CNRS Nantes University UFIP UFIP
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***  6dgka  ***

elNémo ID: 1909272209411923

Job options:

ID        	=	 1909272209411923
JOBID     	=	 6dgka
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 6dgka

ATOM      1  N   ALA A  86      10.909  11.107 -19.511  1.00 66.57           N  
ANISOU    1  N   ALA A  86     6951   7780  10562  -2347   1346   -116       N  
ATOM      2  CA  ALA A  86       9.519  10.731 -19.285  1.00 62.70           C  
ANISOU    2  CA  ALA A  86     6768   7174   9880  -2084   1236   -119       C  
ATOM      3  C   ALA A  86       9.267   9.280 -19.681  1.00 61.01           C  
ANISOU    3  C   ALA A  86     6474   7305   9400  -1819   1305   -120       C  
ATOM      4  O   ALA A  86       9.410   8.900 -20.845  1.00 66.88           O  
ANISOU    4  O   ALA A  86     7276   8196   9940  -1802   1577     89       O  
ATOM      5  CB  ALA A  86       8.585  11.654 -20.051  1.00 62.61           C  
ANISOU    5  CB  ALA A  86     7191   6797   9803  -2114   1364    207       C  
ATOM      6  N   SER A  87       8.880   8.471 -18.705  1.00 53.06           N  
ANISOU    6  N   SER A  87     5380   6421   8361  -1608   1054   -366       N  
ATOM      7  CA  SER A  87       8.538   7.082 -18.956  1.00 45.79           C  
ANISOU    7  CA  SER A  87     4472   5780   7144  -1296   1035   -370       C  
ATOM      8  C   SER A  87       7.028   6.897 -18.914  1.00 35.48           C  
ANISOU    8  C   SER A  87     3551   4353   5578  -1059    875   -253       C  
ATOM      9  O   SER A  87       6.273   7.761 -18.445  1.00 35.08           O  
ANISOU    9  O   SER A  87     3688   4033   5608  -1068    763   -221       O  
ATOM     10  CB  SER A  87       9.221   6.152 -17.949  1.00 58.14           C  
ANISOU   10  CB  SER A  87     5706   7602   8782  -1137    814   -649       C  
ATOM     11  OG  SER A  87       9.049   6.626 -16.629  1.00 67.78           O  
ANISOU   11  OG  SER A  87     6939   8708  10105  -1154    496   -846       O  
ATOM     12  N   ARG A  88       6.593   5.766 -19.460  1.00 24.95           N  
ANISOU   12  N   ARG A  88     2316   3202   3960   -852    885   -198       N  
ATOM     13  CA  ARG A  88       5.192   5.391 -19.480  1.00 22.27           C  
ANISOU   13  CA  ARG A  88     2245   2808   3409   -659    716    -92       C  
ATOM     14  C   ARG A  88       5.108   3.898 -19.204  1.00 20.21           C  
ANISOU   14  C   ARG A  88     1945   2747   2987   -449    615   -229       C  
ATOM     15  O   ARG A  88       6.074   3.158 -19.412  1.00 21.19           O  
ANISOU   15  O   ARG A  88     1909   3038   3105   -414    728   -346       O  
ATOM     16  CB  ARG A  88       4.539   5.736 -20.821  1.00 23.44           C  
ANISOU   16  CB  ARG A  88     2666   2892   3347   -708    815    204       C  
ATOM     17  CG  ARG A  88       4.493   7.233 -21.100  1.00 43.16           C  
ANISOU   17  CG  ARG A  88     5276   5110   6013   -880    907    413       C  
ATOM     18  CD  ARG A  88       3.450   7.561 -22.131  1.00 49.65           C  
ANISOU   18  CD  ARG A  88     6406   5846   6611   -821    852    750       C  
ATOM     19  NE  ARG A  88       3.632   6.785 -23.348  1.00 50.78           N  
ANISOU   19  NE  ARG A  88     6701   6228   6366   -843    961    844       N  
ATOM     20  CZ  ARG A  88       2.796   6.811 -24.379  1.00 63.54           C  
ANISOU   20  CZ  ARG A  88     8614   7866   7663   -798    849   1114       C  
ATOM     21  NH1 ARG A  88       1.710   7.581 -24.345  1.00 63.33           N  
ANISOU   21  NH1 ARG A  88     8696   7640   7727   -696    618   1356       N  
ATOM     22  NH2 ARG A  88       3.046   6.065 -25.447  1.00 67.46           N  
ANISOU   22  NH2 ARG A  88     9304   8588   7741   -832    957   1129       N  
ATOM     23  N   TYR A  89       3.943   3.467 -18.737  1.00 18.00           N  
ANISOU   23  N   TYR A  89     1799   2423   2616   -304    428   -202       N  
ATOM     24  CA  TYR A  89       3.735   2.087 -18.323  1.00 16.48           C  
ANISOU   24  CA  TYR A  89     1615   2334   2311   -135    324   -303       C  
ATOM     25  C   TYR A  89       2.406   1.601 -18.872  1.00 22.14           C  
ANISOU   25  C   TYR A  89     2529   3017   2867   -106    226   -163       C  
ATOM     26  O   TYR A  89       1.418   2.331 -18.841  1.00 21.36           O  
ANISOU   26  O   TYR A  89     2473   2824   2818   -123    150    -18       O  
ATOM     27  CB  TYR A  89       3.755   1.952 -16.794  1.00 15.59           C  
ANISOU   27  CB  TYR A  89     1413   2217   2293    -23    178   -434       C  
ATOM     28  CG  TYR A  89       5.011   2.512 -16.189  1.00 17.26           C  
ANISOU   28  CG  TYR A  89     1407   2481   2670    -86    168   -593       C  
ATOM     29  CD1 TYR A  89       6.164   1.745 -16.106  1.00 18.53           C  
ANISOU   29  CD1 TYR A  89     1358   2804   2878     -6    163   -709       C  
ATOM     30  CD2 TYR A  89       5.064   3.832 -15.737  1.00 18.37           C  
ANISOU   30  CD2 TYR A  89     1530   2489   2960   -231    150   -637       C  
ATOM     31  CE1 TYR A  89       7.337   2.255 -15.567  1.00 23.43           C  
ANISOU   31  CE1 TYR A  89     1688   3514   3700    -90     97   -854       C  
ATOM     32  CE2 TYR A  89       6.243   4.354 -15.190  1.00 20.73           C  
ANISOU   32  CE2 TYR A  89     1605   2832   3439   -360     88   -816       C  
ATOM     33  CZ  TYR A  89       7.371   3.562 -15.109  1.00 22.02           C  
ANISOU   33  CZ  TYR A  89     1493   3216   3656   -301     41   -916       C  
ATOM     34  OH  TYR A  89       8.541   4.075 -14.573  1.00 25.15           O  
ANISOU   34  OH  TYR A  89     1580   3697   4278   -451    -77  -1090       O  
ATOM     35  N   LEU A  90       2.380   0.357 -19.348  1.00 15.64           N  
ANISOU   35  N   LEU A  90     1806   2253   1884    -57    215   -222       N  
ATOM     36  CA  LEU A  90       1.161  -0.273 -19.846  1.00 15.56           C  
ANISOU   36  CA  LEU A  90     1958   2213   1741    -88     65   -137       C  
ATOM     37  C   LEU A  90       0.916  -1.529 -19.022  1.00 16.07           C  
ANISOU   37  C   LEU A  90     2034   2230   1843      4     -9   -234       C  
ATOM     38  O   LEU A  90       1.807  -2.375 -18.906  1.00 15.64           O  
ANISOU   38  O   LEU A  90     2004   2172   1768    107     69   -378       O  
ATOM     39  CB  LEU A  90       1.306  -0.615 -21.332  1.00 17.62           C  
ANISOU   39  CB  LEU A  90     2437   2532   1725   -175    111   -140       C  
ATOM     40  CG  LEU A  90       0.219  -1.423 -22.025  1.00 18.69           C  
ANISOU   40  CG  LEU A  90     2773   2654   1674   -258   -105   -123       C  
ATOM     41  CD1 LEU A  90      -1.074  -0.610 -22.092  1.00 22.51           C  
ANISOU   41  CD1 LEU A  90     3180   3141   2233   -325   -337    118       C  
ATOM     42  CD2 LEU A  90       0.691  -1.849 -23.418  1.00 21.51           C  
ANISOU   42  CD2 LEU A  90     3427   3077   1668   -320    -14   -220       C  
ATOM     43  N   THR A  91      -0.274  -1.652 -18.444  1.00 14.17           N  
ANISOU   43  N   THR A  91     1763   1938   1684    -19   -132   -131       N  
ATOM     44  CA  THR A  91      -0.518  -2.767 -17.544  1.00 14.85           C  
ANISOU   44  CA  THR A  91     1881   1947   1816     39   -154   -165       C  
ATOM     45  C   THR A  91      -1.898  -3.358 -17.779  1.00 20.17           C  
ANISOU   45  C   THR A  91     2576   2561   2527   -110   -280    -60       C  
ATOM     46  O   THR A  91      -2.835  -2.667 -18.198  1.00 15.43           O  
ANISOU   46  O   THR A  91     1859   2018   1984   -200   -377     69       O  
ATOM     47  CB  THR A  91      -0.360  -2.343 -16.059  1.00 15.25           C  
ANISOU   47  CB  THR A  91     1827   2012   1956    167    -99   -151       C  
ATOM     48  OG1 THR A  91      -0.546  -3.489 -15.213  1.00 16.71           O  
ANISOU   48  OG1 THR A  91     2107   2115   2127    228   -101   -127       O  
ATOM     49  CG2 THR A  91      -1.354  -1.240 -15.670  1.00 16.20           C  
ANISOU   49  CG2 THR A  91     1825   2148   2181    142    -81    -35       C  
ATOM     50  N   ASP A  92      -1.997  -4.672 -17.534  1.00 15.84           N  
ANISOU   50  N   ASP A  92     2162   1876   1981   -139   -294   -107       N  
ATOM     51  CA  ASP A  92      -3.267  -5.372 -17.484  1.00 18.22           C  
ANISOU   51  CA  ASP A  92     2442   2087   2394   -333   -393    -10       C  
ATOM     52  C   ASP A  92      -3.982  -5.195 -16.154  1.00 17.26           C  
ANISOU   52  C   ASP A  92     2147   1977   2435   -301   -273    159       C  
ATOM     53  O   ASP A  92      -5.165  -5.525 -16.067  1.00 20.82           O  
ANISOU   53  O   ASP A  92     2460   2403   3049   -484   -307    284       O  
ATOM     54  CB  ASP A  92      -3.053  -6.873 -17.709  1.00 22.16           C  
ANISOU   54  CB  ASP A  92     3211   2350   2860   -404   -418   -128       C  
ATOM     55  CG  ASP A  92      -2.176  -7.167 -18.903  1.00 30.93           C  
ANISOU   55  CG  ASP A  92     4555   3430   3766   -368   -441   -352       C  
ATOM     56  OD1 ASP A  92      -2.587  -6.805 -20.024  1.00 21.49           O  
ANISOU   56  OD1 ASP A  92     3394   2334   2436   -524   -584   -391       O  
ATOM     57  OD2 ASP A  92      -1.098  -7.793 -18.730  1.00 21.69           O  
ANISOU   57  OD2 ASP A  92     3541   2141   2558   -165   -311   -481       O  
ATOM     58  N   MET A  93      -3.287  -4.697 -15.130  1.00 16.36           N  
ANISOU   58  N   MET A  93     2033   1915   2269    -90   -131    154       N  
ATOM     59  CA  MET A  93      -3.767  -4.701 -13.755  1.00 17.81           C  
ANISOU   59  CA  MET A  93     2178   2104   2485    -24     32    279       C  
ATOM     60  C   MET A  93      -4.321  -3.343 -13.325  1.00 19.90           C  
ANISOU   60  C   MET A  93     2234   2507   2818     51    136    322       C  
ATOM     61  O   MET A  93      -3.837  -2.287 -13.741  1.00 16.61           O  
ANISOU   61  O   MET A  93     1771   2151   2391    125     86    232       O  
ATOM     62  CB  MET A  93      -2.640  -5.097 -12.806  1.00 16.39           C  
ANISOU   62  CB  MET A  93     2202   1893   2133    181     74    228       C  
ATOM     63  CG  MET A  93      -2.308  -6.592 -12.820  1.00 20.33           C  
ANISOU   63  CG  MET A  93     2935   2178   2612    178     38    259       C  
ATOM     64  SD  MET A  93      -0.826  -6.970 -11.833  1.00 20.50           S  
ANISOU   64  SD  MET A  93     3142   2195   2452    506     -9    228       S  
ATOM     65  CE  MET A  93       0.430  -6.360 -12.982  1.00 16.93           C  
ANISOU   65  CE  MET A  93     2537   1862   2035    594   -116    -29       C  
ATOM     66  N   THR A  94      -5.332  -3.384 -12.454  1.00 22.90           N  
ANISOU   66  N   THR A  94     2507   2907   3286     38    326    462       N  
ATOM     67  CA  THR A  94      -5.754  -2.161 -11.791  1.00 24.05           C  
ANISOU   67  CA  THR A  94     2521   3145   3473    190    504    460       C  
ATOM     68  C   THR A  94      -4.706  -1.740 -10.773  1.00 20.66           C  
ANISOU   68  C   THR A  94     2336   2737   2778    377    567    308       C  
ATOM     69  O   THR A  94      -3.865  -2.531 -10.352  1.00 18.34           O  
ANISOU   69  O   THR A  94     2262   2420   2287    408    497    281       O  
ATOM     70  CB  THR A  94      -7.074  -2.349 -11.060  1.00 23.38           C  
ANISOU   70  CB  THR A  94     2244   3101   3539    154    776    636       C  
ATOM     71  OG1 THR A  94      -6.896  -3.382 -10.074  1.00 22.57           O  
ANISOU   71  OG1 THR A  94     2382   2951   3243    128    935    717       O  
ATOM     72  CG2 THR A  94      -8.184  -2.718 -12.031  1.00 25.83           C  
ANISOU   72  CG2 THR A  94     2218   3424   4173    -66    653    783       C  
ATOM     73  N   LEU A  95      -4.787  -0.475 -10.354  1.00 19.95           N  
ANISOU   73  N   LEU A  95     2211   2674   2696    512    675    205       N  
ATOM     74  CA  LEU A  95      -3.923   0.002  -9.281  1.00 23.68           C  
ANISOU   74  CA  LEU A  95     2927   3172   2899    651    705     20       C  
ATOM     75  C   LEU A  95      -4.037  -0.888  -8.053  1.00 28.23           C  
ANISOU   75  C   LEU A  95     3726   3806   3194    705    853    106       C  
ATOM     76  O   LEU A  95      -3.029  -1.235  -7.429  1.00 23.98           O  
ANISOU   76  O   LEU A  95     3428   3308   2376    774    705     28       O  
ATOM     77  CB  LEU A  95      -4.285   1.444  -8.926  1.00 30.14           C  
ANISOU   77  CB  LEU A  95     3720   3944   3787    776    861   -120       C  
ATOM     78  CG  LEU A  95      -3.459   2.035  -7.782  1.00 32.63           C  
ANISOU   78  CG  LEU A  95     4329   4270   3798    879    859   -378       C  
ATOM     79  CD1 LEU A  95      -2.024   2.131  -8.210  1.00 31.00           C  
ANISOU   79  CD1 LEU A  95     4159   4062   3556    789    529   -527       C  
ATOM     80  CD2 LEU A  95      -3.987   3.384  -7.388  1.00 30.44           C  
ANISOU   80  CD2 LEU A  95     4087   3875   3605   1011   1073   -544       C  
ATOM     81  N   GLU A  96      -5.258  -1.288  -7.704  1.00 22.91           N  
ANISOU   81  N   GLU A  96     2959   3146   2600    671   1142    300       N  
ATOM     82  CA  GLU A  96      -5.440  -2.105  -6.505  1.00 25.69           C  
ANISOU   82  CA  GLU A  96     3568   3540   2653    705   1358    441       C  
ATOM     83  C   GLU A  96      -4.815  -3.484  -6.681  1.00 25.14           C  
ANISOU   83  C   GLU A  96     3666   3382   2503    617   1152    587       C  
ATOM     84  O   GLU A  96      -4.247  -4.037  -5.732  1.00 26.95           O  
ANISOU   84  O   GLU A  96     4232   3628   2382    721   1136    650       O  
ATOM     85  CB  GLU A  96      -6.924  -2.222  -6.168  1.00 30.17           C  
ANISOU   85  CB  GLU A  96     3928   4142   3393    649   1784    643       C  
ATOM     86  CG  GLU A  96      -7.213  -2.875  -4.822  1.00 38.14           C  
ANISOU   86  CG  GLU A  96     5239   5207   4043    686   2132    815       C  
ATOM     87  CD  GLU A  96      -7.264  -4.395  -4.897  1.00 41.66           C  
ANISOU   87  CD  GLU A  96     5785   5531   4512    483   2098   1110       C  
ATOM     88  OE1 GLU A  96      -7.566  -4.930  -5.982  1.00 38.25           O  
ANISOU   88  OE1 GLU A  96     5081   4982   4470    270   1926   1183       O  
ATOM     89  OE2 GLU A  96      -6.999  -5.058  -3.873  1.00 42.58           O  
ANISOU   89  OE2 GLU A  96     6283   5639   4258    528   2189   1247       O  
ATOM     90  N   GLU A  97      -4.924  -4.052  -7.886  1.00 24.69           N  
ANISOU   90  N   GLU A  97     3417   3215   2751    448    982    639       N  
ATOM     91  CA  GLU A  97      -4.333  -5.355  -8.182  1.00 25.59           C  
ANISOU   91  CA  GLU A  97     3711   3170   2844    389    804    731       C  
ATOM     92  C   GLU A  97      -2.815  -5.342  -8.047  1.00 24.96           C  
ANISOU   92  C   GLU A  97     3817   3115   2550    593    530    574       C  
ATOM     93  O   GLU A  97      -2.223  -6.350  -7.646  1.00 23.66           O  
ANISOU   93  O   GLU A  97     3896   2845   2249    686    439    686       O  
ATOM     94  CB  GLU A  97      -4.725  -5.798  -9.593  1.00 22.58           C  
ANISOU   94  CB  GLU A  97     3121   2667   2791    168    664    725       C  
ATOM     95  CG  GLU A  97      -6.069  -6.505  -9.663  1.00 25.73           C  
ANISOU   95  CG  GLU A  97     3376   2972   3430    -99    841    941       C  
ATOM     96  CD  GLU A  97      -6.460  -6.919 -11.082  1.00 35.55           C  
ANISOU   96  CD  GLU A  97     4444   4111   4951   -351    613    885       C  
ATOM     97  OE1 GLU A  97      -6.265  -6.119 -12.019  1.00 30.23           O  
ANISOU   97  OE1 GLU A  97     3617   3546   4325   -320    423    728       O  
ATOM     98  OE2 GLU A  97      -6.958  -8.053 -11.261  1.00 41.58           O  
ANISOU   98  OE2 GLU A  97     5267   4668   5864   -598    615    999       O  
ATOM     99  N   MET A  98      -2.178  -4.208  -8.355  1.00 20.27           N  
ANISOU   99  N   MET A  98     3093   2647   1962    664    396    338       N  
ATOM    100  CA  MET A  98      -0.726  -4.082  -8.299  1.00 19.83           C  
ANISOU  100  CA  MET A  98     3089   2654   1791    813    129    173       C  
ATOM    101  C   MET A  98      -0.228  -3.759  -6.898  1.00 27.38           C  
ANISOU  101  C   MET A  98     4265   3746   2392    978     68    127       C  
ATOM    102  O   MET A  98       0.907  -4.109  -6.563  1.00 25.12           O  
ANISOU  102  O   MET A  98     4053   3517   1976   1125   -198     86       O  
ATOM    103  CB  MET A  98      -0.250  -2.987  -9.256  1.00 22.11           C  
ANISOU  103  CB  MET A  98     3135   2999   2268    749     34    -42       C  
ATOM    104  CG  MET A  98      -0.529  -3.279 -10.709  1.00 22.11           C  
ANISOU  104  CG  MET A  98     2984   2906   2511    607     33    -16       C  
ATOM    105  SD  MET A  98       0.437  -2.251 -11.823  1.00 20.37           S  
ANISOU  105  SD  MET A  98     2569   2748   2421    559    -70   -210       S  
ATOM    106  CE  MET A  98      -0.395  -0.685 -11.696  1.00 18.81           C  
ANISOU  106  CE  MET A  98     2286   2556   2307    495     43   -233       C  
ATOM    107  N   SER A  99      -1.044  -3.078  -6.088  1.00 26.90           N  
ANISOU  107  N   SER A  99     4304   3751   2165    973    299    117       N  
ATOM    108  CA  SER A  99      -0.673  -2.646  -4.750  1.00 31.88           C  
ANISOU  108  CA  SER A  99     5220   4523   2369   1112    255     18       C  
ATOM    109  C   SER A  99      -1.056  -3.651  -3.677  1.00 32.52           C  
ANISOU  109  C   SER A  99     5656   4614   2086   1201    400    299       C  
ATOM    110  O   SER A  99      -0.589  -3.530  -2.544  1.00 38.53           O  
ANISOU  110  O   SER A  99     6721   5506   2411   1329    284    254       O  
ATOM    111  CB  SER A  99      -1.346  -1.307  -4.419  1.00 37.48           C  
ANISOU  111  CB  SER A  99     5921   5268   3052   1093    492   -188       C  
ATOM    112  OG  SER A  99      -1.182  -0.383  -5.471  1.00 48.55           O  
ANISOU  112  OG  SER A  99     7026   6595   4824    997    414   -368       O  
ATOM    113  N   ARG A 100      -1.883  -4.637  -4.002  1.00 35.26           N  
ANISOU  113  N   ARG A 100     5599   4765   3035    900   -283   -757       N  
ATOM    114  CA  ARG A 100      -2.452  -5.496  -2.976  1.00 38.09           C  
ANISOU  114  CA  ARG A 100     6073   5386   3013   1272     65   -447       C  
ATOM    115  C   ARG A 100      -1.377  -6.385  -2.358  1.00 37.87           C  
ANISOU  115  C   ARG A 100     6232   5471   2684   1213   -242   -603       C  
ATOM    116  O   ARG A 100      -0.548  -6.965  -3.061  1.00 38.78           O  
ANISOU  116  O   ARG A 100     6125   5548   3063    797   -568   -654       O  
ATOM    117  CB  ARG A 100      -3.566  -6.351  -3.574  1.00 36.58           C  
ANISOU  117  CB  ARG A 100     5362   5384   3151   1115    420    198       C  
ATOM    118  CG  ARG A 100      -4.390  -7.119  -2.558  1.00 40.18           C  
ANISOU  118  CG  ARG A 100     5858   6132   3275   1519    842    650       C  
ATOM    119  CD  ARG A 100      -5.151  -8.224  -3.256  1.00 38.21           C  
ANISOU  119  CD  ARG A 100     5094   6036   3389   1152    995   1270       C  
ATOM    120  NE  ARG A 100      -5.982  -7.684  -4.324  1.00 36.94           N  
ANISOU  120  NE  ARG A 100     4522   5840   3674    892   1118   1553       N  
ATOM    121  CZ  ARG A 100      -6.474  -8.406  -5.324  1.00 43.75           C  
ANISOU  121  CZ  ARG A 100     4935   6758   4928    358   1090   1977       C  
ATOM    122  NH1 ARG A 100      -6.214  -9.705  -5.389  1.00 44.35           N  
ANISOU  122  NH1 ARG A 100     4973   6855   5021     55    965   2124       N  
ATOM    123  NH2 ARG A 100      -7.227  -7.830  -6.256  1.00 37.03           N  
ANISOU  123  NH2 ARG A 100     3699   5928   4445    113   1180   2266       N  
ATOM    124  N   ASP A 101      -1.387  -6.480  -1.032  1.00 42.29           N  
ANISOU  124  N   ASP A 101     7202   6190   2676   1659   -114   -650       N  
ATOM    125  CA  ASP A 101      -0.520  -7.427  -0.352  1.00 45.99           C  
ANISOU  125  CA  ASP A 101     7785   6841   2849   1644   -341   -653       C  
ATOM    126  C   ASP A 101      -1.065  -8.841  -0.515  1.00 47.23           C  
ANISOU  126  C   ASP A 101     7553   7185   3207   1564    -76    -87       C  
ATOM    127  O   ASP A 101      -2.279  -9.067  -0.553  1.00 44.52           O  
ANISOU  127  O   ASP A 101     7004   6950   2963   1704    356    348       O  
ATOM    128  CB  ASP A 101      -0.385  -7.074   1.132  1.00 58.27           C  
ANISOU  128  CB  ASP A 101     9774   8478   3889   2015   -288   -808       C  
ATOM    129  CG  ASP A 101       0.546  -5.898   1.366  1.00 70.07           C  
ANISOU  129  CG  ASP A 101    11506   9694   5422   1810   -663  -1283       C  
ATOM    130  OD1 ASP A 101       1.694  -5.940   0.870  1.00 75.25           O  
ANISOU  130  OD1 ASP A 101    11951  10262   6379   1359  -1058  -1395       O  
ATOM    131  OD2 ASP A 101       0.124  -4.927   2.030  1.00 74.35           O  
ANISOU  131  OD2 ASP A 101    12409  10117   5724   2088   -510  -1471       O  
ATOM    132  N   TRP A 102      -0.149  -9.796  -0.643  1.00 41.33           N  
ANISOU  132  N   TRP A 102     6697   6460   2547   1322   -344    -54       N  
ATOM    133  CA  TRP A 102      -0.525 -11.194  -0.737  1.00 38.61           C  
ANISOU  133  CA  TRP A 102     6077   6209   2383   1231   -137    444       C  
ATOM    134  C   TRP A 102       0.589 -12.020  -0.113  1.00 44.62           C  
ANISOU  134  C   TRP A 102     6949   7070   2936   1272   -379    434       C  
ATOM    135  O   TRP A 102       1.722 -11.554   0.046  1.00 41.35           O  
ANISOU  135  O   TRP A 102     6706   6640   2367   1231   -765     70       O  
ATOM    136  CB  TRP A 102      -0.779 -11.615  -2.193  1.00 34.33           C  
ANISOU  136  CB  TRP A 102     5150   5450   2442    735   -141    589       C  
ATOM    137  CG  TRP A 102       0.476 -11.850  -2.976  1.00 35.80           C  
ANISOU  137  CG  TRP A 102     5276   5453   2875    398   -518    306       C  
ATOM    138  CD1 TRP A 102       1.337 -10.903  -3.450  1.00 40.27           C  
ANISOU  138  CD1 TRP A 102     5884   5909   3506    256   -864   -128       C  
ATOM    139  CD2 TRP A 102       1.016 -13.120  -3.377  1.00 31.46           C  
ANISOU  139  CD2 TRP A 102     4610   4802   2541    193   -561    481       C  
ATOM    140  NE1 TRP A 102       2.381 -11.503  -4.118  1.00 39.84           N  
ANISOU  140  NE1 TRP A 102     5699   5754   3683     -3  -1101   -197       N  
ATOM    141  CE2 TRP A 102       2.207 -12.862  -4.090  1.00 35.49           C  
ANISOU  141  CE2 TRP A 102     5078   5183   3223    -19   -897    149       C  
ATOM    142  CE3 TRP A 102       0.613 -14.447  -3.196  1.00 34.12           C  
ANISOU  142  CE3 TRP A 102     4890   5122   2953    181   -336    907       C  
ATOM    143  CZ2 TRP A 102       3.003 -13.884  -4.614  1.00 32.20           C  
ANISOU  143  CZ2 TRP A 102     4579   4629   3025   -173   -957    222       C  
ATOM    144  CZ3 TRP A 102       1.402 -15.463  -3.729  1.00 30.17           C  
ANISOU  144  CZ3 TRP A 102     4358   4417   2690     -8   -422    939       C  
ATOM    145  CH2 TRP A 102       2.579 -15.172  -4.431  1.00 28.04           C  
ANISOU  145  CH2 TRP A 102     4061   4027   2565   -151   -702    593       C  
ATOM    146  N   PHE A 103       0.266 -13.252   0.247  1.00 40.69           N  
ANISOU  146  N   PHE A 103     6326   6682   2451   1339   -165    896       N  
ATOM    147  CA  PHE A 103       1.312 -14.160   0.690  1.00 54.02           C  
ANISOU  147  CA  PHE A 103     8041   8432   4052   1361   -360    981       C  
ATOM    148  C   PHE A 103       0.886 -15.594   0.416  1.00 49.73           C  
ANISOU  148  C   PHE A 103     7271   7792   3831   1236   -125   1487       C  
ATOM    149  O   PHE A 103      -0.278 -15.884   0.121  1.00 44.27           O  
ANISOU  149  O   PHE A 103     6430   7065   3326   1149    168   1813       O  
ATOM    150  CB  PHE A 103       1.638 -13.952   2.167  1.00 58.27           C  
ANISOU  150  CB  PHE A 103     8814   9229   4097   1683   -401    920       C  
ATOM    151  CG  PHE A 103       0.481 -14.186   3.061  1.00 61.80           C  
ANISOU  151  CG  PHE A 103     9259   9856   4365   1969     -1   1238       C  
ATOM    152  CD1 PHE A 103       0.246 -15.448   3.580  1.00 72.57           C  
ANISOU  152  CD1 PHE A 103    10447  11314   5810   2025    179   1700       C  
ATOM    153  CD2 PHE A 103      -0.382 -13.154   3.374  1.00 57.05           C  
ANISOU  153  CD2 PHE A 103     8806   9305   3564   2193    207   1092       C  
ATOM    154  CE1 PHE A 103      -0.825 -15.678   4.397  1.00 78.32           C  
ANISOU  154  CE1 PHE A 103    11104  12220   6435   2264    518   2002       C  
ATOM    155  CE2 PHE A 103      -1.451 -13.374   4.188  1.00 72.15           C  
ANISOU  155  CE2 PHE A 103    10662  11402   5352   2490    587   1418       C  
ATOM    156  CZ  PHE A 103      -1.668 -14.641   4.706  1.00 80.27           C  
ANISOU  156  CZ  PHE A 103    11469  12558   6472   2509    723   1870       C  
ATOM    157  N   MET A 104       1.854 -16.492   0.540  1.00 41.67           N  
ANISOU  157  N   MET A 104     6230   6723   2879   1224   -266   1589       N  
ATOM    158  CA  MET A 104       1.707 -17.876   0.123  1.00 44.69           C  
ANISOU  158  CA  MET A 104     6471   6874   3635   1063    -96   1986       C  
ATOM    159  C   MET A 104       1.411 -18.774   1.316  1.00 45.73           C  
ANISOU  159  C   MET A 104     6603   7211   3560   1341     92   2446       C  
ATOM    160  O   MET A 104       2.158 -18.774   2.298  1.00 48.32           O  
ANISOU  160  O   MET A 104     6997   7758   3607   1573    -40   2389       O  
ATOM    161  CB  MET A 104       2.979 -18.342  -0.579  1.00 39.92           C  
ANISOU  161  CB  MET A 104     5834   6016   3320    909   -305   1821       C  
ATOM    162  CG  MET A 104       3.259 -17.626  -1.890  1.00 35.96           C  
ANISOU  162  CG  MET A 104     5271   5280   3111    573   -466   1397       C  
ATOM    163  SD  MET A 104       4.993 -17.739  -2.371  1.00 43.01           S  
ANISOU  163  SD  MET A 104     6109   6083   4151    563   -755   1185       S  
ATOM    164  CE  MET A 104       5.739 -16.474  -1.349  1.00 38.55           C  
ANISOU  164  CE  MET A 104     5620   5940   3089    778  -1138    933       C  
ATOM    165  N   LEU A 105       0.315 -19.534   1.219  1.00 46.73           N  
ANISOU  165  N   LEU A 105     6597   7202   3957   1193    357   2786       N  
ATOM    166  CA  LEU A 105       0.069 -20.646   2.132  1.00 51.16           C  
ANISOU  166  CA  LEU A 105     7075   7810   4552   1311    500   3142       C  
ATOM    167  C   LEU A 105       1.265 -21.589   2.179  1.00 57.93           C  
ANISOU  167  C   LEU A 105     7971   8509   5530   1359    389   3248       C  
ATOM    168  O   LEU A 105       1.790 -21.899   3.253  1.00 54.66           O  
ANISOU  168  O   LEU A 105     7540   8333   4896   1618    355   3363       O  
ATOM    169  CB  LEU A 105      -1.175 -21.409   1.679  1.00 55.80           C  
ANISOU  169  CB  LEU A 105     7511   8179   5512   1016    691   3428       C  
ATOM    170  CG  LEU A 105      -2.290 -21.736   2.653  1.00 64.20           C  
ANISOU  170  CG  LEU A 105     8400   9489   6505   1159    886   3735       C  
ATOM    171  CD1 LEU A 105      -3.484 -20.835   2.377  1.00 60.36           C  
ANISOU  171  CD1 LEU A 105     7782   9130   6021   1106   1003   3696       C  
ATOM    172  CD2 LEU A 105      -2.669 -23.205   2.513  1.00 71.39           C  
ANISOU  172  CD2 LEU A 105     9229  10125   7771    922    934   4071       C  
ATOM    173  N   MET A 106       1.694 -22.074   1.010  1.00 49.06           N  
ANISOU  173  N   MET A 106     6892   6970   4778   1112    357   3232       N  
ATOM    174  CA  MET A 106       2.827 -22.988   0.876  1.00 50.11           C  
ANISOU  174  CA  MET A 106     7062   6866   5112   1194    317   3347       C  
ATOM    175  C   MET A 106       3.798 -22.319  -0.082  1.00 46.73           C  
ANISOU  175  C   MET A 106     6680   6317   4759   1127    124   2987       C  
ATOM    176  O   MET A 106       3.718 -22.524  -1.303  1.00 44.50           O  
ANISOU  176  O   MET A 106     6453   5607   4847    803    171   2790       O  
ATOM    177  CB  MET A 106       2.401 -24.358   0.353  1.00 51.70           C  
ANISOU  177  CB  MET A 106     7314   6568   5759    952    506   3587       C  
ATOM    178  CG  MET A 106       1.343 -25.068   1.169  1.00 63.83           C  
ANISOU  178  CG  MET A 106     8757   8202   7293    931    644   3889       C  
ATOM    179  SD  MET A 106       0.812 -26.597   0.361  1.00 71.16           S  
ANISOU  179  SD  MET A 106     9840   8492   8706    541    757   4054       S  
ATOM    180  CE  MET A 106       2.388 -27.406   0.058  1.00 71.83           C  
ANISOU  180  CE  MET A 106    10078   8195   9017    750    781   4057       C  
ATOM    181  N   PRO A 107       4.713 -21.496   0.419  1.00 46.39           N  
ANISOU  181  N   PRO A 107     6166   7277   4183   2034     33   2588       N  
ATOM    182  CA  PRO A 107       5.563 -20.712  -0.483  1.00 47.85           C  
ANISOU  182  CA  PRO A 107     6190   7508   4485   2059    -32   2474       C  
ATOM    183  C   PRO A 107       6.477 -21.585  -1.333  1.00 52.33           C  
ANISOU  183  C   PRO A 107     6678   7749   5454   2360    271   2750       C  
ATOM    184  O   PRO A 107       7.013 -22.598  -0.880  1.00 51.22           O  
ANISOU  184  O   PRO A 107     6396   7599   5465   2583    411   3116       O  
ATOM    185  CB  PRO A 107       6.365 -19.817   0.470  1.00 52.93           C  
ANISOU  185  CB  PRO A 107     6500   8747   4865   1928   -431   2461       C  
ATOM    186  CG  PRO A 107       6.288 -20.494   1.802  1.00 55.50           C  
ANISOU  186  CG  PRO A 107     6789   9285   5013   1944   -506   2736       C  
ATOM    187  CD  PRO A 107       4.955 -21.181   1.836  1.00 51.32           C  
ANISOU  187  CD  PRO A 107     6610   8405   4484   1941   -262   2678       C  
ATOM    188  N   LYS A 108       6.612 -21.191  -2.595  1.00 44.03           N  
ANISOU  188  N   LYS A 108     5752   6385   4592   2349    422   2561       N  
ATOM    189  CA  LYS A 108       7.650 -21.684  -3.491  1.00 46.08           C  
ANISOU  189  CA  LYS A 108     5918   6346   5245   2592    738   2733       C  
ATOM    190  C   LYS A 108       8.287 -20.465  -4.136  1.00 44.39           C  
ANISOU  190  C   LYS A 108     5483   6318   5066   2532    532   2537       C  
ATOM    191  O   LYS A 108       7.587 -19.650  -4.746  1.00 40.71           O  
ANISOU  191  O   LYS A 108     5237   5718   4512   2160    447   2030       O  
ATOM    192  CB  LYS A 108       7.080 -22.622  -4.559  1.00 46.84           C  
ANISOU  192  CB  LYS A 108     6522   5707   5567   2545   1242   2608       C  
ATOM    193  CG  LYS A 108       8.128 -23.279  -5.435  1.00 53.98           C  
ANISOU  193  CG  LYS A 108     7402   6257   6852   2760   1694   2735       C  
ATOM    194  CD  LYS A 108       9.023 -24.176  -4.591  1.00 70.63           C  
ANISOU  194  CD  LYS A 108     9132   8590   9114   3099   1800   3224       C  
ATOM    195  CE  LYS A 108      10.066 -24.898  -5.432  1.00 78.08           C  
ANISOU  195  CE  LYS A 108    10042   9175  10450   3319   2339   3396       C  
ATOM    196  NZ  LYS A 108      10.975 -25.726  -4.593  1.00 84.19           N  
ANISOU  196  NZ  LYS A 108    10391  10183  11415   3641   2445   3950       N  
ATOM    197  N   GLN A 109       9.596 -20.320  -3.980  1.00 47.40           N  
ANISOU  197  N   GLN A 109     5386   7007   5616   2677    439   2762       N  
ATOM    198  CA  GLN A 109      10.325 -19.208  -4.564  1.00 46.00           C  
ANISOU  198  CA  GLN A 109     4920   7045   5512   2582    228   2566       C  
ATOM    199  C   GLN A 109      11.440 -19.737  -5.454  1.00 58.05           C  
ANISOU  199  C   GLN A 109     6299   8241   7514   2820    645   2771       C  
ATOM    200  O   GLN A 109      12.004 -20.805  -5.198  1.00 53.77           O  
ANISOU  200  O   GLN A 109     5672   7575   7182   3051    947   3167       O  
ATOM    201  CB  GLN A 109      10.920 -18.301  -3.490  1.00 47.91           C  
ANISOU  201  CB  GLN A 109     4745   7995   5463   2336   -321   2559       C  
ATOM    202  CG  GLN A 109       9.956 -17.308  -2.907  1.00 50.12           C  
ANISOU  202  CG  GLN A 109     5209   8551   5283   1960   -683   2127       C  
ATOM    203  CD  GLN A 109      10.496 -16.677  -1.645  1.00 57.96           C  
ANISOU  203  CD  GLN A 109     5987  10048   5986   1671  -1082   2128       C  
ATOM    204  OE1 GLN A 109      11.594 -17.013  -1.195  1.00 57.68           O  
ANISOU  204  OE1 GLN A 109     5625  10222   6068   1757  -1157   2516       O  
ATOM    205  NE2 GLN A 109       9.731 -15.759  -1.064  1.00 59.91           N  
ANISOU  205  NE2 GLN A 109     6462  10425   5878   1314  -1289   1709       N  
ATOM    206  N   LYS A 110      11.728 -18.984  -6.516  1.00 49.96           N  
ANISOU  206  N   LYS A 110     5262   7066   6655   2730    696   2472       N  
ATOM    207  CA  LYS A 110      12.869 -19.224  -7.392  1.00 57.51           C  
ANISOU  207  CA  LYS A 110     6059   7774   8020   2879   1066   2599       C  
ATOM    208  C   LYS A 110      13.369 -17.873  -7.885  1.00 57.87           C  
ANISOU  208  C   LYS A 110     5795   8121   8074   2666    739   2301       C  
ATOM    209  O   LYS A 110      12.654 -16.867  -7.827  1.00 42.34           O  
ANISOU  209  O   LYS A 110     3946   6348   5792   2255    347   1815       O  
ATOM    210  CB  LYS A 110      12.514 -20.122  -8.587  1.00 59.13           C  
ANISOU  210  CB  LYS A 110     6860   7151   8454   2912   1756   2446       C  
ATOM    211  CG  LYS A 110      12.087 -21.541  -8.238  1.00 63.79           C  
ANISOU  211  CG  LYS A 110     7783   7417   9039   3043   2134   2694       C  
ATOM    212  CD  LYS A 110      10.758 -21.903  -8.892  1.00 58.63           C  
ANISOU  212  CD  LYS A 110     7852   6210   8212   2745   2362   2298       C  
ATOM    213  CE  LYS A 110      10.435 -23.381  -8.708  1.00 67.68           C  
ANISOU  213  CE  LYS A 110     9303   7052   9361   2825   2778   2484       C  
ATOM    214  NZ  LYS A 110       9.199 -23.784  -9.437  1.00 64.40           N  
ANISOU  214  NZ  LYS A 110     9541   6196   8733   2410   2940   2066       N  
ATOM    215  N   VAL A 111      14.609 -17.856  -8.368  1.00 60.44           N  
ANISOU  215  N   VAL A 111     5828   8441   8695   2745    900   2478       N  
ATOM    216  CA  VAL A 111      15.197 -16.666  -8.977  1.00 59.04           C  
ANISOU  216  CA  VAL A 111     5385   8477   8571   2521    658   2201       C  
ATOM    217  C   VAL A 111      15.861 -17.099 -10.277  1.00 67.83           C  
ANISOU  217  C   VAL A 111     6653   9041  10080   2654   1263   2205       C  
ATOM    218  O   VAL A 111      16.882 -17.798 -10.253  1.00 72.49           O  
ANISOU  218  O   VAL A 111     7057   9569  10918   2886   1549   2650       O  
ATOM    219  CB  VAL A 111      16.208 -15.966  -8.058  1.00 59.47           C  
ANISOU  219  CB  VAL A 111     4926   9186   8485   2356    115   2413       C  
ATOM    220  CG1 VAL A 111      16.954 -14.884  -8.820  1.00 55.80           C  
ANISOU  220  CG1 VAL A 111     4253   8821   8126   2130    -40   2153       C  
ATOM    221  CG2 VAL A 111      15.517 -15.372  -6.855  1.00 50.08           C  
ANISOU  221  CG2 VAL A 111     3764   8451   6813   2061   -441   2245       C  
ATOM    222  N   ALA A 112      15.287 -16.689 -11.406  1.00 60.30           N  
ANISOU  222  N   ALA A 112     6069   7677   9164   2458   1485   1716       N  
ATOM    223  CA  ALA A 112      15.860 -16.930 -12.722  1.00 64.83           C  
ANISOU  223  CA  ALA A 112     6901   7735   9995   2427   2019   1604       C  
ATOM    224  C   ALA A 112      16.107 -15.589 -13.395  1.00 67.65           C  
ANISOU  224  C   ALA A 112     7034   8297  10372   2141   1750   1217       C  
ATOM    225  O   ALA A 112      15.233 -14.714 -13.386  1.00 56.64           O  
ANISOU  225  O   ALA A 112     5779   7048   8692   1724   1330    755       O  
ATOM    226  CB  ALA A 112      14.940 -17.797 -13.583  1.00 70.15           C  
ANISOU  226  CB  ALA A 112     8400   7658  10597   2253   2557   1338       C  
ATOM    227  N   GLY A 113      17.287 -15.436 -13.987  1.00 73.37           N  
ANISOU  227  N   GLY A 113     7526   9029  11323   2198   1904   1363       N  
ATOM    228  CA  GLY A 113      17.636 -14.112 -14.436  1.00 72.23           C  
ANISOU  228  CA  GLY A 113     7070   9198  11175   1919   1549   1059       C  
ATOM    229  C   GLY A 113      17.735 -13.184 -13.243  1.00 70.19           C  
ANISOU  229  C   GLY A 113     6300   9701  10670   1775    760   1106       C  
ATOM    230  O   GLY A 113      18.078 -13.587 -12.126  1.00 73.69           O  
ANISOU  230  O   GLY A 113     6527  10454  11016   1935    539   1500       O  
ATOM    231  N   SER A 114      17.416 -11.916 -13.477  1.00 63.20           N  
ANISOU  231  N   SER A 114     5327   9063   9624   1364    329    659       N  
ATOM    232  CA  SER A 114      17.381 -10.921 -12.411  1.00 68.65           C  
ANISOU  232  CA  SER A 114     5875  10247   9960   1039   -389    501       C  
ATOM    233  C   SER A 114      15.965 -10.715 -11.892  1.00 52.07           C  
ANISOU  233  C   SER A 114     4084   8167   7535    804   -620    206       C  
ATOM    234  O   SER A 114      15.540  -9.581 -11.653  1.00 50.22           O  
ANISOU  234  O   SER A 114     4140   7892   7050    355   -951    -75       O  
ATOM    235  CB  SER A 114      17.974  -9.605 -12.898  1.00 80.09           C  
ANISOU  235  CB  SER A 114     7287  11693  11451    671   -676    192       C  
ATOM    236  OG  SER A 114      18.179  -8.715 -11.816  1.00 89.81           O  
ANISOU  236  OG  SER A 114     8611  13060  12451    422  -1154    179       O  
ATOM    237  N   LEU A 115      15.217 -11.804 -11.707  1.00 38.56           N  
ANISOU  237  N   LEU A 115     2632   6224   5794   1052   -307    337       N  
ATOM    238  CA  LEU A 115      13.796 -11.731 -11.385  1.00 33.54           C  
ANISOU  238  CA  LEU A 115     2450   5439   4854    795   -429     -5       C  
ATOM    239  C   LEU A 115      13.458 -12.732 -10.291  1.00 36.99           C  
ANISOU  239  C   LEU A 115     2935   5963   5155   1094   -378    370       C  
ATOM    240  O   LEU A 115      13.887 -13.891 -10.335  1.00 36.00           O  
ANISOU  240  O   LEU A 115     2806   5613   5258   1496     31    796       O  
ATOM    241  CB  LEU A 115      12.930 -12.011 -12.620  1.00 32.26           C  
ANISOU  241  CB  LEU A 115     2861   4618   4780    572    -46   -341       C  
ATOM    242  CG  LEU A 115      12.995 -11.022 -13.784  1.00 30.41           C  
ANISOU  242  CG  LEU A 115     2680   4240   4634    182   -103   -748       C  
ATOM    243  CD1 LEU A 115      12.270 -11.605 -14.980  1.00 31.07           C  
ANISOU  243  CD1 LEU A 115     3365   3664   4778    -40    324   -931       C  
ATOM    244  CD2 LEU A 115      12.357  -9.699 -13.372  1.00 27.41           C  
ANISOU  244  CD2 LEU A 115     2278   4135   4002   -187   -591  -1048       C  
ATOM    245  N   CYS A 116      12.683 -12.276  -9.318  1.00 31.07           N  
ANISOU  245  N   CYS A 116     2248   5508   4048    899   -749    219       N  
ATOM    246  CA  CYS A 116      12.192 -13.134  -8.257  1.00 32.99           C  
ANISOU  246  CA  CYS A 116     2591   5840   4102   1111   -730    519       C  
ATOM    247  C   CYS A 116      10.856 -13.731  -8.671  1.00 36.05           C  
ANISOU  247  C   CYS A 116     3538   5688   4471   1024   -423    317       C  
ATOM    248  O   CYS A 116       9.967 -13.013  -9.148  1.00 27.19           O  
ANISOU  248  O   CYS A 116     2662   4392   3277    658   -505   -113       O  
ATOM    249  CB  CYS A 116      12.038 -12.357  -6.956  1.00 33.74           C  
ANISOU  249  CB  CYS A 116     2595   6425   3802    876  -1195    448       C  
ATOM    250  SG  CYS A 116      11.365 -13.400  -5.646  1.00 50.19           S  
ANISOU  250  SG  CYS A 116     4806   8662   5602   1107  -1180    808       S  
ATOM    251  N   ILE A 117      10.724 -15.041  -8.495  1.00 32.23           N  
ANISOU  251  N   ILE A 117     3232   4940   4074   1342    -77    676       N  
ATOM    252  CA  ILE A 117       9.527 -15.780  -8.860  1.00 30.26           C  
ANISOU  252  CA  ILE A 117     3524   4173   3798   1247    221    577       C  
ATOM    253  C   ILE A 117       8.952 -16.396  -7.591  1.00 32.18           C  
ANISOU  253  C   ILE A 117     3798   4625   3805   1415    129    853       C  
ATOM    254  O   ILE A 117       9.634 -17.167  -6.905  1.00 36.03           O  
ANISOU  254  O   ILE A 117     4063   5288   4340   1795    199   1324       O  
ATOM    255  CB  ILE A 117       9.831 -16.861  -9.907  1.00 34.42           C  
ANISOU  255  CB  ILE A 117     4373   4082   4623   1419    803    723       C  
ATOM    256  CG1 ILE A 117      10.564 -16.239 -11.103  1.00 32.99           C  
ANISOU  256  CG1 ILE A 117     4134   3744   4658   1271    918    482       C  
ATOM    257  CG2 ILE A 117       8.542 -17.549 -10.328  1.00 30.18           C  
ANISOU  257  CG2 ILE A 117     4454   3019   3993   1181   1046    602       C  
ATOM    258  CD1 ILE A 117      11.478 -17.198 -11.846  1.00 35.21           C  
ANISOU  258  CD1 ILE A 117     4521   3581   5276   1607   1530    750       C  
ATOM    259  N   ARG A 118       7.704 -16.061  -7.274  1.00 28.98           N  
ANISOU  259  N   ARG A 118     3636   4203   3171   1140    -12    613       N  
ATOM    260  CA  ARG A 118       7.030 -16.656  -6.129  1.00 30.40           C  
ANISOU  260  CA  ARG A 118     3900   4535   3114   1267    -51    851       C  
ATOM    261  C   ARG A 118       5.712 -17.265  -6.577  1.00 28.27           C  
ANISOU  261  C   ARG A 118     4106   3771   2863   1093    194    789       C  
ATOM    262  O   ARG A 118       5.039 -16.735  -7.470  1.00 28.38           O  
ANISOU  262  O   ARG A 118     4319   3511   2954    733    202    480       O  
ATOM    263  CB  ARG A 118       6.750 -15.635  -5.019  1.00 30.12           C  
ANISOU  263  CB  ARG A 118     3681   5034   2729   1102   -450    687       C  
ATOM    264  CG  ARG A 118       7.883 -14.689  -4.704  1.00 42.04           C  
ANISOU  264  CG  ARG A 118     4787   7038   4147   1060   -787    629       C  
ATOM    265  CD  ARG A 118       7.407 -13.651  -3.701  1.00 52.31           C  
ANISOU  265  CD  ARG A 118     6092   8736   5048    794  -1094    370       C  
ATOM    266  NE  ARG A 118       8.133 -12.393  -3.813  1.00 59.02           N  
ANISOU  266  NE  ARG A 118     6801   9624   6001    493  -1260     84       N  
ATOM    267  CZ  ARG A 118       9.174 -12.065  -3.059  1.00 69.09           C  
ANISOU  267  CZ  ARG A 118     7898  11146   7206    430  -1452    227       C  
ATOM    268  NH1 ARG A 118       9.612 -12.904  -2.130  1.00 79.19           N  
ANISOU  268  NH1 ARG A 118     9051  12710   8328    613  -1528    639       N  
ATOM    269  NH2 ARG A 118       9.776 -10.895  -3.231  1.00 71.68           N  
ANISOU  269  NH2 ARG A 118     8207  11391   7638    178  -1564      4       N  
ATOM    270  N   MET A 119       5.342 -18.380  -5.953  1.00 30.50           N  
ANISOU  270  N   MET A 119     4554   3958   3076   1314    365   1134       N  
ATOM    271  CA  MET A 119       4.010 -18.919  -6.183  1.00 30.30           C  
ANISOU  271  CA  MET A 119     4950   3547   3015   1101    526   1127       C  
ATOM    272  C   MET A 119       3.574 -19.753  -4.992  1.00 31.36           C  
ANISOU  272  C   MET A 119     5120   3836   2961   1337    550   1482       C  
ATOM    273  O   MET A 119       4.394 -20.251  -4.206  1.00 34.86           O  
ANISOU  273  O   MET A 119     5338   4547   3360   1700    538   1811       O  
ATOM    274  CB  MET A 119       3.920 -19.754  -7.473  1.00 35.31           C  
ANISOU  274  CB  MET A 119     6027   3524   3866    977    909   1135       C  
ATOM    275  CG  MET A 119       4.830 -20.940  -7.534  1.00 40.98           C  
ANISOU  275  CG  MET A 119     6828   3995   4749   1379   1288   1464       C  
ATOM    276  SD  MET A 119       4.309 -22.161  -8.770  1.00 39.80           S  
ANISOU  276  SD  MET A 119     7081   3322   4719   1024   1635   1202       S  
ATOM    277  CE  MET A 119       3.363 -23.281  -7.746  1.00 46.09           C  
ANISOU  277  CE  MET A 119     7919   4183   5409   1082   1600   1404       C  
ATOM    278  N   ASP A 120       2.260 -19.896  -4.868  1.00 29.84           N  
ANISOU  278  N   ASP A 120     5181   3485   2670   1109    572   1467       N  
ATOM    279  CA  ASP A 120       1.665 -20.686  -3.795  1.00 31.94           C  
ANISOU  279  CA  ASP A 120     5398   3876   2860   1177    566   1638       C  
ATOM    280  C   ASP A 120       1.493 -22.121  -4.288  1.00 33.75           C  
ANISOU  280  C   ASP A 120     5836   3676   3310   1157    824   1731       C  
ATOM    281  O   ASP A 120       0.715 -22.380  -5.212  1.00 34.03           O  
ANISOU  281  O   ASP A 120     6063   3389   3478    813    878   1550       O  
ATOM    282  CB  ASP A 120       0.330 -20.082  -3.357  1.00 29.95           C  
ANISOU  282  CB  ASP A 120     5151   3726   2502    893    439   1500       C  
ATOM    283  CG  ASP A 120      -0.097 -20.559  -1.980  1.00 41.69           C  
ANISOU  283  CG  ASP A 120     6551   5463   3824   1005    400   1665       C  
ATOM    284  OD1 ASP A 120       0.420 -21.611  -1.545  1.00 38.37           O  
ANISOU  284  OD1 ASP A 120     6117   5036   3425   1228    475   1892       O  
ATOM    285  OD2 ASP A 120      -0.930 -19.881  -1.329  1.00 36.77           O  
ANISOU  285  OD2 ASP A 120     5887   5023   3061    877    331   1577       O  
ATOM    286  N   GLN A 121       2.230 -23.052  -3.677  1.00 34.44           N  
ANISOU  286  N   GLN A 121     5986   4688   2412    -52   -178   1501       N  
ATOM    287  CA  GLN A 121       2.077 -24.474  -3.971  1.00 43.20           C  
ANISOU  287  CA  GLN A 121     7229   5526   3658     -9   -230   1685       C  
ATOM    288  C   GLN A 121       0.719 -25.028  -3.559  1.00 48.24           C  
ANISOU  288  C   GLN A 121     8016   6024   4288   -241    -45   1776       C  
ATOM    289  O   GLN A 121       0.350 -26.117  -4.012  1.00 47.10           O  
ANISOU  289  O   GLN A 121     7986   5605   4304   -257    -72   1883       O  
ATOM    290  CB  GLN A 121       3.166 -25.282  -3.262  1.00 45.88           C  
ANISOU  290  CB  GLN A 121     7602   5906   3923    138   -402   1906       C  
ATOM    291  CG  GLN A 121       4.557 -25.137  -3.848  1.00 58.00           C  
ANISOU  291  CG  GLN A 121     8962   7485   5591    360   -597   1910       C  
ATOM    292  CD  GLN A 121       4.830 -26.141  -4.960  1.00 68.42           C  
ANISOU  292  CD  GLN A 121    10344   8463   7191    527   -632   1939       C  
ATOM    293  OE1 GLN A 121       4.007 -26.344  -5.854  1.00 66.71           O  
ANISOU  293  OE1 GLN A 121    10232   8027   7088    485   -522   1803       O  
ATOM    294  NE2 GLN A 121       5.991 -26.783  -4.899  1.00 73.82           N  
ANISOU  294  NE2 GLN A 121    10978   9083   7988    719   -785   2116       N  
ATOM    295  N   ALA A 122      -0.024 -24.326  -2.701  1.00 42.89           N  
ANISOU  295  N   ALA A 122     7335   5514   3448   -433    167   1732       N  
ATOM    296  CA  ALA A 122      -1.311 -24.829  -2.239  1.00 43.20           C  
ANISOU  296  CA  ALA A 122     7455   5443   3517   -671    399   1851       C  
ATOM    297  C   ALA A 122      -2.411 -24.712  -3.286  1.00 46.08           C  
ANISOU  297  C   ALA A 122     7707   5622   4179   -828    504   1796       C  
ATOM    298  O   ALA A 122      -3.477 -25.318  -3.109  1.00 44.43           O  
ANISOU  298  O   ALA A 122     7502   5271   4108  -1036    659   1931       O  
ATOM    299  CB  ALA A 122      -1.740 -24.092  -0.967  1.00 42.36           C  
ANISOU  299  CB  ALA A 122     7362   5571   3163   -810    656   1809       C  
ATOM    300  N   ILE A 123      -2.178 -23.967  -4.364  1.00 34.31           N  
ANISOU  300  N   ILE A 123     6099   4126   2812   -748    407   1625       N  
ATOM    301  CA  ILE A 123      -3.210 -23.702  -5.359  1.00 37.11           C  
ANISOU  301  CA  ILE A 123     6317   4327   3457   -926    458   1587       C  
ATOM    302  C   ILE A 123      -3.245 -24.852  -6.354  1.00 41.83           C  
ANISOU  302  C   ILE A 123     7043   4598   4254   -904    210   1649       C  
ATOM    303  O   ILE A 123      -2.237 -25.149  -7.004  1.00 40.61           O  
ANISOU  303  O   ILE A 123     6998   4365   4065   -657      6   1570       O  
ATOM    304  CB  ILE A 123      -2.953 -22.371  -6.077  1.00 34.46           C  
ANISOU  304  CB  ILE A 123     5711   4147   3236   -789    432   1319       C  
ATOM    305  CG1 ILE A 123      -2.882 -21.218  -5.065  1.00 42.49           C  
ANISOU  305  CG1 ILE A 123     6630   5452   4063   -799    687   1199       C  
ATOM    306  CG2 ILE A 123      -4.015 -22.144  -7.138  1.00 37.29           C  
ANISOU  306  CG2 ILE A 123     5812   4366   3992   -911    398   1262       C  
ATOM    307  CD1 ILE A 123      -4.038 -21.180  -4.070  1.00 49.57           C  
ANISOU  307  CD1 ILE A 123     7478   6390   4966  -1033   1066   1287       C  
ATOM    308  N   MET A 124      -4.414 -25.477  -6.502  1.00 43.45           N  
ANISOU  308  N   MET A 124     7198   4613   4701  -1161    254   1761       N  
ATOM    309  CA  MET A 124      -4.576 -26.622  -7.390  1.00 39.90           C  
ANISOU  309  CA  MET A 124     6896   3838   4425  -1188     26   1776       C  
ATOM    310  C   MET A 124      -5.916 -26.541  -8.106  1.00 40.63           C  
ANISOU  310  C   MET A 124     6766   3802   4869  -1485    -23   1780       C  
ATOM    311  O   MET A 124      -6.905 -26.056  -7.551  1.00 48.72           O  
ANISOU  311  O   MET A 124     7495   4948   6069  -1694    200   1869       O  
ATOM    312  CB  MET A 124      -4.470 -27.946  -6.615  1.00 43.23           C  
ANISOU  312  CB  MET A 124     7529   4125   4771  -1186     60   1951       C  
ATOM    313  CG  MET A 124      -3.066 -28.240  -6.097  1.00 52.62           C  
ANISOU  313  CG  MET A 124     8885   5401   5706   -871      4   1969       C  
ATOM    314  SD  MET A 124      -2.965 -29.728  -5.094  1.00 76.96           S  
ANISOU  314  SD  MET A 124    12186   8331   8722   -880     34   2231       S  
ATOM    315  CE  MET A 124      -1.447 -30.459  -5.710  1.00 73.03           C  
ANISOU  315  CE  MET A 124    11850   7681   8217   -510   -181   2184       C  
ATOM    316  N   ASP A 125      -5.926 -27.007  -9.360  1.00 41.29           N  
ANISOU  316  N   ASP A 125     6963   3660   5064  -1484   -307   1664       N  
ATOM    317  CA  ASP A 125      -7.155 -27.176 -10.142  1.00 47.25           C  
ANISOU  317  CA  ASP A 125     7533   4283   6138  -1764   -467   1662       C  
ATOM    318  C   ASP A 125      -7.890 -25.853 -10.355  1.00 47.06           C  
ANISOU  318  C   ASP A 125     7065   4456   6360  -1867   -428   1645       C  
ATOM    319  O   ASP A 125      -9.121 -25.792 -10.305  1.00 55.02           O  
ANISOU  319  O   ASP A 125     7731   5480   7696  -2095   -390   1733       O  
ATOM    320  CB  ASP A 125      -8.080 -28.203  -9.483  1.00 56.78           C  
ANISOU  320  CB  ASP A 125     8711   5362   7502  -2007   -362   1845       C  
ATOM    321  CG  ASP A 125      -7.376 -29.514  -9.190  1.00 70.66           C  
ANISOU  321  CG  ASP A 125    10877   6912   9059  -1897   -383   1893       C  
ATOM    322  OD1 ASP A 125      -6.727 -30.059 -10.108  1.00 78.56           O  
ANISOU  322  OD1 ASP A 125    12167   7727   9956  -1763   -602   1746       O  
ATOM    323  OD2 ASP A 125      -7.462 -29.996  -8.039  1.00 72.88           O  
ANISOU  323  OD2 ASP A 125    11191   7215   9287  -1930   -158   2079       O  
ATOM    324  N   LYS A 126      -7.140 -24.783 -10.602  1.00 38.62           N  
ANISOU  324  N   LYS A 126     5970   3535   5169  -1678   -427   1533       N  
ATOM    325  CA  LYS A 126      -7.720 -23.469 -10.820  1.00 40.29           C  
ANISOU  325  CA  LYS A 126     5735   3940   5631  -1699   -370   1487       C  
ATOM    326  C   LYS A 126      -7.381 -22.966 -12.218  1.00 42.44           C  
ANISOU  326  C   LYS A 126     6070   4154   5900  -1598   -694   1325       C  
ATOM    327  O   LYS A 126      -6.416 -23.413 -12.842  1.00 41.64           O  
ANISOU  327  O   LYS A 126     6375   3924   5523  -1442   -850   1212       O  
ATOM    328  CB  LYS A 126      -7.219 -22.457  -9.776  1.00 42.05           C  
ANISOU  328  CB  LYS A 126     5803   4479   5697  -1479      1   1397       C  
ATOM    329  CG  LYS A 126      -7.629 -22.778  -8.345  1.00 49.38           C  
ANISOU  329  CG  LYS A 126     6696   5496   6571  -1595    372   1550       C  
ATOM    330  CD  LYS A 126      -9.112 -22.550  -8.133  1.00 59.29           C  
ANISOU  330  CD  LYS A 126     7501   6750   8276  -1851    568   1699       C  
ATOM    331  CE  LYS A 126      -9.515 -22.853  -6.700  1.00 67.05           C  
ANISOU  331  CE  LYS A 126     8494   7820   9161  -1954   1020   1831       C  
ATOM    332  NZ  LYS A 126      -8.697 -22.058  -5.746  1.00 71.13           N  
ANISOU  332  NZ  LYS A 126     9153   8584   9287  -1745   1318   1691       N  
ATOM    333  N   ASN A 127      -8.198 -22.030 -12.705  1.00 40.72           N  
ANISOU  333  N   ASN A 127     5448   4019   6006  -1679   -770   1336       N  
ATOM    334  CA  ASN A 127      -7.887 -21.263 -13.906  1.00 35.02           C  
ANISOU  334  CA  ASN A 127     4746   3300   5261  -1565  -1027   1204       C  
ATOM    335  C   ASN A 127      -7.169 -19.991 -13.482  1.00 36.92           C  
ANISOU  335  C   ASN A 127     4820   3804   5405  -1267   -752   1056       C  
ATOM    336  O   ASN A 127      -7.666 -19.248 -12.630  1.00 35.39           O  
ANISOU  336  O   ASN A 127     4259   3776   5413  -1251   -456   1087       O  
ATOM    337  CB  ASN A 127      -9.149 -20.915 -14.697  1.00 42.74           C  
ANISOU  337  CB  ASN A 127     5374   4275   6592  -1720  -1280   1286       C  
ATOM    338  CG  ASN A 127      -9.815 -22.139 -15.303  1.00 59.05           C  
ANISOU  338  CG  ASN A 127     7629   6167   8641  -1921  -1576   1343       C  
ATOM    339  OD1 ASN A 127      -9.143 -23.057 -15.781  1.00 63.82           O  
ANISOU  339  OD1 ASN A 127     8725   6604   8920  -1915  -1722   1246       O  
ATOM    340  ND2 ASN A 127     -11.141 -22.160 -15.281  1.00 66.79           N  
ANISOU  340  ND2 ASN A 127     8221   7176   9978  -2084  -1644   1499       N  
ATOM    341  N   ILE A 128      -6.000 -19.750 -14.063  1.00 33.28           N  
ANISOU  341  N   ILE A 128     4643   3358   4642  -1041   -820    893       N  
ATOM    342  CA  ILE A 128      -5.127 -18.661 -13.639  1.00 32.23           C  
ANISOU  342  CA  ILE A 128     4411   3451   4382   -784   -586    750       C  
ATOM    343  C   ILE A 128      -4.771 -17.821 -14.859  1.00 28.50           C  
ANISOU  343  C   ILE A 128     3960   2967   3901   -681   -770    655       C  
ATOM    344  O   ILE A 128      -4.574 -18.356 -15.956  1.00 28.66           O  
ANISOU  344  O   ILE A 128     4286   2813   3790   -716  -1032    643       O  
ATOM    345  CB  ILE A 128      -3.867 -19.210 -12.932  1.00 27.02           C  
ANISOU  345  CB  ILE A 128     4041   2856   3371   -603   -441    689       C  
ATOM    346  CG1 ILE A 128      -4.267 -19.925 -11.636  1.00 29.24           C  
ANISOU  346  CG1 ILE A 128     4316   3163   3632   -719   -250    816       C  
ATOM    347  CG2 ILE A 128      -2.861 -18.084 -12.625  1.00 24.83           C  
ANISOU  347  CG2 ILE A 128     3672   2801   2963   -380   -281    543       C  
ATOM    348  CD1 ILE A 128      -3.100 -20.556 -10.894  1.00 33.80           C  
ANISOU  348  CD1 ILE A 128     5175   3788   3881   -558   -178    824       C  
ATOM    349  N   ILE A 129      -4.739 -16.500 -14.683  1.00 25.64           N  
ANISOU  349  N   ILE A 129     3314   2762   3668   -572   -621    591       N  
ATOM    350  CA  ILE A 129      -4.298 -15.588 -15.733  1.00 23.25           C  
ANISOU  350  CA  ILE A 129     3037   2456   3341   -463   -750    520       C  
ATOM    351  C   ILE A 129      -3.093 -14.812 -15.219  1.00 22.00           C  
ANISOU  351  C   ILE A 129     2888   2470   3001   -248   -505    367       C  
ATOM    352  O   ILE A 129      -3.109 -14.305 -14.092  1.00 23.91           O  
ANISOU  352  O   ILE A 129     2941   2849   3293   -219   -250    317       O  
ATOM    353  CB  ILE A 129      -5.424 -14.638 -16.184  1.00 28.97           C  
ANISOU  353  CB  ILE A 129     3397   3151   4457   -550   -862    624       C  
ATOM    354  CG1 ILE A 129      -4.891 -13.648 -17.224  1.00 27.36           C  
ANISOU  354  CG1 ILE A 129     3263   2939   4193   -434   -984    575       C  
ATOM    355  CG2 ILE A 129      -6.035 -13.924 -14.989  1.00 25.97           C  
ANISOU  355  CG2 ILE A 129     2615   2885   4365   -526   -523    629       C  
ATOM    356  CD1 ILE A 129      -5.952 -13.027 -18.078  1.00 36.62           C  
ANISOU  356  CD1 ILE A 129     4205   4012   5696   -541  -1265    743       C  
ATOM    357  N   LEU A 130      -2.046 -14.739 -16.039  1.00 22.46           N  
ANISOU  357  N   LEU A 130     3183   2511   2839   -119   -575    294       N  
ATOM    358  CA  LEU A 130      -0.889 -13.905 -15.747  1.00 21.04           C  
ANISOU  358  CA  LEU A 130     2963   2484   2548     50   -395    177       C  
ATOM    359  C   LEU A 130      -1.118 -12.520 -16.330  1.00 19.70           C  
ANISOU  359  C   LEU A 130     2608   2317   2561     62   -404    157       C  
ATOM    360  O   LEU A 130      -1.444 -12.392 -17.516  1.00 17.66           O  
ANISOU  360  O   LEU A 130     2445   1935   2332     23   -604    224       O  
ATOM    361  CB  LEU A 130       0.385 -14.501 -16.343  1.00 19.53           C  
ANISOU  361  CB  LEU A 130     3063   2266   2093    198   -407    141       C  
ATOM    362  CG  LEU A 130       0.703 -15.960 -16.035  1.00 22.43           C  
ANISOU  362  CG  LEU A 130     3674   2550   2298    234   -421    184       C  
ATOM    363  CD1 LEU A 130       2.129 -16.277 -16.481  1.00 22.36           C  
ANISOU  363  CD1 LEU A 130     3849   2535   2110    454   -334    147       C  
ATOM    364  CD2 LEU A 130       0.512 -16.214 -14.561  1.00 19.26           C  
ANISOU  364  CD2 LEU A 130     3128   2273   1915    187   -315    219       C  
ATOM    365  N   LYS A 131      -0.957 -11.490 -15.487  1.00 16.54           N  
ANISOU  365  N   LYS A 131     1987   2035   2262    100   -197     69       N  
ATOM    366  CA  LYS A 131      -1.118 -10.094 -15.868  1.00 17.51           C  
ANISOU  366  CA  LYS A 131     1936   2128   2590    127   -158     43       C  
ATOM    367  C   LYS A 131       0.168  -9.336 -15.572  1.00 18.89           C  
ANISOU  367  C   LYS A 131     2134   2413   2630    211    -12    -89       C  
ATOM    368  O   LYS A 131       0.864  -9.634 -14.603  1.00 18.37           O  
ANISOU  368  O   LYS A 131     2100   2481   2398    221     95   -171       O  
ATOM    369  CB  LYS A 131      -2.278  -9.431 -15.112  1.00 17.24           C  
ANISOU  369  CB  LYS A 131     1605   2064   2883     81     -7     49       C  
ATOM    370  CG  LYS A 131      -3.588 -10.154 -15.280  1.00 21.79           C  
ANISOU  370  CG  LYS A 131     2055   2547   3675    -28   -139    214       C  
ATOM    371  CD  LYS A 131      -4.751  -9.295 -14.816  1.00 23.93           C  
ANISOU  371  CD  LYS A 131     1955   2756   4382    -28     36    261       C  
ATOM    372  CE  LYS A 131      -6.058 -10.068 -14.881  1.00 33.47           C  
ANISOU  372  CE  LYS A 131     2955   3891   5870   -162    -85    461       C  
ATOM    373  NZ  LYS A 131      -7.165  -9.296 -14.271  1.00 38.41           N  
ANISOU  373  NZ  LYS A 131     3202   4461   6932   -122    178    511       N  
ATOM    374  N   ALA A 132       0.482  -8.339 -16.401  1.00 13.30           N  
ANISOU  374  N   ALA A 132     1406   1644   2002    246    -35    -84       N  
ATOM    375  CA  ALA A 132       1.792  -7.714 -16.296  1.00 12.04           C  
ANISOU  375  CA  ALA A 132     1265   1576   1732    291     73   -178       C  
ATOM    376  C   ALA A 132       1.686  -6.198 -16.419  1.00 14.03           C  
ANISOU  376  C   ALA A 132     1384   1742   2206    274    158   -221       C  
ATOM    377  O   ALA A 132       0.731  -5.659 -16.983  1.00 17.00           O  
ANISOU  377  O   ALA A 132     1683   1965   2811    273     95   -131       O  
ATOM    378  CB  ALA A 132       2.761  -8.237 -17.368  1.00 15.93           C  
ANISOU  378  CB  ALA A 132     1954   2071   2027    365      9   -111       C  
ATOM    379  N   ASN A 133       2.702  -5.527 -15.873  1.00 13.82           N  
ANISOU  379  N   ASN A 133     1323   1798   2130    250    277   -341       N  
ATOM    380  CA  ASN A 133       2.948  -4.095 -16.046  1.00 13.13           C  
ANISOU  380  CA  ASN A 133     1164   1605   2219    215    363   -393       C  
ATOM    381  C   ASN A 133       4.319  -3.941 -16.694  1.00 17.16           C  
ANISOU  381  C   ASN A 133     1720   2185   2614    212    356   -353       C  
ATOM    382  O   ASN A 133       5.319  -4.415 -16.135  1.00 17.56           O  
ANISOU  382  O   ASN A 133     1751   2409   2513    195    366   -401       O  
ATOM    383  CB  ASN A 133       2.905  -3.369 -14.696  1.00 15.31           C  
ANISOU  383  CB  ASN A 133     1379   1888   2550    132    527   -596       C  
ATOM    384  CG  ASN A 133       3.194  -1.881 -14.816  1.00 23.95           C  
ANISOU  384  CG  ASN A 133     2443   2822   3836     76    624   -675       C  
ATOM    385  OD1 ASN A 133       2.811  -1.255 -15.800  1.00 24.86           O  
ANISOU  385  OD1 ASN A 133     2531   2760   4155    129    597   -551       O  
ATOM    386  ND2 ASN A 133       3.843  -1.301 -13.797  1.00 19.85           N  
ANISOU  386  ND2 ASN A 133     1959   2341   3242    -53    715   -874       N  
ATOM    387  N   PHE A 134       4.362  -3.318 -17.880  1.00 15.94           N  
ANISOU  387  N   PHE A 134     1617   1899   2543    229    339   -233       N  
ATOM    388  CA  PHE A 134       5.602  -3.061 -18.611  1.00 16.02           C  
ANISOU  388  CA  PHE A 134     1662   1949   2476    220    403   -166       C  
ATOM    389  C   PHE A 134       5.845  -1.570 -18.779  1.00 17.32           C  
ANISOU  389  C   PHE A 134     1762   1972   2849    125    485   -173       C  
ATOM    390  O   PHE A 134       4.909  -0.800 -18.992  1.00 17.60           O  
ANISOU  390  O   PHE A 134     1804   1807   3075    127    459   -141       O  
ATOM    391  CB  PHE A 134       5.580  -3.635 -20.016  1.00 16.95           C  
ANISOU  391  CB  PHE A 134     1992   2011   2436    299    356      4       C  
ATOM    392  CG  PHE A 134       5.787  -5.122 -20.077  1.00 19.96           C  
ANISOU  392  CG  PHE A 134     2500   2499   2585    393    329     11       C  
ATOM    393  CD1 PHE A 134       4.709  -5.986 -20.024  1.00 21.70           C  
ANISOU  393  CD1 PHE A 134     2825   2672   2747    410    170     22       C  
ATOM    394  CD2 PHE A 134       7.060  -5.651 -20.220  1.00 22.87           C  
ANISOU  394  CD2 PHE A 134     2868   2986   2835    466    473     25       C  
ATOM    395  CE1 PHE A 134       4.907  -7.358 -20.102  1.00 20.56           C  
ANISOU  395  CE1 PHE A 134     2843   2572   2397    487    150     25       C  
ATOM    396  CE2 PHE A 134       7.257  -7.013 -20.309  1.00 26.72           C  
ANISOU  396  CE2 PHE A 134     3496   3515   3143    587    479     37       C  
ATOM    397  CZ  PHE A 134       6.183  -7.865 -20.246  1.00 22.70           C  
ANISOU  397  CZ  PHE A 134     3149   2932   2543    591    313     26       C  
ATOM    398  N   SER A 135       7.112  -1.174 -18.764  1.00 16.13           N  
ANISOU  398  N   SER A 135     1531   1900   2696     45    580   -181       N  
ATOM    399  CA  SER A 135       7.438   0.140 -19.298  1.00 18.17           C  
ANISOU  399  CA  SER A 135     1781   1989   3134    -57    663   -124       C  
ATOM    400  C   SER A 135       7.342   0.080 -20.818  1.00 20.20           C  
ANISOU  400  C   SER A 135     2223   2149   3302     17    678    103       C  
ATOM    401  O   SER A 135       7.467  -0.991 -21.421  1.00 21.80           O  
ANISOU  401  O   SER A 135     2556   2453   3275    121    671    181       O  
ATOM    402  CB  SER A 135       8.834   0.575 -18.863  1.00 22.79           C  
ANISOU  402  CB  SER A 135     2197   2687   3775   -209    745   -172       C  
ATOM    403  OG  SER A 135       9.809  -0.252 -19.461  1.00 28.75           O  
ANISOU  403  OG  SER A 135     2906   3617   4400   -135    821    -40       O  
ATOM    404  N   VAL A 136       7.096   1.233 -21.442  1.00 19.83           N  
ANISOU  404  N   VAL A 136     2239   1878   3417    -42    699    211       N  
ATOM    405  CA  VAL A 136       6.883   1.310 -22.886  1.00 20.99           C  
ANISOU  405  CA  VAL A 136     2627   1906   3442     -2    676    453       C  
ATOM    406  C   VAL A 136       7.623   2.516 -23.455  1.00 24.19           C  
ANISOU  406  C   VAL A 136     3051   2168   3974   -128    831    579       C  
ATOM    407  O   VAL A 136       7.588   3.607 -22.879  1.00 30.00           O  
ANISOU  407  O   VAL A 136     3662   2746   4992   -228    855    509       O  
ATOM    408  CB  VAL A 136       5.379   1.389 -23.244  1.00 35.30           C  
ANISOU  408  CB  VAL A 136     4544   3540   5329     72    440    556       C  
ATOM    409  CG1 VAL A 136       4.696   0.070 -22.975  1.00 37.20           C  
ANISOU  409  CG1 VAL A 136     4808   3915   5410    162    288    492       C  
ATOM    410  CG2 VAL A 136       4.697   2.487 -22.463  1.00 39.37           C  
ANISOU  410  CG2 VAL A 136     4878   3856   6225     56    432    477       C  
ATOM    411  N   ILE A 137       8.280   2.315 -24.600  1.00 26.48           N  
ANISOU  411  N   ILE A 137     3421   2958   3683    -76   1867    320       N  
ATOM    412  CA  ILE A 137       8.998   3.354 -25.333  1.00 34.21           C  
ANISOU  412  CA  ILE A 137     4654   3770   4575   -275   2069    234       C  
ATOM    413  C   ILE A 137       8.523   3.302 -26.774  1.00 41.05           C  
ANISOU  413  C   ILE A 137     5767   4510   5320   -279   2085    347       C  
ATOM    414  O   ILE A 137       8.570   2.239 -27.399  1.00 40.55           O  
ANISOU  414  O   ILE A 137     5597   4535   5277   -284   2049    350       O  
ATOM    415  CB  ILE A 137      10.530   3.163 -25.301  1.00 34.17           C  
ANISOU  415  CB  ILE A 137     4465   3873   4646   -515   2214     24       C  
ATOM    416  CG1 ILE A 137      11.048   2.863 -23.894  1.00 39.25           C  
ANISOU  416  CG1 ILE A 137     4788   4712   5413   -510   2126    -61       C  
ATOM    417  CG2 ILE A 137      11.237   4.394 -25.892  1.00 41.98           C  
ANISOU  417  CG2 ILE A 137     5739   4703   5509   -781   2423    -78       C  
ATOM    418  CD1 ILE A 137      11.089   4.060 -22.982  1.00 42.78           C  
ANISOU  418  CD1 ILE A 137     5365   5102   5789   -611   2180   -114       C  
ATOM    419  N   PHE A 138       8.075   4.440 -27.301  1.00 42.98           N  
ANISOU  419  N   PHE A 138     6370   4534   5427   -284   2133    440       N  
ATOM    420  CA  PHE A 138       7.626   4.536 -28.691  1.00 51.73           C  
ANISOU  420  CA  PHE A 138     7767   5515   6374   -318   2121    577       C  
ATOM    421  C   PHE A 138       6.691   3.383 -29.059  1.00 51.59           C  
ANISOU  421  C   PHE A 138     7597   5647   6358   -159   1924    713       C  
ATOM    422  O   PHE A 138       6.873   2.708 -30.074  1.00 57.80           O  
ANISOU  422  O   PHE A 138     8439   6463   7061   -293   1949    708       O  
ATOM    423  CB  PHE A 138       8.818   4.576 -29.650  1.00 62.16           C  
ANISOU  423  CB  PHE A 138     9219   6794   7605   -655   2343    429       C  
ATOM    424  CG  PHE A 138       9.823   5.648 -29.339  1.00 73.55           C  
ANISOU  424  CG  PHE A 138    10768   8145   9031   -864   2486    253       C  
ATOM    425  CD1 PHE A 138       9.418   6.948 -29.077  1.00 78.69           C  
ANISOU  425  CD1 PHE A 138    11755   8547   9596   -834   2515    341       C  
ATOM    426  CD2 PHE A 138      11.178   5.352 -29.308  1.00 75.68           C  
ANISOU  426  CD2 PHE A 138    10807   8574   9376  -1080   2583     -1       C  
ATOM    427  CE1 PHE A 138      10.348   7.934 -28.788  1.00 81.56           C  
ANISOU  427  CE1 PHE A 138    12253   8819   9919  -1070   2653    164       C  
ATOM    428  CE2 PHE A 138      12.110   6.329 -29.018  1.00 79.01           C  
ANISOU  428  CE2 PHE A 138    11312   8947   9760  -1307   2700   -163       C  
ATOM    429  CZ  PHE A 138      11.695   7.624 -28.759  1.00 82.10           C  
ANISOU  429  CZ  PHE A 138    12070   9087  10038  -1328   2742    -88       C  
ATOM    430  N   ASP A 139       5.702   3.134 -28.198  1.00 41.90           N  
ANISOU  430  N   ASP A 139     6180   4529   5212     91   1746    812       N  
ATOM    431  CA  ASP A 139       4.683   2.097 -28.366  1.00 44.05           C  
ANISOU  431  CA  ASP A 139     6293   4971   5473    220   1547    945       C  
ATOM    432  C   ASP A 139       5.242   0.673 -28.312  1.00 41.82           C  
ANISOU  432  C   ASP A 139     5784   4836   5269    115   1550    833       C  
ATOM    433  O   ASP A 139       4.505  -0.289 -28.581  1.00 44.49           O  
ANISOU  433  O   ASP A 139     6046   5290   5570    150   1408    923       O  
ATOM    434  CB  ASP A 139       3.898   2.294 -29.672  1.00 54.33           C  
ANISOU  434  CB  ASP A 139     7848   6206   6588    221   1447   1134       C  
ATOM    435  CG  ASP A 139       2.472   1.758 -29.593  1.00 66.58           C  
ANISOU  435  CG  ASP A 139     9237   7944   8116    412   1203   1317       C  
ATOM    436  OD1 ASP A 139       1.603   2.461 -29.032  0.24 66.44           O  
ANISOU  436  OD1 ASP A 139     9169   7936   8139    654   1110   1422       O  
ATOM    437  OD2 ASP A 139       2.218   0.640 -30.099  1.00 70.43           O  
ANISOU  437  OD2 ASP A 139     9647   8572   8540    308   1117   1342       O  
ATOM    438  N   ARG A 140       6.510   0.498 -27.957  1.00 32.94           N  
ANISOU  438  N   ARG A 140     4549   3711   4256     -7   1700    640       N  
ATOM    439  CA  ARG A 140       7.135  -0.820 -27.859  1.00 29.36           C  
ANISOU  439  CA  ARG A 140     3879   3359   3918    -47   1704    529       C  
ATOM    440  C   ARG A 140       7.324  -1.199 -26.390  1.00 26.97           C  
ANISOU  440  C   ARG A 140     3293   3179   3775     58   1609    492       C  
ATOM    441  O   ARG A 140       7.804  -0.387 -25.588  1.00 26.45           O  
ANISOU  441  O   ARG A 140     3175   3118   3755     41   1663    425       O  
ATOM    442  CB  ARG A 140       8.475  -0.827 -28.591  1.00 33.41           C  
ANISOU  442  CB  ARG A 140     4423   3817   4455   -242   1936    333       C  
ATOM    443  CG  ARG A 140       9.228  -2.138 -28.529  1.00 29.96           C  
ANISOU  443  CG  ARG A 140     3753   3451   4177   -230   1967    193       C  
ATOM    444  CD  ARG A 140      10.516  -2.040 -29.348  1.00 34.05           C  
ANISOU  444  CD  ARG A 140     4275   3944   4719   -418   2239    -29       C  
ATOM    445  NE  ARG A 140      11.267  -3.295 -29.359  1.00 33.91           N  
ANISOU  445  NE  ARG A 140     4025   3974   4885   -351   2280   -182       N  
ATOM    446  CZ  ARG A 140      12.086  -3.674 -28.385  1.00 35.28           C  
ANISOU  446  CZ  ARG A 140     3877   4250   5276   -234   2210   -271       C  
ATOM    447  NH1 ARG A 140      12.248  -2.891 -27.324  1.00 31.85           N  
ANISOU  447  NH1 ARG A 140     3326   3904   4872   -224   2113   -234       N  
ATOM    448  NH2 ARG A 140      12.736  -4.831 -28.468  1.00 33.00           N  
ANISOU  448  NH2 ARG A 140     3405   3968   5166   -125   2232   -392       N  
ATOM    449  N   LEU A 141       6.935  -2.423 -26.035  1.00 24.45           N  
ANISOU  449  N   LEU A 141     2829   2950   3512    135   1464    543       N  
ATOM    450  CA  LEU A 141       7.116  -2.897 -24.665  1.00 23.47           C  
ANISOU  450  CA  LEU A 141     2474   2936   3507    208   1347    535       C  
ATOM    451  C   LEU A 141       8.600  -3.026 -24.365  1.00 27.23           C  
ANISOU  451  C   LEU A 141     2782   3424   4139    157   1439    366       C  
ATOM    452  O   LEU A 141       9.356  -3.593 -25.154  1.00 26.82           O  
ANISOU  452  O   LEU A 141     2709   3321   4159    121   1545    258       O  
ATOM    453  CB  LEU A 141       6.427  -4.246 -24.465  1.00 22.46           C  
ANISOU  453  CB  LEU A 141     2290   2863   3380    261   1176    635       C  
ATOM    454  CG  LEU A 141       4.915  -4.293 -24.636  1.00 22.89           C  
ANISOU  454  CG  LEU A 141     2428   2987   3282    286   1057    799       C  
ATOM    455  CD1 LEU A 141       4.444  -5.746 -24.615  1.00 23.21           C  
ANISOU  455  CD1 LEU A 141     2454   3060   3305    254    923    864       C  
ATOM    456  CD2 LEU A 141       4.281  -3.527 -23.510  1.00 27.29           C  
ANISOU  456  CD2 LEU A 141     2896   3658   3816    359   1000    854       C  
ATOM    457  N   GLU A 142       9.026  -2.513 -23.216  1.00 23.93           N  
ANISOU  457  N   GLU A 142     2225   3095   3771    147   1403    330       N  
ATOM    458  CA  GLU A 142      10.449  -2.400 -22.935  1.00 25.23           C  
ANISOU  458  CA  GLU A 142     2197   3322   4066     70   1483    170       C  
ATOM    459  C   GLU A 142      10.872  -3.340 -21.806  1.00 30.03           C  
ANISOU  459  C   GLU A 142     2548   4054   4806    157   1283    198       C  
ATOM    460  O   GLU A 142      11.563  -4.320 -22.062  1.00 35.01           O  
ANISOU  460  O   GLU A 142     3031   4680   5589    238   1259    149       O  
ATOM    461  CB  GLU A 142      10.814  -0.946 -22.618  1.00 34.05           C  
ANISOU  461  CB  GLU A 142     3386   4444   5107    -81   1611     87       C  
ATOM    462  CG  GLU A 142      12.291  -0.709 -22.430  1.00 38.10           C  
ANISOU  462  CG  GLU A 142     3686   5067   5722   -227   1711    -94       C  
ATOM    463  CD  GLU A 142      13.090  -0.820 -23.729  1.00 54.56           C  
ANISOU  463  CD  GLU A 142     5802   7103   7823   -308   1870   -226       C  
ATOM    464  OE1 GLU A 142      12.497  -0.690 -24.825  1.00 44.38           O  
ANISOU  464  OE1 GLU A 142     4772   5662   6429   -324   1974   -187       O  
ATOM    465  OE2 GLU A 142      14.323  -1.033 -23.646  1.00 64.38           O  
ANISOU  465  OE2 GLU A 142     6814   8482   9164   -361   1874   -363       O  
ATOM    466  N   THR A 143      10.475  -3.058 -20.569  1.00 27.60           N  
ANISOU  466  N   THR A 143     2205   3845   4436    146   1143    274       N  
ATOM    467  CA  THR A 143      11.001  -3.710 -19.367  1.00 33.15           C  
ANISOU  467  CA  THR A 143     2690   4685   5219    172    937    311       C  
ATOM    468  C   THR A 143       9.839  -4.214 -18.525  1.00 27.32           C  
ANISOU  468  C   THR A 143     2037   3978   4367    212    752    482       C  
ATOM    469  O   THR A 143       8.879  -3.473 -18.306  1.00 23.94           O  
ANISOU  469  O   THR A 143     1748   3558   3789    167    806    513       O  
ATOM    470  CB  THR A 143      11.836  -2.720 -18.529  1.00 40.28           C  
ANISOU  470  CB  THR A 143     3472   5733   6100     10    962    206       C  
ATOM    471  OG1 THR A 143      12.971  -2.267 -19.278  1.00 46.82           O  
ANISOU  471  OG1 THR A 143     4192   6574   7022    -77   1144     34       O  
ATOM    472  CG2 THR A 143      12.307  -3.356 -17.226  1.00 47.04           C  
ANISOU  472  CG2 THR A 143     4119   6758   6996     15    702    278       C  
ATOM    473  N   LEU A 144       9.913  -5.460 -18.046  1.00 25.72           N  
ANISOU  473  N   LEU A 144     2499   2859   4414    282   -287    318       N  
ATOM    474  CA  LEU A 144       8.882  -5.936 -17.122  1.00 24.11           C  
ANISOU  474  CA  LEU A 144     2398   2596   4166    258   -318    134       C  
ATOM    475  C   LEU A 144       9.005  -5.210 -15.782  1.00 26.52           C  
ANISOU  475  C   LEU A 144     2750   2809   4517    -54   -183   -160       C  
ATOM    476  O   LEU A 144      10.077  -5.204 -15.166  1.00 23.49           O  
ANISOU  476  O   LEU A 144     2314   2621   3989   -270   -247   -286       O  
ATOM    477  CB  LEU A 144       8.994  -7.442 -16.904  1.00 23.82           C  
ANISOU  477  CB  LEU A 144     2421   2851   3780    364   -548    147       C  
ATOM    478  CG  LEU A 144       7.986  -8.029 -15.909  1.00 21.82           C  
ANISOU  478  CG  LEU A 144     2234   2551   3507    334   -583      7       C  
ATOM    479  CD1 LEU A 144       6.559  -7.949 -16.461  1.00 18.44           C  
ANISOU  479  CD1 LEU A 144     1898   1967   3141    393   -454     98       C  
ATOM    480  CD2 LEU A 144       8.328  -9.474 -15.510  1.00 23.68           C  
ANISOU  480  CD2 LEU A 144     2625   3058   3316    328   -645     18       C  
ATOM    481  N   ILE A 145       7.917  -4.586 -15.328  1.00 19.32           N  
ANISOU  481  N   ILE A 145     1942   1618   3781    -53     -5   -265       N  
ATOM    482  CA  ILE A 145       7.923  -3.962 -14.008  1.00 19.49           C  
ANISOU  482  CA  ILE A 145     2085   1531   3788   -279    114   -561       C  
ATOM    483  C   ILE A 145       7.386  -4.916 -12.946  1.00 23.03           C  
ANISOU  483  C   ILE A 145     2582   2153   4016   -232     44   -681       C  
ATOM    484  O   ILE A 145       7.943  -5.021 -11.848  1.00 20.66           O  
ANISOU  484  O   ILE A 145     2344   1987   3519   -394      2   -910       O  
ATOM    485  CB  ILE A 145       7.121  -2.643 -14.028  1.00 21.70           C  
ANISOU  485  CB  ILE A 145     2510   1395   4341   -256    394   -605       C  
ATOM    486  CG1 ILE A 145       7.678  -1.669 -15.079  1.00 23.11           C  
ANISOU  486  CG1 ILE A 145     2671   1364   4747   -304    499   -462       C  
ATOM    487  CG2 ILE A 145       7.119  -1.999 -12.653  1.00 28.88           C  
ANISOU  487  CG2 ILE A 145     3624   2159   5188   -444    506   -932       C  
ATOM    488  CD1 ILE A 145       9.165  -1.395 -14.976  1.00 31.09           C  
ANISOU  488  CD1 ILE A 145     3608   2485   5722   -633    406   -534       C  
ATOM    489  N   LEU A 146       6.293  -5.608 -13.245  1.00 16.93           N  
ANISOU  489  N   LEU A 146     1776   1385   3273    -17     29   -519       N  
ATOM    490  CA  LEU A 146       5.624  -6.459 -12.276  1.00 16.51           C  
ANISOU  490  CA  LEU A 146     1756   1452   3064     26     15   -574       C  
ATOM    491  C   LEU A 146       4.705  -7.406 -13.030  1.00 18.26           C  
ANISOU  491  C   LEU A 146     1881   1715   3342    202   -103   -322       C  
ATOM    492  O   LEU A 146       4.022  -6.989 -13.967  1.00 18.37           O  
ANISOU  492  O   LEU A 146     1820   1580   3578    329    -62   -160       O  
ATOM    493  CB  LEU A 146       4.811  -5.628 -11.274  1.00 22.38           C  
ANISOU  493  CB  LEU A 146     2614   2003   3887     33    279   -728       C  
ATOM    494  CG  LEU A 146       3.931  -6.425 -10.295  1.00 23.78           C  
ANISOU  494  CG  LEU A 146     2799   2299   3938    126    335   -716       C  
ATOM    495  CD1 LEU A 146       4.800  -7.186  -9.315  1.00 26.62           C  
ANISOU  495  CD1 LEU A 146     3241   2907   3968     25    210   -886       C  
ATOM    496  CD2 LEU A 146       2.947  -5.500  -9.547  1.00 28.23           C  
ANISOU  496  CD2 LEU A 146     3462   2665   4601    243    645   -785       C  
ATOM    497  N   LEU A 147       4.717  -8.684 -12.638  1.00 16.27           N  
ANISOU  497  N   LEU A 147     1648   1659   2876    206   -265   -290       N  
ATOM    498  CA  LEU A 147       3.768  -9.663 -13.148  1.00 17.45           C  
ANISOU  498  CA  LEU A 147     1739   1813   3077    301   -402    -80       C  
ATOM    499  C   LEU A 147       3.117 -10.364 -11.965  1.00 17.77           C  
ANISOU  499  C   LEU A 147     1802   1926   3023    255   -327   -100       C  
ATOM    500  O   LEU A 147       3.803 -10.753 -11.019  1.00 15.29           O  
ANISOU  500  O   LEU A 147     1603   1754   2453    202   -319   -242       O  
ATOM    501  CB  LEU A 147       4.446 -10.706 -14.066  1.00 16.34           C  
ANISOU  501  CB  LEU A 147     1711   1811   2686    325   -631     27       C  
ATOM    502  CG  LEU A 147       3.569 -11.859 -14.608  1.00 19.38           C  
ANISOU  502  CG  LEU A 147     2186   2227   2951    289   -647    148       C  
ATOM    503  CD1 LEU A 147       4.153 -12.357 -15.922  1.00 21.35           C  
ANISOU  503  CD1 LEU A 147     2559   2508   3043    294   -664    161       C  
ATOM    504  CD2 LEU A 147       3.450 -13.037 -13.613  1.00 16.66           C  
ANISOU  504  CD2 LEU A 147     1905   1934   2490    251   -732    150       C  
ATOM    505  N   ARG A 148       1.800 -10.550 -12.030  1.00 16.99           N  
ANISOU  505  N   ARG A 148     1572   1759   3124    288   -271     70       N  
ATOM    506  CA  ARG A 148       1.080 -11.250 -10.979  1.00 15.64           C  
ANISOU  506  CA  ARG A 148     1383   1660   2901    248   -171    126       C  
ATOM    507  C   ARG A 148       0.132 -12.267 -11.595  1.00 15.88           C  
ANISOU  507  C   ARG A 148     1289   1676   3068    202   -364    381       C  
ATOM    508  O   ARG A 148      -0.440 -12.037 -12.661  1.00 20.90           O  
ANISOU  508  O   ARG A 148     1782   2239   3921    239   -480    512       O  
ATOM    509  CB  ARG A 148       0.312 -10.260 -10.061  1.00 17.87           C  
ANISOU  509  CB  ARG A 148     1597   1897   3298    323    185     84       C  
ATOM    510  CG  ARG A 148       1.228  -9.560  -9.050  1.00 18.46           C  
ANISOU  510  CG  ARG A 148     1876   1984   3153    325    341   -212       C  
ATOM    511  CD  ARG A 148       0.493  -8.624  -8.091  1.00 22.18           C  
ANISOU  511  CD  ARG A 148     2378   2381   3670    454    687   -274       C  
ATOM    512  NE  ARG A 148       1.366  -8.284  -6.973  1.00 24.62           N  
ANISOU  512  NE  ARG A 148     2929   2727   3696    438    762   -576       N  
ATOM    513  CZ  ARG A 148       0.999  -7.608  -5.887  1.00 24.69           C  
ANISOU  513  CZ  ARG A 148     3082   2688   3610    575   1031   -706       C  
ATOM    514  NH1 ARG A 148      -0.245  -7.156  -5.745  1.00 26.66           N  
ANISOU  514  NH1 ARG A 148     3243   2862   4025    772   1301   -530       N  
ATOM    515  NH2 ARG A 148       1.897  -7.390  -4.930  1.00 25.70           N  
ANISOU  515  NH2 ARG A 148     3449   2868   3449    542   1021  -1010       N  
ATOM    516  N   ALA A 149      -0.015 -13.396 -10.918  1.00 19.49           N  
ANISOU  516  N   ALA A 149     1816   2198   3390    114   -409    449       N  
ATOM    517  CA  ALA A 149      -0.905 -14.466 -11.339  1.00 21.59           C  
ANISOU  517  CA  ALA A 149     1997   2420   3787     -6   -606    685       C  
ATOM    518  C   ALA A 149      -2.174 -14.404 -10.508  1.00 20.71           C  
ANISOU  518  C   ALA A 149     1637   2355   3879    -56   -346    869       C  
ATOM    519  O   ALA A 149      -2.102 -14.345  -9.274  1.00 26.99           O  
ANISOU  519  O   ALA A 149     2489   3232   4535     -9    -73    819       O  
ATOM    520  CB  ALA A 149      -0.228 -15.830 -11.173  1.00 20.29           C  
ANISOU  520  CB  ALA A 149     2117   2254   3338    -74   -816    679       C  
ATOM    521  N   PHE A 150      -3.331 -14.452 -11.178  1.00 21.68           N  
ANISOU  521  N   PHE A 150     1471   2458   4308   -131   -437   1098       N  
ATOM    522  CA  PHE A 150      -4.630 -14.299 -10.532  1.00 25.61           C  
ANISOU  522  CA  PHE A 150     1637   3056   5036   -155   -180   1339       C  
ATOM    523  C   PHE A 150      -5.539 -15.483 -10.841  1.00 27.02           C  
ANISOU  523  C   PHE A 150     1677   3218   5373   -413   -412   1601       C  
ATOM    524  O   PHE A 150      -5.606 -15.933 -11.987  1.00 38.73           O  
ANISOU  524  O   PHE A 150     3287   4584   6842   -494   -756   1579       O  
ATOM    525  CB  PHE A 150      -5.343 -13.022 -11.010  1.00 31.29           C  
ANISOU  525  CB  PHE A 150     2167   3805   5918     26    -18   1365       C  
ATOM    526  CG  PHE A 150      -4.608 -11.760 -10.705  1.00 25.87           C  
ANISOU  526  CG  PHE A 150     1591   3084   5154    260    232   1141       C  
ATOM    527  CD1 PHE A 150      -3.630 -11.285 -11.566  1.00 23.81           C  
ANISOU  527  CD1 PHE A 150     1540   2707   4801    304     64    932       C  
ATOM    528  CD2 PHE A 150      -4.909 -11.029  -9.572  1.00 28.57           C  
ANISOU  528  CD2 PHE A 150     1918   3484   5453    434    641   1123       C  
ATOM    529  CE1 PHE A 150      -2.957 -10.115 -11.287  1.00 21.52           C  
ANISOU  529  CE1 PHE A 150     1395   2340   4443    460    282    719       C  
ATOM    530  CE2 PHE A 150      -4.241  -9.852  -9.293  1.00 28.82           C  
ANISOU  530  CE2 PHE A 150     2176   3415   5359    612    839    863       C  
ATOM    531  CZ  PHE A 150      -3.264  -9.394 -10.156  1.00 23.43           C  
ANISOU  531  CZ  PHE A 150     1667   2596   4638    591    652    661       C  
ATOM    532  N   THR A 151      -6.275 -15.951  -9.830  1.00 31.04           N  
ANISOU  532  N   THR A 151     2035   3816   5941   -499   -186   1810       N  
ATOM    533  CA  THR A 151      -7.344 -16.921 -10.060  1.00 33.01           C  
ANISOU  533  CA  THR A 151     2176   4051   6316   -715   -363   2035       C  
ATOM    534  C   THR A 151      -8.630 -16.211 -10.494  1.00 43.25           C  
ANISOU  534  C   THR A 151     3172   5467   7792   -630   -294   2177       C  
ATOM    535  O   THR A 151      -8.688 -14.984 -10.604  1.00 42.06           O  
ANISOU  535  O   THR A 151     2956   5384   7643   -391    -98   2101       O  
ATOM    536  CB  THR A 151      -7.621 -17.743  -8.808  1.00 40.57           C  
ANISOU  536  CB  THR A 151     3113   5058   7244   -829   -137   2216       C  
ATOM    537  OG1 THR A 151      -8.073 -16.871  -7.763  1.00 40.83           O  
ANISOU  537  OG1 THR A 151     2957   5276   7281   -591    329   2300       O  
ATOM    538  CG2 THR A 151      -6.372 -18.511  -8.362  1.00 33.29           C  
ANISOU  538  CG2 THR A 151     2563   4004   6082   -912   -182   2109       C  
ATOM    539  N   GLU A 152      -9.694 -16.997 -10.703  1.00 45.53           N  
ANISOU  539  N   GLU A 152     3289   5784   8225   -836   -445   2394       N  
ATOM    540  CA  GLU A 152     -10.984 -16.433 -11.103  1.00 51.16           C  
ANISOU  540  CA  GLU A 152     3683   6652   9104   -788   -397   2569       C  
ATOM    541  C   GLU A 152     -11.615 -15.615  -9.984  1.00 51.53           C  
ANISOU  541  C   GLU A 152     3501   6905   9174   -563     63   2724       C  
ATOM    542  O   GLU A 152     -12.251 -14.586 -10.245  1.00 51.12           O  
ANISOU  542  O   GLU A 152     3284   6977   9161   -359    205   2773       O  
ATOM    543  CB  GLU A 152     -11.943 -17.539 -11.530  1.00 57.86           C  
ANISOU  543  CB  GLU A 152     4379   7496  10108  -1099   -679   2768       C  
ATOM    544  CG  GLU A 152     -11.572 -18.238 -12.811  1.00 63.36           C  
ANISOU  544  CG  GLU A 152     5318   7989  10767  -1269  -1145   2626       C  
ATOM    545  CD  GLU A 152     -12.667 -19.176 -13.274  1.00 81.01           C  
ANISOU  545  CD  GLU A 152     7374  10231  13174  -1574  -1415   2817       C  
ATOM    546  OE1 GLU A 152     -13.860 -18.812 -13.140  1.00 87.22           O  
ANISOU  546  OE1 GLU A 152     7763  11240  14137  -1590  -1287   3037       O  
ATOM    547  OE2 GLU A 152     -12.337 -20.278 -13.759  1.00 84.10           O  
ANISOU  547  OE2 GLU A 152     8032  10408  13516  -1792  -1757   2751       O  
ATOM    548  N   GLU A 153     -11.483 -16.066  -8.737  1.00 54.61           N  
ANISOU  548  N   GLU A 153     3910   7332   9509   -568    312   2813       N  
ATOM    549  CA  GLU A 153     -11.904 -15.245  -7.607  1.00 62.26           C  
ANISOU  549  CA  GLU A 153     4766   8469  10419   -274    773   2922       C  
ATOM    550  C   GLU A 153     -11.065 -13.984  -7.460  1.00 60.81           C  
ANISOU  550  C   GLU A 153     4795   8245  10063     43    985   2658       C  
ATOM    551  O   GLU A 153     -11.304 -13.200  -6.534  1.00 64.54           O  
ANISOU  551  O   GLU A 153     5277   8815  10430    334   1360   2691       O  
ATOM    552  CB  GLU A 153     -11.848 -16.053  -6.306  1.00 70.88           C  
ANISOU  552  CB  GLU A 153     5896   9595  11439   -316   1004   3056       C  
ATOM    553  CG  GLU A 153     -12.932 -17.112  -6.174  1.00 80.57           C  
ANISOU  553  CG  GLU A 153     6864  10894  12856   -582    919   3378       C  
ATOM    554  CD  GLU A 153     -12.499 -18.479  -6.673  1.00 86.68           C  
ANISOU  554  CD  GLU A 153     7800  11466  13670   -973    550   3328       C  
ATOM    555  OE1 GLU A 153     -11.283 -18.694  -6.866  1.00 87.30           O  
ANISOU  555  OE1 GLU A 153     8214  11371  13585   -999    420   3076       O  
ATOM    556  OE2 GLU A 153     -13.379 -19.343  -6.866  1.00 92.38           O  
ANISOU  556  OE2 GLU A 153     8330  12197  14575  -1254    388   3547       O  
ATOM    557  N   GLY A 154     -10.086 -13.779  -8.339  1.00 55.83           N  
ANISOU  557  N   GLY A 154     4366   7460   9389      3    750   2395       N  
ATOM    558  CA  GLY A 154      -9.259 -12.596  -8.315  1.00 45.77           C  
ANISOU  558  CA  GLY A 154     3292   6119   7979    258    916   2131       C  
ATOM    559  C   GLY A 154      -8.102 -12.640  -7.346  1.00 42.65           C  
ANISOU  559  C   GLY A 154     3141   5679   7385    337   1109   1933       C  
ATOM    560  O   GLY A 154      -7.379 -11.643  -7.234  1.00 38.10           O  
ANISOU  560  O   GLY A 154     2756   5035   6686    542   1254   1681       O  
ATOM    561  N   ALA A 155      -7.897 -13.757  -6.651  1.00 40.80           N  
ANISOU  561  N   ALA A 155     2935   5474   7093    180   1120   2029       N  
ATOM    562  CA  ALA A 155      -6.811 -13.853  -5.686  1.00 34.55           C  
ANISOU  562  CA  ALA A 155     2399   4683   6044    279   1332   1849       C  
ATOM    563  C   ALA A 155      -5.464 -13.960  -6.388  1.00 36.99           C  
ANISOU  563  C   ALA A 155     3058   4828   6168    184    978   1495       C  
ATOM    564  O   ALA A 155      -5.334 -14.614  -7.430  1.00 31.39           O  
ANISOU  564  O   ALA A 155     2333   4025   5568    -37    603   1529       O  
ATOM    565  CB  ALA A 155      -7.007 -15.065  -4.771  1.00 36.40           C  
ANISOU  565  CB  ALA A 155     2658   4979   6193    155   1433   2063       C  
ATOM    566  N   ILE A 156      -4.456 -13.325  -5.797  1.00 29.06           N  
ANISOU  566  N   ILE A 156     2372   3803   4865    362   1093   1164       N  
ATOM    567  CA  ILE A 156      -3.081 -13.409  -6.287  1.00 26.23           C  
ANISOU  567  CA  ILE A 156     2314   3357   4295    293    807    853       C  
ATOM    568  C   ILE A 156      -2.477 -14.719  -5.809  1.00 29.03           C  
ANISOU  568  C   ILE A 156     2884   3749   4397    189    680    857       C  
ATOM    569  O   ILE A 156      -2.578 -15.061  -4.625  1.00 27.62           O  
ANISOU  569  O   ILE A 156     2788   3668   4036    284    922    901       O  
ATOM    570  CB  ILE A 156      -2.256 -12.219  -5.783  1.00 26.91           C  
ANISOU  570  CB  ILE A 156     2621   3425   4177    475    963    511       C  
ATOM    571  CG1 ILE A 156      -2.854 -10.900  -6.268  1.00 29.57           C  
ANISOU  571  CG1 ILE A 156     2817   3669   4749    607   1115    516       C  
ATOM    572  CG2 ILE A 156      -0.793 -12.362  -6.193  1.00 22.45           C  
ANISOU  572  CG2 ILE A 156     2301   2838   3390    386    681    235       C  
ATOM    573  CD1 ILE A 156      -2.343  -9.711  -5.507  1.00 27.85           C  
ANISOU  573  CD1 ILE A 156     2850   3386   4348    789   1343    217       C  
ATOM    574  N   VAL A 157      -1.844 -15.461  -6.718  1.00 23.06           N  
ANISOU  574  N   VAL A 157     2254   2913   3595     43    319    822       N  
ATOM    575  CA  VAL A 157      -1.227 -16.735  -6.358  1.00 25.44           C  
ANISOU  575  CA  VAL A 157     2819   3224   3622    -14    192    834       C  
ATOM    576  C   VAL A 157       0.204 -16.857  -6.857  1.00 22.78           C  
ANISOU  576  C   VAL A 157     2756   2904   2995     40    -63    585       C  
ATOM    577  O   VAL A 157       0.842 -17.887  -6.622  1.00 25.32           O  
ANISOU  577  O   VAL A 157     3336   3252   3035     56   -174    584       O  
ATOM    578  CB  VAL A 157      -2.065 -17.939  -6.845  1.00 29.72           C  
ANISOU  578  CB  VAL A 157     3290   3636   4365   -247     11   1143       C  
ATOM    579  CG1 VAL A 157      -3.498 -17.867  -6.297  1.00 29.25           C  
ANISOU  579  CG1 VAL A 157     2881   3623   4611   -321    282   1452       C  
ATOM    580  CG2 VAL A 157      -2.054 -18.031  -8.360  1.00 27.52           C  
ANISOU  580  CG2 VAL A 157     2983   3216   4256   -368   -379   1144       C  
ATOM    581  N   GLY A 158       0.734 -15.838  -7.522  1.00 20.10           N  
ANISOU  581  N   GLY A 158     2367   2563   2705     90   -135    403       N  
ATOM    582  CA  GLY A 158       2.123 -15.844  -7.933  1.00 17.88           C  
ANISOU  582  CA  GLY A 158     2281   2356   2156    153   -333    203       C  
ATOM    583  C   GLY A 158       2.543 -14.455  -8.351  1.00 22.05           C  
ANISOU  583  C   GLY A 158     2703   2879   2797    184   -290     22       C  
ATOM    584  O   GLY A 158       1.710 -13.570  -8.571  1.00 19.78           O  
ANISOU  584  O   GLY A 158     2229   2483   2802    176   -150     68       O  
ATOM    585  N   GLU A 159       3.850 -14.271  -8.442  1.00 17.16           N  
ANISOU  585  N   GLU A 159     2201   2385   1935    225   -397   -162       N  
ATOM    586  CA  GLU A 159       4.387 -12.952  -8.729  1.00 14.18           C  
ANISOU  586  CA  GLU A 159     1744   1988   1655    206   -347   -336       C  
ATOM    587  C   GLU A 159       5.796 -13.106  -9.287  1.00 24.67           C  
ANISOU  587  C   GLU A 159     3138   3473   2761    225   -557   -411       C  
ATOM    588  O   GLU A 159       6.568 -13.932  -8.805  1.00 22.64           O  
ANISOU  588  O   GLU A 159     2999   3369   2232    251   -582   -401       O  
ATOM    589  CB  GLU A 159       4.403 -12.091  -7.464  1.00 19.61           C  
ANISOU  589  CB  GLU A 159     2467   2712   2273    209    -98   -554       C  
ATOM    590  CG  GLU A 159       4.894 -10.665  -7.668  1.00 25.94           C  
ANISOU  590  CG  GLU A 159     3241   3419   3196    143    -37   -752       C  
ATOM    591  CD  GLU A 159       4.717  -9.828  -6.409  1.00 38.01           C  
ANISOU  591  CD  GLU A 159     4880   4914   4649    166    197   -979       C  
ATOM    592  OE1 GLU A 159       5.198 -10.248  -5.335  1.00 49.10           O  
ANISOU  592  OE1 GLU A 159     6410   6509   5736    203    201  -1124       O  
ATOM    593  OE2 GLU A 159       4.073  -8.770  -6.490  1.00 39.48           O  
ANISOU  593  OE2 GLU A 159     5057   4881   5063    189    379  -1006       O  
ATOM    594  N   ILE A 160       6.111 -12.316 -10.306  1.00 19.04           N  
ANISOU  594  N   ILE A 160     2326   2680   2229    204   -613   -401       N  
ATOM    595  CA  ILE A 160       7.475 -12.154 -10.808  1.00 19.23           C  
ANISOU  595  CA  ILE A 160     2351   2831   2124    188   -669   -399       C  
ATOM    596  C   ILE A 160       7.823 -10.682 -10.662  1.00 20.46           C  
ANISOU  596  C   ILE A 160     2395   2956   2422     71   -605   -621       C  
ATOM    597  O   ILE A 160       7.100  -9.825 -11.176  1.00 16.47           O  
ANISOU  597  O   ILE A 160     1828   2198   2232     52   -485   -578       O  
ATOM    598  CB  ILE A 160       7.587 -12.599 -12.276  1.00 15.47           C  
ANISOU  598  CB  ILE A 160     1883   2255   1740    219   -660   -142       C  
ATOM    599  CG1 ILE A 160       7.284 -14.091 -12.400  1.00 13.78           C  
ANISOU  599  CG1 ILE A 160     1784   2000   1452    248   -633    -35       C  
ATOM    600  CG2 ILE A 160       8.986 -12.247 -12.851  1.00 16.98           C  
ANISOU  600  CG2 ILE A 160     2041   2536   1876    184   -632    -94       C  
ATOM    601  CD1 ILE A 160       7.157 -14.589 -13.847  1.00 17.69           C  
ANISOU  601  CD1 ILE A 160     2346   2358   2018    318   -657     22       C  
ATOM    602  N   SER A 161       8.915 -10.376  -9.967  1.00 19.28           N  
ANISOU  602  N   SER A 161     2256   2975   2093    -32   -584   -758       N  
ATOM    603  CA  SER A 161       9.251  -8.973  -9.766  1.00 25.24           C  
ANISOU  603  CA  SER A 161     2946   3644   3002   -228   -514  -1001       C  
ATOM    604  C   SER A 161      10.758  -8.820  -9.761  1.00 29.18           C  
ANISOU  604  C   SER A 161     3389   4334   3364   -320   -585   -940       C  
ATOM    605  O   SER A 161      11.474  -9.781  -9.455  1.00 25.77           O  
ANISOU  605  O   SER A 161     3008   4060   2723   -212   -623   -784       O  
ATOM    606  CB  SER A 161       8.643  -8.411  -8.465  1.00 30.44           C  
ANISOU  606  CB  SER A 161     3738   4175   3651   -287   -336  -1244       C  
ATOM    607  OG  SER A 161       8.826  -9.274  -7.358  1.00 39.47           O  
ANISOU  607  OG  SER A 161     4985   5516   4496   -195   -346  -1220       O  
ATOM    608  N   PRO A 162      11.273  -7.654 -10.142  1.00 33.11           N  
ANISOU  608  N   PRO A 162     3779   4755   4048   -528   -578  -1044       N  
ATOM    609  CA  PRO A 162      12.720  -7.426 -10.088  1.00 33.46           C  
ANISOU  609  CA  PRO A 162     3718   5002   3995   -648   -664  -1002       C  
ATOM    610  C   PRO A 162      13.207  -7.326  -8.656  1.00 39.92           C  
ANISOU  610  C   PRO A 162     4628   5905   4633   -726   -677  -1180       C  
ATOM    611  O   PRO A 162      12.492  -6.871  -7.759  1.00 41.24           O  
ANISOU  611  O   PRO A 162     4952   5905   4812   -771   -597  -1385       O  
ATOM    612  CB  PRO A 162      12.902  -6.090 -10.817  1.00 40.19           C  
ANISOU  612  CB  PRO A 162     4445   5655   5170   -906   -616  -1058       C  
ATOM    613  CG  PRO A 162      11.651  -5.906 -11.614  1.00 43.52           C  
ANISOU  613  CG  PRO A 162     4908   5762   5864   -786   -488   -997       C  
ATOM    614  CD  PRO A 162      10.567  -6.550 -10.812  1.00 39.26           C  
ANISOU  614  CD  PRO A 162     4540   5172   5205   -621   -442  -1088       C  
ATOM    615  N   LEU A 163      14.429  -7.759  -8.454  1.00 70.94           N  
ANISOU  615  N   LEU A 163     6856   9452  10648  -1363   -292   -351       N  
ATOM    616  CA  LEU A 163      15.063  -7.523  -7.168  1.00 74.69           C  
ANISOU  616  CA  LEU A 163     7069  10282  11026  -1450   -573   -542       C  
ATOM    617  C   LEU A 163      15.792  -6.190  -7.205  1.00 71.09           C  
ANISOU  617  C   LEU A 163     6367   9661  10984  -1582   -677   -806       C  
ATOM    618  O   LEU A 163      16.531  -5.925  -8.160  1.00 71.43           O  
ANISOU  618  O   LEU A 163     6315   9421  11403  -1606   -550   -629       O  
ATOM    619  CB  LEU A 163      16.039  -8.638  -6.826  1.00 83.52           C  
ANISOU  619  CB  LEU A 163     8076  11599  12058  -1364   -670   -242       C  
ATOM    620  CG  LEU A 163      15.386  -9.976  -6.485  1.00 88.10           C  
ANISOU  620  CG  LEU A 163     8874  12373  12225  -1278   -717     26       C  
ATOM    621  CD1 LEU A 163      16.409 -10.955  -5.924  1.00 91.86           C  
ANISOU  621  CD1 LEU A 163     9218  13056  12628  -1208   -922    259       C  
ATOM    622  CD2 LEU A 163      14.239  -9.761  -5.509  1.00 90.38           C  
ANISOU  622  CD2 LEU A 163     9225  13011  12105  -1387   -821   -179       C  
ATOM    623  N   PRO A 164      15.599  -5.328  -6.209  1.00 69.13           N  
ANISOU  623  N   PRO A 164     5996   9596  10674  -1669   -935  -1219       N  
ATOM    624  CA  PRO A 164      16.277  -4.022  -6.246  1.00 72.09           C  
ANISOU  624  CA  PRO A 164     6153   9739  11500  -1810  -1123  -1471       C  
ATOM    625  C   PRO A 164      17.790  -4.140  -6.255  1.00 72.82           C  
ANISOU  625  C   PRO A 164     5946   9844  11876  -1876  -1195  -1251       C  
ATOM    626  O   PRO A 164      18.465  -3.373  -6.953  1.00 69.35           O  
ANISOU  626  O   PRO A 164     5353   9101  11895  -2014  -1201  -1180       O  
ATOM    627  CB  PRO A 164      15.760  -3.327  -4.978  1.00 76.02           C  
ANISOU  627  CB  PRO A 164     6581  10528  11776  -1808  -1451  -1992       C  
ATOM    628  CG  PRO A 164      15.312  -4.442  -4.084  1.00 74.47           C  
ANISOU  628  CG  PRO A 164     6435  10863  10996  -1698  -1439  -1904       C  
ATOM    629  CD  PRO A 164      14.790  -5.509  -4.993  1.00 69.30           C  
ANISOU  629  CD  PRO A 164     6045  10080  10207  -1632  -1105  -1469       C  
ATOM    630  N   SER A 165      18.337  -5.112  -5.521  1.00 80.11           N  
ANISOU  630  N   SER A 165     6773  11131  12534  -1792  -1261  -1108       N  
ATOM    631  CA  SER A 165      19.773  -5.290  -5.350  1.00 89.34           C  
ANISOU  631  CA  SER A 165     7637  12393  13914  -1826  -1366   -944       C  
ATOM    632  C   SER A 165      20.443  -6.000  -6.531  1.00 89.91           C  
ANISOU  632  C   SER A 165     7682  12325  14154  -1737  -1092   -503       C  
ATOM    633  O   SER A 165      21.584  -6.458  -6.391  1.00 94.13           O  
ANISOU  633  O   SER A 165     7975  13027  14763  -1696  -1153   -331       O  
ATOM    634  CB  SER A 165      20.050  -6.064  -4.057  1.00 91.43           C  
ANISOU  634  CB  SER A 165     7821  13115  13805  -1751  -1577   -984       C  
ATOM    635  OG  SER A 165      19.422  -5.453  -2.943  1.00 91.94           O  
ANISOU  635  OG  SER A 165     7874  13419  13639  -1788  -1826  -1407       O  
ATOM    636  N   LEU A 166      19.781  -6.103  -7.679  1.00 85.81           N  
ANISOU  636  N   LEU A 166     7385  11538  13679  -1677   -809   -341       N  
ATOM    637  CA  LEU A 166      20.335  -6.795  -8.831  1.00 84.76           C  
ANISOU  637  CA  LEU A 166     7224  11332  13651  -1529   -556     33       C  
ATOM    638  C   LEU A 166      20.156  -5.951 -10.084  1.00 84.76           C  
ANISOU  638  C   LEU A 166     7230  11004  13973  -1630   -341    118       C  
ATOM    639  O   LEU A 166      19.237  -5.129 -10.155  1.00 83.02           O  
ANISOU  639  O   LEU A 166     7182  10545  13815  -1756   -352    -92       O  
ATOM    640  CB  LEU A 166      19.666  -8.166  -9.024  1.00 81.48           C  
ANISOU  640  CB  LEU A 166     7119  10966  12873  -1272   -438    216       C  
ATOM    641  CG  LEU A 166      19.938  -9.206  -7.930  1.00 79.00           C  
ANISOU  641  CG  LEU A 166     6802  10970  12246  -1172   -670    256       C  
ATOM    642  CD1 LEU A 166      19.245 -10.521  -8.251  1.00 71.66           C  
ANISOU  642  CD1 LEU A 166     6197   9999  11030   -952   -615    487       C  
ATOM    643  CD2 LEU A 166      21.437  -9.414  -7.735  1.00 78.25           C  
ANISOU  643  CD2 LEU A 166     6353  11067  12313  -1125   -790    354       C  
ATOM    644  N   PRO A 167      21.030  -6.129 -11.096  1.00 87.37           N  
ANISOU  644  N   PRO A 167     7350  11351  14495  -1568   -157    426       N  
ATOM    645  CA  PRO A 167      20.923  -5.313 -12.317  1.00 85.28           C  
ANISOU  645  CA  PRO A 167     7048  10833  14522  -1693     43    571       C  
ATOM    646  C   PRO A 167      19.734  -5.697 -13.187  1.00 74.90           C  
ANISOU  646  C   PRO A 167     6124   9294  13042  -1524    303    620       C  
ATOM    647  O   PRO A 167      18.954  -6.583 -12.822  1.00 69.06           O  
ANISOU  647  O   PRO A 167     5686   8580  11973  -1330    311    545       O  
ATOM    648  CB  PRO A 167      22.255  -5.574 -13.033  1.00 89.24           C  
ANISOU  648  CB  PRO A 167     7156  11585  15168  -1632    164    905       C  
ATOM    649  CG  PRO A 167      22.697  -6.907 -12.533  1.00 91.32           C  
ANISOU  649  CG  PRO A 167     7418  12147  15132  -1320    117    936       C  
ATOM    650  CD  PRO A 167      22.224  -6.994 -11.110  1.00 92.34           C  
ANISOU  650  CD  PRO A 167     7715  12290  15081  -1388   -161    642       C  
ATOM    651  N   GLY A 168      19.593  -5.042 -14.342  1.00 65.25           N  
ANISOU  651  N   GLY A 168     4888   7858  12047  -1615    498    775       N  
ATOM    652  CA  GLY A 168      18.404  -5.210 -15.151  1.00 58.96           C  
ANISOU  652  CA  GLY A 168     4466   6804  11133  -1489    720    781       C  
ATOM    653  C   GLY A 168      18.337  -6.562 -15.837  1.00 58.63           C  
ANISOU  653  C   GLY A 168     4568   6887  10822  -1102    939    986       C  
ATOM    654  O   GLY A 168      19.330  -7.267 -16.001  1.00 52.45           O  
ANISOU  654  O   GLY A 168     3548   6391   9992   -912    962   1165       O  
ATOM    655  N   HIS A 169      17.128  -6.925 -16.255  1.00 56.90           N  
ANISOU  655  N   HIS A 169     4744   6441  10432   -962   1069    937       N  
ATOM    656  CA  HIS A 169      16.885  -8.191 -16.929  1.00 55.16           C  
ANISOU  656  CA  HIS A 169     4726   6250   9981   -581   1214   1095       C  
ATOM    657  C   HIS A 169      16.715  -7.982 -18.432  1.00 51.67           C  
ANISOU  657  C   HIS A 169     4317   5675   9641   -464   1509   1276       C  
ATOM    658  O   HIS A 169      16.528  -6.864 -18.915  1.00 53.90           O  
ANISOU  658  O   HIS A 169     4545   5786  10150   -714   1603   1287       O  
ATOM    659  CB  HIS A 169      15.653  -8.886 -16.340  1.00 49.62           C  
ANISOU  659  CB  HIS A 169     4438   5418   8999   -499   1120    958       C  
ATOM    660  CG  HIS A 169      14.505  -7.961 -16.072  1.00 51.24           C  
ANISOU  660  CG  HIS A 169     4850   5391   9227   -741   1120    727       C  
ATOM    661  ND1 HIS A 169      14.437  -7.163 -14.948  1.00 55.48           N  
ANISOU  661  ND1 HIS A 169     5286   6002   9792  -1004    907    465       N  
ATOM    662  CD2 HIS A 169      13.376  -7.711 -16.778  1.00 50.19           C  
ANISOU  662  CD2 HIS A 169     5014   4974   9083   -724   1282    682       C  
ATOM    663  CE1 HIS A 169      13.319  -6.460 -14.976  1.00 56.26           C  
ANISOU  663  CE1 HIS A 169     5601   5886   9889  -1118    928    250       C  
ATOM    664  NE2 HIS A 169      12.658  -6.773 -16.077  1.00 49.39           N  
ANISOU  664  NE2 HIS A 169     4977   4789   9001   -967   1162    388       N  
ATOM    665  N   THR A 170      16.809  -9.081 -19.173  1.00 52.59           N  
ANISOU  665  N   THR A 170     4517   5879   9587    -66   1616   1419       N  
ATOM    666  CA  THR A 170      16.643  -9.090 -20.619  1.00 50.25           C  
ANISOU  666  CA  THR A 170     4255   5529   9310    139   1891   1579       C  
ATOM    667  C   THR A 170      15.305  -9.719 -20.985  1.00 39.60           C  
ANISOU  667  C   THR A 170     3398   3857   7790    344   1940   1504       C  
ATOM    668  O   THR A 170      14.621 -10.306 -20.145  1.00 37.93           O  
ANISOU  668  O   THR A 170     3462   3525   7425    350   1753   1380       O  
ATOM    669  CB  THR A 170      17.781  -9.862 -21.295  1.00 51.08           C  
ANISOU  669  CB  THR A 170     4052   6025   9332    515   1956   1756       C  
ATOM    670  OG1 THR A 170      17.754 -11.226 -20.853  1.00 50.71           O  
ANISOU  670  OG1 THR A 170     4193   6008   9066    876   1747   1681       O  
ATOM    671  CG2 THR A 170      19.129  -9.245 -20.948  1.00 56.21           C  
ANISOU  671  CG2 THR A 170     4172   7040  10143    295   1911   1860       C  
ATOM    672  N   ASP A 171      14.953  -9.618 -22.270  1.00 40.79           N  
ANISOU  672  N   ASP A 171     3902   5710   5889    917   1772   1004       N  
ATOM    673  CA  ASP A 171      13.749 -10.283 -22.762  1.00 33.59           C  
ANISOU  673  CA  ASP A 171     3491   4724   4548   1005   1725    841       C  
ATOM    674  C   ASP A 171      13.760 -11.775 -22.432  1.00 38.74           C  
ANISOU  674  C   ASP A 171     4368   5374   4975   1276   1714    582       C  
ATOM    675  O   ASP A 171      12.747 -12.329 -21.997  1.00 30.19           O  
ANISOU  675  O   ASP A 171     3591   4129   3749   1259   1488    378       O  
ATOM    676  CB  ASP A 171      13.609 -10.083 -24.276  1.00 36.03           C  
ANISOU  676  CB  ASP A 171     3988   5163   4539   1053   2005   1040       C  
ATOM    677  CG  ASP A 171      13.256  -8.652 -24.660  1.00 38.15           C  
ANISOU  677  CG  ASP A 171     4163   5364   4969    777   1964   1302       C  
ATOM    678  OD1 ASP A 171      12.828  -7.871 -23.780  1.00 39.06           O  
ANISOU  678  OD1 ASP A 171     4162   5282   5395    557   1672   1264       O  
ATOM    679  OD2 ASP A 171      13.395  -8.316 -25.856  1.00 39.40           O  
ANISOU  679  OD2 ASP A 171     4397   5657   4915    807   2227   1548       O  
ATOM    680  N   GLU A 172      14.896 -12.450 -22.641  1.00 41.19           N  
ANISOU  680  N   GLU A 172     4524   5856   5272   1537   1963    606       N  
ATOM    681  CA  GLU A 172      14.919 -13.887 -22.384  1.00 48.03           C  
ANISOU  681  CA  GLU A 172     5653   6671   5923   1822   1941    364       C  
ATOM    682  C   GLU A 172      14.847 -14.198 -20.895  1.00 40.93           C  
ANISOU  682  C   GLU A 172     4672   5625   5254   1787   1634    205       C  
ATOM    683  O   GLU A 172      14.302 -15.237 -20.509  1.00 39.96           O  
ANISOU  683  O   GLU A 172     4881   5347   4954   1875   1481      6       O  
ATOM    684  CB  GLU A 172      16.156 -14.529 -23.016  1.00 64.58           C  
ANISOU  684  CB  GLU A 172     7655   8934   7950   2028   2145    404       C  
ATOM    685  CG  GLU A 172      15.900 -15.078 -24.422  1.00 76.78           C  
ANISOU  685  CG  GLU A 172     9595  10517   9061   2170   2313    381       C  
ATOM    686  CD  GLU A 172      14.808 -16.148 -24.454  1.00 85.03           C  
ANISOU  686  CD  GLU A 172    11169  11328   9810   2218   2087    115       C  
ATOM    687  OE1 GLU A 172      14.625 -16.852 -23.436  1.00 91.35           O  
ANISOU  687  OE1 GLU A 172    12024  11964  10720   2220   1865    -46       O  
ATOM    688  OE2 GLU A 172      14.128 -16.285 -25.495  1.00 83.28           O  
ANISOU  688  OE2 GLU A 172    11303  11079   9260   2229   2104     83       O  
ATOM    689  N   ASP A 173      15.363 -13.312 -20.041  1.00 40.68           N  
ANISOU  689  N   ASP A 173     4236   5615   5604   1618   1494    293       N  
ATOM    690  CA  ASP A 173      15.148 -13.477 -18.608  1.00 37.01           C  
ANISOU  690  CA  ASP A 173     3761   5012   5291   1575   1166    137       C  
ATOM    691  C   ASP A 173      13.663 -13.445 -18.261  1.00 33.18           C  
ANISOU  691  C   ASP A 173     3633   4331   4643   1410    955     14       C  
ATOM    692  O   ASP A 173      13.203 -14.219 -17.414  1.00 32.05           O  
ANISOU  692  O   ASP A 173     3694   4073   4413   1479    792   -135       O  
ATOM    693  CB  ASP A 173      15.898 -12.398 -17.830  1.00 42.91           C  
ANISOU  693  CB  ASP A 173     4053   5796   6454   1403   1003    230       C  
ATOM    694  CG  ASP A 173      17.396 -12.469 -18.041  1.00 58.26           C  
ANISOU  694  CG  ASP A 173     5550   7954   8631   1548   1181    375       C  
ATOM    695  OD1 ASP A 173      17.951 -13.588 -17.994  1.00 61.09           O  
ANISOU  695  OD1 ASP A 173     5995   8373   8842   1794   1228    274       O  
ATOM    696  OD2 ASP A 173      18.015 -11.408 -18.271  1.00 62.41           O  
ANISOU  696  OD2 ASP A 173     5685   8558   9471   1348   1221    576       O  
ATOM    697  N   VAL A 174      12.898 -12.550 -18.897  1.00 26.48           N  
ANISOU  697  N   VAL A 174     2846   3451   3765   1198    963    102       N  
ATOM    698  CA  VAL A 174      11.459 -12.494 -18.635  1.00 23.80           C  
ANISOU  698  CA  VAL A 174     2786   2959   3298   1058    779      9       C  
ATOM    699  C   VAL A 174      10.781 -13.774 -19.118  1.00 26.20           C  
ANISOU  699  C   VAL A 174     3476   3201   3278   1175    815   -104       C  
ATOM    700  O   VAL A 174       9.980 -14.381 -18.396  1.00 22.52           O  
ANISOU  700  O   VAL A 174     3196   2610   2752   1150    654   -217       O  
ATOM    701  CB  VAL A 174      10.831 -11.250 -19.288  1.00 23.52           C  
ANISOU  701  CB  VAL A 174     2719   2904   3314    845    769    145       C  
ATOM    702  CG1 VAL A 174       9.309 -11.271 -19.142  1.00 21.32           C  
ANISOU  702  CG1 VAL A 174     2692   2507   2903    741    598     64       C  
ATOM    703  CG2 VAL A 174      11.407  -9.965 -18.705  1.00 24.13           C  
ANISOU  703  CG2 VAL A 174     2461   2957   3751    697    670    236       C  
ATOM    704  N   LYS A 175      11.075 -14.199 -20.357  1.00 25.51           N  
ANISOU  704  N   LYS A 175     3530   3190   2971   1301   1024    -69       N  
ATOM    705  CA  LYS A 175      10.398 -15.380 -20.894  1.00 28.63           C  
ANISOU  705  CA  LYS A 175     4345   3476   3056   1396   1002   -208       C  
ATOM    706  C   LYS A 175      10.728 -16.620 -20.072  1.00 29.17           C  
ANISOU  706  C   LYS A 175     4530   3431   3121   1579    946   -351       C  
ATOM    707  O   LYS A 175       9.848 -17.453 -19.812  1.00 32.01           O  
ANISOU  707  O   LYS A 175     5163   3613   3384   1499    770   -448       O  
ATOM    708  CB  LYS A 175      10.758 -15.583 -22.377  1.00 34.64           C  
ANISOU  708  CB  LYS A 175     5283   4348   3531   1554   1237   -173       C  
ATOM    709  CG  LYS A 175      10.044 -14.583 -23.301  1.00 31.11           C  
ANISOU  709  CG  LYS A 175     4880   3959   2983   1367   1230    -36       C  
ATOM    710  CD  LYS A 175      10.428 -14.724 -24.778  1.00 40.37           C  
ANISOU  710  CD  LYS A 175     6258   5274   3806   1551   1480     23       C  
ATOM    711  CE  LYS A 175      10.304 -13.374 -25.479  1.00 43.47           C  
ANISOU  711  CE  LYS A 175     6504   5791   4220   1389   1562    281       C  
ATOM    712  NZ  LYS A 175      10.711 -13.388 -26.925  1.00 53.42           N  
ANISOU  712  NZ  LYS A 175     7964   7234   5099   1580   1847    394       N  
ATOM    713  N   ASN A 176      11.987 -16.746 -19.635  1.00 31.59           N  
ANISOU  713  N   ASN A 176     4572   3845   3585   1729   1027   -316       N  
ATOM    714  CA  ASN A 176      12.395 -17.857 -18.783  1.00 40.14           C  
ANISOU  714  CA  ASN A 176     5703   4841   4709   1809    898   -393       C  
ATOM    715  C   ASN A 176      11.641 -17.841 -17.459  1.00 35.82           C  
ANISOU  715  C   ASN A 176     5178   4169   4262   1667    669   -423       C  
ATOM    716  O   ASN A 176      11.135 -18.873 -17.004  1.00 28.57           O  
ANISOU  716  O   ASN A 176     4494   3103   3260   1639    548   -469       O  
ATOM    717  CB  ASN A 176      13.906 -17.789 -18.547  1.00 62.96           C  
ANISOU  717  CB  ASN A 176     8249   7895   7779   1984   1006   -335       C  
ATOM    718  CG  ASN A 176      14.440 -18.992 -17.790  1.00 83.43           C  
ANISOU  718  CG  ASN A 176    10912  10402  10387   2119    898   -401       C  
ATOM    719  OD1 ASN A 176      13.893 -20.090 -17.883  1.00 94.22           O  
ANISOU  719  OD1 ASN A 176    12619  11601  11579   2135    827   -474       O  
ATOM    720  ND2 ASN A 176      15.518 -18.789 -17.036  1.00 84.75           N  
ANISOU  720  ND2 ASN A 176    10747  10673  10779   2216    869   -361       N  
ATOM    721  N   ALA A 177      11.541 -16.665 -16.835  1.00 27.78           N  
ANISOU  721  N   ALA A 177     3924   3209   3421   1583    614   -381       N  
ATOM    722  CA  ALA A 177      10.848 -16.558 -15.558  1.00 22.09           C  
ANISOU  722  CA  ALA A 177     3230   2405   2758   1474    413   -409       C  
ATOM    723  C   ALA A 177       9.374 -16.910 -15.692  1.00 29.77           C  
ANISOU  723  C   ALA A 177     4488   3239   3582   1318    351   -428       C  
ATOM    724  O   ALA A 177       8.809 -17.591 -14.828  1.00 26.35           O  
ANISOU  724  O   ALA A 177     4185   2716   3109   1271    247   -429       O  
ATOM    725  CB  ALA A 177      11.009 -15.146 -14.991  1.00 21.30           C  
ANISOU  725  CB  ALA A 177     2834   2388   2870   1375    325   -376       C  
ATOM    726  N   VAL A 178       8.727 -16.437 -16.754  1.00 22.08           N  
ANISOU  726  N   VAL A 178     3577   2272   2540   1198    403   -407       N  
ATOM    727  CA  VAL A 178       7.325 -16.784 -16.965  1.00 21.26           C  
ANISOU  727  CA  VAL A 178     3694   2051   2331   1021    306   -414       C  
ATOM    728  C   VAL A 178       7.184 -18.286 -17.165  1.00 22.26           C  
ANISOU  728  C   VAL A 178     4145   2003   2311   1091    281   -484       C  
ATOM    729  O   VAL A 178       6.257 -18.913 -16.642  1.00 25.54           O  
ANISOU  729  O   VAL A 178     4711   2273   2719    971    170   -474       O  
ATOM    730  CB  VAL A 178       6.740 -15.996 -18.153  1.00 24.00           C  
ANISOU  730  CB  VAL A 178     4035   2459   2624    880    320   -365       C  
ATOM    731  CG1 VAL A 178       5.408 -16.595 -18.570  1.00 23.41           C  
ANISOU  731  CG1 VAL A 178     4196   2263   2437    718    185   -386       C  
ATOM    732  CG2 VAL A 178       6.554 -14.544 -17.789  1.00 20.89           C  
ANISOU  732  CG2 VAL A 178     3364   2162   2410    767    288   -281       C  
ATOM    733  N   GLY A 179       8.104 -18.887 -17.919  1.00 23.26           N  
ANISOU  733  N   GLY A 179     4329   2161   2347   1242    374   -517       N  
ATOM    734  CA  GLY A 179       8.050 -20.323 -18.123  1.00 25.08           C  
ANISOU  734  CA  GLY A 179     4824   2235   2471   1281    312   -565       C  
ATOM    735  C   GLY A 179       8.177 -21.103 -16.834  1.00 30.68           C  
ANISOU  735  C   GLY A 179     5536   2855   3266   1307    236   -529       C  
ATOM    736  O   GLY A 179       7.561 -22.156 -16.686  1.00 27.14           O  
ANISOU  736  O   GLY A 179     5335   2207   2771   1242    137   -536       O  
ATOM    737  N   VAL A 180       8.965 -20.592 -15.885  1.00 30.58           N  
ANISOU  737  N   VAL A 180     5268   2976   3374   1399    265   -485       N  
ATOM    738  CA  VAL A 180       9.104 -21.254 -14.592  1.00 31.92           C  
ANISOU  738  CA  VAL A 180     5466   3082   3579   1450    184   -439       C  
ATOM    739  C   VAL A 180       7.809 -21.144 -13.798  1.00 28.75           C  
ANISOU  739  C   VAL A 180     5160   2585   3181   1279    105   -378       C  
ATOM    740  O   VAL A 180       7.354 -22.121 -13.187  1.00 26.91           O  
ANISOU  740  O   VAL A 180     5136   2180   2908   1260     50   -324       O  
ATOM    741  CB  VAL A 180      10.303 -20.664 -13.827  1.00 24.66           C  
ANISOU  741  CB  VAL A 180     4258   2336   2774   1595    192   -424       C  
ATOM    742  CG1 VAL A 180      10.208 -20.996 -12.340  1.00 30.62           C  
ANISOU  742  CG1 VAL A 180     5053   3059   3524   1632     79   -368       C  
ATOM    743  CG2 VAL A 180      11.604 -21.167 -14.415  1.00 33.37           C  
ANISOU  743  CG2 VAL A 180     5296   3492   3890   1803    279   -455       C  
ATOM    744  N   LEU A 181       7.179 -19.965 -13.816  1.00 26.11           N  
ANISOU  744  N   LEU A 181     4685   2339   2897   1163    112   -374       N  
ATOM    745  CA  LEU A 181       5.915 -19.789 -13.109  1.00 26.73           C  
ANISOU  745  CA  LEU A 181     4840   2332   2983   1031     71   -309       C  
ATOM    746  C   LEU A 181       4.816 -20.642 -13.725  1.00 29.85           C  
ANISOU  746  C   LEU A 181     5466   2527   3349    823     18   -274       C  
ATOM    747  O   LEU A 181       4.038 -21.274 -13.001  1.00 27.84           O  
ANISOU  747  O   LEU A 181     5303   2163   3112    703    -13   -153       O  
ATOM    748  CB  LEU A 181       5.506 -18.317 -13.106  1.00 21.77           C  
ANISOU  748  CB  LEU A 181     3941   1897   2433    925     78   -302       C  
ATOM    749  CG  LEU A 181       4.198 -17.958 -12.386  1.00 24.61           C  
ANISOU  749  CG  LEU A 181     4230   2303   2816    762     65   -201       C  
ATOM    750  CD1 LEU A 181       4.193 -18.444 -10.914  1.00 23.35           C  
ANISOU  750  CD1 LEU A 181     4137   2145   2591    866     80   -123       C  
ATOM    751  CD2 LEU A 181       3.922 -16.445 -12.455  1.00 21.70           C  
ANISOU  751  CD2 LEU A 181     3615   2098   2532    722     62   -224       C  
ATOM    752  N   ILE A 182       4.727 -20.668 -15.057  1.00 27.32           N  
ANISOU  752  N   ILE A 182     5238   2159   2981    766     -5   -363       N  
ATOM    753  CA  ILE A 182       3.680 -21.455 -15.703  1.00 26.36           C  
ANISOU  753  CA  ILE A 182     5341   1833   2843    543   -131   -359       C  
ATOM    754  C   ILE A 182       3.862 -22.933 -15.389  1.00 33.90           C  
ANISOU  754  C   ILE A 182     6547   2557   3777    578   -183   -345       C  
ATOM    755  O   ILE A 182       2.901 -23.634 -15.053  1.00 32.14           O  
ANISOU  755  O   ILE A 182     6456   2126   3630    360   -284   -245       O  
ATOM    756  CB  ILE A 182       3.676 -21.194 -17.222  1.00 28.30           C  
ANISOU  756  CB  ILE A 182     5682   2094   2976    526   -173   -482       C  
ATOM    757  CG1 ILE A 182       3.067 -19.835 -17.534  1.00 26.17           C  
ANISOU  757  CG1 ILE A 182     5125   2056   2760    386   -174   -418       C  
ATOM    758  CG2 ILE A 182       2.909 -22.285 -17.958  1.00 31.74           C  
ANISOU  758  CG2 ILE A 182     6393   2302   3363    350   -359   -525       C  
ATOM    759  CD1 ILE A 182       3.046 -19.533 -19.033  1.00 29.80           C  
ANISOU  759  CD1 ILE A 182     5703   2552   3068    382   -219   -503       C  
ATOM    760  N   GLY A 183       5.102 -23.423 -15.475  1.00 26.97           N  
ANISOU  760  N   GLY A 183     5683   1737   2828    827   -117   -408       N  
ATOM    761  CA  GLY A 183       5.352 -24.826 -15.202  1.00 32.84           C  
ANISOU  761  CA  GLY A 183     6651   2274   3553    887   -172   -396       C  
ATOM    762  C   GLY A 183       5.050 -25.189 -13.763  1.00 38.78           C  
ANISOU  762  C   GLY A 183     7422   2933   4379    852   -175   -234       C  
ATOM    763  O   GLY A 183       4.485 -26.251 -13.489  1.00 33.02           O  
ANISOU  763  O   GLY A 183     6900   1953   3693    724   -258   -152       O  
ATOM    764  N   GLY A 184       5.412 -24.307 -12.827  1.00 35.57           N  
ANISOU  764  N   GLY A 184     6805   2726   3984    964    -90   -172       N  
ATOM    765  CA  GLY A 184       5.072 -24.537 -11.431  1.00 40.12           C  
ANISOU  765  CA  GLY A 184     7425   3248   4572    963    -75      6       C  
ATOM    766  C   GLY A 184       3.575 -24.633 -11.204  1.00 34.36           C  
ANISOU  766  C   GLY A 184     6772   2360   3922    655    -89    186       C  
ATOM    767  O   GLY A 184       3.096 -25.548 -10.533  1.00 33.66           O  
ANISOU  767  O   GLY A 184     6823   2103   3865    547    -99    370       O  
ATOM    768  N   LEU A 185       2.814 -23.690 -11.769  1.00 27.22           N  
ANISOU  768  N   LEU A 185     5660   1609   3075    467    -85    159       N  
ATOM    769  CA  LEU A 185       1.362 -23.724 -11.616  1.00 33.40           C  
ANISOU  769  CA  LEU A 185     6332   2386   3972    130    -96    343       C  
ATOM    770  C   LEU A 185       0.750 -24.929 -12.314  1.00 37.21           C  
ANISOU  770  C   LEU A 185     7080   2505   4555   -123   -258    373       C  
ATOM    771  O   LEU A 185      -0.161 -25.564 -11.772  1.00 33.40           O  
ANISOU  771  O   LEU A 185     6606   1891   4195   -373   -266    608       O  
ATOM    772  CB  LEU A 185       0.743 -22.438 -12.152  1.00 26.19           C  
ANISOU  772  CB  LEU A 185     5102   1740   3108     21    -85    292       C  
ATOM    773  CG  LEU A 185       1.214 -21.228 -11.351  1.00 23.99           C  
ANISOU  773  CG  LEU A 185     4587   1766   2763    239     44    267       C  
ATOM    774  CD1 LEU A 185       0.868 -19.946 -12.077  1.00 25.75           C  
ANISOU  774  CD1 LEU A 185     4561   2184   3038    187     29    178       C  
ATOM    775  CD2 LEU A 185       0.590 -21.252  -9.971  1.00 25.20           C  
ANISOU  775  CD2 LEU A 185     4653   2028   2893    233    172    480       C  
ATOM    776  N   GLU A 186       1.224 -25.248 -13.523  1.00 31.45           N  
ANISOU  776  N   GLU A 186     6523   1654   3772    -65   -384    139       N  
ATOM    777  CA  GLU A 186       0.677 -26.379 -14.260  1.00 36.52           C  
ANISOU  777  CA  GLU A 186     7338   2055   4484   -273   -570    100       C  
ATOM    778  C   GLU A 186       0.994 -27.714 -13.605  1.00 37.62           C  
ANISOU  778  C   GLU A 186     7674   1966   4654   -218   -576    187       C  
ATOM    779  O   GLU A 186       0.272 -28.683 -13.843  1.00 40.99           O  
ANISOU  779  O   GLU A 186     8213   2151   5209   -459   -722    243       O  
ATOM    780  CB  GLU A 186       1.195 -26.381 -15.693  1.00 38.98           C  
ANISOU  780  CB  GLU A 186     7775   2386   4650   -148   -667   -171       C  
ATOM    781  CG  GLU A 186       0.534 -25.332 -16.550  1.00 39.98           C  
ANISOU  781  CG  GLU A 186     7759   2661   4771   -300   -741   -229       C  
ATOM    782  CD  GLU A 186       1.051 -25.310 -17.977  1.00 45.45           C  
ANISOU  782  CD  GLU A 186     8602   3399   5266   -149   -809   -455       C  
ATOM    783  OE1 GLU A 186       2.115 -25.916 -18.258  1.00 49.44           O  
ANISOU  783  OE1 GLU A 186     9271   3879   5635    125   -736   -565       O  
ATOM    784  OE2 GLU A 186       0.378 -24.679 -18.816  1.00 43.33           O  
ANISOU  784  OE2 GLU A 186     8282   3208   4976   -299   -931   -497       O  
ATOM    785  N   ALA A 187       2.061 -27.791 -12.804  1.00 38.48           N  
ANISOU  785  N   ALA A 187     7818   2144   4660     93   -445    199       N  
ATOM    786  CA  ALA A 187       2.358 -29.020 -12.082  1.00 43.13           C  
ANISOU  786  CA  ALA A 187     8593   2517   5277    157   -456    312       C  
ATOM    787  C   ALA A 187       1.298 -29.325 -11.030  1.00 44.98           C  
ANISOU  787  C   ALA A 187     8767   2660   5664   -115   -410    649       C  
ATOM    788  O   ALA A 187       1.131 -30.488 -10.651  1.00 46.28           O  
ANISOU  788  O   ALA A 187     9091   2570   5924   -195   -458    785       O  
ATOM    789  CB  ALA A 187       3.740 -28.932 -11.433  1.00 42.10           C  
ANISOU  789  CB  ALA A 187     8463   2532   4999    554   -351    262       C  
ATOM    790  N   ASN A 188       0.571 -28.313 -10.563  1.00 39.67           N  
ANISOU  790  N   ASN A 188     7858   2199   5016   -253   -298    810       N  
ATOM    791  CA  ASN A 188      -0.533 -28.494  -9.631  1.00 41.75           C  
ANISOU  791  CA  ASN A 188     7991   2462   5411   -521   -194   1176       C  
ATOM    792  C   ASN A 188      -1.883 -28.472 -10.333  1.00 47.79           C  
ANISOU  792  C   ASN A 188     8571   3179   6409   -944   -293   1249       C  
ATOM    793  O   ASN A 188      -2.895 -28.105  -9.729  1.00 48.37           O  
ANISOU  793  O   ASN A 188     8383   3404   6592  -1168   -157   1538       O  
ATOM    794  CB  ASN A 188      -0.464 -27.437  -8.533  1.00 43.21           C  
ANISOU  794  CB  ASN A 188     8021   2968   5428   -355     33   1336       C  
ATOM    795  CG  ASN A 188       0.753 -27.611  -7.656  1.00 42.26           C  
ANISOU  795  CG  ASN A 188     8051   2908   5098     40     89   1299       C  
ATOM    796  OD1 ASN A 188       1.155 -28.735  -7.371  1.00 47.43           O  
ANISOU  796  OD1 ASN A 188     8892   3355   5773     96     28   1352       O  
ATOM    797  ND2 ASN A 188       1.362 -26.504  -7.245  1.00 45.06           N  
ANISOU  797  ND2 ASN A 188     8314   3544   5264    319    179   1199       N  
ATOM    798  N   ASP A 189      -1.901 -28.852 -11.612  1.00 48.55           N  
ANISOU  798  N   ASP A 189     8779   3107   6560  -1033   -525    988       N  
ATOM    799  CA  ASP A 189      -3.122 -29.049 -12.389  1.00 48.43           C  
ANISOU  799  CA  ASP A 189     8623   3018   6762  -1419   -703   1010       C  
ATOM    800  C   ASP A 189      -3.916 -27.759 -12.558  1.00 44.35           C  
ANISOU  800  C   ASP A 189     7747   2808   6297  -1573   -665   1074       C  
ATOM    801  O   ASP A 189      -5.132 -27.788 -12.751  1.00 51.91           O  
ANISOU  801  O   ASP A 189     8441   3807   7476  -1906   -743   1219       O  
ATOM    802  CB  ASP A 189      -3.982 -30.151 -11.772  1.00 53.94           C  
ANISOU  802  CB  ASP A 189     9288   3504   7702  -1707   -693   1301       C  
ATOM    803  CG  ASP A 189      -3.188 -31.414 -11.531  1.00 63.51           C  
ANISOU  803  CG  ASP A 189    10861   4392   8878  -1545   -733   1266       C  
ATOM    804  OD1 ASP A 189      -2.328 -31.730 -12.384  1.00 59.83           O  
ANISOU  804  OD1 ASP A 189    10669   3800   8266  -1331   -891    944       O  
ATOM    805  OD2 ASP A 189      -3.398 -32.072 -10.488  1.00 69.47           O  
ANISOU  805  OD2 ASP A 189    11622   5041   9733  -1604   -587   1573       O  
ATOM    806  N   ASN A 190      -3.235 -26.619 -12.508  1.00 41.24           N  
ANISOU  806  N   ASN A 190     7322   2635   5714  -1322   -555    966       N  
ATOM    807  CA  ASN A 190      -3.861 -25.350 -12.840  1.00 37.89           C  
ANISOU  807  CA  ASN A 190     6562   2511   5326  -1409   -543    969       C  
ATOM    808  C   ASN A 190      -3.749 -25.098 -14.340  1.00 40.25           C  
ANISOU  808  C   ASN A 190     6976   2744   5576  -1432   -802    672       C  
ATOM    809  O   ASN A 190      -2.787 -25.510 -14.989  1.00 43.10           O  
ANISOU  809  O   ASN A 190     7645   2970   5760  -1207   -871    413       O  
ATOM    810  CB  ASN A 190      -3.216 -24.199 -12.064  1.00 34.33           C  
ANISOU  810  CB  ASN A 190     5918   2440   4687  -1048   -272    936       C  
ATOM    811  CG  ASN A 190      -3.311 -24.384 -10.566  1.00 42.08           C  
ANISOU  811  CG  ASN A 190     6831   3525   5634   -970    -19   1210       C  
ATOM    812  OD1 ASN A 190      -4.399 -24.329  -9.989  1.00 38.48           O  
ANISOU  812  OD1 ASN A 190     6099   3206   5314  -1170    104   1490       O  
ATOM    813  ND2 ASN A 190      -2.166 -24.612  -9.922  1.00 40.29           N  
ANISOU  813  ND2 ASN A 190     6845   3252   5210   -660     64   1147       N  
ATOM    814  N   THR A 191      -4.760 -24.444 -14.894  1.00 40.90           N  
ANISOU  814  N   THR A 191     6746   3004   5788  -1646   -917    711       N  
ATOM    815  CA  THR A 191      -4.738 -24.030 -16.289  1.00 42.21           C  
ANISOU  815  CA  THR A 191     6999   3174   5863  -1646  -1158    460       C  
ATOM    816  C   THR A 191      -4.374 -22.556 -16.320  1.00 41.39           C  
ANISOU  816  C   THR A 191     6642   3457   5627  -1374   -975    393       C  
ATOM    817  O   THR A 191      -5.047 -21.737 -15.688  1.00 42.15           O  
ANISOU  817  O   THR A 191     6342   3830   5841  -1395   -834    568       O  
ATOM    818  CB  THR A 191      -6.080 -24.268 -16.974  1.00 48.31           C  
ANISOU  818  CB  THR A 191     7558   3959   6839  -1979  -1426    526       C  
ATOM    819  OG1 THR A 191      -6.351 -25.676 -17.020  1.00 54.24           O  
ANISOU  819  OG1 THR A 191     8491   4437   7681  -2129  -1556    538       O  
ATOM    820  CG2 THR A 191      -6.040 -23.713 -18.389  1.00 50.01           C  
ANISOU  820  CG2 THR A 191     7873   4238   6892  -1919  -1663    288       C  
ATOM    821  N   VAL A 192      -3.301 -22.228 -17.028  1.00 34.99           N  
ANISOU  821  N   VAL A 192     6060   2652   4582  -1108   -964    153       N  
ATOM    822  CA  VAL A 192      -2.727 -20.891 -17.000  1.00 30.44           C  
ANISOU  822  CA  VAL A 192     5289   2379   3899   -849   -784    100       C  
ATOM    823  C   VAL A 192      -2.766 -20.321 -18.409  1.00 32.39           C  
ANISOU  823  C   VAL A 192     5601   2680   4025   -843   -952    -42       C  
ATOM    824  O   VAL A 192      -2.395 -21.001 -19.372  1.00 33.94           O  
ANISOU  824  O   VAL A 192     6150   2684   4063   -829  -1105   -210       O  
ATOM    825  CB  VAL A 192      -1.287 -20.900 -16.455  1.00 28.22           C  
ANISOU  825  CB  VAL A 192     5155   2100   3468   -525   -573      4       C  
ATOM    826  CG1 VAL A 192      -0.751 -19.461 -16.322  1.00 23.37           C  
ANISOU  826  CG1 VAL A 192     4300   1770   2810   -317   -419    -25       C  
ATOM    827  CG2 VAL A 192      -1.239 -21.634 -15.126  1.00 31.27           C  
ANISOU  827  CG2 VAL A 192     5562   2398   3921   -519   -454    150       C  
ATOM    828  N   ARG A 193      -3.233 -19.086 -18.525  1.00 32.89           N  
ANISOU  828  N   ARG A 193     5358   2997   4143   -828   -926     29       N  
ATOM    829  CA  ARG A 193      -3.138 -18.334 -19.763  1.00 34.18           C  
ANISOU  829  CA  ARG A 193     5575   3250   4163   -766  -1039    -61       C  
ATOM    830  C   ARG A 193      -2.508 -16.987 -19.437  1.00 32.05           C  
ANISOU  830  C   ARG A 193     5101   3198   3879   -540   -817    -33       C  
ATOM    831  O   ARG A 193      -2.461 -16.577 -18.272  1.00 22.56           O  
ANISOU  831  O   ARG A 193     3683   2088   2800   -468   -643     45       O  
ATOM    832  CB  ARG A 193      -4.506 -18.157 -20.416  1.00 35.61           C  
ANISOU  832  CB  ARG A 193     5596   3475   4460  -1011  -1325     22       C  
ATOM    833  CG  ARG A 193      -5.491 -17.440 -19.530  1.00 39.50           C  
ANISOU  833  CG  ARG A 193     5626   4164   5216  -1083  -1249    228       C  
ATOM    834  CD  ARG A 193      -6.927 -17.577 -20.035  1.00 52.53           C  
ANISOU  834  CD  ARG A 193     7062   5841   7057  -1363  -1554    343       C  
ATOM    835  NE  ARG A 193      -7.794 -16.574 -19.417  1.00 59.66           N  
ANISOU  835  NE  ARG A 193     7492   7000   8177  -1328  -1452    531       N  
ATOM    836  CZ  ARG A 193      -8.280 -16.666 -18.181  1.00 66.89           C  
ANISOU  836  CZ  ARG A 193     8116   8011   9289  -1354  -1237    699       C  
ATOM    837  NH1 ARG A 193      -7.991 -17.718 -17.422  1.00 66.88           N  
ANISOU  837  NH1 ARG A 193     8248   7861   9302  -1446  -1117    732       N  
ATOM    838  NH2 ARG A 193      -9.053 -15.701 -17.698  1.00 69.45           N  
ANISOU  838  NH2 ARG A 193     8032   8580   9775  -1257  -1128    845       N  
ATOM    839  N   VAL A 194      -2.020 -16.303 -20.476  1.00 28.27           N  
ANISOU  839  N   VAL A 194     4717   2785   3239   -428   -833    -92       N  
ATOM    840  CA  VAL A 194      -1.331 -15.031 -20.300  1.00 23.95           C  
ANISOU  840  CA  VAL A 194     4007   2387   2705   -249   -651    -55       C  
ATOM    841  C   VAL A 194      -2.150 -13.924 -20.943  1.00 22.25           C  
ANISOU  841  C   VAL A 194     3626   2289   2538   -294   -777     49       C  
ATOM    842  O   VAL A 194      -2.899 -14.137 -21.908  1.00 24.25           O  
ANISOU  842  O   VAL A 194     3970   2531   2712   -411  -1008     59       O  
ATOM    843  CB  VAL A 194       0.112 -15.041 -20.861  1.00 21.42           C  
ANISOU  843  CB  VAL A 194     3888   2057   2194    -58   -495   -145       C  
ATOM    844  CG1 VAL A 194       0.840 -16.301 -20.405  1.00 32.08           C  
ANISOU  844  CG1 VAL A 194     5439   3269   3482     16   -418   -256       C  
ATOM    845  CG2 VAL A 194       0.127 -14.908 -22.380  1.00 30.45           C  
ANISOU  845  CG2 VAL A 194     5247   3223   3100    -42   -588   -164       C  
ATOM    846  N   SER A 195      -1.986 -12.722 -20.398  1.00 23.39           N  
ANISOU  846  N   SER A 195     3546   2528   2813   -185   -656    118       N  
ATOM    847  CA  SER A 195      -2.718 -11.557 -20.860  1.00 21.39           C  
ANISOU  847  CA  SER A 195     3128   2359   2641   -180   -760    232       C  
ATOM    848  C   SER A 195      -2.298 -11.164 -22.277  1.00 28.13           C  
ANISOU  848  C   SER A 195     4183   3219   3287   -146   -825    262       C  
ATOM    849  O   SER A 195      -1.269 -11.593 -22.799  1.00 22.59           O  
ANISOU  849  O   SER A 195     3710   2486   2387    -85   -716    196       O  
ATOM    850  CB  SER A 195      -2.475 -10.379 -19.919  1.00 20.00           C  
ANISOU  850  CB  SER A 195     2739   2218   2643    -41   -618    265       C  
ATOM    851  OG  SER A 195      -1.140  -9.896 -20.078  1.00 22.01           O  
ANISOU  851  OG  SER A 195     3090   2430   2843     57   -481    235       O  
ATOM    852  N   GLU A 196      -3.119 -10.300 -22.884  1.00 24.82           N  
ANISOU  852  N   GLU A 196     2796   2953   3682    169   -126   -584       N  
ATOM    853  CA  GLU A 196      -2.810  -9.739 -24.199  1.00 35.43           C  
ANISOU  853  CA  GLU A 196     4112   4493   4855    279   -352   -360       C  
ATOM    854  C   GLU A 196      -1.434  -9.072 -24.228  1.00 22.89           C  
ANISOU  854  C   GLU A 196     2698   2807   3192    352   -288   -118       C  
ATOM    855  O   GLU A 196      -0.697  -9.191 -25.218  1.00 25.85           O  
ANISOU  855  O   GLU A 196     3195   3306   3320    358   -327      3       O  
ATOM    856  CB  GLU A 196      -3.908  -8.743 -24.579  1.00 43.70           C  
ANISOU  856  CB  GLU A 196     4895   5622   6088    425   -576   -275       C  
ATOM    857  CG  GLU A 196      -3.584  -7.770 -25.688  1.00 55.16           C  
ANISOU  857  CG  GLU A 196     6384   7182   7394    630   -767     89       C  
ATOM    858  CD  GLU A 196      -4.724  -6.795 -25.920  1.00 67.73           C  
ANISOU  858  CD  GLU A 196     7714   8814   9206    862   -985    212       C  
ATOM    859  OE1 GLU A 196      -5.576  -6.663 -25.014  1.00 66.73           O  
ANISOU  859  OE1 GLU A 196     7362   8554   9439    835   -934      0       O  
ATOM    860  OE2 GLU A 196      -4.777  -6.171 -27.003  1.00 77.40           O  
ANISOU  860  OE2 GLU A 196     8967  10202  10239   1092  -1194    527       O  
ATOM    861  N   THR A 197      -1.070  -8.370 -23.157  1.00 21.67           N  
ANISOU  861  N   THR A 197     2534   2448   3252    374   -158   -107       N  
ATOM    862  CA  THR A 197       0.200  -7.651 -23.135  1.00 21.05           C  
ANISOU  862  CA  THR A 197     2541   2292   3167    407    -61     17       C  
ATOM    863  C   THR A 197       1.375  -8.616 -23.146  1.00 19.72           C  
ANISOU  863  C   THR A 197     2533   2202   2758    363     18    -71       C  
ATOM    864  O   THR A 197       2.358  -8.400 -23.868  1.00 20.05           O  
ANISOU  864  O   THR A 197     2646   2283   2689    363     54     12       O  
ATOM    865  CB  THR A 197       0.280  -6.746 -21.906  1.00 22.35           C  
ANISOU  865  CB  THR A 197     2598   2275   3619    401     79    -67       C  
ATOM    866  OG1 THR A 197      -0.883  -5.915 -21.832  1.00 24.34           O  
ANISOU  866  OG1 THR A 197     2676   2410   4163    452     38    -15       O  
ATOM    867  CG2 THR A 197       1.502  -5.862 -22.002  1.00 20.91           C  
ANISOU  867  CG2 THR A 197     2431   2019   3494    398    217    -17       C  
ATOM    868  N   LEU A 198       1.305  -9.679 -22.339  1.00 18.73           N  
ANISOU  868  N   LEU A 198     2477   2072   2568    342     84   -235       N  
ATOM    869  CA  LEU A 198       2.346 -10.706 -22.389  1.00 18.19           C  
ANISOU  869  CA  LEU A 198     2559   2055   2298    368    156   -291       C  
ATOM    870  C   LEU A 198       2.372 -11.418 -23.728  1.00 18.96           C  
ANISOU  870  C   LEU A 198     2723   2256   2222    299    128   -276       C  
ATOM    871  O   LEU A 198       3.449 -11.787 -24.204  1.00 21.88           O  
ANISOU  871  O   LEU A 198     3167   2673   2473    309    184   -287       O  
ATOM    872  CB  LEU A 198       2.144 -11.715 -21.260  1.00 17.94           C  
ANISOU  872  CB  LEU A 198     2651   1942   2223    413    274   -398       C  
ATOM    873  CG  LEU A 198       2.541 -11.084 -19.928  1.00 22.09           C  
ANISOU  873  CG  LEU A 198     3137   2462   2794    500    297   -438       C  
ATOM    874  CD1 LEU A 198       1.911 -11.812 -18.778  1.00 23.43           C  
ANISOU  874  CD1 LEU A 198     3462   2536   2906    528    429   -492       C  
ATOM    875  CD2 LEU A 198       4.076 -11.123 -19.804  1.00 17.84           C  
ANISOU  875  CD2 LEU A 198     2593   2055   2131    637    271   -467       C  
ATOM    876  N   GLN A 199       1.205 -11.606 -24.358  1.00 20.07           N  
ANISOU  876  N   GLN A 199     2802   2472   2350    218     44   -304       N  
ATOM    877  CA  GLN A 199       1.166 -12.235 -25.679  1.00 32.06           C  
ANISOU  877  CA  GLN A 199     4352   4175   3655    124      4   -350       C  
ATOM    878  C   GLN A 199       1.921 -11.405 -26.706  1.00 28.84           C  
ANISOU  878  C   GLN A 199     3983   3877   3096    149    -69   -155       C  
ATOM    879  O   GLN A 199       2.549 -11.949 -27.621  1.00 31.99           O  
ANISOU  879  O   GLN A 199     4478   4393   3285     67    -12   -199       O  
ATOM    880  CB  GLN A 199      -0.278 -12.430 -26.150  1.00 27.76           C  
ANISOU  880  CB  GLN A 199     3650   3789   3111     46   -123   -479       C  
ATOM    881  CG  GLN A 199      -1.061 -13.486 -25.401  1.00 30.99           C  
ANISOU  881  CG  GLN A 199     4039   4075   3661    -67     57   -758       C  
ATOM    882  CD  GLN A 199      -2.543 -13.423 -25.721  1.00 37.48           C  
ANISOU  882  CD  GLN A 199     4600   5072   4571   -146    -76   -960       C  
ATOM    883  OE1 GLN A 199      -2.928 -13.263 -26.878  1.00 45.28           O  
ANISOU  883  OE1 GLN A 199     5444   6384   5377   -156   -299   -991       O  
ATOM    884  NE2 GLN A 199      -3.381 -13.518 -24.693  1.00 40.47           N  
ANISOU  884  NE2 GLN A 199     4899   5269   5209   -193     54  -1118       N  
ATOM    885  N   ARG A 200       1.852 -10.084 -26.594  1.00 24.05           N  
ANISOU  885  N   ARG A 200     3324   3202   2610    246   -136     53       N  
ATOM    886  CA  ARG A 200       2.615  -9.268 -27.527  1.00 25.78           C  
ANISOU  886  CA  ARG A 200     3647   3446   2703    262    -99    261       C  
ATOM    887  C   ARG A 200       4.097  -9.316 -27.191  1.00 23.68           C  
ANISOU  887  C   ARG A 200     3442   3064   2491    214    116    165       C  
ATOM    888  O   ARG A 200       4.945  -9.376 -28.090  1.00 25.97           O  
ANISOU  888  O   ARG A 200     3844   3411   2612    137    226    181       O  
ATOM    889  CB  ARG A 200       2.097  -7.830 -27.533  1.00 29.06           C  
ANISOU  889  CB  ARG A 200     4016   3744   3283    397   -153    528       C  
ATOM    890  CG  ARG A 200       2.987  -6.875 -28.325  1.00 39.02           C  
ANISOU  890  CG  ARG A 200     5447   4908   4471    409     15    767       C  
ATOM    891  CD  ARG A 200       2.215  -5.701 -28.893  1.00 48.49           C  
ANISOU  891  CD  ARG A 200     6690   6044   5691    600    -64   1137       C  
ATOM    892  NE  ARG A 200       1.128  -6.144 -29.758  1.00 56.93           N  
ANISOU  892  NE  ARG A 200     7731   7449   6449    711   -388   1229       N  
ATOM    893  CZ  ARG A 200       1.254  -6.393 -31.057  1.00 57.44           C  
ANISOU  893  CZ  ARG A 200     7975   7789   6059    715   -467   1367       C  
ATOM    894  NH1 ARG A 200       2.427  -6.246 -31.657  1.00 59.41           N  
ANISOU  894  NH1 ARG A 200     8479   7959   6136    596   -201   1452       N  
ATOM    895  NH2 ARG A 200       0.202  -6.791 -31.756  1.00 55.58           N  
ANISOU  895  NH2 ARG A 200     7641   7944   5532    820   -801   1371       N  
ATOM    896  N   PHE A 201       4.427  -9.334 -25.898  1.00 21.92           N  
ANISOU  896  N   PHE A 201     3127   2719   2482    260    176     25       N  
ATOM    897  CA  PHE A 201       5.827  -9.365 -25.497  1.00 21.28           C  
ANISOU  897  CA  PHE A 201     3018   2610   2456    258    325   -129       C  
ATOM    898  C   PHE A 201       6.506 -10.666 -25.918  1.00 23.97           C  
ANISOU  898  C   PHE A 201     3434   3042   2631    239    372   -270       C  
ATOM    899  O   PHE A 201       7.723 -10.689 -26.117  1.00 22.78           O  
ANISOU  899  O   PHE A 201     3251   2910   2495    223    496   -395       O  
ATOM    900  CB  PHE A 201       5.955  -9.182 -23.985  1.00 21.61           C  
ANISOU  900  CB  PHE A 201     2929   2605   2676    348    321   -271       C  
ATOM    901  CG  PHE A 201       7.371  -9.132 -23.516  1.00 23.54           C  
ANISOU  901  CG  PHE A 201     3061   2915   2969    385    415   -487       C  
ATOM    902  CD1 PHE A 201       8.080  -7.934 -23.547  1.00 27.42           C  
ANISOU  902  CD1 PHE A 201     3417   3356   3644    298    569   -582       C  
ATOM    903  CD2 PHE A 201       8.002 -10.270 -23.048  1.00 23.89           C  
ANISOU  903  CD2 PHE A 201     3113   3063   2902    521    375   -621       C  
ATOM    904  CE1 PHE A 201       9.399  -7.880 -23.131  1.00 25.50           C  
ANISOU  904  CE1 PHE A 201     2986   3231   3471    311    655   -885       C  
ATOM    905  CE2 PHE A 201       9.331 -10.222 -22.636  1.00 23.15           C  
ANISOU  905  CE2 PHE A 201     2845   3099   2854    607    409   -859       C  
ATOM    906  CZ  PHE A 201      10.022  -9.026 -22.670  1.00 22.64           C  
ANISOU  906  CZ  PHE A 201     2582   3048   2970    485    534  -1030       C  
ATOM    907  N   ALA A 202       5.742 -11.751 -26.049  1.00 20.34           N  
ANISOU  907  N   ALA A 202     3047   2619   2062    228    318   -298       N  
ATOM    908  CA  ALA A 202       6.342 -13.052 -26.336  1.00 25.35           C  
ANISOU  908  CA  ALA A 202     3752   3266   2612    220    430   -452       C  
ATOM    909  C   ALA A 202       7.144 -13.025 -27.628  1.00 28.48           C  
ANISOU  909  C   ALA A 202     4190   3755   2876     82    535   -493       C  
ATOM    910  O   ALA A 202       8.177 -13.696 -27.738  1.00 22.68           O  
ANISOU  910  O   ALA A 202     3447   3000   2170    100    673   -653       O  
ATOM    911  CB  ALA A 202       5.258 -14.125 -26.418  1.00 26.96           C  
ANISOU  911  CB  ALA A 202     4026   3455   2763    158    445   -520       C  
ATOM    912  N   TRP A 203       6.678 -12.272 -28.628  1.00 25.26           N  
ANISOU  912  N   TRP A 203     3838   3452   2308    -35    483   -345       N  
ATOM    913  CA  TRP A 203       7.280 -12.324 -29.949  1.00 27.06           C  
ANISOU  913  CA  TRP A 203     4171   3794   2318   -195    612   -371       C  
ATOM    914  C   TRP A 203       7.851 -11.006 -30.423  1.00 27.90           C  
ANISOU  914  C   TRP A 203     4344   3851   2406   -231    718   -198       C  
ATOM    915  O   TRP A 203       8.601 -11.010 -31.411  1.00 28.69           O  
ANISOU  915  O   TRP A 203     4557   4001   2343   -380    911   -244       O  
ATOM    916  CB  TRP A 203       6.260 -12.790 -31.006  1.00 28.09           C  
ANISOU  916  CB  TRP A 203     4376   4161   2136   -315    503   -358       C  
ATOM    917  CG  TRP A 203       5.430 -13.931 -30.582  1.00 32.25           C  
ANISOU  917  CG  TRP A 203     4827   4705   2722   -328    455   -553       C  
ATOM    918  CD1 TRP A 203       4.156 -13.883 -30.111  1.00 38.48           C  
ANISOU  918  CD1 TRP A 203     5526   5528   3567   -275    279   -527       C  
ATOM    919  CD2 TRP A 203       5.810 -15.309 -30.586  1.00 26.75           C  
ANISOU  919  CD2 TRP A 203     4140   3939   2086   -413    660   -835       C  
ATOM    920  NE1 TRP A 203       3.715 -15.149 -29.821  1.00 34.25           N  
ANISOU  920  NE1 TRP A 203     4958   4942   3115   -356    396   -793       N  
ATOM    921  CE2 TRP A 203       4.716 -16.042 -30.103  1.00 30.18           C  
ANISOU  921  CE2 TRP A 203     4520   4339   2606   -428    639   -961       C  
ATOM    922  CE3 TRP A 203       6.976 -15.991 -30.943  1.00 29.10           C  
ANISOU  922  CE3 TRP A 203     4476   4163   2418   -475    901  -1010       C  
ATOM    923  CZ2 TRP A 203       4.747 -17.430 -29.970  1.00 27.37           C  
ANISOU  923  CZ2 TRP A 203     4193   3836   2369   -505    896  -1226       C  
ATOM    924  CZ3 TRP A 203       7.001 -17.367 -30.826  1.00 30.36           C  
ANISOU  924  CZ3 TRP A 203     4640   4195   2699   -517   1109  -1259       C  
ATOM    925  CH2 TRP A 203       5.899 -18.071 -30.332  1.00 29.70           C  
ANISOU  925  CH2 TRP A 203     4546   4035   2702   -529   1126  -1348       C  
ATOM    926  N   ARG A 204       7.495  -9.879 -29.793  1.00 29.35           N  
ANISOU  926  N   ARG A 204     4480   3907   2763   -125    660    -16       N  
ATOM    927  CA  ARG A 204       7.760  -8.593 -30.429  1.00 31.90           C  
ANISOU  927  CA  ARG A 204     4935   4127   3060   -163    821    213       C  
ATOM    928  C   ARG A 204       9.254  -8.412 -30.661  1.00 29.61           C  
ANISOU  928  C   ARG A 204     4646   3735   2871   -311   1160      7       C  
ATOM    929  O   ARG A 204      10.076  -8.713 -29.786  1.00 28.16           O  
ANISOU  929  O   ARG A 204     4246   3511   2942   -295   1219   -295       O  
ATOM    930  CB  ARG A 204       7.196  -7.434 -29.590  1.00 28.29           C  
ANISOU  930  CB  ARG A 204     4393   3476   2880    -31    780    385       C  
ATOM    931  CG  ARG A 204       7.860  -7.199 -28.222  1.00 29.12           C  
ANISOU  931  CG  ARG A 204     4264   3445   3355    -17    872    117       C  
ATOM    932  CD  ARG A 204       8.875  -6.057 -28.331  1.00 28.35           C  
ANISOU  932  CD  ARG A 204     4160   3140   3473   -131   1234     58       C  
ATOM    933  NE  ARG A 204       9.534  -5.700 -27.070  1.00 27.45           N  
ANISOU  933  NE  ARG A 204     3761   2974   3695   -140   1322   -277       N  
ATOM    934  CZ  ARG A 204      10.541  -6.380 -26.522  1.00 29.28           C  
ANISOU  934  CZ  ARG A 204     3786   3363   3976   -147   1318   -653       C  
ATOM    935  NH1 ARG A 204      10.993  -7.495 -27.097  1.00 31.82           N  
ANISOU  935  NH1 ARG A 204     4164   3830   4095   -147   1266   -729       N  
ATOM    936  NH2 ARG A 204      11.099  -5.949 -25.394  1.00 26.80           N  
ANISOU  936  NH2 ARG A 204     3185   3085   3913   -136   1363   -976       N  
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.