CNRS Nantes University UFIP UFIP
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***  test 1  ***

elNémo ID: 22012619325799739

Job options:

ID        	=	 22012619325799739
JOBID     	=	 test 1
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 test 1

CRYST1   32.364   53.389   74.944  90.00  90.00  90.00 P 21 21 21    1
ATOM      1  N  ACYS A   1      11.779  15.793   0.053  0.50 20.48           N  
ANISOU    1  N  ACYS A   1     3180   2574   2026   -173    -11    517       N  
ATOM      2  N  BCYS A   1      11.756  15.735   0.087  0.50 19.68           N  
ANISOU    2  N  BCYS A   1     3160   2439   1878   -206    -13    544       N  
ATOM      3  CA ACYS A   1      10.809  15.332   1.089  0.50 20.58           C  
ANISOU    3  CA ACYS A   1     3141   2610   2069   -103     18    483       C  
ATOM      4  CA BCYS A   1      10.835  15.087   1.084  0.50 18.98           C  
ANISOU    4  CA BCYS A   1     3141   2290   1778   -185    -35    491       C  
ATOM      5  C  ACYS A   1       9.616  14.557   0.470  0.50 18.36           C  
ANISOU    5  C  ACYS A   1     2930   2296   1750   -122    -28    697       C  
ATOM      6  C  BCYS A   1       9.607  14.451   0.450  0.50 17.13           C  
ANISOU    6  C  BCYS A   1     2901   2072   1533   -171     -3    788       C  
ATOM      7  O  ACYS A   1       8.889  13.873   1.201  0.50 19.39           O  
ANISOU    7  O  ACYS A   1     3009   2378   1979   -122     40    611       O  
ATOM      8  O  BCYS A   1       8.849  13.725   1.133  0.50 17.03           O  
ANISOU    8  O  BCYS A   1     3105   1839   1524   -133    169   1085       O  
ATOM      9  CB ACYS A   1      10.327  16.539   1.937  0.50 21.46           C  
ANISOU    9  CB ACYS A   1     3132   2734   2285   -107     68    392       C  
ATOM     10  CB BCYS A   1      10.384  16.019   2.194  0.50 18.90           C  
ANISOU   10  CB BCYS A   1     3134   2359   1687    -38     53    522       C  
ATOM     11  SG ACYS A   1      10.477  16.496   3.830  0.50 26.49           S  
ANISOU   11  SG ACYS A   1     3936   3564   2564    102    667    534       S  
ATOM     12  SG BCYS A   1      11.719  16.784   3.088  0.50 24.58           S  
ANISOU   12  SG BCYS A   1     3916   3366   2056   -263     19   -523       S  
ATOM     13  N   ASP A   2       9.467  14.575  -0.860  1.00 18.05           N  
ANISOU   13  N   ASP A   2     2859   2441   1555   -266   -131    820       N  
ATOM     14  CA  ASP A   2       8.416  13.853  -1.473  1.00 18.44           C  
ANISOU   14  CA  ASP A   2     3028   2499   1477   -351   -122    915       C  
ATOM     15  C   ASP A   2       8.594  12.336  -1.275  1.00 17.83           C  
ANISOU   15  C   ASP A   2     3102   2533   1140   -304    -27    830       C  
ATOM     16  O   ASP A   2       7.587  11.660  -1.364  1.00 19.15           O  
ANISOU   16  O   ASP A   2     3004   2855   1416   -441     31    662       O  
ATOM     17  CB  ASP A   2       8.220  14.232  -2.900  1.00 19.63           C  
ANISOU   17  CB  ASP A   2     3211   2608   1639   -445   -124    823       C  
ATOM     18  CG  ASP A   2       7.662  15.655  -3.078  1.00 21.34           C  
ANISOU   18  CG  ASP A   2     3322   2859   1926    -68   -516   1160       C  
ATOM     19  OD1 ASP A   2       6.970  16.176  -2.168  1.00 27.85           O  
ANISOU   19  OD1 ASP A   2     4028   3860   2692    381   -249   1139       O  
ATOM     20  OD2 ASP A   2       7.923  16.278  -4.088  1.00 25.97           O1-
ANISOU   20  OD2 ASP A   2     3676   3570   2621   -429   -603   1071       O1-
ATOM     21  N   ALA A   3       9.822  11.816  -1.047  1.00 16.97           N  
ANISOU   21  N   ALA A   3     3010   2458    980   -430    331    706       N  
ATOM     22  CA  ALA A   3      10.015  10.383  -0.794  1.00 17.47           C  
ANISOU   22  CA  ALA A   3     3122   2407   1109   -153    241    622       C  
ATOM     23  C   ALA A   3       9.287   9.911   0.449  1.00 13.97           C  
ANISOU   23  C   ALA A   3     3017   1785    503   -130    285    326       C  
ATOM     24  O   ALA A   3       9.019   8.724   0.591  1.00 15.18           O  
ANISOU   24  O   ALA A   3     3283   1748    736      6    510     31       O  
ATOM     25  CB  ALA A   3      11.465  10.076  -0.649  1.00 19.89           C  
ANISOU   25  CB  ALA A   3     3172   2583   1802   -203    246    819       C  
ATOM     26  N   PHE A   4       8.996  10.840   1.361  1.00 12.69           N  
ANISOU   26  N   PHE A   4     2769   1545    506   -161    133    318       N  
ATOM     27  CA  PHE A   4       8.264  10.487   2.581  1.00 11.93           C  
ANISOU   27  CA  PHE A   4     2680   1331    521    -16    138    162       C  
ATOM     28  C   PHE A   4       6.758  10.530   2.431  1.00 10.76           C  
ANISOU   28  C   PHE A   4     2567   1133    386    -49     91     42       C  
ATOM     29  O   PHE A   4       6.040   9.971   3.248  1.00 12.08           O  
ANISOU   29  O   PHE A   4     2748   1373    468   -214    135    247       O  
ATOM     30  CB  PHE A   4       8.645  11.433   3.727  1.00 12.73           C  
ANISOU   30  CB  PHE A   4     2603   1427    807    -52     27    -11       C  
ATOM     31  CG  PHE A   4      10.069  11.305   4.160  1.00 12.26           C  
ANISOU   31  CG  PHE A   4     2570   1396    691     11    -32    -65       C  
ATOM     32  CD1 PHE A   4      10.447  10.284   5.009  1.00 13.61           C  
ANISOU   32  CD1 PHE A   4     2782   1800    588    -93    -47    181       C  
ATOM     33  CD2 PHE A   4      11.022  12.214   3.759  1.00 15.76           C  
ANISOU   33  CD2 PHE A   4     2885   2139    963   -111   -328    402       C  
ATOM     34  CE1 PHE A   4      11.738  10.164   5.416  1.00 15.22           C  
ANISOU   34  CE1 PHE A   4     2826   2221    734    126   -112    108       C  
ATOM     35  CE2 PHE A   4      12.335  12.061   4.125  1.00 16.62           C  
ANISOU   35  CE2 PHE A   4     2725   2638    951   -366    139    249       C  
ATOM     36  CZ  PHE A   4      12.690  11.033   4.990  1.00 14.48           C  
ANISOU   36  CZ  PHE A   4     2489   2221    792    101   -116   -197       C  
ATOM     37  N   VAL A   5       6.278  11.249   1.424  1.00 11.20           N  
ANISOU   37  N   VAL A   5     2698   1250    306    -29     76    224       N  
ATOM     38  CA  VAL A   5       4.862  11.496   1.328  1.00 11.54           C  
ANISOU   38  CA  VAL A   5     2629   1227    528   -128    173    -31       C  
ATOM     39  C   VAL A   5       4.135  10.193   1.034  1.00 11.80           C  
ANISOU   39  C   VAL A   5     2735   1289    456   -257    110   -225       C  
ATOM     40  O   VAL A   5       4.523   9.396   0.166  1.00 15.61           O  
ANISOU   40  O   VAL A   5     3312   1658    961   -499    528   -510       O  
ATOM     41  CB  VAL A   5       4.607  12.579   0.295  1.00 12.55           C  
ANISOU   41  CB  VAL A   5     2774   1210    782     12     76    198       C  
ATOM     42  CG1 VAL A   5       3.152  12.606  -0.252  1.00 16.21           C  
ANISOU   42  CG1 VAL A   5     3416   1783    958   -100   -371    141       C  
ATOM     43  CG2 VAL A   5       5.141  13.916   0.796  1.00 14.35           C  
ANISOU   43  CG2 VAL A   5     3054   1278   1118   -221   -173    269       C  
ATOM     44  N   GLY A   6       2.988  10.031   1.653  1.00 11.59           N  
ANISOU   44  N   GLY A   6     2673   1303    427   -278     80   -133       N  
ATOM     45  CA  GLY A   6       2.165   8.885   1.426  1.00 12.62           C  
ANISOU   45  CA  GLY A   6     2700   1572    522   -234     77   -130       C  
ATOM     46  C   GLY A   6       1.499   8.402   2.667  1.00 10.77           C  
ANISOU   46  C   GLY A   6     2341   1318    434   -214   -132    -89       C  
ATOM     47  O   GLY A   6       1.442   9.081   3.668  1.00 12.82           O  
ANISOU   47  O   GLY A   6     2926   1391    551   -342    147   -194       O  
ATOM     48  N   THR A   7       0.980   7.201   2.550  1.00 11.21           N  
ANISOU   48  N   THR A   7     2530   1333    394   -174   -215    -58       N  
ATOM     49  CA  THR A   7       0.238   6.535   3.616  1.00 11.96           C  
ANISOU   49  CA  THR A   7     2563   1212    767    -39   -128    -78       C  
ATOM     50  C   THR A   7       1.011   5.279   3.974  1.00 11.23           C  
ANISOU   50  C   THR A   7     2419   1259    588    -98   -186     -1       C  
ATOM     51  O   THR A   7       1.261   4.449   3.110  1.00 13.32           O  
ANISOU   51  O   THR A   7     3028   1392    639     82   -363    -90       O  
ATOM     52  CB  THR A   7      -1.162   6.185   3.147  1.00 13.79           C  
ANISOU   52  CB  THR A   7     2542   1288   1407    -42    -93    150       C  
ATOM     53  CG2 THR A   7      -2.042   5.761   4.247  1.00 17.93           C  
ANISOU   53  CG2 THR A   7     2876   2123   1814   -172     -5    -40       C  
ATOM     54  OG1 THR A   7      -1.729   7.307   2.452  1.00 18.84           O  
ANISOU   54  OG1 THR A   7     2954   1840   2364    -90   -489    130       O  
ATOM     55  N   TRP A   8       1.350   5.157   5.249  1.00 10.74           N  
ANISOU   55  N   TRP A   8     2446   1295    336     42     21     82       N  
ATOM     56  CA  TRP A   8       2.259   4.155   5.759  1.00 10.97           C  
ANISOU   56  CA  TRP A   8     2552   1224    390    -71     76     96       C  
ATOM     57  C   TRP A   8       1.597   3.390   6.876  1.00 10.82           C  
ANISOU   57  C   TRP A   8     2622   1135    353   -133    176     -5       C  
ATOM     58  O   TRP A   8       0.761   3.944   7.601  1.00 14.92           O  
ANISOU   58  O   TRP A   8     3378   1369    922    -12    704    172       O  
ATOM     59  CB  TRP A   8       3.510   4.836   6.296  1.00 10.42           C  
ANISOU   59  CB  TRP A   8     2473   1177    309     38     97    220       C  
ATOM     60  CG  TRP A   8       4.243   5.666   5.273  1.00 10.22           C  
ANISOU   60  CG  TRP A   8     2453   1170    260     -7   -127     -1       C  
ATOM     61  CD1 TRP A   8       4.142   7.004   5.047  1.00 10.43           C  
ANISOU   61  CD1 TRP A   8     2412   1245    305    -77     24     62       C  
ATOM     62  CD2 TRP A   8       5.236   5.176   4.372  1.00 10.16           C  
ANISOU   62  CD2 TRP A   8     2380   1057    422    -30    -63    137       C  
ATOM     63  CE2 TRP A   8       5.682   6.267   3.609  1.00 10.34           C  
ANISOU   63  CE2 TRP A   8     2339   1321    267   -163     90   -113       C  
ATOM     64  CE3 TRP A   8       5.778   3.912   4.120  1.00 10.69           C  
ANISOU   64  CE3 TRP A   8     2470   1184    404   -192    -82    -38       C  
ATOM     65  NE1 TRP A   8       5.005   7.378   4.030  1.00 11.16           N  
ANISOU   65  NE1 TRP A   8     2604   1226    408   -198    137     53       N  
ATOM     66  CZ2 TRP A   8       6.660   6.125   2.627  1.00 11.66           C  
ANISOU   66  CZ2 TRP A   8     2558   1500    371   -296     22    -41       C  
ATOM     67  CZ3 TRP A   8       6.763   3.778   3.173  1.00 11.56           C  
ANISOU   67  CZ3 TRP A   8     2332   1273    786    -31    -69   -172       C  
ATOM     68  CH2 TRP A   8       7.163   4.866   2.406  1.00 12.21           C  
ANISOU   68  CH2 TRP A   8     2385   1588    666   -152    239   -385       C  
ATOM     69  N   LYS A   9       1.920   2.130   7.023  1.00 10.50           N  
ANISOU   69  N   LYS A   9     2493   1123    371   -150    -56    164       N  
ATOM     70  CA  LYS A   9       1.380   1.290   8.104  1.00 11.25           C  
ANISOU   70  CA  LYS A   9     2458   1381    433   -156    -51    195       C  
ATOM     71  C   LYS A   9       2.505   0.612   8.842  1.00 10.45           C  
ANISOU   71  C   LYS A   9     2299   1179    491   -179     29    194       C  
ATOM     72  O   LYS A   9       3.447   0.130   8.245  1.00 11.06           O  
ANISOU   72  O   LYS A   9     2425   1362    413    -97    -24     70       O  
ATOM     73  CB  LYS A   9       0.463   0.256   7.499  1.00 13.67           C  
ANISOU   73  CB  LYS A   9     2544   1663    988   -285    -51    565       C  
ATOM     74  CG  LYS A   9       1.056  -0.687   6.523  1.00 20.11           C  
ANISOU   74  CG  LYS A   9     3382   2446   1813   -317   -239    208       C  
ATOM     75  CD  LYS A   9       0.019  -1.643   5.988  1.00 25.34           C  
ANISOU   75  CD  LYS A   9     3891   3111   2623   -606   -309   -204       C  
ATOM     76  CE  LYS A   9       0.667  -2.635   5.032  1.00 27.06           C  
ANISOU   76  CE  LYS A   9     4027   3352   2901   -822   -280   -769       C  
ATOM     77  NZ  LYS A   9       0.484  -2.414   3.549  1.00 32.18           N1+
ANISOU   77  NZ  LYS A   9     4567   4142   3516   -480   -449    -21       N1+
ATOM     78  N   LEU A  10       2.422   0.612  10.175  1.00 11.73           N  
ANISOU   78  N   LEU A  10     2369   1560    527   -129    -42    266       N  
ATOM     79  CA  LEU A  10       3.468  -0.006  11.001  1.00 11.33           C  
ANISOU   79  CA  LEU A  10     2237   1530    536   -313    -90    192       C  
ATOM     80  C   LEU A  10       3.436  -1.501  10.785  1.00 12.05           C  
ANISOU   80  C   LEU A  10     2408   1571    599   -315   -127    317       C  
ATOM     81  O   LEU A  10       2.376  -2.096  10.992  1.00 14.46           O  
ANISOU   81  O   LEU A  10     2585   1794   1115   -471   -144    470       O  
ATOM     82  CB  LEU A  10       3.254   0.313  12.477  1.00 12.37           C  
ANISOU   82  CB  LEU A  10     2426   1850    421   -315     58    240       C  
ATOM     83  CG  LEU A  10       4.334  -0.246  13.396  1.00 12.95           C  
ANISOU   83  CG  LEU A  10     2568   1768    584   -306   -225    260       C  
ATOM     84  CD1 LEU A  10       5.653   0.444  13.213  1.00 13.42           C  
ANISOU   84  CD1 LEU A  10     2362   1950    787    -17    -20    137       C  
ATOM     85  CD2 LEU A  10       3.881  -0.178  14.887  1.00 15.73           C  
ANISOU   85  CD2 LEU A  10     2826   2632    517     11     33    283       C  
ATOM     86  N   VAL A  11       4.593  -2.078  10.473  1.00 11.83           N  
ANISOU   86  N   VAL A  11     2608   1172    716   -222   -365    132       N  
ATOM     87  CA  VAL A  11       4.713  -3.531  10.340  1.00 14.22           C  
ANISOU   87  CA  VAL A  11     3007   1390   1005   -106   -483    105       C  
ATOM     88  C   VAL A  11       5.633  -4.243  11.315  1.00 14.97           C  
ANISOU   88  C   VAL A  11     3076   1328   1284   -155   -586    459       C  
ATOM     89  O   VAL A  11       5.518  -5.445  11.488  1.00 19.17           O  
ANISOU   89  O   VAL A  11     3797   1425   2059   -291  -1008    609       O  
ATOM     90  CB  VAL A  11       5.074  -3.935   8.931  1.00 15.39           C  
ANISOU   90  CB  VAL A  11     3209   1258   1379     57   -429   -102       C  
ATOM     91  CG1 VAL A  11       3.989  -3.467   7.993  1.00 17.72           C  
ANISOU   91  CG1 VAL A  11     3577   1809   1345    164   -592    -69       C  
ATOM     92  CG2 VAL A  11       6.488  -3.468   8.493  1.00 16.81           C  
ANISOU   92  CG2 VAL A  11     3363   1906   1118    173    -55   -232       C  
ATOM     93  N   SER A  12       6.565  -3.539  11.949  1.00 13.74           N  
ANISOU   93  N   SER A  12     2994   1348    876   -176   -459    187       N  
ATOM     94  CA  SER A  12       7.390  -4.157  12.974  1.00 14.10           C  
ANISOU   94  CA  SER A  12     3045   1320    992    -11   -462    228       C  
ATOM     95  C   SER A  12       7.890  -3.096  13.912  1.00 12.27           C  
ANISOU   95  C   SER A  12     2601   1289    772    -41   -302    276       C  
ATOM     96  O   SER A  12       8.071  -1.931  13.540  1.00 12.69           O  
ANISOU   96  O   SER A  12     2812   1368    640   -183   -210    445       O  
ATOM     97  CB  SER A  12       8.522  -4.928  12.349  1.00 17.16           C  
ANISOU   97  CB  SER A  12     3292   2042   1183    134   -438    189       C  
ATOM     98  OG  SER A  12       9.489  -4.078  11.805  1.00 17.97           O  
ANISOU   98  OG  SER A  12     3608   2082   1138    276   -278    188       O  
ATOM     99  N   SER A  13       8.180  -3.542  15.111  1.00 13.20           N  
ANISOU   99  N   SER A  13     2876   1263    873   -298   -436    512       N  
ATOM    100  CA  SER A  13       8.727  -2.701  16.134  1.00 13.68           C  
ANISOU  100  CA  SER A  13     2825   1457    915   -297   -483    439       C  
ATOM    101  C   SER A  13       9.685  -3.511  16.994  1.00 13.84           C  
ANISOU  101  C   SER A  13     2779   1567    909   -306   -233    639       C  
ATOM    102  O   SER A  13       9.368  -4.656  17.344  1.00 16.68           O  
ANISOU  102  O   SER A  13     3267   1603   1466   -494   -634    764       O  
ATOM    103  CB  SER A  13       7.531  -2.169  16.971  1.00 15.44           C  
ANISOU  103  CB  SER A  13     3141   1774    951   -329   -495    270       C  
ATOM    104  OG  SER A  13       7.893  -1.283  17.992  1.00 17.10           O  
ANISOU  104  OG  SER A  13     3655   2023    818   -269   -688    244       O  
ATOM    105  N   GLU A  14      10.824  -2.927  17.320  1.00 11.91           N  
ANISOU  105  N   GLU A  14     2688   1230    606   -144   -290    275       N  
ATOM    106  CA AGLU A  14      11.878  -3.514  18.147  0.50 12.88           C  
ANISOU  106  CA AGLU A  14     2784   1127    983      9   -235    105       C  
ATOM    107  CA BGLU A  14      11.738  -3.542  18.228  0.50 11.40           C  
ANISOU  107  CA BGLU A  14     2626    959    745     23   -201    -15       C  
ATOM    108  C   GLU A  14      12.147  -2.556  19.305  1.00 10.73           C  
ANISOU  108  C   GLU A  14     2416   1075    584     61    -78     82       C  
ATOM    109  O   GLU A  14      12.417  -1.379  19.033  1.00 11.44           O  
ANISOU  109  O   GLU A  14     2780   1064    502    -78   -255     83       O  
ATOM    110  CB AGLU A  14      13.236  -3.628  17.367  0.50 14.59           C  
ANISOU  110  CB AGLU A  14     2901   1268   1375      6   -281     87       C  
ATOM    111  CB BGLU A  14      12.975  -4.025  17.450  0.50 11.91           C  
ANISOU  111  CB BGLU A  14     2540   1130    852     74   -214   -211       C  
ATOM    112  CG AGLU A  14      13.383  -4.318  16.010  0.50 18.96           C  
ANISOU  112  CG AGLU A  14     3393   1734   2076    125   -147    -99       C  
ATOM    113  CG BGLU A  14      12.805  -5.143  16.500  0.50 13.49           C  
ANISOU  113  CG BGLU A  14     2730   1255   1139     29     53   -491       C  
ATOM    114  CD AGLU A  14      14.705  -3.846  15.331  0.50 23.07           C  
ANISOU  114  CD AGLU A  14     3796   2400   2570    325    143     -1       C  
ATOM    115  CD BGLU A  14      12.765  -6.504  17.158  0.50 14.19           C  
ANISOU  115  CD BGLU A  14     2728   1584   1076    231     56   -490       C  
ATOM    116  OE1AGLU A  14      15.703  -3.486  16.048  0.50 21.79           O  
ANISOU  116  OE1AGLU A  14     3798   1602   2876    691    250   -137       O  
ATOM    117  OE1BGLU A  14      13.014  -6.578  18.372  0.50 16.35           O  
ANISOU  117  OE1BGLU A  14     3057   1532   1621    150   -736   -562       O  
ATOM    118  OE2AGLU A  14      14.734  -3.769  14.075  0.50 23.71           O1-
ANISOU  118  OE2AGLU A  14     4386   1911   2712    337    498    -48       O1-
ATOM    119  OE2BGLU A  14      12.455  -7.485  16.469  0.50 17.79           O1-
ANISOU  119  OE2BGLU A  14     3266   1786   1707    254     95   -870       O1-
ATOM    120  N   ASN A  15      12.167  -3.058  20.527  1.00 10.64           N  
ANISOU  120  N   ASN A  15     2361   1146    533    -57   -145    225       N  
ATOM    121  CA AASN A  15      12.670  -2.335  21.699  0.50  9.72           C  
ANISOU  121  CA AASN A  15     2309   1062    323     75   -176    160       C  
ATOM    122  CA BASN A  15      12.615  -2.319  21.708  0.50 11.06           C  
ANISOU  122  CA BASN A  15     2445   1237    518     68   -160    102       C  
ATOM    123  C   ASN A  15      11.825  -1.109  22.058  1.00 10.22           C  
ANISOU  123  C   ASN A  15     2327   1141    415     15    -41    116       C  
ATOM    124  O   ASN A  15      12.305  -0.240  22.784  1.00 11.03           O  
ANISOU  124  O   ASN A  15     2435   1219    536      5   -115     64       O  
ATOM    125  CB AASN A  15      14.172  -1.996  21.542  0.50 10.16           C  
ANISOU  125  CB AASN A  15     2362   1094    402     78   -203    202       C  
ATOM    126  CB BASN A  15      14.063  -1.929  21.588  0.50 12.10           C  
ANISOU  126  CB BASN A  15     2579   1391    627     54   -134     67       C  
ATOM    127  CG AASN A  15      14.948  -2.010  22.862  0.50  8.63           C  
ANISOU  127  CG AASN A  15     2119    807    354    204   -149    189       C  
ATOM    128  CG BASN A  15      14.901  -3.086  21.382  0.50 16.49           C  
ANISOU  128  CG BASN A  15     2796   2095   1372    188   -142    -11       C  
ATOM    129  ND2AASN A  15      15.777  -0.996  23.073  0.50  9.36           N  
ANISOU  129  ND2AASN A  15     2162   1006    387    133     26    153       N  
ATOM    130  ND2BASN A  15      15.502  -3.202  20.230  0.50 22.26           N  
ANISOU  130  ND2BASN A  15     3501   2965   1991    671    316    214       N  
ATOM    131  OD1AASN A  15      14.809  -2.935  23.662  0.50 10.02           O  
ANISOU  131  OD1AASN A  15     2321    862    624     -5   -153    346       O  
ATOM    132  OD1BASN A  15      14.954  -3.934  22.243  0.50 18.79           O  
ANISOU  132  OD1BASN A  15     3839   1557   1740    432    120    -23       O  
ATOM    133  N   PHE A  16      10.586  -1.038  21.600  1.00 11.10           N  
ANISOU  133  N   PHE A  16     2358   1190    669    -46     -4    -13       N  
ATOM    134  CA  PHE A  16       9.770   0.140  21.861  1.00 11.60           C  
ANISOU  134  CA  PHE A  16     2364   1546    496      0    -81     31       C  
ATOM    135  C   PHE A  16       9.404   0.277  23.320  1.00 11.48           C  
ANISOU  135  C   PHE A  16     2379   1360    621    -66   -120    117       C  
ATOM    136  O   PHE A  16       9.331   1.403  23.828  1.00 11.02           O  
ANISOU  136  O   PHE A  16     2445   1215    524   -181    -13     50       O  
ATOM    137  CB  PHE A  16       8.539   0.145  20.934  1.00 12.43           C  
ANISOU  137  CB  PHE A  16     2355   1689    675    120   -126     -6       C  
ATOM    138  CG  PHE A  16       7.790   1.457  20.912  1.00 13.17           C  
ANISOU  138  CG  PHE A  16     2549   2132    320    226    -37     -2       C  
ATOM    139  CD1 PHE A  16       8.434   2.638  20.570  1.00 13.46           C  
ANISOU  139  CD1 PHE A  16     2587   1789    736    384   -115   -106       C  
ATOM    140  CD2 PHE A  16       6.439   1.482  21.144  1.00 14.47           C  
ANISOU  140  CD2 PHE A  16     2739   2157    600    344    -27   -249       C  
ATOM    141  CE1 PHE A  16       7.721   3.845  20.477  1.00 14.75           C  
ANISOU  141  CE1 PHE A  16     2968   1805    830    253   -159      2       C  
ATOM    142  CE2 PHE A  16       5.724   2.660  21.038  1.00 15.15           C  
ANISOU  142  CE2 PHE A  16     2712   2396    648    473     44   -122       C  
ATOM    143  CZ  PHE A  16       6.374   3.813  20.730  1.00 14.50           C  
ANISOU  143  CZ  PHE A  16     2980   1997    529    595   -276   -115       C  
ATOM    144  N   ASP A  17       9.128  -0.812  24.023  1.00 11.92           N  
ANISOU  144  N   ASP A  17     2590   1164    772    -96    137     -7       N  
ATOM    145  CA  ASP A  17       8.817  -0.719  25.447  1.00 12.07           C  
ANISOU  145  CA  ASP A  17     2644   1314    625   -113    206    172       C  
ATOM    146  C   ASP A  17      10.004  -0.114  26.192  1.00 12.00           C  
ANISOU  146  C   ASP A  17     2535   1264    759    -83     30    449       C  
ATOM    147  O   ASP A  17       9.822   0.782  27.021  1.00 12.36           O  
ANISOU  147  O   ASP A  17     2867   1281    547    -86     77    123       O  
ATOM    148  CB  ASP A  17       8.424  -2.080  25.988  1.00 14.58           C  
ANISOU  148  CB  ASP A  17     2892   1550   1097   -119    229    249       C  
ATOM    149  CG  ASP A  17       7.882  -1.990  27.377  1.00 16.68           C  
ANISOU  149  CG  ASP A  17     3061   1929   1347   -352    279    632       C  
ATOM    150  OD1 ASP A  17       8.504  -2.522  28.287  1.00 22.59           O  
ANISOU  150  OD1 ASP A  17     3571   3517   1495   -145     62    704       O  
ATOM    151  OD2 ASP A  17       6.845  -1.378  27.579  1.00 18.00           O1-
ANISOU  151  OD2 ASP A  17     3413   2346   1077    -59    447    434       O1-
ATOM    152  N   ASP A  18      11.213  -0.572  25.910  1.00 11.99           N  
ANISOU  152  N   ASP A  18     2584   1233    739     25    128    304       N  
ATOM    153  CA AASP A  18      12.373  -0.051  26.577  0.50 13.22           C  
ANISOU  153  CA AASP A  18     2577   1563    881     12     27    438       C  
ATOM    154  CA BASP A  18      12.403  -0.043  26.577  0.50 13.30           C  
ANISOU  154  CA BASP A  18     2600   1582    869     47     -5    442       C  
ATOM    155  C   ASP A  18      12.607   1.430  26.252  1.00 11.80           C  
ANISOU  155  C   ASP A  18     2381   1396    703      7     44    239       C  
ATOM    156  O   ASP A  18      12.964   2.232  27.122  1.00 12.68           O  
ANISOU  156  O   ASP A  18     2644   1597    576     54   -121    148       O  
ATOM    157  CB AASP A  18      13.583  -0.905  26.251  0.50 14.84           C  
ANISOU  157  CB AASP A  18     2650   1793   1193     39    108    394       C  
ATOM    158  CB BASP A  18      13.686  -0.806  26.234  0.50 15.11           C  
ANISOU  158  CB BASP A  18     2706   1731   1303     80     45    415       C  
ATOM    159  CG AASP A  18      13.614  -2.193  27.041  0.50 19.56           C  
ANISOU  159  CG AASP A  18     2995   1999   2436    -24    322    473       C  
ATOM    160  CG BASP A  18      14.000  -1.942  27.214  0.50 19.86           C  
ANISOU  160  CG BASP A  18     3091   2338   2114    293     25    529       C  
ATOM    161  OD1AASP A  18      12.834  -2.312  27.995  0.50 21.04           O  
ANISOU  161  OD1AASP A  18     4086   2208   1698    327    366    809       O  
ATOM    162  OD1BASP A  18      14.921  -1.843  28.057  0.50 23.66           O  
ANISOU  162  OD1BASP A  18     4031   2551   2407    534   -413    783       O  
ATOM    163  OD2AASP A  18      14.456  -3.055  26.750  0.50 22.13           O1-
ANISOU  163  OD2AASP A  18     3424   2308   2676    146    335    235       O1-
ATOM    164  OD2BASP A  18      13.350  -2.988  27.090  0.50 19.88           O1-
ANISOU  164  OD2BASP A  18     3619   1721   2212    325    819    955       O1-
ATOM    165  N   TYR A  19      12.400   1.822  25.004  1.00 10.73           N  
ANISOU  165  N   TYR A  19     2432   1235    410    -27    -69    216       N  
ATOM    166  CA  TYR A  19      12.433   3.241  24.646  1.00 10.44           C  
ANISOU  166  CA  TYR A  19     2257   1343    363    -64     -2    183       C  
ATOM    167  C   TYR A  19      11.427   4.049  25.450  1.00 10.49           C  
ANISOU  167  C   TYR A  19     2418   1166    400    -45     13    221       C  
ATOM    168  O   TYR A  19      11.774   5.104  26.031  1.00 11.09           O  
ANISOU  168  O   TYR A  19     2590   1328    295   -242    -85     82       O  
ATOM    169  CB  TYR A  19      12.208   3.410  23.123  1.00 10.35           C  
ANISOU  169  CB  TYR A  19     2294   1301    337      1      7    -55       C  
ATOM    170  CG  TYR A  19      11.996   4.856  22.720  1.00 10.11           C  
ANISOU  170  CG  TYR A  19     2283   1289    270    -87     76    -49       C  
ATOM    171  CD1 TYR A  19      13.066   5.736  22.628  1.00 10.39           C  
ANISOU  171  CD1 TYR A  19     2357   1322    265    -99     53     28       C  
ATOM    172  CD2 TYR A  19      10.714   5.358  22.495  1.00 11.06           C  
ANISOU  172  CD2 TYR A  19     2466   1480    256    -49     26     57       C  
ATOM    173  CE1 TYR A  19      12.862   7.084  22.328  1.00 10.14           C  
ANISOU  173  CE1 TYR A  19     2348   1148    356   -238    105     73       C  
ATOM    174  CE2 TYR A  19      10.516   6.703  22.184  1.00 10.66           C  
ANISOU  174  CE2 TYR A  19     2284   1398    368     91    -84      1       C  
ATOM    175  CZ  TYR A  19      11.586   7.549  22.096  1.00 10.54           C  
ANISOU  175  CZ  TYR A  19     2497   1240    268   -167    -36   -118       C  
ATOM    176  OH  TYR A  19      11.375   8.872  21.791  1.00 11.49           O  
ANISOU  176  OH  TYR A  19     2620   1204    541     50    -83    130       O  
ATOM    177  N   MET A  20      10.191   3.591  25.496  1.00 10.25           N  
ANISOU  177  N   MET A  20     2388   1190    316    -81     79     63       N  
ATOM    178  CA  MET A  20       9.182   4.310  26.225  1.00 10.47           C  
ANISOU  178  CA  MET A  20     2349   1371    258    -32     16     71       C  
ATOM    179  C   MET A  20       9.529   4.402  27.725  1.00 11.27           C  
ANISOU  179  C   MET A  20     2460   1354    467   -152     57    135       C  
ATOM    180  O   MET A  20       9.298   5.426  28.365  1.00 11.68           O  
ANISOU  180  O   MET A  20     2718   1397    321   -227     -1    -16       O  
ATOM    181  CB  MET A  20       7.788   3.693  26.047  1.00 10.79           C  
ANISOU  181  CB  MET A  20     2347   1495    257    -49     65     51       C  
ATOM    182  CG  MET A  20       7.193   3.944  24.686  1.00 11.80           C  
ANISOU  182  CG  MET A  20     2596   1570    318     13     40    162       C  
ATOM    183  SD  MET A  20       5.446   3.473  24.599  1.00 13.76           S  
ANISOU  183  SD  MET A  20     2553   2243    431    -64     -5     -9       S  
ATOM    184  CE  MET A  20       5.619   1.696  24.635  1.00 14.37           C  
ANISOU  184  CE  MET A  20     2616   2101    740   -303    -63   -226       C  
ATOM    185  N   LYS A  21      10.090   3.329  28.295  1.00 11.50           N  
ANISOU  185  N   LYS A  21     2621   1494    253   -168     22     -8       N  
ATOM    186  CA  LYS A  21      10.530   3.385  29.700  1.00 13.03           C  
ANISOU  186  CA  LYS A  21     2759   1886    305   -234     28    193       C  
ATOM    187  C   LYS A  21      11.567   4.475  29.865  1.00 13.48           C  
ANISOU  187  C   LYS A  21     2800   2030    292   -273   -167    128       C  
ATOM    188  O   LYS A  21      11.504   5.224  30.850  1.00 15.65           O  
ANISOU  188  O   LYS A  21     3242   2359    342   -445   -109    -89       O  
ATOM    189  CB  LYS A  21      11.151   2.052  30.142  1.00 14.47           C  
ANISOU  189  CB  LYS A  21     2880   2303    312    -99     -7    347       C  
ATOM    190  CG  LYS A  21      10.187   0.935  30.378  1.00 16.40           C  
ANISOU  190  CG  LYS A  21     3117   2357    757     67    -40    463       C  
ATOM    191  CD  LYS A  21      10.865  -0.265  30.980  1.00 19.47           C  
ANISOU  191  CD  LYS A  21     3474   2248   1676     38    -11   1018       C  
ATOM    192  CE  LYS A  21       9.901  -1.301  31.234  1.00 23.54           C  
ANISOU  192  CE  LYS A  21     3887   2688   2366     12   -256    960       C  
ATOM    193  NZ  LYS A  21      10.600  -2.408  31.872  1.00 27.40           N1+
ANISOU  193  NZ  LYS A  21     4672   2379   3359    163   -258   1317       N1+
ATOM    194  N   GLU A  22      12.523   4.583  28.957  1.00 14.08           N  
ANISOU  194  N   GLU A  22     2851   2140    359   -358   -165     56       N  
ATOM    195  CA  GLU A  22      13.580   5.561  29.050  1.00 15.23           C  
ANISOU  195  CA  GLU A  22     2993   2419    373   -420   -194     30       C  
ATOM    196  C   GLU A  22      13.002   6.960  28.993  1.00 14.67           C  
ANISOU  196  C   GLU A  22     3138   2121    312   -495   -110   -151       C  
ATOM    197  O   GLU A  22      13.446   7.881  29.686  1.00 17.43           O  
ANISOU  197  O   GLU A  22     3636   2497    488   -729   -291   -208       O  
ATOM    198  CB  GLU A  22      14.670   5.292  28.000  1.00 16.01           C  
ANISOU  198  CB  GLU A  22     2978   2412    693   -451   -123     75       C  
ATOM    199  CG  GLU A  22      16.055   5.731  28.251  1.00 19.25           C  
ANISOU  199  CG  GLU A  22     3191   2911   1212   -213   -380    -64       C  
ATOM    200  CD  GLU A  22      16.786   4.901  29.346  1.00 22.45           C  
ANISOU  200  CD  GLU A  22     3538   3089   1903   -362   -553    265       C  
ATOM    201  OE1 GLU A  22      16.247   3.898  29.849  1.00 24.82           O  
ANISOU  201  OE1 GLU A  22     3749   3390   2289   -449   -728    421       O  
ATOM    202  OE2 GLU A  22      17.949   5.241  29.693  1.00 25.26           O1-
ANISOU  202  OE2 GLU A  22     4225   3136   2235    -20  -1017    -97       O1-
ATOM    203  N   VAL A  23      11.977   7.149  28.147  1.00 13.91           N  
ANISOU  203  N   VAL A  23     3042   1885    355   -396    -42    -69       N  
ATOM    204  CA  VAL A  23      11.311   8.426  28.005  1.00 13.94           C  
ANISOU  204  CA  VAL A  23     3149   1872    274   -457      9   -162       C  
ATOM    205  C   VAL A  23      10.568   8.785  29.304  1.00 14.53           C  
ANISOU  205  C   VAL A  23     3335   1729    457   -478    151   -179       C  
ATOM    206  O   VAL A  23      10.423   9.942  29.589  1.00 17.08           O  
ANISOU  206  O   VAL A  23     4088   1712    691   -506    534   -282       O  
ATOM    207  CB  VAL A  23      10.383   8.353  26.762  1.00 14.93           C  
ANISOU  207  CB  VAL A  23     3299   1834    540   -339     86    -96       C  
ATOM    208  CG1 VAL A  23       9.428   9.509  26.742  1.00 15.61           C  
ANISOU  208  CG1 VAL A  23     3444   1484   1000   -121   -205     36       C  
ATOM    209  CG2 VAL A  23      11.211   8.333  25.497  1.00 15.37           C  
ANISOU  209  CG2 VAL A  23     3471   2011    356    -46    259     40       C  
ATOM    210  N   GLY A  24      10.078   7.809  30.026  1.00 13.42           N  
ANISOU  210  N   GLY A  24     3242   1578    279   -471    176    -66       N  
ATOM    211  CA  GLY A  24       9.322   8.018  31.271  1.00 14.36           C  
ANISOU  211  CA  GLY A  24     3123   1803    529   -391    189    -54       C  
ATOM    212  C   GLY A  24       7.840   7.674  31.143  1.00 13.58           C  
ANISOU  212  C   GLY A  24     2998   1643    517   -251    292    -46       C  
ATOM    213  O   GLY A  24       7.038   8.065  32.006  1.00 15.89           O  
ANISOU  213  O   GLY A  24     3172   2069    793   -375    313   -179       O  
ATOM    214  N   VAL A  25       7.448   6.907  30.126  1.00 12.33           N  
ANISOU  214  N   VAL A  25     2887   1240    556   -199     54     10       N  
ATOM    215  CA  VAL A  25       6.051   6.550  29.965  1.00 12.01           C  
ANISOU  215  CA  VAL A  25     2771   1321    470    -54      1     88       C  
ATOM    216  C   VAL A  25       5.663   5.510  31.018  1.00 11.97           C  
ANISOU  216  C   VAL A  25     2616   1521    411   -172    -65    -98       C  
ATOM    217  O   VAL A  25       6.417   4.557  31.260  1.00 13.04           O  
ANISOU  217  O   VAL A  25     2982   1637    335   -247   -125    216       O  
ATOM    218  CB  VAL A  25       5.832   5.972  28.552  1.00 11.89           C  
ANISOU  218  CB  VAL A  25     2723   1242    552     20    -34     12       C  
ATOM    219  CG1 VAL A  25       4.376   5.704  28.365  1.00 13.64           C  
ANISOU  219  CG1 VAL A  25     2832   1826    524   -155   -116    116       C  
ATOM    220  CG2 VAL A  25       6.399   6.929  27.439  1.00 13.83           C  
ANISOU  220  CG2 VAL A  25     3209   1573    472   -126    -76    429       C  
ATOM    221  N   GLY A  26       4.496   5.708  31.631  1.00 13.16           N  
ANISOU  221  N   GLY A  26     2771   1807    420   -174     40     67       N  
ATOM    222  CA  GLY A  26       4.044   4.797  32.660  1.00 13.49           C  
ANISOU  222  CA  GLY A  26     2627   2076    419   -300      1    -25       C  
ATOM    223  C   GLY A  26       3.516   3.477  32.141  1.00 12.70           C  
ANISOU  223  C   GLY A  26     2569   1912    344   -222     20     54       C  
ATOM    224  O   GLY A  26       3.271   3.306  30.962  1.00 13.37           O  
ANISOU  224  O   GLY A  26     2810   2012    256   -360    -51    -57       O  
ATOM    225  N   PHE A  27       3.312   2.539  33.052  1.00 12.98           N  
ANISOU  225  N   PHE A  27     2817   1842    270   -227   -127     27       N  
ATOM    226  CA  PHE A  27       3.019   1.164  32.678  1.00 12.73           C  
ANISOU  226  CA  PHE A  27     2579   1802    455   -245    -51    151       C  
ATOM    227  C   PHE A  27       1.808   1.033  31.769  1.00 12.01           C  
ANISOU  227  C   PHE A  27     2471   1573    518   -324      4    213       C  
ATOM    228  O   PHE A  27       1.891   0.417  30.706  1.00 12.82           O  
ANISOU  228  O   PHE A  27     2802   1756    314   -345    -97     70       O  
ATOM    229  CB  PHE A  27       2.776   0.349  33.985  1.00 13.49           C  
ANISOU  229  CB  PHE A  27     2697   1929    498   -243    -30    220       C  
ATOM    230  CG  PHE A  27       2.389  -1.077  33.702  1.00 14.03           C  
ANISOU  230  CG  PHE A  27     2922   1970    437   -309   -367    433       C  
ATOM    231  CD1 PHE A  27       3.341  -2.087  33.593  1.00 16.44           C  
ANISOU  231  CD1 PHE A  27     3412   2274    557   -459    -83    326       C  
ATOM    232  CD2 PHE A  27       1.083  -1.400  33.586  1.00 16.06           C  
ANISOU  232  CD2 PHE A  27     3110   2001    990   -225   -435    709       C  
ATOM    233  CE1 PHE A  27       2.945  -3.403  33.331  1.00 18.94           C  
ANISOU  233  CE1 PHE A  27     3672   2220   1301   -254     87    352       C  
ATOM    234  CE2 PHE A  27       0.688  -2.718  33.314  1.00 17.27           C  
ANISOU  234  CE2 PHE A  27     3445   2248    869   -608   -458    764       C  
ATOM    235  CZ  PHE A  27       1.610  -3.691  33.184  1.00 18.12           C  
ANISOU  235  CZ  PHE A  27     3786   2236    860   -448   -408    213       C  
ATOM    236  N   ALA A  28       0.652   1.549  32.171  1.00 12.82           N  
ANISOU  236  N   ALA A  28     2626   1785    459   -260     59     79       N  
ATOM    237  CA  ALA A  28      -0.589   1.308  31.402  1.00 13.32           C  
ANISOU  237  CA  ALA A  28     2548   1857    655   -219    -15    338       C  
ATOM    238  C   ALA A  28      -0.489   1.943  30.036  1.00 12.79           C  
ANISOU  238  C   ALA A  28     2548   1680    632   -248    -60    190       C  
ATOM    239  O   ALA A  28      -0.913   1.350  29.040  1.00 14.25           O  
ANISOU  239  O   ALA A  28     2749   1917    747   -382   -194     28       O  
ATOM    240  CB  ALA A  28      -1.792   1.838  32.162  1.00 15.40           C  
ANISOU  240  CB  ALA A  28     2641   2030   1178   -138    300    297       C  
ATOM    241  N   THR A  29       0.093   3.143  29.944  1.00 12.77           N  
ANISOU  241  N   THR A  29     2687   1707    456   -287    -82     83       N  
ATOM    242  CA  THR A  29       0.284   3.793  28.662  1.00 12.17           C  
ANISOU  242  CA  THR A  29     2455   1667    502   -141   -117    250       C  
ATOM    243  C   THR A  29       1.222   2.964  27.812  1.00 12.22           C  
ANISOU  243  C   THR A  29     2444   1641    555   -193    -13     48       C  
ATOM    244  O   THR A  29       0.959   2.789  26.597  1.00 12.78           O  
ANISOU  244  O   THR A  29     2705   1814    335   -224   -216     31       O  
ATOM    245  CB  THR A  29       0.743   5.234  28.835  1.00 13.70           C  
ANISOU  245  CB  THR A  29     2716   1578    909   -176    -57    314       C  
ATOM    246  CG2 THR A  29       0.916   5.905  27.494  1.00 15.00           C  
ANISOU  246  CG2 THR A  29     2760   1613   1326   -128   -141    568       C  
ATOM    247  OG1 THR A  29      -0.249   5.958  29.574  1.00 16.63           O  
ANISOU  247  OG1 THR A  29     3001   2012   1303    107      0    226       O  
ATOM    248  N   ARG A  30       2.326   2.457  28.347  1.00 11.99           N  
ANISOU  248  N   ARG A  30     2545   1746    264   -227   -112    101       N  
ATOM    249  CA  ARG A  30       3.228   1.629  27.543  1.00 11.70           C  
ANISOU  249  CA  ARG A  30     2407   1762    275   -162     90    159       C  
ATOM    250  C   ARG A  30       2.554   0.428  27.006  1.00 11.96           C  
ANISOU  250  C   ARG A  30     2337   1906    300   -189    -57    278       C  
ATOM    251  O   ARG A  30       2.775   0.057  25.849  1.00 12.84           O  
ANISOU  251  O   ARG A  30     2500   2105    272   -180      0    188       O  
ATOM    252  CB  ARG A  30       4.495   1.133  28.314  1.00 12.50           C  
ANISOU  252  CB  ARG A  30     2638   1810    299   -254    -41    260       C  
ATOM    253  CG  ARG A  30       5.449   2.228  28.696  1.00 12.52           C  
ANISOU  253  CG  ARG A  30     2727   1630    396    -79      7    171       C  
ATOM    254  CD  ARG A  30       6.827   1.679  28.975  1.00 11.86           C  
ANISOU  254  CD  ARG A  30     2564   1680    259   -144      2     91       C  
ATOM    255  NE  ARG A  30       6.764   0.510  29.877  1.00 12.22           N  
ANISOU  255  NE  ARG A  30     2717   1577    348    -97     37     28       N  
ATOM    256  CZ  ARG A  30       6.631   0.549  31.184  1.00 12.31           C  
ANISOU  256  CZ  ARG A  30     2629   1491    555   -109     13    214       C  
ATOM    257  NH1 ARG A  30       6.508   1.701  31.846  1.00 12.80           N1+
ANISOU  257  NH1 ARG A  30     3017   1507    336   -170    -86    224       N1+
ATOM    258  NH2 ARG A  30       6.588  -0.596  31.866  1.00 13.87           N  
ANISOU  258  NH2 ARG A  30     3270   1697    300     32    147     95       N  
ATOM    259  N   LYS A  31       1.754  -0.250  27.810  1.00 12.58           N  
ANISOU  259  N   LYS A  31     2537   1942    300   -264      9     94       N  
ATOM    260  CA  LYS A  31       1.110  -1.472  27.353  1.00 12.96           C  
ANISOU  260  CA  LYS A  31     2578   1774    570   -193      0    -49       C  
ATOM    261  C   LYS A  31       0.150  -1.187  26.198  1.00 12.97           C  
ANISOU  261  C   LYS A  31     2406   2031    489   -175    -62   -100       C  
ATOM    262  O   LYS A  31       0.150  -1.905  25.177  1.00 14.42           O  
ANISOU  262  O   LYS A  31     2657   2164    658   -122    -31   -333       O  
ATOM    263  CB  LYS A  31       0.358  -2.184  28.486  1.00 14.24           C  
ANISOU  263  CB  LYS A  31     2898   1814    698   -273   -103    -13       C  
ATOM    264  CG  LYS A  31       1.294  -2.725  29.572  1.00 17.39           C  
ANISOU  264  CG  LYS A  31     3240   2388    980   -371   -110    414       C  
ATOM    265  CD  LYS A  31       2.302  -3.755  29.049  1.00 22.75           C  
ANISOU  265  CD  LYS A  31     3871   3068   1703    279   -306    625       C  
ATOM    266  CE  LYS A  31       3.511  -4.034  29.929  1.00 26.27           C  
ANISOU  266  CE  LYS A  31     3930   3910   2141    387   -167    -69       C  
ATOM    267  NZ  LYS A  31       4.716  -4.348  29.079  1.00 28.30           N1+
ANISOU  267  NZ  LYS A  31     4070   4126   2557    615   -115    -32       N1+
ATOM    268  N   VAL A  32      -0.676  -0.175  26.325  1.00 12.62           N  
ANISOU  268  N   VAL A  32     2400   2011    381   -128    -67   -176       N  
ATOM    269  CA AVAL A  32      -1.652   0.161  25.269  0.50 13.49           C  
ANISOU  269  CA AVAL A  32     2415   2108    601   -137    -80   -256       C  
ATOM    270  CA BVAL A  32      -1.641   0.092  25.241  0.50 13.53           C  
ANISOU  270  CA BVAL A  32     2410   2150    578   -152    -97   -256       C  
ATOM    271  C   VAL A  32      -0.964   0.765  24.058  1.00 12.95           C  
ANISOU  271  C   VAL A  32     2273   2140    507   -178   -111   -152       C  
ATOM    272  O   VAL A  32      -1.309   0.476  22.909  1.00 13.63           O  
ANISOU  272  O   VAL A  32     2350   2409    417   -246    -50   -292       O  
ATOM    273  CB AVAL A  32      -2.735   1.158  25.852  0.50 13.38           C  
ANISOU  273  CB AVAL A  32     2437   2093    554    -87    -30   -426       C  
ATOM    274  CB BVAL A  32      -2.899   0.882  25.781  0.50 13.95           C  
ANISOU  274  CB BVAL A  32     2421   2290    588    -96    -24   -253       C  
ATOM    275  CG1AVAL A  32      -3.683   1.596  24.756  0.50 13.72           C  
ANISOU  275  CG1AVAL A  32     2288   2109    814     27   -134   -137       C  
ATOM    276  CG1BVAL A  32      -3.686   0.015  26.784  0.50 14.03           C  
ANISOU  276  CG1BVAL A  32     2310   2326    692   -326   -109   -200       C  
ATOM    277  CG2AVAL A  32      -3.519   0.518  27.035  0.50 15.00           C  
ANISOU  277  CG2AVAL A  32     2680   2209    808   -331    104   -273       C  
ATOM    278  CG2BVAL A  32      -2.484   2.236  26.353  0.50 15.57           C  
ANISOU  278  CG2BVAL A  32     2705   2139   1069     26     75   -274       C  
ATOM    279  N   ALA A  33       0.025   1.621  24.274  1.00 12.99           N  
ANISOU  279  N   ALA A  33     2418   2150    367   -106   -202    -79       N  
ATOM    280  CA  ALA A  33       0.724   2.241  23.145  1.00 13.95           C  
ANISOU  280  CA  ALA A  33     2526   2335    437   -130   -127    253       C  
ATOM    281  C   ALA A  33       1.503   1.183  22.395  1.00 13.95           C  
ANISOU  281  C   ALA A  33     2435   2476    386    -99   -114    284       C  
ATOM    282  O   ALA A  33       1.617   1.265  21.168  1.00 14.87           O  
ANISOU  282  O   ALA A  33     2682   2631    334   -200     18    435       O  
ATOM    283  CB  ALA A  33       1.627   3.373  23.627  1.00 14.55           C  
ANISOU  283  CB  ALA A  33     2483   2415    628   -221    -61    269       C  
ATOM    284  N   GLY A  34       2.070   0.192  23.064  1.00 14.21           N  
ANISOU  284  N   GLY A  34     2506   2529    362     98     -9    247       N  
ATOM    285  CA  GLY A  34       2.851  -0.833  22.415  1.00 14.96           C  
ANISOU  285  CA  GLY A  34     2406   2641    636    212    -11    247       C  
ATOM    286  C   GLY A  34       2.044  -1.746  21.505  1.00 14.74           C  
ANISOU  286  C   GLY A  34     2516   2570    514    200     55    250       C  
ATOM    287  O   GLY A  34       2.600  -2.272  20.560  1.00 16.58           O  
ANISOU  287  O   GLY A  34     2547   2980    773    235    284     51       O  
ATOM    288  N   MET A  35       0.745  -1.910  21.760  1.00 13.97           N  
ANISOU  288  N   MET A  35     2539   2179    587    119    324    446       N  
ATOM    289  CA  MET A  35      -0.124  -2.725  20.910  1.00 14.13           C  
ANISOU  289  CA  MET A  35     2542   2007    819     40    299    509       C  
ATOM    290  C   MET A  35      -0.450  -2.053  19.558  1.00 13.25           C  
ANISOU  290  C   MET A  35     2519   1789    725    -10    268    551       C  
ATOM    291  O   MET A  35      -0.730  -2.729  18.547  1.00 15.27           O  
ANISOU  291  O   MET A  35     2717   1878   1206   -166     55    434       O  
ATOM    292  CB  MET A  35      -1.434  -3.043  21.584  1.00 14.86           C  
ANISOU  292  CB  MET A  35     2650   1709   1287     81    448    575       C  
ATOM    293  CG  MET A  35      -1.304  -3.950  22.773  1.00 14.18           C  
ANISOU  293  CG  MET A  35     3183   1578    627   -211    563    129       C  
ATOM    294  SD  MET A  35      -0.669  -5.547  22.430  1.00 14.44           S  
ANISOU  294  SD  MET A  35     3065   1555    865     49    224    230       S  
ATOM    295  CE  MET A  35      -1.749  -6.264  21.252  1.00 20.72           C  
ANISOU  295  CE  MET A  35     4571   2249   1050    -61   -436    524       C  
ATOM    296  N   ALA A  36      -0.390  -0.727  19.511  1.00 13.36           N  
ANISOU  296  N   ALA A  36     2392   1789    894    -80     92    524       N  
ATOM    297  CA  ALA A  36      -0.896  -0.027  18.347  1.00 13.21           C  
ANISOU  297  CA  ALA A  36     2339   1900    780    -21    154    417       C  
ATOM    298  C   ALA A  36      -0.095  -0.295  17.102  1.00 12.35           C  
ANISOU  298  C   ALA A  36     2362   1634    695   -233     51    277       C  
ATOM    299  O   ALA A  36       1.112  -0.426  17.140  1.00 13.23           O  
ANISOU  299  O   ALA A  36     2352   2035    639   -134     22    288       O  
ATOM    300  CB  ALA A  36      -0.911   1.473  18.649  1.00 14.87           C  
ANISOU  300  CB  ALA A  36     2834   1934    882    147    259    329       C  
ATOM    301  N   LYS A  37      -0.809  -0.356  16.005  1.00 13.09           N  
ANISOU  301  N   LYS A  37     2407   1757    807   -290    -31    305       N  
ATOM    302  CA  LYS A  37      -0.252  -0.521  14.676  1.00 13.23           C  
ANISOU  302  CA  LYS A  37     2585   1640    801   -274     46    115       C  
ATOM    303  C   LYS A  37      -0.730   0.663  13.852  1.00 12.35           C  
ANISOU  303  C   LYS A  37     2523   1714    455   -321    124     53       C  
ATOM    304  O   LYS A  37      -1.652   0.557  13.042  1.00 14.00           O  
ANISOU  304  O   LYS A  37     2549   2092    675   -454   -121    262       O  
ATOM    305  CB  LYS A  37      -0.644  -1.856  14.049  1.00 15.55           C  
ANISOU  305  CB  LYS A  37     2869   1931   1105   -285     80    104       C  
ATOM    306  CG  LYS A  37      -0.037  -3.066  14.748  1.00 19.68           C  
ANISOU  306  CG  LYS A  37     3155   1978   2345   -363    -76    188       C  
ATOM    307  CD  LYS A  37       1.428  -3.201  14.383  1.00 21.59           C  
ANISOU  307  CD  LYS A  37     3429   2854   1918     16   -100    411       C  
ATOM    308  CE  LYS A  37       2.008  -4.530  14.735  1.00 24.71           C  
ANISOU  308  CE  LYS A  37     3933   3160   2293     63    -26    345       C  
ATOM    309  NZ  LYS A  37       1.812  -4.835  16.144  1.00 26.50           N1+
ANISOU  309  NZ  LYS A  37     4678   2954   2436    383    149    748       N1+
ATOM    310  N   PRO A  38      -0.154   1.835  14.037  1.00 12.03           N  
ANISOU  310  N   PRO A  38     2459   1568    541   -189     69     59       N  
ATOM    311  CA  PRO A  38      -0.699   3.027  13.435  1.00 12.50           C  
ANISOU  311  CA  PRO A  38     2630   1613    506   -118    217    145       C  
ATOM    312  C   PRO A  38      -0.517   3.103  11.943  1.00 12.59           C  
ANISOU  312  C   PRO A  38     2540   1470    770   -160    353     32       C  
ATOM    313  O   PRO A  38       0.383   2.496  11.358  1.00 13.09           O  
ANISOU  313  O   PRO A  38     2797   1630    544   -175    373    143       O  
ATOM    314  CB  PRO A  38       0.119   4.159  14.048  1.00 15.08           C  
ANISOU  314  CB  PRO A  38     2974   1842    912    -64    177    -13       C  
ATOM    315  CG  PRO A  38       1.263   3.493  14.682  1.00 18.40           C  
ANISOU  315  CG  PRO A  38     2877   2189   1925   -552   -182    152       C  
ATOM    316  CD  PRO A  38       0.917   2.149  14.985  1.00 12.61           C  
ANISOU  316  CD  PRO A  38     2472   1660    658   -289     19   -131       C  
ATOM    317  N   ASN A  39      -1.376   3.915  11.356  1.00 12.33           N  
ANISOU  317  N   ASN A  39     2772   1498    413    -82    362     98       N  
ATOM    318  CA  ASN A  39      -1.157   4.434  10.016  1.00 13.93           C  
ANISOU  318  CA  ASN A  39     3136   1490    666    -91    407     99       C  
ATOM    319  C   ASN A  39      -0.620   5.819  10.120  1.00 14.61           C  
ANISOU  319  C   ASN A  39     3433   1405    711   -143    571    -86       C  
ATOM    320  O   ASN A  39      -1.069   6.623  10.906  1.00 19.55           O  
ANISOU  320  O   ASN A  39     4155   1620   1650   -483   1386   -328       O  
ATOM    321  CB  ASN A  39      -2.453   4.428   9.266  1.00 16.71           C  
ANISOU  321  CB  ASN A  39     3520   1876    953     51    -20    242       C  
ATOM    322  CG  ASN A  39      -2.657   3.157   8.506  1.00 19.85           C  
ANISOU  322  CG  ASN A  39     3635   2239   1665    -34   -119    234       C  
ATOM    323  ND2 ASN A  39      -3.140   3.278   7.273  1.00 27.04           N  
ANISOU  323  ND2 ASN A  39     4488   3835   1949    260   -295   -204       N  
ATOM    324  OD1 ASN A  39      -2.347   2.071   9.023  1.00 26.09           O  
ANISOU  324  OD1 ASN A  39     5225   2721   1963   -145   -802    258       O  
ATOM    325  N   MET A  40       0.388   6.105   9.325  1.00 13.65           N  
ANISOU  325  N   MET A  40     3323   1274    586   -157    511    109       N  
ATOM    326  CA  MET A  40       0.983   7.404   9.324  1.00 13.42           C  
ANISOU  326  CA  MET A  40     3103   1348    648    -98    380     -8       C  
ATOM    327  C   MET A  40       0.822   7.991   7.932  1.00 12.45           C  
ANISOU  327  C   MET A  40     2912   1311    504    -91    432    137       C  
ATOM    328  O   MET A  40       1.153   7.364   6.944  1.00 13.84           O  
ANISOU  328  O   MET A  40     3407   1293    556    156    482    147       O  
ATOM    329  CB  MET A  40       2.453   7.261   9.702  1.00 14.63           C  
ANISOU  329  CB  MET A  40     3339   1469    750    -45    268     -2       C  
ATOM    330  CG  MET A  40       3.242   8.567   9.584  1.00 15.43           C  
ANISOU  330  CG  MET A  40     3414   1299   1147     47      1    201       C  
ATOM    331  SD  MET A  40       4.897   8.428  10.218  1.00 17.10           S  
ANISOU  331  SD  MET A  40     3724   1585   1187    -90   -232    -63       S  
ATOM    332  CE  MET A  40       5.583   7.094   9.262  1.00 19.34           C  
ANISOU  332  CE  MET A  40     3726   2671    949   -190    196     38       C  
ATOM    333  N   ILE A  41       0.292   9.200   7.871  1.00 12.38           N  
ANISOU  333  N   ILE A  41     2773   1308    621    -84    272    -40       N  
ATOM    334  CA  ILE A  41       0.072   9.899   6.623  1.00 11.80           C  
ANISOU  334  CA  ILE A  41     2701   1313    467   -172    132     -3       C  
ATOM    335  C   ILE A  41       0.952  11.115   6.620  1.00 10.73           C  
ANISOU  335  C   ILE A  41     2639   1031    406   -132     99     -4       C  
ATOM    336  O   ILE A  41       0.860  11.987   7.511  1.00 12.18           O  
ANISOU  336  O   ILE A  41     2929   1194    503   -257    229    -47       O  
ATOM    337  CB  ILE A  41      -1.410  10.356   6.479  1.00 14.32           C  
ANISOU  337  CB  ILE A  41     2725   1579   1134   -181    128   -165       C  
ATOM    338  CG1 ILE A  41      -2.367   9.147   6.596  1.00 18.60           C  
ANISOU  338  CG1 ILE A  41     2990   2063   2012   -360    205   -408       C  
ATOM    339  CG2 ILE A  41      -1.634  11.092   5.129  1.00 18.36           C  
ANISOU  339  CG2 ILE A  41     3168   2285   1524   -191   -278    -50       C  
ATOM    340  CD1 ILE A  41      -3.838   9.601   6.651  1.00 23.91           C  
ANISOU  340  CD1 ILE A  41     3215   2862   3005   -460   -124   -404       C  
ATOM    341  N   ILE A  42       1.821  11.205   5.622  1.00 10.51           N  
ANISOU  341  N   ILE A  42     2642   1090    260   -126     97    -17       N  
ATOM    342  CA  ILE A  42       2.776  12.317   5.496  1.00 10.38           C  
ANISOU  342  CA  ILE A  42     2565   1125    254    -12     45     -5       C  
ATOM    343  C   ILE A  42       2.428  13.057   4.235  1.00 10.50           C  
ANISOU  343  C   ILE A  42     2457   1275    258    -74   -104      5       C  
ATOM    344  O   ILE A  42       2.271  12.467   3.168  1.00 11.34           O  
ANISOU  344  O   ILE A  42     2858   1166    284    -87   -178     13       O  
ATOM    345  CB  ILE A  42       4.225  11.813   5.485  1.00 10.74           C  
ANISOU  345  CB  ILE A  42     2603   1220    255    -62     76    -12       C  
ATOM    346  CG1 ILE A  42       4.521  11.039   6.778  1.00 11.28           C  
ANISOU  346  CG1 ILE A  42     2727   1295    264    -30    -75     94       C  
ATOM    347  CG2 ILE A  42       5.199  12.955   5.295  1.00 11.26           C  
ANISOU  347  CG2 ILE A  42     2565   1285    426    -93     -4     52       C  
ATOM    348  CD1 ILE A  42       5.930  10.440   6.831  1.00 13.68           C  
ANISOU  348  CD1 ILE A  42     3063   1536    597    318   -223     79       C  
ATOM    349  N   SER A  43       2.274  14.378   4.359  1.00 10.64           N  
ANISOU  349  N   SER A  43     2668   1099    274     -7   -221     23       N  
ATOM    350  CA  SER A  43       1.968  15.201   3.209  1.00 11.09           C  
ANISOU  350  CA  SER A  43     2612   1203    397     -3   -184     44       C  
ATOM    351  C   SER A  43       2.746  16.492   3.287  1.00 10.81           C  
ANISOU  351  C   SER A  43     2791   1055    259    -12   -115    -23       C  
ATOM    352  O   SER A  43       3.227  16.891   4.359  1.00 11.20           O  
ANISOU  352  O   SER A  43     2795   1202    258     16   -103    -28       O  
ATOM    353  CB  SER A  43       0.479  15.473   3.171  1.00 13.33           C  
ANISOU  353  CB  SER A  43     2884   1292    886    -13   -293    296       C  
ATOM    354  OG  SER A  43       0.015  16.126   4.312  1.00 16.35           O  
ANISOU  354  OG  SER A  43     3014   1920   1277    202   -151    232       O  
ATOM    355  N   VAL A  44       2.869  17.136   2.135  1.00 10.99           N  
ANISOU  355  N   VAL A  44     2814   1086    272    -67   -148     98       N  
ATOM    356  CA  VAL A  44       3.574  18.395   2.035  1.00 11.44           C  
ANISOU  356  CA  VAL A  44     2914   1127    304    -60   -235    167       C  
ATOM    357  C   VAL A  44       2.737  19.372   1.244  1.00 11.86           C  
ANISOU  357  C   VAL A  44     3004   1232    270    -20   -138     98       C  
ATOM    358  O   VAL A  44       2.152  19.010   0.210  1.00 15.69           O  
ANISOU  358  O   VAL A  44     4159   1402    399     17   -743     69       O  
ATOM    359  CB  VAL A  44       4.963  18.251   1.369  1.00 13.36           C  
ANISOU  359  CB  VAL A  44     2998   1386    691    -54   -264     54       C  
ATOM    360  CG1 VAL A  44       5.663  19.584   1.298  1.00 19.69           C  
ANISOU  360  CG1 VAL A  44     3283   1716   2481   -356     11    366       C  
ATOM    361  CG2 VAL A  44       5.799  17.240   2.082  1.00 16.18           C  
ANISOU  361  CG2 VAL A  44     3003   1956   1187    -67   -357     -9       C  
ATOM    362  N   ASN A  45       2.686  20.600   1.695  1.00 11.46           N  
ANISOU  362  N   ASN A  45     2843   1240    269    -45   -201     21       N  
ATOM    363  CA  ASN A  45       1.982  21.684   1.014  1.00 11.12           C  
ANISOU  363  CA  ASN A  45     2714   1226    285    -88   -271     28       C  
ATOM    364  C   ASN A  45       2.850  22.908   1.170  1.00 11.76           C  
ANISOU  364  C   ASN A  45     2781   1319    368     -6   -136    225       C  
ATOM    365  O   ASN A  45       2.956  23.496   2.241  1.00 11.55           O  
ANISOU  365  O   ASN A  45     2727   1332    329    -43   -210     76       O  
ATOM    366  CB  ASN A  45       0.589  21.821   1.589  1.00 12.16           C  
ANISOU  366  CB  ASN A  45     2707   1347    563    -68   -245     89       C  
ATOM    367  CG  ASN A  45      -0.276  22.849   0.913  1.00 12.72           C  
ANISOU  367  CG  ASN A  45     2661   1710    461    -85   -313     52       C  
ATOM    368  ND2 ASN A  45       0.329  23.893   0.416  1.00 12.39           N  
ANISOU  368  ND2 ASN A  45     2626   1496    584   -258   -428    301       N  
ATOM    369  OD1 ASN A  45      -1.533  22.657   0.829  1.00 14.61           O  
ANISOU  369  OD1 ASN A  45     2757   1877    914   -269   -142   -111       O  
ATOM    370  N   GLY A  46       3.513  23.267   0.091  1.00 12.82           N  
ANISOU  370  N   GLY A  46     3113   1481    275   -257   -129    149       N  
ATOM    371  CA  GLY A  46       4.466  24.358   0.166  1.00 13.60           C  
ANISOU  371  CA  GLY A  46     2903   1673    590   -246    -53    274       C  
ATOM    372  C   GLY A  46       5.601  24.018   1.117  1.00 13.46           C  
ANISOU  372  C   GLY A  46     2755   1752    605   -259     76    293       C  
ATOM    373  O   GLY A  46       6.216  22.956   1.008  1.00 15.61           O  
ANISOU  373  O   GLY A  46     2943   1973   1015    -72     64     47       O  
ATOM    374  N   ASP A  47       5.841  24.878   2.094  1.00 13.22           N  
ANISOU  374  N   ASP A  47     2791   1610    621   -258    -51    270       N  
ATOM    375  CA  ASP A  47       6.874  24.640   3.104  1.00 13.92           C  
ANISOU  375  CA  ASP A  47     2668   1795    827   -190    -52    342       C  
ATOM    376  C   ASP A  47       6.381  23.802   4.278  1.00 11.72           C  
ANISOU  376  C   ASP A  47     2491   1431    528    -50    -45    191       C  
ATOM    377  O   ASP A  47       7.183  23.495   5.165  1.00 12.76           O  
ANISOU  377  O   ASP A  47     2432   1791    622    -56    -75    198       O  
ATOM    378  CB  ASP A  47       7.405  25.991   3.620  1.00 15.29           C  
ANISOU  378  CB  ASP A  47     2842   1985    982   -375   -222    376       C  
ATOM    379  CG  ASP A  47       8.104  26.788   2.587  1.00 21.56           C  
ANISOU  379  CG  ASP A  47     3353   2667   2170   -504   -186    415       C  
ATOM    380  OD1 ASP A  47       8.684  26.187   1.675  1.00 27.03           O  
ANISOU  380  OD1 ASP A  47     3831   4239   2197  -1028    814    730       O  
ATOM    381  OD2 ASP A  47       8.102  28.027   2.730  1.00 28.42           O1-
ANISOU  381  OD2 ASP A  47     4802   2998   2995   -840   -554    792       O1-
ATOM    382  N   VAL A  48       5.098  23.537   4.319  1.00 10.38           N  
ANISOU  382  N   VAL A  48     2376   1257    311    -42    -88    235       N  
ATOM    383  CA  VAL A  48       4.520  22.886   5.503  1.00  9.87           C  
ANISOU  383  CA  VAL A  48     2284   1194    271    -36    -46    127       C  
ATOM    384  C   VAL A  48       4.420  21.394   5.305  1.00  9.73           C  
ANISOU  384  C   VAL A  48     2243   1185    267    -70   -162     36       C  
ATOM    385  O   VAL A  48       3.766  20.911   4.375  1.00 11.03           O  
ANISOU  385  O   VAL A  48     2568   1302    317    -46   -267     83       O  
ATOM    386  CB  VAL A  48       3.129  23.433   5.798  1.00 11.16           C  
ANISOU  386  CB  VAL A  48     2382   1443    412      0   -110    138       C  
ATOM    387  CG1 VAL A  48       2.589  22.794   7.103  1.00 12.50           C  
ANISOU  387  CG1 VAL A  48     2625   1560    562    -54    167    270       C  
ATOM    388  CG2 VAL A  48       3.194  24.988   6.008  1.00 13.64           C  
ANISOU  388  CG2 VAL A  48     2904   1263   1015    204     94    139       C  
ATOM    389  N   ILE A  49       5.034  20.639   6.223  1.00  9.40           N  
ANISOU  389  N   ILE A  49     2269   1036    265   -151   -113     75       N  
ATOM    390  CA  ILE A  49       4.950  19.192   6.253  1.00  9.38           C  
ANISOU  390  CA  ILE A  49     2154   1153    255   -145    -47    -29       C  
ATOM    391  C   ILE A  49       3.947  18.818   7.331  1.00  9.30           C  
ANISOU  391  C   ILE A  49     2182   1096    254    -70    -42     26       C  
ATOM    392  O   ILE A  49       3.997  19.404   8.450  1.00  9.68           O  
ANISOU  392  O   ILE A  49     2247   1170    261   -141    -42    -78       O  
ATOM    393  CB  ILE A  49       6.320  18.585   6.523  1.00 10.41           C  
ANISOU  393  CB  ILE A  49     2357   1337    261    -72     86    -69       C  
ATOM    394  CG1 ILE A  49       7.337  19.004   5.475  1.00 11.25           C  
ANISOU  394  CG1 ILE A  49     2347   1554    372    -67    196    -51       C  
ATOM    395  CG2 ILE A  49       6.271  17.053   6.629  1.00 11.59           C  
ANISOU  395  CG2 ILE A  49     2550   1193    658     92   -160    -65       C  
ATOM    396  CD1 ILE A  49       8.788  18.773   5.893  1.00 16.87           C  
ANISOU  396  CD1 ILE A  49     2642   2717   1050    -46    123    248       C  
ATOM    397  N   THR A  50       3.095  17.861   7.049  1.00  9.55           N  
ANISOU  397  N   THR A  50     2178   1193    255   -133      8    -47       N  
ATOM    398  CA  THR A  50       2.175  17.332   8.062  1.00  9.79           C  
ANISOU  398  CA  THR A  50     2233   1224    263   -189    121     35       C  
ATOM    399  C   THR A  50       2.417  15.845   8.197  1.00  9.46           C  
ANISOU  399  C   THR A  50     2080   1258    253   -142      7    -25       C  
ATOM    400  O   THR A  50       2.531  15.087   7.218  1.00 10.55           O  
ANISOU  400  O   THR A  50     2613   1140    254   -162    -24     23       O  
ATOM    401  CB  THR A  50       0.690  17.591   7.659  1.00 10.58           C  
ANISOU  401  CB  THR A  50     2348   1262    408   -298      5    -94       C  
ATOM    402  CG2 THR A  50      -0.298  17.046   8.633  1.00 12.81           C  
ANISOU  402  CG2 THR A  50     2510   1566    788   -368    194     26       C  
ATOM    403  OG1 THR A  50       0.499  18.994   7.533  1.00 11.69           O  
ANISOU  403  OG1 THR A  50     2351   1480    609    -48    -29     31       O  
ATOM    404  N   ILE A  51       2.528  15.395   9.465  1.00  9.56           N  
ANISOU  404  N   ILE A  51     2270   1105    256   -113      4     48       N  
ATOM    405  CA  ILE A  51       2.617  13.991   9.810  1.00  9.90           C  
ANISOU  405  CA  ILE A  51     2354   1139    269   -191     29    -36       C  
ATOM    406  C   ILE A  51       1.428  13.665  10.724  1.00 10.10           C  
ANISOU  406  C   ILE A  51     2349   1222    265   -166     90     81       C  
ATOM    407  O   ILE A  51       1.346  14.194  11.843  1.00 11.30           O  
ANISOU  407  O   ILE A  51     2684   1349    259    -40     55    -24       O  
ATOM    408  CB  ILE A  51       3.942  13.622  10.507  1.00  9.83           C  
ANISOU  408  CB  ILE A  51     2334   1139    260   -156     57    -75       C  
ATOM    409  CG1 ILE A  51       5.130  13.995   9.615  1.00 11.15           C  
ANISOU  409  CG1 ILE A  51     2376   1324    535   -124    141   -214       C  
ATOM    410  CG2 ILE A  51       3.955  12.168  10.906  1.00 12.16           C  
ANISOU  410  CG2 ILE A  51     2765   1126    727     22     98    106       C  
ATOM    411  CD1 ILE A  51       6.467  13.736  10.226  1.00 13.59           C  
ANISOU  411  CD1 ILE A  51     2493   1801    870     59    -59    -91       C  
ATOM    412  N   LYS A  52       0.508  12.854  10.244  1.00 10.57           N  
ANISOU  412  N   LYS A  52     2427   1286    304   -223    130    -16       N  
ATOM    413  CA  LYS A  52      -0.641  12.390  10.989  1.00 12.22           C  
ANISOU  413  CA  LYS A  52     2617   1332    693   -195    309    -64       C  
ATOM    414  C   LYS A  52      -0.438  10.941  11.350  1.00 12.71           C  
ANISOU  414  C   LYS A  52     2725   1397    706   -288    373   -251       C  
ATOM    415  O   LYS A  52      -0.054  10.145  10.506  1.00 15.39           O  
ANISOU  415  O   LYS A  52     3700   1270    878   -272    737    -33       O  
ATOM    416  CB  LYS A  52      -1.894  12.529  10.138  1.00 15.27           C  
ANISOU  416  CB  LYS A  52     2543   2072   1187   -149    341   -326       C  
ATOM    417  CG  LYS A  52      -3.232  12.322  10.743  1.00 20.28           C  
ANISOU  417  CG  LYS A  52     3220   2642   1842   -369    104    299       C  
ATOM    418  CD  LYS A  52      -4.297  12.670   9.705  1.00 26.04           C  
ANISOU  418  CD  LYS A  52     3465   3717   2709   -150   -241    113       C  
ATOM    419  CE  LYS A  52      -4.211  14.142   9.323  1.00 32.14           C  
ANISOU  419  CE  LYS A  52     4015   4129   4068   -310   -430    -67       C  
ATOM    420  NZ  LYS A  52      -3.347  14.503   8.155  1.00 35.98           N1+
ANISOU  420  NZ  LYS A  52     4349   4783   4537   -245   -270   -324       N1+
ATOM    421  N   SER A  53      -0.767  10.597  12.579  1.00 12.19           N  
ANISOU  421  N   SER A  53     2761   1288    582   -258    315   -108       N  
ATOM    422  CA  SER A  53      -0.774   9.201  13.040  1.00 12.51           C  
ANISOU  422  CA  SER A  53     2709   1400    642   -226    316     49       C  
ATOM    423  C   SER A  53      -2.209   8.853  13.453  1.00 12.23           C  
ANISOU  423  C   SER A  53     2680   1519    446   -328    330    -48       C  
ATOM    424  O   SER A  53      -2.772   9.518  14.298  1.00 14.50           O  
ANISOU  424  O   SER A  53     3030   1630    847   -440    522   -178       O  
ATOM    425  CB  SER A  53       0.154   9.024  14.213  1.00 14.18           C  
ANISOU  425  CB  SER A  53     2745   1635   1006   -203    301     15       C  
ATOM    426  OG  SER A  53       0.188   7.670  14.671  1.00 16.98           O  
ANISOU  426  OG  SER A  53     3485   1793   1173   -227    109    332       O  
ATOM    427  N   GLU A  54      -2.748   7.843  12.783  1.00 13.04           N  
ANISOU  427  N   GLU A  54     2720   1694    540   -363    248    -24       N  
ATOM    428  CA  GLU A  54      -4.066   7.326  13.074  1.00 14.03           C  
ANISOU  428  CA  GLU A  54     2742   1764    825   -353    171     18       C  
ATOM    429  C   GLU A  54      -3.865   6.014  13.803  1.00 13.56           C  
ANISOU  429  C   GLU A  54     2630   1776    744   -294    327     86       C  
ATOM    430  O   GLU A  54      -3.309   5.070  13.221  1.00 13.62           O  
ANISOU  430  O   GLU A  54     2828   1756    591   -165    261    112       O  
ATOM    431  CB  GLU A  54      -4.848   7.099  11.804  1.00 16.04           C  
ANISOU  431  CB  GLU A  54     2949   1918   1225   -373     47    130       C  
ATOM    432  CG  GLU A  54      -5.049   8.356  10.985  1.00 21.64           C  
ANISOU  432  CG  GLU A  54     3500   2526   2194   -377     75    374       C  
ATOM    433  CD  GLU A  54      -5.991   8.170   9.872  1.00 27.44           C  
ANISOU  433  CD  GLU A  54     4028   3383   3012   -169   -407    423       C  
ATOM    434  OE1 GLU A  54      -5.846   7.171   9.169  1.00 29.86           O  
ANISOU  434  OE1 GLU A  54     4922   4364   2057   -449  -1033      4       O  
ATOM    435  OE2 GLU A  54      -6.856   9.046   9.676  1.00 35.75           O1-
ANISOU  435  OE2 GLU A  54     4641   4534   4407    232   -391    267       O1-
ATOM    436  N  ASER A  55      -4.334   5.863  15.042  0.50 15.07           N  
ANISOU  436  N  ASER A  55     2719   2066    940   -154    327    139       N  
ATOM    437  N  BSER A  55      -4.268   6.043  15.053  0.50 13.51           N  
ANISOU  437  N  BSER A  55     2705   1784    643    -86    249    154       N  
ATOM    438  CA ASER A  55      -4.315   4.516  15.684  0.50 15.37           C  
ANISOU  438  CA ASER A  55     2640   2207    992    -73    398    318       C  
ATOM    439  CA BSER A  55      -3.808   5.080  15.985  0.50 13.06           C  
ANISOU  439  CA BSER A  55     2678   1505    777     52    203    217       C  
ATOM    440  C  ASER A  55      -5.434   4.308  16.667  0.50 14.74           C  
ANISOU  440  C  ASER A  55     2744   1888    968   -109    506    276       C  
ATOM    441  C  BSER A  55      -4.924   4.690  16.910  0.50 12.89           C  
ANISOU  441  C  BSER A  55     2929   1427    538     26    287    246       C  
ATOM    442  O  ASER A  55      -6.253   5.169  16.922  0.50 14.71           O  
ANISOU  442  O  ASER A  55     2719   1705   1163   -138    370    357       O  
ATOM    443  O  BSER A  55      -5.666   5.514  17.410  0.50 13.92           O  
ANISOU  443  O  BSER A  55     3096   1364    827    269    399    290       O  
ATOM    444  CB ASER A  55      -2.974   4.219  16.393  0.50 17.49           C  
ANISOU  444  CB ASER A  55     2785   2375   1483      9    365    218       C  
ATOM    445  CB BSER A  55      -2.660   5.643  16.784  0.50 13.33           C  
ANISOU  445  CB BSER A  55     2730   1500    832     19    167    253       C  
ATOM    446  OG ASER A  55      -2.986   4.608  17.740  0.50 16.04           O  
ANISOU  446  OG ASER A  55     2370   2293   1429    -40    589    685       O  
ATOM    447  OG BSER A  55      -2.207   4.707  17.735  0.50 14.76           O  
ANISOU  447  OG BSER A  55     2486   2259    861    230    313    622       O  
ATOM    448  N  ATHR A  56      -5.453   3.096  17.183  0.50 14.80           N  
ANISOU  448  N  ATHR A  56     2977   1803    844      1    532    254       N  
ATOM    449  N  BTHR A  56      -5.050   3.415  17.133  0.50 14.08           N  
ANISOU  449  N  BTHR A  56     3092   1479    778     90    202    229       N  
ATOM    450  CA ATHR A  56      -6.202   2.726  18.346  0.50 14.70           C  
ANISOU  450  CA ATHR A  56     3226   1737    620    -94    589    223       C  
ATOM    451  CA BTHR A  56      -6.101   2.881  17.971  0.50 15.49           C  
ANISOU  451  CA BTHR A  56     3336   1588    960     -5    155    365       C  
ATOM    452  C  ATHR A  56      -5.652   3.238  19.684  0.50 15.06           C  
ANISOU  452  C  ATHR A  56     3203   1726    792    -32    521    173       C  
ATOM    453  C  BTHR A  56      -5.947   3.391  19.424  0.50 15.82           C  
ANISOU  453  C  BTHR A  56     3383   1587   1038   -102    240    301       C  
ATOM    454  O  ATHR A  56      -6.333   3.072  20.661  0.50 15.13           O  
ANISOU  454  O  ATHR A  56     3463   1813    472   -146    570    339       O  
ATOM    455  O  BTHR A  56      -6.946   3.574  20.180  0.50 17.81           O  
ANISOU  455  O  BTHR A  56     3604   1942   1221   -294    228    502       O  
ATOM    456  CB ATHR A  56      -6.102   1.199  18.438  0.50 14.88           C  
ANISOU  456  CB ATHR A  56     3178   1713    763    -72    572    287       C  
ATOM    457  CB BTHR A  56      -5.917   1.360  17.771  0.50 15.14           C  
ANISOU  457  CB BTHR A  56     3273   1607    872     56    131    327       C  
ATOM    458  CG2ATHR A  56      -7.066   0.542  17.407  0.50 17.49           C  
ANISOU  458  CG2ATHR A  56     3878   1723   1041   -244    523    417       C  
ATOM    459  CG2BTHR A  56      -5.919   0.598  18.984  0.50 14.88           C  
ANISOU  459  CG2BTHR A  56     3277   1488    887    173    190    680       C  
ATOM    460  OG1ATHR A  56      -4.716   0.799  18.185  0.50 11.67           O  
ANISOU  460  OG1ATHR A  56     2807   1326    297    228    220      8       O  
ATOM    461  OG1BTHR A  56      -6.837   0.855  16.773  0.50 17.78           O  
ANISOU  461  OG1BTHR A  56     3769   2250    737     44   -216    165       O  
ATOM    462  N  APHE A  57      -4.402   3.717  19.736  0.50 16.00           N  
ANISOU  462  N  APHE A  57     3437   1797    845    -47    460    173       N  
ATOM    463  N  BPHE A  57      -4.680   3.605  19.781  0.50 15.88           N  
ANISOU  463  N  BPHE A  57     3455   1604    974    -99    233    267       N  
ATOM    464  CA APHE A  57      -3.819   4.236  21.000  0.50 16.58           C  
ANISOU  464  CA APHE A  57     3378   1943    979    -51    411    130       C  
ATOM    465  CA BPHE A  57      -4.274   4.262  21.026  0.50 15.66           C  
ANISOU  465  CA BPHE A  57     3384   1719    844   -132    292    247       C  
ATOM    466  C  APHE A  57      -4.154   5.721  21.163  0.50 16.50           C  
ANISOU  466  C  APHE A  57     3389   1874   1003    -26    534    195       C  
ATOM    467  C  BPHE A  57      -4.595   5.750  20.979  0.50 15.27           C  
ANISOU  467  C  BPHE A  57     3275   1757    770    -55    333    275       C  
ATOM    468  O  APHE A  57      -4.810   6.133  22.129  0.50 16.78           O  
ANISOU  468  O  APHE A  57     3581   1976    817    -58    583    108       O  
ATOM    469  O  BPHE A  57      -5.631   6.154  21.484  0.50 16.74           O  
ANISOU  469  O  BPHE A  57     3233   1875   1249    -45    363    498       O  
ATOM    470  CB APHE A  57      -2.278   4.025  21.086  0.50 17.06           C  
ANISOU  470  CB APHE A  57     3483   1997   1001     -4    362    175       C  
ATOM    471  CB BPHE A  57      -2.764   4.055  21.300  0.50 15.93           C  
ANISOU  471  CB BPHE A  57     3479   1747    825     10    322    299       C  
ATOM    472  CG APHE A  57      -1.599   4.801  22.199  0.50 18.62           C  
ANISOU  472  CG APHE A  57     3407   2151   1514     58    255    176       C  
ATOM    473  CG BPHE A  57      -2.217   4.883  22.451  0.50 17.75           C  
ANISOU  473  CG BPHE A  57     3702   2160    881     48    103    426       C  
ATOM    474  CD1APHE A  57      -2.050   4.732  23.497  0.50 18.03           C  
ANISOU  474  CD1APHE A  57     3130   2152   1568      5    209    160       C  
ATOM    475  CD1BPHE A  57      -2.856   4.919  23.662  0.50 18.26           C  
ANISOU  475  CD1BPHE A  57     3848   2218    872     44     24    223       C  
ATOM    476  CD2APHE A  57      -0.505   5.609  21.920  0.50 19.66           C  
ANISOU  476  CD2APHE A  57     3547   2203   1718    -32    306    347       C  
ATOM    477  CD2BPHE A  57      -1.051   5.637  22.292  0.50 19.16           C  
ANISOU  477  CD2BPHE A  57     3499   2453   1324     67   -111    278       C  
ATOM    478  CE1APHE A  57      -1.419   5.449  24.486  0.50 19.24           C  
ANISOU  478  CE1APHE A  57     3162   2526   1620    -64    138    147       C  
ATOM    479  CE1BPHE A  57      -2.353   5.707  24.713  0.50 20.84           C  
ANISOU  479  CE1BPHE A  57     3745   2675   1497     56   -470    181       C  
ATOM    480  CE2APHE A  57       0.133   6.325  22.910  0.50 19.25           C  
ANISOU  480  CE2APHE A  57     3520   2272   1520    -27    378    783       C  
ATOM    481  CE2BPHE A  57      -0.556   6.411  23.330  0.50 20.63           C  
ANISOU  481  CE2BPHE A  57     3716   2584   1538    307   -320    493       C  
ATOM    482  CZ APHE A  57      -0.332   6.257  24.189  0.50 19.24           C  
ANISOU  482  CZ APHE A  57     3340   2465   1503     72    241    357       C  
ATOM    483  CZ BPHE A  57      -1.209   6.441  24.529  0.50 20.42           C  
ANISOU  483  CZ BPHE A  57     3841   2379   1539    187   -357    555       C  
ATOM    484  N  ALYS A  58      -3.709   6.541  20.224  0.50 16.85           N  
ANISOU  484  N  ALYS A  58     3292   1781   1327    -31    580    250       N  
ATOM    485  N  BLYS A  58      -3.698   6.572  20.418  0.50 15.79           N  
ANISOU  485  N  BLYS A  58     3131   1708   1159    -56    349    264       N  
ATOM    486  CA ALYS A  58      -3.938   7.993  20.304  0.50 16.58           C  
ANISOU  486  CA ALYS A  58     3047   1836   1416    -63    503    229       C  
ATOM    487  CA BLYS A  58      -3.912   8.053  20.355  0.50 16.04           C  
ANISOU  487  CA BLYS A  58     2960   1877   1255   -106    320    111       C  
ATOM    488  C  ALYS A  58      -3.593   8.565  18.939  0.50 16.64           C  
ANISOU  488  C  ALYS A  58     2954   1907   1458    -93    615    202       C  
ATOM    489  C  BLYS A  58      -3.557   8.673  19.013  0.50 15.63           C  
ANISOU  489  C  BLYS A  58     2837   1912   1189   -205    414     43       C  
ATOM    490  O  ALYS A  58      -2.519   8.291  18.420  0.50 19.47           O  
ANISOU  490  O  ALYS A  58     3279   2200   1916    164    621    405       O  
ATOM    491  O  BLYS A  58      -2.384   8.680  18.673  0.50 14.74           O  
ANISOU  491  O  BLYS A  58     2917   1861    823   -376     94   -172       O  
ATOM    492  CB ALYS A  58      -3.113   8.620  21.467  0.50 16.71           C  
ANISOU  492  CB ALYS A  58     2996   1828   1525   -154    389    238       C  
ATOM    493  CB BLYS A  58      -3.066   8.786  21.411  0.50 17.19           C  
ANISOU  493  CB BLYS A  58     2948   1991   1592   -146    223     85       C  
ATOM    494  CG ALYS A  58      -3.220  10.144  21.607  0.50 15.35           C  
ANISOU  494  CG ALYS A  58     2902   1717   1213   -238    268    191       C  
ATOM    495  CG BLYS A  58      -3.164   8.273  22.779  0.50 20.95           C  
ANISOU  495  CG BLYS A  58     3311   2724   1925    -79    160     72       C  
ATOM    496  CD ALYS A  58      -4.602  10.495  22.071  0.50 17.30           C  
ANISOU  496  CD ALYS A  58     3003   2039   1529   -143     90   -215       C  
ATOM    497  CD BLYS A  58      -4.383   8.792  23.448  0.50 23.29           C  
ANISOU  497  CD BLYS A  58     3380   3199   2269    -79    178    -53       C  
ATOM    498  CE ALYS A  58      -4.901  11.990  21.946  0.50 19.71           C  
ANISOU  498  CE ALYS A  58     3137   2365   1984    -74     61     -9       C  
ATOM    499  CE BLYS A  58      -4.622   8.013  24.713  0.50 23.47           C  
ANISOU  499  CE BLYS A  58     3273   3664   1979     24    272    -54       C  
ATOM    500  NZ ALYS A  58      -5.358  12.327  20.539  0.50 22.60           N1+
ANISOU  500  NZ ALYS A  58     3782   2813   1991     88    194     79       N1+
ATOM    501  NZ BLYS A  58      -4.757   8.948  25.862  0.50 25.11           N1+
ANISOU  501  NZ BLYS A  58     3812   4064   1663    -24    305      8       N1+
ATOM    502  N   ASN A  59      -4.549   9.292  18.350  1.00 15.05           N  
ANISOU  502  N   ASN A  59     2689   1755   1271   -204    688    179       N  
ATOM    503  CA  ASN A  59      -4.318   9.981  17.084  1.00 14.87           C  
ANISOU  503  CA  ASN A  59     2749   1609   1293   -188    695    -17       C  
ATOM    504  C   ASN A  59      -3.531  11.225  17.364  1.00 15.15           C  
ANISOU  504  C   ASN A  59     3054   1519   1181   -220    647    -62       C  
ATOM    505  O   ASN A  59      -3.755  11.918  18.363  1.00 17.57           O  
ANISOU  505  O   ASN A  59     3400   1750   1526   -311    964   -276       O  
ATOM    506  CB  ASN A  59      -5.638  10.367  16.456  1.00 15.99           C  
ANISOU  506  CB  ASN A  59     2998   1731   1344    -40    504    232       C  
ATOM    507  CG  ASN A  59      -6.538   9.185  16.121  1.00 18.22           C  
ANISOU  507  CG  ASN A  59     2607   2433   1882    -19    199     85       C  
ATOM    508  ND2 ASN A  59      -7.834   9.283  16.486  1.00 24.00           N  
ANISOU  508  ND2 ASN A  59     3035   3122   2962     41    561     11       N  
ATOM    509  OD1 ASN A  59      -6.105   8.214  15.557  1.00 16.55           O  
ANISOU  509  OD1 ASN A  59     2744   1935   1609     -4    403    237       O  
ATOM    510  N   THR A  60      -2.604  11.526  16.462  1.00 13.31           N  
ANISOU  510  N   THR A  60     2839   1429    788   -246    578     50       N  
ATOM    511  CA  THR A  60      -1.828  12.732  16.582  1.00 13.23           C  
ANISOU  511  CA  THR A  60     2852   1494    679   -184    507     -5       C  
ATOM    512  C   THR A  60      -1.709  13.365  15.210  1.00 11.87           C  
ANISOU  512  C   THR A  60     2572   1318    619   -145    402     34       C  
ATOM    513  O   THR A  60      -1.765  12.679  14.184  1.00 12.53           O  
ANISOU  513  O   THR A  60     2774   1333    651   -188    343    -29       O  
ATOM    514  CB  THR A  60      -0.385  12.458  17.148  1.00 13.70           C  
ANISOU  514  CB  THR A  60     2911   1586    707   -194    344     -3       C  
ATOM    515  CG2 THR A  60      -0.378  11.897  18.598  1.00 16.21           C  
ANISOU  515  CG2 THR A  60     3386   1872    898   -217    350    149       C  
ATOM    516  OG1 THR A  60       0.369  11.624  16.281  1.00 14.42           O  
ANISOU  516  OG1 THR A  60     2838   1750    888    -56    242    130       O  
ATOM    517  N   GLU A  61      -1.412  14.654  15.189  1.00 12.20           N  
ANISOU  517  N   GLU A  61     2752   1195    687   -217    353    -26       N  
ATOM    518  CA  GLU A  61      -1.105  15.359  13.933  1.00 12.38           C  
ANISOU  518  CA  GLU A  61     2558   1381    764   -158    285    -13       C  
ATOM    519  C   GLU A  61      -0.200  16.509  14.237  1.00 12.23           C  
ANISOU  519  C   GLU A  61     2663   1310    672   -114    275    -76       C  
ATOM    520  O   GLU A  61      -0.477  17.285  15.187  1.00 14.29           O  
ANISOU  520  O   GLU A  61     2978   1504    945   -143    573   -259       O  
ATOM    521  CB  GLU A  61      -2.395  15.811  13.274  1.00 15.10           C  
ANISOU  521  CB  GLU A  61     2769   1719   1249   -193    222    128       C  
ATOM    522  CG  GLU A  61      -2.246  16.495  11.993  1.00 18.90           C  
ANISOU  522  CG  GLU A  61     2861   2565   1754   -156     10    752       C  
ATOM    523  CD  GLU A  61      -3.544  17.039  11.453  1.00 25.91           C  
ANISOU  523  CD  GLU A  61     2978   3753   3112   -146     19   1062       C  
ATOM    524  OE1 GLU A  61      -3.485  18.099  10.840  1.00 29.53           O  
ANISOU  524  OE1 GLU A  61     3026   4271   3920   -407   -397   1361       O  
ATOM    525  OE2 GLU A  61      -4.604  16.426  11.649  1.00 31.17           O1-
ANISOU  525  OE2 GLU A  61     3257   4654   3932   -416   -304    931       O1-
ATOM    526  N   ILE A  62       0.928  16.600  13.536  1.00 10.31           N  
ANISOU  526  N   ILE A  62     2454   1181    281   -230    166    -36       N  
ATOM    527  CA  ILE A  62       1.799  17.727  13.612  1.00 10.26           C  
ANISOU  527  CA  ILE A  62     2451   1165    282   -151     74    -27       C  
ATOM    528  C   ILE A  62       1.997  18.325  12.226  1.00  9.90           C  
ANISOU  528  C   ILE A  62     2270   1230    260   -264     97     38       C  
ATOM    529  O   ILE A  62       2.100  17.589  11.240  1.00 11.35           O  
ANISOU  529  O   ILE A  62     2833   1215    264   -294     90    -96       O  
ATOM    530  CB  ILE A  62       3.154  17.362  14.245  1.00 10.78           C  
ANISOU  530  CB  ILE A  62     2557   1283    254   -278    -39    -24       C  
ATOM    531  CG1 ILE A  62       3.910  16.276  13.506  1.00 11.87           C  
ANISOU  531  CG1 ILE A  62     2459   1515    536   -218    -57     12       C  
ATOM    532  CG2 ILE A  62       2.949  16.932  15.734  1.00 13.36           C  
ANISOU  532  CG2 ILE A  62     2884   1899    290      6     91    238       C  
ATOM    533  CD1 ILE A  62       5.323  16.051  13.976  1.00 13.97           C  
ANISOU  533  CD1 ILE A  62     2434   1856   1018    -51   -282    -81       C  
ATOM    534  N   SER A  63       2.040  19.644  12.176  1.00  9.83           N  
ANISOU  534  N   SER A  63     2343   1128    262    -56    131     22       N  
ATOM    535  CA  SER A  63       2.407  20.388  10.962  1.00  9.10           C  
ANISOU  535  CA  SER A  63     2098   1105    253    -74     27     -4       C  
ATOM    536  C   SER A  63       3.513  21.336  11.294  1.00  9.52           C  
ANISOU  536  C   SER A  63     2117   1010    488    -31     39    -28       C  
ATOM    537  O   SER A  63       3.498  21.955  12.388  1.00 10.67           O  
ANISOU  537  O   SER A  63     2362   1167    524   -122    167   -233       O  
ATOM    538  CB  SER A  63       1.238  21.164  10.404  1.00 10.21           C  
ANISOU  538  CB  SER A  63     2234   1349    296     24     61    -74       C  
ATOM    539  OG  SER A  63       0.205  20.311   9.912  1.00 12.87           O  
ANISOU  539  OG  SER A  63     2493   1698    696    -46   -189    -47       O  
ATOM    540  N   PHE A  64       4.508  21.453  10.429  1.00  9.04           N  
ANISOU  540  N   PHE A  64     2110   1067    256   -165     13    -54       N  
ATOM    541  CA  PHE A  64       5.706  22.172  10.763  1.00  9.35           C  
ANISOU  541  CA  PHE A  64     2175   1123    255    -99    -13    -46       C  
ATOM    542  C   PHE A  64       6.435  22.606   9.496  1.00  8.77           C  
ANISOU  542  C   PHE A  64     2186    891    255   -111    -40     29       C  
ATOM    543  O   PHE A  64       6.206  22.058   8.402  1.00  9.65           O  
ANISOU  543  O   PHE A  64     2239   1161    263   -124   -107    -58       O  
ATOM    544  CB  PHE A  64       6.618  21.331  11.673  1.00  9.96           C  
ANISOU  544  CB  PHE A  64     2252   1178    354   -205    -35    118       C  
ATOM    545  CG  PHE A  64       6.968  20.016  11.051  1.00  9.44           C  
ANISOU  545  CG  PHE A  64     2185   1132    267    -23   -152    -10       C  
ATOM    546  CD1 PHE A  64       6.181  18.887  11.191  1.00  9.75           C  
ANISOU  546  CD1 PHE A  64     2156   1230    317    -65   -108     19       C  
ATOM    547  CD2 PHE A  64       8.100  19.879  10.295  1.00  9.85           C  
ANISOU  547  CD2 PHE A  64     2237   1108    397     21    -78    134       C  
ATOM    548  CE1 PHE A  64       6.459  17.712  10.590  1.00 11.29           C  
ANISOU  548  CE1 PHE A  64     2460   1373    457    -80   -315    -15       C  
ATOM    549  CE2 PHE A  64       8.388  18.670   9.691  1.00 11.32           C  
ANISOU  549  CE2 PHE A  64     2351   1663    287    125     16    220       C  
ATOM    550  CZ  PHE A  64       7.586  17.584   9.838  1.00 11.37           C  
ANISOU  550  CZ  PHE A  64     2603   1374    340      9   -231      4       C  
ATOM    551  N   ILE A  65       7.341  23.528   9.695  1.00  9.17           N  
ANISOU  551  N   ILE A  65     2159   1069    253   -124      3      4       N  
ATOM    552  CA  ILE A  65       8.299  23.992   8.711  1.00  9.29           C  
ANISOU  552  CA  ILE A  65     2183   1071    274    -40     20    -34       C  
ATOM    553  C   ILE A  65       9.702  23.561   9.171  1.00  9.02           C  
ANISOU  553  C   ILE A  65     2119   1025    281      5    -26    103       C  
ATOM    554  O   ILE A  65      10.010  23.665  10.369  1.00  9.48           O  
ANISOU  554  O   ILE A  65     2242   1048    311    -58    -63     -2       O  
ATOM    555  CB  ILE A  65       8.222  25.532   8.501  1.00  9.88           C  
ANISOU  555  CB  ILE A  65     2193   1023    536     -9     -6     -9       C  
ATOM    556  CG1 ILE A  65       6.829  25.836   7.940  1.00 11.43           C  
ANISOU  556  CG1 ILE A  65     2385   1268    690    -25   -102    216       C  
ATOM    557  CG2 ILE A  65       9.347  26.020   7.639  1.00 11.05           C  
ANISOU  557  CG2 ILE A  65     2510   1214    474     33    100    172       C  
ATOM    558  CD1 ILE A  65       6.511  27.361   7.880  1.00 15.94           C  
ANISOU  558  CD1 ILE A  65     2877   1413   1764    211   -107     56       C  
ATOM    559  N   LEU A  66      10.508  22.982   8.284  1.00  9.22           N  
ANISOU  559  N   LEU A  66     2184   1046    270     44    153     61       N  
ATOM    560  CA  LEU A  66      11.801  22.513   8.672  1.00  9.55           C  
ANISOU  560  CA  LEU A  66     2207   1057    364     18    136    131       C  
ATOM    561  C   LEU A  66      12.569  23.643   9.339  1.00  9.26           C  
ANISOU  561  C   LEU A  66     2156   1016    344     10     12     95       C  
ATOM    562  O   LEU A  66      12.643  24.766   8.831  1.00 10.37           O  
ANISOU  562  O   LEU A  66     2276   1071    594    -60    -28    164       O  
ATOM    563  CB  LEU A  66      12.574  21.950   7.467  1.00 10.34           C  
ANISOU  563  CB  LEU A  66     2199   1327    402     45    153     99       C  
ATOM    564  CG  LEU A  66      11.945  20.694   6.818  1.00 10.78           C  
ANISOU  564  CG  LEU A  66     2497   1201    398     16    -34   -222       C  
ATOM    565  CD1 LEU A  66      12.640  20.425   5.481  1.00 15.08           C  
ANISOU  565  CD1 LEU A  66     3338   1590    802    204    310   -277       C  
ATOM    566  CD2 LEU A  66      12.054  19.533   7.745  1.00 12.90           C  
ANISOU  566  CD2 LEU A  66     2865   1094    939   -125   -109     64       C  
ATOM    567  N   GLY A  67      13.235  23.300  10.426  1.00  9.74           N  
ANISOU  567  N   GLY A  67     2196   1103    402    -82    -76     87       N  
ATOM    568  CA  GLY A  67      14.079  24.209  11.158  1.00 10.16           C  
ANISOU  568  CA  GLY A  67     2156   1240    461    -17    -92     45       C  
ATOM    569  C   GLY A  67      13.396  25.151  12.123  1.00  9.61           C  
ANISOU  569  C   GLY A  67     2112   1088    448    -49   -123     25       C  
ATOM    570  O   GLY A  67      14.083  25.884  12.830  1.00 10.65           O  
ANISOU  570  O   GLY A  67     2161   1358    524   -122   -158   -101       O  
ATOM    571  N   GLN A  68      12.076  25.106  12.197  1.00  9.30           N  
ANISOU  571  N   GLN A  68     2148    961    424   -122   -122   -113       N  
ATOM    572  CA  GLN A  68      11.268  26.063  12.961  1.00  9.93           C  
ANISOU  572  CA  GLN A  68     2200   1004    568   -116   -156   -124       C  
ATOM    573  C   GLN A  68      10.540  25.370  14.128  1.00  9.96           C  
ANISOU  573  C   GLN A  68     2233    948    602     25    -83    -99       C  
ATOM    574  O   GLN A  68       9.657  24.515  13.910  1.00  9.80           O  
ANISOU  574  O   GLN A  68     2189   1027    507    -65    -25   -164       O  
ATOM    575  CB  GLN A  68      10.273  26.752  12.035  1.00 10.29           C  
ANISOU  575  CB  GLN A  68     2383    889    636    -74   -158    -59       C  
ATOM    576  CG  GLN A  68      11.017  27.465  10.925  1.00 13.30           C  
ANISOU  576  CG  GLN A  68     2811   1369    872   -190   -495    154       C  
ATOM    577  CD  GLN A  68      10.270  28.457  10.131  1.00 15.44           C  
ANISOU  577  CD  GLN A  68     3368   1306   1190    -75   -639    217       C  
ATOM    578  NE2 GLN A  68      10.966  29.016   9.150  1.00 16.72           N  
ANISOU  578  NE2 GLN A  68     4059   1303    991   -312   -563    406       N  
ATOM    579  OE1 GLN A  68       9.091  28.743  10.407  1.00 18.75           O  
ANISOU  579  OE1 GLN A  68     3440   1372   2311    137  -1054    371       O  
ATOM    580  N   GLU A  69      10.934  25.715  15.335  1.00  9.35           N  
ANISOU  580  N   GLU A  69     2215    980    357    -90   -101   -131       N  
ATOM    581  CA  GLU A  69      10.432  25.059  16.536  1.00 10.30           C  
ANISOU  581  CA  GLU A  69     2361   1050    502      6      6    179       C  
ATOM    582  C   GLU A  69       8.936  25.208  16.677  1.00  9.61           C  
ANISOU  582  C   GLU A  69     2370    987    295     14     68    -78       C  
ATOM    583  O   GLU A  69       8.388  26.273  16.321  1.00 10.57           O  
ANISOU  583  O   GLU A  69     2309    910    796     65    -66    -25       O  
ATOM    584  CB  GLU A  69      11.140  25.640  17.776  1.00 12.46           C  
ANISOU  584  CB  GLU A  69     2446   1786    502    -15    -61    173       C  
ATOM    585  CG  GLU A  69      10.837  25.032  19.080  1.00 15.74           C  
ANISOU  585  CG  GLU A  69     3382   1786    812   -299   -157    179       C  
ATOM    586  CD  GLU A  69      11.775  25.499  20.099  1.00 24.08           C  
ANISOU  586  CD  GLU A  69     4365   3400   1384   -169   -669    -68       C  
ATOM    587  OE1 GLU A  69      11.717  26.713  20.399  1.00 31.87           O  
ANISOU  587  OE1 GLU A  69     5206   4493   2409  -1043  -1098  -1144       O  
ATOM    588  OE2 GLU A  69      12.566  24.630  20.597  1.00 26.40           O1-
ANISOU  588  OE2 GLU A  69     4681   3721   1625     48  -1029   -309       O1-
ATOM    589  N   PHE A  70       8.296  24.185  17.219  1.00  9.52           N  
ANISOU  589  N   PHE A  70     2299    933    384    -29    102    -16       N  
ATOM    590  CA  PHE A  70       6.880  24.191  17.455  1.00  9.76           C  
ANISOU  590  CA  PHE A  70     2297    993    418     50    136    -50       C  
ATOM    591  C   PHE A  70       6.559  23.415  18.724  1.00  9.88           C  
ANISOU  591  C   PHE A  70     2341    918    491    147    248    -53       C  
ATOM    592  O   PHE A  70       7.344  22.627  19.215  1.00 10.78           O  
ANISOU  592  O   PHE A  70     2370   1263    460    365    133     46       O  
ATOM    593  CB  PHE A  70       6.123  23.598  16.254  1.00  9.57           C  
ANISOU  593  CB  PHE A  70     2173   1060    403    117     59    -37       C  
ATOM    594  CG  PHE A  70       6.475  22.174  15.908  1.00  9.86           C  
ANISOU  594  CG  PHE A  70     2317   1172    255    -38      0     46       C  
ATOM    595  CD1 PHE A  70       7.584  21.875  15.133  1.00  9.16           C  
ANISOU  595  CD1 PHE A  70     2127   1093    258     29     54    -57       C  
ATOM    596  CD2 PHE A  70       5.687  21.133  16.318  1.00 11.31           C  
ANISOU  596  CD2 PHE A  70     2371   1412    514    -29    277   -187       C  
ATOM    597  CE1 PHE A  70       7.870  20.594  14.765  1.00  9.82           C  
ANISOU  597  CE1 PHE A  70     2321   1140    269     36    -14    -52       C  
ATOM    598  CE2 PHE A  70       5.998  19.838  15.966  1.00 11.83           C  
ANISOU  598  CE2 PHE A  70     2626   1410    457   -207    195   -110       C  
ATOM    599  CZ  PHE A  70       7.079  19.553  15.210  1.00 10.49           C  
ANISOU  599  CZ  PHE A  70     2431   1268    287    137    -22   -184       C  
ATOM    600  N   ASP A  71       5.346  23.631  19.217  1.00 10.87           N  
ANISOU  600  N   ASP A  71     2315   1093    720    339    269    186       N  
ATOM    601  CA  ASP A  71       4.788  22.904  20.382  1.00 11.52           C  
ANISOU  601  CA  ASP A  71     2562   1369    444    204    430     74       C  
ATOM    602  C   ASP A  71       4.111  21.657  19.906  1.00 12.04           C  
ANISOU  602  C   ASP A  71     2577   1534    461     43    289     97       C  
ATOM    603  O   ASP A  71       3.398  21.623  18.860  1.00 14.01           O  
ANISOU  603  O   ASP A  71     2741   1625    954    167    139    337       O  
ATOM    604  CB  ASP A  71       3.702  23.741  21.037  1.00 12.78           C  
ANISOU  604  CB  ASP A  71     2598   1667    590    313    278     47       C  
ATOM    605  CG  ASP A  71       4.222  24.948  21.649  1.00 14.19           C  
ANISOU  605  CG  ASP A  71     2834   2108    450    226   -234   -306       C  
ATOM    606  OD1 ASP A  71       5.202  24.813  22.442  1.00 14.99           O  
ANISOU  606  OD1 ASP A  71     3161   1795    738    308   -223   -297       O  
ATOM    607  OD2 ASP A  71       3.634  26.040  21.445  1.00 14.87           O1-
ANISOU  607  OD2 ASP A  71     2880   1854    916    259   -152    -15       O1-
ATOM    608  N   GLU A  72       4.363  20.554  20.633  1.00 12.19           N  
ANISOU  608  N   GLU A  72     2577   1409    645    129    354    298       N  
ATOM    609  CA  GLU A  72       3.807  19.239  20.276  1.00 12.71           C  
ANISOU  609  CA  GLU A  72     2417   1504    906    107    250    322       C  
ATOM    610  C   GLU A  72       3.315  18.572  21.545  1.00 12.97           C  
ANISOU  610  C   GLU A  72     2573   1383    971    161    158    367       C  
ATOM    611  O   GLU A  72       3.995  18.597  22.566  1.00 14.84           O  
ANISOU  611  O   GLU A  72     2865   2017    754    -58    346    387       O  
ATOM    612  CB  GLU A  72       4.900  18.373  19.581  1.00 12.12           C  
ANISOU  612  CB  GLU A  72     2479   1425    698     94    321    254       C  
ATOM    613  CG  GLU A  72       4.498  16.939  19.298  1.00 12.61           C  
ANISOU  613  CG  GLU A  72     2695   1578    517    100     59    345       C  
ATOM    614  CD  GLU A  72       5.544  16.120  18.600  1.00 12.45           C  
ANISOU  614  CD  GLU A  72     2747   1548    436     85    239     91       C  
ATOM    615  OE1 GLU A  72       6.688  16.541  18.514  1.00 12.73           O  
ANISOU  615  OE1 GLU A  72     2549   1513    774    -30    144    -26       O  
ATOM    616  OE2 GLU A  72       5.210  14.990  18.154  1.00 14.37           O1-
ANISOU  616  OE2 GLU A  72     2844   1593   1021      1    108    -18       O1-
ATOM    617  N   VAL A  73       2.130  18.000  21.505  1.00 14.77           N  
ANISOU  617  N   VAL A  73     2617   1739   1256     57    289    583       N  
ATOM    618  CA  VAL A  73       1.686  17.151  22.613  1.00 15.39           C  
ANISOU  618  CA  VAL A  73     2474   1839   1532     67    384    539       C  
ATOM    619  C   VAL A  73       1.766  15.719  22.043  1.00 14.89           C  
ANISOU  619  C   VAL A  73     2514   1915   1228     64    241    534       C  
ATOM    620  O   VAL A  73       1.071  15.362  21.106  1.00 15.98           O  
ANISOU  620  O   VAL A  73     2751   1820   1497    -59    -70    534       O  
ATOM    621  CB  VAL A  73       0.277  17.522  23.083  1.00 16.57           C  
ANISOU  621  CB  VAL A  73     2703   2044   1548     64    610    432       C  
ATOM    622  CG1 VAL A  73      -0.170  16.563  24.194  1.00 18.94           C  
ANISOU  622  CG1 VAL A  73     2882   2429   1885    118    803    575       C  
ATOM    623  CG2 VAL A  73       0.221  18.957  23.605  1.00 18.86           C  
ANISOU  623  CG2 VAL A  73     2871   1944   2350    359    650    243       C  
ATOM    624  N   THR A  74       2.649  14.912  22.582  1.00 13.43           N  
ANISOU  624  N   THR A  74     2498   1994    608    230    216    398       N  
ATOM    625  CA  THR A  74       2.939  13.606  22.039  1.00 13.31           C  
ANISOU  625  CA  THR A  74     2541   1890    624     96    284    318       C  
ATOM    626  C   THR A  74       1.811  12.611  22.353  1.00 13.92           C  
ANISOU  626  C   THR A  74     2562   1961    765    132    189    373       C  
ATOM    627  O   THR A  74       0.969  12.889  23.172  1.00 14.74           O  
ANISOU  627  O   THR A  74     2828   1817    954    103    437    441       O  
ATOM    628  CB  THR A  74       4.263  13.045  22.561  1.00 12.09           C  
ANISOU  628  CB  THR A  74     2401   1867    325    111    303    222       C  
ATOM    629  CG2 THR A  74       5.378  14.012  22.348  1.00 13.24           C  
ANISOU  629  CG2 THR A  74     2760   1648    620     52    278    233       C  
ATOM    630  OG1 THR A  74       4.122  12.814  23.969  1.00 13.17           O  
ANISOU  630  OG1 THR A  74     2627   1909    465    239    222    337       O  
ATOM    631  N   ALA A  75       1.848  11.450  21.707  1.00 14.54           N  
ANISOU  631  N   ALA A  75     2682   2025    818    -46    311    333       N  
ATOM    632  CA  ALA A  75       0.801  10.416  21.869  1.00 14.45           C  
ANISOU  632  CA  ALA A  75     2667   1955    867    -74    126    279       C  
ATOM    633  C   ALA A  75       0.683  10.021  23.367  1.00 15.56           C  
ANISOU  633  C   ALA A  75     2695   2060   1157   -180    235    273       C  
ATOM    634  O   ALA A  75      -0.417   9.758  23.835  1.00 17.13           O  
ANISOU  634  O   ALA A  75     3020   2321   1165   -229    369    376       O  
ATOM    635  CB  ALA A  75       1.066   9.203  21.029  1.00 15.31           C  
ANISOU  635  CB  ALA A  75     2761   1958   1099   -160     78    169       C  
ATOM    636  N   ASP A  76       1.812   9.961  24.064  1.00 14.96           N  
ANISOU  636  N   ASP A  76     2867   1865    950    -94    257    436       N  
ATOM    637  CA  ASP A  76       1.854   9.635  25.520  1.00 15.20           C  
ANISOU  637  CA  ASP A  76     2905   2004    867   -220    221    426       C  
ATOM    638  C   ASP A  76       1.630  10.854  26.427  1.00 16.03           C  
ANISOU  638  C   ASP A  76     3145   2057    888   -190    425    448       C  
ATOM    639  O   ASP A  76       1.766  10.757  27.627  1.00 18.58           O  
ANISOU  639  O   ASP A  76     3650   2642    767    -19    360    492       O  
ATOM    640  CB  ASP A  76       3.180   8.927  25.824  1.00 15.92           C  
ANISOU  640  CB  ASP A  76     3059   1958   1029   -175    244    343       C  
ATOM    641  CG  ASP A  76       4.395   9.772  25.538  1.00 14.71           C  
ANISOU  641  CG  ASP A  76     2960   1830    798     -6   -219    268       C  
ATOM    642  OD1 ASP A  76       4.582  10.204  24.365  1.00 14.41           O  
ANISOU  642  OD1 ASP A  76     3149   1843    482    -92    -89    421       O  
ATOM    643  OD2 ASP A  76       5.152  10.002  26.490  1.00 14.80           O1-
ANISOU  643  OD2 ASP A  76     3410   1618    595    -42     -2    336       O1-
ATOM    644  N   ASP A  77       1.288  11.997  25.843  1.00 15.94           N  
ANISOU  644  N   ASP A  77     3142   2066    847   -122    626    338       N  
ATOM    645  CA  ASP A  77       0.864  13.190  26.577  1.00 17.86           C  
ANISOU  645  CA  ASP A  77     3232   2357   1198    -96    767    226       C  
ATOM    646  C   ASP A  77       2.000  14.008  27.174  1.00 17.68           C  
ANISOU  646  C   ASP A  77     3318   2283   1117    -36    644    159       C  
ATOM    647  O   ASP A  77       1.780  14.758  28.123  1.00 20.25           O  
ANISOU  647  O   ASP A  77     3525   2606   1563    -19    852   -322       O  
ATOM    648  CB  ASP A  77      -0.271  12.944  27.589  1.00 19.18           C  
ANISOU  648  CB  ASP A  77     3389   2486   1411   -175    937    273       C  
ATOM    649  CG  ASP A  77      -1.167  14.156  27.791  1.00 23.75           C  
ANISOU  649  CG  ASP A  77     3774   3211   2037    -54   1089    228       C  
ATOM    650  OD1 ASP A  77      -1.694  14.273  28.912  1.00 30.29           O  
ANISOU  650  OD1 ASP A  77     4566   4191   2752    252   1686   -157       O  
ATOM    651  OD2 ASP A  77      -1.393  14.961  26.859  1.00 29.24           O1-
ANISOU  651  OD2 ASP A  77     4453   3955   2698    -35   1229    585       O1-
ATOM    652  N   ARG A  78       3.192  13.946  26.604  1.00 15.25           N  
ANISOU  652  N   ARG A  78     3199   1853    743     53    590    329       N  
ATOM    653  CA  ARG A  78       4.213  14.896  26.948  1.00 14.82           C  
ANISOU  653  CA  ARG A  78     3165   1873    592     72    460    217       C  
ATOM    654  C   ARG A  78       3.967  16.176  26.178  1.00 14.42           C  
ANISOU  654  C   ARG A  78     3212   1782    485    152    472    215       C  
ATOM    655  O   ARG A  78       3.609  16.142  25.014  1.00 15.50           O  
ANISOU  655  O   ARG A  78     3487   1624    777    186    314    169       O  
ATOM    656  CB  ARG A  78       5.615  14.410  26.654  1.00 13.78           C  
ANISOU  656  CB  ARG A  78     3176   1521    538     55    319    266       C  
ATOM    657  CG  ARG A  78       6.119  13.312  27.534  1.00 13.52           C  
ANISOU  657  CG  ARG A  78     3091   1396    649     51    307    127       C  
ATOM    658  CD  ARG A  78       7.422  12.710  27.025  1.00 13.57           C  
ANISOU  658  CD  ARG A  78     3195   1554    407      4     10    168       C  
ATOM    659  NE  ARG A  78       7.150  11.854  25.887  1.00 12.99           N  
ANISOU  659  NE  ARG A  78     3058   1398    477    119   -121    158       N  
ATOM    660  CZ  ARG A  78       7.715  11.914  24.678  1.00 12.77           C  
ANISOU  660  CZ  ARG A  78     2650   1485    714    231    -66     45       C  
ATOM    661  NH1 ARG A  78       8.775  12.686  24.439  1.00 13.13           N1+
ANISOU  661  NH1 ARG A  78     2869   1629    488    -73    -86    127       N1+
ATOM    662  NH2 ARG A  78       7.286  11.086  23.732  1.00 12.38           N  
ANISOU  662  NH2 ARG A  78     2734   1314    654    -33   -121     21       N  
ATOM    663  N   LYS A  79       4.207  17.309  26.811  1.00 14.87           N  
ANISOU  663  N   LYS A  79     3327   1817    505    214    593    166       N  
ATOM    664  CA  LYS A  79       4.179  18.623  26.180  1.00 15.03           C  
ANISOU  664  CA  LYS A  79     3104   1772    833    355    521    138       C  
ATOM    665  C   LYS A  79       5.618  18.991  25.888  1.00 13.93           C  
ANISOU  665  C   LYS A  79     3028   1503    761    320    329    125       C  
ATOM    666  O   LYS A  79       6.417  19.269  26.792  1.00 16.10           O  
ANISOU  666  O   LYS A  79     3473   2222    421    309    523    -43       O  
ATOM    667  CB  LYS A  79       3.473  19.640  27.055  1.00 16.85           C  
ANISOU  667  CB  LYS A  79     3434   1944   1022    371    521    207       C  
ATOM    668  CG  LYS A  79       2.121  19.214  27.572  1.00 22.73           C  
ANISOU  668  CG  LYS A  79     3543   2705   2388    593    711    -29       C  
ATOM    669  CD  LYS A  79       1.041  18.792  26.626  1.00 28.57           C  
ANISOU  669  CD  LYS A  79     4101   3442   3311    393    573    -66       C  
ATOM    670  CE  LYS A  79      -0.304  18.536  27.357  1.00 31.76           C  
ANISOU  670  CE  LYS A  79     4325   3850   3892    289    550     49       C  
ATOM    671  NZ  LYS A  79      -0.289  17.377  28.302  1.00 33.42           N1+
ANISOU  671  NZ  LYS A  79     4837   4131   3729    309    511    157       N1+
ATOM    672  N   VAL A  80       5.991  18.955  24.608  1.00 12.54           N  
ANISOU  672  N   VAL A  80     2873   1538    353    243    242     46       N  
ATOM    673  CA  VAL A  80       7.372  19.084  24.226  1.00 11.96           C  
ANISOU  673  CA  VAL A  80     2807   1395    339    216    102     69       C  
ATOM    674  C   VAL A  80       7.545  20.244  23.221  1.00 11.33           C  
ANISOU  674  C   VAL A  80     2755   1254    294    301    181   -137       C  
ATOM    675  O   VAL A  80       6.575  20.684  22.593  1.00 12.65           O  
ANISOU  675  O   VAL A  80     2866   1377    561    313    311    132       O  
ATOM    676  CB  VAL A  80       7.909  17.746  23.579  1.00 12.12           C  
ANISOU  676  CB  VAL A  80     2855   1184    564    184    168     30       C  
ATOM    677  CG1 VAL A  80       7.606  16.543  24.482  1.00 13.28           C  
ANISOU  677  CG1 VAL A  80     3409   1184    450    237    110    236       C  
ATOM    678  CG2 VAL A  80       7.304  17.490  22.194  1.00 12.63           C  
ANISOU  678  CG2 VAL A  80     3213   1327    259     68    128    -14       C  
ATOM    679  N   LYS A  81       8.782  20.681  23.119  1.00 11.33           N  
ANISOU  679  N   LYS A  81     2840   1139    326    175     83    -24       N  
ATOM    680  CA  LYS A  81       9.180  21.655  22.095  1.00 11.42           C  
ANISOU  680  CA  LYS A  81     2920    969    450    269     48      5       C  
ATOM    681  C   LYS A  81       9.975  20.875  21.077  1.00 10.67           C  
ANISOU  681  C   LYS A  81     2651   1004    398    111     94   -128       C  
ATOM    682  O   LYS A  81      10.993  20.274  21.420  1.00 11.39           O  
ANISOU  682  O   LYS A  81     2719   1295    310    247   -143   -125       O  
ATOM    683  CB  LYS A  81      10.049  22.733  22.728  1.00 13.42           C  
ANISOU  683  CB  LYS A  81     3275   1149    674     46    221     14       C  
ATOM    684  CG  LYS A  81       9.405  23.579  23.735  1.00 19.38           C  
ANISOU  684  CG  LYS A  81     3782   1992   1588    162    -25   -552       C  
ATOM    685  CD  LYS A  81       8.374  24.486  23.195  1.00 22.36           C  
ANISOU  685  CD  LYS A  81     4020   2569   1907    180      0   -355       C  
ATOM    686  CE  LYS A  81       7.785  25.347  24.308  1.00 25.14           C  
ANISOU  686  CE  LYS A  81     4151   2897   2505    187   -452   -602       C  
ATOM    687  NZ  LYS A  81       6.954  26.479  23.827  1.00 26.85           N1+
ANISOU  687  NZ  LYS A  81     4905   2900   2394    135  -1090   -524       N1+
ATOM    688  N   SER A  82       9.515  20.934  19.831  1.00 10.31           N  
ANISOU  688  N   SER A  82     2580   1082    255    179     68     14       N  
ATOM    689  CA  SER A  82      10.050  20.090  18.771  1.00  9.26           C  
ANISOU  689  CA  SER A  82     2357    890    269     64     62    -22       C  
ATOM    690  C   SER A  82      10.652  20.923  17.654  1.00  9.38           C  
ANISOU  690  C   SER A  82     2339    955    267     67    -44     91       C  
ATOM    691  O   SER A  82      10.143  21.974  17.296  1.00  9.80           O  
ANISOU  691  O   SER A  82     2376    982    366    168    115     98       O  
ATOM    692  CB  SER A  82       8.938  19.256  18.206  1.00 10.23           C  
ANISOU  692  CB  SER A  82     2420   1193    271     20    127     62       C  
ATOM    693  OG  SER A  82       8.568  18.274  19.144  1.00 11.88           O  
ANISOU  693  OG  SER A  82     2710   1088    715     45    251    287       O  
ATOM    694  N   THR A  83      11.759  20.406  17.086  1.00  8.94           N  
ANISOU  694  N   THR A  83     2163    972    259    145    -10     64       N  
ATOM    695  CA  THR A  83      12.327  20.979  15.898  1.00  9.30           C  
ANISOU  695  CA  THR A  83     2328    940    264     10     89     69       C  
ATOM    696  C   THR A  83      12.663  19.835  14.970  1.00  9.54           C  
ANISOU  696  C   THR A  83     2377    990    257     83    -28     51       C  
ATOM    697  O   THR A  83      13.293  18.863  15.371  1.00 10.36           O  
ANISOU  697  O   THR A  83     2646   1032    257    258    -26    -55       O  
ATOM    698  CB  THR A  83      13.608  21.776  16.209  1.00 10.75           C  
ANISOU  698  CB  THR A  83     2254   1041    789    162    143     32       C  
ATOM    699  CG2 THR A  83      14.057  22.519  14.964  1.00 13.66           C  
ANISOU  699  CG2 THR A  83     2745   1225   1218   -125    199    132       C  
ATOM    700  OG1 THR A  83      13.353  22.700  17.260  1.00 12.44           O  
ANISOU  700  OG1 THR A  83     2706   1222    795   -101   -165   -229       O  
ATOM    701  N   ILE A  84      12.212  19.951  13.697  1.00  9.62           N  
ANISOU  701  N   ILE A  84     2383   1014    258    115    -60     49       N  
ATOM    702  CA  ILE A  84      12.430  18.928  12.698  1.00  9.16           C  
ANISOU  702  CA  ILE A  84     2270    951    257    101     92     -3       C  
ATOM    703  C   ILE A  84      13.234  19.533  11.591  1.00  9.49           C  
ANISOU  703  C   ILE A  84     2456    885    261      1     70     60       C  
ATOM    704  O   ILE A  84      12.904  20.594  11.051  1.00 10.10           O  
ANISOU  704  O   ILE A  84     2594    969    273     87    110    106       O  
ATOM    705  CB  ILE A  84      11.116  18.310  12.197  1.00  9.51           C  
ANISOU  705  CB  ILE A  84     2334    980    298    182     28    180       C  
ATOM    706  CG1 ILE A  84      10.353  17.720  13.403  1.00  9.59           C  
ANISOU  706  CG1 ILE A  84     2217   1139    285     75    -16    168       C  
ATOM    707  CG2 ILE A  84      11.420  17.229  11.154  1.00 10.98           C  
ANISOU  707  CG2 ILE A  84     2608   1087    474     20    215   -209       C  
ATOM    708  CD1 ILE A  84       9.035  17.163  13.072  1.00 10.64           C  
ANISOU  708  CD1 ILE A  84     2389   1274    380    100     90    109       C  
ATOM    709  N   THR A  85      14.329  18.854  11.215  1.00  9.77           N  
ANISOU  709  N   THR A  85     2377   1055    278    115    225     43       N  
ATOM    710  CA  THR A  85      15.189  19.262  10.127  1.00 10.49           C  
ANISOU  710  CA  THR A  85     2444   1081    457     76    179    -56       C  
ATOM    711  C   THR A  85      15.436  18.086   9.228  1.00 10.82           C  
ANISOU  711  C   THR A  85     2659   1103    346    -74    313    126       C  
ATOM    712  O   THR A  85      15.122  16.948   9.536  1.00 11.57           O  
ANISOU  712  O   THR A  85     2961   1124    312     80    382     76       O  
ATOM    713  CB  THR A  85      16.516  19.806  10.668  1.00 11.90           C  
ANISOU  713  CB  THR A  85     2349   1282    890     67    190     68       C  
ATOM    714  CG2 THR A  85      16.310  21.130  11.430  1.00 13.66           C  
ANISOU  714  CG2 THR A  85     2763   1377   1048    -13     34   -533       C  
ATOM    715  OG1 THR A  85      17.107  18.788  11.482  1.00 14.64           O  
ANISOU  715  OG1 THR A  85     2938   1672    949    247   -108   -146       O  
ATOM    716  N   LEU A  86      15.995  18.354   8.051  1.00 12.86           N  
ANISOU  716  N   LEU A  86     3125   1246    513   -154    504    -70       N  
ATOM    717  CA  LEU A  86      16.601  17.316   7.169  1.00 15.17           C  
ANISOU  717  CA  LEU A  86     3254   1450   1057   -287    491   -136       C  
ATOM    718  C   LEU A  86      18.143  17.221   7.410  1.00 17.41           C  
ANISOU  718  C   LEU A  86     3134   1749   1730   -343    742   -138       C  
ATOM    719  O   LEU A  86      18.871  18.272   7.516  1.00 20.25           O  
ANISOU  719  O   LEU A  86     3281   2086   2325   -447    440   -343       O  
ATOM    720  CB  LEU A  86      16.293  17.555   5.747  1.00 16.96           C  
ANISOU  720  CB  LEU A  86     3751   1829    862   -284    625     65       C  
ATOM    721  CG  LEU A  86      14.918  17.177   5.324  1.00 18.07           C  
ANISOU  721  CG  LEU A  86     3407   2113   1346     44    451    552       C  
ATOM    722  CD1 LEU A  86      14.660  17.746   3.919  1.00 19.24           C  
ANISOU  722  CD1 LEU A  86     4077   2199   1032    610    821    508       C  
ATOM    723  CD2 LEU A  86      14.770  15.554   5.177  1.00 16.85           C  
ANISOU  723  CD2 LEU A  86     3522   1860   1017   -150    101    118       C  
ATOM    724  N   ASP A  87      18.658  16.021   7.521  1.00 16.96           N  
ANISOU  724  N   ASP A  87     3047   1974   1420   -378    612   -589       N  
ATOM    725  CA  ASP A  87      20.109  15.792   7.622  1.00 18.78           C  
ANISOU  725  CA  ASP A  87     2972   2385   1778   -416    424   -433       C  
ATOM    726  C   ASP A  87      20.312  14.835   6.510  1.00 15.93           C  
ANISOU  726  C   ASP A  87     2729   2161   1161   -293    409   -390       C  
ATOM    727  O   ASP A  87      20.025  13.679   6.690  1.00 16.93           O  
ANISOU  727  O   ASP A  87     2936   2199   1297   -459    338   -176       O  
ATOM    728  CB  ASP A  87      20.498  15.183   9.009  1.00 21.62           C  
ANISOU  728  CB  ASP A  87     3135   2985   2093   -424    324   -312       C  
ATOM    729  CG  ASP A  87      21.985  14.785   9.120  1.00 26.45           C  
ANISOU  729  CG  ASP A  87     3615   3759   2675   -205    134     16       C  
ATOM    730  OD1 ASP A  87      22.798  15.121   8.236  1.00 31.83           O  
ANISOU  730  OD1 ASP A  87     3504   5031   3557   -408    130    116       O  
ATOM    731  OD2 ASP A  87      22.354  14.104  10.110  1.00 34.08           O1-
ANISOU  731  OD2 ASP A  87     4305   4996   3648     32   -219    154       O1-
ATOM    732  N  AGLY A  88      20.885  15.261   5.390  0.50 15.92           N  
ANISOU  732  N  AGLY A  88     2675   1893   1481   -285    419   -251       N  
ATOM    733  N  BGLY A  88      20.750  15.332   5.351  0.50 15.56           N  
ANISOU  733  N  BGLY A  88     2706   1866   1340   -356    490   -270       N  
ATOM    734  CA AGLY A  88      21.243  14.306   4.386  0.50 15.05           C  
ANISOU  734  CA AGLY A  88     2533   1956   1229   -141    320   -233       C  
ATOM    735  CA BGLY A  88      20.770  14.540   4.168  0.50 14.37           C  
ANISOU  735  CA BGLY A  88     2548   1891   1020   -225    597   -269       C  
ATOM    736  C  AGLY A  88      20.099  13.371   4.053  0.50 13.93           C  
ANISOU  736  C  AGLY A  88     2456   1899    937    -42    272   -197       C  
ATOM    737  C  BGLY A  88      19.362  14.193   3.813  0.50 13.72           C  
ANISOU  737  C  BGLY A  88     2544   1947    721   -159    535   -337       C  
ATOM    738  O  AGLY A  88      20.281  12.171   4.045  0.50 14.78           O  
ANISOU  738  O  AGLY A  88     2679   1847   1089    112    208   -312       O  
ATOM    739  O  BGLY A  88      18.515  15.057   3.727  0.50 14.73           O  
ANISOU  739  O  BGLY A  88     2874   1910    811   -129    472   -160       O  
ATOM    740  N  AGLY A  89      18.909  13.911   3.830  0.50 13.36           N  
ANISOU  740  N  AGLY A  89     2517   1899    659    133    361   -100       N  
ATOM    741  N  BGLY A  89      19.111  12.897   3.673  0.50 12.92           N  
ANISOU  741  N  BGLY A  89     2418   1948    543   -286    603   -274       N  
ATOM    742  CA AGLY A  89      17.786  13.110   3.450  0.50 12.64           C  
ANISOU  742  CA AGLY A  89     2616   1823    364     75    329   -159       C  
ATOM    743  CA BGLY A  89      17.805  12.342   3.417  0.50 13.66           C  
ANISOU  743  CA BGLY A  89     2604   1968    615   -237    315   -493       C  
ATOM    744  C  AGLY A  89      17.002  12.388   4.580  0.50 13.03           C  
ANISOU  744  C  AGLY A  89     2618   1883    448    -76    197   -110       C  
ATOM    745  C  BGLY A  89      17.115  11.873   4.672  0.50 13.01           C  
ANISOU  745  C  BGLY A  89     2505   1780    657   -196    291   -522       C  
ATOM    746  O  AGLY A  89      15.918  11.877   4.306  0.50 12.76           O  
ANISOU  746  O  AGLY A  89     2723   1811    311   -177    -19    -57       O  
ATOM    747  O  BGLY A  89      16.194  11.059   4.605  0.50 14.06           O  
ANISOU  747  O  BGLY A  89     2626   1756    959   -106     93   -850       O  
ATOM    748  N   VAL A  90      17.485  12.388   5.845  1.00 12.85           N  
ANISOU  748  N   VAL A  90     2588   1887    407   -305    314   -274       N  
ATOM    749  CA  VAL A  90      16.844  11.877   7.041  1.00 11.91           C  
ANISOU  749  CA  VAL A  90     2527   1494    503   -199    360   -257       C  
ATOM    750  C   VAL A  90      16.122  13.008   7.730  1.00 10.20           C  
ANISOU  750  C   VAL A  90     2335   1260    278   -129      2   -158       C  
ATOM    751  O   VAL A  90      16.681  14.078   7.957  1.00 11.49           O  
ANISOU  751  O   VAL A  90     2687   1293    386   -241    211    -57       O  
ATOM    752  CB  VAL A  90      17.905  11.318   7.985  1.00 13.19           C  
ANISOU  752  CB  VAL A  90     2715   1481    814    -51    457   -119       C  
ATOM    753  CG1 VAL A  90      17.294  10.815   9.299  1.00 12.81           C  
ANISOU  753  CG1 VAL A  90     2504   1597    765    185    200    126       C  
ATOM    754  CG2 VAL A  90      18.730  10.204   7.371  1.00 16.28           C  
ANISOU  754  CG2 VAL A  90     2897   1632   1655    129    612   -274       C  
ATOM    755  N   LEU A  91      14.845  12.790   8.036  1.00 10.13           N  
ANISOU  755  N   LEU A  91     2329   1252    265   -226     72   -106       N  
ATOM    756  CA  LEU A  91      14.115  13.753   8.850  1.00 10.08           C  
ANISOU  756  CA  LEU A  91     2431   1105    292    -10     94    173       C  
ATOM    757  C   LEU A  91      14.498  13.524  10.301  1.00  9.40           C  
ANISOU  757  C   LEU A  91     2351    928    293    138    230    114       C  
ATOM    758  O   LEU A  91      14.336  12.412  10.813  1.00 10.22           O  
ANISOU  758  O   LEU A  91     2645    969    267    122    183      4       O  
ATOM    759  CB  LEU A  91      12.601  13.570   8.708  1.00 12.48           C  
ANISOU  759  CB  LEU A  91     2736   1381    624   -147     74    284       C  
ATOM    760  CG  LEU A  91      11.964  14.174   7.449  1.00 13.17           C  
ANISOU  760  CG  LEU A  91     2834   1722    446     29     41    -64       C  
ATOM    761  CD1 LEU A  91      10.578  13.621   7.325  1.00 16.74           C  
ANISOU  761  CD1 LEU A  91     2881   2401   1077     -1   -158    -26       C  
ATOM    762  CD2 LEU A  91      11.948  15.694   7.605  1.00 13.25           C  
ANISOU  762  CD2 LEU A  91     3004   1071    957    227     18    255       C  
ATOM    763  N   VAL A  92      15.014  14.556  10.946  1.00  9.66           N  
ANISOU  763  N   VAL A  92     2405   1005    258    149     75     48       N  
ATOM    764  CA  VAL A  92      15.483  14.459  12.351  1.00  9.76           C  
ANISOU  764  CA  VAL A  92     2419   1032    254    261    -20     23       C  
ATOM    765  C   VAL A  92      14.595  15.313  13.206  1.00  9.83           C  
ANISOU  765  C   VAL A  92     2528    921    285    220     11     34       C  
ATOM    766  O   VAL A  92      14.541  16.539  13.011  1.00 10.95           O  
ANISOU  766  O   VAL A  92     2792   1015    351    171    220     48       O  
ATOM    767  CB  VAL A  92      16.955  14.929  12.419  1.00 11.03           C  
ANISOU  767  CB  VAL A  92     2488   1343    360    227      4   -120       C  
ATOM    768  CG1 VAL A  92      17.476  14.826  13.868  1.00 13.01           C  
ANISOU  768  CG1 VAL A  92     2786   1735    420    180    -60    -44       C  
ATOM    769  CG2 VAL A  92      17.876  14.098  11.497  1.00 13.47           C  
ANISOU  769  CG2 VAL A  92     2646   1753    719     68     68   -237       C  
ATOM    770  N   HIS A  93      13.929  14.671  14.149  1.00  9.82           N  
ANISOU  770  N   HIS A  93     2567    868    294    255    185    116       N  
ATOM    771  CA  HIS A  93      12.891  15.311  14.989  1.00  9.58           C  
ANISOU  771  CA  HIS A  93     2393    947    298    360    124    175       C  
ATOM    772  C   HIS A  93      13.346  15.258  16.416  1.00  9.68           C  
ANISOU  772  C   HIS A  93     2493    919    266    338    -23     85       C  
ATOM    773  O   HIS A  93      13.465  14.185  17.007  1.00 10.49           O  
ANISOU  773  O   HIS A  93     2784    939    259    211    -89     40       O  
ATOM    774  CB  HIS A  93      11.628  14.553  14.802  1.00 10.07           C  
ANISOU  774  CB  HIS A  93     2390   1161    272    484     98    132       C  
ATOM    775  CG  HIS A  93      10.444  14.969  15.564  1.00 10.27           C  
ANISOU  775  CG  HIS A  93     2296   1214    390    385      4    251       C  
ATOM    776  CD2 HIS A  93      10.221  15.937  16.510  1.00 11.87           C  
ANISOU  776  CD2 HIS A  93     2663   1340    505    516    120    367       C  
ATOM    777  ND1 HIS A  93       9.252  14.318  15.363  1.00 13.49           N  
ANISOU  777  ND1 HIS A  93     2471   1830    823    479    254    561       N  
ATOM    778  CE1 HIS A  93       8.350  14.848  16.162  1.00 13.77           C  
ANISOU  778  CE1 HIS A  93     2271   2135    825    417    484    849       C  
ATOM    779  NE2 HIS A  93       8.898  15.854  16.843  1.00 14.78           N  
ANISOU  779  NE2 HIS A  93     2844   1929    840    492    414    716       N  
ATOM    780  N   VAL A  94      13.710  16.410  16.988  1.00  9.83           N  
ANISOU  780  N   VAL A  94     2547    904    284    229    -22    116       N  
ATOM    781  CA  VAL A  94      14.165  16.495  18.374  1.00  9.97           C  
ANISOU  781  CA  VAL A  94     2385   1126    274    227    -30    113       C  
ATOM    782  C   VAL A  94      13.052  17.057  19.201  1.00  9.51           C  
ANISOU  782  C   VAL A  94     2427    904    281    118    -63    127       C  
ATOM    783  O   VAL A  94      12.511  18.106  18.892  1.00 11.10           O  
ANISOU  783  O   VAL A  94     2791   1115    309    419    185    214       O  
ATOM    784  CB  VAL A  94      15.460  17.335  18.492  1.00 11.50           C  
ANISOU  784  CB  VAL A  94     2489   1393    488    248     -3     37       C  
ATOM    785  CG1 VAL A  94      15.948  17.367  19.905  1.00 15.55           C  
ANISOU  785  CG1 VAL A  94     2912   2191    802   -123   -406     -1       C  
ATOM    786  CG2 VAL A  94      16.522  16.855  17.524  1.00 16.17           C  
ANISOU  786  CG2 VAL A  94     3008   2187    948    469    203    131       C  
ATOM    787  N   GLN A  95      12.762  16.372  20.309  1.00  9.78           N  
ANISOU  787  N   GLN A  95     2535    913    265    153    -35     84       N  
ATOM    788  CA  GLN A  95      11.742  16.791  21.294  1.00 10.47           C  
ANISOU  788  CA  GLN A  95     2598   1123    256    148    -29     43       C  
ATOM    789  C   GLN A  95      12.420  17.121  22.609  1.00 10.42           C  
ANISOU  789  C   GLN A  95     2735    950    273    148   -199     44       C  
ATOM    790  O   GLN A  95      13.173  16.295  23.145  1.00 11.59           O  
ANISOU  790  O   GLN A  95     2943   1193    268    214   -114    -50       O  
ATOM    791  CB  GLN A  95      10.775  15.656  21.546  1.00 10.58           C  
ANISOU  791  CB  GLN A  95     2574   1185    260    170     -1     82       C  
ATOM    792  CG  GLN A  95       9.942  15.272  20.340  1.00 10.51           C  
ANISOU  792  CG  GLN A  95     2694   1042    256     94    -28    -49       C  
ATOM    793  CD  GLN A  95       8.994  14.100  20.537  1.00 10.33           C  
ANISOU  793  CD  GLN A  95     2399   1097    428    145    159     15       C  
ATOM    794  NE2 GLN A  95       9.313  13.218  21.425  1.00 10.30           N  
ANISOU  794  NE2 GLN A  95     2550   1076    284     -6    -80    152       N  
ATOM    795  OE1 GLN A  95       7.956  13.979  19.793  1.00 13.11           O  
ANISOU  795  OE1 GLN A  95     2524   1729    726     62    -15    143       O  
ATOM    796  N   LYS A  96      12.129  18.263  23.160  1.00 10.91           N  
ANISOU  796  N   LYS A  96     2844   1033    268    111   -195    -10       N  
ATOM    797  CA  LYS A  96      12.683  18.747  24.440  1.00 12.23           C  
ANISOU  797  CA  LYS A  96     2951   1323    374    168   -148   -120       C  
ATOM    798  C   LYS A  96      11.547  18.967  25.438  1.00 12.13           C  
ANISOU  798  C   LYS A  96     3038   1286    285    161    -86    -87       C  
ATOM    799  O   LYS A  96      10.559  19.630  25.130  1.00 13.18           O  
ANISOU  799  O   LYS A  96     3392   1359    254    280    -23    -41       O  
ATOM    800  CB  LYS A  96      13.368  20.080  24.241  1.00 13.53           C  
ANISOU  800  CB  LYS A  96     2815   1738    588    -16   -188   -113       C  
ATOM    801  CG  LYS A  96      14.486  20.154  23.275  1.00 15.82           C  
ANISOU  801  CG  LYS A  96     3255   1819    936     43   -147   -125       C  
ATOM    802  CD  LYS A  96      15.654  19.275  23.580  1.00 17.26           C  
ANISOU  802  CD  LYS A  96     3263   1928   1365    -27   -195    -68       C  
ATOM    803  CE  LYS A  96      16.811  19.555  22.670  1.00 17.81           C  
ANISOU  803  CE  LYS A  96     2944   1969   1851   -331   -232   -263       C  
ATOM    804  NZ  LYS A  96      17.987  18.698  22.917  1.00 18.81           N1+
ANISOU  804  NZ  LYS A  96     3027   2029   2089   -242     -7    -21       N1+
ATOM    805  N   TRP A  97      11.729  18.452  26.651  1.00 13.11           N  
ANISOU  805  N   TRP A  97     3323   1391    265    290    -45    -70       N  
ATOM    806  CA  TRP A  97      10.763  18.681  27.722  1.00 14.56           C  
ANISOU  806  CA  TRP A  97     3467   1741    322    297    -36   -181       C  
ATOM    807  C   TRP A  97      11.409  18.362  29.051  1.00 15.62           C  
ANISOU  807  C   TRP A  97     3777   1875    280    284   -150   -195       C  
ATOM    808  O   TRP A  97      12.221  17.438  29.136  1.00 16.75           O  
ANISOU  808  O   TRP A  97     4067   2023    274    451   -250   -124       O  
ATOM    809  CB  TRP A  97       9.472  17.836  27.554  1.00 14.80           C  
ANISOU  809  CB  TRP A  97     3454   1772    397    280    142    -67       C  
ATOM    810  CG  TRP A  97       9.661  16.387  27.939  1.00 14.34           C  
ANISOU  810  CG  TRP A  97     3378   1524    547    150    372   -118       C  
ATOM    811  CD1 TRP A  97       9.152  15.778  29.026  1.00 16.04           C  
ANISOU  811  CD1 TRP A  97     3706   1828    558    263    612     20       C  
ATOM    812  CD2 TRP A  97      10.432  15.377  27.246  1.00 13.52           C  
ANISOU  812  CD2 TRP A  97     3209   1527    401     97     98    -64       C  
ATOM    813  CE2 TRP A  97      10.332  14.205  28.009  1.00 13.80           C  
ANISOU  813  CE2 TRP A  97     3338   1376    527    -86    175     44       C  
ATOM    814  CE3 TRP A  97      11.191  15.347  26.076  1.00 13.55           C  
ANISOU  814  CE3 TRP A  97     3414   1350    384    -60    144   -126       C  
ATOM    815  NE1 TRP A  97       9.541  14.479  29.091  1.00 15.14           N  
ANISOU  815  NE1 TRP A  97     3657   1724    372    200    366     24       N  
ATOM    816  CZ2 TRP A  97      10.982  13.044  27.666  1.00 13.99           C  
ANISOU  816  CZ2 TRP A  97     3213   1415    688   -153    -18    164       C  
ATOM    817  CZ3 TRP A  97      11.804  14.185  25.736  1.00 13.42           C  
ANISOU  817  CZ3 TRP A  97     3114   1533    450   -176     96   -117       C  
ATOM    818  CH2 TRP A  97      11.715  13.048  26.536  1.00 14.06           C  
ANISOU  818  CH2 TRP A  97     3203   1408    729   -109    148   -344       C  
ATOM    819  N   ASP A  98      11.101  19.161  30.055  1.00 17.52           N  
ANISOU  819  N   ASP A  98     4167   2126    362    288    -75   -327       N  
ATOM    820  CA  ASP A  98      11.525  18.836  31.427  1.00 19.29           C  
ANISOU  820  CA  ASP A  98     4374   2505    450    191   -204   -263       C  
ATOM    821  C   ASP A  98      13.024  18.581  31.533  1.00 19.43           C  
ANISOU  821  C   ASP A  98     4417   2498    467    140   -322   -486       C  
ATOM    822  O   ASP A  98      13.461  17.702  32.307  1.00 22.28           O  
ANISOU  822  O   ASP A  98     4929   2959    578    368   -374   -271       O  
ATOM    823  CB  ASP A  98      10.788  17.591  31.928  1.00 21.97           C  
ANISOU  823  CB  ASP A  98     4716   3010    619     42   -217     59       C  
ATOM    824  N   GLY A  99      13.812  19.314  30.764  1.00 19.49           N  
ANISOU  824  N   GLY A  99     4234   2248    920    168   -432   -522       N  
ATOM    825  CA  GLY A  99      15.246  19.144  30.743  1.00 19.44           C  
ANISOU  825  CA  GLY A  99     4031   2186   1166    -15   -630   -637       C  
ATOM    826  C   GLY A  99      15.768  17.870  30.068  1.00 19.18           C  
ANISOU  826  C   GLY A  99     3883   2237   1166     41   -668   -544       C  
ATOM    827  O   GLY A  99      16.986  17.598  30.095  1.00 22.62           O  
ANISOU  827  O   GLY A  99     3981   2827   1786      6   -943   -741       O  
ATOM    828  N   LYS A 100      14.893  17.116  29.398  1.00 16.96           N  
ANISOU  828  N   LYS A 100     3785   2007    651      0   -651   -373       N  
ATOM    829  CA  LYS A 100      15.170  15.873  28.689  1.00 15.51           C  
ANISOU  829  CA  LYS A 100     3437   1911    543     84   -509   -252       C  
ATOM    830  C   LYS A 100      15.098  16.122  27.192  1.00 13.62           C  
ANISOU  830  C   LYS A 100     3243   1512    419    126   -629    -43       C  
ATOM    831  O   LYS A 100      14.536  17.105  26.740  1.00 14.11           O  
ANISOU  831  O   LYS A 100     3489   1441    431    142   -490    -84       O  
ATOM    832  CB  LYS A 100      14.121  14.852  29.089  1.00 14.92           C  
ANISOU  832  CB  LYS A 100     3577   1781    309    202   -248    -76       C  
ATOM    833  CG  LYS A 100      14.097  14.520  30.641  1.00 19.78           C  
ANISOU  833  CG  LYS A 100     4042   2690    785     22   -313     70       C  
ATOM    834  CD  LYS A 100      12.877  13.656  31.001  1.00 22.24           C  
ANISOU  834  CD  LYS A 100     4151   3198   1100    135    127    399       C  
ATOM    835  CE  LYS A 100      12.645  13.366  32.464  1.00 26.13           C  
ANISOU  835  CE  LYS A 100     4601   3567   1760      3    257    464       C  
ATOM    836  NZ  LYS A 100      11.306  12.728  32.573  1.00 32.12           N1+
ANISOU  836  NZ  LYS A 100     4821   4786   2597     10    116    716       N1+
ATOM    837  N   SER A 101      15.602  15.152  26.436  1.00 12.96           N  
ANISOU  837  N   SER A 101     3234   1198    492     44   -507    -92       N  
ATOM    838  CA  SER A 101      15.579  15.254  24.970  1.00 12.11           C  
ANISOU  838  CA  SER A 101     2864   1340    394     -3   -350     -5       C  
ATOM    839  C   SER A 101      15.509  13.858  24.412  1.00 11.63           C  
ANISOU  839  C   SER A 101     2864   1231    323     46   -309    176       C  
ATOM    840  O   SER A 101      16.111  12.936  24.933  1.00 12.94           O  
ANISOU  840  O   SER A 101     3044   1355    515    119   -486     36       O  
ATOM    841  CB  SER A 101      16.858  15.897  24.513  1.00 13.83           C  
ANISOU  841  CB  SER A 101     3086   1484    684   -176   -287     28       C  
ATOM    842  OG  SER A 101      16.884  16.098  23.152  1.00 15.40           O  
ANISOU  842  OG  SER A 101     3448   1433    968   -278   -174     26       O  
ATOM    843  N   THR A 102      14.758  13.686  23.323  1.00 10.26           N  
ANISOU  843  N   THR A 102     2503   1096    296     24   -291     52       N  
ATOM    844  CA  THR A 102      14.732  12.453  22.544  1.00  9.56           C  
ANISOU  844  CA  THR A 102     2320   1038    271     95   -170     50       C  
ATOM    845  C   THR A 102      14.722  12.839  21.085  1.00  9.54           C  
ANISOU  845  C   THR A 102     2233   1059    331    168   -142     20       C  
ATOM    846  O   THR A 102      14.230  13.899  20.713  1.00 10.45           O  
ANISOU  846  O   THR A 102     2642   1063    263    206    -70     73       O  
ATOM    847  CB  THR A 102      13.528  11.601  22.914  1.00 10.29           C  
ANISOU  847  CB  THR A 102     2501   1133    272    -31   -157    -85       C  
ATOM    848  CG2 THR A 102      12.213  12.195  22.604  1.00 11.61           C  
ANISOU  848  CG2 THR A 102     2771   1192    446    105   -122     24       C  
ATOM    849  OG1 THR A 102      13.615  10.341  22.288  1.00 11.55           O  
ANISOU  849  OG1 THR A 102     2650   1066    672    -51    -53     21       O  
ATOM    850  N   THR A 103      15.314  11.983  20.244  1.00 10.04           N  
ANISOU  850  N   THR A 103     2516    942    354    259   -120     85       N  
ATOM    851  CA  THR A 103      15.401  12.212  18.803  1.00 10.19           C  
ANISOU  851  CA  THR A 103     2541   1069    259    163     25     68       C  
ATOM    852  C   THR A 103      14.776  11.055  18.055  1.00 10.18           C  
ANISOU  852  C   THR A 103     2667    942    259    247    -49     51       C  
ATOM    853  O   THR A 103      15.020   9.889  18.333  1.00 11.52           O  
ANISOU  853  O   THR A 103     3104    910    361    262   -251     38       O  
ATOM    854  CB  THR A 103      16.868  12.400  18.394  1.00 11.80           C  
ANISOU  854  CB  THR A 103     2666   1179    637    150      5    -81       C  
ATOM    855  CG2 THR A 103      16.983  12.631  16.900  1.00 13.89           C  
ANISOU  855  CG2 THR A 103     3030   1749    496     45    303     70       C  
ATOM    856  OG1 THR A 103      17.395  13.536  19.051  1.00 15.15           O  
ANISOU  856  OG1 THR A 103     2914   1899    941   -222     60     48       O  
ATOM    857  N   ILE A 104      13.894  11.429  17.122  1.00  9.95           N  
ANISOU  857  N   ILE A 104     2656    840    284    180   -114    113       N  
ATOM    858  CA  ILE A 104      13.209  10.487  16.255  1.00 10.13           C  
ANISOU  858  CA  ILE A 104     2661    920    266     94     83     87       C  
ATOM    859  C   ILE A 104      13.715  10.741  14.839  1.00  9.55           C  
ANISOU  859  C   ILE A 104     2550    807    271    270     80     97       C  
ATOM    860  O   ILE A 104      13.578  11.839  14.339  1.00 10.37           O  
ANISOU  860  O   ILE A 104     2722    963    255    374     46     38       O  
ATOM    861  CB  ILE A 104      11.701  10.675  16.292  1.00 10.65           C  
ANISOU  861  CB  ILE A 104     2711   1054    280    115     42    148       C  
ATOM    862  CG1 ILE A 104      11.170  10.513  17.721  1.00 12.49           C  
ANISOU  862  CG1 ILE A 104     2740   1527    478     77    345    169       C  
ATOM    863  CG2 ILE A 104      11.001   9.668  15.341  1.00 13.18           C  
ANISOU  863  CG2 ILE A 104     2901   1625    479     52    -35     -6       C  
ATOM    864  CD1 ILE A 104       9.922  11.280  17.918  1.00 18.56           C  
ANISOU  864  CD1 ILE A 104     3063   2828   1161    314    670    314       C  
ATOM    865  N   LYS A 105      14.333   9.759  14.223  1.00  9.15           N  
ANISOU  865  N   LYS A 105     2409    805    261    154     63     63       N  
ATOM    866  CA  LYS A 105      14.793   9.846  12.851  1.00  9.58           C  
ANISOU  866  CA  LYS A 105     2415    970    253     89     27    -13       C  
ATOM    867  C   LYS A 105      13.902   9.041  11.949  1.00  9.50           C  
ANISOU  867  C   LYS A 105     2419    930    259    -25    -17     54       C  
ATOM    868  O   LYS A 105      13.518   7.928  12.286  1.00 11.20           O  
ANISOU  868  O   LYS A 105     3044    936    274   -126   -161     53       O  
ATOM    869  CB  LYS A 105      16.242   9.382  12.725  1.00 10.88           C  
ANISOU  869  CB  LYS A 105     2509   1369    254     59    -32     19       C  
ATOM    870  CG  LYS A 105      17.256  10.368  13.422  1.00 14.79           C  
ANISOU  870  CG  LYS A 105     2591   1945   1083    182   -168   -139       C  
ATOM    871  CD  LYS A 105      18.697  10.013  13.246  1.00 20.24           C  
ANISOU  871  CD  LYS A 105     2680   3003   2005    -86   -144     18       C  
ATOM    872  CE  LYS A 105      19.624  11.020  13.881  1.00 23.24           C  
ANISOU  872  CE  LYS A 105     3009   3060   2761   -164   -270    312       C  
ATOM    873  NZ  LYS A 105      21.053  10.597  13.664  1.00 28.01           N1+
ANISOU  873  NZ  LYS A 105     3406   3683   3550   -195    -53    201       N1+
ATOM    874  N   ARG A 106      13.590   9.594  10.786  1.00  9.67           N  
ANISOU  874  N   ARG A 106     2438    962    272    -14     23    116       N  
ATOM    875  CA  ARG A 106      12.744   8.911   9.783  1.00 10.19           C  
ANISOU  875  CA  ARG A 106     2426   1177    266   -212    119     68       C  
ATOM    876  C   ARG A 106      13.537   8.894   8.458  1.00 10.01           C  
ANISOU  876  C   ARG A 106     2436   1021    345   -172     42     33       C  
ATOM    877  O   ARG A 106      13.987   9.930   8.011  1.00 10.19           O  
ANISOU  877  O   ARG A 106     2564   1051    255   -146     69     -4       O  
ATOM    878  CB  ARG A 106      11.405   9.622   9.663  1.00 11.07           C  
ANISOU  878  CB  ARG A 106     2525   1417    262   -246     51     88       C  
ATOM    879  CG  ARG A 106      10.625   9.606  10.962  1.00 12.10           C  
ANISOU  879  CG  ARG A 106     2550   1684    363    -69    138    148       C  
ATOM    880  CD  ARG A 106       9.345  10.379  10.922  1.00 15.46           C  
ANISOU  880  CD  ARG A 106     2698   2704    470   -222    142     82       C  
ATOM    881  NE  ARG A 106       8.519  10.310  12.123  1.00 15.77           N  
ANISOU  881  NE  ARG A 106     2728   2724    537   -187    180    176       N  
ATOM    882  CZ  ARG A 106       8.440  11.241  13.061  1.00 15.21           C  
ANISOU  882  CZ  ARG A 106     2414   2708    655     89    202    252       C  
ATOM    883  NH1 ARG A 106       9.258  12.257  13.098  1.00 14.73           N1+
ANISOU  883  NH1 ARG A 106     2681   2127    787    276    215    267       N1+
ATOM    884  NH2 ARG A 106       7.574  11.093  14.032  1.00 17.19           N  
ANISOU  884  NH2 ARG A 106     2660   3233    635   -150    441    -15       N  
ATOM    885  N   LYS A 107      13.664   7.714   7.894  1.00 10.02           N  
ANISOU  885  N   LYS A 107     2510    998    298   -201    134     19       N  
ATOM    886  CA  LYS A 107      14.490   7.555   6.670  1.00 11.22           C  
ANISOU  886  CA  LYS A 107     2513   1292    457   -217    174   -122       C  
ATOM    887  C   LYS A 107      13.873   6.520   5.783  1.00 10.78           C  
ANISOU  887  C   LYS A 107     2516   1308    269   -299    135     70       C  
ATOM    888  O   LYS A 107      13.360   5.506   6.213  1.00 13.52           O  
ANISOU  888  O   LYS A 107     3326   1549    259   -573    131    -42       O  
ATOM    889  CB  LYS A 107      15.925   7.157   7.018  1.00 14.04           C  
ANISOU  889  CB  LYS A 107     2685   1884    763   -107    167   -412       C  
ATOM    890  CG  LYS A 107      16.926   7.188   5.891  1.00 17.03           C  
ANISOU  890  CG  LYS A 107     2983   2249   1238   -163     50   -534       C  
ATOM    891  CD  LYS A 107      18.336   6.788   6.317  1.00 20.32           C  
ANISOU  891  CD  LYS A 107     3135   2810   1774     76    129   -756       C  
ATOM    892  CE  LYS A 107      19.383   7.281   5.294  1.00 23.25           C  
ANISOU  892  CE  LYS A 107     3561   3243   2028   -146    313  -1019       C  
ATOM    893  NZ  LYS A 107      18.827   7.316   3.942  1.00 31.66           N1+
ANISOU  893  NZ  LYS A 107     4459   4633   2938   -166    -27   -285       N1+
ATOM    894  N   ARG A 108      13.927   6.760   4.481  1.00 10.87           N  
ANISOU  894  N   ARG A 108     2462   1394    274   -222    190    -25       N  
ATOM    895  CA  ARG A 108      13.528   5.764   3.492  1.00 11.79           C  
ANISOU  895  CA  ARG A 108     2481   1675    322   -180    160     33       C  
ATOM    896  C   ARG A 108      14.614   4.709   3.329  1.00 12.80           C  
ANISOU  896  C   ARG A 108     2481   1868    512   -223    179   -211       C  
ATOM    897  O   ARG A 108      15.775   5.041   3.091  1.00 14.69           O  
ANISOU  897  O   ARG A 108     2759   1798   1021   -139    279   -639       O  
ATOM    898  CB  ARG A 108      13.243   6.412   2.160  1.00 13.65           C  
ANISOU  898  CB  ARG A 108     2745   2054    385   -218    191    147       C  
ATOM    899  CG  ARG A 108      11.922   7.092   2.131  1.00 15.19           C  
ANISOU  899  CG  ARG A 108     3083   2072    615      5    -52    571       C  
ATOM    900  CD  ARG A 108      10.726   6.146   2.215  1.00 17.77           C  
ANISOU  900  CD  ARG A 108     2739   2895   1118    -81   -172    996       C  
ATOM    901  NE  ARG A 108      10.849   5.056   1.209  1.00 20.48           N  
ANISOU  901  NE  ARG A 108     2966   2882   1932    -81   -360    807       N  
ATOM    902  CZ  ARG A 108      10.547   5.192  -0.079  1.00 17.57           C  
ANISOU  902  CZ  ARG A 108     2872   1611   2192    -92   -456    126       C  
ATOM    903  NH1 ARG A 108      10.015   6.289  -0.615  1.00 18.23           N1+
ANISOU  903  NH1 ARG A 108     3305   2548   1070    -88   -659    369       N1+
ATOM    904  NH2 ARG A 108      10.757   4.177  -0.887  1.00 21.70           N  
ANISOU  904  NH2 ARG A 108     3199   2711   2334    202   -399   -369       N  
ATOM    905  N   GLU A 109      14.210   3.444   3.354  1.00 11.97           N  
ANISOU  905  N   GLU A 109     2465   1685    396    -72    170   -292       N  
ATOM    906  CA  GLU A 109      15.117   2.317   3.099  1.00 12.87           C  
ANISOU  906  CA  GLU A 109     2596   1835    456    -60     61   -237       C  
ATOM    907  C   GLU A 109      14.358   1.338   2.232  1.00 12.42           C  
ANISOU  907  C   GLU A 109     2538   1580    598     18    160   -183       C  
ATOM    908  O   GLU A 109      13.355   0.774   2.684  1.00 12.35           O  
ANISOU  908  O   GLU A 109     2674   1729    288   -209    198   -182       O  
ATOM    909  CB  GLU A 109      15.503   1.627   4.418  1.00 14.27           C  
ANISOU  909  CB  GLU A 109     2728   2009    685     89    -70    -47       C  
ATOM    910  CG  GLU A 109      16.238   2.535   5.396  1.00 18.33           C  
ANISOU  910  CG  GLU A 109     3081   2663   1219    106   -376   -171       C  
ATOM    911  CD  GLU A 109      17.654   2.778   5.022  1.00 22.49           C  
ANISOU  911  CD  GLU A 109     3567   3407   1569    -69     44   -439       C  
ATOM    912  OE1 GLU A 109      18.355   3.467   5.780  1.00 26.66           O  
ANISOU  912  OE1 GLU A 109     3759   3946   2422   -383    149   -759       O  
ATOM    913  OE2 GLU A 109      18.095   2.284   3.983  1.00 28.36           O1-
ANISOU  913  OE2 GLU A 109     4269   4024   2481    162    549   -734       O1-
ATOM    914  N   ASP A 110      14.789   1.170   0.989  1.00 11.55           N  
ANISOU  914  N   ASP A 110     2568   1523    296    -10    249   -111       N  
ATOM    915  CA  ASP A 110      14.044   0.357   0.047  1.00 11.42           C  
ANISOU  915  CA  ASP A 110     2659   1404    276   -110    230    -41       C  
ATOM    916  C   ASP A 110      12.632   0.877  -0.021  1.00 10.90           C  
ANISOU  916  C   ASP A 110     2404   1469    267   -111    146    -82       C  
ATOM    917  O   ASP A 110      12.471   2.109  -0.129  1.00 11.77           O  
ANISOU  917  O   ASP A 110     2666   1540    264    -16    156    -31       O  
ATOM    918  CB  ASP A 110      14.178  -1.131   0.354  1.00 11.93           C  
ANISOU  918  CB  ASP A 110     2720   1454    358     62    248   -113       C  
ATOM    919  CG  ASP A 110      15.592  -1.611   0.303  1.00 15.41           C  
ANISOU  919  CG  ASP A 110     2997   1978    877     46    258    163       C  
ATOM    920  OD1 ASP A 110      16.326  -1.157  -0.565  1.00 18.50           O  
ANISOU  920  OD1 ASP A 110     3141   2338   1548    386    532    177       O  
ATOM    921  OD2 ASP A 110      15.967  -2.490   1.110  1.00 23.23           O1-
ANISOU  921  OD2 ASP A 110     3586   2983   2255    625     50   1115       O1-
ATOM    922  N   ASP A 111      11.595   0.079   0.032  1.00 11.98           N  
ANISOU  922  N   ASP A 111     2690   1571    290    -20    115   -204       N  
ATOM    923  CA  ASP A 111      10.235   0.559  -0.024  1.00 12.40           C  
ANISOU  923  CA  ASP A 111     2679   1731    298   -101     57   -149       C  
ATOM    924  C   ASP A 111       9.658   0.901   1.356  1.00 12.58           C  
ANISOU  924  C   ASP A 111     2594   1660    526    -44     73   -299       C  
ATOM    925  O   ASP A 111       8.456   1.137   1.464  1.00 15.60           O  
ANISOU  925  O   ASP A 111     2750   2487    686     66     32   -688       O  
ATOM    926  CB  ASP A 111       9.345  -0.446  -0.760  1.00 12.60           C  
ANISOU  926  CB  ASP A 111     2627   1887    272    -64    -19   -174       C  
ATOM    927  CG  ASP A 111       9.665  -0.523  -2.240  1.00 13.54           C  
ANISOU  927  CG  ASP A 111     2953   1753    438    -63     37   -187       C  
ATOM    928  OD1 ASP A 111       9.894   0.535  -2.843  1.00 15.32           O  
ANISOU  928  OD1 ASP A 111     3512   1809    498   -220      9    -69       O  
ATOM    929  OD2 ASP A 111       9.669  -1.615  -2.781  1.00 16.36           O1-
ANISOU  929  OD2 ASP A 111     3936   1791    487   -187    268   -304       O1-
ATOM    930  N   LYS A 112      10.485   0.874   2.390  1.00 11.44           N  
ANISOU  930  N   LYS A 112     2577   1495    275    -43    198    -85       N  
ATOM    931  CA  LYS A 112      10.046   1.104   3.739  1.00 11.22           C  
ANISOU  931  CA  LYS A 112     2613   1355    295    -52    306    -55       C  
ATOM    932  C   LYS A 112      10.371   2.489   4.192  1.00 10.62           C  
ANISOU  932  C   LYS A 112     2399   1349    286    -72    254     49       C  
ATOM    933  O   LYS A 112      11.232   3.161   3.661  1.00 11.21           O  
ANISOU  933  O   LYS A 112     2523   1432    302   -182    173    -39       O  
ATOM    934  CB  LYS A 112      10.714   0.080   4.654  1.00 12.86           C  
ANISOU  934  CB  LYS A 112     2999   1546    342    100    443   -122       C  
ATOM    935  CG  LYS A 112      10.359  -1.334   4.263  1.00 17.60           C  
ANISOU  935  CG  LYS A 112     3575   1908   1202    221    640   -166       C  
ATOM    936  CD  LYS A 112      11.010  -2.390   5.006  1.00 23.96           C  
ANISOU  936  CD  LYS A 112     4323   2956   1824    553    519   -310       C  
ATOM    937  CE  LYS A 112      10.685  -3.763   4.368  1.00 28.47           C  
ANISOU  937  CE  LYS A 112     4782   3188   2845    284    212   -342       C  
ATOM    938  NZ  LYS A 112      11.634  -4.794   4.775  1.00 31.43           N1+
ANISOU  938  NZ  LYS A 112     5314   4009   2615    382   -224    -86       N1+
ATOM    939  N   LEU A 113       9.712   2.878   5.264  1.00 10.00           N  
ANISOU  939  N   LEU A 113     2377   1159    264   -107    154      2       N  
ATOM    940  CA  LEU A 113      10.030   4.088   6.007  1.00  9.84           C  
ANISOU  940  CA  LEU A 113     2300   1183    255   -132     61     23       C  
ATOM    941  C   LEU A 113      10.395   3.619   7.434  1.00 10.08           C  
ANISOU  941  C   LEU A 113     2391   1119    317   -191    271     29       C  
ATOM    942  O   LEU A 113       9.586   3.006   8.107  1.00 11.11           O  
ANISOU  942  O   LEU A 113     2476   1480    263   -269    125     42       O  
ATOM    943  CB  LEU A 113       8.840   5.046   5.983  1.00 11.19           C  
ANISOU  943  CB  LEU A 113     2530   1364    357   -241     69   -103       C  
ATOM    944  CG  LEU A 113       9.049   6.444   6.662  1.00 14.06           C  
ANISOU  944  CG  LEU A 113     2786   1843    713    -90    -89   -415       C  
ATOM    945  CD1 LEU A 113       7.884   7.345   6.237  1.00 16.70           C  
ANISOU  945  CD1 LEU A 113     3025   2001   1317    329   -184   -101       C  
ATOM    946  CD2 LEU A 113       9.253   6.482   8.054  1.00 17.47           C  
ANISOU  946  CD2 LEU A 113     3172   2423   1042    108     95    108       C  
ATOM    947  N   VAL A 114      11.669   3.797   7.774  1.00  9.88           N  
ANISOU  947  N   VAL A 114     2257   1234    261   -169     65     70       N  
ATOM    948  CA  VAL A 114      12.188   3.326   9.083  1.00 10.41           C  
ANISOU  948  CA  VAL A 114     2414   1229    309   -177    -29    207       C  
ATOM    949  C   VAL A 114      12.225   4.513  10.021  1.00 11.18           C  
ANISOU  949  C   VAL A 114     2542   1396    310   -308     86    205       C  
ATOM    950  O   VAL A 114      12.707   5.602   9.685  1.00 11.79           O  
ANISOU  950  O   VAL A 114     2723   1449    306   -372    140     14       O  
ATOM    951  CB  VAL A 114      13.574   2.730   8.892  1.00 12.47           C  
ANISOU  951  CB  VAL A 114     2607   1487    645   -122     -7    268       C  
ATOM    952  CG1 VAL A 114      14.142   2.208  10.181  1.00 13.88           C  
ANISOU  952  CG1 VAL A 114     2856   1799    615    138    -79    350       C  
ATOM    953  CG2 VAL A 114      13.547   1.568   7.854  1.00 14.86           C  
ANISOU  953  CG2 VAL A 114     2968   1661   1017    256    258   -202       C  
ATOM    954  N   VAL A 115      11.711   4.270  11.227  1.00 11.20           N  
ANISOU  954  N   VAL A 115     2772   1194    288   -287    -52    182       N  
ATOM    955  CA  VAL A 115      11.635   5.259  12.301  1.00 10.92           C  
ANISOU  955  CA  VAL A 115     2696   1117    335   -270   -209     24       C  
ATOM    956  C   VAL A 115      12.514   4.775  13.440  1.00 10.70           C  
ANISOU  956  C   VAL A 115     2677   1102    283   -235   -170    138       C  
ATOM    957  O   VAL A 115      12.264   3.721  14.020  1.00 13.93           O  
ANISOU  957  O   VAL A 115     3270   1458    563   -576   -462    358       O  
ATOM    958  CB  VAL A 115      10.194   5.472  12.730  1.00 11.60           C  
ANISOU  958  CB  VAL A 115     2764   1349    293   -292   -169     30       C  
ATOM    959  CG1 VAL A 115      10.068   6.582  13.782  1.00 13.97           C  
ANISOU  959  CG1 VAL A 115     3063   1901    342   -112   -287   -122       C  
ATOM    960  CG2 VAL A 115       9.310   5.790  11.537  1.00 13.12           C  
ANISOU  960  CG2 VAL A 115     2779   1565    641   -445   -209    193       C  
ATOM    961  N   GLU A 116      13.548   5.534  13.759  1.00 10.15           N  
ANISOU  961  N   GLU A 116     2608    978    270   -199    -83    106       N  
ATOM    962  CA AGLU A 116      14.484   5.206  14.857  0.50 10.37           C  
ANISOU  962  CA AGLU A 116     2650    908    380     24    -98    117       C  
ATOM    963  CA BGLU A 116      14.458   5.210  14.866  0.50 10.92           C  
ANISOU  963  CA BGLU A 116     2672    956    521    -34   -112     87       C  
ATOM    964  C   GLU A 116      14.266   6.222  15.961  1.00  9.95           C  
ANISOU  964  C   GLU A 116     2554    941    285     44   -219     18       C  
ATOM    965  O   GLU A 116      14.465   7.409  15.739  1.00 11.58           O  
ANISOU  965  O   GLU A 116     3145    982    271     97    -71     34       O  
ATOM    966  CB AGLU A 116      15.938   5.242  14.337  0.50 12.43           C  
ANISOU  966  CB AGLU A 116     2820   1074    826    128    -58     17       C  
ATOM    967  CB BGLU A 116      15.902   5.297  14.411  0.50 13.33           C  
ANISOU  967  CB BGLU A 116     2839   1227    995     22    -99     19       C  
ATOM    968  CG AGLU A 116      17.017   4.875  15.363  0.50 13.22           C  
ANISOU  968  CG AGLU A 116     2807   1571    645    442    169    418       C  
ATOM    969  CG BGLU A 116      16.502   4.098  13.766  0.50 16.39           C  
ANISOU  969  CG BGLU A 116     2924   1612   1689    -12    102    150       C  
ATOM    970  CD AGLU A 116      18.407   5.538  15.141  0.50 18.16           C  
ANISOU  970  CD AGLU A 116     3208   2229   1460    156     26    132       C  
ATOM    971  CD BGLU A 116      18.013   4.073  14.066  0.50 20.78           C  
ANISOU  971  CD BGLU A 116     3073   2657   2163    137    -62    -73       C  
ATOM    972  OE1AGLU A 116      18.536   6.798  15.082  0.50 19.19           O  
ANISOU  972  OE1AGLU A 116     3237   2377   1675    179    291    483       O  
ATOM    973  OE1BGLU A 116      18.579   5.084  14.547  0.50 22.55           O  
ANISOU  973  OE1BGLU A 116     2967   3444   2154    393   -580   -322       O  
ATOM    974  OE2AGLU A 116      19.399   4.788  15.041  0.50 19.99           O1-
ANISOU  974  OE2AGLU A 116     3224   3091   1280    219    310    422       O1-
ATOM    975  OE2BGLU A 116      18.637   3.045  13.805  0.50 22.11           O1-
ANISOU  975  OE2BGLU A 116     3369   2867   2162    540   -131    345       O1-
ATOM    976  N   CYS A 117      13.872   5.744  17.136  1.00 10.08           N  
ANISOU  976  N   CYS A 117     2572    945    313     98   -130    152       N  
ATOM    977  CA  CYS A 117      13.590   6.569  18.288  1.00 10.43           C  
ANISOU  977  CA  CYS A 117     2585    947    429    220   -148    -42       C  
ATOM    978  C   CYS A 117      14.719   6.344  19.289  1.00 10.43           C  
ANISOU  978  C   CYS A 117     2610   1015    336    220   -160     38       C  
ATOM    979  O   CYS A 117      14.939   5.214  19.697  1.00 11.37           O  
ANISOU  979  O   CYS A 117     2867   1009    442    131   -389     66       O  
ATOM    980  CB  CYS A 117      12.231   6.141  18.917  1.00 12.20           C  
ANISOU  980  CB  CYS A 117     2701   1616    317    404   -291    -46       C  
ATOM    981  SG  CYS A 117      10.844   6.160  17.765  1.00 16.58           S  
ANISOU  981  SG  CYS A 117     2916   2711    673    272   -204    328       S  
ATOM    982  N   VAL A 118      15.369   7.402  19.714  1.00 10.58           N  
ANISOU  982  N   VAL A 118     2549   1036    434    200   -151     42       N  
ATOM    983  CA  VAL A 118      16.542   7.307  20.563  1.00 11.24           C  
ANISOU  983  CA  VAL A 118     2533   1014    723    171    -89    -70       C  
ATOM    984  C   VAL A 118      16.374   8.159  21.810  1.00 11.61           C  
ANISOU  984  C   VAL A 118     2530   1047    833    225   -214     28       C  
ATOM    985  O   VAL A 118      16.043   9.346  21.731  1.00 11.70           O  
ANISOU  985  O   VAL A 118     2879   1052    513    231   -155    -13       O  
ATOM    986  CB  VAL A 118      17.839   7.702  19.796  1.00 13.96           C  
ANISOU  986  CB  VAL A 118     2644   1354   1304     15      0    -80       C  
ATOM    987  CG1 VAL A 118      19.018   7.678  20.700  1.00 18.35           C  
ANISOU  987  CG1 VAL A 118     2722   2030   2219    -55      6   -280       C  
ATOM    988  CG2 VAL A 118      18.056   6.805  18.593  1.00 16.06           C  
ANISOU  988  CG2 VAL A 118     2921   1741   1438    -47    506   -258       C  
ATOM    989  N   MET A 119      16.604   7.552  22.971  1.00 12.29           N  
ANISOU  989  N   MET A 119     2737   1113    819    280   -361     88       N  
ATOM    990  CA  MET A 119      16.628   8.307  24.252  1.00 13.64           C  
ANISOU  990  CA  MET A 119     2958   1282    940    216   -500     46       C  
ATOM    991  C   MET A 119      17.831   7.706  24.966  1.00 14.41           C  
ANISOU  991  C   MET A 119     2835   1558   1079    184   -441   -103       C  
ATOM    992  O   MET A 119      17.846   6.546  25.355  1.00 13.94           O  
ANISOU  992  O   MET A 119     2950   1400    944    279   -560    -51       O  
ATOM    993  CB  MET A 119      15.299   8.034  25.010  1.00 14.83           C  
ANISOU  993  CB  MET A 119     3090   1848    695    459   -468   -181       C  
ATOM    994  CG  MET A 119      15.181   8.461  26.442  1.00 17.07           C  
ANISOU  994  CG  MET A 119     3742   1802    941     18   -380     38       C  
ATOM    995  SD  MET A 119      14.822  10.194  26.368  1.00 23.10           S  
ANISOU  995  SD  MET A 119     5376   1873   1528    865  -1441   -468       S  
ATOM    996  CE  MET A 119      14.873  10.868  27.989  1.00 18.84           C  
ANISOU  996  CE  MET A 119     4256   1561   1340    -55   -342   -102       C  
ATOM    997  N  ALYS A 120      18.860   8.502  25.253  0.50 17.56           N  
ANISOU  997  N  ALYS A 120     3014   1852   1805    110   -372     11       N  
ATOM    998  N  BLYS A 120      18.833   8.561  25.058  0.50 15.24           N  
ANISOU  998  N  BLYS A 120     2793   1578   1420    140   -398     -7       N  
ATOM    999  CA ALYS A 120      20.056   8.077  26.030  0.50 19.93           C  
ANISOU  999  CA ALYS A 120     2998   2353   2221     54   -254     -5       C  
ATOM   1000  CA BLYS A 120      20.072   8.244  25.612  0.50 15.06           C  
ANISOU 1000  CA BLYS A 120     2619   1693   1408     54   -336    151       C  
ATOM   1001  C  ALYS A 120      20.472   6.617  26.031  0.50 19.32           C  
ANISOU 1001  C  ALYS A 120     2917   2311   2111     25   -221    -33       C  
ATOM   1002  C  BLYS A 120      20.636   7.019  24.885  0.50 12.36           C  
ANISOU 1002  C  BLYS A 120     2378   1323    992     36   -362    188       C  
ATOM   1003  O  ALYS A 120      20.377   5.919  27.042  0.50 21.04           O  
ANISOU 1003  O  ALYS A 120     3176   2582   2236   -105   -246   -181       O  
ATOM   1004  O  BLYS A 120      20.775   6.992  23.650  0.50 13.32           O  
ANISOU 1004  O  BLYS A 120     2488   1339   1232    107    -98    490       O  
ATOM   1005  CB ALYS A 120      19.939   8.467  27.484  0.50 20.55           C  
ANISOU 1005  CB ALYS A 120     3049   2409   2350    136   -273    -44       C  
ATOM   1006  CB BLYS A 120      19.872   8.015  27.130  0.50 13.94           C  
ANISOU 1006  CB BLYS A 120     2646   1381   1269     45   -520      2       C  
ATOM   1007  CG ALYS A 120      18.722   8.034  28.195  0.50 20.92           C  
ANISOU 1007  CG ALYS A 120     3073   2522   2351    131   -415     63       C  
ATOM   1008  CG BLYS A 120      19.397   9.311  27.931  0.50 16.02           C  
ANISOU 1008  CG BLYS A 120     2633   2077   1376    262   -679   -234       C  
ATOM   1009  CD ALYS A 120      18.245   9.251  28.926  0.50 23.16           C  
ANISOU 1009  CD ALYS A 120     3308   2783   2708    201   -323    -63       C  
ATOM   1010  CD BLYS A 120      19.145   8.908  29.380  0.50 19.90           C  
ANISOU 1010  CD BLYS A 120     3125   2627   1807     73   -571   -354       C  
ATOM   1011  CE ALYS A 120      19.447   9.927  29.526  0.50 25.15           C  
ANISOU 1011  CE ALYS A 120     3477   3126   2951    -10   -225    108       C  
ATOM   1012  CE BLYS A 120      18.698  10.057  30.253  0.50 22.72           C  
ANISOU 1012  CE BLYS A 120     3304   3156   2172     12   -129   -378       C  
ATOM   1013  NZ ALYS A 120      20.101   9.020  30.501  0.50 26.28           N1+
ANISOU 1013  NZ ALYS A 120     3899   3398   2686    -34   -268    258       N1+
ATOM   1014  NZ BLYS A 120      19.715  10.422  31.270  0.50 24.58           N1+
ANISOU 1014  NZ BLYS A 120     3601   3076   2661    -73   -421   -193       N1+
ATOM   1015  N  AGLY A 121      21.022   6.189  24.912  0.50 18.52           N  
ANISOU 1015  N  AGLY A 121     2763   2329   1943     48   -164     -2       N  
ATOM   1016  N  BGLY A 121      20.935   5.940  25.615  0.50 13.01           N  
ANISOU 1016  N  BGLY A 121     2299   1582   1061    104   -239    333       N  
ATOM   1017  CA AGLY A 121      21.542   4.864  24.769  0.50 17.31           C  
ANISOU 1017  CA AGLY A 121     2620   2085   1868     36   -122    114       C  
ATOM   1018  CA BGLY A 121      21.525   4.784  25.004  0.50 14.87           C  
ANISOU 1018  CA BGLY A 121     2401   1765   1483     60   -173    242       C  
ATOM   1019  C   GLY A 121      20.507   3.822  24.406  1.00 13.86           C  
ANISOU 1019  C   GLY A 121     2363   1801   1101     85   -206    188       C  
ATOM   1020  O   GLY A 121      20.877   2.763  23.972  1.00 14.92           O  
ANISOU 1020  O   GLY A 121     2485   1831   1352    287     57    351       O  
ATOM   1021  N   VAL A 122      19.215   4.133  24.519  1.00 12.64           N  
ANISOU 1021  N   VAL A 122     2479   1478    846     99   -205    262       N  
ATOM   1022  CA  VAL A 122      18.141   3.196  24.132  1.00 11.27           C  
ANISOU 1022  CA  VAL A 122     2367   1253    663    262   -153    216       C  
ATOM   1023  C   VAL A 122      17.535   3.591  22.808  1.00 11.35           C  
ANISOU 1023  C   VAL A 122     2343   1167    800    157   -209    161       C  
ATOM   1024  O   VAL A 122      17.065   4.728  22.658  1.00 12.27           O  
ANISOU 1024  O   VAL A 122     2793   1184    684    322   -405     85       O  
ATOM   1025  CB  VAL A 122      17.055   3.116  25.223  1.00 12.33           C  
ANISOU 1025  CB  VAL A 122     2416   1473    796    234   -122    164       C  
ATOM   1026  CG1 VAL A 122      16.000   2.173  24.790  1.00 14.92           C  
ANISOU 1026  CG1 VAL A 122     2501   1906   1260     82     82    262       C  
ATOM   1027  CG2 VAL A 122      17.661   2.699  26.559  1.00 14.98           C  
ANISOU 1027  CG2 VAL A 122     2864   1989    836    391    -19    471       C  
ATOM   1028  N   THR A 123      17.552   2.669  21.850  1.00 11.41           N  
ANISOU 1028  N   THR A 123     2413   1134    786    172   -264    128       N  
ATOM   1029  CA  THR A 123      16.997   2.850  20.536  1.00 11.34           C  
ANISOU 1029  CA  THR A 123     2431   1270    606    200   -243    116       C  
ATOM   1030  C   THR A 123      15.821   1.906  20.315  1.00 10.97           C  
ANISOU 1030  C   THR A 123     2441    930    794    134   -351      5       C  
ATOM   1031  O   THR A 123      15.891   0.738  20.678  1.00 14.84           O  
ANISOU 1031  O   THR A 123     2887   1161   1587     39   -555    383       O  
ATOM   1032  CB  THR A 123      18.046   2.603  19.494  1.00 13.52           C  
ANISOU 1032  CB  THR A 123     2663   1628    844    139    -62     63       C  
ATOM   1033  CG2 THR A 123      17.482   2.772  18.064  1.00 15.20           C  
ANISOU 1033  CG2 THR A 123     2980   2083    709    196    123    142       C  
ATOM   1034  OG1 THR A 123      19.104   3.528  19.695  1.00 17.28           O  
ANISOU 1034  OG1 THR A 123     3197   2035   1333   -135    493    -58       O  
ATOM   1035  N   SER A 124      14.796   2.392  19.690  1.00 11.18           N  
ANISOU 1035  N   SER A 124     2547   1163    536     25   -371    220       N  
ATOM   1036  CA  SER A 124      13.762   1.572  19.133  1.00 11.24           C  
ANISOU 1036  CA  SER A 124     2525   1115    627    -22   -330    334       C  
ATOM   1037  C   SER A 124      13.669   1.784  17.651  1.00 10.51           C  
ANISOU 1037  C   SER A 124     2395   1092    506     79   -154    161       C  
ATOM   1038  O   SER A 124      13.704   2.910  17.172  1.00 12.38           O  
ANISOU 1038  O   SER A 124     3198   1046    460    -70   -172    188       O  
ATOM   1039  CB  SER A 124      12.394   1.871  19.770  1.00 11.30           C  
ANISOU 1039  CB  SER A 124     2575   1222    493    -78   -212    313       C  
ATOM   1040  OG  SER A 124      11.311   1.208  19.171  1.00 12.17           O  
ANISOU 1040  OG  SER A 124     2614   1447    561    -16    -85    114       O  
ATOM   1041  N   THR A 125      13.514   0.719  16.893  1.00 10.09           N  
ANISOU 1041  N   THR A 125     2436    953    443    -67   -222    249       N  
ATOM   1042  CA  THR A 125      13.347   0.749  15.450  1.00  9.95           C  
ANISOU 1042  CA  THR A 125     2232   1237    308     79    -34    230       C  
ATOM   1043  C   THR A 125      11.961   0.282  15.085  1.00 10.22           C  
ANISOU 1043  C   THR A 125     2379   1212    291   -110   -141    134       C  
ATOM   1044  O   THR A 125      11.562  -0.839  15.438  1.00 12.01           O  
ANISOU 1044  O   THR A 125     2743   1198    621   -277   -224    210       O  
ATOM   1045  CB  THR A 125      14.425  -0.093  14.777  1.00 12.87           C  
ANISOU 1045  CB  THR A 125     2513   1616    759    223    -25     18       C  
ATOM   1046  CG2 THR A 125      14.275  -0.064  13.230  1.00 15.67           C  
ANISOU 1046  CG2 THR A 125     3010   2168    776    281    182    163       C  
ATOM   1047  OG1 THR A 125      15.733   0.388  15.139  1.00 15.31           O  
ANISOU 1047  OG1 THR A 125     2508   1965   1344    270    265    -49       O  
ATOM   1048  N   ARG A 126      11.251   1.134  14.352  1.00 10.26           N  
ANISOU 1048  N   ARG A 126     2249   1292    356   -188    -24    192       N  
ATOM   1049  CA  ARG A 126       9.885   0.878  13.931  1.00 10.42           C  
ANISOU 1049  CA  ARG A 126     2333   1304    321   -326     -3    261       C  
ATOM   1050  C   ARG A 126       9.836   0.987  12.408  1.00 10.61           C  
ANISOU 1050  C   ARG A 126     2346   1396    288   -335    -34    199       C  
ATOM   1051  O   ARG A 126      10.283   1.969  11.843  1.00 13.91           O  
ANISOU 1051  O   ARG A 126     3278   1676    330   -784   -147    275       O  
ATOM   1052  CB  ARG A 126       8.943   1.868  14.601  1.00 12.07           C  
ANISOU 1052  CB  ARG A 126     2311   1862    410   -216    -94    232       C  
ATOM   1053  CG  ARG A 126       8.895   1.533  16.090  1.00 14.77           C  
ANISOU 1053  CG  ARG A 126     2755   2318    539     44    -75      6       C  
ATOM   1054  CD  ARG A 126       8.177   2.447  16.934  1.00 16.54           C  
ANISOU 1054  CD  ARG A 126     2918   2586    778     75   -147    380       C  
ATOM   1055  NE  ARG A 126       6.766   2.736  16.699  1.00 16.96           N  
ANISOU 1055  NE  ARG A 126     2851   2920    671    -72     62    -42       N  
ATOM   1056  CZ  ARG A 126       5.719   2.121  17.266  1.00 15.41           C  
ANISOU 1056  CZ  ARG A 126     2713   2500    640   -399    -77    -33       C  
ATOM   1057  NH1 ARG A 126       5.819   0.955  17.900  1.00 16.40           N1+
ANISOU 1057  NH1 ARG A 126     3112   2645    470   -186   -222     46       N1+
ATOM   1058  NH2 ARG A 126       4.547   2.646  17.143  1.00 16.99           N  
ANISOU 1058  NH2 ARG A 126     2899   2580    973   -502     65    136       N  
ATOM   1059  N   VAL A 127       9.312  -0.027  11.752  1.00  9.75           N  
ANISOU 1059  N   VAL A 127     2312   1122    268   -198     37    106       N  
ATOM   1060  CA  VAL A 127       9.348  -0.107  10.283  1.00 10.20           C  
ANISOU 1060  CA  VAL A 127     2190   1409    277    -48    168     98       C  
ATOM   1061  C   VAL A 127       7.941  -0.001   9.785  1.00  9.62           C  
ANISOU 1061  C   VAL A 127     2177   1181    296      3    174    -12       C  
ATOM   1062  O   VAL A 127       7.038  -0.720  10.210  1.00 10.80           O  
ANISOU 1062  O   VAL A 127     2358   1467    278   -148     43    106       O  
ATOM   1063  CB  VAL A 127       9.971  -1.414   9.841  1.00 11.77           C  
ANISOU 1063  CB  VAL A 127     2459   1513    500    131    -92    104       C  
ATOM   1064  CG1 VAL A 127       9.937  -1.494   8.284  1.00 14.40           C  
ANISOU 1064  CG1 VAL A 127     2989   1992    487    267     14   -167       C  
ATOM   1065  CG2 VAL A 127      11.368  -1.545  10.373  1.00 15.59           C  
ANISOU 1065  CG2 VAL A 127     2743   2174   1004    301    -53     32       C  
ATOM   1066  N   TYR A 128       7.754   0.946   8.863  1.00 10.02           N  
ANISOU 1066  N   TYR A 128     2303   1183    321    -85     19     68       N  
ATOM   1067  CA  TYR A 128       6.483   1.159   8.180  1.00  9.65           C  
ANISOU 1067  CA  TYR A 128     2143   1253    268   -104     80    102       C  
ATOM   1068  C   TYR A 128       6.609   0.760   6.696  1.00 10.56           C  
ANISOU 1068  C   TYR A 128     2261   1256    494    -59    -45    -18       C  
ATOM   1069  O   TYR A 128       7.657   0.957   6.078  1.00 11.48           O  
ANISOU 1069  O   TYR A 128     2462   1563    334   -165     91   -164       O  
ATOM   1070  CB  TYR A 128       6.074   2.622   8.233  1.00  9.59           C  
ANISOU 1070  CB  TYR A 128     2158   1199    286   -112      9    175       C  
ATOM   1071  CG  TYR A 128       5.661   3.134   9.616  1.00  9.71           C  
ANISOU 1071  CG  TYR A 128     2354   1071    263   -126    -34     89       C  
ATOM   1072  CD1 TYR A 128       6.600   3.405  10.595  1.00 11.15           C  
ANISOU 1072  CD1 TYR A 128     2393   1293    551    -72   -133     26       C  
ATOM   1073  CD2 TYR A 128       4.329   3.352   9.919  1.00 10.31           C  
ANISOU 1073  CD2 TYR A 128     2272   1069    574    -43     22    191       C  
ATOM   1074  CE1 TYR A 128       6.190   3.911  11.861  1.00 11.83           C  
ANISOU 1074  CE1 TYR A 128     2604   1552    337   -127   -141   -150       C  
ATOM   1075  CE2 TYR A 128       3.917   3.849  11.134  1.00 11.43           C  
ANISOU 1075  CE2 TYR A 128     2375   1391    575    -80    248      3       C  
ATOM   1076  CZ  TYR A 128       4.838   4.126  12.092  1.00 11.26           C  
ANISOU 1076  CZ  TYR A 128     2496   1329    453   -169     78     63       C  
ATOM   1077  OH  TYR A 128       4.402   4.599  13.311  1.00 14.08           O  
ANISOU 1077  OH  TYR A 128     2821   2107    422     63    186   -180       O  
ATOM   1078  N   GLU A 129       5.534   0.219   6.171  1.00 11.31           N  
ANISOU 1078  N   GLU A 129     2391   1456    447   -273    -28   -147       N  
ATOM   1079  CA AGLU A 129       5.380  -0.132   4.759  0.50 11.39           C  
ANISOU 1079  CA AGLU A 129     2382   1423    522    -79    -60   -399       C  
ATOM   1080  CA BGLU A 129       5.485   0.000   4.718  0.50 11.97           C  
ANISOU 1080  CA BGLU A 129     2481   1525    539    -72   -106   -373       C  
ATOM   1081  C   GLU A 129       4.289   0.727   4.166  1.00 10.98           C  
ANISOU 1081  C   GLU A 129     2353   1453    365   -158    -63   -246       C  
ATOM   1082  O   GLU A 129       3.444   1.205   4.857  1.00 11.46           O  
ANISOU 1082  O   GLU A 129     2522   1298    533    -38   -108    -76       O  
ATOM   1083  CB AGLU A 129       5.016  -1.616   4.649  0.50 12.45           C  
ANISOU 1083  CB AGLU A 129     2445   1543    742   -105    -68   -362       C  
ATOM   1084  CB BGLU A 129       5.483  -1.483   4.358  0.50 13.55           C  
ANISOU 1084  CB BGLU A 129     2731   1639    778     23   -208   -247       C  
ATOM   1085  CG AGLU A 129       6.234  -2.518   4.929  0.50 16.98           C  
ANISOU 1085  CG AGLU A 129     3152   2085   1213    151   -371   -418       C  
ATOM   1086  CG BGLU A 129       4.223  -2.207   4.799  0.50 17.95           C  
ANISOU 1086  CG BGLU A 129     3138   2260   1421   -229   -288   -394       C  
ATOM   1087  CD AGLU A 129       5.995  -3.950   4.588  0.50 21.61           C  
ANISOU 1087  CD AGLU A 129     3957   2285   1968     53   -396   -444       C  
ATOM   1088  CD BGLU A 129       4.238  -3.738   4.509  0.50 22.48           C  
ANISOU 1088  CD BGLU A 129     3890   2520   2132   -204   -427   -458       C  
ATOM   1089  OE1AGLU A 129       5.208  -4.198   3.644  0.50 24.00           O  
ANISOU 1089  OE1AGLU A 129     4700   2393   2025     -8   -629   -481       O  
ATOM   1090  OE1BGLU A 129       3.164  -4.296   4.248  0.50 24.75           O  
ANISOU 1090  OE1BGLU A 129     4267   2436   2701   -416   -332   -252       O  
ATOM   1091  OE2AGLU A 129       6.574  -4.808   5.285  0.50 25.35           O1-
ANISOU 1091  OE2AGLU A 129     4717   2766   2149    244   -558   -575       O1-
ATOM   1092  OE2BGLU A 129       5.311  -4.378   4.557  0.50 23.84           O1-
ANISOU 1092  OE2BGLU A 129     4338   2440   2279   -105   -571   -698       O1-
ATOM   1093  N   ARG A 130       4.247   0.845   2.841  1.00 12.39           N  
ANISOU 1093  N   ARG A 130     2664   1652    389    -92   -141   -352       N  
ATOM   1094  CA  ARG A 130       3.153   1.551   2.203  1.00 12.69           C  
ANISOU 1094  CA  ARG A 130     2665   1660    494    -64   -143   -153       C  
ATOM   1095  C   ARG A 130       1.843   0.883   2.486  1.00 13.49           C  
ANISOU 1095  C   ARG A 130     2664   1720    739   -145   -343   -210       C  
ATOM   1096  O   ARG A 130       1.722  -0.356   2.378  1.00 15.91           O  
ANISOU 1096  O   ARG A 130     3167   1460   1418    -55   -649   -226       O  
ATOM   1097  CB  ARG A 130       3.357   1.634   0.711  1.00 14.77           C  
ANISOU 1097  CB  ARG A 130     2784   2411    418   -130   -225   -146       C  
ATOM   1098  CG  ARG A 130       4.555   2.356   0.336  1.00 16.70           C  
ANISOU 1098  CG  ARG A 130     3200   2524    621   -209    -20    352       C  
ATOM   1099  CD  ARG A 130       4.264   3.781   0.216  1.00 19.29           C  
ANISOU 1099  CD  ARG A 130     3263   2415   1650   -185   -320   -214       C  
ATOM   1100  NE  ARG A 130       5.418   4.476  -0.342  1.00 20.01           N  
ANISOU 1100  NE  ARG A 130     3363   2054   2183    -84   -337    312       N  
ATOM   1101  CZ  ARG A 130       5.490   5.782  -0.530  1.00 16.19           C  
ANISOU 1101  CZ  ARG A 130     3076   1983   1092    -71   -273    133       C  
ATOM   1102  NH1 ARG A 130       4.450   6.504  -0.351  1.00 16.77           N1+
ANISOU 1102  NH1 ARG A 130     3245   2213    913    -69   -165     70       N1+
ATOM   1103  NH2 ARG A 130       6.626   6.322  -0.899  1.00 19.62           N  
ANISOU 1103  NH2 ARG A 130     3530   2656   1265   -115    244    500       N  
ATOM   1104  N   ALA A 131       0.815   1.660   2.769  1.00 15.10           N  
ANISOU 1104  N   ALA A 131     2719   1744   1274   -197   -385   -224       N  
ATOM   1105  CA  ALA A 131      -0.490   1.075   3.058  1.00 18.72           C  
ANISOU 1105  CA  ALA A 131     2899   2130   2083   -258   -336   -128       C  
ATOM   1106  C   ALA A 131      -1.124   0.543   1.782  1.00 21.44           C  
ANISOU 1106  C   ALA A 131     3196   2358   2590   -340   -350   -139       C  
ATOM   1107  O   ALA A 131      -0.721   0.956   0.699  1.00 22.42           O  
ANISOU 1107  O   ALA A 131     3348   2640   2530   -369   -808    -41       O  
ATOM   1108  CB  ALA A 131      -1.377   2.088   3.806  1.00 21.27           C  
ANISOU 1108  CB  ALA A 131     3064   2482   2533   -292    -95   -144       C  
TER   
HETATM 1109  CAAAFBZ A 133       7.319   8.707  17.358  0.50 19.36           C  
ANISOU 1109  CAAAFBZ A 133     3012   2713   1631    150    -18   1043       C  
HETATM 1110  CAABFBZ A 133       7.670   8.115  17.789  0.50 17.24           C  
ANISOU 1110  CAABFBZ A 133     3225   1893   1431    253   -353   -716       C  
HETATM 1111  CADAFBZ A 133       6.004   7.792  22.273  0.50 20.69           C  
ANISOU 1111  CADAFBZ A 133     2930   2673   2255    130    189   -210       C  
HETATM 1112  CADBFBZ A 133       5.407   7.397  22.237  0.50 17.14           C  
ANISOU 1112  CADBFBZ A 133     3194   2117   1199    421   -295   -579       C  
HETATM 1113  CAEAFBZ A 133       5.131   8.523  21.468  0.50 21.30           C  
ANISOU 1113  CAEAFBZ A 133     3075   2862   2155    117    219     -2       C  
HETATM 1114  CAEBFBZ A 133       4.440   7.066  21.291  0.50 17.59           C  
ANISOU 1114  CAEBFBZ A 133     3120   2252   1310    451   -230   -420       C  
HETATM 1115  CAFAFBZ A 133       6.979   7.028  21.642  0.50 20.05           C  
ANISOU 1115  CAFAFBZ A 133     2984   2874   1760    290   -144   -268       C  
HETATM 1116  CAFBFBZ A 133       6.672   7.775  21.776  0.50 17.72           C  
ANISOU 1116  CAFBFBZ A 133     3163   2376   1192    196   -531   -857       C  
HETATM 1117  CAGAFBZ A 133       5.206   8.521  20.079  0.50 20.59           C  
ANISOU 1117  CAGAFBZ A 133     3099   2590   2134    167     58   -167       C  
HETATM 1118  CAGBFBZ A 133       4.700   7.125  19.931  0.50 17.27           C  
ANISOU 1118  CAGBFBZ A 133     2999   2270   1289    374   -324   -275       C  
HETATM 1119  CAHAFBZ A 133       7.051   7.021  20.243  0.50 20.23           C  
ANISOU 1119  CAHAFBZ A 133     3111   2835   1738    151   -156   -511       C  
HETATM 1120  CAHBFBZ A 133       6.941   7.835  20.406  0.50 18.60           C  
ANISOU 1120  CAHBFBZ A 133     3253   2568   1244    361   -582   -615       C  
HETATM 1121  CAIAFBZ A 133       6.523   6.357  17.312  0.50 19.46           C  
ANISOU 1121  CAIAFBZ A 133     3373   2155   1863    184    168    228       C  
HETATM 1122  CAIBFBZ A 133       6.179   6.138  17.358  0.50 16.08           C  
ANISOU 1122  CAIBFBZ A 133     3130   2063    916    351   -325   -576       C  
HETATM 1123  CAJAFBZ A 133       5.988   6.129  15.874  0.50 18.80           C  
ANISOU 1123  CAJAFBZ A 133     3635   1802   1703     51    173    480       C  
HETATM 1124  CAJBFBZ A 133       6.014   6.112  15.824  0.50 15.91           C  
ANISOU 1124  CAJBFBZ A 133     3290   1898    855    277   -295   -517       C  
HETATM 1125  CAKAFBZ A 133       6.184   7.770  19.438  0.50 20.10           C  
ANISOU 1125  CAKAFBZ A 133     3134   2494   2006    179     -6   -143       C  
HETATM 1126  CAKBFBZ A 133       5.960   7.510  19.488  0.50 16.42           C  
ANISOU 1126  CAKBFBZ A 133     2972   2233   1032    427   -415   -613       C  
HETATM 1127  CALAFBZ A 133       6.241   7.766  17.885  0.50 20.53           C  
ANISOU 1127  CALAFBZ A 133     3282   2401   2117     73    249     88       C  
HETATM 1128  CALBFBZ A 133       6.267   7.554  18.001  0.50 16.96           C  
ANISOU 1128  CALBFBZ A 133     3272   2246    927    322   -177   -853       C  
HETATM 1129  OABAFBZ A 133       5.635   7.109  15.177  0.50 18.90           O  
ANISOU 1129  OABAFBZ A 133     3578   1772   1828     60    219    283       O  
HETATM 1130  OABBFBZ A 133       5.676   7.157  15.235  0.50 17.64           O  
ANISOU 1130  OABBFBZ A 133     3420   2075   1207    274    -84   -257       O  
HETATM 1131  OACAFBZ A 133       5.926   4.939  15.490  0.50 19.29           O  
ANISOU 1131  OACAFBZ A 133     3884   1939   1503    297     93     -5       O  
HETATM 1132  OACBFBZ A 133       6.126   5.002  15.267  0.50 16.26           O  
ANISOU 1132  OACBFBZ A 133     3781   1949    448    709   -541   -494       O  
HETATM 1133  O   HOH A 134      10.455  22.054  12.801  1.00  9.68           O  
ANISOU 1133  O   HOH A 134     2346   1032    298     45     18     73       O  
HETATM 1134  O   HOH A 135      18.691   0.008  22.066  1.00 11.73           O  
ANISOU 1134  O   HOH A 135     2394   1239    823    208    -75     84       O  
HETATM 1135  O   HOH A 136       2.745  -7.735  16.893  1.00 39.72           O  
ANISOU 1135  O   HOH A 136     6034   4803   4253   1312   -836  -1828       O  
HETATM 1136  O   HOH A 137       6.281  23.748  -4.014  1.00 42.77           O  
ANISOU 1136  O   HOH A 137     4664   6272   5315    424   -230    801       O  
HETATM 1137  O   HOH A 138       7.220  24.848  12.379  1.00 11.52           O  
ANISOU 1137  O   HOH A 138     2225   1593    556    -37     48   -320       O  
HETATM 1138  O   HOH A 139      20.117  16.981  24.217  1.00 45.36           O  
ANISOU 1138  O   HOH A 139     5173   4090   7971   -240  -1532    969       O  
HETATM 1139  O   HOH A 140      -3.785  -0.601  22.289  1.00 12.93           O  
ANISOU 1139  O   HOH A 140     2556   1621    733   -248    -88    246       O  
HETATM 1140  O   HOH A 141       1.107  20.239   5.139  1.00 14.89           O  
ANISOU 1140  O   HOH A 141     2782   2004    870   -116   -207    314       O  
HETATM 1141  O   HOH A 142      -3.731  -1.145  19.583  1.00 13.97           O  
ANISOU 1141  O   HOH A 142     2408   1806   1092   -441     74    246       O  
HETATM 1142  O   HOH A 143      -8.225   5.546  21.604  1.00 45.80           O  
ANISOU 1142  O   HOH A 143     3725   7987   5688  -1237    405   1498       O  
HETATM 1143  O   HOH A 144       8.595  21.595  26.655  1.00 68.64           O  
ANISOU 1143  O   HOH A 144    16849   5599   3630   2524  -2319  -1690       O  
HETATM 1144  O   HOH A 145       6.313  19.934  29.712  1.00105.05           O  
ANISOU 1144  O   HOH A 145    18034  17780   4099   5741   1291    523       O  
HETATM 1145  O   HOH A 146      11.877  12.407  12.160  1.00 11.51           O  
ANISOU 1145  O   HOH A 146     2748   1231    393    123    233     60       O  
HETATM 1146  O   HOH A 147       1.800   3.883  19.630  1.00 34.68           O  
ANISOU 1146  O   HOH A 147     5302   4951   2923    257    258   1324       O  
HETATM 1147  O   HOH A 148      -6.866   5.144  23.866  1.00 88.16           O  
ANISOU 1147  O   HOH A 148    18241   8832   6422  -5580   3262  -3958       O  
HETATM 1148  O   HOH A 149      -3.562   3.185  28.808  1.00 30.99           O  
ANISOU 1148  O   HOH A 149     4917   3846   3008     28  -1140    135       O  
HETATM 1149  O   HOH A 150       9.781  23.013   5.438  1.00 13.95           O  
ANISOU 1149  O   HOH A 150     2600   2210    490    315    -50     42       O  
HETATM 1150  O   HOH A 151       0.049  -2.559   9.802  1.00 32.86           O  
ANISOU 1150  O   HOH A 151     3717   4612   4156  -1244   -745   1379       O  
HETATM 1151  O   HOH A 152      -4.667  -2.372  24.206  1.00 11.83           O  
ANISOU 1151  O   HOH A 152     2446   1503    545    -64    -81    240       O  
HETATM 1152  O   HOH A 153       1.710   5.759   0.130  1.00 16.90           O  
ANISOU 1152  O   HOH A 153     3593   2000    827   -349   -194   -246       O  
HETATM 1153  O   HOH A 154      -4.982   3.751  30.948  1.00 36.04           O  
ANISOU 1153  O   HOH A 154     6273   3634   3786    261    997    466       O  
HETATM 1154  O   HOH A 155       4.704  -3.545  16.263  1.00 53.00           O  
ANISOU 1154  O   HOH A 155     5425   4837   9873   1097  -2017   1278       O  
HETATM 1155  O   HOH A 156       3.114   8.276  30.910  1.00 25.74           O  
ANISOU 1155  O   HOH A 156     4468   2662   2650    436    512    553       O  
HETATM 1156  O   HOH A 157       3.521  11.395  19.314  1.00 16.02           O  
ANISOU 1156  O   HOH A 157     2856   2219   1010   -187    270    197       O  
HETATM 1157  O   HOH A 158       8.872  10.506  21.424  1.00 14.52           O  
ANISOU 1157  O   HOH A 158     3166   1609    741   -185    258    124       O  
HETATM 1158  O   HOH A 159       8.845  -3.027  20.091  1.00 17.71           O  
ANISOU 1158  O   HOH A 159     3454   2242   1030     88    -20   -322       O  
HETATM 1159  O   HOH A 160      -0.597  14.332   6.411  1.00 15.73           O  
ANISOU 1159  O   HOH A 160     3253   1653   1070      1   -225     27       O  
HETATM 1160  O   HOH A 161      21.846   9.918   5.449  1.00 33.20           O  
ANISOU 1160  O   HOH A 161     3712   5216   3683    299   1009   -633       O  
HETATM 1161  O   HOH A 162      12.453  10.484  31.531  1.00140.81           O  
ANISOU 1161  O   HOH A 162    30132  15157   8212 -11415   -858  -1690       O  
HETATM 1162  O   HOH A 163       1.703  15.760  -0.147  1.00 18.93           O  
ANISOU 1162  O   HOH A 163     4462   2096    636   -169   -683   -221       O  
HETATM 1163  O   HOH A 164       5.886  -7.408  13.349  1.00 38.42           O  
ANISOU 1163  O   HOH A 164     5616   2630   6351   -947  -2048   1162       O  
HETATM 1164  O   HOH A 165      18.177   0.833   1.685  1.00 37.98           O  
ANISOU 1164  O   HOH A 165     3872   8216   2342    -62    673   -448       O  
HETATM 1165  O   HOH A 166       4.406  -4.502  26.339  1.00 44.34           O  
ANISOU 1165  O   HOH A 166     7158   7231   2457   1185   1131    281       O  
HETATM 1166  O   HOH A 167      16.210  18.837  14.202  1.00 17.80           O  
ANISOU 1166  O   HOH A 167     3592   2059   1111   -140   -233    -62       O  
HETATM 1167  O   HOH A 168      13.106  21.646  19.888  1.00 17.62           O  
ANISOU 1167  O   HOH A 168     3297   2814    583   -253    -89     27       O  
HETATM 1168  O   HOH A 169       6.396  11.418  19.573  1.00 15.88           O  
ANISOU 1168  O   HOH A 169     2864   1791   1377   -144    148     56       O  
HETATM 1169  O   HOH A 170      13.100  12.122  -3.273  1.00 63.91           O  
ANISOU 1169  O   HOH A 170    11696   7126   5460  -1740   -757    145       O  
HETATM 1170  O   HOH A 171      16.389  21.123   7.295  1.00 18.19           O  
ANISOU 1170  O   HOH A 171     3855   1614   1442   -412     78    207       O  
HETATM 1171  O   HOH A 172      15.233   9.057   3.243  1.00 18.25           O  
ANISOU 1171  O   HOH A 172     3906   1883   1145   -558    488    118       O  
HETATM 1172  O   HOH A 173       4.141  27.136   2.505  1.00 17.62           O  
ANISOU 1172  O   HOH A 173     3271   2043   1381     51   -209     17       O  
HETATM 1173  O   HOH A 174      14.490   0.676  31.721  1.00 29.44           O  
ANISOU 1173  O   HOH A 174     4880   4072   2233   -133   -265    932       O  
HETATM 1174  O   HOH A 175      20.161  20.241  14.212  1.00 25.36           O  
ANISOU 1174  O   HOH A 175     4523   2671   2441     53    116   -326       O  
HETATM 1175  O   HOH A 176       1.429   2.512  -2.579  1.00 39.05           O  
ANISOU 1175  O   HOH A 176     6417   6156   2263    787   -471  -1260       O  
HETATM 1176  O   HOH A 177      -5.951   3.201  27.293  1.00 29.56           O  
ANISOU 1176  O   HOH A 177     3773   3339   4117   -360   -237   -523       O  
HETATM 1177  O   HOH A 178      11.465  -3.105  13.710  1.00 19.03           O  
ANISOU 1177  O   HOH A 178     4403   1803   1023   -232    -49     84       O  
HETATM 1178  O   HOH A 179      14.045  -2.182  31.402  1.00 35.61           O  
ANISOU 1178  O   HOH A 179     5368   4648   3513   1101   1456    554       O  
HETATM 1179  O   HOH A 180       2.902  13.842  18.210  1.00 19.96           O  
ANISOU 1179  O   HOH A 180     3123   2095   2365   -285     50    275       O  
HETATM 1180  O   HOH A 181      18.960  17.860  14.834  1.00 30.91           O  
ANISOU 1180  O   HOH A 181     4741   3266   3736   -324   -871    201       O  
HETATM 1181  O   HOH A 182       2.622   6.759  13.707  1.00 20.31           O  
ANISOU 1181  O   HOH A 182     3374   1935   2408   -330    882   -275       O  
HETATM 1182  O   HOH A 183      19.778  20.030   4.928  1.00 46.93           O  
ANISOU 1182  O   HOH A 183     7244   3389   7196   -726  -1552   -203       O  
HETATM 1183  O   HOH A 184       2.882   0.886  18.682  1.00 20.72           O  
ANISOU 1183  O   HOH A 184     3034   3932    906  -1233    208   -122       O  
HETATM 1184  O   HOH A 185       1.898  12.695  14.263  1.00 21.31           O  
ANISOU 1184  O   HOH A 185     3925   2828   1343    -98    248   1191       O  
HETATM 1185  O   HOH A 186       1.674  26.185   2.278  1.00 18.15           O  
ANISOU 1185  O   HOH A 186     3239   1843   1813    111    -88   -229       O  
HETATM 1186  O   HOH A 187       7.028  27.670  11.942  1.00 20.26           O  
ANISOU 1186  O   HOH A 187     2962   2669   2065    773   -511   -485       O  
HETATM 1187  O   HOH A 188      -0.644  18.705   3.772  1.00 19.74           O  
ANISOU 1187  O   HOH A 188     3796   1877   1826     73  -1038    105       O  
HETATM 1188  O   HOH A 189       2.973   5.839  16.790  1.00 73.20           O  
ANISOU 1188  O   HOH A 189    13250  10320   4240  -2967   -116  -1820       O  
HETATM 1189  O   HOH A 190      14.722  25.125  17.374  1.00 16.90           O  
ANISOU 1189  O   HOH A 190     2945   1889   1585     -9   -601   -138       O  
HETATM 1190  O   HOH A 191      11.381  -2.746   0.864  1.00 18.74           O  
ANISOU 1190  O   HOH A 191     4166   1762   1193   -260    -44      2       O  
HETATM 1191  O   HOH A 192       2.225   9.807  17.398  1.00 17.93           O  
ANISOU 1191  O   HOH A 192     3281   2407   1123   -220    278     -7       O  
HETATM 1192  O   HOH A 193      11.517  -5.762  21.044  1.00 23.78           O  
ANISOU 1192  O   HOH A 193     4663   1204   3165     74    297    618       O  
HETATM 1193  O   HOH A 194      -6.097   0.823  22.091  1.00 18.77           O  
ANISOU 1193  O   HOH A 194     3086   1637   2405   -265   -867    519       O  
HETATM 1194  O   HOH A 195       0.232   3.005  34.679  1.00 23.81           O  
ANISOU 1194  O   HOH A 195     5753   2599    694    555    216    -73       O  
HETATM 1195  O   HOH A 196      20.255  11.058  20.158  1.00 39.89           O  
ANISOU 1195  O   HOH A 196     5678   3992   5486   -922   -501  -1088       O  
HETATM 1196  O   HOH A 197       6.306  -0.507   1.379  1.00 20.23           O  
ANISOU 1196  O   HOH A 197     3211   2989   1486   -116    412   -605       O  
HETATM 1197  O   HOH A 198       3.500   3.676  35.727  1.00 25.23           O  
ANISOU 1197  O   HOH A 198     5940   2600   1047  -1136   -297    165       O  
HETATM 1198  O   HOH A 199      22.695   6.191  29.193  1.00 43.53           O  
ANISOU 1198  O   HOH A 199     7814   2936   5788    296  -2537    993       O  
HETATM 1199  O  AHOH A 200       1.027  15.694  18.510  0.50 17.42           O  
ANISOU 1199  O  AHOH A 200     3981   2159    479   -410    434    118       O  
HETATM 1200  O  BHOH A 200       0.482  18.580  19.254  0.50 24.34           O  
ANISOU 1200  O  BHOH A 200     3661   2540   3047  -1077  -1852   1651       O  
HETATM 1201  O   HOH A 201      14.779   1.567  29.188  1.00 24.77           O  
ANISOU 1201  O   HOH A 201     3790   4471   1149   1031   -585    595       O  
HETATM 1202  O   HOH A 202       2.196  -3.676  24.702  1.00 23.80           O  
ANISOU 1202  O   HOH A 202     3329   4081   1630    581   -198   -158       O  
HETATM 1203  O   HOH A 203       8.675  -3.499  22.947  1.00 29.18           O  
ANISOU 1203  O   HOH A 203     6296   2266   2525   -841   1128   -488       O  
HETATM 1204  O   HOH A 204       5.171  22.595  24.114  1.00 24.32           O  
ANISOU 1204  O   HOH A 204     4725   2677   1838   1057    210    -22       O  
HETATM 1205  O   HOH A 205      15.406  19.770  27.364  1.00 24.31           O  
ANISOU 1205  O   HOH A 205     5891   2146   1199   -710   -789   -196       O  
HETATM 1206  O   HOH A 206       0.496   5.041  32.287  1.00 22.73           O  
ANISOU 1206  O   HOH A 206     4770   2785   1081   -279    234    -82       O  
HETATM 1207  O   HOH A 207       0.276   3.416  -0.275  1.00 21.46           O  
ANISOU 1207  O   HOH A 207     3585   2297   2268   -183   -773   -487       O  
HETATM 1208  O   HOH A 208      -1.902  15.884  17.808  1.00 24.41           O  
ANISOU 1208  O   HOH A 208     5391   2321   1560   -276    862   -669       O  
HETATM 1209  O   HOH A 209      17.845  13.911  21.772  1.00 20.67           O  
ANISOU 1209  O   HOH A 209     3594   3068   1192   -228   -111   -433       O  
HETATM 1210  O   HOH A 210      11.324  13.592  -5.357  1.00 45.18           O  
ANISOU 1210  O   HOH A 210     4984   3635   8545   -544   2100  -1355       O  
HETATM 1211  O   HOH A 211       6.576   8.372  12.992  1.00 21.00           O  
ANISOU 1211  O   HOH A 211     3325   3779    874   -575     47    159       O  
HETATM 1212  O   HOH A 212      -2.673  20.049   1.501  1.00 26.72           O  
ANISOU 1212  O   HOH A 212     4875   3601   1676  -2132    204    -53       O  
HETATM 1213  O   HOH A 213      15.386  -2.645   3.840  1.00 38.63           O  
ANISOU 1213  O   HOH A 213     8441   2451   3783    -36   1154   -128       O  
HETATM 1214  O   HOH A 214       2.851  -2.549  17.656  1.00 25.53           O  
ANISOU 1214  O   HOH A 214     4868   3150   1680    656   -754    199       O  
HETATM 1215  O   HOH A 215       7.012  -3.033  30.534  1.00 24.64           O  
ANISOU 1215  O   HOH A 215     6193   1802   1366   -370    955    -12       O  
HETATM 1216  O   HOH A 216       5.016  -1.572  25.409  1.00 23.14           O  
ANISOU 1216  O   HOH A 216     3820   3373   1600    459   -117   -471       O  
HETATM 1217  O   HOH A 217      13.187  21.173  28.471  1.00 25.65           O  
ANISOU 1217  O   HOH A 217     5384   2790   1569    228   -407   -275       O  
HETATM 1218  O   HOH A 218      18.327  11.294  24.301  1.00 31.54           O  
ANISOU 1218  O   HOH A 218     4228   1744   6009    386   -604    296       O  
HETATM 1219  O   HOH A 219       9.022  12.051  30.743  1.00 23.96           O  
ANISOU 1219  O   HOH A 219     5086   2753   1265    -23    643    344       O  
HETATM 1220  O   HOH A 220      17.543  13.416  28.020  1.00 26.60           O  
ANISOU 1220  O   HOH A 220     4312   2814   2980    442  -1092    572       O  
HETATM 1221  O   HOH A 221       4.823  10.044  29.236  1.00 24.29           O  
ANISOU 1221  O   HOH A 221     5723   2548    955   -271    113    504       O  
HETATM 1222  O   HOH A 222      18.765   4.770   2.368  1.00 27.39           O  
ANISOU 1222  O   HOH A 222     6869   3071    464    796   -554   -651       O  
HETATM 1223  O   HOH A 223      17.382   9.039  16.433  1.00 25.12           O  
ANISOU 1223  O   HOH A 223     4397   3151   1995    576     20    637       O  
HETATM 1224  O   HOH A 224      -7.181   9.454  19.644  1.00 33.25           O  
ANISOU 1224  O   HOH A 224     3400   7454   1777     74    429    -49       O  
HETATM 1225  O   HOH A 225      -1.888  20.176  11.480  1.00 35.86           O  
ANISOU 1225  O   HOH A 225     5466   2449   5710   -715   3383   -332       O  
HETATM 1226  O   HOH A 226      18.598  17.341   2.345  1.00 31.17           O  
ANISOU 1226  O   HOH A 226     5497   3667   2679   -220   1450   -733       O  
HETATM 1227  O   HOH A 227      -7.973   6.294  14.894  1.00 38.78           O  
ANISOU 1227  O   HOH A 227     5038   3190   6504  -1106  -1770    837       O  
HETATM 1228  O   HOH A 228       0.186   4.987  18.323  1.00 45.69           O  
ANISOU 1228  O   HOH A 228     6180   5501   5678  -2024  -1767   2338       O  
HETATM 1229  O   HOH A 229       2.408  -5.352  19.808  1.00 34.98           O  
ANISOU 1229  O   HOH A 229     5308   4919   3063    497   -193  -1205       O  
HETATM 1230  O   HOH A 230      -0.562  -5.133  17.441  1.00 33.60           O  
ANISOU 1230  O   HOH A 230     3772   2570   6422    352    968   1176       O  
HETATM 1231  O   HOH A 231      -4.800  11.591  13.359  1.00 33.49           O  
ANISOU 1231  O   HOH A 231     3963   6547   2214   1486    139   1259       O  
HETATM 1232  O   HOH A 232       7.530  -5.977  15.286  1.00 80.48           O  
ANISOU 1232  O   HOH A 232    10538  12355   7686  -6170  -7045   -452       O  
HETATM 1233  O   HOH A 233      19.735  10.033  17.639  1.00 30.90           O  
ANISOU 1233  O   HOH A 233     4804   3603   3332    846   1114    564       O  
HETATM 1234  O   HOH A 234      -7.692   6.520  19.026  1.00 31.28           O  
ANISOU 1234  O   HOH A 234     4084   3847   3953    364    576   -736       O  
HETATM 1235  O   HOH A 235      20.076  16.550  20.290  1.00 52.78           O  
ANISOU 1235  O   HOH A 235     5700   5686   8665    661   -123  -3854       O  
HETATM 1236  O   HOH A 236      23.782  11.638  18.115  1.00 42.02           O  
ANISOU 1236  O   HOH A 236     3294   6129   6542   -283    416  -1169       O  
HETATM 1237  O   HOH A 237       8.726  -6.070  20.158  1.00 34.62           O  
ANISOU 1237  O   HOH A 237     4693   4189   4272    786    664    -11       O  
HETATM 1238  O   HOH A 238       5.338  -1.772  19.859  1.00 36.95           O  
ANISOU 1238  O   HOH A 238     4304   4969   4765  -1778   2222  -2405       O  
HETATM 1239  O   HOH A 239      21.042   5.142  21.515  1.00 30.13           O  
ANISOU 1239  O   HOH A 239     6246   3234   1968   1457   -306    280       O  
HETATM 1240  O   HOH A 240      -6.869  13.782  18.029  1.00 47.09           O  
ANISOU 1240  O   HOH A 240     6348   4508   7036  -1096   2167  -2747       O  
HETATM 1241  O   HOH A 241       9.184  21.238  29.603  1.00 26.02           O  
ANISOU 1241  O   HOH A 241     5215   2969   1702   1136     56   -459       O  
HETATM 1242  O   HOH A 242       0.039   7.893  17.515  1.00 25.91           O  
ANISOU 1242  O   HOH A 242     3869   4367   1608    277    422    489       O  
HETATM 1243  O   HOH A 243      17.722   0.847  13.302  1.00 29.71           O  
ANISOU 1243  O   HOH A 243     3747   3458   4082   -122   1083   -608       O  
HETATM 1244  O   HOH A 244       0.880   7.214  -1.985  1.00 25.47           O  
ANISOU 1244  O   HOH A 244     4313   4119   1245   -197   -529    566       O  
HETATM 1245  O   HOH A 245      15.123   8.320  -0.936  1.00 24.67           O  
ANISOU 1245  O   HOH A 245     4940   2424   2008   -697    439   -116       O  
HETATM 1246  O   HOH A 246      21.160   7.942  15.070  1.00 45.14           O  
ANISOU 1246  O   HOH A 246     3754   5927   7469    618    999   2266       O  
HETATM 1247  O   HOH A 247      -2.215   4.503  -0.412  1.00 36.07           O  
ANISOU 1247  O   HOH A 247     4863   4499   4343   -855   -778   1421       O  
HETATM 1248  O   HOH A 248       5.842  -2.611  22.983  1.00 38.56           O  
ANISOU 1248  O   HOH A 248     5494   6846   2309   2244   -674   -905       O  
HETATM 1249  O   HOH A 249      16.473  -5.617  17.875  1.00 31.29           O  
ANISOU 1249  O   HOH A 249     4605   1957   5325    626  -1946  -1006       O  
HETATM 1250  O   HOH A 250       5.087  29.029   4.242  1.00 29.35           O  
ANISOU 1250  O   HOH A 250     4255   2724   4170   -633   -326  -1303       O  
HETATM 1251  O   HOH A 251      15.625   9.803   1.009  1.00 94.35           O  
ANISOU 1251  O   HOH A 251     7168  24866   3812  -5015   1799   5203       O  
HETATM 1252  O   HOH A 252      15.918  22.196   4.736  1.00 63.02           O  
ANISOU 1252  O   HOH A 252    13743   6233   3967  -4413  -1817   4561       O  
HETATM 1253  O   HOH A 253       5.194  19.261  -8.206  1.00 33.15           O  
ANISOU 1253  O   HOH A 253     3920   5609   3065    -26    116    303       O  
HETATM 1254  O   HOH A 254      19.681  14.785  18.344  1.00 26.87           O  
ANISOU 1254  O   HOH A 254     3078   3293   3837   -303    -87   1363       O  
HETATM 1255  O   HOH A 255       9.004  -3.969  -1.933  1.00 34.94           O  
ANISOU 1255  O   HOH A 255     7768   3388   2119  -1319    768   -196       O  
HETATM 1256  O   HOH A 256      11.184  22.268  26.602  1.00 32.10           O  
ANISOU 1256  O   HOH A 256     7341   3028   1827    -94    398   -315       O  
HETATM 1257  O   HOH A 257       6.189  19.155  -2.709  1.00 46.40           O  
ANISOU 1257  O   HOH A 257     8440   5739   3451   2690   2087   1249       O  
HETATM 1258  O   HOH A 258       8.824   4.952  32.755  1.00 26.93           O  
ANISOU 1258  O   HOH A 258     4575   2836   2821   -608  -1559    453       O  
HETATM 1259  O   HOH A 259      -7.859   9.805  22.474  1.00 52.62           O  
ANISOU 1259  O   HOH A 259     6816  10333   2842    552  -1183    856       O  
HETATM 1260  O   HOH A 260      20.724   4.395  17.579  1.00 33.71           O  
ANISOU 1260  O   HOH A 260     4561   4221   4025    669   1688   1968       O  
HETATM 1261  O   HOH A 261      10.741  -3.859  28.323  1.00 77.55           O  
ANISOU 1261  O   HOH A 261     7744   9496  12223   3430   1318   4660       O  
HETATM 1262  O   HOH A 262       6.249  12.303  16.699  1.00 31.04           O  
ANISOU 1262  O   HOH A 262     2701   7111   1982   -399    338   1449       O  
HETATM 1263  O   HOH A 263       9.329  14.977  -5.866  1.00 39.76           O  
ANISOU 1263  O   HOH A 263     5929   5082   4093      3   -158   1783       O  
HETATM 1264  O   HOH A 264      18.349  11.628  21.882  1.00 41.47           O  
ANISOU 1264  O   HOH A 264     3838   7289   4629   1650  -1235  -2723       O  
HETATM 1265  O   HOH A 265       2.530  -6.395  11.756  1.00 34.26           O  
ANISOU 1265  O   HOH A 265     5386   3945   3686   -525   1086    441       O  
HETATM 1266  O   HOH A 266       4.583  28.303   0.134  1.00 38.68           O  
ANISOU 1266  O   HOH A 266     8147   3725   2825   -943   -825   1111       O  
HETATM 1267  O  AHOH A 267       7.889   2.352  -2.875  0.50 24.99           O  
ANISOU 1267  O  AHOH A 267     4730   3034   1732   -290   -226    181       O  
HETATM 1268  O  BHOH A 267       9.611   3.093  -2.738  0.50 22.68           O  
ANISOU 1268  O  BHOH A 267     5258   1765   1595    292   -453   -494       O  
HETATM 1269  O   HOH A 268       9.421  28.808  15.294  1.00 23.05           O  
ANISOU 1269  O   HOH A 268     4149   2018   2589     66    357     83       O  
HETATM 1270  O   HOH A 269       3.218  21.290  23.989  1.00 35.06           O  
ANISOU 1270  O   HOH A 269     7662   3086   2571   1575   1794     40       O  
HETATM 1271  O   HOH A 270       3.972  16.612  -2.007  1.00 29.91           O  
ANISOU 1271  O   HOH A 270     5980   3533   1850   -959    413    173       O  
HETATM 1272  O   HOH A 271      17.666  21.238  14.942  1.00 23.86           O  
ANISOU 1272  O   HOH A 271     5029   2625   1411   -184   -638   -346       O  
HETATM 1273  O   HOH A 272      -9.448   4.024  20.676  1.00 22.88           O  
ANISOU 1273  O   HOH A 272     4855   2166   1671    500   1072    337       O  
HETATM 1274  O   HOH A 273      -3.765   1.768  15.050  1.00 23.02           O  
ANISOU 1274  O   HOH A 273     4091   2132   2521    420   1189    258       O  
HETATM 1275  O   HOH A 274      13.002  -7.467  20.088  1.00 43.08           O  
ANISOU 1275  O   HOH A 274     5732   2404   8230    813  -1166   -713       O  
HETATM 1276  O  AHOH A 275       4.484  11.673  14.838  0.50 23.95           O  
ANISOU 1276  O  AHOH A 275     4000   3413   1685    658   -800   -816       O  
HETATM 1277  O  BHOH A 275       4.123  13.245  15.571  0.50 25.30           O  
ANISOU 1277  O  BHOH A 275     5706   3019    888   -351   -240   -217       O  
HETATM 1278  O   HOH A 276      20.843   2.493  21.395  1.00 35.83           O  
ANISOU 1278  O   HOH A 276     4158   7085   2368   -150   -416  -1456       O  
HETATM 1279  O   HOH A 277      -3.663  17.977  23.869  1.00108.93           O  
ANISOU 1279  O   HOH A 277     3508  13818  24062   5342    906  -9142       O  
HETATM 1280  O   HOH A 278      20.488   4.934  28.349  0.50 16.76           O  
ANISOU 1280  O   HOH A 278     3462   2050    853     66   -205    335       O  
HETATM 1281  O   HOH A 279      17.221  21.153  17.700  1.00 30.20           O  
ANISOU 1281  O   HOH A 279     4475   5314   1685   -204   -348    129       O  
HETATM 1282  O  AHOH A 280      11.478  24.741   4.310  0.50 27.35           O  
ANISOU 1282  O  AHOH A 280     3455   5045   1891  -1618    581   1843       O  
HETATM 1283  O  BHOH A 280      12.706  25.401   6.083  0.50 23.12           O  
ANISOU 1283  O  BHOH A 280     6067   2161    555   -502     79    420       O  
HETATM 1284  O   HOH A 281      -1.531  14.222  21.851  1.00 31.26           O  
ANISOU 1284  O   HOH A 281     4224   5200   2452   -366    170   -404       O  
HETATM 1285  O   HOH A 282      18.341  -2.172  14.333  1.00 31.30           O  
ANISOU 1285  O   HOH A 282     4596   4143   3153   -190     25   1316       O  
HETATM 1286  O   HOH A 283      19.209  20.523   7.253  1.00 36.27           O  
ANISOU 1286  O   HOH A 283     6135   3405   4239  -1275   1764  -1675       O  
HETATM 1287  O   HOH A 284      -1.652   9.272  26.208  1.00 43.27           O  
ANISOU 1287  O   HOH A 284     6805   4642   4991    -80   2437     68       O  
HETATM 1288  O   HOH A 285       0.394   9.025  29.392  1.00 38.87           O  
ANISOU 1288  O   HOH A 285     7352   4468   2950   -994   1533    936       O  
HETATM 1289  O   HOH A 286      13.304  28.441   7.857  1.00 33.83           O  
ANISOU 1289  O   HOH A 286     5952   5175   1727   -441   -484   -743       O  
HETATM 1290  O   HOH A 287      11.822  -3.130  24.855  1.00 28.39           O  
ANISOU 1290  O   HOH A 287     6580   1965   2241   -230   1418    385       O  
HETATM 1291  O   HOH A 288       3.044  -2.319   1.125  1.00 33.38           O  
ANISOU 1291  O   HOH A 288     5236   3165   4282     81    102  -1973       O  
HETATM 1292  O   HOH A 289      12.340  -1.430  34.233  1.00 42.37           O  
ANISOU 1292  O   HOH A 289     6520   6621   2956   1741    428   2556       O  
HETATM 1293  O   HOH A 290      21.861  11.619   7.681  1.00 38.58           O  
ANISOU 1293  O   HOH A 290     4208   4608   5842   -556   -973   1615       O  
HETATM 1294  O   HOH A 291       6.543  21.653  -1.448  1.00 33.87           O  
ANISOU 1294  O   HOH A 291     6646   4162   2058   -344   1430   -436       O  
HETATM 1295  O   HOH A 292      12.823   6.160  32.965  1.00 63.17           O  
ANISOU 1295  O   HOH A 292     8834  12935   2231    -77  -3449  -2709       O  
HETATM 1296  O   HOH A 293      -4.078  11.781  25.808  1.00 41.59           O  
ANISOU 1296  O   HOH A 293     6129   5286   4385   -405    519    271       O  
HETATM 1297  O   HOH A 294      -2.719  -1.920   3.826  1.00 44.12           O  
ANISOU 1297  O   HOH A 294     5346   4798   6617  -2008   -477   -108       O  
HETATM 1298  O   HOH A 295      -2.362  18.880  16.062  1.00 41.50           O  
ANISOU 1298  O   HOH A 295     4039   5474   6252    766   1082  -1861       O  
HETATM 1299  O   HOH A 296      15.113   4.118  32.592  1.00 40.75           O  
ANISOU 1299  O   HOH A 296     7333   4978   3172   -527  -1145    227       O  
HETATM 1300  O   HOH A 297      17.167  12.467  30.593  1.00 37.09           O  
ANISOU 1300  O   HOH A 297     6074   5612   2406    970   -945    299       O  
HETATM 1301  O   HOH A 298      11.709  27.883   5.387  1.00 35.46           O  
ANISOU 1301  O   HOH A 298     6601   3820   3049      0    835    901       O  
HETATM 1302  O   HOH A 299      -2.052  12.843  23.427  1.00 39.97           O  
ANISOU 1302  O   HOH A 299     3648   5358   6180   -208    656   -437       O  
HETATM 1303  O   HOH A 300      10.106  -0.757  34.531  1.00 42.86           O  
ANISOU 1303  O   HOH A 300     5975   6819   3489    -27    -76   1404       O  
HETATM 1304  O   HOH A 301      12.908   2.673  33.505  1.00 43.36           O  
ANISOU 1304  O   HOH A 301     7265   6683   2524  -1122   -737    713       O  
HETATM 1305  O   HOH A 302      -4.585  11.790  28.960  1.00 55.41           O  
ANISOU 1305  O   HOH A 302     7743   7344   5964   1095  -1414  -1083       O  
HETATM 1306  O   HOH A 303       7.558  25.947  -0.868  1.00 36.34           O  
ANISOU 1306  O   HOH A 303     5360   6128   2317  -1373    259     67       O  
HETATM 1307  O   HOH A 304      10.159  -7.236  15.244  1.00 36.75           O  
ANISOU 1307  O   HOH A 304     5176   2765   6022    -79    -85    572       O  
HETATM 1308  O   HOH A 305       8.651  -4.143  32.601  1.00 39.83           O  
ANISOU 1308  O   HOH A 305     6942   4905   3287   -347   1956   -309       O  
HETATM 1309  O   HOH A 306      19.107  12.635  26.198  1.00 39.26           O  
ANISOU 1309  O   HOH A 306     6293   5476   3147     74    374    654       O  
HETATM 1310  O   HOH A 307      19.708  18.963  11.732  1.00 43.45           O  
ANISOU 1310  O   HOH A 307     4161   5659   6686   1804    463   1256       O  
HETATM 1311  O   HOH A 308       0.156  17.543  17.998  1.00 38.66           O  
ANISOU 1311  O   HOH A 308     5633   5739   3315    733   1674    662       O  
HETATM 1312  O   HOH A 309      13.435  -3.953   2.405  1.00 36.15           O  
ANISOU 1312  O   HOH A 309     6307   3359   4069   1299   -263   1241       O  
HETATM 1313  O   HOH A 310      10.800  18.261  34.067  1.00 35.93           O  
ANISOU 1313  O   HOH A 310     6500   5533   1615   -225    446    616       O  
HETATM 1314  O   HOH A 311      15.659  -5.277   4.676  1.00 42.89           O  
ANISOU 1314  O   HOH A 311     8228   4551   3515   1666    242   1169       O  
HETATM 1315  O   HOH A 312      -5.523  11.006  31.351  1.00 44.60           O  
ANISOU 1315  O   HOH A 312     6179   6127   4638    510   -967   1050       O  
HETATM 1316  O   HOH A 313       8.578  17.282  32.212  1.00 44.69           O  
ANISOU 1316  O   HOH A 313     6017   9342   1621   1419     68   -944       O  
HETATM 1317  O   HOH A 314      16.412  -1.008  17.606  1.00 29.12           O  
ANISOU 1317  O   HOH A 314     5970   3196   1895   1060  -1464   -134       O  
HETATM 1318  O   HOH A 315      -1.543   7.605  -0.427  1.00 29.25           O  
ANISOU 1318  O   HOH A 315     4938   4794   1380  -1362    157     46       O  
HETATM 1319  O   HOH A 316      10.113  21.406   2.977  1.00 41.62           O  
ANISOU 1319  O   HOH A 316     7265   5866   2683    759   1300   -711       O  
HETATM 1320  O   HOH A 317      23.326   2.144  20.506  1.00 23.04           O  
ANISOU 1320  O   HOH A 317     3482   2064   3208    110    687     99       O  
HETATM 1321  O   HOH A 318      10.384  -5.220   9.401  1.00 32.59           O  
ANISOU 1321  O   HOH A 318     7608   2904   1869    848    602   -230       O  
HETATM 1322  O   HOH A 319      -3.232  14.286  19.692  1.00 29.49           O  
ANISOU 1322  O   HOH A 319     4923   2933   3348   -440   1088   -555       O  
HETATM 1323  O   HOH A 320      10.175  28.742  19.922  1.00 41.24           O  
ANISOU 1323  O   HOH A 320     5169   6592   3908  -1140   -187  -2991       O  
HETATM 1324  O   HOH A 321      17.160   7.095   2.158  1.00 32.39           O  
ANISOU 1324  O   HOH A 321     6372   3297   2637  -1742   1604    -30       O  
HETATM 1325  O   HOH A 322       7.705   3.207  -0.669  1.00 31.76           O  
ANISOU 1325  O   HOH A 322     5619   4014   2435   1866   1528    995       O  
HETATM 1326  O   HOH A 323      -2.728   5.921  28.670  1.00 40.71           O  
ANISOU 1326  O   HOH A 323     5377   4367   5722    929  -1905  -1700       O  
HETATM 1327  O   HOH A 324       2.064  22.845  25.930  1.00 53.74           O  
ANISOU 1327  O   HOH A 324    10158   6457   3801   2778    279   4461       O  
HETATM 1328  O   HOH A 325       7.140  29.303  13.869  1.00 24.23           O  
ANISOU 1328  O   HOH A 325     4680   2618   1906    -65    122   -335       O  
HETATM 1329  O   HOH A 326       6.383   9.135  -1.784  1.00 21.50           O  
ANISOU 1329  O   HOH A 326     3757   2275   2135   -393    713   -455       O  
HETATM 1330  O   HOH A 327       4.918  16.969  29.671  1.00 28.32           O  
ANISOU 1330  O   HOH A 327     6569   2938   1252   -380    636    -89       O  
HETATM 1331  O   HOH A 328      21.630  17.943   4.649  1.00 43.28           O  
ANISOU 1331  O   HOH A 328     5778   2639   8027   -638   3777   -136       O  
HETATM 1332  O   HOH A 329      -2.286  19.497   6.726  1.00 33.31           O  
ANISOU 1332  O   HOH A 329     3941   4199   4515    154  -1369   1294       O  
HETATM 1333  O   HOH A 330       7.855  -6.494  17.894  1.00 36.04           O  
ANISOU 1333  O   HOH A 330     6429   3048   4216   -961  -1948   1500       O  
HETATM 1334  O   HOH A 331      15.761  26.181   8.680  1.00 31.63           O  
ANISOU 1334  O   HOH A 331     5455   4974   1586  -1642    -11   -166       O  
HETATM 1335  O   HOH A 332       2.991  12.169  29.996  1.00 33.64           O  
ANISOU 1335  O   HOH A 332     6394   4023   2363    665    -76    -46       O  
HETATM 1336  O   HOH A 333      16.031  23.272   8.578  1.00 35.14           O  
ANISOU 1336  O   HOH A 333     4336   3477   5538   -250   1483   -892       O  
HETATM 1337  O   HOH A 334       4.074   9.313  15.359  1.00 30.37           O  
ANISOU 1337  O   HOH A 334     6289   3022   2227   1409   1970    738       O  
HETATM 1338  O   HOH A 335       3.077  -4.636  22.477  1.00 33.30           O  
ANISOU 1338  O   HOH A 335     6209   3859   2583    583    341    686       O  
CONECT 1109 1127
CONECT 1110 1128
CONECT 1111 1113 1115
CONECT 1112 1114 1116
CONECT 1113 1111 1117
CONECT 1114 1112 1118
CONECT 1115 1111 1119
CONECT 1116 1112 1120
CONECT 1117 1113 1125
CONECT 1118 1114 1126
CONECT 1119 1115 1125
CONECT 1120 1116 1126
CONECT 1121 1123 1127
CONECT 1122 1124 1128
CONECT 1123 1121 1129 1131
CONECT 1124 1122 1130 1132
CONECT 1125 1117 1119 1127
CONECT 1126 1118 1120 1128
CONECT 1127 1109 1121 1125
CONECT 1128 1110 1122 1126
CONECT 1129 1123
CONECT 1130 1124
CONECT 1131 1123
CONECT 1132 1124
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.