PHE A 202      21.343   4.922 -17.115  1.00 34.11           C  
ANISOU 1560  CE2 PHE A 202     4916   3916   4130   1644    533    343       C  
ATOM   1561  CZ  PHE A 202      21.721   5.245 -18.402  1.00 32.75           C  
ANISOU 1561  CZ  PHE A 202     4738   3753   3951   1645    514    339       C  
ATOM   1562  N   LEU A 203      22.535  -2.041 -17.532  1.00 44.73           N  
ANISOU 1562  N   LEU A 203     6250   5289   5455   1629    449    315       N  
ATOM   1563  CA  LEU A 203      22.472  -3.331 -16.839  1.00 45.02           C  
ANISOU 1563  CA  LEU A 203     6288   5324   5494   1626    448    313       C  
ATOM   1564  C   LEU A 203      22.888  -3.188 -15.375  1.00 43.40           C  
ANISOU 1564  C   LEU A 203     6104   5117   5271   1623    471    315       C  
ATOM   1565  O   LEU A 203      23.972  -2.686 -15.075  1.00 48.15           O  
ANISOU 1565  O   LEU A 203     6727   5729   5838   1620    476    312       O  
ATOM   1566  CB  LEU A 203      23.350  -4.360 -17.547  1.00 48.22           C  
ANISOU 1566  CB  LEU A 203     6697   5745   5879   1622    422    304       C  
ATOM   1567  CG  LEU A 203      23.613  -5.725 -16.905  1.00 43.59           C  
ANISOU 1567  CG  LEU A 203     6116   5161   5285   1618    418    300       C  
ATOM   1568  CD1 LEU A 203      22.340  -6.481 -16.565  1.00 46.13           C  
ANISOU 1568  CD1 LEU A 203     6417   5467   5645   1620    420    304       C  
ATOM   1569  CD2 LEU A 203      24.452  -6.542 -17.842  1.00 38.83           C  
ANISOU 1569  CD2 LEU A 203     5515   4574   4663   1615    391    291       C  
ATOM   1570  N   LEU A 204      22.015  -3.620 -14.472  1.00 41.25           N  
ANISOU 1570  N   LEU A 204     5823   4830   5020   1624    485    319       N  
ATOM   1571  CA  LEU A 204      22.238  -3.465 -13.036  1.00 43.90           C  
ANISOU 1571  CA  LEU A 204     6177   5162   5343   1621    509    322       C  
ATOM   1572  C   LEU A 204      22.333  -4.808 -12.300  1.00 49.49           C  
ANISOU 1572  C   LEU A 204     6887   5868   6047   1618    506    320       C  
ATOM   1573  O   LEU A 204      21.457  -5.666 -12.432  1.00 53.27           O  
ANISOU 1573  O   LEU A 204     7348   6339   6554   1619    499    320       O  
ATOM   1574  CB  LEU A 204      21.122  -2.610 -12.414  1.00 42.55           C  
ANISOU 1574  CB  LEU A 204     5996   4972   5198   1625    532    331       C  
ATOM   1575  CG  LEU A 204      20.814  -2.752 -10.904  1.00 41.49           C  
ANISOU 1575  CG  LEU A 204     5871   4828   5066   1624    557    336       C  
ATOM   1576  CD1 LEU A 204      21.727  -1.917  -9.988  1.00 34.89           C  
ANISOU 1576  CD1 LEU A 204     5061   3996   4198   1621    576    337       C  
ATOM   1577  CD2 LEU A 204      19.364  -2.450 -10.622  1.00 40.46           C  
ANISOU 1577  CD2 LEU A 204     5720   4678   4974   1628    571    343       C  
ATOM   1578  N   THR A 205      23.401  -4.983 -11.528  1.00 45.37           N  
ANISOU 1578  N   THR A 205     6389   5356   5492   1613    512    317       N  
ATOM   1579  CA  THR A 205      23.535  -6.144 -10.657  1.00 43.80           C  
ANISOU 1579  CA  THR A 205     6197   5158   5289   1610    514    315       C  
ATOM   1580  C   THR A 205      23.814  -5.663  -9.246  1.00 49.44           C  
ANISOU 1580  C   THR A 205     6931   5868   5988   1608    540    319       C  
ATOM   1581  O   THR A 205      24.549  -4.690  -9.044  1.00 51.60           O  
ANISOU 1581  O   THR A 205     7222   6147   6238   1607    550    320       O  
ATOM   1582  CB  THR A 205      24.679  -7.095 -11.092  1.00 35.81           C  
ANISOU 1582  CB  THR A 205     5195   4163   4248   1605    492    306       C  
ATOM   1583  CG2 THR A 205      24.633  -7.352 -12.592  1.00 26.96           C  
ANISOU 1583  CG2 THR A 205     4059   3048   3135   1607    465    301       C  
ATOM   1584  OG1 THR A 205      25.952  -6.543 -10.721  1.00 37.41           O  
ANISOU 1584  OG1 THR A 205     5425   4378   4411   1602    497    304       O  
ATOM   1585  N   LEU A 206      23.232  -6.356  -8.274  1.00 51.25           N  
ANISOU 1585  N   LEU A 206     7157   6086   6231   1607    552    322       N  
ATOM   1586  CA  LEU A 206      23.303  -5.953  -6.876  1.00 52.01           C  
ANISOU 1586  CA  LEU A 206     7268   6175   6317   1605    578    327       C  
ATOM   1587  C   LEU A 206      23.242  -7.217  -6.045  1.00 54.29           C  
ANISOU 1587  C   LEU A 206     7560   6462   6608   1602    579    326       C  
ATOM   1588  O   LEU A 206      22.306  -8.001  -6.180  1.00 58.18           O  
ANISOU 1588  O   LEU A 206     8032   6944   7128   1604    573    326       O  
ATOM   1589  CB  LEU A 206      22.117  -5.039  -6.550  1.00 53.46           C  
ANISOU 1589  CB  LEU A 206     7440   6342   6531   1610    599    335       C  
ATOM   1590  CG  LEU A 206      22.056  -4.289  -5.220  1.00 47.75           C  
ANISOU 1590  CG  LEU A 206     6731   5610   5801   1609    629    341       C  
ATOM   1591  CD1 LEU A 206      23.202  -3.312  -5.099  1.00 47.59           C  
ANISOU 1591  CD1 LEU A 206     6735   5601   5746   1607    635    340       C  
ATOM   1592  CD2 LEU A 206      20.738  -3.565  -5.131  1.00 44.50           C  
ANISOU 1592  CD2 LEU A 206     6302   5181   5423   1614    644    348       C  
ATOM   1593  N   HIS A 207      24.239  -7.440  -5.199  1.00 59.91           N  
ANISOU 1593  N   HIS A 207     8294   7181   7287   1598    585    324       N  
ATOM   1594  CA  HIS A 207      24.289  -8.713  -4.485  1.00 63.72           C  
ANISOU 1594  CA  HIS A 207     8780   7663   7769   1595    584    322       C  
ATOM   1595  C   HIS A 207      25.018  -8.702  -3.147  1.00 60.44           C  
ANISOU 1595  C   HIS A 207     8389   7249   7326   1590    602    323       C  
ATOM   1596  O   HIS A 207      24.658  -9.470  -2.260  1.00 68.67           O  
ANISOU 1596  O   HIS A 207     9430   8284   8376   1589    610    325       O  
ATOM   1597  CB  HIS A 207      24.874  -9.810  -5.376  1.00 67.85           C  
ANISOU 1597  CB  HIS A 207     9299   8199   8281   1593    555    313       C  
ATOM   1598  CG  HIS A 207      24.546 -11.190  -4.912  1.00 73.32           C  
ANISOU 1598  CG  HIS A 207     9985   8887   8985   1591    550    312       C  
ATOM   1599  CD2 HIS A 207      23.456 -11.967  -5.126  1.00 76.77           C  
ANISOU 1599  CD2 HIS A 207    10399   9314   9456   1593    544    313       C  
ATOM   1600  ND1 HIS A 207      25.386 -11.925  -4.103  1.00 73.46           N  
ANISOU 1600  ND1 HIS A 207    10022   8913   8978   1586    552    309       N  
ATOM   1601  CE1 HIS A 207      24.834 -13.095  -3.845  1.00 75.94           C  
ANISOU 1601  CE1 HIS A 207    10324   9220   9309   1586    547    308       C  
ATOM   1602  NE2 HIS A 207      23.661 -13.147  -4.455  1.00 78.78           N  
ANISOU 1602  NE2 HIS A 207    10658   9569   9705   1590    542    311       N  
ATOM   1603  N   ARG A 208      26.036  -7.857  -3.007  1.00 45.13           N  
ANISOU 1603  N   ARG A 208     6471   5320   5355   1588    607    323       N  
ATOM   1604  CA  ARG A 208      26.806  -7.783  -1.773  1.00 45.63           C  
ANISOU 1604  CA  ARG A 208     6559   5385   5392   1584    623    325       C  
ATOM   1605  C   ARG A 208      25.936  -7.705  -0.511  1.00 53.27           C  
ANISOU 1605  C   ARG A 208     7526   6337   6379   1585    649    332       C  
ATOM   1606  O   ARG A 208      24.906  -7.029  -0.500  1.00 56.51           O  
ANISOU 1606  O   ARG A 208     7921   6733   6815   1589    662    337       O  
ATOM   1607  CB  ARG A 208      27.766  -6.605  -1.836  1.00 46.95           C  
ANISOU 1607  CB  ARG A 208     6746   5562   5530   1583    628    325       C  
ATOM   1608  CG  ARG A 208      28.790  -6.763  -2.923  1.00 58.82           C  
ANISOU 1608  CG  ARG A 208     8256   7084   7010   1581    603    318       C  
ATOM   1609  CD  ARG A 208      29.754  -7.859  -2.569  1.00 66.19           C  
ANISOU 1609  CD  ARG A 208     9204   8029   7917   1577    591    312       C  
ATOM   1610  NE  ARG A 208      30.511  -7.489  -1.381  1.00 71.86           N  
ANISOU 1610  NE  ARG A 208     9948   8749   8608   1573    609    316       N  
ATOM   1611  CZ  ARG A 208      31.797  -7.165  -1.399  1.00 76.32           C  
ANISOU 1611  CZ  ARG A 208    10534   9327   9136   1569    603    313       C  
ATOM   1612  NH1 ARG A 208      32.462  -7.185  -2.554  1.00 79.19           N1+
ANISOU 1612  NH1 ARG A 208    10897   9705   9484   1569    580    307       N1+
ATOM   1613  NH2 ARG A 208      32.417  -6.836  -0.270  1.00 72.30           N  
ANISOU 1613  NH2 ARG A 208    10048   8819   8605   1566    619    317       N  
ATOM   1614  N   ALA A 209      26.342  -8.419   0.538  1.00 54.13           N  
ANISOU 1614  N   ALA A 209     7647   6446   6472   1581    657    332       N  
ATOM   1615  CA  ALA A 209      25.607  -8.419   1.798  1.00 58.12           C  
ANISOU 1615  CA  ALA A 209     8154   6937   6993   1581    682    338       C  
ATOM   1616  C   ALA A 209      25.507  -7.005   2.365  1.00 66.10           C  
ANISOU 1616  C   ALA A 209     9175   7941   8001   1582    705    345       C  
ATOM   1617  O   ALA A 209      24.424  -6.562   2.767  1.00 68.24           O  
ANISOU 1617  O   ALA A 209     9434   8196   8298   1585    723    351       O  
ATOM   1618  CB  ALA A 209      26.269  -9.344   2.795  1.00 58.55           C  
ANISOU 1618  CB  ALA A 209     8225   6995   7026   1576    684    337       C  
ATOM   1619  N   GLU A 210      26.630  -6.286   2.355  1.00 64.97           N  
ANISOU 1619  N   GLU A 210     9052   7808   7825   1579    705    344       N  
ATOM   1620  CA  GLU A 210      26.673  -4.899   2.826  1.00 64.31           C  
ANISOU 1620  CA  GLU A 210     8979   7719   7735   1579    726    350       C  
ATOM   1621  C   GLU A 210      25.600  -3.999   2.197  1.00 61.65           C  
ANISOU 1621  C   GLU A 210     8623   7372   7429   1585    732    354       C  
ATOM   1622  O   GLU A 210      25.390  -2.878   2.656  1.00 65.50           O  
ANISOU 1622  O   GLU A 210     9116   7852   7918   1586    752    360       O  
ATOM   1623  CB  GLU A 210      28.058  -4.280   2.592  1.00 66.65           C  
ANISOU 1623  CB  GLU A 210     9299   8031   7994   1576    719    348       C  
ATOM   1624  CG  GLU A 210      28.383  -4.042   1.118  1.00 71.55           C  
ANISOU 1624  CG  GLU A 210     9911   8663   8612   1579    696    342       C  
ATOM   1625  CD  GLU A 210      29.401  -2.930   0.896  1.00 72.39           C  
ANISOU 1625  CD  GLU A 210    10036   8779   8689   1577    696    343       C  
ATOM   1626  OE1 GLU A 210      30.624  -3.196   0.985  1.00 68.83           O  
ANISOU 1626  OE1 GLU A 210     9605   8342   8205   1573    687    339       O  
ATOM   1627  OE2 GLU A 210      28.969  -1.789   0.621  1.00 71.31           O1-
ANISOU 1627  OE2 GLU A 210     9895   8637   8564   1580    706    347       O1-
ATOM   1628  N   ASN A 211      24.928  -4.486   1.156  1.00 55.74           N  
ANISOU 1628  N   ASN A 211     7852   6623   6705   1589    715    351       N  
ATOM   1629  CA  ASN A 211      23.914  -3.700   0.456  1.00 61.21           C  
ANISOU 1629  CA  ASN A 211     8524   7306   7427   1594    717    354       C  
ATOM   1630  C   ASN A 211      22.500  -4.244   0.611  1.00 69.63           C  
ANISOU 1630  C   ASN A 211     9567   8357   8532   1598    723    357       C  
ATOM   1631  O   ASN A 211      21.550  -3.475   0.799  1.00 73.14           O  
ANISOU 1631  O   ASN A 211    10002   8789   9000   1601    740    363       O  
ATOM   1632  CB  ASN A 211      24.229  -3.591  -1.044  1.00 57.89           C  
ANISOU 1632  CB  ASN A 211     8094   6897   7004   1596    692    349       C  
ATOM   1633  CG  ASN A 211      25.322  -2.581  -1.353  1.00 51.40           C  
ANISOU 1633  CG  ASN A 211     7291   6086   6151   1595    691    347       C  
ATOM   1634  ND2 ASN A 211      26.049  -2.820  -2.430  1.00 48.07           N  
ANISOU 1634  ND2 ASN A 211     6869   5679   5715   1594    667    341       N  
ATOM   1635  OD1 ASN A 211      25.504  -1.600  -0.640  1.00 55.08           O  
ANISOU 1635  OD1 ASN A 211     7772   6550   6608   1594    711    352       O  
ATOM   1636  N   VAL A 212      22.361  -5.564   0.511  1.00 70.10           N  
ANISOU 1636  N   VAL A 212     9618   8419   8599   1597    709    353       N  
ATOM   1637  CA  VAL A 212      21.037  -6.188   0.493  1.00 71.45           C  
ANISOU 1637  CA  VAL A 212     9764   8575   8807   1600    710    356       C  
ATOM   1638  C   VAL A 212      20.497  -6.505   1.888  1.00 70.15           C  
ANISOU 1638  C   VAL A 212     9604   8399   8651   1599    733    361       C  
ATOM   1639  O   VAL A 212      19.281  -6.531   2.087  1.00 67.38           O  
ANISOU 1639  O   VAL A 212     9235   8034   8332   1603    743    366       O  
ATOM   1640  CB  VAL A 212      21.000  -7.468  -0.387  1.00 50.75           C  
ANISOU 1640  CB  VAL A 212     7128   5960   6194   1600    682    349       C  
ATOM   1641  CG1 VAL A 212      21.141  -7.112  -1.855  1.00 47.64           C  
ANISOU 1641  CG1 VAL A 212     6724   5574   5803   1603    660    346       C  
ATOM   1642  CG2 VAL A 212      22.092  -8.434   0.034  1.00 53.03           C  
ANISOU 1642  CG2 VAL A 212     7434   6261   6453   1595    673    344       C  
ATOM   1643  N   ASP A 213      21.399  -6.753   2.841  1.00 69.51           N  
ANISOU 1643  N   ASP A 213     9545   8323   8541   1594    741    360       N  
ATOM   1644  CA  ASP A 213      21.011  -7.015   4.229  1.00 69.62           C  
ANISOU 1644  CA  ASP A 213     9566   8326   8559   1592    764    365       C  
ATOM   1645  C   ASP A 213      20.561  -5.722   4.889  1.00 76.49           C  
ANISOU 1645  C   ASP A 213    10441   9186   9435   1594    791    372       C  
ATOM   1646  O   ASP A 213      19.545  -5.683   5.586  1.00 81.17           O  
ANISOU 1646  O   ASP A 213    11026   9765  10051   1596    809    378       O  
ATOM   1647  CB  ASP A 213      22.178  -7.597   5.027  1.00 63.27           C  
ANISOU 1647  CB  ASP A 213     8787   7533   7722   1586    764    362       C  
ATOM   1648  CG  ASP A 213      22.557  -8.991   4.579  1.00 61.85           C  
ANISOU 1648  CG  ASP A 213     8602   7361   7536   1584    740    355       C  
ATOM   1649  OD1 ASP A 213      21.783  -9.607   3.807  1.00 58.87           O  
ANISOU 1649  OD1 ASP A 213     8202   6981   7186   1588    726    353       O  
ATOM   1650  OD2 ASP A 213      23.629  -9.469   5.015  1.00 61.23           O1-
ANISOU 1650  OD2 ASP A 213     8543   7293   7428   1580    736    352       O1-
ATOM   1651  N   ASN A 214      21.342  -4.672   4.656  1.00 73.36           N  
ANISOU 1651  N   ASN A 214    10060   8798   9017   1593    793    372       N  
ATOM   1652  CA  ASN A 214      21.096  -3.340   5.190  1.00 67.45           C  
ANISOU 1652  CA  ASN A 214     9318   8040   8269   1594    817    379       C  
ATOM   1653  C   ASN A 214      19.903  -2.654   4.523  1.00 70.70           C  
ANISOU 1653  C   ASN A 214     9707   8441   8714   1600    820    383       C  
ATOM   1654  O   ASN A 214      20.046  -2.096   3.439  1.00 77.49           O  
ANISOU 1654  O   ASN A 214    10560   9307   9574   1603    807    380       O  
ATOM   1655  CB  ASN A 214      22.363  -2.501   4.998  1.00 61.02           C  
ANISOU 1655  CB  ASN A 214     8526   7239   7421   1591    814    377       C  
ATOM   1656  CG  ASN A 214      22.293  -1.160   5.687  1.00 59.65           C  
ANISOU 1656  CG  ASN A 214     8364   7058   7242   1592    839    384       C  
ATOM   1657  ND2 ASN A 214      23.443  -0.679   6.172  1.00 56.39           N  
ANISOU 1657  ND2 ASN A 214     7976   6653   6796   1587    844    384       N  
ATOM   1658  OD1 ASN A 214      21.223  -0.557   5.785  1.00 56.94           O  
ANISOU 1658  OD1 ASN A 214     8007   6701   6925   1596    854    389       O  
ATOM   1659  N   LYS A 215      18.748  -2.678   5.189  1.00 67.97           N  
ANISOU 1659  N   LYS A 215     9350   8080   8396   1603    838    388       N  
ATOM   1660  CA  LYS A 215      17.506  -2.069   4.691  1.00 71.24           C  
ANISOU 1660  CA  LYS A 215     9742   8483   8844   1609    844    393       C  
ATOM   1661  C   LYS A 215      17.682  -0.628   4.224  1.00 69.66           C  
ANISOU 1661  C   LYS A 215     9546   8283   8638   1611    849    395       C  
ATOM   1662  O   LYS A 215      17.033  -0.183   3.267  1.00 64.69           O  
ANISOU 1662  O   LYS A 215     8899   7651   8030   1615    842    395       O  
ATOM   1663  CB  LYS A 215      16.433  -2.117   5.784  1.00 77.10           C  
ANISOU 1663  CB  LYS A 215    10479   9209   9609   1610    868    399       C  
ATOM   1664  CG  LYS A 215      16.986  -1.822   7.174  1.00 83.79           C  
ANISOU 1664  CG  LYS A 215    11350  10054  10433   1606    892    403       C  
ATOM   1665  CD  LYS A 215      16.034  -2.241   8.290  1.00 86.78           C  
ANISOU 1665  CD  LYS A 215    11724  10418  10831   1606    913    408       C  
ATOM   1666  CE  LYS A 215      16.645  -1.953   9.662  1.00 85.73           C  
ANISOU 1666  CE  LYS A 215    11615  10283  10674   1601    936    411       C  
ATOM   1667  NZ  LYS A 215      15.741  -2.316  10.788  1.00 83.03           N1+
ANISOU 1667  NZ  LYS A 215    11270   9928  10350   1601    957    417       N1+
ATOM   1668  N   GLU A 216      18.570   0.089   4.907  1.00 74.27           N  
ANISOU 1668  N   GLU A 216    10154   8872   9194   1607    863    396       N  
ATOM   1669  CA  GLU A 216      18.847   1.488   4.600  1.00 77.37           C  
ANISOU 1669  CA  GLU A 216    10554   9265   9578   1608    871    399       C  
ATOM   1670  C   GLU A 216      19.479   1.634   3.221  1.00 76.27           C  
ANISOU 1670  C   GLU A 216    10411   9140   9429   1609    845    393       C  
ATOM   1671  O   GLU A 216      18.884   2.217   2.314  1.00 78.18           O  
ANISOU 1671  O   GLU A 216    10637   9379   9690   1614    839    394       O  
ATOM   1672  CB  GLU A 216      19.774   2.084   5.659  1.00 80.92           C  
ANISOU 1672  CB  GLU A 216    11031   9718   9997   1603    888    401       C  
ATOM   1673  CG  GLU A 216      19.452   3.504   6.024  1.00 87.17           C  
ANISOU 1673  CG  GLU A 216    11828  10501  10793   1605    911    407       C  
ATOM   1674  CD  GLU A 216      18.063   3.638   6.603  1.00 90.58           C  
ANISOU 1674  CD  GLU A 216    12244  10915  11257   1609    931    414       C  
ATOM   1675  OE1 GLU A 216      17.885   3.335   7.806  1.00 89.60           O  
ANISOU 1675  OE1 GLU A 216    12129  10783  11131   1606    950    417       O  
ATOM   1676  OE2 GLU A 216      17.150   4.040   5.849  1.00 92.60           O1-
ANISOU 1676  OE2 GLU A 216    12480  11164  11539   1614    929    415       O1-
ATOM   1677  N   ARG A 217      20.686   1.094   3.069  1.00 71.49           N  
ANISOU 1677  N   ARG A 217     9820   8549   8793   1605    829    387       N  
ATOM   1678  CA  ARG A 217      21.419   1.175   1.811  1.00 60.14           C  
ANISOU 1678  CA  ARG A 217     8383   7126   7343   1605    805    381       C  
ATOM   1679  C   ARG A 217      20.592   0.630   0.658  1.00 57.07           C  
ANISOU 1679  C   ARG A 217     7967   6736   6983   1610    785    378       C  
ATOM   1680  O   ARG A 217      20.613   1.186  -0.431  1.00 56.89           O  
ANISOU 1680  O   ARG A 217     7935   6717   6963   1612    772    377       O  
ATOM   1681  CB  ARG A 217      22.752   0.432   1.906  1.00 56.69           C  
ANISOU 1681  CB  ARG A 217     7965   6705   6871   1600    790    375       C  
ATOM   1682  CG  ARG A 217      23.590   0.810   3.113  1.00 55.23           C  
ANISOU 1682  CG  ARG A 217     7807   6521   6657   1595    808    378       C  
ATOM   1683  CD  ARG A 217      25.026   0.365   2.949  1.00 62.01           C  
ANISOU 1683  CD  ARG A 217     8685   7397   7479   1590    792    372       C  
ATOM   1684  NE  ARG A 217      25.683   1.060   1.840  1.00 70.51           N  
ANISOU 1684  NE  ARG A 217     9764   8486   8542   1591    776    369       N  
ATOM   1685  CZ  ARG A 217      26.998   1.057   1.626  1.00 76.84           C  
ANISOU 1685  CZ  ARG A 217    10584   9302   9309   1588    764    365       C  
ATOM   1686  NH1 ARG A 217      27.811   0.397   2.446  1.00 81.25           N1+
ANISOU 1686  NH1 ARG A 217    11161   9866   9843   1583    765    363       N1+
ATOM   1687  NH2 ARG A 217      27.505   1.720   0.594  1.00 75.30           N  
ANISOU 1687  NH2 ARG A 217    10390   9117   9104   1589    750    362       N  
ATOM   1688  N   LEU A 218      19.846  -0.442   0.902  1.00 57.84           N  
ANISOU 1688  N   LEU A 218     8050   6826   7101   1610    782    378       N  
ATOM   1689  CA  LEU A 218      19.009  -1.017  -0.146  1.00 60.04           C  
ANISOU 1689  CA  LEU A 218     8303   7102   7408   1614    763    376       C  
ATOM   1690  C   LEU A 218      17.909  -0.066  -0.596  1.00 61.58           C  
ANISOU 1690  C   LEU A 218     8480   7285   7633   1620    772    382       C  
ATOM   1691  O   LEU A 218      17.759   0.190  -1.801  1.00 60.35           O  
ANISOU 1691  O   LEU A 218     8310   7133   7487   1623    755    380       O  
ATOM   1692  CB  LEU A 218      18.413  -2.356   0.278  1.00 58.03           C  
ANISOU 1692  CB  LEU A 218     8037   6841   7171   1614    760    376       C  
ATOM   1693  CG  LEU A 218      17.593  -3.119  -0.772  1.00 59.29           C  
ANISOU 1693  CG  LEU A 218     8170   6998   7359   1618    739    373       C  
ATOM   1694  CD1 LEU A 218      18.256  -3.152  -2.148  1.00 53.28           C  
ANISOU 1694  CD1 LEU A 218     7406   6251   6588   1618    711    367       C  
ATOM   1695  CD2 LEU A 218      17.366  -4.534  -0.277  1.00 66.77           C  
ANISOU 1695  CD2 LEU A 218     9113   7943   8314   1616    734    371       C  
ATOM   1696  N   LYS A 219      17.140   0.451   0.362  1.00 67.02           N  
ANISOU 1696  N   LYS A 219     9168   7960   8336   1622    798    389       N  
ATOM   1697  CA  LYS A 219      16.126   1.465   0.048  1.00 68.30           C  
ANISOU 1697  CA  LYS A 219     9315   8111   8524   1627    809    394       C  
ATOM   1698  C   LYS A 219      16.755   2.608  -0.769  1.00 56.39           C  
ANISOU 1698  C   LYS A 219     7813   6610   7001   1628    803    393       C  
ATOM   1699  O   LYS A 219      16.290   2.924  -1.883  1.00 44.34           O  
ANISOU 1699  O   LYS A 219     6271   5085   5493   1632    790    393       O  
ATOM   1700  CB  LYS A 219      15.465   1.987   1.338  1.00 75.06           C  
ANISOU 1700  CB  LYS A 219    10177   8953   9390   1627    840    402       C  
ATOM   1701  CG  LYS A 219      14.540   3.205   1.175  1.00 82.84           C  
ANISOU 1701  CG  LYS A 219    11152   9927  10398   1632    855    408       C  
ATOM   1702  CD  LYS A 219      13.281   2.880   0.374  1.00 90.66           C  
ANISOU 1702  CD  LYS A 219    12113  10909  11426   1638    845    410       C  
ATOM   1703  CE  LYS A 219      12.319   4.067   0.300  1.00 93.14           C  
ANISOU 1703  CE  LYS A 219    12417  11211  11763   1643    861    417       C  
ATOM   1704  NZ  LYS A 219      11.225   3.859  -0.699  1.00 93.14           N1+
ANISOU 1704  NZ  LYS A 219    12388  11204  11796   1648    847    418       N1+
ATOM   1705  N   ASN A 220      17.831   3.181  -0.219  1.00 54.50           N  
ANISOU 1705  N   ASN A 220     7599   6379   6729   1624    812    393       N  
ATOM   1706  CA  ASN A 220      18.606   4.243  -0.869  1.00 54.42           C  
ANISOU 1706  CA  ASN A 220     7599   6379   6701   1624    808    392       C  
ATOM   1707  C   ASN A 220      18.890   3.964  -2.340  1.00 57.39           C  
ANISOU 1707  C   ASN A 220     7963   6765   7077   1625    779    386       C  
ATOM   1708  O   ASN A 220      18.451   4.707  -3.215  1.00 62.76           O  
ANISOU 1708  O   ASN A 220     8631   7443   7772   1629    774    387       O  
ATOM   1709  CB  ASN A 220      19.940   4.438  -0.154  1.00 51.88           C  
ANISOU 1709  CB  ASN A 220     7306   6066   6339   1618    814    390       C  
ATOM   1710  CG  ASN A 220      19.907   5.554   0.859  1.00 57.35           C  
ANISOU 1710  CG  ASN A 220     8013   6751   7026   1617    843    396       C  
ATOM   1711  ND2 ASN A 220      20.727   5.426   1.897  1.00 57.61           N  
ANISOU 1711  ND2 ASN A 220     8069   6787   7033   1612    853    397       N  
ATOM   1712  OD1 ASN A 220      19.166   6.530   0.712  1.00 61.73           O  
ANISOU 1712  OD1 ASN A 220     8559   7296   7600   1621    855    401       O  
ATOM   1713  N   ILE A 221      19.631   2.886  -2.588  1.00 52.05           N  
ANISOU 1713  N   ILE A 221     7292   6101   6384   1622    759    379       N  
ATOM   1714  CA  ILE A 221      19.974   2.435  -3.931  1.00 44.05           C  
ANISOU 1714  CA  ILE A 221     6269   5098   5369   1623    730    373       C  
ATOM   1715  C   ILE A 221      18.770   2.266  -4.866  1.00 49.12           C  
ANISOU 1715  C   ILE A 221     6882   5733   6049   1628    719    374       C  
ATOM   1716  O   ILE A 221      18.778   2.779  -5.990  1.00 51.77           O  
ANISOU 1716  O   ILE A 221     7209   6073   6388   1631    706    373       O  
ATOM   1717  CB  ILE A 221      20.780   1.131  -3.871  1.00 42.25           C  
ANISOU 1717  CB  ILE A 221     6050   4883   5122   1618    713    366       C  
ATOM   1718  CG1 ILE A 221      22.170   1.405  -3.273  1.00 45.12           C  
ANISOU 1718  CG1 ILE A 221     6442   5257   5444   1613    718    364       C  
ATOM   1719  CG2 ILE A 221      20.890   0.502  -5.253  1.00 36.84           C  
ANISOU 1719  CG2 ILE A 221     5350   4207   4442   1620    683    360       C  
ATOM   1720  CD1 ILE A 221      22.976   0.138  -2.935  1.00 42.36           C  
ANISOU 1720  CD1 ILE A 221     6104   4918   5073   1608    706    358       C  
ATOM   1721  N   VAL A 222      17.737   1.558  -4.418  1.00 53.54           N  
ANISOU 1721  N   VAL A 222     7427   6280   6636   1630    725    377       N  
ATOM   1722  CA  VAL A 222      16.527   1.425  -5.236  1.00 53.33           C  
ANISOU 1722  CA  VAL A 222     7373   6244   6646   1635    716    379       C  
ATOM   1723  C   VAL A 222      16.001   2.803  -5.686  1.00 51.82           C  
ANISOU 1723  C   VAL A 222     7175   6047   6468   1640    725    384       C  
ATOM   1724  O   VAL A 222      15.757   3.052  -6.881  1.00 49.31           O  
ANISOU 1724  O   VAL A 222     6842   5732   6163   1643    708    382       O  
ATOM   1725  CB  VAL A 222      15.420   0.632  -4.498  1.00 53.51           C  
ANISOU 1725  CB  VAL A 222     7382   6253   6696   1636    725    382       C  
ATOM   1726  CG1 VAL A 222      14.188   0.540  -5.348  1.00 55.02           C  
ANISOU 1726  CG1 VAL A 222     7545   6434   6924   1642    715    385       C  
ATOM   1727  CG2 VAL A 222      15.895  -0.769  -4.143  1.00 48.74           C  
ANISOU 1727  CG2 VAL A 222     6784   5655   6081   1632    714    377       C  
ATOM   1728  N   GLU A 223      15.875   3.716  -4.731  1.00 55.37           N  
ANISOU 1728  N   GLU A 223     7635   6489   6914   1640    752    389       N  
ATOM   1729  CA  GLU A 223      15.383   5.044  -5.067  1.00 60.38           C  
ANISOU 1729  CA  GLU A 223     8264   7117   7561   1644    762    394       C  
ATOM   1730  C   GLU A 223      16.340   5.768  -6.018  1.00 58.84           C  
ANISOU 1730  C   GLU A 223     8077   6935   7343   1643    749    390       C  
ATOM   1731  O   GLU A 223      15.904   6.500  -6.907  1.00 57.95           O  
ANISOU 1731  O   GLU A 223     7952   6820   7245   1647    744    392       O  
ATOM   1732  CB  GLU A 223      15.102   5.867  -3.805  1.00 67.80           C  
ANISOU 1732  CB  GLU A 223     9215   8046   8499   1643    794    401       C  
ATOM   1733  CG  GLU A 223      13.762   6.591  -3.851  1.00 77.67           C  
ANISOU 1733  CG  GLU A 223    10448   9281   9784   1649    808    408       C  
ATOM   1734  CD  GLU A 223      13.463   7.345  -2.575  1.00 89.13           C  
ANISOU 1734  CD  GLU A 223    11910  10722  11234   1648    840    415       C  
ATOM   1735  OE1 GLU A 223      13.984   6.928  -1.516  1.00 93.02           O  
ANISOU 1735  OE1 GLU A 223    12420  11215  11708   1644    851    414       O  
ATOM   1736  OE2 GLU A 223      12.714   8.352  -2.631  1.00 90.74           O1-
ANISOU 1736  OE2 GLU A 223    12105  10915  11455   1652    853    420       O1-
ATOM   1737  N   GLY A 224      17.640   5.546  -5.834  1.00 60.93           N  
ANISOU 1737  N   GLY A 224     8363   7214   7573   1638    743    386       N  
ATOM   1738  CA  GLY A 224      18.657   6.076  -6.730  1.00 57.42           C  
ANISOU 1738  CA  GLY A 224     7928   6784   7105   1637    728    381       C  
ATOM   1739  C   GLY A 224      18.376   5.661  -8.162  1.00 48.91           C  
ANISOU 1739  C   GLY A 224     6830   5710   6042   1640    701    377       C  
ATOM   1740  O   GLY A 224      18.356   6.496  -9.075  1.00 46.91           O  
ANISOU 1740  O   GLY A 224     6571   5460   5792   1643    695    378       O  
ATOM   1741  N   ILE A 225      18.132   4.366  -8.344  1.00 44.47           N  
ANISOU 1741  N   ILE A 225     6257   5149   5490   1639    686    374       N  
ATOM   1742  CA  ILE A 225      17.778   3.818  -9.648  1.00 52.84           C  
ANISOU 1742  CA  ILE A 225     7297   6213   6567   1642    660    370       C  
ATOM   1743  C   ILE A 225      16.579   4.553 -10.219  1.00 60.90           C  
ANISOU 1743  C   ILE A 225     8296   7221   7621   1648    664    376       C  
ATOM   1744  O   ILE A 225      16.572   4.931 -11.392  1.00 59.06           O  
ANISOU 1744  O   ILE A 225     8053   6993   7394   1650    648    374       O  
ATOM   1745  CB  ILE A 225      17.436   2.311  -9.571  1.00 52.54           C  
ANISOU 1745  CB  ILE A 225     7248   6173   6541   1641    647    367       C  
ATOM   1746  CG1 ILE A 225      18.607   1.518  -8.982  1.00 55.93           C  
ANISOU 1746  CG1 ILE A 225     7699   6614   6938   1635    643    362       C  
ATOM   1747  CG2 ILE A 225      17.054   1.768 -10.951  1.00 48.48           C  
ANISOU 1747  CG2 ILE A 225     6713   5663   6046   1643    620    364       C  
ATOM   1748  CD1 ILE A 225      19.820   1.433  -9.887  1.00 58.76           C  
ANISOU 1748  CD1 ILE A 225     8067   6991   7267   1632    622    355       C  
ATOM   1749  N   PHE A 226      15.565   4.753  -9.379  1.00 65.23           N  
ANISOU 1749  N   PHE A 226     8837   7754   8193   1650    685    382       N  
ATOM   1750  CA  PHE A 226      14.377   5.498  -9.805  1.00 61.94           C  
ANISOU 1750  CA  PHE A 226     8401   7324   7808   1656    691    388       C  
ATOM   1751  C   PHE A 226      14.682   6.927 -10.296  1.00 57.49           C  
ANISOU 1751  C   PHE A 226     7843   6764   7236   1658    696    390       C  
ATOM   1752  O   PHE A 226      14.217   7.339 -11.362  1.00 57.50           O  
ANISOU 1752  O   PHE A 226     7828   6764   7254   1662    684    391       O  
ATOM   1753  CB  PHE A 226      13.334   5.513  -8.691  1.00 63.78           C  
ANISOU 1753  CB  PHE A 226     8629   7541   8063   1658    715    395       C  
ATOM   1754  CG  PHE A 226      12.642   4.194  -8.497  1.00 68.55           C  
ANISOU 1754  CG  PHE A 226     9219   8139   8688   1658    707    394       C  
ATOM   1755  CD1 PHE A 226      11.882   3.643  -9.517  1.00 70.93           C  
ANISOU 1755  CD1 PHE A 226     9496   8438   9016   1661    686    393       C  
ATOM   1756  CD2 PHE A 226      12.739   3.511  -7.295  1.00 68.67           C  
ANISOU 1756  CD2 PHE A 226     9244   8151   8695   1654    720    394       C  
ATOM   1757  CE1 PHE A 226      11.238   2.435  -9.349  1.00 72.05           C  
ANISOU 1757  CE1 PHE A 226     9625   8574   9176   1661    679    393       C  
ATOM   1758  CE2 PHE A 226      12.095   2.304  -7.122  1.00 69.92           C  
ANISOU 1758  CE2 PHE A 226     9390   8305   8873   1654    713    394       C  
ATOM   1759  CZ  PHE A 226      11.347   1.762  -8.149  1.00 74.09           C  
ANISOU 1759  CZ  PHE A 226     9894   8829   9427   1658    692    393       C  
ATOM   1760  N   GLU A 227      15.463   7.675  -9.521  1.00 53.16           N  
ANISOU 1760  N   GLU A 227     7318   6220   6662   1655    714    391       N  
ATOM   1761  CA  GLU A 227      15.876   9.012  -9.925  1.00 52.37           C  
ANISOU 1761  CA  GLU A 227     7225   6123   6550   1656    719    393       C  
ATOM   1762  C   GLU A 227      16.567   8.973 -11.289  1.00 49.96           C  
ANISOU 1762  C   GLU A 227     6917   5832   6233   1656    692    387       C  
ATOM   1763  O   GLU A 227      16.248   9.776 -12.177  1.00 47.33           O  
ANISOU 1763  O   GLU A 227     6573   5498   5912   1660    687    389       O  
ATOM   1764  CB  GLU A 227      16.799   9.625  -8.873  1.00 55.55           C  
ANISOU 1764  CB  GLU A 227     7655   6530   6923   1652    739    394       C  
ATOM   1765  CG  GLU A 227      17.224  11.059  -9.170  1.00 59.88           C  
ANISOU 1765  CG  GLU A 227     8212   7080   7459   1654    747    396       C  
ATOM   1766  CD  GLU A 227      16.412  12.082  -8.404  1.00 61.31           C  
ANISOU 1766  CD  GLU A 227     8392   7246   7655   1656    774    404       C  
ATOM   1767  OE1 GLU A 227      15.503  11.669  -7.661  1.00 62.19           O  
ANISOU 1767  OE1 GLU A 227     8495   7346   7788   1657    787    408       O  
ATOM   1768  OE2 GLU A 227      16.680  13.295  -8.541  1.00 61.64           O1-
ANISOU 1768  OE2 GLU A 227     8442   7290   7690   1657    783    406       O1-
ATOM   1769  N   ILE A 228      17.503   8.032 -11.445  1.00 49.32           N  
ANISOU 1769  N   ILE A 228     6845   5764   6130   1652    675    380       N  
ATOM   1770  CA  ILE A 228      18.188   7.804 -12.718  1.00 47.30           C  
ANISOU 1770  CA  ILE A 228     6587   5522   5862   1652    648    374       C  
ATOM   1771  C   ILE A 228      17.193   7.562 -13.849  1.00 45.11           C  
ANISOU 1771  C   ILE A 228     6282   5240   5618   1656    632    375       C  
ATOM   1772  O   ILE A 228      17.347   8.099 -14.949  1.00 44.80           O  
ANISOU 1772  O   ILE A 228     6237   5206   5578   1658    618    373       O  
ATOM   1773  CB  ILE A 228      19.116   6.577 -12.647  1.00 54.19           C  
ANISOU 1773  CB  ILE A 228     7471   6408   6711   1647    633    367       C  
ATOM   1774  CG1 ILE A 228      20.459   6.928 -12.034  1.00 59.13           C  
ANISOU 1774  CG1 ILE A 228     8126   7046   7297   1642    640    364       C  
ATOM   1775  CG2 ILE A 228      19.405   6.028 -14.025  1.00 57.25           C  
ANISOU 1775  CG2 ILE A 228     7848   6807   7099   1647    603    361       C  
ATOM   1776  CD1 ILE A 228      21.380   5.726 -12.009  1.00 63.15           C  
ANISOU 1776  CD1 ILE A 228     8644   7567   7782   1637    624    357       C  
ATOM   1777  N   ILE A 229      16.178   6.744 -13.582  1.00 46.28           N  
ANISOU 1777  N   ILE A 229     6414   5377   5794   1658    632    377       N  
ATOM   1778  CA  ILE A 229      15.177   6.429 -14.599  1.00 55.91           C  
ANISOU 1778  CA  ILE A 229     7607   6591   7046   1662    615    378       C  
ATOM   1779  C   ILE A 229      14.399   7.666 -15.016  1.00 55.51           C  
ANISOU 1779  C   ILE A 229     7544   6530   7016   1667    625    384       C  
ATOM   1780  O   ILE A 229      14.467   8.069 -16.179  1.00 57.37           O  
ANISOU 1780  O   ILE A 229     7772   6772   7255   1670    609    382       O  
ATOM   1781  CB  ILE A 229      14.174   5.352 -14.139  1.00 59.64           C  
ANISOU 1781  CB  ILE A 229     8064   7051   7546   1663    616    379       C  
ATOM   1782  CG1 ILE A 229      14.901   4.056 -13.803  1.00 54.80           C  
ANISOU 1782  CG1 ILE A 229     7461   6448   6914   1658    605    373       C  
ATOM   1783  CG2 ILE A 229      13.115   5.106 -15.218  1.00 55.97           C  
ANISOU 1783  CG2 ILE A 229     7572   6580   7115   1668    599    381       C  
ATOM   1784  CD1 ILE A 229      14.174   3.224 -12.781  1.00 55.27           C  
ANISOU 1784  CD1 ILE A 229     7515   6495   6989   1658    616    376       C  
ATOM   1785  N   GLU A 230      13.677   8.270 -14.070  1.00 55.57           N  
ANISOU 1785  N   GLU A 230     7552   6524   7036   1669    650    390       N  
ATOM   1786  CA  GLU A 230      12.900   9.477 -14.369  1.00 60.08           C  
ANISOU 1786  CA  GLU A 230     8114   7087   7628   1674    661    397       C  
ATOM   1787  C   GLU A 230      13.712  10.604 -15.022  1.00 56.48           C  
ANISOU 1787  C   GLU A 230     7668   6640   7152   1675    659    395       C  
ATOM   1788  O   GLU A 230      13.169  11.369 -15.830  1.00 62.44           O  
ANISOU 1788  O   GLU A 230     8409   7391   7923   1679    655    399       O  
ATOM   1789  CB  GLU A 230      12.105   9.976 -13.155  1.00 64.21           C  
ANISOU 1789  CB  GLU A 230     8638   7594   8164   1676    691    404       C  
ATOM   1790  CG  GLU A 230      10.660   9.469 -13.163  1.00 73.16           C  
ANISOU 1790  CG  GLU A 230     9748   8713   9337   1680    691    408       C  
ATOM   1791  CD  GLU A 230       9.637  10.533 -12.776  1.00 82.92           C  
ANISOU 1791  CD  GLU A 230    10975   9934  10595   1685    713    416       C  
ATOM   1792  OE1 GLU A 230       9.893  11.291 -11.810  1.00 86.04           O  
ANISOU 1792  OE1 GLU A 230    11387  10326  10977   1683    738    419       O  
ATOM   1793  OE2 GLU A 230       8.574  10.605 -13.440  1.00 82.52           O1-
ANISOU 1793  OE2 GLU A 230    10902   9875  10576   1690    707    420       O1-
ATOM   1794  N   ILE A 231      15.005  10.694 -14.705  1.00 46.58           N  
ANISOU 1794  N   ILE A 231     6438   5399   5862   1670    659    391       N  
ATOM   1795  CA  ILE A 231      15.862  11.624 -15.436  1.00 43.82           C  
ANISOU 1795  CA  ILE A 231     6098   5060   5491   1670    653    389       C  
ATOM   1796  C   ILE A 231      16.132  11.183 -16.877  1.00 47.26           C  
ANISOU 1796  C   ILE A 231     6523   5508   5928   1670    623    384       C  
ATOM   1797  O   ILE A 231      15.777  11.895 -17.816  1.00 53.83           O  
ANISOU 1797  O   ILE A 231     7343   6338   6772   1674    617    386       O  
ATOM   1798  CB  ILE A 231      17.224  11.880 -14.755  1.00 37.44           C  
ANISOU 1798  CB  ILE A 231     5319   4265   4643   1665    662    386       C  
ATOM   1799  CG1 ILE A 231      17.052  12.504 -13.378  1.00 32.05           C  
ANISOU 1799  CG1 ILE A 231     4649   3571   3957   1664    692    392       C  
ATOM   1800  CG2 ILE A 231      18.089  12.809 -15.621  1.00 31.17           C  
ANISOU 1800  CG2 ILE A 231     4533   3482   3828   1665    653    384       C  
ATOM   1801  CD1 ILE A 231      18.358  13.079 -12.852  1.00 27.61           C  
ANISOU 1801  CD1 ILE A 231     4114   3020   3356   1660    700    390       C  
ATOM   1802  N   TYR A 232      16.753  10.017 -17.061  1.00 43.27           N  
ANISOU 1802  N   TYR A 232     6021   5012   5408   1667    606    377       N  
ATOM   1803  CA  TYR A 232      17.266   9.658 -18.385  1.00 41.94           C  
ANISOU 1803  CA  TYR A 232     5847   4857   5233   1666    578    372       C  
ATOM   1804  C   TYR A 232      16.279   8.865 -19.243  1.00 45.60           C  
ANISOU 1804  C   TYR A 232     6283   5314   5728   1669    559    372       C  
ATOM   1805  O   TYR A 232      16.533   8.657 -20.439  1.00 49.94           O  
ANISOU 1805  O   TYR A 232     6826   5873   6277   1670    536    368       O  
ATOM   1806  CB  TYR A 232      18.637   8.958 -18.291  1.00 42.08           C  
ANISOU 1806  CB  TYR A 232     5884   4891   5213   1661    566    364       C  
ATOM   1807  CG  TYR A 232      19.670   9.764 -17.532  1.00 39.99           C  
ANISOU 1807  CG  TYR A 232     5647   4633   4915   1658    583    364       C  
ATOM   1808  CD1 TYR A 232      19.744   9.695 -16.149  1.00 37.43           C  
ANISOU 1808  CD1 TYR A 232     5336   4303   4583   1655    605    366       C  
ATOM   1809  CD2 TYR A 232      20.564  10.602 -18.196  1.00 41.99           C  
ANISOU 1809  CD2 TYR A 232     5911   4899   5146   1657    577    362       C  
ATOM   1810  CE1 TYR A 232      20.668  10.440 -15.442  1.00 37.59           C  
ANISOU 1810  CE1 TYR A 232     5381   4329   4574   1653    620    367       C  
ATOM   1811  CE2 TYR A 232      21.496  11.352 -17.496  1.00 41.40           C  
ANISOU 1811  CE2 TYR A 232     5860   4829   5040   1655    592    362       C  
ATOM   1812  CZ  TYR A 232      21.536  11.263 -16.116  1.00 45.01           C  
ANISOU 1812  CZ  TYR A 232     6330   5280   5491   1652    613    365       C  
ATOM   1813  OH  TYR A 232      22.446  11.991 -15.389  1.00 54.07           O  
ANISOU 1813  OH  TYR A 232     7502   6432   6609   1649    628    365       O  
ATOM   1814  N   ASP A 233      15.153   8.467 -18.643  1.00 45.71           N  
ANISOU 1814  N   ASP A 233     6285   5313   5771   1672    569    376       N  
ATOM   1815  CA  ASP A 233      14.109   7.685 -19.331  1.00 57.90           C  
ANISOU 1815  CA  ASP A 233     7802   6849   7348   1674    553    377       C  
ATOM   1816  C   ASP A 233      14.746   6.527 -20.105  1.00 57.81           C  
ANISOU 1816  C   ASP A 233     7789   6850   7325   1671    525    369       C  
ATOM   1817  O   ASP A 233      14.737   6.500 -21.347  1.00 55.62           O  
ANISOU 1817  O   ASP A 233     7501   6579   7055   1673    504    367       O  
ATOM   1818  CB  ASP A 233      13.252   8.569 -20.261  1.00 62.64           C  
ANISOU 1818  CB  ASP A 233     8384   7442   7974   1680    549    382       C  
ATOM   1819  CG  ASP A 233      11.890   7.945 -20.596  1.00 61.23           C  
ANISOU 1819  CG  ASP A 233     8179   7251   7836   1684    541    385       C  
ATOM   1820  OD1 ASP A 233      11.135   7.584 -19.661  1.00 60.56           O  
ANISOU 1820  OD1 ASP A 233     8089   7154   7767   1685    556    389       O  
ATOM   1821  OD2 ASP A 233      11.577   7.824 -21.800  1.00 59.97           O1-
ANISOU 1821  OD2 ASP A 233     8002   7093   7690   1686    521    384       O1-
ATOM   1822  N   LYS A 234      15.309   5.593 -19.341  1.00 53.10           N  
ANISOU 1822  N   LYS A 234     7205   6259   6712   1667    526    366       N  
ATOM   1823  CA  LYS A 234      16.177   4.549 -19.860  1.00 49.58           C  
ANISOU 1823  CA  LYS A 234     6764   5827   6246   1663    504    358       C  
ATOM   1824  C   LYS A 234      15.829   3.237 -19.180  1.00 52.84           C  
ANISOU 1824  C   LYS A 234     7173   6235   6668   1661    502    357       C  
ATOM   1825  O   LYS A 234      15.659   3.188 -17.952  1.00 50.39           O  
ANISOU 1825  O   LYS A 234     6871   5917   6357   1659    523    359       O  
ATOM   1826  CB  LYS A 234      17.640   4.903 -19.568  1.00 44.78           C  
ANISOU 1826  CB  LYS A 234     6185   5235   5596   1658    507    353       C  
ATOM   1827  CG  LYS A 234      18.560   4.806 -20.774  1.00 44.36           C  
ANISOU 1827  CG  LYS A 234     6134   5198   5522   1657    483    347       C  
ATOM   1828  CD  LYS A 234      18.921   6.179 -21.332  1.00 45.14           C  
ANISOU 1828  CD  LYS A 234     6238   5301   5611   1659    487    348       C  
ATOM   1829  CE  LYS A 234      19.313   6.085 -22.805  1.00 45.16           C  
ANISOU 1829  CE  LYS A 234     6234   5316   5610   1659    461    343       C  
ATOM   1830  NZ  LYS A 234      20.095   7.266 -23.271  1.00 46.82           N1+
ANISOU 1830  NZ  LYS A 234     6456   5535   5797   1660    462    343       N1+
ATOM   1831  N   ALA A 235      15.717   2.174 -19.975  1.00 53.46           N  
ANISOU 1831  N   ALA A 235     7238   6317   6756   1660    478    352       N  
ATOM   1832  CA  ALA A 235      15.422   0.846 -19.433  1.00 45.81           C  
ANISOU 1832  CA  ALA A 235     6266   5345   5797   1658    474    351       C  
ATOM   1833  C   ALA A 235      16.574   0.320 -18.570  1.00 48.87           C  
ANISOU 1833  C   ALA A 235     6678   5743   6149   1652    479    346       C  
ATOM   1834  O   ALA A 235      17.741   0.472 -18.921  1.00 47.70           O  
ANISOU 1834  O   ALA A 235     6545   5609   5969   1649    471    340       O  
ATOM   1835  CB  ALA A 235      15.098  -0.135 -20.552  1.00 32.13           C  
ANISOU 1835  CB  ALA A 235     4514   3615   4081   1658    446    347       C  
ATOM   1836  N   ILE A 236      16.236  -0.287 -17.436  1.00 49.87           N  
ANISOU 1836  N   ILE A 236     6807   5861   6281   1651    493    348       N  
ATOM   1837  CA  ILE A 236      17.220  -0.964 -16.600  1.00 44.59           C  
ANISOU 1837  CA  ILE A 236     6158   5201   5582   1645    496    343       C  
ATOM   1838  C   ILE A 236      16.932  -2.458 -16.568  1.00 48.45           C  
ANISOU 1838  C   ILE A 236     6638   5689   6083   1643    482    340       C  
ATOM   1839  O   ILE A 236      15.835  -2.861 -16.191  1.00 47.85           O  
ANISOU 1839  O   ILE A 236     6546   5599   6037   1646    488    344       O  
ATOM   1840  CB  ILE A 236      17.151  -0.494 -15.158  1.00 41.21           C  
ANISOU 1840  CB  ILE A 236     5745   4765   5148   1645    525    348       C  
ATOM   1841  CG1 ILE A 236      17.025   1.027 -15.076  1.00 38.31           C  
ANISOU 1841  CG1 ILE A 236     5382   4394   4780   1648    543    353       C  
ATOM   1842  CG2 ILE A 236      18.360  -1.005 -14.392  1.00 45.01           C  
ANISOU 1842  CG2 ILE A 236     6251   5258   5593   1639    528    343       C  
ATOM   1843  CD1 ILE A 236      18.265   1.775 -15.461  1.00 35.38           C  
ANISOU 1843  CD1 ILE A 236     5031   4038   4376   1646    540    349       C  
ATOM   1844  N   ILE A 237      17.907  -3.281 -16.957  1.00 50.16           N  
ANISOU 1844  N   ILE A 237     6863   5920   6276   1639    463    333       N  
ATOM   1845  CA  ILE A 237      17.747  -4.730 -16.853  1.00 46.66           C  
ANISOU 1845  CA  ILE A 237     6413   5476   5840   1637    451    329       C  
ATOM   1846  C   ILE A 237      18.376  -5.238 -15.561  1.00 52.65           C  
ANISOU 1846  C   ILE A 237     7192   6237   6577   1633    464    328       C  
ATOM   1847  O   ILE A 237      19.500  -4.864 -15.212  1.00 48.73           O  
ANISOU 1847  O   ILE A 237     6717   5751   6045   1630    470    325       O  
ATOM   1848  CB  ILE A 237      18.353  -5.477 -18.039  1.00 41.83           C  
ANISOU 1848  CB  ILE A 237     5798   4878   5219   1635    421    322       C  
ATOM   1849  CG1 ILE A 237      17.952  -4.812 -19.347  1.00 39.64           C  
ANISOU 1849  CG1 ILE A 237     5504   4600   4957   1639    408    323       C  
ATOM   1850  CG2 ILE A 237      17.905  -6.927 -18.039  1.00 42.26           C  
ANISOU 1850  CG2 ILE A 237     5839   4929   5290   1634    408    320       C  
ATOM   1851  CD1 ILE A 237      18.193  -5.679 -20.547  1.00 37.41           C  
ANISOU 1851  CD1 ILE A 237     5212   4328   4676   1637    379    317       C  
ATOM   1852  N   PHE A 238      17.643  -6.097 -14.858  1.00 58.04           N  
ANISOU 1852  N   PHE A 238     7865   6909   7279   1633    470    330       N  
ATOM   1853  CA  PHE A 238      18.034  -6.513 -13.526  1.00 60.73           C  
ANISOU 1853  CA  PHE A 238     8223   7249   7603   1629    486    330       C  
ATOM   1854  C   PHE A 238      17.992  -8.026 -13.381  1.00 66.72           C  
ANISOU 1854  C   PHE A 238     8977   8008   8367   1627    473    326       C  
ATOM   1855  O   PHE A 238      16.921  -8.601 -13.176  1.00 71.61           O  
ANISOU 1855  O   PHE A 238     9577   8614   9016   1629    474    330       O  
ATOM   1856  CB  PHE A 238      17.089  -5.878 -12.511  1.00 62.79           C  
ANISOU 1856  CB  PHE A 238     8480   7493   7883   1632    513    338       C  
ATOM   1857  CG  PHE A 238      17.575  -5.946 -11.097  1.00 65.25           C  
ANISOU 1857  CG  PHE A 238     8813   7805   8176   1629    534    339       C  
ATOM   1858  CD1 PHE A 238      18.881  -6.290 -10.811  1.00 68.24           C  
ANISOU 1858  CD1 PHE A 238     9213   8197   8516   1624    530    333       C  
ATOM   1859  CD2 PHE A 238      16.719  -5.666 -10.048  1.00 65.13           C  
ANISOU 1859  CD2 PHE A 238     8795   7774   8178   1631    558    346       C  
ATOM   1860  CE1 PHE A 238      19.329  -6.350  -9.496  1.00 70.30           C  
ANISOU 1860  CE1 PHE A 238     9494   8458   8759   1621    549    334       C  
ATOM   1861  CE2 PHE A 238      17.161  -5.726  -8.738  1.00 66.59           C  
ANISOU 1861  CE2 PHE A 238     8999   7958   8344   1628    578    347       C  
ATOM   1862  CZ  PHE A 238      18.469  -6.066  -8.461  1.00 65.85           C  
ANISOU 1862  CZ  PHE A 238     8928   7879   8213   1622    573    341       C  
ATOM   1863  N   SER A 239      19.152  -8.670 -13.495  1.00 66.00           N  
ANISOU 1863  N   SER A 239     8900   7932   8245   1622    460    319       N  
ATOM   1864  CA  SER A 239      19.265 -10.076 -13.127  1.00 65.77           C  
ANISOU 1864  CA  SER A 239     8871   7905   8215   1619    451    315       C  
ATOM   1865  C   SER A 239      19.318 -10.149 -11.603  1.00 64.77           C  
ANISOU 1865  C   SER A 239     8758   7771   8079   1617    475    318       C  
ATOM   1866  O   SER A 239      20.093  -9.436 -10.945  1.00 58.48           O  
ANISOU 1866  O   SER A 239     7984   6981   7256   1615    490    319       O  
ATOM   1867  CB  SER A 239      20.491 -10.732 -13.758  1.00 65.99           C  
ANISOU 1867  CB  SER A 239     8910   7951   8212   1615    429    307       C  
ATOM   1868  OG  SER A 239      21.681 -10.124 -13.292  1.00 68.16           O  
ANISOU 1868  OG  SER A 239     9212   8238   8449   1612    438    304       O  
ATOM   1869  N   ILE A 240      18.470 -11.005 -11.049  1.00 63.95           N  
ANISOU 1869  N   ILE A 240     8643   7656   8000   1617    478    321       N  
ATOM   1870  CA  ILE A 240      18.221 -10.993  -9.626  1.00 66.21           C  
ANISOU 1870  CA  ILE A 240     8939   7933   8286   1617    503    325       C  
ATOM   1871  C   ILE A 240      18.317 -12.397  -9.026  1.00 72.44           C  
ANISOU 1871  C   ILE A 240     9728   8721   9073   1613    498    322       C  
ATOM   1872  O   ILE A 240      17.487 -13.267  -9.289  1.00 75.30           O  
ANISOU 1872  O   ILE A 240    10071   9076   9463   1614    488    323       O  
ATOM   1873  CB  ILE A 240      16.862 -10.296  -9.322  1.00 68.30           C  
ANISOU 1873  CB  ILE A 240     9187   8179   8585   1622    521    334       C  
ATOM   1874  CG1 ILE A 240      16.589 -10.237  -7.825  1.00 66.40           C  
ANISOU 1874  CG1 ILE A 240     8956   7929   8344   1621    548    338       C  
ATOM   1875  CG2 ILE A 240      15.706 -10.971 -10.056  1.00 70.06           C  
ANISOU 1875  CG2 ILE A 240     9381   8392   8846   1625    505    335       C  
ATOM   1876  CD1 ILE A 240      15.418  -9.360  -7.487  1.00 62.50           C  
ANISOU 1876  CD1 ILE A 240     8450   7419   7878   1626    568    347       C  
ATOM   1877  N   HIS A 241      19.365 -12.614  -8.240  1.00 76.23           N  
ANISOU 1877  N   HIS A 241    10232   9212   9521   1609    505    319       N  
ATOM   1878  CA  HIS A 241      19.553 -13.877  -7.539  1.00 82.37           C  
ANISOU 1878  CA  HIS A 241    11014   9989  10293   1605    502    317       C  
ATOM   1879  C   HIS A 241      18.503 -14.017  -6.438  1.00 82.54           C  
ANISOU 1879  C   HIS A 241    11028   9994  10340   1607    524    324       C  
ATOM   1880  O   HIS A 241      17.907 -13.015  -6.034  1.00 78.57           O  
ANISOU 1880  O   HIS A 241    10524   9481   9848   1610    544    330       O  
ATOM   1881  CB  HIS A 241      20.974 -13.957  -6.980  1.00 85.53           C  
ANISOU 1881  CB  HIS A 241    11443  10405  10651   1600    505    312       C  
ATOM   1882  CG  HIS A 241      21.982 -14.426  -7.977  1.00 84.98           C  
ANISOU 1882  CG  HIS A 241    11378  10352  10558   1597    479    304       C  
ATOM   1883  CD2 HIS A 241      23.205 -14.981  -7.821  1.00 86.12           C  
ANISOU 1883  CD2 HIS A 241    11541  10511  10668   1593    471    298       C  
ATOM   1884  ND1 HIS A 241      21.764 -14.362  -9.340  1.00 84.91           N  
ANISOU 1884  ND1 HIS A 241    11353  10346  10562   1600    458    301       N  
ATOM   1885  CE1 HIS A 241      22.811 -14.849  -9.975  1.00 86.28           C  
ANISOU 1885  CE1 HIS A 241    11536  10537  10710   1596    439    294       C  
ATOM   1886  NE2 HIS A 241      23.703 -15.233  -9.075  1.00 88.48           N  
ANISOU 1886  NE2 HIS A 241    11836  10822  10959   1592    446    291       N  
ATOM   1887  N   PRO A 242      18.258 -15.257  -5.964  1.00 85.72           N  
ANISOU 1887  N   PRO A 242    11426  10393  10752   1605    520    322       N  
ATOM   1888  CA  PRO A 242      17.197 -15.489  -4.974  1.00 88.72           C  
ANISOU 1888  CA  PRO A 242    11797  10755  11156   1607    538    329       C  
ATOM   1889  C   PRO A 242      17.337 -14.629  -3.711  1.00 92.69           C  
ANISOU 1889  C   PRO A 242    12318  11255  11646   1606    568    334       C  
ATOM   1890  O   PRO A 242      16.337 -14.082  -3.216  1.00 93.00           O  
ANISOU 1890  O   PRO A 242    12348  11279  11708   1610    587    340       O  
ATOM   1891  CB  PRO A 242      17.371 -16.970  -4.626  1.00 88.05           C  
ANISOU 1891  CB  PRO A 242    11712  10673  11070   1603    528    325       C  
ATOM   1892  CG  PRO A 242      17.983 -17.568  -5.835  1.00 87.42           C  
ANISOU 1892  CG  PRO A 242    11629  10607  10982   1602    498    318       C  
ATOM   1893  CD  PRO A 242      18.913 -16.518  -6.361  1.00 86.51           C  
ANISOU 1893  CD  PRO A 242    11527  10503  10839   1601    497    315       C  
ATOM   1894  N   ARG A 243      18.564 -14.506  -3.210  1.00 92.70           N  
ANISOU 1894  N   ARG A 243    12345  11268  11610   1602    573    330       N  
ATOM   1895  CA  ARG A 243      18.821 -13.754  -1.985  1.00 90.88           C  
ANISOU 1895  CA  ARG A 243    12134  11034  11364   1601    600    335       C  
ATOM   1896  C   ARG A 243      18.321 -12.315  -2.046  1.00 88.74           C  
ANISOU 1896  C   ARG A 243    11860  10756  11102   1604    617    341       C  
ATOM   1897  O   ARG A 243      17.696 -11.825  -1.102  1.00 91.78           O  
ANISOU 1897  O   ARG A 243    12245  11128  11497   1606    641    347       O  
ATOM   1898  CB  ARG A 243      20.306 -13.752  -1.660  1.00 94.27           C  
ANISOU 1898  CB  ARG A 243    12590  11480  11750   1596    599    330       C  
ATOM   1899  CG  ARG A 243      20.590 -13.196  -0.291  1.00101.69           C  
ANISOU 1899  CG  ARG A 243    13550  12415  12673   1593    626    334       C  
ATOM   1900  CD  ARG A 243      21.917 -13.690   0.213  1.00110.08           C  
ANISOU 1900  CD  ARG A 243    14637  13492  13698   1588    623    330       C  
ATOM   1901  NE  ARG A 243      23.023 -13.036  -0.470  1.00113.86           N  
ANISOU 1901  NE  ARG A 243    15130  13986  14147   1586    612    326       N  
ATOM   1902  CZ  ARG A 243      23.620 -11.943  -0.014  1.00117.56           C  
ANISOU 1902  CZ  ARG A 243    15617  14458  14594   1585    628    328       C  
ATOM   1903  NH1 ARG A 243      23.210 -11.394   1.122  1.00118.90           N1+
ANISOU 1903  NH1 ARG A 243    15794  14616  14768   1585    655    335       N1+
ATOM   1904  NH2 ARG A 243      24.626 -11.403  -0.686  1.00119.60           N  
ANISOU 1904  NH2 ARG A 243    15887  14730  14825   1584    617    324       N  
ATOM   1905  N   THR A 244      18.601 -11.639  -3.156  1.00 83.34           N  
ANISOU 1905  N   THR A 244    11173  10079  10414   1606    604    338       N  
ATOM   1906  CA  THR A 244      18.168 -10.259  -3.331  1.00 72.90           C  
ANISOU 1906  CA  THR A 244     9847   8751   9100   1610    617    343       C  
ATOM   1907  C   THR A 244      16.650 -10.142  -3.288  1.00 75.88           C  
ANISOU 1907  C   THR A 244    10201   9110   9518   1615    626    350       C  
ATOM   1908  O   THR A 244      16.131  -9.358  -2.498  1.00 77.85           O  
ANISOU 1908  O   THR A 244    10454   9350   9776   1617    650    356       O  
ATOM   1909  CB  THR A 244      18.717  -9.629  -4.628  1.00 65.79           C  
ANISOU 1909  CB  THR A 244     8946   7862   8189   1611    599    340       C  
ATOM   1910  CG2 THR A 244      17.971  -8.352  -4.965  1.00 65.75           C  
ANISOU 1910  CG2 THR A 244     8930   7847   8203   1616    610    345       C  
ATOM   1911  OG1 THR A 244      20.093  -9.292  -4.445  1.00 64.35           O  
ANISOU 1911  OG1 THR A 244     8789   7695   7968   1607    600    336       O  
ATOM   1912  N   LYS A 245      15.945 -10.919  -4.119  1.00 74.77           N  
ANISOU 1912  N   LYS A 245    10038   8966   9404   1617    607    348       N  
ATOM   1913  CA  LYS A 245      14.473 -10.900  -4.143  1.00 70.47           C  
ANISOU 1913  CA  LYS A 245     9470   8405   8900   1622    613    354       C  
ATOM   1914  C   LYS A 245      13.890 -11.171  -2.750  1.00 67.23           C  
ANISOU 1914  C   LYS A 245     9063   7983   8499   1622    636    359       C  
ATOM   1915  O   LYS A 245      12.888 -10.558  -2.360  1.00 57.41           O  
ANISOU 1915  O   LYS A 245     7811   6726   7278   1625    654    366       O  
ATOM   1916  CB  LYS A 245      13.902 -11.873  -5.193  1.00 70.21           C  
ANISOU 1916  CB  LYS A 245     9414   8371   8892   1624    586    351       C  
ATOM   1917  CG  LYS A 245      12.374 -11.965  -5.199  1.00 71.72           C  
ANISOU 1917  CG  LYS A 245     9580   8545   9125   1629    591    357       C  
ATOM   1918  CD  LYS A 245      11.813 -12.608  -6.469  1.00 78.47           C  
ANISOU 1918  CD  LYS A 245    10412   9399  10004   1631    564    355       C  
ATOM   1919  CE  LYS A 245      10.267 -12.682  -6.420  1.00 84.69           C  
ANISOU 1919  CE  LYS A 245    11175  10169  10833   1636    569    362       C  
ATOM   1920  NZ  LYS A 245       9.588 -13.021  -7.724  1.00 83.69           N1+
ANISOU 1920  NZ  LYS A 245    11025  10041  10734   1639    544    361       N1+
ATOM   1921  N   LYS A 246      14.533 -12.073  -2.001  1.00 75.54           N  
ANISOU 1921  N   LYS A 246    10129   9041   9533   1617    637    356       N  
ATOM   1922  CA  LYS A 246      14.231 -12.240  -0.576  1.00 81.49           C  
ANISOU 1922  CA  LYS A 246    10891   9785  10287   1616    662    361       C  
ATOM   1923  C   LYS A 246      14.305 -10.894   0.160  1.00 87.10           C  
ANISOU 1923  C   LYS A 246    11616  10492  10987   1616    689    366       C  
ATOM   1924  O   LYS A 246      13.306 -10.417   0.718  1.00 89.10           O  
ANISOU 1924  O   LYS A 246    11861  10731  11262   1620    708    373       O  
ATOM   1925  CB  LYS A 246      15.186 -13.251   0.078  1.00 83.02           C  
ANISOU 1925  CB  LYS A 246    11102   9987  10455   1610    658    356       C  
ATOM   1926  CG  LYS A 246      15.137 -13.267   1.615  1.00 86.14           C  
ANISOU 1926  CG  LYS A 246    11512  10376  10843   1608    685    360       C  
ATOM   1927  CD  LYS A 246      15.994 -14.384   2.225  1.00 86.78           C  
ANISOU 1927  CD  LYS A 246    11607  10465  10901   1603    680    356       C  
ATOM   1928  CE  LYS A 246      15.730 -14.545   3.731  1.00 83.26           C  
ANISOU 1928  CE  LYS A 246    11171  10009  10454   1601    705    361       C  
ATOM   1929  NZ  LYS A 246      16.476 -15.697   4.324  1.00 77.54           N1+
ANISOU 1929  NZ  LYS A 246    10459   9292   9710   1596    700    357       N1+
ATOM   1930  N   ARG A 247      15.482 -10.274   0.135  1.00 88.26           N  
ANISOU 1930  N   ARG A 247    11784  10651  11101   1613    689    363       N  
ATOM   1931  CA  ARG A 247      15.698  -9.022   0.859  1.00 89.18           C  
ANISOU 1931  CA  ARG A 247    11917  10765  11203   1613    714    368       C  
ATOM   1932  C   ARG A 247      14.866  -7.831   0.342  1.00 92.69           C  
ANISOU 1932  C   ARG A 247    12348  11201  11669   1619    722    373       C  
ATOM   1933  O   ARG A 247      14.793  -6.786   0.997  1.00 93.90           O  
ANISOU 1933  O   ARG A 247    12512  11349  11818   1619    745    378       O  
ATOM   1934  CB  ARG A 247      17.187  -8.668   0.873  1.00 87.72           C  
ANISOU 1934  CB  ARG A 247    11756  10595  10976   1609    711    363       C  
ATOM   1935  CG  ARG A 247      18.064  -9.717   1.531  1.00 86.75           C  
ANISOU 1935  CG  ARG A 247    11650  10482  10830   1603    707    359       C  
ATOM   1936  CD  ARG A 247      17.756  -9.831   2.998  1.00 88.01           C  
ANISOU 1936  CD  ARG A 247    11818  10630  10990   1602    732    364       C  
ATOM   1937  NE  ARG A 247      18.643 -10.773   3.668  1.00 92.46           N  
ANISOU 1937  NE  ARG A 247    12399  11202  11529   1597    729    360       N  
ATOM   1938  CZ  ARG A 247      18.878 -10.765   4.977  1.00 97.07           C  
ANISOU 1938  CZ  ARG A 247    12999  11782  12099   1594    750    364       C  
ATOM   1939  NH1 ARG A 247      18.296  -9.856   5.750  1.00 98.28           N1+
ANISOU 1939  NH1 ARG A 247    13156  11925  12262   1595    776    371       N1+
ATOM   1940  NH2 ARG A 247      19.698 -11.659   5.515  1.00 97.55           N  
ANISOU 1940  NH2 ARG A 247    13075  11852  12138   1589    746    360       N  
ATOM   1941  N   LEU A 248      14.238  -7.984  -0.822  1.00 92.43           N  
ANISOU 1941  N   LEU A 248    12293  11166  11660   1622    703    372       N  
ATOM   1942  CA  LEU A 248      13.449  -6.897  -1.407  1.00 93.19           C  
ANISOU 1942  CA  LEU A 248    12376  11255  11778   1627    708    376       C  
ATOM   1943  C   LEU A 248      11.965  -7.031  -1.115  1.00 97.82           C  
ANISOU 1943  C   LEU A 248    12942  11825  12402   1632    719    383       C  
ATOM   1944  O   LEU A 248      11.288  -6.032  -0.873  1.00100.42           O  
ANISOU 1944  O   LEU A 248    13267  12144  12745   1635    737    389       O  
ATOM   1945  CB  LEU A 248      13.665  -6.792  -2.917  1.00 88.81           C  
ANISOU 1945  CB  LEU A 248    11810  10709  11225   1629    682    372       C  
ATOM   1946  CG  LEU A 248      14.892  -6.009  -3.383  1.00 86.12           C  
ANISOU 1946  CG  LEU A 248    11487  10383  10852   1627    676    368       C  
ATOM   1947  CD1 LEU A 248      14.918  -5.970  -4.894  1.00 89.57           C  
ANISOU 1947  CD1 LEU A 248    11910  10826  11296   1629    651    364       C  
ATOM   1948  CD2 LEU A 248      14.907  -4.601  -2.818  1.00 79.97           C  
ANISOU 1948  CD2 LEU A 248    10720   9599  10065   1628    701    373       C  
ATOM   1949  N   LYS A 249      11.450  -8.258  -1.157  1.00 96.95           N  
ANISOU 1949  N   LYS A 249    12818  11711  12310   1632    707    381       N  
ATOM   1950  CA  LYS A 249      10.074  -8.477  -0.734  1.00 89.38           C  
ANISOU 1950  CA  LYS A 249    11841  10735  11385   1636    718    387       C  
ATOM   1951  C   LYS A 249      10.006  -8.274   0.777  1.00 83.69           C  
ANISOU 1951  C   LYS A 249    11135  10008  10657   1634    748    392       C  
ATOM   1952  O   LYS A 249       8.990  -7.824   1.305  1.00 75.54           O  
ANISOU 1952  O   LYS A 249    10094   8961   9645   1637    767    399       O  
ATOM   1953  CB  LYS A 249       9.577  -9.867  -1.145  1.00 87.92           C  
ANISOU 1953  CB  LYS A 249    11637  10547  11219   1636    697    385       C  
ATOM   1954  CG  LYS A 249       9.650 -10.123  -2.644  1.00 87.69           C  
ANISOU 1954  CG  LYS A 249    11594  10526  11199   1638    667    380       C  
ATOM   1955  CD  LYS A 249       8.814 -11.319  -3.083  1.00 91.58           C  
ANISOU 1955  CD  LYS A 249    12064  11012  11720   1639    649    379       C  
ATOM   1956  CE  LYS A 249       7.344 -10.954  -3.245  1.00 95.46           C  
ANISOU 1956  CE  LYS A 249    12533  11488  12249   1645    656    386       C  
ATOM   1957  NZ  LYS A 249       6.587 -12.008  -3.981  1.00 97.91           N1+
ANISOU 1957  NZ  LYS A 249    12820  11793  12587   1647    633    385       N1+
ATOM   1958  N   GLU A 250      11.111  -8.588   1.458  1.00 89.51           N  
ANISOU 1958  N   GLU A 250    11894  10753  11361   1629    751    389       N  
ATOM   1959  CA  GLU A 250      11.230  -8.378   2.905  1.00 93.15           C  
ANISOU 1959  CA  GLU A 250    12373  11209  11810   1626    779    393       C  
ATOM   1960  C   GLU A 250      11.140  -6.896   3.288  1.00 96.42           C  
ANISOU 1960  C   GLU A 250    12797  11620  12221   1628    803    398       C  
ATOM   1961  O   GLU A 250      10.329  -6.510   4.135  1.00 98.71           O  
ANISOU 1961  O   GLU A 250    13084  11896  12524   1629    826    405       O  
ATOM   1962  CB  GLU A 250      12.537  -8.991   3.439  1.00 90.11           C  
ANISOU 1962  CB  GLU A 250    12011  10837  11390   1620    776    387       C  
ATOM   1963  CG  GLU A 250      12.868  -8.629   4.889  1.00 91.48           C  
ANISOU 1963  CG  GLU A 250    12206  11008  11546   1617    804    391       C  
ATOM   1964  CD  GLU A 250      14.162  -9.269   5.381  1.00 95.45           C  
ANISOU 1964  CD  GLU A 250    12732  11523  12014   1610    799    386       C  
ATOM   1965  OE1 GLU A 250      14.721 -10.115   4.651  1.00 99.92           O  
ANISOU 1965  OE1 GLU A 250    13295  12099  12572   1609    774    379       O  
ATOM   1966  OE2 GLU A 250      14.622  -8.928   6.496  1.00 92.79           O1-
ANISOU 1966  OE2 GLU A 250    12415  11185  11657   1607    820    389       O1-
ATOM   1967  N   PHE A 251      11.965  -6.070   2.650  1.00 93.20           N  
ANISOU 1967  N   PHE A 251    12398  11221  11791   1627    796    395       N  
ATOM   1968  CA  PHE A 251      12.051  -4.654   2.990  1.00 88.28           C  
ANISOU 1968  CA  PHE A 251    11787  10596  11161   1628    817    400       C  
ATOM   1969  C   PHE A 251      11.028  -3.774   2.268  1.00 85.37           C  
ANISOU 1969  C   PHE A 251    11398  10218  10820   1634    819    404       C  
ATOM   1970  O   PHE A 251      11.174  -2.552   2.227  1.00 84.64           O  
ANISOU 1970  O   PHE A 251    11313  10126  10721   1635    830    407       O  
ATOM   1971  CB  PHE A 251      13.469  -4.147   2.744  1.00 87.14           C  
ANISOU 1971  CB  PHE A 251    11663  10466  10979   1624    811    395       C  
ATOM   1972  CG  PHE A 251      14.468  -4.659   3.736  1.00 86.04           C  
ANISOU 1972  CG  PHE A 251    11548  10335  10810   1618    817    393       C  
ATOM   1973  CD1 PHE A 251      14.128  -4.789   5.068  1.00 86.68           C  
ANISOU 1973  CD1 PHE A 251    11637  10406  10892   1616    841    398       C  
ATOM   1974  CD2 PHE A 251      15.745  -5.012   3.338  1.00 86.52           C  
ANISOU 1974  CD2 PHE A 251    11623  10411  10840   1614    800    386       C  
ATOM   1975  CE1 PHE A 251      15.042  -5.259   5.989  1.00 88.94           C  
ANISOU 1975  CE1 PHE A 251    11944  10698  11150   1611    847    396       C  
ATOM   1976  CE2 PHE A 251      16.665  -5.481   4.252  1.00 87.79           C  
ANISOU 1976  CE2 PHE A 251    11806  10579  10973   1609    805    384       C  
ATOM   1977  CZ  PHE A 251      16.313  -5.606   5.581  1.00 89.89           C  
ANISOU 1977  CZ  PHE A 251    12079  10835  11241   1607    829    389       C  
ATOM   1978  N   ASN A 252       9.995  -4.404   1.713  1.00 84.79           N  
ANISOU 1978  N   ASN A 252    11300  10137  10778   1637    807    405       N  
ATOM   1979  CA  ASN A 252       8.873  -3.700   1.082  1.00 87.99           C  
ANISOU 1979  CA  ASN A 252    11685  10532  11214   1643    809    410       C  
ATOM   1980  C   ASN A 252       9.259  -2.860  -0.137  1.00 85.97           C  
ANISOU 1980  C   ASN A 252    11426  10284  10953   1645    794    408       C  
ATOM   1981  O   ASN A 252       8.596  -1.871  -0.468  1.00 84.42           O  
ANISOU 1981  O   ASN A 252    11222  10081  10773   1650    802    412       O  
ATOM   1982  CB  ASN A 252       8.114  -2.851   2.111  1.00 92.03           C  
ANISOU 1982  CB  ASN A 252    12199  11030  11736   1645    840    418       C  
ATOM   1983  CG  ASN A 252       7.477  -3.690   3.202  1.00 93.58           C  
ANISOU 1983  CG  ASN A 252    12394  11217  11945   1645    854    422       C  
ATOM   1984  ND2 ASN A 252       6.181  -3.944   3.068  1.00 94.98           N  
ANISOU 1984  ND2 ASN A 252    12549  11382  12157   1649    855    426       N  
ATOM   1985  OD1 ASN A 252       8.142  -4.107   4.154  1.00 92.57           O  
ANISOU 1985  OD1 ASN A 252    12284  11093  11796   1640    864    420       O  
ATOM   1986  N   LEU A 253      10.324  -3.279  -0.814  1.00 84.70           N  
ANISOU 1986  N   LEU A 253    11273  10138  10769   1642    772    400       N  
ATOM   1987  CA  LEU A 253      10.851  -2.543  -1.956  1.00 79.74           C  
ANISOU 1987  CA  LEU A 253    10646   9520  10133   1643    757    397       C  
ATOM   1988  C   LEU A 253      10.523  -3.222  -3.287  1.00 81.73           C  
ANISOU 1988  C   LEU A 253    10876   9775  10403   1646    728    393       C  
ATOM   1989  O   LEU A 253      10.330  -2.555  -4.304  1.00 83.46           O  
ANISOU 1989  O   LEU A 253    11085   9995  10630   1649    718    394       O  
ATOM   1990  CB  LEU A 253      12.361  -2.368  -1.795  1.00 69.55           C  
ANISOU 1990  CB  LEU A 253     9380   8244   8801   1638    755    392       C  
ATOM   1991  CG  LEU A 253      12.757  -1.792  -0.434  1.00 64.96           C  
ANISOU 1991  CG  LEU A 253     8821   7660   8200   1635    783    396       C  
ATOM   1992  CD1 LEU A 253      14.259  -1.722  -0.247  1.00 65.78           C  
ANISOU 1992  CD1 LEU A 253     8951   7779   8263   1630    780    391       C  
ATOM   1993  CD2 LEU A 253      12.141  -0.418  -0.251  1.00 61.36           C  
ANISOU 1993  CD2 LEU A 253     8364   7195   7756   1639    804    403       C  
ATOM   1994  N   PHE A 254      10.448  -4.548  -3.262  1.00 83.09           N  
ANISOU 1994  N   PHE A 254    11041   9948  10580   1644    714    390       N  
ATOM   1995  CA  PHE A 254      10.259  -5.351  -4.466  1.00 87.20           C  
ANISOU 1995  CA  PHE A 254    11545  10473  11116   1645    685    386       C  
ATOM   1996  C   PHE A 254       9.054  -4.899  -5.294  1.00 84.37           C  
ANISOU 1996  C   PHE A 254    11161  10104  10792   1651    680    390       C  
ATOM   1997  O   PHE A 254       9.127  -4.789  -6.527  1.00 83.14           O  
ANISOU 1997  O   PHE A 254    10995   9954  10641   1653    658    387       O  
ATOM   1998  CB  PHE A 254      10.149  -6.839  -4.094  1.00 91.53           C  
ANISOU 1998  CB  PHE A 254    12089  11020  11670   1643    675    383       C  
ATOM   1999  CG  PHE A 254       9.918  -7.751  -5.270  1.00 96.35           C  
ANISOU 1999  CG  PHE A 254    12679  11633  12295   1644    645    379       C  
ATOM   2000  CD1 PHE A 254      10.939  -8.025  -6.167  1.00 97.34           C  
ANISOU 2000  CD1 PHE A 254    12810  11774  12400   1641    622    372       C  
ATOM   2001  CD2 PHE A 254       8.682  -8.344  -5.473  1.00100.89           C  
ANISOU 2001  CD2 PHE A 254    13231  12197  12906   1647    640    382       C  
ATOM   2002  CE1 PHE A 254      10.727  -8.865  -7.254  1.00 99.39           C  
ANISOU 2002  CE1 PHE A 254    13053  12036  12674   1642    595    368       C  
ATOM   2003  CE2 PHE A 254       8.466  -9.189  -6.552  1.00103.78           C  
ANISOU 2003  CE2 PHE A 254    13580  12565  13287   1648    612    378       C  
ATOM   2004  CZ  PHE A 254       9.491  -9.448  -7.445  1.00101.82           C  
ANISOU 2004  CZ  PHE A 254    13337  12332  13018   1645    589    371       C  
ATOM   2005  N   ASP A 255       7.949  -4.621  -4.617  1.00 81.31           N  
ANISOU 2005  N   ASP A 255    10765   9702  10429   1655    699    397       N  
ATOM   2006  CA  ASP A 255       6.734  -4.279  -5.331  1.00 82.17           C  
ANISOU 2006  CA  ASP A 255    10849   9800  10572   1661    695    402       C  
ATOM   2007  C   ASP A 255       6.908  -2.990  -6.130  1.00 77.55           C  
ANISOU 2007  C   ASP A 255    10264   9218   9982   1663    694    402       C  
ATOM   2008  O   ASP A 255       6.423  -2.881  -7.263  1.00 71.71           O  
ANISOU 2008  O   ASP A 255     9507   8478   9262   1667    677    402       O  
ATOM   2009  CB  ASP A 255       5.541  -4.208  -4.376  1.00 88.56           C  
ANISOU 2009  CB  ASP A 255    11650  10592  11405   1663    718    409       C  
ATOM   2010  CG  ASP A 255       4.704  -5.478  -4.399  1.00 90.36           C  
ANISOU 2010  CG  ASP A 255    11861  10814  11660   1665    706    409       C  
ATOM   2011  OD1 ASP A 255       4.738  -6.187  -5.427  1.00 90.67           O  
ANISOU 2011  OD1 ASP A 255    11887  10858  11706   1665    679    405       O  
ATOM   2012  OD2 ASP A 255       4.007  -5.761  -3.399  1.00 90.87           O1-
ANISOU 2012  OD2 ASP A 255    11923  10867  11736   1665    725    414       O1-
ATOM   2013  N   LYS A 256       7.630  -2.036  -5.546  1.00 80.53           N  
ANISOU 2013  N   LYS A 256    10663   9600  10335   1661    712    403       N  
ATOM   2014  CA  LYS A 256       7.932  -0.769  -6.214  1.00 83.87           C  
ANISOU 2014  CA  LYS A 256    11089  10027  10751   1663    713    404       C  
ATOM   2015  C   LYS A 256       8.696  -1.008  -7.524  1.00 80.91           C  
ANISOU 2015  C   LYS A 256    10712   9666  10365   1662    684    397       C  
ATOM   2016  O   LYS A 256       8.494  -0.298  -8.522  1.00 71.74           O  
ANISOU 2016  O   LYS A 256     9541   8506   9212   1665    675    398       O  
ATOM   2017  CB  LYS A 256       8.737   0.146  -5.286  1.00 85.46           C  
ANISOU 2017  CB  LYS A 256    11315  10231  10923   1660    737    406       C  
ATOM   2018  CG  LYS A 256       8.556   1.641  -5.552  1.00 86.37           C  
ANISOU 2018  CG  LYS A 256    11432  10344  11041   1663    749    410       C  
ATOM   2019  CD  LYS A 256       7.956   2.351  -4.337  1.00 86.86           C  
ANISOU 2019  CD  LYS A 256    11499  10393  11109   1664    781    417       C  
ATOM   2020  CE  LYS A 256       8.751   2.045  -3.066  1.00 86.23           C  
ANISOU 2020  CE  LYS A 256    11444  10318  11003   1659    797    416       C  
ATOM   2021  NZ  LYS A 256       8.102   2.592  -1.846  1.00 83.91           N1+
ANISOU 2021  NZ  LYS A 256    11155  10011  10717   1660    828    424       N1+
ATOM   2022  N   LEU A 257       9.561  -2.024  -7.509  1.00 79.51           N  
ANISOU 2022  N   LEU A 257    10544   9500  10168   1657    670    391       N  
ATOM   2023  CA  LEU A 257      10.346  -2.399  -8.680  1.00 74.47           C  
ANISOU 2023  CA  LEU A 257     9904   8875   9516   1656    642    384       C  
ATOM   2024  C   LEU A 257       9.515  -3.097  -9.747  1.00 73.70           C  
ANISOU 2024  C   LEU A 257     9781   8773   9448   1659    618    383       C  
ATOM   2025  O   LEU A 257       9.651  -2.802 -10.932  1.00 69.27           O  
ANISOU 2025  O   LEU A 257     9212   8218   8890   1660    600    381       O  
ATOM   2026  CB  LEU A 257      11.525  -3.283  -8.284  1.00 71.95           C  
ANISOU 2026  CB  LEU A 257     9604   8568   9166   1650    634    378       C  
ATOM   2027  CG  LEU A 257      12.650  -2.617  -7.491  1.00 71.59           C  
ANISOU 2027  CG  LEU A 257     9586   8530   9084   1646    651    377       C  
ATOM   2028  CD1 LEU A 257      13.777  -3.600  -7.269  1.00 71.27           C  
ANISOU 2028  CD1 LEU A 257     9561   8503   9015   1640    640    370       C  
ATOM   2029  CD2 LEU A 257      13.167  -1.382  -8.199  1.00 71.28           C  
ANISOU 2029  CD2 LEU A 257     9553   8498   9032   1647    650    376       C  
ATOM   2030  N   LYS A 258       8.667  -4.033  -9.335  1.00 82.07           N  
ANISOU 2030  N   LYS A 258    10828   9824  10532   1660    618    385       N  
ATOM   2031  CA  LYS A 258       7.751  -4.648 -10.288  1.00 92.22           C  
ANISOU 2031  CA  LYS A 258    12088  11103  11848   1663    598    385       C  
ATOM   2032  C   LYS A 258       6.890  -3.572 -10.946  1.00 96.38           C  
ANISOU 2032  C   LYS A 258    12600  11622  12398   1669    601    391       C  
ATOM   2033  O   LYS A 258       6.558  -3.672 -12.129  1.00 96.32           O  
ANISOU 2033  O   LYS A 258    12576  11616  12407   1671    579    389       O  
ATOM   2034  CB  LYS A 258       6.857  -5.693  -9.613  1.00 98.59           C  
ANISOU 2034  CB  LYS A 258    12883  11899  12678   1663    601    388       C  
ATOM   2035  CG  LYS A 258       7.524  -7.034  -9.349  1.00100.60           C  
ANISOU 2035  CG  LYS A 258    13144  12160  12918   1658    589    382       C  
ATOM   2036  CD  LYS A 258       6.504  -8.174  -9.386  1.00102.57           C  
ANISOU 2036  CD  LYS A 258    13373  12400  13198   1660    578    383       C  
ATOM   2037  CE  LYS A 258       5.307  -7.893  -8.479  1.00102.09           C  
ANISOU 2037  CE  LYS A 258    13304  12323  13162   1664    602    391       C  
ATOM   2038  NZ  LYS A 258       4.372  -9.049  -8.391  1.00 99.98           N1+
ANISOU 2038  NZ  LYS A 258    13019  12046  12922   1665    593    392       N1+
ATOM   2039  N   SER A 259       6.547  -2.542 -10.169  1.00 98.15           N  
ANISOU 2039  N   SER A 259    12831  11839  12623   1671    627    396       N  
ATOM   2040  CA  SER A 259       5.718  -1.430 -10.644  1.00 94.67           C  
ANISOU 2040  CA  SER A 259    12377  11390  12203   1676    634    402       C  
ATOM   2041  C   SER A 259       6.337  -0.723 -11.835  1.00 85.31           C  
ANISOU 2041  C   SER A 259    11193  10215  11007   1677    618    399       C  
ATOM   2042  O   SER A 259       5.810  -0.779 -12.945  1.00 83.32           O  
ANISOU 2042  O   SER A 259    10921   9961  10774   1680    599    399       O  
ATOM   2043  CB  SER A 259       5.516  -0.402  -9.533  1.00 97.47           C  
ANISOU 2043  CB  SER A 259    12744  11737  12554   1677    666    408       C  
ATOM   2044  OG  SER A 259       5.591  -1.013  -8.262  1.00 99.99           O  
ANISOU 2044  OG  SER A 259    13074  12052  12865   1674    682    409       O  
ATOM   2045  N   ASN A 260       7.457  -0.054 -11.579  1.00 77.87           N  
ANISOU 2045  N   ASN A 260    10273   9283  10032   1673    626    397       N  
ATOM   2046  CA  ASN A 260       8.147   0.738 -12.587  1.00 70.85           C  
ANISOU 2046  CA  ASN A 260     9387   8404   9128   1674    615    394       C  
ATOM   2047  C   ASN A 260       8.294   0.024 -13.924  1.00 68.83           C  
ANISOU 2047  C   ASN A 260     9118   8156   8878   1674    583    389       C  
ATOM   2048  O   ASN A 260       9.090  -0.895 -14.061  1.00 67.57           O  
ANISOU 2048  O   ASN A 260     8966   8007   8701   1669    568    383       O  
ATOM   2049  CB  ASN A 260       9.515   1.173 -12.067  1.00 66.16           C  
ANISOU 2049  CB  ASN A 260     8821   7822   8494   1669    624    391       C  
ATOM   2050  CG  ASN A 260      10.131   2.272 -12.905  1.00 65.72           C  
ANISOU 2050  CG  ASN A 260     8771   7776   8424   1670    619    389       C  
ATOM   2051  ND2 ASN A 260      10.643   3.300 -12.242  1.00 63.13           N  
ANISOU 2051  ND2 ASN A 260     8462   7449   8077   1669    640    392       N  
ATOM   2052  OD1 ASN A 260      10.138   2.206 -14.139  1.00 66.60           O  
ANISOU 2052  OD1 ASN A 260     8871   7893   8543   1671    597    387       O  
ATOM   2053  N   LYS A 261       7.525   0.465 -14.912  1.00 74.17           N  
ANISOU 2053  N   LYS A 261     9775   8827   9578   1678    572    391       N  
ATOM   2054  CA  LYS A 261       7.511  -0.198 -16.213  1.00 80.49           C  
ANISOU 2054  CA  LYS A 261    10560   9634  10389   1679    542    387       C  
ATOM   2055  C   LYS A 261       8.778   0.042 -17.042  1.00 74.37           C  
ANISOU 2055  C   LYS A 261     9798   8876   9584   1675    526    381       C  
ATOM   2056  O   LYS A 261       8.930  -0.538 -18.117  1.00 74.91           O  
ANISOU 2056  O   LYS A 261     9856   8951   9655   1675    501    377       O  
ATOM   2057  CB  LYS A 261       6.247   0.177 -17.013  1.00 88.49           C  
ANISOU 2057  CB  LYS A 261    11549  10636  11438   1685    536    392       C  
ATOM   2058  CG  LYS A 261       6.410   1.345 -17.988  1.00 91.11           C  
ANISOU 2058  CG  LYS A 261    11878  10972  11768   1687    531    393       C  
ATOM   2059  CD  LYS A 261       6.434   0.865 -19.438  1.00 90.79           C  
ANISOU 2059  CD  LYS A 261    11822  10938  11736   1688    500    390       C  
ATOM   2060  CE  LYS A 261       6.720   2.011 -20.411  1.00 90.57           C  
ANISOU 2060  CE  LYS A 261    11795  10916  11703   1690    495    390       C  
ATOM   2061  NZ  LYS A 261       8.158   2.410 -20.457  1.00 87.63           N1+
ANISOU 2061  NZ  LYS A 261    11445  10559  11291   1686    494    385       N1+
ATOM   2062  N   LYS A 262       9.684   0.890 -16.554  1.00 70.30           N  
ANISOU 2062  N   LYS A 262     9304   8367   9039   1673    542    381       N  
ATOM   2063  CA  LYS A 262      10.950   1.127 -17.260  1.00 64.09           C  
ANISOU 2063  CA  LYS A 262     8531   7597   8222   1670    528    375       C  
ATOM   2064  C   LYS A 262      12.015   0.138 -16.809  1.00 64.18           C  
ANISOU 2064  C   LYS A 262     8560   7621   8206   1664    522    368       C  
ATOM   2065  O   LYS A 262      13.027  -0.046 -17.487  1.00 57.82           O  
ANISOU 2065  O   LYS A 262     7763   6830   7376   1661    505    362       O  
ATOM   2066  CB  LYS A 262      11.451   2.564 -17.082  1.00 54.63           C  
ANISOU 2066  CB  LYS A 262     7348   6402   7005   1671    545    377       C  
ATOM   2067  CG  LYS A 262      11.074   3.494 -18.226  1.00 52.44           C  
ANISOU 2067  CG  LYS A 262     7058   6125   6743   1675    537    379       C  
ATOM   2068  CD  LYS A 262      11.635   3.018 -19.563  1.00 53.29           C  
ANISOU 2068  CD  LYS A 262     7160   6245   6843   1674    507    373       C  
ATOM   2069  CE  LYS A 262      11.208   3.929 -20.721  1.00 52.93           C  
ANISOU 2069  CE  LYS A 262     7100   6198   6812   1679    498    376       C  
ATOM   2070  NZ  LYS A 262      12.323   4.339 -21.637  1.00 48.93           N1+
ANISOU 2070  NZ  LYS A 262     6605   5708   6279   1677    484    371       N1+
ATOM   2071  N   ILE A 263      11.774  -0.487 -15.656  1.00 65.64           N  
ANISOU 2071  N   ILE A 263     8749   7799   8392   1663    536    369       N  
ATOM   2072  CA  ILE A 263      12.628  -1.550 -15.139  1.00 58.55           C  
ANISOU 2072  CA  ILE A 263     7866   6910   7472   1657    530    364       C  
ATOM   2073  C   ILE A 263      12.184  -2.917 -15.656  1.00 66.08           C  
ANISOU 2073  C   ILE A 263     8801   7862   8443   1657    508    361       C  
ATOM   2074  O   ILE A 263      11.004  -3.260 -15.566  1.00 73.46           O  
ANISOU 2074  O   ILE A 263     9718   8783   9411   1660    510    365       O  
ATOM   2075  CB  ILE A 263      12.595  -1.576 -13.616  1.00 47.00           C  
ANISOU 2075  CB  ILE A 263     6416   5440   6001   1656    556    367       C  
ATOM   2076  CG1 ILE A 263      13.151  -0.266 -13.059  1.00 51.69           C  
ANISOU 2076  CG1 ILE A 263     7030   6037   6574   1655    578    369       C  
ATOM   2077  CG2 ILE A 263      13.381  -2.765 -13.075  1.00 37.85           C  
ANISOU 2077  CG2 ILE A 263     5271   4290   4822   1650    550    361       C  
ATOM   2078  CD1 ILE A 263      13.398  -0.322 -11.562  1.00 53.80           C  
ANISOU 2078  CD1 ILE A 263     7315   6301   6827   1653    602    371       C  
ATOM   2079  N   LYS A 264      13.133  -3.684 -16.199  1.00 60.83           N  
ANISOU 2079  N   LYS A 264     8143   7211   7757   1653    488    354       N  
ATOM   2080  CA  LYS A 264      12.893  -5.043 -16.692  1.00 53.62           C  
ANISOU 2080  CA  LYS A 264     7217   6299   6858   1652    465    350       C  
ATOM   2081  C   LYS A 264      13.640  -6.069 -15.819  1.00 58.84           C  
ANISOU 2081  C   LYS A 264     7894   6966   7497   1646    467    346       C  
ATOM   2082  O   LYS A 264      14.869  -6.082 -15.773  1.00 63.97           O  
ANISOU 2082  O   LYS A 264     8563   7630   8112   1642    464    340       O  
ATOM   2083  CB  LYS A 264      13.310  -5.136 -18.174  1.00 46.28           C  
ANISOU 2083  CB  LYS A 264     6280   5381   5925   1651    438    345       C  
ATOM   2084  CG  LYS A 264      13.195  -6.509 -18.823  1.00 48.25           C  
ANISOU 2084  CG  LYS A 264     6516   5632   6184   1650    413    341       C  
ATOM   2085  CD  LYS A 264      11.923  -7.234 -18.414  1.00 57.08           C  
ANISOU 2085  CD  LYS A 264     7615   6734   7338   1652    415    345       C  
ATOM   2086  CE  LYS A 264      11.969  -8.701 -18.816  1.00 64.90           C  
ANISOU 2086  CE  LYS A 264     8597   7728   8334   1649    393    341       C  
ATOM   2087  NZ  LYS A 264      11.017  -9.542 -18.025  1.00 69.65           N1+
ANISOU 2087  NZ  LYS A 264     9187   8316   8961   1650    399    344       N1+
ATOM   2088  N   ILE A 265      12.897  -6.922 -15.119  1.00 61.73           N  
ANISOU 2088  N   ILE A 265     8252   7322   7883   1646    472    348       N  
ATOM   2089  CA  ILE A 265      13.500  -7.888 -14.188  1.00 63.87           C  
ANISOU 2089  CA  ILE A 265     8537   7597   8135   1642    476    344       C  
ATOM   2090  C   ILE A 265      13.602  -9.317 -14.759  1.00 68.96           C  
ANISOU 2090  C   ILE A 265     9171   8246   8784   1639    450    339       C  
ATOM   2091  O   ILE A 265      12.681  -9.805 -15.422  1.00 69.29           O  
ANISOU 2091  O   ILE A 265     9191   8280   8857   1642    436    341       O  
ATOM   2092  CB  ILE A 265      12.750  -7.902 -12.840  1.00 55.23           C  
ANISOU 2092  CB  ILE A 265     7443   6489   7055   1643    501    350       C  
ATOM   2093  CG1 ILE A 265      12.809  -6.521 -12.199  1.00 62.60           C  
ANISOU 2093  CG1 ILE A 265     8389   7418   7978   1645    527    355       C  
ATOM   2094  CG2 ILE A 265      13.349  -8.911 -11.891  1.00 50.56           C  
ANISOU 2094  CG2 ILE A 265     6866   5901   6445   1638    504    347       C  
ATOM   2095  CD1 ILE A 265      12.145  -6.452 -10.838  1.00 69.87           C  
ANISOU 2095  CD1 ILE A 265     9312   8325   8909   1645    553    361       C  
ATOM   2096  N   ILE A 266      14.731  -9.979 -14.515  1.00 70.70           N  
ANISOU 2096  N   ILE A 266     9410   8480   8974   1634    444    333       N  
ATOM   2097  CA  ILE A 266      14.932 -11.331 -15.026  1.00 77.05           C  
ANISOU 2097  CA  ILE A 266    10206   9289   9779   1631    420    327       C  
ATOM   2098  C   ILE A 266      15.483 -12.300 -13.988  1.00 83.13           C  
ANISOU 2098  C   ILE A 266    10991  10062  10531   1627    426    324       C  
ATOM   2099  O   ILE A 266      16.175 -11.907 -13.049  1.00 81.07           O  
ANISOU 2099  O   ILE A 266    10752   9806  10246   1625    443    324       O  
ATOM   2100  CB  ILE A 266      15.871 -11.360 -16.260  1.00 47.35           C  
ANISOU 2100  CB  ILE A 266     6449   5544   5997   1629    397    321       C  
ATOM   2101  CG1 ILE A 266      17.239 -10.760 -15.919  1.00 39.64           C  
ANISOU 2101  CG1 ILE A 266     5500   4583   4978   1626    404    317       C  
ATOM   2102  CG2 ILE A 266      15.232 -10.647 -17.447  1.00 50.97           C  
ANISOU 2102  CG2 ILE A 266     6889   5999   6478   1634    386    323       C  
ATOM   2103  CD1 ILE A 266      18.149 -10.604 -17.125  1.00 34.30           C  
ANISOU 2103  CD1 ILE A 266     4829   3923   4281   1625    383    310       C  
ATOM   2104  N   GLU A 267      15.159 -13.575 -14.176  1.00 89.47           N  
ANISOU 2104  N   GLU A 267    11782  10864  11350   1626    410    322       N  
ATOM   2105  CA  GLU A 267      15.794 -14.652 -13.433  1.00 92.24           C  
ANISOU 2105  CA  GLU A 267    12145  11219  11682   1621    409    318       C  
ATOM   2106  C   GLU A 267      17.280 -14.680 -13.790  1.00 86.79           C  
ANISOU 2106  C   GLU A 267    11476  10549  10951   1617    398    310       C  
ATOM   2107  O   GLU A 267      17.652 -14.327 -14.912  1.00 89.79           O  
ANISOU 2107  O   GLU A 267    11853  10938  11324   1617    382    307       O  
ATOM   2108  CB  GLU A 267      15.128 -15.985 -13.787  1.00 96.93           C  
ANISOU 2108  CB  GLU A 267    12720  11807  12301   1621    391    317       C  
ATOM   2109  CG  GLU A 267      13.748 -16.165 -13.177  1.00100.12           C  
ANISOU 2109  CG  GLU A 267    13106  12192  12742   1624    403    324       C  
ATOM   2110  CD  GLU A 267      13.788 -16.180 -11.657  1.00100.86           C  
ANISOU 2110  CD  GLU A 267    13214  12280  12827   1623    429    327       C  
ATOM   2111  OE1 GLU A 267      13.220 -15.257 -11.031  1.00102.64           O  
ANISOU 2111  OE1 GLU A 267    13441  12496  13062   1626    451    333       O  
ATOM   2112  OE2 GLU A 267      14.394 -17.117 -11.091  1.00 97.47           O1-
ANISOU 2112  OE2 GLU A 267    12796  11857  12381   1619    426    323       O1-
ATOM   2113  N   PRO A 268      18.136 -15.092 -12.839  1.00 75.71           N  
ANISOU 2113  N   PRO A 268    10093   9152   9520   1612    407    307       N  
ATOM   2114  CA  PRO A 268      19.582 -15.154 -13.096  1.00 67.97           C  
ANISOU 2114  CA  PRO A 268     9134   8191   8500   1608    397    300       C  
ATOM   2115  C   PRO A 268      19.907 -15.950 -14.365  1.00 56.60           C  
ANISOU 2115  C   PRO A 268     7685   6762   7058   1607    367    294       C  
ATOM   2116  O   PRO A 268      19.165 -16.867 -14.690  1.00 47.97           O  
ANISOU 2116  O   PRO A 268     6573   5661   5992   1607    355    294       O  
ATOM   2117  CB  PRO A 268      20.137 -15.856 -11.842  1.00 67.00           C  
ANISOU 2117  CB  PRO A 268     9029   8071   8357   1604    408    298       C  
ATOM   2118  CG  PRO A 268      18.948 -16.475 -11.165  1.00 69.64           C  
ANISOU 2118  CG  PRO A 268     9348   8388   8725   1606    417    304       C  
ATOM   2119  CD  PRO A 268      17.795 -15.577 -11.492  1.00 73.53           C  
ANISOU 2119  CD  PRO A 268     9822   8867   9249   1611    425    311       C  
ATOM   2120  N   VAL A 269      20.973 -15.583 -15.078  1.00 59.29           N  
ANISOU 2120  N   VAL A 269     8039   7119   7370   1605    356    288       N  
ATOM   2121  CA  VAL A 269      21.331 -16.255 -16.333  1.00 56.05           C  
ANISOU 2121  CA  VAL A 269     7621   6719   6956   1604    327    281       C  
ATOM   2122  C   VAL A 269      22.780 -16.717 -16.411  1.00 45.24           C  
ANISOU 2122  C   VAL A 269     6274   5370   5546   1599    316    273       C  
ATOM   2123  O   VAL A 269      23.587 -16.469 -15.506  1.00 44.80           O  
ANISOU 2123  O   VAL A 269     6240   5320   5462   1596    330    271       O  
ATOM   2124  CB  VAL A 269      21.031 -15.392 -17.576  1.00 56.93           C  
ANISOU 2124  CB  VAL A 269     7721   6832   7080   1607    317    283       C  
ATOM   2125  CG1 VAL A 269      19.607 -14.876 -17.513  1.00 60.09           C  
ANISOU 2125  CG1 VAL A 269     8099   7213   7520   1612    328    291       C  
ATOM   2126  CG2 VAL A 269      22.024 -14.243 -17.685  1.00 53.85           C  
ANISOU 2126  CG2 VAL A 269     7350   6454   6656   1607    324    280       C  
ATOM   2127  N   GLY A 270      23.093 -17.377 -17.520  1.00 35.66           N  
ANISOU 2127  N   GLY A 270     5053   4166   4329   1597    291    267       N  
ATOM   2128  CA  GLY A 270      24.339 -18.104 -17.659  1.00 37.08           C  
ANISOU 2128  CA  GLY A 270     5251   4363   4475   1593    277    257       C  
ATOM   2129  C   GLY A 270      25.505 -17.243 -18.067  1.00 39.88           C  
ANISOU 2129  C   GLY A 270     5625   4735   4793   1592    275    253       C  
ATOM   2130  O   GLY A 270      25.335 -16.050 -18.319  1.00 39.58           O  
ANISOU 2130  O   GLY A 270     5587   4695   4758   1595    284    256       O  
ATOM   2131  N   TYR A 271      26.686 -17.856 -18.132  1.00 35.68           N  
ANISOU 2131  N   TYR A 271     5110   4219   4227   1587    264    244       N  
ATOM   2132  CA  TYR A 271      27.922 -17.136 -18.436  1.00 29.69           C  
ANISOU 2132  CA  TYR A 271     4374   3478   3431   1586    261    239       C  
ATOM   2133  C   TYR A 271      27.816 -16.241 -19.687  1.00 34.69           C  
ANISOU 2133  C   TYR A 271     4997   4114   4068   1589    252    238       C  
ATOM   2134  O   TYR A 271      28.021 -15.010 -19.616  1.00 30.13           O  
ANISOU 2134  O   TYR A 271     4429   3539   3481   1591    264    241       O  
ATOM   2135  CB  TYR A 271      29.102 -18.114 -18.566  1.00 27.23           C  
ANISOU 2135  CB  TYR A 271     4077   3183   3085   1581    245    228       C  
ATOM   2136  CG  TYR A 271      30.390 -17.413 -18.895  1.00 25.24           C  
ANISOU 2136  CG  TYR A 271     3847   2950   2793   1580    242    222       C  
ATOM   2137  CD1 TYR A 271      30.882 -16.443 -18.055  1.00 20.11           C  
ANISOU 2137  CD1 TYR A 271     3216   2301   2123   1579    262    225       C  
ATOM   2138  CD2 TYR A 271      31.097 -17.696 -20.053  1.00 28.98           C  
ANISOU 2138  CD2 TYR A 271     4323   3439   3249   1578    219    213       C  
ATOM   2139  CE1 TYR A 271      32.027 -15.771 -18.335  1.00 19.95           C  
ANISOU 2139  CE1 TYR A 271     3216   2297   2067   1578    259    220       C  
ATOM   2140  CE2 TYR A 271      32.273 -17.008 -20.348  1.00 29.84           C  
ANISOU 2140  CE2 TYR A 271     4452   3565   3321   1577    216    207       C  
ATOM   2141  CZ  TYR A 271      32.726 -16.042 -19.466  1.00 27.58           C  
ANISOU 2141  CZ  TYR A 271     4184   3278   3016   1577    237    211       C  
ATOM   2142  OH  TYR A 271      33.883 -15.326 -19.687  1.00 31.16           O  
ANISOU 2142  OH  TYR A 271     4659   3749   3434   1576    235    206       O  
ATOM   2143  N   LEU A 272      27.466 -16.867 -20.814  1.00 38.62           N  
ANISOU 2143  N   LEU A 272     5477   4614   4582   1589    230    235       N  
ATOM   2144  CA  LEU A 272      27.442 -16.212 -22.125  1.00 34.56           C  
ANISOU 2144  CA  LEU A 272     4954   4105   4071   1592    216    234       C  
ATOM   2145  C   LEU A 272      26.261 -15.261 -22.332  1.00 43.43           C  
ANISOU 2145  C   LEU A 272     6060   5213   5229   1597    227    243       C  
ATOM   2146  O   LEU A 272      26.396 -14.233 -23.006  1.00 44.13           O  
ANISOU 2146  O   LEU A 272     6148   5305   5313   1599    227    244       O  
ATOM   2147  CB  LEU A 272      27.425 -17.263 -23.218  1.00 29.21           C  
ANISOU 2147  CB  LEU A 272     4264   3433   3400   1590    190    228       C  
ATOM   2148  CG  LEU A 272      28.633 -18.185 -23.278  1.00 31.81           C  
ANISOU 2148  CG  LEU A 272     4611   3781   3695   1585    175    217       C  
ATOM   2149  CD1 LEU A 272      28.412 -19.231 -24.337  1.00 28.89           C  
ANISOU 2149  CD1 LEU A 272     4226   3414   3338   1584    150    212       C  
ATOM   2150  CD2 LEU A 272      29.880 -17.396 -23.586  1.00 35.24           C  
ANISOU 2150  CD2 LEU A 272     5067   4232   4089   1584    174    211       C  
ATOM   2151  N   GLU A 273      25.103 -15.613 -21.775  1.00 44.29           N  
ANISOU 2151  N   GLU A 273     6152   5304   5373   1599    236    250       N  
ATOM   2152  CA  GLU A 273      23.944 -14.735 -21.838  1.00 44.25           C  
ANISOU 2152  CA  GLU A 273     6130   5283   5401   1604    248    259       C  
ATOM   2153  C   GLU A 273      24.324 -13.437 -21.182  1.00 41.99           C  
ANISOU 2153  C   GLU A 273     5861   4998   5097   1605    270    263       C  
ATOM   2154  O   GLU A 273      24.110 -12.351 -21.726  1.00 49.26           O  
ANISOU 2154  O   GLU A 273     6776   5916   6023   1608    273    266       O  
ATOM   2155  CB  GLU A 273      22.752 -15.338 -21.098  1.00 54.44           C  
ANISOU 2155  CB  GLU A 273     7404   6555   6726   1605    257    266       C  
ATOM   2156  CG  GLU A 273      22.022 -16.430 -21.872  1.00 66.94           C  
ANISOU 2156  CG  GLU A 273     8964   8133   8337   1605    236    265       C  
ATOM   2157  CD  GLU A 273      22.045 -17.782 -21.167  1.00 73.96           C  
ANISOU 2157  CD  GLU A 273     9854   9019   9227   1602    233    263       C  
ATOM   2158  OE1 GLU A 273      23.117 -18.185 -20.653  1.00 72.83           O  
ANISOU 2158  OE1 GLU A 273     9732   8889   9050   1598    234    257       O  
ATOM   2159  OE2 GLU A 273      20.983 -18.440 -21.134  1.00 76.06           O1-
ANISOU 2159  OE2 GLU A 273    10100   9272   9527   1603    230    267       O1-
ATOM   2160  N   PHE A 274      24.924 -13.561 -20.010  1.00 39.19           N  
ANISOU 2160  N   PHE A 274     5525   4645   4720   1602    284    262       N  
ATOM   2161  CA  PHE A 274      25.265 -12.398 -19.214  1.00 37.84           C  
ANISOU 2161  CA  PHE A 274     5371   4474   4533   1603    307    265       C  
ATOM   2162  C   PHE A 274      26.401 -11.589 -19.821  1.00 41.39           C  
ANISOU 2162  C   PHE A 274     5838   4940   4949   1602    302    260       C  
ATOM   2163  O   PHE A 274      26.483 -10.367 -19.633  1.00 41.65           O  
ANISOU 2163  O   PHE A 274     5878   4972   4976   1604    316    264       O  
ATOM   2164  CB  PHE A 274      25.619 -12.807 -17.799  1.00 35.78           C  
ANISOU 2164  CB  PHE A 274     5127   4211   4258   1600    324    266       C  
ATOM   2165  CG  PHE A 274      25.630 -11.670 -16.865  1.00 32.68           C  
ANISOU 2165  CG  PHE A 274     4746   3813   3858   1601    350    272       C  
ATOM   2166  CD1 PHE A 274      24.439 -11.055 -16.509  1.00 31.44           C  
ANISOU 2166  CD1 PHE A 274     4574   3638   3733   1605    366    281       C  
ATOM   2167  CD2 PHE A 274      26.825 -11.179 -16.373  1.00 29.17           C  
ANISOU 2167  CD2 PHE A 274     4327   3380   3374   1598    357    269       C  
ATOM   2168  CE1 PHE A 274      24.440  -9.982 -15.663  1.00 31.36           C  
ANISOU 2168  CE1 PHE A 274     4576   3623   3717   1606    391    286       C  
ATOM   2169  CE2 PHE A 274      26.845 -10.112 -15.520  1.00 31.73           C  
ANISOU 2169  CE2 PHE A 274     4664   3700   3693   1599    381    275       C  
ATOM   2170  CZ  PHE A 274      25.650  -9.504 -15.163  1.00 34.95           C  
ANISOU 2170  CZ  PHE A 274     5057   4089   4133   1603    398    283       C  
ATOM   2171  N   LEU A 275      27.282 -12.279 -20.538  1.00 42.15           N  
ANISOU 2171  N   LEU A 275     5940   5052   5023   1599    280    252       N  
ATOM   2172  CA  LEU A 275      28.313 -11.611 -21.328  1.00 42.34           C  
ANISOU 2172  CA  LEU A 275     5978   5093   5017   1598    271    246       C  
ATOM   2173  C   LEU A 275      27.692 -10.752 -22.434  1.00 49.66           C  
ANISOU 2173  C   LEU A 275     6888   6016   5964   1603    265    249       C  
ATOM   2174  O   LEU A 275      28.164  -9.632 -22.720  1.00 54.29           O  
ANISOU 2174  O   LEU A 275     7484   6609   6535   1604    270    249       O  
ATOM   2175  CB  LEU A 275      29.247 -12.645 -21.940  1.00 38.20           C  
ANISOU 2175  CB  LEU A 275     5460   4585   4468   1594    248    235       C  
ATOM   2176  CG  LEU A 275      30.642 -12.769 -21.348  1.00 41.49           C  
ANISOU 2176  CG  LEU A 275     5906   5019   4841   1590    250    229       C  
ATOM   2177  CD1 LEU A 275      31.386 -13.820 -22.128  1.00 46.45           C  
ANISOU 2177  CD1 LEU A 275     6537   5661   5450   1587    225    218       C  
ATOM   2178  CD2 LEU A 275      31.363 -11.449 -21.421  1.00 40.37           C  
ANISOU 2178  CD2 LEU A 275     5780   4885   4674   1591    259    229       C  
HETATM 2179  N   MSE A 276      26.638 -11.288 -23.056  1.00 49.27           N  
ANISOU 2179  N   MSE A 276     6813   5956   5950   1605    254    252       N  
HETATM 2180  CA  MSE A 276      25.847 -10.538 -24.035  1.00 45.20           C  
ANISOU 2180  CA  MSE A 276     6279   5434   5460   1609    250    256       C  
HETATM 2181  C   MSE A 276      25.250  -9.281 -23.412  1.00 44.13           C  
ANISOU 2181  C   MSE A 276     6143   5286   5337   1613    274    265       C  
HETATM 2182  O   MSE A 276      25.413  -8.175 -23.934  1.00 43.99           O  
ANISOU 2182  O   MSE A 276     6128   5273   5315   1615    276    266       O  
HETATM 2183  CB  MSE A 276      24.712 -11.394 -24.578  1.00 41.00           C  
ANISOU 2183  CB  MSE A 276     5720   4891   4966   1611    237    259       C  
HETATM 2184  CG  MSE A 276      25.058 -12.204 -25.792  1.00 50.52           C  
ANISOU 2184  CG  MSE A 276     6919   6108   6167   1609    209    251       C  
HETATM 2185  CE  MSE A 276      26.205 -10.179 -27.611  1.00 74.36           C  
ANISOU 2185  CE  MSE A 276     9951   9150   9153   1611    198    247       C  
HETATM 2186 SE   MSE A 276      24.614 -11.299 -27.450  1.00 78.69          SE  
ANISOU 2186 SE   MSE A 276    10470   9677   9753   1613    194    253      SE  
ATOM   2187  N   LEU A 277      24.549  -9.467 -22.297  1.00 35.98           N  
ANISOU 2187  N   LEU A 277     5108   4240   4324   1613    292    271       N  
ATOM   2188  CA  LEU A 277      23.957  -8.353 -21.582  1.00 30.76           C  
ANISOU 2188  CA  LEU A 277     4447   3567   3675   1617    316    279       C  
ATOM   2189  C   LEU A 277      24.996  -7.296 -21.195  1.00 33.24           C  
ANISOU 2189  C   LEU A 277     4785   3890   3953   1615    329    278       C  
ATOM   2190  O   LEU A 277      24.707  -6.099 -21.204  1.00 36.77           O  
ANISOU 2190  O   LEU A 277     5231   4332   4407   1619    342    283       O  
ATOM   2191  CB  LEU A 277      23.211  -8.852 -20.343  1.00 29.27           C  
ANISOU 2191  CB  LEU A 277     4254   3363   3505   1617    333    284       C  
ATOM   2192  CG  LEU A 277      22.021  -9.767 -20.598  1.00 33.70           C  
ANISOU 2192  CG  LEU A 277     4790   3911   4104   1618    324    287       C  
ATOM   2193  CD1 LEU A 277      21.249  -9.998 -19.326  1.00 36.88           C  
ANISOU 2193  CD1 LEU A 277     5190   4298   4525   1619    344    293       C  
ATOM   2194  CD2 LEU A 277      21.121  -9.158 -21.637  1.00 44.64           C  
ANISOU 2194  CD2 LEU A 277     6153   5288   5519   1623    316    291       C  
ATOM   2195  N   GLU A 278      26.207  -7.721 -20.857  1.00 27.20           N  
ANISOU 2195  N   GLU A 278     4042   3141   3153   1611    325    271       N  
ATOM   2196  CA  GLU A 278      27.222  -6.744 -20.499  1.00 27.00           C  
ANISOU 2196  CA  GLU A 278     4040   3125   3093   1610    337    270       C  
ATOM   2197  C   GLU A 278      27.718  -5.946 -21.710  1.00 36.06           C  
ANISOU 2197  C   GLU A 278     5188   4284   4228   1611    324    267       C  
ATOM   2198  O   GLU A 278      27.740  -4.706 -21.662  1.00 31.66           O  
ANISOU 2198  O   GLU A 278     4637   3725   3669   1614    337    271       O  
ATOM   2199  CB  GLU A 278      28.381  -7.406 -19.762  1.00 30.74           C  
ANISOU 2199  CB  GLU A 278     4537   3611   3531   1605    336    264       C  
ATOM   2200  CG  GLU A 278      28.078  -7.761 -18.321  1.00 36.87           C  
ANISOU 2200  CG  GLU A 278     5320   4377   4312   1603    356    268       C  
ATOM   2201  CD  GLU A 278      29.175  -8.595 -17.674  1.00 37.39           C  
ANISOU 2201  CD  GLU A 278     5406   4454   4344   1598    353    262       C  
ATOM   2202  OE1 GLU A 278      29.893  -9.304 -18.404  1.00 30.97           O  
ANISOU 2202  OE1 GLU A 278     4598   3656   3514   1596    332    254       O  
ATOM   2203  OE2 GLU A 278      29.315  -8.540 -16.433  1.00 42.81           O1-
ANISOU 2203  OE2 GLU A 278     6107   5137   5022   1597    372    265       O1-
ATOM   2204  N   LYS A 279      28.113  -6.644 -22.786  1.00 39.04           N  
ANISOU 2204  N   LYS A 279     5562   4673   4600   1610    299    259       N  
ATOM   2205  CA  LYS A 279      28.688  -5.963 -23.961  1.00 40.18           C  
ANISOU 2205  CA  LYS A 279     5708   4830   4729   1611    286    255       C  
ATOM   2206  C   LYS A 279      27.766  -4.888 -24.525  1.00 37.46           C  
ANISOU 2206  C   LYS A 279     5347   4474   4412   1616    292    263       C  
ATOM   2207  O   LYS A 279      28.199  -3.778 -24.836  1.00 36.43           O  
ANISOU 2207  O   LYS A 279     5225   4349   4268   1617    296    263       O  
ATOM   2208  CB  LYS A 279      29.053  -6.948 -25.079  1.00 42.49           C  
ANISOU 2208  CB  LYS A 279     5994   5134   5016   1609    258    247       C  
ATOM   2209  CG  LYS A 279      29.687  -6.286 -26.308  1.00 41.45           C  
ANISOU 2209  CG  LYS A 279     5865   5016   4867   1610    244    242       C  
ATOM   2210  CD  LYS A 279      28.792  -6.370 -27.535  1.00 48.27           C  
ANISOU 2210  CD  LYS A 279     6704   5874   5762   1613    228    244       C  
ATOM   2211  CE  LYS A 279      29.445  -5.716 -28.748  1.00 52.31           C  
ANISOU 2211  CE  LYS A 279     7218   6399   6256   1614    214    239       C  
ATOM   2212  NZ  LYS A 279      28.713  -5.982 -30.027  1.00 54.41           N1+
ANISOU 2212  NZ  LYS A 279     7462   6663   6549   1616    195    239       N1+
ATOM   2213  N   ASN A 280      26.487  -5.219 -24.631  1.00 39.83           N  
ANISOU 2213  N   ASN A 280     5623   4758   4751   1619    291    268       N  
ATOM   2214  CA  ASN A 280      25.528  -4.322 -25.268  1.00 47.36           C  
ANISOU 2214  CA  ASN A 280     6559   5702   5735   1624    294    275       C  
ATOM   2215  C   ASN A 280      24.785  -3.334 -24.348  1.00 47.07           C  
ANISOU 2215  C   ASN A 280     6520   5649   5715   1627    321    284       C  
ATOM   2216  O   ASN A 280      23.815  -2.706 -24.760  1.00 44.03           O  
ANISOU 2216  O   ASN A 280     6118   5253   5360   1631    324    290       O  
ATOM   2217  CB  ASN A 280      24.574  -5.117 -26.163  1.00 44.63           C  
ANISOU 2217  CB  ASN A 280     6187   5349   5423   1625    276    276       C  
ATOM   2218  CG  ASN A 280      25.306  -5.815 -27.287  1.00 45.85           C  
ANISOU 2218  CG  ASN A 280     6341   5519   5560   1623    249    267       C  
ATOM   2219  ND2 ASN A 280      25.305  -7.135 -27.257  1.00 47.54           N  
ANISOU 2219  ND2 ASN A 280     6552   5736   5777   1620    237    263       N  
ATOM   2220  OD1 ASN A 280      25.886  -5.170 -28.163  1.00 44.36           O  
ANISOU 2220  OD1 ASN A 280     6157   5341   5355   1623    241    263       O  
ATOM   2221  N   ALA A 281      25.264  -3.182 -23.118  1.00 43.32           N  
ANISOU 2221  N   ALA A 281     6064   5174   5221   1625    340    285       N  
ATOM   2222  CA  ALA A 281      24.752  -2.150 -22.224  1.00 32.34           C  
ANISOU 2222  CA  ALA A 281     4676   3771   3840   1627    366    293       C  
ATOM   2223  C   ALA A 281      25.386  -0.807 -22.549  1.00 29.40           C  
ANISOU 2223  C   ALA A 281     4316   3406   3448   1628    372    294       C  
ATOM   2224  O   ALA A 281      26.435  -0.742 -23.205  1.00 35.87           O  
ANISOU 2224  O   ALA A 281     5148   4243   4239   1626    358    287       O  
ATOM   2225  CB  ALA A 281      25.014  -2.519 -20.779  1.00 21.44           C  
ANISOU 2225  CB  ALA A 281     3312   2388   2448   1624    384    294       C  
ATOM   2226  N   GLU A 282      24.744   0.260 -22.086  1.00 25.51           N  
ANISOU 2226  N   GLU A 282     3821   2902   2971   1632    392    301       N  
ATOM   2227  CA  GLU A 282      25.213   1.609 -22.336  1.00 34.26           C  
ANISOU 2227  CA  GLU A 282     4939   4014   4064   1633    400    303       C  
ATOM   2228  C   GLU A 282      26.060   2.026 -21.159  1.00 40.84           C  
ANISOU 2228  C   GLU A 282     5798   4852   4868   1630    419    303       C  
ATOM   2229  O   GLU A 282      27.033   2.765 -21.305  1.00 45.02           O  
ANISOU 2229  O   GLU A 282     6345   5393   5368   1629    420    301       O  
ATOM   2230  CB  GLU A 282      24.034   2.568 -22.493  1.00 39.82           C  
ANISOU 2230  CB  GLU A 282     5626   4703   4802   1639    412    311       C  
ATOM   2231  CG  GLU A 282      24.443   3.988 -22.864  1.00 46.18           C  
ANISOU 2231  CG  GLU A 282     6439   5512   5594   1641    419    313       C  
ATOM   2232  CD  GLU A 282      23.262   4.857 -23.282  1.00 54.36           C  
ANISOU 2232  CD  GLU A 282     7455   6534   6665   1646    426    321       C  
ATOM   2233  OE1 GLU A 282      22.111   4.554 -22.894  1.00 54.58           O  
ANISOU 2233  OE1 GLU A 282     7467   6547   6725   1648    433    326       O  
ATOM   2234  OE2 GLU A 282      23.489   5.847 -24.006  1.00 58.67           O1-
ANISOU 2234  OE2 GLU A 282     8001   7084   7205   1648    424    321       O1-
ATOM   2235  N   LEU A 283      25.658   1.567 -19.979  1.00 39.47           N  
ANISOU 2235  N   LEU A 283     5627   4668   4702   1629    435    306       N  
ATOM   2236  CA  LEU A 283      26.505   1.633 -18.795  1.00 33.23           C  
ANISOU 2236  CA  LEU A 283     4861   3882   3883   1625    450    306       C  
ATOM   2237  C   LEU A 283      26.030   0.533 -17.893  1.00 32.33           C  
ANISOU 2237  C   LEU A 283     4744   3760   3781   1623    455    307       C  
ATOM   2238  O   LEU A 283      24.910   0.049 -18.053  1.00 31.80           O  
ANISOU 2238  O   LEU A 283     4655   3681   3748   1626    453    310       O  
ATOM   2239  CB  LEU A 283      26.465   3.000 -18.095  1.00 32.51           C  
ANISOU 2239  CB  LEU A 283     4781   3784   3788   1627    475    313       C  
ATOM   2240  CG  LEU A 283      25.316   3.404 -17.176  1.00 39.11           C  
ANISOU 2240  CG  LEU A 283     5607   4600   4652   1630    499    321       C  
ATOM   2241  CD1 LEU A 283      25.557   2.958 -15.749  1.00 42.93           C  
ANISOU 2241  CD1 LEU A 283     6107   5081   5124   1626    515    322       C  
ATOM   2242  CD2 LEU A 283      25.155   4.898 -17.224  1.00 45.04           C  
ANISOU 2242  CD2 LEU A 283     6360   5346   5406   1633    514    327       C  
ATOM   2243  N   ILE A 284      26.893   0.135 -16.963  1.00 30.72           N  
ANISOU 2243  N   ILE A 284     4561   3562   3548   1619    462    304       N  
ATOM   2244  CA  ILE A 284      26.633  -0.988 -16.078  1.00 30.37           C  
ANISOU 2244  CA  ILE A 284     4516   3512   3510   1617    465    304       C  
ATOM   2245  C   ILE A 284      26.735  -0.500 -14.647  1.00 26.91           C  
ANISOU 2245  C   ILE A 284     4094   3067   3063   1615    492    309       C  
ATOM   2246  O   ILE A 284      27.614   0.308 -14.339  1.00 31.47           O  
ANISOU 2246  O   ILE A 284     4692   3652   3612   1614    501    309       O  
ATOM   2247  CB  ILE A 284      27.674  -2.103 -16.336  1.00 34.95           C  
ANISOU 2247  CB  ILE A 284     5108   4109   4063   1612    445    295       C  
ATOM   2248  CG1 ILE A 284      27.260  -2.955 -17.530  1.00 30.41           C  
ANISOU 2248  CG1 ILE A 284     4512   3537   3506   1613    420    291       C  
ATOM   2249  CG2 ILE A 284      27.881  -2.973 -15.101  1.00 34.68           C  
ANISOU 2249  CG2 ILE A 284     5084   4072   4019   1609    455    295       C  
ATOM   2250  CD1 ILE A 284      28.336  -3.881 -17.987  1.00 33.28           C  
ANISOU 2250  CD1 ILE A 284     4886   3918   3841   1609    399    281       C  
ATOM   2251  N   LEU A 285      25.830  -0.974 -13.790  1.00 26.27           N  
ANISOU 2251  N   LEU A 285     4005   2972   3005   1616    505    314       N  
ATOM   2252  CA  LEU A 285      25.743  -0.560 -12.377  1.00 27.20           C  
ANISOU 2252  CA  LEU A 285     4136   3081   3119   1615    532    319       C  
ATOM   2253  C   LEU A 285      25.795  -1.776 -11.486  1.00 33.06           C  
ANISOU 2253  C   LEU A 285     4882   3820   3858   1611    534    318       C  
ATOM   2254  O   LEU A 285      24.890  -2.621 -11.529  1.00 30.84           O  
ANISOU 2254  O   LEU A 285     4582   3530   3604   1613    529    318       O  
ATOM   2255  CB  LEU A 285      24.417   0.138 -12.097  1.00 30.61           C  
ANISOU 2255  CB  LEU A 285     4551   3494   3586   1619    550    327       C  
ATOM   2256  CG  LEU A 285      24.098   1.428 -12.836  1.00 37.16           C  
ANISOU 2256  CG  LEU A 285     5373   4320   4425   1623    553    331       C  
ATOM   2257  CD1 LEU A 285      22.605   1.581 -12.907  1.00 45.63           C  
ANISOU 2257  CD1 LEU A 285     6422   5376   5541   1628    561    337       C  
ATOM   2258  CD2 LEU A 285      24.716   2.588 -12.109  1.00 33.58           C  
ANISOU 2258  CD2 LEU A 285     4941   3869   3950   1622    573    334       C  
ATOM   2259  N   THR A 286      26.830  -1.865 -10.659  1.00 38.51           N  
ANISOU 2259  N   THR A 286     5597   4519   4515   1607    541    316       N  
ATOM   2260  CA  THR A 286      27.090  -3.124  -9.969  1.00 39.87           C  
ANISOU 2260  CA  THR A 286     5776   4694   4680   1603    537    313       C  
ATOM   2261  C   THR A 286      27.786  -2.943  -8.631  1.00 42.47           C  
ANISOU 2261  C   THR A 286     6129   5024   4983   1599    557    315       C  
ATOM   2262  O   THR A 286      28.351  -1.882  -8.365  1.00 43.86           O  
ANISOU 2262  O   THR A 286     6321   5203   5141   1599    568    317       O  
ATOM   2263  CB  THR A 286      27.973  -4.061 -10.848  1.00 41.36           C  
ANISOU 2263  CB  THR A 286     5966   4899   4848   1600    510    303       C  
ATOM   2264  CG2 THR A 286      29.382  -3.523 -10.957  1.00 36.18           C  
ANISOU 2264  CG2 THR A 286     5335   4260   4151   1597    506    300       C  
ATOM   2265  OG1 THR A 286      28.014  -5.377 -10.275  1.00 49.26           O  
ANISOU 2265  OG1 THR A 286     6968   5900   5847   1597    505    301       O  
ATOM   2266  N   ASP A 287      27.740  -3.989  -7.801  1.00 42.16           N  
ANISOU 2266  N   ASP A 287     6094   4982   4945   1597    559    314       N  
ATOM   2267  CA  ASP A 287      28.598  -4.089  -6.610  1.00 41.27           C  
ANISOU 2267  CA  ASP A 287     6006   4874   4803   1592    572    315       C  
ATOM   2268  C   ASP A 287      29.678  -5.173  -6.733  1.00 40.65           C  
ANISOU 2268  C   ASP A 287     5939   4810   4695   1587    553    307       C  
ATOM   2269  O   ASP A 287      30.616  -5.216  -5.924  1.00 40.49           O  
ANISOU 2269  O   ASP A 287     5942   4797   4645   1583    560    307       O  
ATOM   2270  CB  ASP A 287      27.777  -4.287  -5.332  1.00 41.25           C  
ANISOU 2270  CB  ASP A 287     6000   4854   4818   1592    595    321       C  
ATOM   2271  CG  ASP A 287      26.812  -5.439  -5.434  1.00 46.41           C  
ANISOU 2271  CG  ASP A 287     6632   5499   5501   1593    588    320       C  
ATOM   2272  OD1 ASP A 287      27.161  -6.444  -6.089  1.00 53.67           O  
ANISOU 2272  OD1 ASP A 287     7548   6428   6416   1592    565    314       O  
ATOM   2273  OD2 ASP A 287      25.705  -5.341  -4.860  1.00 38.24           O1-
ANISOU 2273  OD2 ASP A 287     5586   4449   4495   1596    604    326       O1-
ATOM   2274  N   SER A 288      29.552  -6.024  -7.756  1.00 35.11           N  
ANISOU 2274  N   SER A 288     5222   4114   4002   1588    530    301       N  
ATOM   2275  CA  SER A 288      30.511  -7.113  -7.997  1.00 32.05           C  
ANISOU 2275  CA  SER A 288     4845   3742   3591   1584    510    293       C  
ATOM   2276  C   SER A 288      31.850  -6.680  -8.618  1.00 38.96           C  
ANISOU 2276  C   SER A 288     5739   4637   4429   1582    496    288       C  
ATOM   2277  O   SER A 288      31.865  -5.975  -9.626  1.00 48.08           O  
ANISOU 2277  O   SER A 288     6887   5796   5586   1585    488    286       O  
ATOM   2278  CB  SER A 288      29.884  -8.171  -8.886  1.00 28.41           C  
ANISOU 2278  CB  SER A 288     4360   3280   3153   1586    489    289       C  
ATOM   2279  OG  SER A 288      30.873  -9.094  -9.282  1.00 31.46           O  
ANISOU 2279  OG  SER A 288     4756   3682   3514   1582    468    280       O  
ATOM   2280  N   GLY A 289      32.966  -7.118  -8.033  1.00 34.01           N  
ANISOU 2280  N   GLY A 289     5134   4021   3768   1577    494    284       N  
ATOM   2281  CA  GLY A 289      34.290  -6.847  -8.589  1.00 35.41           C  
ANISOU 2281  CA  GLY A 289     5329   4217   3908   1575    480    279       C  
ATOM   2282  C   GLY A 289      34.521  -7.513  -9.943  1.00 39.91           C  
ANISOU 2282  C   GLY A 289     5888   4799   4477   1576    452    270       C  
ATOM   2283  O   GLY A 289      35.197  -6.971 -10.841  1.00 41.40           O  
ANISOU 2283  O   GLY A 289     6082   5000   4648   1576    440    266       O  
ATOM   2284  N   GLY A 290      33.926  -8.695 -10.094  1.00 34.32           N  
ANISOU 2284  N   GLY A 290     5165   4087   3789   1576    442    267       N  
ATOM   2285  CA  GLY A 290      33.951  -9.417 -11.348  1.00 27.08           C  
ANISOU 2285  CA  GLY A 290     4234   3179   2877   1576    416    259       C  
ATOM   2286  C   GLY A 290      33.347  -8.626 -12.481  1.00 29.12           C  
ANISOU 2286  C   GLY A 290     4475   3433   3155   1581    410    261       C  
ATOM   2287  O   GLY A 290      33.982  -8.425 -13.508  1.00 30.29           O  
ANISOU 2287  O   GLY A 290     4626   3596   3288   1581    393    255       O  
ATOM   2288  N   VAL A 291      32.115  -8.171 -12.284  1.00 32.48           N  
ANISOU 2288  N   VAL A 291     4884   3842   3616   1584    424    268       N  
ATOM   2289  CA  VAL A 291      31.418  -7.370 -13.280  1.00 31.84           C  
ANISOU 2289  CA  VAL A 291     4784   3756   3557   1589    421    270       C  
ATOM   2290  C   VAL A 291      32.131  -6.044 -13.599  1.00 34.50           C  
ANISOU 2290  C   VAL A 291     5136   4102   3872   1590    425    271       C  
ATOM   2291  O   VAL A 291      32.118  -5.583 -14.742  1.00 36.02           O  
ANISOU 2291  O   VAL A 291     5319   4299   4068   1592    413    269       O  
ATOM   2292  CB  VAL A 291      29.975  -7.094 -12.847  1.00 30.05           C  
ANISOU 2292  CB  VAL A 291     4538   3508   3371   1593    438    279       C  
ATOM   2293  CG1 VAL A 291      29.266  -6.208 -13.867  1.00 26.74           C  
ANISOU 2293  CG1 VAL A 291     4102   3084   2975   1598    435    282       C  
ATOM   2294  CG2 VAL A 291      29.230  -8.398 -12.653  1.00 20.69           C  
ANISOU 2294  CG2 VAL A 291     3337   2314   2209   1592    432    278       C  
ATOM   2295  N   GLN A 292      32.752  -5.436 -12.593  1.00 35.59           N  
ANISOU 2295  N   GLN A 292     5295   4241   3988   1587    443    274       N  
ATOM   2296  CA  GLN A 292      33.562  -4.251 -12.819  1.00 20.17           C  
ANISOU 2296  CA  GLN A 292     3358   2297   2010   1587    446    275       C  
ATOM   2297  C   GLN A 292      34.645  -4.583 -13.831  1.00 27.84           C  
ANISOU 2297  C   GLN A 292     4338   3288   2953   1586    422    265       C  
ATOM   2298  O   GLN A 292      34.857  -3.851 -14.818  1.00 24.06           O  
ANISOU 2298  O   GLN A 292     3856   2816   2470   1588    413    263       O  
ATOM   2299  CB  GLN A 292      34.219  -3.807 -11.522  1.00 20.11           C  
ANISOU 2299  CB  GLN A 292     3375   2289   1978   1584    466    279       C  
ATOM   2300  CG  GLN A 292      33.244  -3.399 -10.444  1.00 35.76           C  
ANISOU 2300  CG  GLN A 292     5352   4252   3984   1586    492    288       C  
ATOM   2301  CD  GLN A 292      33.938  -2.824  -9.226  1.00 35.25           C  
ANISOU 2301  CD  GLN A 292     5311   4187   3894   1583    512    292       C  
ATOM   2302  NE2 GLN A 292      33.596  -3.333  -8.060  1.00 34.07           N  
ANISOU 2302  NE2 GLN A 292     5165   4028   3752   1581    527    296       N  
ATOM   2303  OE1 GLN A 292      34.779  -1.938  -9.339  1.00 38.07           O  
ANISOU 2303  OE1 GLN A 292     5685   4553   4227   1582    513    293       O  
ATOM   2304  N   GLU A 293      35.317  -5.705 -13.573  1.00 31.68           N  
ANISOU 2304  N   GLU A 293     4833   3783   3420   1582    411    259       N  
ATOM   2305  CA  GLU A 293      36.416  -6.196 -14.412  1.00 30.33           C  
ANISOU 2305  CA  GLU A 293     4672   3633   3220   1579    387    249       C  
ATOM   2306  C   GLU A 293      35.957  -6.399 -15.851  1.00 28.68           C  
ANISOU 2306  C   GLU A 293     4443   3427   3029   1582    367    245       C  
ATOM   2307  O   GLU A 293      36.546  -5.876 -16.815  1.00 36.48           O  
ANISOU 2307  O   GLU A 293     5434   4426   4001   1583    355    240       O  
ATOM   2308  CB  GLU A 293      36.889  -7.532 -13.852  1.00 27.43           C  
ANISOU 2308  CB  GLU A 293     4313   3271   2839   1575    380    245       C  
ATOM   2309  CG  GLU A 293      38.314  -7.902 -14.109  1.00 31.40           C  
ANISOU 2309  CG  GLU A 293     4836   3794   3299   1571    364    236       C  
ATOM   2310  CD  GLU A 293      38.601  -9.324 -13.658  1.00 40.61           C  
ANISOU 2310  CD  GLU A 293     6007   4965   4458   1567    355    231       C  
ATOM   2311  OE1 GLU A 293      37.640 -10.139 -13.592  1.00 42.61           O  
ANISOU 2311  OE1 GLU A 293     6242   5207   4742   1568    354    232       O  
ATOM   2312  OE2 GLU A 293      39.783  -9.623 -13.366  1.00 41.00           O1-
ANISOU 2312  OE2 GLU A 293     6078   5029   4472   1563    349    226       O1-
ATOM   2313  N   GLU A 294      34.891  -7.168 -15.992  1.00 24.12           N  
ANISOU 2313  N   GLU A 294     3843   2838   2485   1584    363    246       N  
ATOM   2314  CA  GLU A 294      34.389  -7.497 -17.314  1.00 26.52           C  
ANISOU 2314  CA  GLU A 294     4126   3143   2809   1586    344    242       C  
ATOM   2315  C   GLU A 294      33.958  -6.257 -18.078  1.00 26.89           C  
ANISOU 2315  C   GLU A 294     4163   3186   2869   1590    347    246       C  
ATOM   2316  O   GLU A 294      34.243  -6.147 -19.263  1.00 29.46           O  
ANISOU 2316  O   GLU A 294     4484   3521   3189   1591    329    241       O  
ATOM   2317  CB  GLU A 294      33.258  -8.521 -17.240  1.00 31.69           C  
ANISOU 2317  CB  GLU A 294     4759   3784   3499   1587    341    244       C  
ATOM   2318  CG  GLU A 294      33.701  -9.851 -16.679  1.00 41.53           C  
ANISOU 2318  CG  GLU A 294     6012   5035   4732   1583    334    239       C  
ATOM   2319  CD  GLU A 294      32.784 -10.989 -17.083  1.00 56.84           C  
ANISOU 2319  CD  GLU A 294     7929   6967   6703   1584    321    238       C  
ATOM   2320  OE1 GLU A 294      33.297 -11.969 -17.672  1.00 68.03           O  
ANISOU 2320  OE1 GLU A 294     9346   8395   8108   1581    300    229       O  
ATOM   2321  OE2 GLU A 294      31.563 -10.908 -16.811  1.00 51.34           O1-
ANISOU 2321  OE2 GLU A 294     7213   6252   6041   1587    332    245       O1-
ATOM   2322  N   ALA A 295      33.290  -5.318 -17.406  1.00 26.48           N  
ANISOU 2322  N   ALA A 295     4109   3120   2833   1593    369    255       N  
ATOM   2323  CA  ALA A 295      32.840  -4.108 -18.073  1.00 21.93           C  
ANISOU 2323  CA  ALA A 295     3523   2539   2271   1597    373    259       C  
ATOM   2324  C   ALA A 295      34.044  -3.315 -18.553  1.00 25.19           C  
ANISOU 2324  C   ALA A 295     3954   2968   2648   1596    368    255       C  
ATOM   2325  O   ALA A 295      34.071  -2.810 -19.675  1.00 23.62           O  
ANISOU 2325  O   ALA A 295     3749   2776   2452   1598    356    253       O  
ATOM   2326  CB  ALA A 295      32.009  -3.284 -17.153  1.00 20.38           C  
ANISOU 2326  CB  ALA A 295     3323   2325   2094   1599    399    269       C  
ATOM   2327  N   CYS A 296      35.051  -3.215 -17.705  1.00 19.91           N  
ANISOU 2327  N   CYS A 296     3311   2307   1946   1592    376    254       N  
ATOM   2328  CA  CYS A 296      36.235  -2.475 -18.083  1.00 19.75           C  
ANISOU 2328  CA  CYS A 296     3310   2303   1891   1591    371    250       C  
ATOM   2329  C   CYS A 296      36.905  -3.070 -19.311  1.00 32.45           C  
ANISOU 2329  C   CYS A 296     4917   3928   3483   1590    344    240       C  
ATOM   2330  O   CYS A 296      37.406  -2.349 -20.177  1.00 28.71           O  
ANISOU 2330  O   CYS A 296     4447   3465   2997   1591    335    237       O  
ATOM   2331  CB  CYS A 296      37.213  -2.488 -16.938  1.00 19.88           C  
ANISOU 2331  CB  CYS A 296     3352   2325   1875   1587    381    251       C  
ATOM   2332  SG  CYS A 296      38.711  -1.686 -17.329  1.00 26.78           S  
ANISOU 2332  SG  CYS A 296     4251   3220   2705   1585    374    246       S  
ATOM   2333  N   ILE A 297      36.922  -4.399 -19.365  1.00 33.76           N  
ANISOU 2333  N   ILE A 297     5079   4098   3651   1588    330    234       N  
ATOM   2334  CA  ILE A 297      37.504  -5.124 -20.481  1.00 19.43           C  
ANISOU 2334  CA  ILE A 297     3262   2299   1823   1586    304    223       C  
ATOM   2335  C   ILE A 297      36.666  -4.925 -21.748  1.00 26.92           C  
ANISOU 2335  C   ILE A 297     4187   3243   2800   1590    292    223       C  
ATOM   2336  O   ILE A 297      37.205  -4.777 -22.852  1.00 30.88           O  
ANISOU 2336  O   ILE A 297     4688   3757   3287   1590    275    217       O  
ATOM   2337  CB  ILE A 297      37.638  -6.622 -20.110  1.00 24.79           C  
ANISOU 2337  CB  ILE A 297     3941   2980   2497   1583    294    218       C  
ATOM   2338  CG1 ILE A 297      38.815  -6.829 -19.138  1.00 25.59           C  
ANISOU 2338  CG1 ILE A 297     4070   3092   2561   1578    299    216       C  
ATOM   2339  CG2 ILE A 297      37.806  -7.498 -21.339  1.00 21.05           C  
ANISOU 2339  CG2 ILE A 297     3458   2517   2024   1582    267    208       C  
ATOM   2340  CD1 ILE A 297      38.876  -8.211 -18.468  1.00 19.14           C  
ANISOU 2340  CD1 ILE A 297     3256   2275   1743   1575    295    212       C  
ATOM   2341  N   LEU A 298      35.344  -4.896 -21.573  1.00 30.49           N  
ANISOU 2341  N   LEU A 298     4617   3676   3291   1593    302    231       N  
ATOM   2342  CA  LEU A 298      34.373  -4.810 -22.672  1.00 29.88           C  
ANISOU 2342  CA  LEU A 298     4515   3592   3246   1597    291    233       C  
ATOM   2343  C   LEU A 298      34.137  -3.390 -23.157  1.00 32.59           C  
ANISOU 2343  C   LEU A 298     4855   3932   3596   1601    299    238       C  
ATOM   2344  O   LEU A 298      33.256  -3.162 -23.974  1.00 29.89           O  
ANISOU 2344  O   LEU A 298     4492   3583   3283   1605    294    240       O  
ATOM   2345  CB  LEU A 298      33.032  -5.369 -22.223  1.00 20.09           C  
ANISOU 2345  CB  LEU A 298     3254   2333   2047   1599    299    239       C  
ATOM   2346  CG  LEU A 298      32.930  -6.864 -21.996  1.00 28.26           C  
ANISOU 2346  CG  LEU A 298     4283   3367   3085   1596    288    235       C  
ATOM   2347  CD1 LEU A 298      31.619  -7.214 -21.307  1.00 20.25           C  
ANISOU 2347  CD1 LEU A 298     3252   2333   2110   1598    301    243       C  
ATOM   2348  CD2 LEU A 298      33.079  -7.587 -23.326  1.00 20.42           C  
ANISOU 2348  CD2 LEU A 298     3281   2385   2094   1596    261    227       C  
ATOM   2349  N   LYS A 299      34.902  -2.445 -22.616  1.00 41.05           N  
ANISOU 2349  N   LYS A 299     5946   5008   4642   1600    313    239       N  
ATOM   2350  CA  LYS A 299      34.759  -1.024 -22.918  1.00 38.74           C  
ANISOU 2350  CA  LYS A 299     5653   4713   4353   1604    323    245       C  
ATOM   2351  C   LYS A 299      33.363  -0.450 -22.634  1.00 37.65           C  
ANISOU 2351  C   LYS A 299     5495   4554   4255   1608    339    255       C  
ATOM   2352  O   LYS A 299      32.897   0.423 -23.362  1.00 37.23           O  
ANISOU 2352  O   LYS A 299     5431   4497   4217   1612    339    258       O  
ATOM   2353  CB  LYS A 299      35.151  -0.746 -24.364  1.00 39.27           C  
ANISOU 2353  CB  LYS A 299     5716   4793   4412   1605    303    238       C  
ATOM   2354  CG  LYS A 299      36.562  -1.145 -24.708  1.00 45.17           C  
ANISOU 2354  CG  LYS A 299     6484   5562   5118   1601    287    228       C  
ATOM   2355  CD  LYS A 299      37.563  -0.150 -24.173  1.00 52.55           C  
ANISOU 2355  CD  LYS A 299     7443   6505   6021   1600    299    229       C  
ATOM   2356  CE  LYS A 299      38.962  -0.501 -24.639  1.00 58.46           C  
ANISOU 2356  CE  LYS A 299     8210   7275   6728   1596    282    218       C  
ATOM   2357  NZ  LYS A 299      39.984   0.289 -23.925  1.00 61.24           N1+
ANISOU 2357  NZ  LYS A 299     8587   7635   7046   1594    294    219       N1+
ATOM   2358  N   VAL A 300      32.709  -0.940 -21.582  1.00 38.22           N  
ANISOU 2358  N   VAL A 300     5565   4613   4345   1607    353    260       N  
ATOM   2359  CA  VAL A 300      31.426  -0.399 -21.118  1.00 35.50           C  
ANISOU 2359  CA  VAL A 300     5204   4248   4036   1611    371    270       C  
ATOM   2360  C   VAL A 300      31.642   0.382 -19.820  1.00 35.02           C  
ANISOU 2360  C   VAL A 300     5161   4182   3964   1610    397    276       C  
ATOM   2361  O   VAL A 300      32.226  -0.147 -18.868  1.00 43.40           O  
ANISOU 2361  O   VAL A 300     6238   5246   5005   1607    403    274       O  
ATOM   2362  CB  VAL A 300      30.402  -1.525 -20.861  1.00 20.64           C  
ANISOU 2362  CB  VAL A 300     3304   2354   2186   1612    369    271       C  
ATOM   2363  CG1 VAL A 300      29.047  -0.955 -20.513  1.00 20.88           C  
ANISOU 2363  CG1 VAL A 300     3315   2364   2254   1616    386    281       C  
ATOM   2364  CG2 VAL A 300      30.276  -2.422 -22.079  1.00 20.62           C  
ANISOU 2364  CG2 VAL A 300     3285   2358   2192   1612    342    265       C  
ATOM   2365  N   PRO A 301      31.179   1.641 -19.776  1.00 30.73           N  
ANISOU 2365  N   PRO A 301     4614   3629   3432   1614    413    282       N  
ATOM   2366  CA  PRO A 301      31.310   2.470 -18.576  1.00 26.56           C  
ANISOU 2366  CA  PRO A 301     4101   3094   2895   1613    438    289       C  
ATOM   2367  C   PRO A 301      30.708   1.774 -17.367  1.00 26.89           C  
ANISOU 2367  C   PRO A 301     4141   3123   2951   1612    453    293       C  
ATOM   2368  O   PRO A 301      29.699   1.063 -17.481  1.00 24.89           O  
ANISOU 2368  O   PRO A 301     3868   2860   2729   1614    449    294       O  
ATOM   2369  CB  PRO A 301      30.487   3.711 -18.922  1.00 24.45           C  
ANISOU 2369  CB  PRO A 301     3822   2817   2653   1618    450    296       C  
ATOM   2370  CG  PRO A 301      30.429   3.742 -20.385  1.00 22.49           C  
ANISOU 2370  CG  PRO A 301     3559   2575   2410   1620    428    292       C  
ATOM   2371  CD  PRO A 301      30.404   2.323 -20.822  1.00 31.77           C  
ANISOU 2371  CD  PRO A 301     4726   3756   3590   1618    408    285       C  
ATOM   2372  N   CYS A 302      31.332   1.971 -16.213  1.00 29.07           N  
ANISOU 2372  N   CYS A 302     4439   3400   3205   1609    469    294       N  
ATOM   2373  CA  CYS A 302      30.899   1.274 -15.017  1.00 28.62           C  
ANISOU 2373  CA  CYS A 302     4384   3334   3158   1607    482    298       C  
ATOM   2374  C   CYS A 302      30.723   2.191 -13.805  1.00 37.69           C  
ANISOU 2374  C   CYS A 302     5543   4471   4306   1607    511    305       C  
ATOM   2375  O   CYS A 302      31.595   3.020 -13.465  1.00 42.87           O  
ANISOU 2375  O   CYS A 302     6219   5134   4934   1605    519    306       O  
ATOM   2376  CB  CYS A 302      31.859   0.124 -14.703  1.00 23.84           C  
ANISOU 2376  CB  CYS A 302     3792   2741   2524   1602    471    291       C  
ATOM   2377  SG  CYS A 302      31.304  -0.993 -13.421  1.00 27.78           S  
ANISOU 2377  SG  CYS A 302     4290   3229   3037   1600    482    293       S  
ATOM   2378  N   ILE A 303      29.576   2.023 -13.156  1.00 37.19           N  
ANISOU 2378  N   ILE A 303     5467   4391   4274   1609    526    311       N  
ATOM   2379  CA  ILE A 303      29.289   2.679 -11.890  1.00 37.76           C  
ANISOU 2379  CA  ILE A 303     5548   4451   4349   1609    553    319       C  
ATOM   2380  C   ILE A 303      29.104   1.640 -10.784  1.00 38.23           C  
ANISOU 2380  C   ILE A 303     5611   4505   4411   1606    561    319       C  
ATOM   2381  O   ILE A 303      28.276   0.720 -10.886  1.00 35.08           O  
ANISOU 2381  O   ILE A 303     5194   4099   4037   1607    555    318       O  
ATOM   2382  CB  ILE A 303      28.051   3.609 -11.984  1.00 27.70           C  
ANISOU 2382  CB  ILE A 303     4256   3160   3109   1614    568    326       C  
ATOM   2383  CG1 ILE A 303      28.350   4.778 -12.915  1.00 30.39           C  
ANISOU 2383  CG1 ILE A 303     4597   3508   3443   1616    563    326       C  
ATOM   2384  CG2 ILE A 303      27.687   4.159 -10.626  1.00 26.49           C  
ANISOU 2384  CG2 ILE A 303     4111   2994   2959   1613    597    333       C  
ATOM   2385  CD1 ILE A 303      27.134   5.345 -13.572  1.00 36.36           C  
ANISOU 2385  CD1 ILE A 303     5329   4251   4236   1622    566    330       C  
ATOM   2386  N   THR A 304      29.884   1.816  -9.722  1.00 42.06           N  
ANISOU 2386  N   THR A 304     6119   4992   4868   1602    575    321       N  
ATOM   2387  CA  THR A 304      29.950   0.862  -8.621  1.00 38.06           C  
ANISOU 2387  CA  THR A 304     5621   4483   4358   1598    582    321       C  
ATOM   2388  C   THR A 304      29.288   1.373  -7.334  1.00 41.58           C  
ANISOU 2388  C   THR A 304     6070   4912   4816   1599    611    329       C  
ATOM   2389  O   THR A 304      29.715   2.369  -6.747  1.00 43.30           O  
ANISOU 2389  O   THR A 304     6304   5130   5019   1598    627    333       O  
ATOM   2390  CB  THR A 304      31.417   0.528  -8.301  1.00 34.33           C  
ANISOU 2390  CB  THR A 304     5175   4028   3843   1593    574    316       C  
ATOM   2391  CG2 THR A 304      31.501  -0.429  -7.122  1.00 29.32           C  
ANISOU 2391  CG2 THR A 304     4548   3389   3202   1589    583    317       C  
ATOM   2392  OG1 THR A 304      32.043  -0.035  -9.465  1.00 32.10           O  
ANISOU 2392  OG1 THR A 304     4889   3760   3548   1593    547    308       O  
ATOM   2393  N   LEU A 305      28.260   0.655  -6.896  1.00 40.71           N  
ANISOU 2393  N   LEU A 305     5945   4790   4735   1600    617    331       N  
ATOM   2394  CA  LEU A 305      27.498   0.967  -5.695  1.00 38.56           C  
ANISOU 2394  CA  LEU A 305     5672   4501   4478   1601    643    338       C  
ATOM   2395  C   LEU A 305      28.181   0.473  -4.396  1.00 42.98           C  
ANISOU 2395  C   LEU A 305     6253   5062   5014   1595    655    339       C  
ATOM   2396  O   LEU A 305      27.553  -0.163  -3.552  1.00 45.49           O  
ANISOU 2396  O   LEU A 305     6567   5371   5347   1595    666    341       O  
ATOM   2397  CB  LEU A 305      26.106   0.339  -5.824  1.00 36.59           C  
ANISOU 2397  CB  LEU A 305     5396   4238   4269   1604    643    340       C  
ATOM   2398  CG  LEU A 305      25.449   0.458  -7.209  1.00 34.16           C  
ANISOU 2398  CG  LEU A 305     5065   3929   3985   1609    626    339       C  
ATOM   2399  CD1 LEU A 305      24.223  -0.422  -7.341  1.00 24.37           C  
ANISOU 2399  CD1 LEU A 305     3800   2677   2781   1612    622    340       C  
ATOM   2400  CD2 LEU A 305      25.085   1.910  -7.548  1.00 35.44           C  
ANISOU 2400  CD2 LEU A 305     5223   4086   4156   1613    638    344       C  
ATOM   2401  N   ARG A 306      29.469   0.761  -4.252  1.00 36.48           N  
ANISOU 2401  N   ARG A 306     5454   4253   4154   1592    652    337       N  
ATOM   2402  CA  ARG A 306      30.207   0.501  -3.025  1.00 29.46           C  
ANISOU 2402  CA  ARG A 306     4588   3366   3241   1587    663    338       C  
ATOM   2403  C   ARG A 306      31.107   1.695  -2.817  1.00 34.06           C  
ANISOU 2403  C   ARG A 306     5192   3954   3796   1585    672    341       C  
ATOM   2404  O   ARG A 306      31.208   2.549  -3.691  1.00 31.60           O  
ANISOU 2404  O   ARG A 306     4876   3646   3483   1588    666    340       O  
ATOM   2405  CB  ARG A 306      31.083  -0.737  -3.159  1.00 35.56           C  
ANISOU 2405  CB  ARG A 306     5369   4152   3991   1583    643    331       C  
ATOM   2406  CG  ARG A 306      30.361  -2.004  -3.572  1.00 46.26           C  
ANISOU 2406  CG  ARG A 306     6703   5504   5369   1584    629    327       C  
ATOM   2407  CD  ARG A 306      31.262  -3.210  -3.338  1.00 53.75           C  
ANISOU 2407  CD  ARG A 306     7664   6465   6293   1580    615    321       C  
ATOM   2408  NE  ARG A 306      31.670  -3.281  -1.939  1.00 57.62           N  
ANISOU 2408  NE  ARG A 306     8174   6952   6767   1576    633    325       N  
ATOM   2409  CZ  ARG A 306      32.886  -3.613  -1.517  1.00 54.72           C  
ANISOU 2409  CZ  ARG A 306     7829   6597   6365   1571    628    323       C  
ATOM   2410  NH1 ARG A 306      33.836  -3.926  -2.384  1.00 46.30           N1+
ANISOU 2410  NH1 ARG A 306     6770   5548   5276   1569    605    316       N1+
ATOM   2411  NH2 ARG A 306      33.145  -3.633  -0.217  1.00 59.10           N  
ANISOU 2411  NH2 ARG A 306     8401   7147   6908   1567    646    327       N  
ATOM   2412  N   ASP A 307      31.782   1.761  -1.677  1.00 43.24           N  
ANISOU 2412  N   ASP A 307     6377   5118   4936   1581    685    344       N  
ATOM   2413  CA  ASP A 307      32.651   2.902  -1.412  1.00 48.64           C  
ANISOU 2413  CA  ASP A 307     7081   5806   5594   1579    694    347       C  
ATOM   2414  C   ASP A 307      34.104   2.479  -1.521  1.00 48.64           C  
ANISOU 2414  C   ASP A 307     7102   5823   5555   1574    677    342       C  
ATOM   2415  O   ASP A 307      35.008   3.296  -1.710  1.00 40.79           O  
ANISOU 2415  O   ASP A 307     6123   4838   4536   1573    675    343       O  
ATOM   2416  CB  ASP A 307      32.322   3.534  -0.056  1.00 52.95           C  
ANISOU 2416  CB  ASP A 307     7638   6338   6144   1578    723    355       C  
ATOM   2417  CG  ASP A 307      30.934   4.169  -0.033  1.00 64.41           C  
ANISOU 2417  CG  ASP A 307     9069   7772   7632   1583    740    360       C  
ATOM   2418  OD1 ASP A 307      30.784   5.308  -0.532  1.00 68.91           O  
ANISOU 2418  OD1 ASP A 307     9635   8340   8206   1585    744    363       O  
ATOM   2419  OD2 ASP A 307      29.987   3.523   0.468  1.00 68.36           O1-
ANISOU 2419  OD2 ASP A 307     9557   8261   8156   1584    748    362       O1-
ATOM   2420  N   ASN A 308      34.304   1.176  -1.408  1.00 62.31           N  
ANISOU 2420  N   ASN A 308     8833   7561   7282   1572    665    338       N  
ATOM   2421  CA  ASN A 308      35.592   0.567  -1.685  1.00 70.67           C  
ANISOU 2421  CA  ASN A 308     9908   8637   8306   1568    645    332       C  
ATOM   2422  C   ASN A 308      35.437  -0.513  -2.768  1.00 64.86           C  
ANISOU 2422  C   ASN A 308     9156   7910   7580   1570    620    323       C  
ATOM   2423  O   ASN A 308      34.361  -1.104  -2.920  1.00 66.29           O  
ANISOU 2423  O   ASN A 308     9315   8081   7791   1572    620    323       O  
ATOM   2424  CB  ASN A 308      36.210  -0.001  -0.404  1.00 73.85           C  
ANISOU 2424  CB  ASN A 308    10330   9040   8688   1563    654    334       C  
ATOM   2425  CG  ASN A 308      37.660  -0.397  -0.595  1.00 84.01           C  
ANISOU 2425  CG  ASN A 308    11638  10346   9937   1559    635    330       C  
ATOM   2426  ND2 ASN A 308      38.229  -1.078   0.395  1.00 83.84           N  
ANISOU 2426  ND2 ASN A 308    11632  10325   9897   1555    638    331       N  
ATOM   2427  OD1 ASN A 308      38.265  -0.093  -1.630  1.00 89.33           O  
ANISOU 2427  OD1 ASN A 308    12313  11032  10597   1560    618    325       O  
ATOM   2428  N   THR A 309      36.495  -0.759  -3.533  1.00 51.75           N  
ANISOU 2428  N   THR A 309     7504   6267   5891   1568    598    317       N  
ATOM   2429  CA  THR A 309      36.396  -1.708  -4.639  1.00 53.76           C  
ANISOU 2429  CA  THR A 309     7743   6530   6153   1569    574    309       C  
ATOM   2430  C   THR A 309      37.516  -2.743  -4.586  1.00 54.54           C  
ANISOU 2430  C   THR A 309     7857   6645   6222   1565    556    303       C  
ATOM   2431  O   THR A 309      38.664  -2.412  -4.288  1.00 55.98           O  
ANISOU 2431  O   THR A 309     8062   6838   6370   1561    555    303       O  
ATOM   2432  CB  THR A 309      36.367  -0.973  -6.025  1.00 40.53           C  
ANISOU 2432  CB  THR A 309     6057   4861   4482   1573    560    306       C  
ATOM   2433  CG2 THR A 309      37.515  -0.001  -6.141  1.00 45.00           C  
ANISOU 2433  CG2 THR A 309     6644   5438   5015   1571    559    306       C  
ATOM   2434  OG1 THR A 309      36.433  -1.913  -7.105  1.00 31.30           O  
ANISOU 2434  OG1 THR A 309     4875   3702   3315   1573    535    297       O  
ATOM   2435  N   GLU A 310      37.174  -4.000  -4.862  1.00 48.62           N  
ANISOU 2435  N   GLU A 310     7095   5896   5483   1565    543    297       N  
ATOM   2436  CA  GLU A 310      38.182  -5.046  -4.940  1.00 44.03           C  
ANISOU 2436  CA  GLU A 310     6525   5329   4874   1561    524    290       C  
ATOM   2437  C   GLU A 310      38.869  -5.081  -6.315  1.00 46.81           C  
ANISOU 2437  C   GLU A 310     6876   5699   5210   1561    499    282       C  
ATOM   2438  O   GLU A 310      39.688  -5.955  -6.569  1.00 47.28           O  
ANISOU 2438  O   GLU A 310     6943   5772   5248   1558    481    275       O  
ATOM   2439  CB  GLU A 310      37.601  -6.417  -4.555  1.00 44.30           C  
ANISOU 2439  CB  GLU A 310     6549   5359   4926   1560    521    288       C  
ATOM   2440  CG  GLU A 310      36.531  -6.970  -5.491  1.00 51.62           C  
ANISOU 2440  CG  GLU A 310     7447   6280   5887   1564    510    284       C  
ATOM   2441  CD  GLU A 310      35.133  -6.970  -4.882  1.00 57.35           C  
ANISOU 2441  CD  GLU A 310     8156   6985   6651   1566    529    291       C  
ATOM   2442  OE1 GLU A 310      34.526  -5.882  -4.777  1.00 63.94           O  
ANISOU 2442  OE1 GLU A 310     8985   7809   7501   1569    545    297       O  
ATOM   2443  OE2 GLU A 310      34.633  -8.060  -4.524  1.00 53.15           O1-
ANISOU 2443  OE2 GLU A 310     7614   6448   6134   1566    527    290       O1-
ATOM   2444  N   ARG A 311      38.525  -4.142  -7.201  1.00 48.13           N  
ANISOU 2444  N   ARG A 311     7032   5865   5389   1565    497    283       N  
ATOM   2445  CA  ARG A 311      39.278  -3.928  -8.450  1.00 47.34           C  
ANISOU 2445  CA  ARG A 311     6935   5782   5271   1565    476    276       C  
ATOM   2446  C   ARG A 311      39.478  -2.429  -8.712  1.00 47.17           C  
ANISOU 2446  C   ARG A 311     6920   5761   5243   1567    485    280       C  
ATOM   2447  O   ARG A 311      38.998  -1.899  -9.703  1.00 46.01           O  
ANISOU 2447  O   ARG A 311     6757   5612   5112   1571    479    279       O  
ATOM   2448  CB  ARG A 311      38.591  -4.579  -9.670  1.00 43.13           C  
ANISOU 2448  CB  ARG A 311     6378   5250   4762   1568    457    269       C  
ATOM   2449  CG  ARG A 311      38.129  -6.032  -9.503  1.00 47.48           C  
ANISOU 2449  CG  ARG A 311     6917   5798   5327   1567    449    265       C  
ATOM   2450  CD  ARG A 311      39.233  -7.084  -9.717  1.00 52.17           C  
ANISOU 2450  CD  ARG A 311     7523   6408   5890   1563    428    257       C  
ATOM   2451  NE  ARG A 311      38.646  -8.364 -10.127  1.00 56.53           N  
ANISOU 2451  NE  ARG A 311     8057   6958   6462   1563    415    251       N  
ATOM   2452  CZ  ARG A 311      38.459  -9.409  -9.328  1.00 59.68           C  
ANISOU 2452  CZ  ARG A 311     8457   7353   6866   1561    417    251       C  
ATOM   2453  NH1 ARG A 311      38.842  -9.350  -8.059  1.00 69.61           N1+
ANISOU 2453  NH1 ARG A 311     9732   8607   8108   1558    434    256       N1+
ATOM   2454  NH2 ARG A 311      37.903 -10.523  -9.800  1.00 51.08           N  
ANISOU 2454  NH2 ARG A 311     7351   6262   5797   1562    404    247       N  
ATOM   2455  N   PRO A 312      40.205  -1.742  -7.824  1.00 47.86           N  
ANISOU 2455  N   PRO A 312     7029   5848   5306   1565    498    286       N  
ATOM   2456  CA  PRO A 312      40.382  -0.288  -7.897  1.00 39.56           C  
ANISOU 2456  CA  PRO A 312     5985   4796   4250   1566    509    291       C  
ATOM   2457  C   PRO A 312      41.038   0.239  -9.168  1.00 42.27           C  
ANISOU 2457  C   PRO A 312     6330   5154   4578   1568    491    286       C  
ATOM   2458  O   PRO A 312      40.861   1.415  -9.498  1.00 50.50           O  
ANISOU 2458  O   PRO A 312     7370   6193   5625   1570    499    289       O  
ATOM   2459  CB  PRO A 312      41.274   0.003  -6.695  1.00 37.60           C  
ANISOU 2459  CB  PRO A 312     5764   4549   3974   1562    522    297       C  
ATOM   2460  CG  PRO A 312      41.969  -1.268  -6.428  1.00 37.61           C  
ANISOU 2460  CG  PRO A 312     5775   4561   3955   1558    508    291       C  
ATOM   2461  CD  PRO A 312      40.968  -2.321  -6.708  1.00 42.80           C  
ANISOU 2461  CD  PRO A 312     6410   5212   4642   1560    503    287       C  
ATOM   2462  N   GLU A 313      41.781  -0.608  -9.866  1.00 37.97           N  
ANISOU 2462  N   GLU A 313     5789   4626   4013   1566    468    277       N  
ATOM   2463  CA  GLU A 313      42.461  -0.208 -11.098  1.00 38.22           C  
ANISOU 2463  CA  GLU A 313     5821   4672   4027   1567    449    270       C  
ATOM   2464  C   GLU A 313      41.473   0.287 -12.175  1.00 34.30           C  
ANISOU 2464  C   GLU A 313     5301   4169   3562   1572    447    270       C  
ATOM   2465  O   GLU A 313      41.810   1.152 -12.994  1.00 31.99           O  
ANISOU 2465  O   GLU A 313     5009   3884   3261   1574    441    268       O  
ATOM   2466  CB  GLU A 313      43.344  -1.359 -11.619  1.00 39.20           C  
ANISOU 2466  CB  GLU A 313     5952   4814   4128   1564    425    260       C  
ATOM   2467  CG  GLU A 313      42.608  -2.684 -11.875  1.00 49.37           C  
ANISOU 2467  CG  GLU A 313     7222   6099   5439   1564    415    255       C  
ATOM   2468  CD  GLU A 313      42.353  -3.507 -10.612  1.00 55.78           C  
ANISOU 2468  CD  GLU A 313     8037   6901   6255   1562    426    258       C  
ATOM   2469  OE1 GLU A 313      42.649  -3.016  -9.512  1.00 62.47           O  
ANISOU 2469  OE1 GLU A 313     8901   7743   7091   1560    444    266       O  
ATOM   2470  OE2 GLU A 313      41.853  -4.649 -10.719  1.00 56.69           O1-
ANISOU 2470  OE2 GLU A 313     8140   7014   6386   1561    418    254       O1-
ATOM   2471  N   THR A 314      40.247  -0.239 -12.144  1.00 28.07           N  
ANISOU 2471  N   THR A 314     4491   3367   2809   1574    451    271       N  
ATOM   2472  CA  THR A 314      39.203   0.209 -13.054  1.00 33.15           C  
ANISOU 2472  CA  THR A 314     5110   4002   3485   1579    450    272       C  
ATOM   2473  C   THR A 314      38.829   1.671 -12.797  1.00 34.19           C  
ANISOU 2473  C   THR A 314     5243   4124   3626   1582    470    280       C  
ATOM   2474  O   THR A 314      38.469   2.395 -13.722  1.00 29.63           O  
ANISOU 2474  O   THR A 314     4653   3545   3060   1586    466    280       O  
ATOM   2475  CB  THR A 314      37.946  -0.667 -12.966  1.00 35.34           C  
ANISOU 2475  CB  THR A 314     5364   4265   3799   1581    451    272       C  
ATOM   2476  CG2 THR A 314      38.259  -2.103 -13.361  1.00 29.96           C  
ANISOU 2476  CG2 THR A 314     4679   3594   3110   1579    430    264       C  
ATOM   2477  OG1 THR A 314      37.430  -0.631 -11.629  1.00 35.31           O  
ANISOU 2477  OG1 THR A 314     5364   4247   3807   1581    474    280       O  
ATOM   2478  N   VAL A 315      38.899   2.102 -11.538  1.00 36.77           N  
ANISOU 2478  N   VAL A 315     5582   4441   3946   1580    491    287       N  
ATOM   2479  CA  VAL A 315      38.699   3.513 -11.226  1.00 40.27           C  
ANISOU 2479  CA  VAL A 315     6031   4877   4395   1582    511    295       C  
ATOM   2480  C   VAL A 315      39.909   4.321 -11.690  1.00 44.74           C  
ANISOU 2480  C   VAL A 315     6615   5458   4927   1581    503    293       C  
ATOM   2481  O   VAL A 315      39.769   5.448 -12.163  1.00 48.46           O  
ANISOU 2481  O   VAL A 315     7083   5927   5403   1584    508    296       O  
ATOM   2482  CB  VAL A 315      38.443   3.766  -9.722  1.00 39.83           C  
ANISOU 2482  CB  VAL A 315     5985   4807   4342   1580    536    303       C  
ATOM   2483  CG1 VAL A 315      38.393   5.256  -9.436  1.00 19.91           C  
ANISOU 2483  CG1 VAL A 315     3469   2277   1819   1582    555    311       C  
ATOM   2484  CG2 VAL A 315      37.144   3.091  -9.261  1.00 36.75           C  
ANISOU 2484  CG2 VAL A 315     5575   4400   3987   1582    546    306       C  
ATOM   2485  N   GLU A 316      41.096   3.731 -11.592  1.00 50.53           N  
ANISOU 2485  N   GLU A 316     7366   6206   5626   1577    490    288       N  
ATOM   2486  CA  GLU A 316      42.312   4.464 -11.948  1.00 54.74           C  
ANISOU 2486  CA  GLU A 316     7920   6755   6126   1575    482    287       C  
ATOM   2487  C   GLU A 316      42.390   4.803 -13.445  1.00 51.68           C  
ANISOU 2487  C   GLU A 316     7521   6377   5739   1578    464    281       C  
ATOM   2488  O   GLU A 316      42.881   5.863 -13.810  1.00 55.19           O  
ANISOU 2488  O   GLU A 316     7974   6827   6170   1579    465    283       O  
ATOM   2489  CB  GLU A 316      43.573   3.723 -11.463  1.00 62.26           C  
ANISOU 2489  CB  GLU A 316     8894   7721   7041   1570    472    284       C  
ATOM   2490  CG  GLU A 316      44.903   4.392 -11.840  1.00 72.96           C  
ANISOU 2490  CG  GLU A 316    10270   9092   8358   1568    462    282       C  
ATOM   2491  CD  GLU A 316      45.486   5.287 -10.741  1.00 84.09           C  
ANISOU 2491  CD  GLU A 316    11701  10497   9750   1566    480    292       C  
ATOM   2492  OE1 GLU A 316      44.998   5.242  -9.586  1.00 83.88           O  
ANISOU 2492  OE1 GLU A 316    11678  10457   9737   1565    499    299       O  
ATOM   2493  OE2 GLU A 316      46.446   6.038 -11.041  1.00 88.06           O1-
ANISOU 2493  OE2 GLU A 316    12220  11012  10228   1565    474    293       O1-
ATOM   2494  N   VAL A 317      41.897   3.919 -14.309  1.00 47.73           N  
ANISOU 2494  N   VAL A 317     7001   5879   5254   1580    448    274       N  
ATOM   2495  CA  VAL A 317      41.961   4.174 -15.750  1.00 44.23           C  
ANISOU 2495  CA  VAL A 317     6548   5446   4813   1583    430    268       C  
ATOM   2496  C   VAL A 317      40.808   5.023 -16.269  1.00 36.81           C  
ANISOU 2496  C   VAL A 317     5587   4492   3907   1588    439    272       C  
ATOM   2497  O   VAL A 317      40.838   5.456 -17.425  1.00 38.21           O  
ANISOU 2497  O   VAL A 317     5756   4676   4087   1590    427    269       O  
ATOM   2498  CB  VAL A 317      41.973   2.875 -16.602  1.00 25.30           C  
ANISOU 2498  CB  VAL A 317     4139   3058   2417   1582    406    257       C  
ATOM   2499  CG1 VAL A 317      43.182   2.016 -16.288  1.00 18.91           C  
ANISOU 2499  CG1 VAL A 317     3350   2264   1571   1577    394    251       C  
ATOM   2500  CG2 VAL A 317      40.648   2.131 -16.462  1.00 21.04           C  
ANISOU 2500  CG2 VAL A 317     3576   2502   1916   1584    410    259       C  
ATOM   2501  N   GLY A 318      39.792   5.232 -15.430  1.00 29.13           N  
ANISOU 2501  N   GLY A 318     4605   3500   2962   1589    460    280       N  
ATOM   2502  CA  GLY A 318      38.634   6.017 -15.804  1.00 19.77           C  
ANISOU 2502  CA  GLY A 318     3399   2300   1810   1594    470    286       C  
ATOM   2503  C   GLY A 318      37.394   5.242 -16.182  1.00 30.17           C  
ANISOU 2503  C   GLY A 318     4690   3607   3165   1597    465    285       C  
ATOM   2504  O   GLY A 318      36.352   5.842 -16.446  1.00 28.44           O  
ANISOU 2504  O   GLY A 318     4454   3376   2977   1601    474    290       O  
ATOM   2505  N   ALA A 319      37.499   3.916 -16.204  1.00 34.85           N  
ANISOU 2505  N   ALA A 319     5281   4205   3756   1595    451    279       N  
ATOM   2506  CA  ALA A 319      36.397   3.045 -16.632  1.00 32.08           C  
ANISOU 2506  CA  ALA A 319     4905   3846   3439   1597    444    278       C  
ATOM   2507  C   ALA A 319      35.288   2.942 -15.596  1.00 30.26           C  
ANISOU 2507  C   ALA A 319     4665   3596   3238   1598    465    285       C  
ATOM   2508  O   ALA A 319      34.156   2.568 -15.915  1.00 28.56           O  
ANISOU 2508  O   ALA A 319     4427   3369   3057   1601    463    287       O  
ATOM   2509  CB  ALA A 319      36.932   1.655 -16.940  1.00 27.37           C  
ANISOU 2509  CB  ALA A 319     4310   3261   2828   1594    423    269       C  
ATOM   2510  N   ASN A 320      35.635   3.282 -14.357  1.00 27.63           N  
ANISOU 2510  N   ASN A 320     4349   3258   2890   1596    484    290       N  
ATOM   2511  CA  ASN A 320      34.822   2.978 -13.187  1.00 26.22           C  
ANISOU 2511  CA  ASN A 320     4166   3063   2732   1596    503    296       C  
ATOM   2512  C   ASN A 320      34.782   4.156 -12.215  1.00 28.34           C  
ANISOU 2512  C   ASN A 320     4447   3322   2997   1596    529    305       C  
ATOM   2513  O   ASN A 320      35.775   4.879 -12.021  1.00 25.45           O  
ANISOU 2513  O   ASN A 320     4102   2965   2603   1594    533    305       O  
ATOM   2514  CB  ASN A 320      35.401   1.753 -12.482  1.00 28.84           C  
ANISOU 2514  CB  ASN A 320     4510   3401   3046   1591    498    292       C  
ATOM   2515  CG  ASN A 320      34.403   1.050 -11.571  1.00 29.63           C  
ANISOU 2515  CG  ASN A 320     4600   3485   3173   1591    511    296       C  
ATOM   2516  ND2 ASN A 320      34.897   0.077 -10.806  1.00 29.20           N  
ANISOU 2516  ND2 ASN A 320     4557   3435   3103   1587    510    294       N  
ATOM   2517  OD1 ASN A 320      33.215   1.350 -11.569  1.00 21.17           O  
ANISOU 2517  OD1 ASN A 320     3510   2399   2135   1595    522    301       O  
ATOM   2518  N   ILE A 321      33.621   4.363 -11.617  1.00 27.60           N  
ANISOU 2518  N   ILE A 321     4340   3210   2935   1598    548    311       N  
ATOM   2519  CA  ILE A 321      33.525   5.383 -10.595  1.00 35.45           C  
ANISOU 2519  CA  ILE A 321     5346   4194   3928   1598    573    319       C  
ATOM   2520  C   ILE A 321      32.764   4.842  -9.357  1.00 42.56           C  
ANISOU 2520  C   ILE A 321     6244   5080   4846   1597    592    324       C  
ATOM   2521  O   ILE A 321      31.785   4.081  -9.496  1.00 40.39           O  
ANISOU 2521  O   ILE A 321     5950   4797   4601   1599    589    323       O  
ATOM   2522  CB  ILE A 321      32.934   6.676 -11.204  1.00 48.52           C  
ANISOU 2522  CB  ILE A 321     6991   5843   5601   1603    581    324       C  
ATOM   2523  CG1 ILE A 321      33.141   7.884 -10.300  1.00 54.79           C  
ANISOU 2523  CG1 ILE A 321     7801   6631   6386   1602    605    331       C  
ATOM   2524  CG2 ILE A 321      31.491   6.488 -11.526  1.00 60.27           C  
ANISOU 2524  CG2 ILE A 321     8452   7317   7131   1607    583    326       C  
ATOM   2525  CD1 ILE A 321      33.000   9.199 -11.054  1.00 57.60           C  
ANISOU 2525  CD1 ILE A 321     8152   6986   6748   1606    607    333       C  
ATOM   2526  N   LEU A 322      33.252   5.195  -8.158  1.00 38.30           N  
ANISOU 2526  N   LEU A 322     5725   4538   4289   1594    610    328       N  
ATOM   2527  CA  LEU A 322      32.670   4.712  -6.885  1.00 36.19           C  
ANISOU 2527  CA  LEU A 322     5459   4258   4034   1592    628    333       C  
ATOM   2528  C   LEU A 322      31.641   5.664  -6.260  1.00 35.85           C  
ANISOU 2528  C   LEU A 322     5408   4196   4016   1595    654    341       C  
ATOM   2529  O   LEU A 322      31.995   6.715  -5.735  1.00 38.89           O  
ANISOU 2529  O   LEU A 322     5808   4579   4389   1595    670    346       O  
ATOM   2530  CB  LEU A 322      33.775   4.426  -5.863  1.00 20.66           C  
ANISOU 2530  CB  LEU A 322     3519   2298   2033   1587    633    333       C  
ATOM   2531  CG  LEU A 322      34.760   3.297  -6.184  1.00 25.81           C  
ANISOU 2531  CG  LEU A 322     4179   2967   2659   1583    610    325       C  
ATOM   2532  CD1 LEU A 322      35.956   3.337  -5.267  1.00 22.12           C  
ANISOU 2532  CD1 LEU A 322     3741   2508   2156   1578    616    326       C  
ATOM   2533  CD2 LEU A 322      34.074   1.952  -6.098  1.00 27.17           C  
ANISOU 2533  CD2 LEU A 322     4336   3134   2851   1583    604    322       C  
ATOM   2534  N   VAL A 323      30.367   5.292  -6.303  1.00 36.67           N  
ANISOU 2534  N   VAL A 323     5490   4287   4156   1599    658    343       N  
ATOM   2535  CA  VAL A 323      29.310   6.143  -5.749  1.00 37.65           C  
ANISOU 2535  CA  VAL A 323     5605   4394   4307   1602    682    351       C  
ATOM   2536  C   VAL A 323      28.732   5.645  -4.427  1.00 44.90           C  
ANISOU 2536  C   VAL A 323     6524   5299   5235   1600    702    355       C  
ATOM   2537  O   VAL A 323      28.080   6.400  -3.714  1.00 48.78           O  
ANISOU 2537  O   VAL A 323     7016   5777   5742   1602    725    362       O  
ATOM   2538  CB  VAL A 323      28.130   6.289  -6.712  1.00 34.41           C  
ANISOU 2538  CB  VAL A 323     5167   3975   3932   1608    676    351       C  
ATOM   2539  CG1 VAL A 323      28.577   6.977  -7.958  1.00 21.51           C  
ANISOU 2539  CG1 VAL A 323     3530   2351   2290   1610    661    348       C  
ATOM   2540  CG2 VAL A 323      27.493   4.932  -7.003  1.00 27.52           C  
ANISOU 2540  CG2 VAL A 323     4276   3100   3079   1608    662    348       C  
ATOM   2541  N   GLY A 324      28.970   4.376  -4.113  1.00 48.95           N  
ANISOU 2541  N   GLY A 324     7040   5816   5743   1597    693    351       N  
ATOM   2542  CA  GLY A 324      28.411   3.756  -2.930  1.00 46.30           C  
ANISOU 2542  CA  GLY A 324     6705   5469   5418   1596    709    354       C  
ATOM   2543  C   GLY A 324      26.911   3.921  -2.830  1.00 50.79           C  
ANISOU 2543  C   GLY A 324     7251   6020   6027   1601    722    359       C  
ATOM   2544  O   GLY A 324      26.163   3.689  -3.784  1.00 55.73           O  
ANISOU 2544  O   GLY A 324     7854   6644   6678   1605    709    358       O  
ATOM   2545  N   ASP A 325      26.493   4.372  -1.656  1.00 50.93           N  
ANISOU 2545  N   ASP A 325     7276   6026   6051   1600    748    366       N  
ATOM   2546  CA  ASP A 325      25.095   4.475  -1.265  1.00 49.71           C  
ANISOU 2546  CA  ASP A 325     7103   5854   5933   1604    764    371       C  
ATOM   2547  C   ASP A 325      24.414   5.718  -1.863  1.00 47.92           C  
ANISOU 2547  C   ASP A 325     6864   5620   5725   1609    771    375       C  
ATOM   2548  O   ASP A 325      23.205   5.726  -2.140  1.00 44.45           O  
ANISOU 2548  O   ASP A 325     6402   5168   5319   1613    775    378       O  
ATOM   2549  CB  ASP A 325      25.065   4.544   0.262  1.00 55.00           C  
ANISOU 2549  CB  ASP A 325     7787   6514   6596   1601    790    376       C  
ATOM   2550  CG  ASP A 325      23.686   4.443   0.813  1.00 67.09           C  
ANISOU 2550  CG  ASP A 325     9302   8027   8161   1604    807    382       C  
ATOM   2551  OD1 ASP A 325      22.884   3.710   0.207  1.00 75.54           O  
ANISOU 2551  OD1 ASP A 325    10350   9094   9257   1607    795    380       O  
ATOM   2552  OD2 ASP A 325      23.405   5.090   1.843  1.00 70.99           O1-
ANISOU 2552  OD2 ASP A 325     9804   8511   8657   1603    832    388       O1-
ATOM   2553  N   ASN A 326      25.227   6.751  -2.075  1.00 44.77           N  
ANISOU 2553  N   ASN A 326     6479   5227   5303   1608    773    376       N  
ATOM   2554  CA  ASN A 326      24.797   8.107  -2.405  1.00 50.25           C  
ANISOU 2554  CA  ASN A 326     7169   5915   6009   1611    784    380       C  
ATOM   2555  C   ASN A 326      24.082   8.308  -3.758  1.00 58.50           C  
ANISOU 2555  C   ASN A 326     8189   6959   7078   1617    769    379       C  
ATOM   2556  O   ASN A 326      24.526   7.804  -4.793  1.00 62.27           O  
ANISOU 2556  O   ASN A 326     8661   7448   7549   1617    744    373       O  
ATOM   2557  CB  ASN A 326      26.031   9.007  -2.327  1.00 54.35           C  
ANISOU 2557  CB  ASN A 326     7712   6445   6494   1608    786    380       C  
ATOM   2558  CG  ASN A 326      25.691  10.470  -2.201  1.00 57.84           C  
ANISOU 2558  CG  ASN A 326     8155   6878   6943   1611    805    386       C  
ATOM   2559  ND2 ASN A 326      26.404  11.153  -1.318  1.00 58.84           N  
ANISOU 2559  ND2 ASN A 326     8304   7005   7046   1607    821    390       N  
ATOM   2560  OD1 ASN A 326      24.811  10.989  -2.889  1.00 61.04           O  
ANISOU 2560  OD1 ASN A 326     8542   7276   7374   1616    805    388       O  
ATOM   2561  N   LYS A 327      22.996   9.084  -3.738  1.00 57.90           N  
ANISOU 2561  N   LYS A 327     8100   6870   7031   1621    784    385       N  
ATOM   2562  CA  LYS A 327      22.192   9.359  -4.929  1.00 53.30           C  
ANISOU 2562  CA  LYS A 327     7493   6284   6475   1627    772    385       C  
ATOM   2563  C   LYS A 327      22.730  10.555  -5.722  1.00 58.08           C  
ANISOU 2563  C   LYS A 327     8104   6896   7068   1628    768    385       C  
ATOM   2564  O   LYS A 327      22.498  10.679  -6.934  1.00 59.84           O  
ANISOU 2564  O   LYS A 327     8311   7122   7302   1631    751    382       O  
ATOM   2565  CB  LYS A 327      20.738   9.609  -4.528  1.00 52.70           C  
ANISOU 2565  CB  LYS A 327     7399   6189   6435   1631    790    391       C  
ATOM   2566  CG  LYS A 327      19.792   9.843  -5.696  1.00 58.03           C  
ANISOU 2566  CG  LYS A 327     8049   6860   7141   1637    778    392       C  
ATOM   2567  CD  LYS A 327      18.771  10.923  -5.365  1.00 63.72           C  
ANISOU 2567  CD  LYS A 327     8760   7565   7885   1641    801    400       C  
ATOM   2568  CE  LYS A 327      17.353  10.392  -5.429  1.00 64.51           C  
ANISOU 2568  CE  LYS A 327     8836   7651   8024   1645    802    403       C  
ATOM   2569  NZ  LYS A 327      17.211   9.160  -4.615  1.00 66.94           N1+
ANISOU 2569  NZ  LYS A 327     9145   7956   8333   1642    804    401       N1+
ATOM   2570  N   GLU A 328      23.452  11.439  -5.042  1.00 57.24           N  
ANISOU 2570  N   GLU A 328     8019   6791   6938   1625    784    387       N  
ATOM   2571  CA  GLU A 328      24.079  12.563  -5.728  1.00 55.80           C  
ANISOU 2571  CA  GLU A 328     7844   6616   6741   1626    780    387       C  
ATOM   2572  C   GLU A 328      25.324  12.094  -6.457  1.00 51.21           C  
ANISOU 2572  C   GLU A 328     7273   6054   6130   1623    756    380       C  
ATOM   2573  O   GLU A 328      25.564  12.479  -7.604  1.00 50.78           O  
ANISOU 2573  O   GLU A 328     7213   6008   6074   1625    740    377       O  
ATOM   2574  CB  GLU A 328      24.418  13.696  -4.759  1.00 57.84           C  
ANISOU 2574  CB  GLU A 328     8121   6870   6985   1624    805    393       C  
ATOM   2575  CG  GLU A 328      23.667  14.988  -5.056  1.00 60.09           C  
ANISOU 2575  CG  GLU A 328     8396   7144   7290   1629    818    398       C  
ATOM   2576  CD  GLU A 328      24.206  15.727  -6.264  1.00 58.98           C  
ANISOU 2576  CD  GLU A 328     8255   7014   7140   1631    802    396       C  
ATOM   2577  OE1 GLU A 328      25.438  15.825  -6.392  1.00 59.56           O  
ANISOU 2577  OE1 GLU A 328     8347   7102   7182   1627    793    392       O  
ATOM   2578  OE2 GLU A 328      23.405  16.225  -7.081  1.00 62.30           O1-
ANISOU 2578  OE2 GLU A 328     8656   7430   7585   1636    799    397       O1-
ATOM   2579  N   LYS A 329      26.111  11.257  -5.784  1.00 48.62           N  
ANISOU 2579  N   LYS A 329     6961   5733   5778   1618    753    377       N  
ATOM   2580  CA  LYS A 329      27.284  10.648  -6.395  1.00 40.73           C  
ANISOU 2580  CA  LYS A 329     5972   4752   4750   1615    730    370       C  
ATOM   2581  C   LYS A 329      26.856   9.811  -7.596  1.00 39.89           C  
ANISOU 2581  C   LYS A 329     5845   4651   4662   1618    706    364       C  
ATOM   2582  O   LYS A 329      27.511   9.822  -8.632  1.00 33.02           O  
ANISOU 2582  O   LYS A 329     4975   3793   3777   1618    685    359       O  
ATOM   2583  CB  LYS A 329      28.032   9.787  -5.382  1.00 34.80           C  
ANISOU 2583  CB  LYS A 329     5240   4005   3975   1610    732    368       C  
ATOM   2584  CG  LYS A 329      28.570  10.550  -4.201  1.00 35.43           C  
ANISOU 2584  CG  LYS A 329     5343   4082   4036   1606    755    373       C  
ATOM   2585  CD  LYS A 329      30.049  10.251  -3.971  1.00 42.47           C  
ANISOU 2585  CD  LYS A 329     6260   4990   4887   1601    745    369       C  
ATOM   2586  CE  LYS A 329      30.363  10.121  -2.488  1.00 47.51           C  
ANISOU 2586  CE  LYS A 329     6917   5622   5511   1597    764    373       C  
ATOM   2587  NZ  LYS A 329      29.617   8.961  -1.908  1.00 55.90           N1+
ANISOU 2587  NZ  LYS A 329     7970   6678   6593   1596    767    373       N1+
ATOM   2588  N   LEU A 330      25.738   9.106  -7.443  1.00 40.70           N  
ANISOU 2588  N   LEU A 330     5928   4741   4794   1620    708    366       N  
ATOM   2589  CA  LEU A 330      25.141   8.322  -8.516  1.00 38.32           C  
ANISOU 2589  CA  LEU A 330     5604   4442   4515   1623    686    362       C  
ATOM   2590  C   LEU A 330      24.718   9.161  -9.719  1.00 46.07           C  
ANISOU 2590  C   LEU A 330     6569   5422   5511   1628    678    363       C  
ATOM   2591  O   LEU A 330      25.124   8.875 -10.843  1.00 53.55           O  
ANISOU 2591  O   LEU A 330     7512   6381   6453   1628    655    357       O  
ATOM   2592  CB  LEU A 330      23.934   7.555  -8.003  1.00 37.81           C  
ANISOU 2592  CB  LEU A 330     5522   4363   4482   1625    694    365       C  
ATOM   2593  CG  LEU A 330      23.374   6.584  -9.037  1.00 39.39           C  
ANISOU 2593  CG  LEU A 330     5700   4564   4704   1627    670    360       C  
ATOM   2594  CD1 LEU A 330      24.406   5.486  -9.325  1.00 35.06           C  
ANISOU 2594  CD1 LEU A 330     5160   4031   4129   1623    649    352       C  
ATOM   2595  CD2 LEU A 330      22.011   6.012  -8.620  1.00 36.31           C  
ANISOU 2595  CD2 LEU A 330     5289   4157   4350   1630    679    364       C  
ATOM   2596  N   ILE A 331      23.888  10.176  -9.496  1.00 48.99           N  
ANISOU 2596  N   ILE A 331     6932   5779   5903   1631    697    369       N  
ATOM   2597  CA  ILE A 331      23.470  11.075 -10.583  1.00 49.77           C  
ANISOU 2597  CA  ILE A 331     7017   5876   6016   1636    691    371       C  
ATOM   2598  C   ILE A 331      24.666  11.709 -11.309  1.00 43.42           C  
ANISOU 2598  C   ILE A 331     6227   5088   5182   1635    679    367       C  
ATOM   2599  O   ILE A 331      24.708  11.782 -12.550  1.00 46.15           O  
ANISOU 2599  O   ILE A 331     6561   5441   5531   1637    659    364       O  
ATOM   2600  CB  ILE A 331      22.531  12.187 -10.057  1.00 52.41           C  
ANISOU 2600  CB  ILE A 331     7346   6195   6373   1640    716    379       C  
ATOM   2601  CG1 ILE A 331      21.204  11.590  -9.591  1.00 54.71           C  
ANISOU 2601  CG1 ILE A 331     7618   6471   6699   1642    724    383       C  
ATOM   2602  CG2 ILE A 331      22.266  13.209 -11.131  1.00 56.31           C  
ANISOU 2602  CG2 ILE A 331     7828   6689   6877   1644    710    380       C  
ATOM   2603  CD1 ILE A 331      20.444  10.855 -10.678  1.00 54.12           C  
ANISOU 2603  CD1 ILE A 331     7518   6394   6650   1646    703    380       C  
ATOM   2604  N   LYS A 332      25.649  12.135 -10.521  1.00 37.34           N  
ANISOU 2604  N   LYS A 332     5483   4324   4382   1631    690    367       N  
ATOM   2605  CA  LYS A 332      26.856  12.772 -11.037  1.00 38.84           C  
ANISOU 2605  CA  LYS A 332     5688   4528   4539   1629    681    364       C  
ATOM   2606  C   LYS A 332      27.698  11.805 -11.902  1.00 46.91           C  
ANISOU 2606  C   LYS A 332     6713   5568   5543   1627    653    356       C  
ATOM   2607  O   LYS A 332      28.102  12.140 -13.035  1.00 51.11           O  
ANISOU 2607  O   LYS A 332     7242   6110   6068   1628    636    352       O  
ATOM   2608  CB  LYS A 332      27.670  13.306  -9.856  1.00 36.15           C  
ANISOU 2608  CB  LYS A 332     5375   4189   4172   1625    700    367       C  
ATOM   2609  CG  LYS A 332      28.160  14.728 -10.000  1.00 40.29           C  
ANISOU 2609  CG  LYS A 332     5911   4716   4683   1625    709    370       C  
ATOM   2610  CD  LYS A 332      27.559  15.653  -8.948  1.00 44.68           C  
ANISOU 2610  CD  LYS A 332     6470   5256   5250   1626    738    378       C  
ATOM   2611  CE  LYS A 332      28.332  16.982  -8.859  1.00 51.57           C  
ANISOU 2611  CE  LYS A 332     7360   6132   6101   1625    748    381       C  
ATOM   2612  NZ  LYS A 332      28.587  17.647 -10.195  1.00 49.35           N1+
ANISOU 2612  NZ  LYS A 332     7073   5860   5818   1628    732    379       N1+
ATOM   2613  N   ALA A 333      27.948  10.608 -11.359  1.00 48.12           N  
ANISOU 2613  N   ALA A 333     6872   5725   5688   1623    648    352       N  
ATOM   2614  CA  ALA A 333      28.591   9.500 -12.080  1.00 37.66           C  
ANISOU 2614  CA  ALA A 333     5546   4414   4349   1621    622    344       C  
ATOM   2615  C   ALA A 333      27.902   9.214 -13.407  1.00 41.15           C  
ANISOU 2615  C   ALA A 333     5963   4856   4815   1625    603    342       C  
ATOM   2616  O   ALA A 333      28.540   9.247 -14.448  1.00 43.26           O  
ANISOU 2616  O   ALA A 333     6231   5136   5068   1625    583    336       O  
ATOM   2617  CB  ALA A 333      28.588   8.252 -11.243  1.00 26.99           C  
ANISOU 2617  CB  ALA A 333     4199   3062   2996   1618    623    342       C  
ATOM   2618  N   VAL A 334      26.605   8.921 -13.357  1.00 36.30           N  
ANISOU 2618  N   VAL A 334     5328   4228   4238   1628    608    345       N  
ATOM   2619  CA  VAL A 334      25.834   8.663 -14.562  1.00 32.94           C  
ANISOU 2619  CA  VAL A 334     4877   3800   3839   1632    590    344       C  
ATOM   2620  C   VAL A 334      26.053   9.745 -15.610  1.00 39.55           C  
ANISOU 2620  C   VAL A 334     5711   4642   4673   1635    583    344       C  
ATOM   2621  O   VAL A 334      26.238   9.438 -16.814  1.00 40.08           O  
ANISOU 2621  O   VAL A 334     5770   4719   4740   1636    561    339       O  
ATOM   2622  CB  VAL A 334      24.351   8.562 -14.254  1.00 31.72           C  
ANISOU 2622  CB  VAL A 334     4702   3627   3725   1636    602    350       C  
ATOM   2623  CG1 VAL A 334      23.547   8.392 -15.545  1.00 31.45           C  
ANISOU 2623  CG1 VAL A 334     4641   3590   3719   1641    583    349       C  
ATOM   2624  CG2 VAL A 334      24.113   7.408 -13.319  1.00 32.10           C  
ANISOU 2624  CG2 VAL A 334     4750   3669   3777   1634    606    349       C  
ATOM   2625  N   GLU A 335      26.061  11.003 -15.156  1.00 36.93           N  
ANISOU 2625  N   GLU A 335     5389   4306   4339   1636    603    349       N  
ATOM   2626  CA  GLU A 335      26.318  12.112 -16.079  1.00 40.36           C  
ANISOU 2626  CA  GLU A 335     5822   4745   4768   1639    599    350       C  
ATOM   2627  C   GLU A 335      27.663  11.942 -16.769  1.00 34.76           C  
ANISOU 2627  C   GLU A 335     5127   4055   4023   1636    579    342       C  
ATOM   2628  O   GLU A 335      27.737  11.941 -18.002  1.00 29.30           O  
ANISOU 2628  O   GLU A 335     4426   3371   3334   1638    560    339       O  
ATOM   2629  CB  GLU A 335      26.261  13.463 -15.370  1.00 53.92           C  
ANISOU 2629  CB  GLU A 335     7550   6454   6483   1640    623    357       C  
ATOM   2630  CG  GLU A 335      25.079  14.305 -15.789  1.00 62.45           C  
ANISOU 2630  CG  GLU A 335     8611   7521   7598   1646    632    363       C  
ATOM   2631  CD  GLU A 335      24.966  14.421 -17.293  1.00 67.95           C  
ANISOU 2631  CD  GLU A 335     9291   8224   8303   1649    610    360       C  
ATOM   2632  OE1 GLU A 335      25.722  15.223 -17.874  1.00 73.65           O  
ANISOU 2632  OE1 GLU A 335    10023   8956   9006   1649    605    358       O  
ATOM   2633  OE2 GLU A 335      24.129  13.710 -17.893  1.00 68.39           O1-
ANISOU 2633  OE2 GLU A 335     9325   8275   8385   1651    597    359       O1-
ATOM   2634  N   ILE A 336      28.716  11.774 -15.969  1.00 29.76           N  
ANISOU 2634  N   ILE A 336     4519   3431   3358   1631    584    340       N  
ATOM   2635  CA  ILE A 336      30.056  11.551 -16.521  1.00 28.77           C  
ANISOU 2635  CA  ILE A 336     4410   3326   3197   1628    566    333       C  
ATOM   2636  C   ILE A 336      30.202  10.326 -17.456  1.00 39.16           C  
ANISOU 2636  C   ILE A 336     5715   4652   4513   1627    539    325       C  
ATOM   2637  O   ILE A 336      30.676  10.465 -18.585  1.00 41.10           O  
ANISOU 2637  O   ILE A 336     5958   4909   4748   1628    520    321       O  
ATOM   2638  CB  ILE A 336      31.085  11.495 -15.419  1.00 27.66           C  
ANISOU 2638  CB  ILE A 336     4296   3191   3024   1623    576    333       C  
ATOM   2639  CG1 ILE A 336      31.126  12.855 -14.702  1.00 27.27           C  
ANISOU 2639  CG1 ILE A 336     4259   3134   2970   1623    600    340       C  
ATOM   2640  CG2 ILE A 336      32.449  11.071 -15.978  1.00 26.63           C  
ANISOU 2640  CG2 ILE A 336     4181   3081   2856   1619    555    325       C  
ATOM   2641  CD1 ILE A 336      32.143  12.946 -13.546  1.00 28.45           C  
ANISOU 2641  CD1 ILE A 336     4436   3288   3087   1618    612    341       C  
HETATM 2642  N   MSE A 337      29.777   9.151 -16.990  1.00 41.38           N  
ANISOU 2642  N   MSE A 337     5989   4928   4805   1626    536    324       N  
HETATM 2643  CA  MSE A 337      29.811   7.902 -17.771  1.00 36.69           C  
ANISOU 2643  CA  MSE A 337     5385   4342   4214   1625    512    317       C  
HETATM 2644  C   MSE A 337      29.013   7.870 -19.082  1.00 37.08           C  
ANISOU 2644  C   MSE A 337     5409   4388   4291   1629    496    316       C  
HETATM 2645  O   MSE A 337      29.461   7.249 -20.041  1.00 39.27           O  
ANISOU 2645  O   MSE A 337     5683   4678   4559   1628    473    310       O  
HETATM 2646  CB  MSE A 337      29.431   6.682 -16.913  1.00 26.44           C  
ANISOU 2646  CB  MSE A 337     4084   3037   2925   1623    515    317       C  
HETATM 2647  CG  MSE A 337      30.512   6.271 -15.892  1.00 26.17           C  
ANISOU 2647  CG  MSE A 337     4076   3012   2857   1617    521    314       C  
HETATM 2648  CE  MSE A 337      33.260   6.248 -14.742  1.00 57.90           C  
ANISOU 2648  CE  MSE A 337     8150   7057   6791   1608    522    308       C  
HETATM 2649 SE   MSE A 337      32.375   6.619 -16.425  1.00 53.59          SE  
ANISOU 2649 SE   MSE A 337     7576   6510   6277   1613    505    307      SE  
ATOM   2650  N   LEU A 338      27.846   8.511 -19.142  1.00 36.13           N  
ANISOU 2650  N   LEU A 338     5271   4253   4204   1634    507    323       N  
ATOM   2651  CA  LEU A 338      27.088   8.519 -20.405  1.00 30.54           C  
ANISOU 2651  CA  LEU A 338     4539   3543   3523   1638    491    323       C  
ATOM   2652  C   LEU A 338      27.736   9.382 -21.487  1.00 32.53           C  
ANISOU 2652  C   LEU A 338     4795   3806   3759   1639    480    321       C  
ATOM   2653  O   LEU A 338      27.328   9.361 -22.651  1.00 38.61           O  
ANISOU 2653  O   LEU A 338     5548   4578   4545   1642    464    319       O  
ATOM   2654  CB  LEU A 338      25.657   9.000 -20.185  1.00 30.52           C  
ANISOU 2654  CB  LEU A 338     4517   3520   3560   1642    506    331       C  
ATOM   2655  CG  LEU A 338      24.672   8.003 -19.598  1.00 33.06           C  
ANISOU 2655  CG  LEU A 338     4824   3829   3908   1643    510    333       C  
ATOM   2656  CD1 LEU A 338      23.392   8.707 -19.254  1.00 35.10           C  
ANISOU 2656  CD1 LEU A 338     5068   4069   4201   1647    528    342       C  
ATOM   2657  CD2 LEU A 338      24.398   6.906 -20.582  1.00 39.31           C  
ANISOU 2657  CD2 LEU A 338     5599   4625   4713   1643    485    328       C  
ATOM   2658  N   ASN A 339      28.732  10.164 -21.107  1.00 34.24           N  
ANISOU 2658  N   ASN A 339     5034   4032   3945   1637    489    320       N  
ATOM   2659  CA  ASN A 339      29.365  11.049 -22.061  1.00 43.13           C  
ANISOU 2659  CA  ASN A 339     6164   5168   5055   1638    480    318       C  
ATOM   2660  C   ASN A 339      30.855  10.757 -22.069  1.00 49.07           C  
ANISOU 2660  C   ASN A 339     6940   5939   5764   1634    470    311       C  
ATOM   2661  O   ASN A 339      31.678  11.543 -22.547  1.00 54.14           O  
ANISOU 2661  O   ASN A 339     7594   6592   6383   1633    466    309       O  
ATOM   2662  CB  ASN A 339      29.042  12.508 -21.724  1.00 49.19           C  
ANISOU 2662  CB  ASN A 339     6934   5926   5830   1641    502    326       C  
ATOM   2663  CG  ASN A 339      27.539  12.811 -21.825  1.00 60.34           C  
ANISOU 2663  CG  ASN A 339     8321   7319   7285   1646    510    333       C  
ATOM   2664  ND2 ASN A 339      26.957  13.321 -20.734  1.00 61.51           N  
ANISOU 2664  ND2 ASN A 339     8473   7454   7446   1647    535    340       N  
ATOM   2665  OD1 ASN A 339      26.907  12.560 -22.865  1.00 61.07           O  
ANISOU 2665  OD1 ASN A 339     8394   7410   7400   1649    495    332       O  
ATOM   2666  N   LYS A 340      31.172   9.573 -21.562  1.00 46.37           N  
ANISOU 2666  N   LYS A 340     6604   5601   5412   1630    464    307       N  
ATOM   2667  CA  LYS A 340      32.531   9.093 -21.486  1.00 41.95           C  
ANISOU 2667  CA  LYS A 340     6067   5060   4813   1625    454    299       C  
ATOM   2668  C   LYS A 340      32.954   8.545 -22.821  1.00 43.06           C  
ANISOU 2668  C   LYS A 340     6201   5215   4946   1625    426    291       C  
ATOM   2669  O   LYS A 340      32.414   7.535 -23.279  1.00 41.98           O  
ANISOU 2669  O   LYS A 340     6047   5076   4826   1626    412    288       O  
ATOM   2670  CB  LYS A 340      32.628   7.966 -20.460  1.00 42.73           C  
ANISOU 2670  CB  LYS A 340     6173   5157   4907   1621    457    298       C  
ATOM   2671  CG  LYS A 340      33.666   8.199 -19.386  1.00 44.70           C  
ANISOU 2671  CG  LYS A 340     6449   5412   5122   1617    470    298       C  
ATOM   2672  CD  LYS A 340      35.057   7.978 -19.896  1.00 46.17           C  
ANISOU 2672  CD  LYS A 340     6654   5620   5270   1614    452    290       C  
ATOM   2673  CE  LYS A 340      36.060   8.410 -18.858  1.00 51.94           C  
ANISOU 2673  CE  LYS A 340     7412   6356   5968   1610    465    292       C  
ATOM   2674  NZ  LYS A 340      37.415   8.242 -19.427  1.00 59.70           N1+
ANISOU 2674  NZ  LYS A 340     8411   7359   6912   1607    447    284       N1+
ATOM   2675  N   LYS A 341      33.923   9.206 -23.444  1.00 41.33           N  
ANISOU 2675  N   LYS A 341     5994   5009   4699   1625    419    287       N  
ATOM   2676  CA  LYS A 341      34.642   8.567 -24.529  1.00 39.06           C  
ANISOU 2676  CA  LYS A 341     5708   4740   4395   1623    393    278       C  
ATOM   2677  C   LYS A 341      35.259   7.295 -23.968  1.00 35.75           C  
ANISOU 2677  C   LYS A 341     5300   4328   3956   1619    386    272       C  
ATOM   2678  O   LYS A 341      36.094   7.328 -23.060  1.00 35.71           O  
ANISOU 2678  O   LYS A 341     5316   4328   3923   1615    394    272       O  
ATOM   2679  CB  LYS A 341      35.687   9.495 -25.147  1.00 37.17           C  
ANISOU 2679  CB  LYS A 341     5483   4514   4125   1623    388    275       C  
ATOM   2680  CG  LYS A 341      35.057  10.488 -26.131  1.00 47.94           C  
ANISOU 2680  CG  LYS A 341     6830   5873   5510   1628    386    279       C  
ATOM   2681  CD  LYS A 341      35.939  11.694 -26.398  1.00 58.14           C  
ANISOU 2681  CD  LYS A 341     8139   7175   6777   1628    390    279       C  
ATOM   2682  CE  LYS A 341      35.127  12.977 -26.290  1.00 68.96           C  
ANISOU 2682  CE  LYS A 341     9500   8531   8171   1632    408    288       C  
ATOM   2683  NZ  LYS A 341      35.936  14.193 -26.597  1.00 77.63           N1+
ANISOU 2683  NZ  LYS A 341    10612   9638   9246   1633    411    288       N1+
ATOM   2684  N   ARG A 342      34.803   6.171 -24.499  1.00 30.21           N  
ANISOU 2684  N   ARG A 342     4582   3626   3270   1619    369    268       N  
ATOM   2685  CA  ARG A 342      35.227   4.873 -24.031  1.00 31.01           C  
ANISOU 2685  CA  ARG A 342     4691   3733   3358   1614    361    262       C  
ATOM   2686  C   ARG A 342      36.585   4.419 -24.551  1.00 29.96           C  
ANISOU 2686  C   ARG A 342     4575   3622   3186   1611    343    252       C  
ATOM   2687  O   ARG A 342      36.677   3.410 -25.232  1.00 28.47           O  
ANISOU 2687  O   ARG A 342     4379   3441   2997   1610    323    244       O  
ATOM   2688  CB  ARG A 342      34.164   3.840 -24.380  1.00 31.51           C  
ANISOU 2688  CB  ARG A 342     4730   3787   3455   1616    352    262       C  
ATOM   2689  CG  ARG A 342      32.768   4.270 -23.964  1.00 32.85           C  
ANISOU 2689  CG  ARG A 342     4881   3936   3665   1620    369    272       C  
ATOM   2690  CD  ARG A 342      31.816   3.149 -24.220  1.00 33.16           C  
ANISOU 2690  CD  ARG A 342     4899   3966   3734   1621    358    271       C  
ATOM   2691  NE  ARG A 342      30.420   3.455 -23.947  1.00 32.37           N  
ANISOU 2691  NE  ARG A 342     4778   3846   3674   1624    372    280       N  
ATOM   2692  CZ  ARG A 342      29.466   2.539 -24.059  1.00 37.60           C  
ANISOU 2692  CZ  ARG A 342     5422   4499   4367   1625    365    281       C  
ATOM   2693  NH1 ARG A 342      29.791   1.304 -24.420  1.00 32.89           N1+
ANISOU 2693  NH1 ARG A 342     4823   3911   3763   1623    346    274       N1+
ATOM   2694  NH2 ARG A 342      28.202   2.845 -23.813  1.00 45.45           N  
ANISOU 2694  NH2 ARG A 342     6398   5475   5397   1629    378    289       N  
ATOM   2695  N   ASN A 343      37.650   5.142 -24.235  1.00 35.87           N  
ANISOU 2695  N   ASN A 343     5347   4381   3902   1609    348    251       N  
ATOM   2696  CA  ASN A 343      38.958   4.534 -24.437  1.00 47.77           C  
ANISOU 2696  CA  ASN A 343     6872   5907   5370   1605    332    241       C  
ATOM   2697  C   ASN A 343      39.914   4.638 -23.280  1.00 40.40           C  
ANISOU 2697  C   ASN A 343     5964   4979   4405   1601    344    242       C  
ATOM   2698  O   ASN A 343      40.948   5.285 -23.373  1.00 43.19           O  
ANISOU 2698  O   ASN A 343     6337   5345   4728   1600    343    240       O  
ATOM   2699  CB  ASN A 343      39.659   4.967 -25.723  1.00 59.60           C  
ANISOU 2699  CB  ASN A 343     8373   7422   6851   1606    315    234       C  
ATOM   2700  CG  ASN A 343      40.797   4.004 -26.108  1.00 66.51           C  
ANISOU 2700  CG  ASN A 343     9262   8317   7693   1602    294    222       C  
ATOM   2701  ND2 ASN A 343      40.514   3.082 -27.033  1.00 66.45           N  
ANISOU 2701  ND2 ASN A 343     9239   8313   7697   1602    275    215       N  
ATOM   2702  OD1 ASN A 343      41.901   4.074 -25.557  1.00 66.60           O  
ANISOU 2702  OD1 ASN A 343     9296   8339   7670   1598    296    219       O  
ATOM   2703  N   TRP A 344      39.577   3.959 -22.200  1.00 32.41           N  
ANISOU 2703  N   TRP A 344     4954   3958   3401   1599    355    245       N  
ATOM   2704  CA  TRP A 344      40.502   3.820 -21.098  1.00 33.79           C  
ANISOU 2704  CA  TRP A 344     5154   4139   3545   1595    363    246       C  
ATOM   2705  C   TRP A 344      41.579   2.758 -21.403  1.00 39.63           C  
ANISOU 2705  C   TRP A 344     5905   4897   4254   1591    342    235       C  
ATOM   2706  O   TRP A 344      41.325   1.798 -22.137  1.00 33.55           O  
ANISOU 2706  O   TRP A 344     5123   4132   3495   1591    325    228       O  
ATOM   2707  CB  TRP A 344      39.726   3.472 -19.830  1.00 29.73           C  
ANISOU 2707  CB  TRP A 344     4636   3608   3051   1594    382    253       C  
ATOM   2708  CG  TRP A 344      38.598   2.491 -20.024  1.00 27.23           C  
ANISOU 2708  CG  TRP A 344     4296   3281   2769   1596    377    253       C  
ATOM   2709  CD1 TRP A 344      38.692   1.131 -20.073  1.00 28.27           C  
ANISOU 2709  CD1 TRP A 344     4424   3417   2899   1593    363    246       C  
ATOM   2710  CD2 TRP A 344      37.210   2.796 -20.164  1.00 23.58           C  
ANISOU 2710  CD2 TRP A 344     3811   2801   2349   1600    386    259       C  
ATOM   2711  CE2 TRP A 344      36.525   1.573 -20.295  1.00 25.37           C  
ANISOU 2711  CE2 TRP A 344     4021   3023   2597   1600    376    257       C  
ATOM   2712  CE3 TRP A 344      36.476   3.979 -20.180  1.00 23.12           C  
ANISOU 2712  CE3 TRP A 344     3744   2731   2312   1604    401    267       C  
ATOM   2713  NE1 TRP A 344      37.453   0.572 -20.237  1.00 19.65           N  
ANISOU 2713  NE1 TRP A 344     3309   2312   1846   1596    362    248       N  
ATOM   2714  CZ2 TRP A 344      35.141   1.510 -20.442  1.00 28.69           C  
ANISOU 2714  CZ2 TRP A 344     4416   3426   3059   1604    381    262       C  
ATOM   2715  CZ3 TRP A 344      35.113   3.910 -20.328  1.00 20.14           C  
ANISOU 2715  CZ3 TRP A 344     3341   2336   1974   1608    406    272       C  
ATOM   2716  CH2 TRP A 344      34.456   2.691 -20.454  1.00 20.19           C  
ANISOU 2716  CH2 TRP A 344     3331   2338   2001   1608    396    270       C  
ATOM   2717  N   LYS A 345      42.784   2.942 -20.865  1.00 42.80           N  
ANISOU 2717  N   LYS A 345     6333   5311   4619   1587    343    233       N  
ATOM   2718  CA  LYS A 345      43.785   1.888 -20.936  1.00 38.17           C  
ANISOU 2718  CA  LYS A 345     5760   4741   4003   1583    326    224       C  
ATOM   2719  C   LYS A 345      43.242   0.684 -20.199  1.00 35.23           C  
ANISOU 2719  C   LYS A 345     5381   4360   3645   1581    328    224       C  
ATOM   2720  O   LYS A 345      42.551   0.817 -19.198  1.00 40.73           O  
ANISOU 2720  O   LYS A 345     6074   5041   4360   1582    348    233       O  
ATOM   2721  CB  LYS A 345      45.110   2.323 -20.318  1.00 41.94           C  
ANISOU 2721  CB  LYS A 345     6266   5231   4440   1579    330    224       C  
ATOM   2722  CG  LYS A 345      45.840   3.420 -21.093  1.00 47.83           C  
ANISOU 2722  CG  LYS A 345     7021   5988   5165   1581    324    222       C  
ATOM   2723  CD  LYS A 345      46.964   4.048 -20.249  1.00 61.30           C  
ANISOU 2723  CD  LYS A 345     8754   7700   6836   1577    333    226       C  
ATOM   2724  CE  LYS A 345      46.438   4.658 -18.929  1.00 72.07           C  
ANISOU 2724  CE  LYS A 345    10123   9048   8214   1577    359    239       C  
ATOM   2725  NZ  LYS A 345      46.373   3.702 -17.758  1.00 72.59           N1+
ANISOU 2725  NZ  LYS A 345    10194   9107   8279   1574    366    241       N1+
ATOM   2726  N   ASN A 346      43.518  -0.501 -20.712  1.00 32.47           N  
ANISOU 2726  N   ASN A 346     5028   4020   3289   1579    309    214       N  
ATOM   2727  CA  ASN A 346      43.051  -1.696 -20.047  1.00 29.68           C  
ANISOU 2727  CA  ASN A 346     4668   3659   2948   1578    310    214       C  
ATOM   2728  C   ASN A 346      44.075  -2.064 -18.989  1.00 33.13           C  
ANISOU 2728  C   ASN A 346     5130   4104   3353   1573    314    214       C  
ATOM   2729  O   ASN A 346      45.196  -2.415 -19.325  1.00 38.45           O  
ANISOU 2729  O   ASN A 346     5820   4796   3994   1570    299    205       O  
ATOM   2730  CB  ASN A 346      42.893  -2.815 -21.064  1.00 27.51           C  
ANISOU 2730  CB  ASN A 346     4379   3391   2682   1577    287    204       C  
ATOM   2731  CG  ASN A 346      42.202  -4.031 -20.495  1.00 29.07           C  
ANISOU 2731  CG  ASN A 346     4566   3579   2899   1576    287    205       C  
ATOM   2732  ND2 ASN A 346      41.620  -4.842 -21.372  1.00 25.81           N  
ANISOU 2732  ND2 ASN A 346     4133   3165   2507   1578    271    200       N  
ATOM   2733  OD1 ASN A 346      42.205  -4.256 -19.288  1.00 32.30           O  
ANISOU 2733  OD1 ASN A 346     4985   3982   3307   1574    301    210       O  
ATOM   2734  N   PRO A 347      43.699  -1.966 -17.701  1.00 35.22           N  
ANISOU 2734  N   PRO A 347     5400   4356   3626   1572    334    223       N  
ATOM   2735  CA  PRO A 347      44.660  -2.254 -16.627  1.00 32.20           C  
ANISOU 2735  CA  PRO A 347     5042   3980   3213   1567    339    224       C  
ATOM   2736  C   PRO A 347      44.965  -3.754 -16.459  1.00 34.26           C  
ANISOU 2736  C   PRO A 347     5304   4247   3465   1564    326    217       C  
ATOM   2737  O   PRO A 347      45.864  -4.134 -15.712  1.00 40.00           O  
ANISOU 2737  O   PRO A 347     6052   4982   4164   1560    326    216       O  
ATOM   2738  CB  PRO A 347      43.966  -1.684 -15.376  1.00 32.06           C  
ANISOU 2738  CB  PRO A 347     5025   3943   3213   1568    366    236       C  
ATOM   2739  CG  PRO A 347      42.506  -1.757 -15.686  1.00 31.95           C  
ANISOU 2739  CG  PRO A 347     4983   3913   3243   1572    372    239       C  
ATOM   2740  CD  PRO A 347      42.381  -1.546 -17.176  1.00 34.02           C  
ANISOU 2740  CD  PRO A 347     5232   4183   3513   1575    354    233       C  
ATOM   2741  N   PHE A 348      44.227  -4.595 -17.166  1.00 34.55           N  
ANISOU 2741  N   PHE A 348     5320   4281   3525   1566    314    211       N  
ATOM   2742  CA  PHE A 348      44.409  -6.029 -17.045  1.00 31.68           C  
ANISOU 2742  CA  PHE A 348     4957   3923   3158   1563    301    204       C  
ATOM   2743  C   PHE A 348      45.268  -6.642 -18.155  1.00 31.26           C  
ANISOU 2743  C   PHE A 348     4907   3889   3081   1561    275    191       C  
ATOM   2744  O   PHE A 348      45.680  -7.786 -18.040  1.00 36.39           O  
ANISOU 2744  O   PHE A 348     5561   4547   3720   1558    263    184       O  
ATOM   2745  CB  PHE A 348      43.055  -6.737 -16.990  1.00 31.78           C  
ANISOU 2745  CB  PHE A 348     4945   3919   3212   1565    304    207       C  
ATOM   2746  CG  PHE A 348      42.115  -6.170 -15.971  1.00 31.57           C  
ANISOU 2746  CG  PHE A 348     4913   3873   3211   1567    330    219       C  
ATOM   2747  CD1 PHE A 348      42.322  -6.393 -14.619  1.00 28.86           C  
ANISOU 2747  CD1 PHE A 348     4583   3524   2858   1564    345    224       C  
ATOM   2748  CD2 PHE A 348      41.009  -5.421 -16.367  1.00 33.84           C  
ANISOU 2748  CD2 PHE A 348     5180   4147   3531   1571    338    225       C  
ATOM   2749  CE1 PHE A 348      41.448  -5.878 -13.675  1.00 30.32           C  
ANISOU 2749  CE1 PHE A 348     4764   3691   3067   1565    369    235       C  
ATOM   2750  CE2 PHE A 348      40.123  -4.898 -15.427  1.00 32.95           C  
ANISOU 2750  CE2 PHE A 348     5062   4015   3442   1573    362    235       C  
ATOM   2751  CZ  PHE A 348      40.344  -5.125 -14.082  1.00 33.23           C  
ANISOU 2751  CZ  PHE A 348     5113   4047   3468   1570    377    240       C  
ATOM   2752  N   GLY A 349      45.534  -5.906 -19.230  1.00 26.07           N  
ANISOU 2752  N   GLY A 349     4247   3240   2418   1563    266    187       N  
ATOM   2753  CA  GLY A 349      46.430  -6.413 -20.264  1.00 24.90           C  
ANISOU 2753  CA  GLY A 349     4104   3111   2244   1562    242    174       C  
ATOM   2754  C   GLY A 349      45.921  -6.239 -21.682  1.00 31.97           C  
ANISOU 2754  C   GLY A 349     4981   4008   3159   1565    228    169       C  
ATOM   2755  O   GLY A 349      44.761  -5.891 -21.888  1.00 33.14           O  
ANISOU 2755  O   GLY A 349     5109   4142   3343   1569    236    175       O  
ATOM   2756  N   ASN A 350      46.787  -6.507 -22.660  1.00 35.79           N  
ANISOU 2756  N   ASN A 350     5471   4510   3619   1564    208    156       N  
ATOM   2757  CA  ASN A 350      46.466  -6.250 -24.071  1.00 32.76           C  
ANISOU 2757  CA  ASN A 350     5070   4129   3247   1567    194    151       C  
ATOM   2758  C   ASN A 350      45.526  -7.247 -24.728  1.00 26.68           C  
ANISOU 2758  C   ASN A 350     4277   3353   2508   1568    182    147       C  
ATOM   2759  O   ASN A 350      45.135  -7.056 -25.865  1.00 35.46           O  
ANISOU 2759  O   ASN A 350     5374   4466   3635   1571    171    144       O  
ATOM   2760  CB  ASN A 350      47.743  -6.112 -24.918  1.00 40.02           C  
ANISOU 2760  CB  ASN A 350     6005   5070   4129   1565    178    139       C  
ATOM   2761  CG  ASN A 350      48.601  -7.385 -24.922  1.00 48.22           C  
ANISOU 2761  CG  ASN A 350     7056   6124   5143   1561    161    126       C  
ATOM   2762  ND2 ASN A 350      49.882  -7.227 -25.253  1.00 44.76           N  
ANISOU 2762  ND2 ASN A 350     6637   5704   4666   1558    151    117       N  
ATOM   2763  OD1 ASN A 350      48.120  -8.491 -24.640  1.00 50.95           O  
ANISOU 2763  OD1 ASN A 350     7392   6463   5503   1559    158    125       O  
ATOM   2764  N   GLY A 351      45.190  -8.324 -24.036  1.00 30.14           N  
ANISOU 2764  N   GLY A 351     4711   3784   2956   1566    183    148       N  
ATOM   2765  CA  GLY A 351      44.292  -9.322 -24.590  1.00 29.10           C  
ANISOU 2765  CA  GLY A 351     4557   3645   2854   1567    172    145       C  
ATOM   2766  C   GLY A 351      44.944 -10.414 -25.424  1.00 26.64           C  
ANISOU 2766  C   GLY A 351     4247   3349   2526   1564    147    131       C  
ATOM   2767  O   GLY A 351      44.269 -11.073 -26.207  1.00 25.89           O  
ANISOU 2767  O   GLY A 351     4133   3250   2455   1565    135    128       O  
ATOM   2768  N   LYS A 352      46.248 -10.618 -25.259  1.00 29.82           N  
ANISOU 2768  N   LYS A 352     4673   3769   2889   1561    141    122       N  
ATOM   2769  CA  LYS A 352      46.960 -11.645 -26.027  1.00 36.10           C  
ANISOU 2769  CA  LYS A 352     5471   4579   3664   1558    118    106       C  
ATOM   2770  C   LYS A 352      47.738 -12.608 -25.125  1.00 36.28           C  
ANISOU 2770  C   LYS A 352     5512   4610   3663   1553    117    101       C  
ATOM   2771  O   LYS A 352      48.709 -13.227 -25.546  1.00 37.71           O  
ANISOU 2771  O   LYS A 352     5704   4807   3815   1550    101     88       O  
ATOM   2772  CB  LYS A 352      47.899 -10.994 -27.051  1.00 35.62           C  
ANISOU 2772  CB  LYS A 352     5422   4537   3577   1558    107     97       C  
ATOM   2773  CG  LYS A 352      47.178 -10.117 -28.055  1.00 37.47           C  
ANISOU 2773  CG  LYS A 352     5638   4764   3834   1562    106    100       C  
ATOM   2774  CD  LYS A 352      48.130  -9.456 -29.029  1.00 44.87           C  
ANISOU 2774  CD  LYS A 352     6586   5719   4744   1563     95     90       C  
ATOM   2775  CE  LYS A 352      47.551  -9.459 -30.450  1.00 48.19           C  
ANISOU 2775  CE  LYS A 352     6986   6138   5185   1565     80     86       C  
ATOM   2776  NZ  LYS A 352      48.597  -9.174 -31.479  1.00 48.15           N1+
ANISOU 2776  NZ  LYS A 352     6993   6153   5151   1565     66     72       N1+
ATOM   2777  N   SER A 353      47.291 -12.748 -23.885  1.00 34.61           N  
ANISOU 2777  N   SER A 353     5302   4386   3463   1553    134    112       N  
ATOM   2778  CA  SER A 353      48.078 -13.451 -22.876  1.00 34.52           C  
ANISOU 2778  CA  SER A 353     5309   4380   3425   1548    136    110       C  
ATOM   2779  C   SER A 353      48.093 -14.984 -23.000  1.00 28.89           C  
ANISOU 2779  C   SER A 353     4591   3671   2715   1546    120    100       C  
ATOM   2780  O   SER A 353      49.065 -15.606 -22.641  1.00 27.95           O  
ANISOU 2780  O   SER A 353     4489   3564   2565   1542    114     93       O  
ATOM   2781  CB  SER A 353      47.629 -13.017 -21.482  1.00 38.82           C  
ANISOU 2781  CB  SER A 353     5858   4910   3980   1549    160    124       C  
ATOM   2782  OG  SER A 353      47.725 -11.611 -21.347  1.00 39.41           O  
ANISOU 2782  OG  SER A 353     5940   4984   4050   1551    173    132       O  
ATOM   2783  N   GLY A 354      47.013 -15.582 -23.494  1.00 25.00           N  
ANISOU 2783  N   GLY A 354     4074   3167   2257   1547    115    101       N  
ATOM   2784  CA  GLY A 354      46.993 -17.002 -23.773  1.00 22.87           C  
ANISOU 2784  CA  GLY A 354     3798   2900   1991   1545     98     92       C  
ATOM   2785  C   GLY A 354      48.093 -17.372 -24.752  1.00 32.31           C  
ANISOU 2785  C   GLY A 354     5005   4117   3156   1543     77     75       C  
ATOM   2786  O   GLY A 354      48.907 -18.260 -24.469  1.00 33.63           O  
ANISOU 2786  O   GLY A 354     5185   4295   3299   1539     69     66       O  
ATOM   2787  N   GLU A 355      48.125 -16.680 -25.896  1.00 39.83           N  
ANISOU 2787  N   GLU A 355     5950   5074   4108   1545     69     71       N  
ATOM   2788  CA  GLU A 355      49.182 -16.883 -26.883  1.00 37.74           C  
ANISOU 2788  CA  GLU A 355     5696   4829   3813   1543     50     54       C  
ATOM   2789  C   GLU A 355      50.547 -16.665 -26.259  1.00 36.74           C  
ANISOU 2789  C   GLU A 355     5598   4717   3643   1540     53     49       C  
ATOM   2790  O   GLU A 355      51.405 -17.522 -26.353  1.00 44.91           O  
ANISOU 2790  O   GLU A 355     6645   5765   4653   1537     41     36       O  
ATOM   2791  CB  GLU A 355      49.037 -15.962 -28.102  1.00 46.59           C  
ANISOU 2791  CB  GLU A 355     6808   5953   4941   1547     44     52       C  
ATOM   2792  CG  GLU A 355      47.735 -16.104 -28.887  1.00 66.78           C  
ANISOU 2792  CG  GLU A 355     9337   8496   7540   1550     39     57       C  
ATOM   2793  CD  GLU A 355      47.584 -17.437 -29.614  1.00 77.69           C  
ANISOU 2793  CD  GLU A 355    10707   9880   8930   1548     19     46       C  
ATOM   2794  OE1 GLU A 355      48.539 -18.247 -29.595  1.00 85.88           O  
ANISOU 2794  OE1 GLU A 355    11759  10931   9940   1545      8     33       O  
ATOM   2795  OE2 GLU A 355      46.501 -17.671 -30.207  1.00 75.42           O1-
ANISOU 2795  OE2 GLU A 355    10396   9582   8678   1551     14     51       O1-
ATOM   2796  N   ARG A 356      50.748 -15.526 -25.614  1.00 30.85           N  
ANISOU 2796  N   ARG A 356     4864   3970   2888   1541     70     59       N  
ATOM   2797  CA  ARG A 356      52.064 -15.204 -25.084  1.00 35.37           C  
ANISOU 2797  CA  ARG A 356     5464   4557   3418   1538     72     55       C  
ATOM   2798  C   ARG A 356      52.558 -16.238 -24.081  1.00 39.02           C  
ANISOU 2798  C   ARG A 356     5929   5017   3878   1527     71     53       C  
ATOM   2799  O   ARG A 356      53.719 -16.635 -24.128  1.00 45.76           O  
ANISOU 2799  O   ARG A 356     6774   5872   4741   1503     58     42       O  
ATOM   2800  CB  ARG A 356      52.076 -13.809 -24.471  1.00 36.22           C  
ANISOU 2800  CB  ARG A 356     5580   4660   3522   1540     91     68       C  
ATOM   2801  CG  ARG A 356      53.467 -13.204 -24.342  1.00 43.96           C  
ANISOU 2801  CG  ARG A 356     6556   5640   4507   1514     86     63       C  
ATOM   2802  CD  ARG A 356      53.358 -11.699 -24.106  1.00 56.59           C  
ANISOU 2802  CD  ARG A 356     8161   7235   6104   1519    102     75       C  
ATOM   2803  NE  ARG A 356      51.964 -11.246 -24.182  1.00 63.52           N  
ANISOU 2803  NE  ARG A 356     9045   8110   6979   1545    117     87       N  
ATOM   2804  CZ  ARG A 356      51.505 -10.115 -23.650  1.00 59.64           C  
ANISOU 2804  CZ  ARG A 356     8553   7607   6499   1547    135    101       C  
ATOM   2805  NH1 ARG A 356      52.327  -9.303 -22.998  1.00 56.26           N1+
ANISOU 2805  NH1 ARG A 356     8140   7181   6054   1541    144    106       N1+
ATOM   2806  NH2 ARG A 356      50.220  -9.804 -23.766  1.00 57.44           N  
ANISOU 2806  NH2 ARG A 356     8253   7312   6261   1551    144    110       N  
ATOM   2807  N   ILE A 357      51.668 -16.673 -23.189  1.00 34.17           N  
ANISOU 2807  N   ILE A 357     5315   4392   3276   1534     84     64       N  
ATOM   2808  CA  ILE A 357      51.975 -17.722 -22.225  1.00 27.01           C  
ANISOU 2808  CA  ILE A 357     4418   3486   2360   1531     84     63       C  
ATOM   2809  C   ILE A 357      52.377 -18.991 -22.959  1.00 26.17           C  
ANISOU 2809  C   ILE A 357     4303   3387   2254   1524     62     46       C  
ATOM   2810  O   ILE A 357      53.414 -19.579 -22.656  1.00 28.03           O  
ANISOU 2810  O   ILE A 357     4531   3621   2497   1501     52     38       O  
ATOM   2811  CB  ILE A 357      50.816 -17.983 -21.227  1.00 20.62           C  
ANISOU 2811  CB  ILE A 357     3595   2656   1584   1532    101     77       C  
ATOM   2812  CG1 ILE A 357      50.699 -16.809 -20.254  1.00 26.48           C  
ANISOU 2812  CG1 ILE A 357     4347   3390   2326   1533    123     93       C  
ATOM   2813  CG2 ILE A 357      51.070 -19.242 -20.399  1.00 16.97           C  
ANISOU 2813  CG2 ILE A 357     3140   2195   1114   1528     98     74       C  
ATOM   2814  CD1 ILE A 357      49.353 -16.675 -19.577  1.00 17.30           C  
ANISOU 2814  CD1 ILE A 357     3166   2205   1203   1536    141    107       C  
ATOM   2815  N   VAL A 358      51.588 -19.400 -23.943  1.00 27.28           N  
ANISOU 2815  N   VAL A 358     4428   3526   2412   1530     52     42       N  
ATOM   2816  CA  VAL A 358      51.991 -20.555 -24.756  1.00 39.11           C  
ANISOU 2816  CA  VAL A 358     5923   5034   3902   1528     31     25       C  
ATOM   2817  C   VAL A 358      53.333 -20.379 -25.515  1.00 37.73           C  
ANISOU 2817  C   VAL A 358     5742   4867   3725   1508     15     10       C  
ATOM   2818  O   VAL A 358      54.063 -21.348 -25.714  1.00 36.20           O  
ANISOU 2818  O   VAL A 358     5540   4675   3539   1491      0     -2       O  
ATOM   2819  CB  VAL A 358      50.867 -21.036 -25.709  1.00 32.86           C  
ANISOU 2819  CB  VAL A 358     5104   4233   3149   1530     21     24       C  
ATOM   2820  CG1 VAL A 358      51.362 -22.178 -26.581  1.00 21.78           C  
ANISOU 2820  CG1 VAL A 358     3699   2840   1735   1528     -2      6       C  
ATOM   2821  CG2 VAL A 358      49.638 -21.470 -24.902  1.00 29.68           C  
ANISOU 2821  CG2 VAL A 358     4684   3809   2782   1531     32     38       C  
ATOM   2822  N   ARG A 359      53.678 -19.153 -25.907  1.00 41.83           N  
ANISOU 2822  N   ARG A 359     6260   5387   4246   1503     18     12       N  
ATOM   2823  CA  ARG A 359      54.961 -18.918 -26.577  1.00 43.11           C  
ANISOU 2823  CA  ARG A 359     6410   5553   4418   1479      5      0       C  
ATOM   2824  C   ARG A 359      56.087 -19.125 -25.598  1.00 38.06           C  
ANISOU 2824  C   ARG A 359     5767   4908   3787   1453      6      0       C  
ATOM   2825  O   ARG A 359      57.027 -19.872 -25.863  1.00 31.16           O  
ANISOU 2825  O   ARG A 359     4882   4036   2921   1433     -8    -11       O  
ATOM   2826  CB  ARG A 359      55.066 -17.515 -27.158  1.00 46.08           C  
ANISOU 2826  CB  ARG A 359     6786   5930   4792   1480      9      4       C  
ATOM   2827  CG  ARG A 359      54.317 -17.327 -28.463  1.00 62.99           C  
ANISOU 2827  CG  ARG A 359     8927   8080   6928   1499      1     -1       C  
ATOM   2828  CD  ARG A 359      54.524 -18.502 -29.395  1.00 73.71           C  
ANISOU 2828  CD  ARG A 359    10274   9442   8289   1495    -19    -17       C  
ATOM   2829  NE  ARG A 359      53.264 -19.183 -29.684  1.00 81.61           N  
ANISOU 2829  NE  ARG A 359    11281  10446   9280   1521    -20    -16       N  
ATOM   2830  CZ  ARG A 359      52.445 -18.839 -30.671  1.00 86.92           C  
ANISOU 2830  CZ  ARG A 359    11948  11120   9956   1536    -24    -16       C  
ATOM   2831  NH1 ARG A 359      52.756 -17.823 -31.465  1.00 89.62           N1+
ANISOU 2831  NH1 ARG A 359    12293  11469  10289   1538    -25    -19       N1+
ATOM   2832  NH2 ARG A 359      51.318 -19.510 -30.868  1.00 88.44           N  
ANISOU 2832  NH2 ARG A 359    12119  11299  10185   1537    -28    -11       N  
ATOM   2833  N   ILE A 360      55.976 -18.455 -24.457  1.00 32.96           N  
ANISOU 2833  N   ILE A 360     5129   4255   3139   1454     23     14       N  
ATOM   2834  CA  ILE A 360      56.967 -18.575 -23.397  1.00 27.87           C  
ANISOU 2834  CA  ILE A 360     4483   3605   2502   1431     27     16       C  
ATOM   2835  C   ILE A 360      57.140 -20.019 -22.938  1.00 31.95           C  
ANISOU 2835  C   ILE A 360     4997   4121   3022   1424     19     10       C  
ATOM   2836  O   ILE A 360      58.255 -20.450 -22.676  1.00 37.57           O  
ANISOU 2836  O   ILE A 360     5699   4832   3742   1399     12      3       O  
ATOM   2837  CB  ILE A 360      56.613 -17.679 -22.231  1.00 22.97           C  
ANISOU 2837  CB  ILE A 360     3873   2977   1878   1437     48     32       C  
ATOM   2838  CG1 ILE A 360      56.714 -16.211 -22.678  1.00 20.87           C  
ANISOU 2838  CG1 ILE A 360     3608   2711   1610   1439     53     37       C  
ATOM   2839  CG2 ILE A 360      57.515 -17.985 -21.048  1.00 21.09           C  
ANISOU 2839  CG2 ILE A 360     3634   2732   1646   1416     51     34       C  
ATOM   2840  CD1 ILE A 360      55.752 -15.235 -21.990  1.00 18.29           C  
ANISOU 2840  CD1 ILE A 360     3295   2378   1275   1459     75     54       C  
ATOM   2841  N   LEU A 361      56.048 -20.775 -22.871  1.00 31.62           N  
ANISOU 2841  N   LEU A 361     4961   4079   2973   1445     21     13       N  
ATOM   2842  CA  LEU A 361      56.151 -22.196 -22.564  1.00 31.62           C  
ANISOU 2842  CA  LEU A 361     4959   4080   2976   1440     13      6       C  
ATOM   2843  C   LEU A 361      56.853 -22.970 -23.683  1.00 36.27           C  
ANISOU 2843  C   LEU A 361     5534   4675   3572   1426     -9    -11       C  
ATOM   2844  O   LEU A 361      57.655 -23.871 -23.406  1.00 44.89           O  
ANISOU 2844  O   LEU A 361     6619   5767   4672   1407    -17    -19       O  
ATOM   2845  CB  LEU A 361      54.794 -22.808 -22.194  1.00 16.33           C  
ANISOU 2845  CB  LEU A 361     3033   2141   1030   1466     21     13       C  
ATOM   2846  CG  LEU A 361      54.246 -22.474 -20.779  1.00 49.12           C  
ANISOU 2846  CG  LEU A 361     7198   6285   5178   1475     43     30       C  
ATOM   2847  CD1 LEU A 361      52.955 -23.253 -20.419  1.00 16.59           C  
ANISOU 2847  CD1 LEU A 361     3089   2165   1051   1499     51     37       C  
ATOM   2848  CD2 LEU A 361      55.287 -22.639 -19.674  1.00 16.27           C  
ANISOU 2848  CD2 LEU A 361     3036   2120   1026   1451     46     32       C  
ATOM   2849  N   THR A 362      56.577 -22.614 -24.938  1.00 37.79           N  
ANISOU 2849  N   THR A 362     5723   4873   3761   1435    -17    -18       N  
ATOM   2850  CA  THR A 362      57.306 -23.211 -26.063  1.00 36.03           C  
ANISOU 2850  CA  THR A 362     5487   4656   3546   1421    -36    -34       C  
ATOM   2851  C   THR A 362      58.819 -22.986 -25.941  1.00 40.40           C  
ANISOU 2851  C   THR A 362     6030   5209   4111   1390    -41    -39       C  
ATOM   2852  O   THR A 362      59.592 -23.890 -26.193  1.00 39.49           O  
ANISOU 2852  O   THR A 362     5905   5095   4004   1373    -53    -50       O  
ATOM   2853  CB  THR A 362      56.814 -22.691 -27.439  1.00 30.85           C  
ANISOU 2853  CB  THR A 362     4829   4006   2885   1436    -44    -39       C  
ATOM   2854  CG2 THR A 362      57.711 -23.196 -28.546  1.00 27.56           C  
ANISOU 2854  CG2 THR A 362     4399   3595   2478   1418    -62    -56       C  
ATOM   2855  OG1 THR A 362      55.481 -23.151 -27.695  1.00 36.81           O  
ANISOU 2855  OG1 THR A 362     5592   4764   3631   1463    -43    -37       O  
ATOM   2856  N   TYR A 363      59.236 -21.790 -25.532  1.00 53.99           N  
ANISOU 2856  N   TYR A 363     7753   6927   5833   1383    -31    -32       N  
ATOM   2857  CA  TYR A 363      60.659 -21.506 -25.348  1.00 62.91           C  
ANISOU 2857  CA  TYR A 363     8873   8056   6974   1354    -34    -35       C  
ATOM   2858  C   TYR A 363      61.273 -22.316 -24.211  1.00 67.97           C  
ANISOU 2858  C   TYR A 363     9513   8692   7620   1337    -32    -34       C  
ATOM   2859  O   TYR A 363      62.083 -23.207 -24.455  1.00 78.22           O  
ANISOU 2859  O   TYR A 363    10801   9992   8926   1319    -43    -45       O  
ATOM   2860  CB  TYR A 363      60.914 -20.019 -25.103  1.00 77.87           C  
ANISOU 2860  CB  TYR A 363    10771   9948   8867   1350    -23    -26       C  
ATOM   2861  CG  TYR A 363      62.388 -19.697 -24.929  1.00 96.71           C  
ANISOU 2861  CG  TYR A 363    13147  12334  11264   1321    -26    -30       C  
ATOM   2862  CD1 TYR A 363      63.199 -19.442 -26.034  1.00103.74           C  
ANISOU 2862  CD1 TYR A 363    14026  13229  12161   1307    -37    -41       C  
ATOM   2863  CD2 TYR A 363      62.976 -19.660 -23.661  1.00105.66           C  
ANISOU 2863  CD2 TYR A 363    14282  13461  12401   1306    -18    -23       C  
ATOM   2864  CE1 TYR A 363      64.553 -19.155 -25.886  1.00108.65           C  
ANISOU 2864  CE1 TYR A 363    14638  13851  12793   1279    -39    -44       C  
ATOM   2865  CE2 TYR A 363      64.331 -19.375 -23.500  1.00110.67           C  
ANISOU 2865  CE2 TYR A 363    14908  14097  13046   1279    -21    -27       C  
ATOM   2866  CZ  TYR A 363      65.114 -19.122 -24.618  1.00112.10           C  
ANISOU 2866  CZ  TYR A 363    15077  14282  13233   1266    -32    -37       C  
ATOM   2867  OH  TYR A 363      66.456 -18.839 -24.471  1.00111.39           O  
ANISOU 2867  OH  TYR A 363    14977  14192  13153   1239    -34    -40       O  
ATOM   2868  N   GLY A 364      60.909 -21.987 -22.973  1.00 62.55           N  
ANISOU 2868  N   GLY A 364     8837   8000   6929   1343    -17    -21       N  
ATOM   2869  CA  GLY A 364      61.390 -22.716 -21.811  1.00 61.59           C  
ANISOU 2869  CA  GLY A 364     8716   7874   6813   1329    -14    -19       C  
ATOM   2870  C   GLY A 364      62.900 -22.836 -21.717  1.00 64.09           C  
ANISOU 2870  C   GLY A 364     9020   8191   7141   1298    -21    -25       C  
ATOM   2871  O   GLY A 364      63.589 -21.877 -21.370  1.00 68.40           O  
ANISOU 2871  O   GLY A 364     9564   8734   7689   1285    -16    -21       O  
CONECT    1    2
CONECT    2    1    3    5
CONECT    3    2    4    9
CONECT    4    3
CONECT    5    2    6
CONECT    6    5    8
CONECT    7    8
CONECT    8    6    7
CONECT    9    3
CONECT  296  302
CONECT  302  296  303
CONECT  303  302  304  306
CONECT  304  303  305  310
CONECT  305  304
CONECT  306  303  307
CONECT  307  306  309
CONECT  308  309
CONECT  309  307  308
CONECT  310  304
CONECT  540  547
CONECT  547  540  548
CONECT  548  547  549  551
CONECT  549  548  550  555
CONECT  550  549
CONECT  551  548  552
CONECT  552  551  554
CONECT  553  554
CONECT  554  552  553
CONECT  555  549
CONECT  943  949
CONECT  949  943  950
CONECT  950  949  951  953
CONECT  951  950  952  957
CONECT  952  951
CONECT  953  950  954
CONECT  954  953  956
CONECT  955  956
CONECT  956  954  955
CONECT  957  951
CONECT 2173 2179
CONECT 2179 2173 2180
CONECT 2180 2179 2181 2183
CONECT 2181 2180 2182 2187
CONECT 2182 2181
CONECT 2183 2180 2184
CONECT 2184 2183 2186
CONECT 2185 2186
CONECT 2186 2184 2185
CONECT 2187 2181
CONECT 2636 2642
CONECT 2642 2636 2643
CONECT 2643 2642 2644 2646
CONECT 2644 2643 2645 2650
CONECT 2645 2644
CONECT 2646 2643 2647
CONECT 2647 2646 2649
CONECT 2648 2649
CONECT 2649 2647 2648
CONECT 2650 2644
END



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