CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 1909292211487908

Job options:

ID        	=	 1909292211487908
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


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                                                                                                                                  


A second structure was input as follows:


REMARK Date 2019-05-09 Time 16:33:37 CDT -0500 (1557437617.59 s)
REMARK PHENIX refinement
REMARK 
REMARK ****************** INPUT FILES AND LABELS ******************************
REMARK Reflections:
REMARK   file name      : /Users/pingwei/Cho1810/new_275.mtz
REMARK   labels         : ['IMEAN,SIGIMEAN']
REMARK R-free flags:
REMARK   file name      : /Users/pingwei/Cho1810/new_275.mtz
REMARK   label          : FreeR_flag
REMARK   test_flag_value: 0
REMARK Model file name(s): 
REMARK   /Users/pingwei/Cho1810/new.pdb
REMARK 
REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS *******************
REMARK Start: r_work = 0.2294 r_free = 0.2611 bonds = 0.002 angles = 0.469
REMARK Final: r_work = 0.2281 r_free = 0.2625 bonds = 0.002 angles = 0.449
REMARK ************************************************************************
REMARK 
REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ******************
REMARK leading digit, like 1_, means number of macro-cycle                     
REMARK 0    : statistics at the very beginning when nothing is done yet        
REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling             
REMARK 1_xyz: refinement of coordinates                                        
REMARK 1_wat: ordered solvent update (add / remove)                            
REMARK 1_gbr: group B-factor refinement                                        
REMARK ------------------------------------------------------------------------
REMARK  stage       r-work r-free bonds angles b_min b_max b_ave n_water shift
REMARK       0    : 0.4566 0.4515 0.002  0.47  25.1 172.7  61.3  35      0.000
REMARK       1_bss: 0.2294 0.2611 0.002  0.47  25.6 173.2  61.7  35      0.000
REMARK 1_settarget: 0.2294 0.2611 0.002  0.47  25.6 173.2  61.7  35      0.000
REMARK       1_nqh: 0.2294 0.2611 0.002  0.47  25.6 173.2  61.7  35      0.000
REMARK    1_weight: 0.2294 0.2611 0.002  0.47  25.6 173.2  61.7  35      0.000
REMARK    1_xyzrec: 0.2295 0.2621 0.002  0.45  25.6 173.2  61.7  35      0.018
REMARK       1_adp: 0.2300 0.2654 0.002  0.45  27.3 164.9  62.8  35      0.018
REMARK       2_bss: 0.2301 0.2660 0.002  0.45  27.0 164.5  62.5  35      0.018
REMARK 2_settarget: 0.2301 0.2660 0.002  0.45  27.0 164.5  62.5  35      0.018
REMARK 2_updatecdl: 0.2301 0.2660 0.002  0.46  27.0 164.5  62.5  35      0.018
REMARK       2_nqh: 0.2301 0.2660 0.002  0.46  27.0 164.5  62.5  35      0.018
REMARK       2_sol: 0.2295 0.2639 0.002  0.46  27.0 164.5  62.4  45       n/a
REMARK    2_weight: 0.2295 0.2639 0.002  0.46  27.0 164.5  62.4  45       n/a
REMARK    2_xyzrec: 0.2256 0.2637 0.002  0.50  27.0 164.5  62.4  45       n/a
REMARK       2_adp: 0.2274 0.2648 0.002  0.50  22.8 162.1  59.0  45       n/a
REMARK       3_bss: 0.2256 0.2613 0.002  0.50  24.4 163.7  60.7  45       n/a
REMARK 3_settarget: 0.2256 0.2613 0.002  0.50  24.4 163.7  60.7  45       n/a
REMARK 3_updatecdl: 0.2256 0.2613 0.002  0.50  24.4 163.7  60.7  45       n/a
REMARK     3_setrh: 0.2256 0.2613 0.002  0.50  24.4 163.7  60.7  45       n/a
REMARK       3_nqh: 0.2256 0.2613 0.002  0.50  24.4 163.7  60.7  45       n/a
REMARK       3_sol: 0.2260 0.2610 0.002  0.50  24.4 163.7  60.6  43       n/a
REMARK    3_weight: 0.2260 0.2610 0.002  0.50  24.4 163.7  60.6  43       n/a
REMARK    3_xyzrec: 0.2277 0.2618 0.002  0.45  24.4 163.7  60.6  43       n/a
REMARK       3_adp: 0.2282 0.2626 0.002  0.45  22.6 160.6  59.2  43       n/a
REMARK         end: 0.2281 0.2625 0.002  0.45  24.2 162.1  60.8  34       n/a
REMARK ------------------------------------------------------------------------
REMARK MODEL CONTENT.
REMARK  ELEMENT        ATOM RECORD COUNT   OCCUPANCY SUM
REMARK        C                     2642         2642.00
REMARK        S                       20           20.00
REMARK        O                      847          847.00
REMARK        N                      756          756.00
REMARK    TOTAL                     4265         4265.00

REMARK -----------------------------------------------------------------------
REMARK r_free_flags.md5.hexdigest a7670e66818a5950409921c57ad2422d
REMARK 
REMARK IF THIS FILE IS FOR PDB DEPOSITION: REMOVE ALL FROM THIS LINE UP.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.750   
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.650  
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.94 
REMARK   3   NUMBER OF REFLECTIONS             : 19103     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 19103     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2296
REMARK   3   R VALUE            (WORKING SET) : 0.2281
REMARK   3   FREE R VALUE                     : 0.2625
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.72  
REMARK   3   FREE R VALUE TEST SET COUNT      : 901       
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWORK CCFREE
REMARK   3     1 44.6563 -  4.9953    1.00     3107   136  0.2023 0.2302   0.922  0.907
REMARK   3     2  4.9953 -  3.9657    1.00     3040   139  0.1899 0.2305   0.899  0.849
REMARK   3     3  3.9657 -  3.4646    1.00     3040   157  0.2251 0.2432   0.863  0.834
REMARK   3     4  3.4646 -  3.1479    1.00     3027   141  0.2641 0.3044   0.807  0.779
REMARK   3     5  3.1479 -  2.9223    1.00     2985   167  0.2901 0.3359   0.775  0.743
REMARK   3     6  2.9223 -  2.7501    1.00     3003   161  0.3266 0.3519   0.714  0.604
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP FACTOR   : 4.00    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.44    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.00   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.002   0.021   4286
REMARK   3    ANGLE     :  0.449   9.755   5753
REMARK   3    CHIRALITY :  0.036   0.169    635
REMARK   3    PLANARITY :  0.002   0.026    747
REMARK   3    DIHEDRAL  : 16.873 179.995   2665
REMARK   3    MIN NONBONDED DISTANCE : 1.873 
REMARK   3  REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 5.66
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS : 0.79  %
REMARK   3      ALLOWED  : 3.16  %
REMARK   3      FAVORED  : 96.06 %
REMARK   3    ROTAMER OUTLIERS : 7.58 %
REMARK   3    CBETA DEVIATIONS : 0
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 0.0
REMARK   3      CIS-GENERAL     : 0.0
REMARK   3      TWISTED PROLINE : 0.0
REMARK   3      TWISTED GENERAL : 0.0
REMARK   3  
REMARK   3  ATOMIC DISPLACEMENT PARAMETERS.
REMARK   3   WILSON B : 50.75
REMARK   3   RMS(B_ISO_OR_EQUIVALENT_BONDED) : 2.82
REMARK   3   ATOMS          NUMBER OF ATOMS
REMARK   3                    ISO.  ANISO. 
REMARK   3    ALL         :   4265    4231
REMARK   3    ALL (NO H)  :   4265    4231
REMARK   3    SOLVENT     :     34       0
REMARK   3    NON-SOLVENT :   4231    4231
REMARK   3    HYDROGENS   :      0       0
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 19    
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: chain 'A' and (resid 86 through 99 )
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8793  21.6463  15.1602
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5210 T22:   0.4808                       
REMARK   3      T33:   0.4160 T12:   0.1080                       
REMARK   3      T13:  -0.0166 T23:   0.0312                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.5289 L22:   8.0400                       
REMARK   3      L33:   8.3461 L12:   0.3998                       
REMARK   3      L13:  -1.1101 L23:   0.5474                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.6684 S12:  -0.9056 S13:  -0.5781         
REMARK   3      S21:   0.4536 S22:   0.4409 S23:  -0.4086         
REMARK   3      S31:   0.5310 S32:   1.6983 S33:   0.2817         
REMARK   3   TLS GROUP : 2     
REMARK   3    SELECTION: chain 'A' and (resid 100 through 112 )
REMARK   3    ORIGIN FOR THE GROUP (A):  46.2983  39.4288  10.7791
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5343 T22:   0.4007                       
REMARK   3      T33:   0.4319 T12:   0.1197                       
REMARK   3      T13:   0.0544 T23:   0.0573                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   4.7260 L22:   6.5138                       
REMARK   3      L33:   3.6502 L12:   0.2317                       
REMARK   3      L13:   4.1526 L23:  -0.6122                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.4250 S12:   0.3528 S13:   0.7104         
REMARK   3      S21:   0.4899 S22:   0.0621 S23:   0.2038         
REMARK   3      S31:  -0.8595 S32:  -0.1230 S33:   0.3465         
REMARK   3   TLS GROUP : 3     
REMARK   3    SELECTION: chain 'A' and (resid 113 through 136 )
REMARK   3    ORIGIN FOR THE GROUP (A):  54.4727  35.6418   9.9053
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3722 T22:   0.3918                       
REMARK   3      T33:   0.3298 T12:  -0.0022                       
REMARK   3      T13:   0.0835 T23:  -0.0624                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   5.7273 L22:   5.4924                       
REMARK   3      L33:   6.9284 L12:   1.1871                       
REMARK   3      L13:   0.9722 L23:   1.6029                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0322 S12:  -0.1194 S13:   0.9459         
REMARK   3      S21:   0.1175 S22:  -0.0246 S23:   0.0517         
REMARK   3      S31:  -0.6958 S32:   0.4614 S33:   0.0036         
REMARK   3   TLS GROUP : 4     
REMARK   3    SELECTION: chain 'A' and (resid 137 through 162 )
REMARK   3    ORIGIN FOR THE GROUP (A):  55.2326  28.0538   9.6570
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1999 T22:   0.3124                       
REMARK   3      T33:   0.3309 T12:   0.0418                       
REMARK   3      T13:   0.0279 T23:   0.0595                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   6.9542 L22:   9.0224                       
REMARK   3      L33:   8.0099 L12:  -0.0295                       
REMARK   3      L13:  -0.2383 L23:   0.1145                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.1714 S12:   0.1104 S13:   0.1467         
REMARK   3      S21:   0.0123 S22:   0.0439 S23:  -0.5778         
REMARK   3      S31:  -0.0502 S32:   0.4499 S33:  -0.2036         
REMARK   3   TLS GROUP : 5     
REMARK   3    SELECTION: chain 'A' and (resid 163 through 188 )
REMARK   3    ORIGIN FOR THE GROUP (A):  53.3063  32.5988   1.3118
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3716 T22:   0.3301                       
REMARK   3      T33:   0.4026 T12:  -0.0203                       
REMARK   3      T13:  -0.0456 T23:   0.0518                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   7.8774 L22:   6.6251                       
REMARK   3      L33:   8.2180 L12:   5.6849                       
REMARK   3      L13:   1.8437 L23:   4.0571                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.6523 S12:   0.1968 S13:   0.4607         
REMARK   3      S21:  -1.2636 S22:   0.2951 S23:   0.2497         
REMARK   3      S31:  -0.5846 S32:   0.5185 S33:   0.2981         
REMARK   3   TLS GROUP : 6     
REMARK   3    SELECTION: chain 'A' and (resid 189 through 195 )
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2651  39.1303  11.0123
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5601 T22:   0.7851                       
REMARK   3      T33:   0.6853 T12:  -0.2911                       
REMARK   3      T13:   0.0753 T23:  -0.1983                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   9.4268 L22:   8.4499                       
REMARK   3      L33:   8.8279 L12:  -4.2392                       
REMARK   3      L13:   0.8140 L23:   1.0510                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.5502 S12:  -0.2398 S13:   0.6867         
REMARK   3      S21:   0.4150 S22:   0.9534 S23:  -1.0250         
REMARK   3      S31:  -1.8277 S32:   1.6995 S33:  -0.2648         
REMARK   3   TLS GROUP : 7     
REMARK   3    SELECTION: chain 'A' and (resid 196 through 201 )
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6357  24.6863   8.2434
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5183 T22:   1.0607                       
REMARK   3      T33:   1.2835 T12:  -0.0814                       
REMARK   3      T13:  -0.0502 T23:  -0.1964                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.0732 L22:   2.0056                       
REMARK   3      L33:   4.4996 L12:   0.7312                       
REMARK   3      L13:  -0.5280 L23:  -6.6885                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.9152 S12:   1.4034 S13:  -2.1264         
REMARK   3      S21:   1.0341 S22:   0.1132 S23:  -4.4271         
REMARK   3      S31:  -0.0118 S32:   2.8760 S33:   0.4393         
REMARK   3   TLS GROUP : 8     
REMARK   3    SELECTION: chain 'A' and (resid 202 through 212 )
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8416  39.9452   8.1060
REMARK   3    T TENSOR                                            
REMARK   3      T11:   1.3376 T22:   1.6234                       
REMARK   3      T33:   1.0447 T12:  -0.4329                       
REMARK   3      T13:  -0.1882 T23:  -0.0424                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   6.5219 L22:   6.4206                       
REMARK   3      L33:   2.8408 L12:   1.7219                       
REMARK   3      L13:  -0.0888 L23:  -2.1719                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   1.3461 S12:  -0.8770 S13:  -0.3116         
REMARK   3      S21:   1.6190 S22:  -0.6141 S23:  -0.7340         
REMARK   3      S31:   0.9757 S32:  -0.8674 S33:  -0.6266         
REMARK   3   TLS GROUP : 9     
REMARK   3    SELECTION: chain 'C' and (resid 433 through 534 )
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7080  -1.9172  24.5914
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.8627 T22:   0.6132                       
REMARK   3      T33:   0.4844 T12:   0.0125                       
REMARK   3      T13:   0.0052 T23:  -0.0774                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   6.7923 L22:   8.1171                       
REMARK   3      L33:   4.1663 L12:  -6.5153                       
REMARK   3      L13:   3.3218 L23:  -3.4938                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.3209 S12:  -0.9729 S13:  -0.3125         
REMARK   3      S21:   0.6514 S22:   0.6502 S23:  -0.0512         
REMARK   3      S31:   0.4050 S32:   0.1179 S33:  -0.3000         
REMARK   3   TLS GROUP : 10    
REMARK   3    SELECTION: chain 'C' and (resid 535 through 561 )
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6383 -14.8217  23.7532
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.8541 T22:   0.7250                       
REMARK   3      T33:   0.6206 T12:   0.3085                       
REMARK   3      T13:   0.0593 T23:  -0.0200                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   3.5544 L22:   6.0467                       
REMARK   3      L33:   4.4499 L12:  -0.4213                       
REMARK   3      L13:   0.6652 L23:   0.7693                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.5839 S12:   0.2155 S13:  -0.7422         
REMARK   3      S21:  -1.0680 S22:  -0.0009 S23:   0.2566         
REMARK   3      S31:   1.2351 S32:   0.2005 S33:  -0.4836         
REMARK   3   TLS GROUP : 11    
REMARK   3    SELECTION: chain 'C' and (resid 562 through 597 )
REMARK   3    ORIGIN FOR THE GROUP (A):  44.5629  18.9247  15.8428
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3557 T22:   0.3888                       
REMARK   3      T33:   0.2910 T12:  -0.0419                       
REMARK   3      T13:   0.0147 T23:   0.0071                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   5.5547 L22:   7.5071                       
REMARK   3      L33:   6.4329 L12:  -0.4590                       
REMARK   3      L13:   1.6873 L23:  -1.2425                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.1008 S12:  -0.6120 S13:  -0.0899         
REMARK   3      S21:   0.9950 S22:   0.2130 S23:   0.2897         
REMARK   3      S31:   0.0057 S32:  -0.1442 S33:  -0.0761         
REMARK   3   TLS GROUP : 12    
REMARK   3    SELECTION: chain 'B' and (resid 86 through 99 )
REMARK   3    ORIGIN FOR THE GROUP (A):  45.9693   7.3917 -10.6897
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2879 T22:   0.5018                       
REMARK   3      T33:   0.5271 T12:   0.0210                       
REMARK   3      T13:   0.0648 T23:   0.0347                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   3.8057 L22:   5.2863                       
REMARK   3      L33:   4.3808 L12:  -0.1285                       
REMARK   3      L13:  -3.0391 L23:   1.6961                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.2550 S12:   0.5417 S13:  -0.1799         
REMARK   3      S21:  -0.3281 S22:  -0.2359 S23:  -0.8589         
REMARK   3      S31:   0.1920 S32:   0.3696 S33:   0.1511         
REMARK   3   TLS GROUP : 13    
REMARK   3    SELECTION: chain 'B' and (resid 100 through 120 )
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8066   7.7165  -4.5689
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3547 T22:   0.3931                       
REMARK   3      T33:   0.5041 T12:   0.0475                       
REMARK   3      T13:   0.0717 T23:   0.0039                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   7.9054 L22:   6.1567                       
REMARK   3      L33:   5.9386 L12:   2.0639                       
REMARK   3      L13:   3.6739 L23:   3.5384                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0274 S12:  -0.2709 S13:   0.1020         
REMARK   3      S21:   0.2383 S22:  -0.5083 S23:   1.0197         
REMARK   3      S31:  -0.0379 S32:  -0.7643 S33:   0.3634         
REMARK   3   TLS GROUP : 14    
REMARK   3    SELECTION: chain 'B' and (resid 121 through 151 )
REMARK   3    ORIGIN FOR THE GROUP (A):  39.5170   2.0802  -5.0418
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3656 T22:   0.3079                       
REMARK   3      T33:   0.3989 T12:   0.0600                       
REMARK   3      T13:   0.1279 T23:   0.0310                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   7.0577 L22:   4.8326                       
REMARK   3      L33:   5.1853 L12:   0.8659                       
REMARK   3      L13:   2.7222 L23:   0.9562                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0843 S12:  -0.1113 S13:  -0.5691         
REMARK   3      S21:   0.3066 S22:  -0.0231 S23:   0.1762         
REMARK   3      S31:   0.6391 S32:   0.2605 S33:  -0.1338         
REMARK   3   TLS GROUP : 15    
REMARK   3    SELECTION: chain 'B' and (resid 152 through 170 )
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2377   8.7401  -3.9257
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2129 T22:   0.3819                       
REMARK   3      T33:   0.3770 T12:   0.0219                       
REMARK   3      T13:  -0.0172 T23:   0.0000                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   5.8674 L22:   8.2518                       
REMARK   3      L33:   8.5580 L12:   3.5728                       
REMARK   3      L13:   4.3864 L23:   3.7290                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.1138 S12:   0.1408 S13:  -0.0930         
REMARK   3      S21:  -0.6198 S22:  -0.0184 S23:   0.4564         
REMARK   3      S31:  -0.3266 S32:  -0.3232 S33:   0.1071         
REMARK   3   TLS GROUP : 16    
REMARK   3    SELECTION: chain 'B' and (resid 171 through 195 )
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8917  -2.4860  -0.0551
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5441 T22:   0.3704                       
REMARK   3      T33:   0.5787 T12:   0.0497                       
REMARK   3      T13:   0.0659 T23:   0.0899                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   5.5133 L22:   3.6546                       
REMARK   3      L33:   9.7240 L12:   2.4819                       
REMARK   3      L13:   3.4313 L23:   2.1664                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.2489 S12:  -0.3486 S13:  -0.5913         
REMARK   3      S21:   0.8549 S22:  -0.1014 S23:  -0.0127         
REMARK   3      S31:   0.9205 S32:  -0.5271 S33:  -0.1848         
REMARK   3   TLS GROUP : 17    
REMARK   3    SELECTION: chain 'B' and (resid 196 through 204 )
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7563  -3.9794  -1.5883
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.6617 T22:   0.5956                       
REMARK   3      T33:   0.9564 T12:   0.0775                       
REMARK   3      T13:   0.1668 T23:   0.1595                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   8.0471 L22:   2.5126                       
REMARK   3      L33:   2.0014 L12:  -0.1898                       
REMARK   3      L13:   4.5458 L23:   4.8702                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.1683 S12:  -1.5474 S13:  -2.2779         
REMARK   3      S21:   1.5858 S22:   1.5260 S23:  -0.0945         
REMARK   3      S31:   3.5269 S32:  -0.7406 S33:   0.2015         
REMARK   3   TLS GROUP : 18    
REMARK   3    SELECTION: chain 'D' and (resid 433 through 497 )
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2390   7.8791 -19.5055
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.4792 T22:   0.5529                       
REMARK   3      T33:   0.4780 T12:  -0.0990                       
REMARK   3      T13:  -0.0343 T23:   0.0454                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   4.8852 L22:   2.7672                       
REMARK   3      L33:   3.0935 L12:  -2.1792                       
REMARK   3      L13:  -2.4402 L23:   1.8757                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.1844 S12:   0.8941 S13:   0.4249         
REMARK   3      S21:  -0.0307 S22:  -0.0621 S23:  -0.2994         
REMARK   3      S31:   0.2437 S32:  -0.1088 S33:  -0.0425         
REMARK   3   TLS GROUP : 19    
REMARK   3    SELECTION: chain 'D' and (resid 498 through 597 )
REMARK   3    ORIGIN FOR THE GROUP (A):  69.3843   8.2142 -18.2864
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.4811 T22:   0.5708                       
REMARK   3      T33:   0.4184 T12:   0.0282                       
REMARK   3      T13:  -0.0092 T23:   0.0225                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   7.6025 L22:   2.1074                       
REMARK   3      L33:   1.8953 L12:  -1.9760                       
REMARK   3      L13:  -2.6691 L23:   0.9095                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.2116 S12:   0.5454 S13:   0.3366         
REMARK   3      S21:  -0.2930 S22:  -0.0322 S23:  -0.4730         
REMARK   3      S31:   0.1054 S32:   0.2874 S33:  -0.2681         

REMARK   3
CRYST1   60.980   94.030   67.220  90.00 105.31  90.00 P 1 21 1
SCALE1      0.016399  0.000000  0.004489        0.00000
SCALE2      0.000000  0.010635  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015424        0.00000
ATOM      1  N   ALA A  86      63.983  10.199   4.916  1.00 84.54           N
ANISOU    1  N   ALA A  86    11360   9555  11207   4848   3961    -43       N
ATOM      2  CA  ALA A  86      62.905  10.793   4.134  1.00 78.66           C
ANISOU    2  CA  ALA A  86    11180   8348  10358   4164   4008   -200       C
ATOM      3  C   ALA A  86      61.561  10.643   4.843  1.00 73.81           C
ANISOU    3  C   ALA A  86    11033   7315   9698   3957   3663      4       C
ATOM      4  O   ALA A  86      61.387   9.751   5.675  1.00 75.67           O
ANISOU    4  O   ALA A  86    11384   7439   9926   4295   3517    265       O
ATOM      5  CB  ALA A  86      62.847  10.164   2.747  1.00 80.95           C
ANISOU    5  CB  ALA A  86    12074   8123  10560   3934   4379   -365       C
ATOM      6  N   SER A  87      60.624  11.531   4.504  1.00 68.20           N
ANISOU    6  N   SER A  87    10587   6380   8944   3357   3541   -130       N
ATOM      7  CA  SER A  87      59.267  11.525   5.045  1.00 63.76           C
ANISOU    7  CA  SER A  87    10400   5452   8376   3032   3204     17       C
ATOM      8  C   SER A  87      59.268  11.730   6.557  1.00 62.95           C
ANISOU    8  C   SER A  87     9894   5714   8311   3391   2914    262       C
ATOM      9  O   SER A  87      59.330  10.764   7.325  1.00 65.85           O
ANISOU    9  O   SER A  87    10307   6065   8649   3759   2856    506       O
ATOM     10  CB  SER A  87      58.547  10.225   4.676  1.00 65.50           C
ANISOU   10  CB  SER A  87    11204   5151   8530   2902   3245    128       C
ATOM     11  OG  SER A  87      57.159  10.316   4.946  1.00 61.52           O
ANISOU   11  OG  SER A  87    10937   4416   8020   2411   2935    192       O
ATOM     12  N   ARG A  88      59.193  12.989   6.991  1.00 59.46           N
ANISOU   12  N   ARG A  88     9021   5728   7843   3034   2569    203       N
ATOM     13  CA  ARG A  88      59.227  13.344   8.403  1.00 58.88           C
ANISOU   13  CA  ARG A  88     8558   6079   7734   3259   2231    403       C
ATOM     14  C   ARG A  88      58.176  14.416   8.665  1.00 53.42           C
ANISOU   14  C   ARG A  88     7923   5362   7012   2631   1885    351       C
ATOM     15  O   ARG A  88      57.455  14.844   7.760  1.00 50.41           O
ANISOU   15  O   ARG A  88     7844   4653   6658   2079   1877    182       O
ATOM     16  CB  ARG A  88      60.625  13.825   8.818  1.00 62.32           C
ANISOU   16  CB  ARG A  88     8226   7308   8143   3568   2139    365       C
ATOM     17  CG  ARG A  88      61.730  12.800   8.602  1.00 68.66           C
ANISOU   17  CG  ARG A  88     8857   8213   9018   4285   2477    419       C
ATOM     18  CD  ARG A  88      63.098  13.458   8.499  1.00 72.25           C
ANISOU   18  CD  ARG A  88     8479   9459   9515   4360   2461    256       C
ATOM     19  NE  ARG A  88      63.428  14.246   9.683  1.00 72.25           N
ANISOU   19  NE  ARG A  88     7902  10113   9435   4362   1981    333       N
ATOM     20  CZ  ARG A  88      64.626  14.774   9.916  1.00 76.31           C
ANISOU   20  CZ  ARG A  88     7603  11405   9986   4467   1855    234       C
ATOM     21  NH1 ARG A  88      65.612  14.594   9.047  1.00 80.76           N
ANISOU   21  NH1 ARG A  88     7781  12207  10699   4605   2225     62       N
ATOM     22  NH2 ARG A  88      64.840  15.479  11.019  1.00 76.50           N
ANISOU   22  NH2 ARG A  88     7195  11975   9894   4415   1373    293       N
ATOM     23  N   TYR A  89      58.089  14.851   9.921  1.00 52.69           N
ANISOU   23  N   TYR A  89     7563   5611   6847   2750   1591    500       N
ATOM     24  CA  TYR A  89      57.162  15.913  10.305  1.00 48.25           C
ANISOU   24  CA  TYR A  89     7020   5062   6251   2242   1291    451       C
ATOM     25  C   TYR A  89      57.819  16.739  11.402  1.00 50.40           C
ANISOU   25  C   TYR A  89     6792   5987   6373   2348    987    478       C
ATOM     26  O   TYR A  89      58.036  16.241  12.510  1.00 51.46           O
ANISOU   26  O   TYR A  89     6855   6289   6408   2824    911    702       O
ATOM     27  CB  TYR A  89      55.824  15.339  10.766  1.00 46.58           C
ANISOU   27  CB  TYR A  89     7271   4319   6107   2214   1319    631       C
ATOM     28  CG  TYR A  89      54.846  16.384  11.255  1.00 42.81           C
ANISOU   28  CG  TYR A  89     6772   3869   5627   1788   1054    592       C
ATOM     29  CD1 TYR A  89      54.151  16.209  12.443  1.00 42.75           C
ANISOU   29  CD1 TYR A  89     6867   3797   5581   1942   1012    799       C
ATOM     30  CD2 TYR A  89      54.628  17.550  10.533  1.00 39.91           C
ANISOU   30  CD2 TYR A  89     6320   3567   5275   1261    878    354       C
ATOM     31  CE1 TYR A  89      53.259  17.161  12.896  1.00 39.93           C
ANISOU   31  CE1 TYR A  89     6482   3459   5232   1602    828    750       C
ATOM     32  CE2 TYR A  89      53.740  18.509  10.978  1.00 37.09           C
ANISOU   32  CE2 TYR A  89     5960   3207   4926    946    652    319       C
ATOM     33  CZ  TYR A  89      53.059  18.309  12.160  1.00 37.13           C
ANISOU   33  CZ  TYR A  89     6020   3167   4922   1129    640    508       C
ATOM     34  OH  TYR A  89      52.174  19.261  12.608  1.00 34.91           O
ANISOU   34  OH  TYR A  89     5728   2877   4659    861    472    460       O
ATOM     35  N   LEU A  90      58.128  17.995  11.092  1.00 47.46           N
ANISOU   35  N   LEU A  90     6133   5951   5947   1885    805    250       N
ATOM     36  CA  LEU A  90      58.835  18.889  11.998  1.00 48.72           C
ANISOU   36  CA  LEU A  90     5825   6740   5945   1866    502    210       C
ATOM     37  C   LEU A  90      57.867  19.909  12.584  1.00 45.06           C
ANISOU   37  C   LEU A  90     5544   6187   5388   1469    249    174       C
ATOM     38  O   LEU A  90      56.978  20.405  11.886  1.00 41.58           O
ANISOU   38  O   LEU A  90     5406   5361   5032   1036    270     61       O
ATOM     39  CB  LEU A  90      59.977  19.607  11.274  1.00 50.67           C
ANISOU   39  CB  LEU A  90     5620   7442   6190   1591    518    -41       C
ATOM     40  CG  LEU A  90      60.909  18.715  10.450  1.00 54.53           C
ANISOU   40  CG  LEU A  90     5919   7993   6807   1924    863    -66       C
ATOM     41  CD1 LEU A  90      62.006  19.540   9.795  1.00 56.92           C
ANISOU   41  CD1 LEU A  90     5727   8788   7113   1571    922   -329       C
ATOM     42  CD2 LEU A  90      61.502  17.610  11.310  1.00 59.01           C
ANISOU   42  CD2 LEU A  90     6270   8770   7380   2711    870    181       C
ATOM     43  N   THR A  91      58.045  20.221  13.867  1.00 46.41           N
ANISOU   43  N   THR A  91     5552   6713   5368   1645      0    268       N
ATOM     44  CA  THR A  91      57.151  21.133  14.578  1.00 43.77           C
ANISOU   44  CA  THR A  91     5423   6292   4915   1356   -192    241       C
ATOM     45  C   THR A  91      57.984  22.100  15.409  1.00 46.01           C
ANISOU   45  C   THR A  91     5368   7174   4942   1246   -516    129       C
ATOM     46  O   THR A  91      58.591  21.700  16.407  1.00 49.57           O
ANISOU   46  O   THR A  91     5631   7992   5212   1650   -670    273       O
ATOM     47  CB  THR A  91      56.169  20.370  15.469  1.00 43.44           C
ANISOU   47  CB  THR A  91     5736   5912   4855   1681    -98    503       C
ATOM     48  OG1 THR A  91      56.890  19.457  16.304  1.00 47.57           O
ANISOU   48  OG1 THR A  91     6155   6686   5232   2259   -115    729       O
ATOM     49  CG2 THR A  91      55.167  19.595  14.629  1.00 41.24           C
ANISOU   49  CG2 THR A  91     5812   5011   4847   1623    188    565       C
ATOM     50  N   ASP A  92      58.004  23.371  15.003  1.00 44.46           N
ANISOU   50  N   ASP A  92     5138   7052   4703    691   -641   -126       N
ATOM     51  CA  ASP A  92      58.630  24.413  15.808  1.00 46.63           C
ANISOU   51  CA  ASP A  92     5194   7810   4711    466   -956   -269       C
ATOM     52  C   ASP A  92      57.706  24.950  16.892  1.00 45.37           C
ANISOU   52  C   ASP A  92     5400   7487   4350    446  -1090   -224       C
ATOM     53  O   ASP A  92      58.193  25.521  17.874  1.00 48.08           O
ANISOU   53  O   ASP A  92     5644   8223   4400    408  -1363   -282       O
ATOM     54  CB  ASP A  92      59.078  25.579  14.922  1.00 46.24           C
ANISOU   54  CB  ASP A  92     5037   7860   4672   -161   -993   -569       C
ATOM     55  CG  ASP A  92      60.169  25.192  13.948  1.00 48.68           C
ANISOU   55  CG  ASP A  92     4927   8436   5132   -190   -827   -653       C
ATOM     56  OD1 ASP A  92      61.000  24.323  14.288  1.00 52.33           O
ANISOU   56  OD1 ASP A  92     4980   9279   5622    267   -827   -533       O
ATOM     57  OD2 ASP A  92      60.199  25.768  12.840  1.00 47.44           O
ANISOU   57  OD2 ASP A  92     4870   8102   5054   -650   -681   -834       O
ATOM     58  N   MET A  93      56.395  24.785  16.736  1.00 44.36           N
ANISOU   58  N   MET A  93     5679   6805   4370    459   -900   -137       N
ATOM     59  CA  MET A  93      55.408  25.378  17.624  1.00 41.90           C
ANISOU   59  CA  MET A  93     5708   6291   3920    414   -937   -125       C
ATOM     60  C   MET A  93      54.752  24.316  18.498  1.00 41.55           C
ANISOU   60  C   MET A  93     5864   6067   3856    887   -766    163       C
ATOM     61  O   MET A  93      54.630  23.151  18.108  1.00 41.42           O
ANISOU   61  O   MET A  93     5849   5852   4037   1164   -561    347       O
ATOM     62  CB  MET A  93      54.329  26.121  16.827  1.00 39.40           C
ANISOU   62  CB  MET A  93     5662   5498   3812     58   -846   -257       C
ATOM     63  CG  MET A  93      54.819  27.385  16.138  1.00 37.62           C
ANISOU   63  CG  MET A  93     5414   5360   3519   -449  -1009   -536       C
ATOM     64  SD  MET A  93      53.556  28.177  15.122  1.00 33.61           S
ANISOU   64  SD  MET A  93     5274   4253   3242   -765   -951   -647       S
ATOM     65  CE  MET A  93      53.420  27.005  13.776  1.00 31.95           C
ANISOU   65  CE  MET A  93     4995   3784   3359   -687   -764   -538       C
ATOM     66  N   THR A  94      54.331  24.736  19.686  1.00 42.76           N
ANISOU   66  N   THR A  94     6247   6258   3740    956   -821    195       N
ATOM     67  CA  THR A  94      53.559  23.889  20.578  1.00 43.73           C
ANISOU   67  CA  THR A  94     6654   6156   3804   1328   -596    458       C
ATOM     68  C   THR A  94      52.073  23.997  20.245  1.00 40.78           C
ANISOU   68  C   THR A  94     6509   5251   3733   1180   -302    458       C
ATOM     69  O   THR A  94      51.648  24.833  19.445  1.00 38.23           O
ANISOU   69  O   THR A  94     6156   4756   3611    836   -341    256       O
ATOM     70  CB  THR A  94      53.806  24.275  22.037  1.00 47.19           C
ANISOU   70  CB  THR A  94     7281   6886   3761   1474   -761    490       C
ATOM     71  OG1 THR A  94      53.423  25.641  22.244  1.00 46.35           O
ANISOU   71  OG1 THR A  94     7327   6751   3532   1106   -849    235       O
ATOM     72  CG2 THR A  94      55.276  24.107  22.390  1.00 51.02           C
ANISOU   72  CG2 THR A  94     7469   7952   3965   1643  -1124    501       C
ATOM     73  N   LEU A  95      51.277  23.126  20.872  1.00 41.77           N
ANISOU   73  N   LEU A  95     6863   5117   3892   1446     -7    695       N
ATOM     74  CA  LEU A  95      49.833  23.169  20.664  1.00 40.01           C
ANISOU   74  CA  LEU A  95     6768   4446   3990   1310    289    700       C
ATOM     75  C   LEU A  95      49.246  24.501  21.104  1.00 42.23           C
ANISOU   75  C   LEU A  95     7154   4717   4176   1115    251    500       C
ATOM     76  O   LEU A  95      48.288  24.990  20.494  1.00 42.90           O
ANISOU   76  O   LEU A  95     7197   4514   4590    917    337    389       O
ATOM     77  CB  LEU A  95      49.157  22.019  21.410  1.00 42.19           C
ANISOU   77  CB  LEU A  95     7279   4479   4273   1588    659    988       C
ATOM     78  CG  LEU A  95      49.349  20.630  20.802  1.00 42.50           C
ANISOU   78  CG  LEU A  95     7312   4321   4516   1747    798   1184       C
ATOM     79  CD1 LEU A  95      48.628  19.576  21.624  1.00 45.31           C
ANISOU   79  CD1 LEU A  95     7990   4384   4841   1964   1201   1469       C
ATOM     80  CD2 LEU A  95      48.863  20.614  19.362  1.00 39.41           C
ANISOU   80  CD2 LEU A  95     6736   3651   4586   1435    800   1044       C
ATOM     81  N   GLU A  96      49.804  25.102  22.157  1.00 42.79           N
ANISOU   81  N   GLU A  96     7382   5086   3788   1185    107    448       N
ATOM     82  CA  GLU A  96      49.361  26.427  22.575  1.00 44.07           C
ANISOU   82  CA  GLU A  96     7720   5215   3808   1003     73    225       C
ATOM     83  C   GLU A  96      49.697  27.469  21.516  1.00 42.99           C
ANISOU   83  C   GLU A  96     7437   5088   3811    642   -203    -42       C
ATOM     84  O   GLU A  96      48.860  28.312  21.172  1.00 42.11           O
ANISOU   84  O   GLU A  96     7411   4699   3888    490   -142   -188       O
ATOM     85  CB  GLU A  96      49.994  26.789  23.920  1.00 46.05           C
ANISOU   85  CB  GLU A  96     8241   5786   3471   1120    -57    211       C
ATOM     86  CG  GLU A  96      49.410  28.027  24.592  1.00 47.35           C
ANISOU   86  CG  GLU A  96     8729   5841   3420    997     13      1       C
ATOM     87  CD  GLU A  96      49.952  29.327  24.025  1.00 46.43           C
ANISOU   87  CD  GLU A  96     8583   5813   3245    626   -320   -314       C
ATOM     88  OE1 GLU A  96      51.085  29.323  23.498  1.00 46.09           O
ANISOU   88  OE1 GLU A  96     8290   6078   3144    454   -657   -376       O
ATOM     89  OE2 GLU A  96      49.241  30.351  24.102  1.00 46.54           O
ANISOU   89  OE2 GLU A  96     8833   5572   3278    512   -214   -500       O
ATOM     90  N   GLU A  97      50.922  27.425  20.985  1.00 44.30           N
ANISOU   90  N   GLU A  97     7386   5565   3883    516   -491   -103       N
ATOM     91  CA  GLU A  97      51.330  28.401  19.980  1.00 42.15           C
ANISOU   91  CA  GLU A  97     7025   5295   3693    125   -712   -349       C
ATOM     92  C   GLU A  97      50.528  28.256  18.694  1.00 40.18           C
ANISOU   92  C   GLU A  97     6713   4649   3906     13   -602   -347       C
ATOM     93  O   GLU A  97      50.257  29.255  18.016  1.00 35.37           O
ANISOU   93  O   GLU A  97     6211   3848   3381   -262   -706   -531       O
ATOM     94  CB  GLU A  97      52.826  28.266  19.695  1.00 42.66           C
ANISOU   94  CB  GLU A  97     6804   5813   3591      9   -972   -404       C
ATOM     95  CG  GLU A  97      53.714  28.848  20.785  1.00 43.68           C
ANISOU   95  CG  GLU A  97     6973   6379   3243    -47  -1230   -509       C
ATOM     96  CD  GLU A  97      55.190  28.628  20.516  1.00 45.42           C
ANISOU   96  CD  GLU A  97     6777   7116   3364   -137  -1491   -556       C
ATOM     97  OE1 GLU A  97      55.530  27.605  19.886  1.00 45.59           O
ANISOU   97  OE1 GLU A  97     6508   7190   3624     73  -1400   -404       O
ATOM     98  OE2 GLU A  97      56.009  29.476  20.933  1.00 48.28           O
ANISOU   98  OE2 GLU A  97     7093   7832   3419   -426  -1774   -757       O
ATOM     99  N   MET A  98      50.137  27.030  18.342  1.00 50.21           N
ANISOU   99  N   MET A  98     7860   5768   5451    214   -413   -143       N
ATOM    100  CA  MET A  98      49.323  26.833  17.147  1.00 44.23           C
ANISOU  100  CA  MET A  98     7062   4636   5108     87   -353   -147       C
ATOM    101  C   MET A  98      47.908  27.360  17.346  1.00 39.48           C
ANISOU  101  C   MET A  98     6573   3706   4722    103   -231   -172       C
ATOM    102  O   MET A  98      47.314  27.929  16.422  1.00 31.70           O
ANISOU  102  O   MET A  98     5602   2466   3976    -75   -342   -279       O
ATOM    103  CB  MET A  98      49.283  25.351  16.775  1.00 41.35           C
ANISOU  103  CB  MET A  98     6587   4172   4953    264   -177     59       C
ATOM    104  CG  MET A  98      50.594  24.789  16.264  1.00 43.37           C
ANISOU  104  CG  MET A  98     6696   4686   5098    286   -266     69       C
ATOM    105  SD  MET A  98      50.449  23.032  15.886  1.00 37.93           S
ANISOU  105  SD  MET A  98     6004   3770   4637    546     -7    308       S
ATOM    106  CE  MET A  98      49.026  23.035  14.799  1.00 30.44           C
ANISOU  106  CE  MET A  98     5145   2307   4115    268     47    251       C
ATOM    107  N   SER A  99      47.356  27.187  18.544  1.00 40.53           N
ANISOU  107  N   SER A  99     6789   3845   4766    336      3    -71       N
ATOM    108  CA  SER A  99      45.956  27.480  18.814  1.00 38.24           C
ANISOU  108  CA  SER A  99     6519   3271   4740    412    221    -70       C
ATOM    109  C   SER A  99      45.737  28.826  19.491  1.00 39.61           C
ANISOU  109  C   SER A  99     6914   3443   4695    418    199   -251       C
ATOM    110  O   SER A  99      44.585  29.202  19.723  1.00 38.85           O
ANISOU  110  O   SER A  99     6814   3121   4828    527    398   -275       O
ATOM    111  CB  SER A  99      45.354  26.370  19.679  1.00 42.97           C
ANISOU  111  CB  SER A  99     7102   3819   5408    647    608    160       C
ATOM    112  OG  SER A  99      46.107  26.192  20.866  1.00 51.15           O
ANISOU  112  OG  SER A  99     8345   5119   5971    827    672    242       O
ATOM    113  N   ARG A 100      46.801  29.560  19.806  1.00 43.82           N
ANISOU  113  N   ARG A 100     7352   4992   4307    539    804     96       N
ATOM    114  CA  ARG A 100      46.655  30.809  20.541  1.00 42.67           C
ANISOU  114  CA  ARG A 100     7522   4766   3924    684    984     26       C
ATOM    115  C   ARG A 100      45.903  31.847  19.717  1.00 40.64           C
ANISOU  115  C   ARG A 100     7040   4636   3764    913   1228    -11       C
ATOM    116  O   ARG A 100      46.143  32.006  18.517  1.00 39.51           O
ANISOU  116  O   ARG A 100     6610   4537   3865    939   1138    -11       O
ATOM    117  CB  ARG A 100      48.026  31.358  20.934  1.00 43.00           C
ANISOU  117  CB  ARG A 100     7873   4505   3960    640    664    -71       C
ATOM    118  CG  ARG A 100      47.974  32.572  21.845  1.00 42.78           C
ANISOU  118  CG  ARG A 100     8269   4318   3669    786    743   -168       C
ATOM    119  CD  ARG A 100      49.347  33.196  21.982  1.00 42.62           C
ANISOU  119  CD  ARG A 100     8476   3967   3751    734    356   -233       C
ATOM    120  NE  ARG A 100      50.356  32.206  22.342  1.00 43.14           N
ANISOU  120  NE  ARG A 100     8618   3873   3901    504      7   -197       N
ATOM    121  CZ  ARG A 100      51.665  32.427  22.302  1.00 40.65           C
ANISOU  121  CZ  ARG A 100     8358   3290   3797    409   -376   -221       C
ATOM    122  NH1 ARG A 100      52.126  33.608  21.913  1.00 40.17           N
ANISOU  122  NH1 ARG A 100     8292   3103   3866    493   -456   -247       N
ATOM    123  NH2 ARG A 100      52.514  31.468  22.645  1.00 40.11           N
ANISOU  123  NH2 ARG A 100     8327   3066   3847    221   -710   -204       N
ATOM    124  N   ASP A 101      44.985  32.553  20.371  1.00 45.16           N
ANISOU  124  N   ASP A 101     7753   5271   4135   1086   1532    -50       N
ATOM    125  CA  ASP A 101      44.294  33.661  19.727  1.00 44.26           C
ANISOU  125  CA  ASP A 101     7474   5207   4138   1330   1704   -113       C
ATOM    126  C   ASP A 101      45.232  34.853  19.589  1.00 44.47           C
ANISOU  126  C   ASP A 101     7728   4964   4205   1406   1462   -219       C
ATOM    127  O   ASP A 101      46.065  35.115  20.461  1.00 45.42           O
ANISOU  127  O   ASP A 101     8241   4857   4158   1361   1280   -293       O
ATOM    128  CB  ASP A 101      43.055  34.060  20.532  1.00 45.21           C
ANISOU  128  CB  ASP A 101     7651   5470   4055   1533   2101   -165       C
ATOM    129  CG  ASP A 101      42.054  32.927  20.670  1.00 46.03           C
ANISOU  129  CG  ASP A 101     7475   5861   4154   1424   2355      3       C
ATOM    130  OD1 ASP A 101      41.911  32.138  19.714  1.00 45.07           O
ANISOU  130  OD1 ASP A 101     6994   5828   4303   1295   2240    137       O
ATOM    131  OD2 ASP A 101      41.409  32.827  21.735  1.00 49.28           O
ANISOU  131  OD2 ASP A 101     8029   6413   4282   1461   2660      8       O
ATOM    132  N   TRP A 102      45.095  35.580  18.483  1.00 40.08           N
ANISOU  132  N   TRP A 102     6934   4411   3882   1498   1418   -201       N
ATOM    133  CA  TRP A 102      45.910  36.764  18.256  1.00 40.26           C
ANISOU  133  CA  TRP A 102     7133   4179   3985   1536   1162   -240       C
ATOM    134  C   TRP A 102      45.096  37.784  17.477  1.00 41.12           C
ANISOU  134  C   TRP A 102     7071   4295   4257   1733   1226   -241       C
ATOM    135  O   TRP A 102      44.175  37.432  16.735  1.00 40.57           O
ANISOU  135  O   TRP A 102     6663   4441   4312   1780   1397   -175       O
ATOM    136  CB  TRP A 102      47.213  36.425  17.520  1.00 37.94           C
ANISOU  136  CB  TRP A 102     6718   3841   3855   1299    873   -137       C
ATOM    137  CG  TRP A 102      47.028  35.896  16.136  1.00 37.49           C
ANISOU  137  CG  TRP A 102     6233   4032   3980   1229    915    -27       C
ATOM    138  CD1 TRP A 102      46.394  34.743  15.776  1.00 35.54           C
ANISOU  138  CD1 TRP A 102     5731   4021   3753   1197   1055      2       C
ATOM    139  CD2 TRP A 102      47.508  36.485  14.923  1.00 39.53           C
ANISOU  139  CD2 TRP A 102     6300   4320   4400   1168    782     79       C
ATOM    140  NE1 TRP A 102      46.438  34.585  14.413  1.00 35.36           N
ANISOU  140  NE1 TRP A 102     5399   4161   3876   1155   1010     77       N
ATOM    141  CE2 TRP A 102      47.117  35.641  13.866  1.00 38.06           C
ANISOU  141  CE2 TRP A 102     5774   4406   4279   1130    871    132       C
ATOM    142  CE3 TRP A 102      48.225  37.648  14.627  1.00 42.58           C
ANISOU  142  CE3 TRP A 102     6780   4526   4873   1124    576    155       C
ATOM    143  CZ2 TRP A 102      47.419  35.922  12.536  1.00 39.84           C
ANISOU  143  CZ2 TRP A 102     5781   4765   4591   1063    802    241       C
ATOM    144  CZ3 TRP A 102      48.525  37.924  13.307  1.00 45.30           C
ANISOU  144  CZ3 TRP A 102     6870   5012   5330   1019    514    310       C
ATOM    145  CH2 TRP A 102      48.121  37.066  12.277  1.00 44.45           C
ANISOU  145  CH2 TRP A 102     6453   5213   5224    996    647    342       C
ATOM    146  N   PHE A 103      45.450  39.054  17.656  1.00 46.33           N
ANISOU  146  N   PHE A 103     7982   4677   4946   1842   1025   -309       N
ATOM    147  CA  PHE A 103      44.675  40.174  17.142  1.00 48.07           C
ANISOU  147  CA  PHE A 103     8127   4811   5325   2061   1011   -341       C
ATOM    148  C   PHE A 103      45.571  41.090  16.323  1.00 50.00           C
ANISOU  148  C   PHE A 103     8396   4837   5766   1928    629   -200       C
ATOM    149  O   PHE A 103      46.727  41.329  16.684  1.00 49.75           O
ANISOU  149  O   PHE A 103     8594   4598   5710   1779    367   -169       O
ATOM    150  CB  PHE A 103      44.019  40.945  18.300  1.00 48.58           C
ANISOU  150  CB  PHE A 103     8509   4718   5232   2385   1124   -596       C
ATOM    151  CG  PHE A 103      43.496  42.302  17.919  1.00 50.76           C
ANISOU  151  CG  PHE A 103     8803   4771   5713   2636    965   -679       C
ATOM    152  CD1 PHE A 103      42.432  42.433  17.041  1.00 51.63           C
ANISOU  152  CD1 PHE A 103     8540   5021   6058   2758   1086   -628       C
ATOM    153  CD2 PHE A 103      44.054  43.449  18.463  1.00 53.27           C
ANISOU  153  CD2 PHE A 103     9527   4695   6017   2755    633   -812       C
ATOM    154  CE1 PHE A 103      41.946  43.683  16.699  1.00 53.78           C
ANISOU  154  CE1 PHE A 103     8834   5043   6557   2992    877   -707       C
ATOM    155  CE2 PHE A 103      43.572  44.700  18.127  1.00 55.98           C
ANISOU  155  CE2 PHE A 103     9902   4782   6584   2993    414   -896       C
ATOM    156  CZ  PHE A 103      42.517  44.817  17.244  1.00 56.17           C
ANISOU  156  CZ  PHE A 103     9544   4948   6851   3112    537   -845       C
ATOM    157  N   MET A 104      45.033  41.592  15.215  1.00 45.30           N
ANISOU  157  N   MET A 104     7555   4283   5374   1958    577    -84       N
ATOM    158  CA  MET A 104      45.742  42.500  14.324  1.00 47.23           C
ANISOU  158  CA  MET A 104     7795   4358   5794   1799    226    114       C
ATOM    159  C   MET A 104      45.077  43.869  14.360  1.00 48.58           C
ANISOU  159  C   MET A 104     8114   4223   6120   2040     24     41       C
ATOM    160  O   MET A 104      43.861  43.979  14.169  1.00 49.25           O
ANISOU  160  O   MET A 104     8045   4375   6293   2274    181    -52       O
ATOM    161  CB  MET A 104      45.757  41.965  12.889  1.00 48.53           C
ANISOU  161  CB  MET A 104     7592   4813   6033   1594    265    345       C
ATOM    162  CG  MET A 104      46.583  40.709  12.696  1.00 47.78           C
ANISOU  162  CG  MET A 104     7342   4985   5827   1368    382    399       C
ATOM    163  SD  MET A 104      46.565  40.104  10.995  1.00 49.61           S
ANISOU  163  SD  MET A 104     7196   5575   6081   1189    429    602       S
ATOM    164  CE  MET A 104      44.879  39.519  10.856  1.00 48.45           C
ANISOU  164  CE  MET A 104     6871   5570   5969   1420    659    497       C
ATOM    165  N   LEU A 105      45.877  44.910  14.602  1.00 49.71           N
ANISOU  165  N   LEU A 105     8540   4003   6343   1986   -366     83       N
ATOM    166  CA  LEU A 105      45.342  46.267  14.578  1.00 53.19           C
ANISOU  166  CA  LEU A 105     9144   4086   6979   2208   -668     15       C
ATOM    167  C   LEU A 105      45.091  46.734  13.149  1.00 53.32           C
ANISOU  167  C   LEU A 105     8906   4132   7222   2055   -862    306       C
ATOM    168  O   LEU A 105      44.050  47.337  12.860  1.00 55.41           O
ANISOU  168  O   LEU A 105     9111   4280   7662   2292   -930    228       O
ATOM    169  CB  LEU A 105      46.296  47.221  15.296  1.00 55.59           C
ANISOU  169  CB  LEU A 105     9861   3941   7322   2179  -1109    -14       C
ATOM    170  CG  LEU A 105      45.919  48.703  15.237  1.00 59.69           C
ANISOU  170  CG  LEU A 105    10589   4001   8088   2383  -1558    -69       C
ATOM    171  CD1 LEU A 105      44.568  48.945  15.896  1.00 62.23           C
ANISOU  171  CD1 LEU A 105    10937   4329   8378   2854  -1321   -470       C
ATOM    172  CD2 LEU A 105      46.997  49.560  15.879  1.00 62.09           C
ANISOU  172  CD2 LEU A 105    11173   3993   8425   2204  -1999    -51       C
ATOM    173  N   MET A 106      46.035  46.464  12.242  1.00 51.59           N
ANISOU  173  N   MET A 106     8532   4075   6995   1662   -956    639       N
ATOM    174  CA  MET A 106      45.931  46.821  10.828  1.00 52.00           C
ANISOU  174  CA  MET A 106     8375   4215   7167   1450  -1124    964       C
ATOM    175  C   MET A 106      46.093  45.542  10.015  1.00 48.82           C
ANISOU  175  C   MET A 106     7653   4311   6586   1248   -782   1085       C
ATOM    176  O   MET A 106      47.191  45.239   9.523  1.00 47.94           O
ANISOU  176  O   MET A 106     7448   4379   6387    932   -795   1305       O
ATOM    177  CB  MET A 106      46.976  47.865  10.441  1.00 54.24           C
ANISOU  177  CB  MET A 106     8796   4228   7585   1148  -1594   1284       C
ATOM    178  CG  MET A 106      46.876  49.161  11.230  1.00 57.85           C
ANISOU  178  CG  MET A 106     9610   4123   8249   1350  -2038   1156       C
ATOM    179  SD  MET A 106      45.482  50.181  10.718  1.00 61.11           S
ANISOU  179  SD  MET A 106    10038   4252   8929   1634  -2314   1100       S
ATOM    180  CE  MET A 106      46.104  50.849   9.177  1.00 62.65           C
ANISOU  180  CE  MET A 106    10125   4438   9242   1126  -2731   1700       C
ATOM    181  N   PRO A 107      45.022  44.763   9.857  1.00 50.84           N
ANISOU  181  N   PRO A 107     7720   4794   6802   1435   -487    937       N
ATOM    182  CA  PRO A 107      45.146  43.457   9.194  1.00 50.49           C
ANISOU  182  CA  PRO A 107     7412   5181   6591   1287   -205    994       C
ATOM    183  C   PRO A 107      45.428  43.608   7.706  1.00 51.75           C
ANISOU  183  C   PRO A 107     7428   5522   6712   1022   -342   1308       C
ATOM    184  O   PRO A 107      44.790  44.405   7.014  1.00 53.20           O
ANISOU  184  O   PRO A 107     7626   5568   7019   1036   -570   1450       O
ATOM    185  CB  PRO A 107      43.781  42.800   9.440  1.00 50.13           C
ANISOU  185  CB  PRO A 107     7221   5240   6585   1563     51    787       C
ATOM    186  CG  PRO A 107      43.156  43.589  10.553  1.00 49.75           C
ANISOU  186  CG  PRO A 107     7363   4883   6658   1870     24    560       C
ATOM    187  CD  PRO A 107      43.668  44.983  10.388  1.00 51.00           C
ANISOU  187  CD  PRO A 107     7745   4685   6949   1810   -393    686       C
ATOM    188  N   LYS A 108      46.393  42.830   7.221  1.00 53.80           N
ANISOU  188  N   LYS A 108     7557   6098   6788    788   -207   1407       N
ATOM    189  CA  LYS A 108      46.706  42.743   5.800  1.00 54.26           C
ANISOU  189  CA  LYS A 108     7470   6443   6702    546   -236   1670       C
ATOM    190  C   LYS A 108      46.739  41.273   5.417  1.00 52.77           C
ANISOU  190  C   LYS A 108     7078   6650   6323    564     58   1526       C
ATOM    191  O   LYS A 108      47.490  40.494   6.011  1.00 51.40           O
ANISOU  191  O   LYS A 108     6848   6585   6096    552    219   1380       O
ATOM    192  CB  LYS A 108      48.045  43.413   5.477  1.00 54.63           C
ANISOU  192  CB  LYS A 108     7538   6508   6712    222   -386   1959       C
ATOM    193  CG  LYS A 108      48.460  43.290   4.017  1.00 54.45           C
ANISOU  193  CG  LYS A 108     7362   6868   6459    -48   -344   2243       C
ATOM    194  CD  LYS A 108      49.734  44.071   3.736  1.00 54.82           C
ANISOU  194  CD  LYS A 108     7389   6939   6502   -399   -484   2590       C
ATOM    195  CE  LYS A 108      50.195  43.902   2.292  1.00 54.53           C
ANISOU  195  CE  LYS A 108     7189   7372   6160   -677   -362   2878       C
ATOM    196  NZ  LYS A 108      51.431  44.686   1.999  1.00 55.86           N
ANISOU  196  NZ  LYS A 108     7280   7606   6336  -1061   -468   3278       N
ATOM    197  N   GLN A 109      45.927  40.895   4.435  1.00 46.99           N
ANISOU  197  N   GLN A 109     6252   6091   5509    600     69   1560       N
ATOM    198  CA  GLN A 109      45.825  39.512   3.993  1.00 45.45           C
ANISOU  198  CA  GLN A 109     5894   6221   5152    647    268   1405       C
ATOM    199  C   GLN A 109      46.127  39.420   2.506  1.00 45.18           C
ANISOU  199  C   GLN A 109     5808   6506   4853    469    238   1590       C
ATOM    200  O   GLN A 109      45.549  40.159   1.703  1.00 46.80           O
ANISOU  200  O   GLN A 109     6095   6645   5041    405     40   1799       O
ATOM    201  CB  GLN A 109      44.437  38.936   4.281  1.00 46.22           C
ANISOU  201  CB  GLN A 109     5936   6227   5399    891    298   1231       C
ATOM    202  CG  GLN A 109      44.191  37.585   3.630  1.00 44.83           C
ANISOU  202  CG  GLN A 109     5615   6328   5089    925    384   1114       C
ATOM    203  CD  GLN A 109      42.802  37.048   3.903  1.00 45.62           C
ANISOU  203  CD  GLN A 109     5621   6318   5395   1122    374   1005       C
ATOM    204  OE1 GLN A 109      42.218  37.316   4.952  1.00 45.20           O
ANISOU  204  OE1 GLN A 109     5567   6057   5552   1260    441    931       O
ATOM    205  NE2 GLN A 109      42.263  36.290   2.956  1.00 45.78           N
ANISOU  205  NE2 GLN A 109     5557   6485   5352   1137    286    998       N
ATOM    206  N   LYS A 110      47.034  38.517   2.147  1.00 42.22           N
ANISOU  206  N   LYS A 110     5307   6474   4260    399    422   1501       N
ATOM    207  CA  LYS A 110      47.310  38.177   0.761  1.00 44.19           C
ANISOU  207  CA  LYS A 110     5507   7106   4177    287    466   1590       C
ATOM    208  C   LYS A 110      47.207  36.667   0.600  1.00 42.80           C
ANISOU  208  C   LYS A 110     5216   7152   3895    463    596   1272       C
ATOM    209  O   LYS A 110      47.116  35.921   1.578  1.00 40.40           O
ANISOU  209  O   LYS A 110     4851   6717   3781    611    651   1036       O
ATOM    210  CB  LYS A 110      48.686  38.688   0.315  1.00 46.54           C
ANISOU  210  CB  LYS A 110     5736   7661   4285     20    568   1809       C
ATOM    211  CG  LYS A 110      48.744  40.195   0.125  1.00 48.95           C
ANISOU  211  CG  LYS A 110     6176   7769   4655   -215    351   2204       C
ATOM    212  CD  LYS A 110      49.962  40.610  -0.683  1.00 52.36           C
ANISOU  212  CD  LYS A 110     6506   8560   4827   -536    459   2504       C
ATOM    213  CE  LYS A 110      49.895  42.082  -1.067  1.00 55.44           C
ANISOU  213  CE  LYS A 110     7055   8749   5262   -816    167   2961       C
ATOM    214  NZ  LYS A 110      50.972  42.459  -2.027  1.00 59.60           N
ANISOU  214  NZ  LYS A 110     7470   9697   5479  -1181    290   3329       N
ATOM    215  N   VAL A 111      47.216  36.217  -0.653  1.00 44.78           N
ANISOU  215  N   VAL A 111     5466   7727   3823    443    610   1269       N
ATOM    216  CA  VAL A 111      46.984  34.817  -0.987  1.00 44.21           C
ANISOU  216  CA  VAL A 111     5330   7825   3642    633    637    958       C
ATOM    217  C   VAL A 111      48.051  34.356  -1.972  1.00 46.86           C
ANISOU  217  C   VAL A 111     5590   8638   3576    585    819    880       C
ATOM    218  O   VAL A 111      48.249  34.981  -3.020  1.00 50.01           O
ANISOU  218  O   VAL A 111     6072   9283   3646    424    842   1107       O
ATOM    219  CB  VAL A 111      45.576  34.603  -1.573  1.00 44.56           C
ANISOU  219  CB  VAL A 111     5488   7731   3710    742    394    963       C
ATOM    220  CG1 VAL A 111      45.460  33.224  -2.179  1.00 45.01           C
ANISOU  220  CG1 VAL A 111     5522   7985   3597    908    353    671       C
ATOM    221  CG2 VAL A 111      44.520  34.797  -0.494  1.00 42.25           C
ANISOU  221  CG2 VAL A 111     5177   7025   3853    847    285    965       C
ATOM    222  N   ALA A 112      48.732  33.262  -1.635  1.00 46.08           N
ANISOU  222  N   ALA A 112     5333   8676   3499    727    943    558       N
ATOM    223  CA  ALA A 112      49.713  32.620  -2.508  1.00 48.97           C
ANISOU  223  CA  ALA A 112     5581   9512   3515    771   1137    374       C
ATOM    224  C   ALA A 112      49.244  31.187  -2.745  1.00 48.64           C
ANISOU  224  C   ALA A 112     5554   9479   3446   1053   1000    -26       C
ATOM    225  O   ALA A 112      49.520  30.293  -1.939  1.00 46.78           O
ANISOU  225  O   ALA A 112     5195   9112   3469   1195    967   -298       O
ATOM    226  CB  ALA A 112      51.112  32.665  -1.896  1.00 49.19           C
ANISOU  226  CB  ALA A 112     5359   9671   3659    699   1365    335       C
ATOM    227  N   GLY A 113      48.535  30.970  -3.848  1.00 39.53           N
ANISOU  227  N   GLY A 113     5494   6421   3105    531   -263    810       N
ATOM    228  CA  GLY A 113      47.922  29.682  -4.096  1.00 38.76           C
ANISOU  228  CA  GLY A 113     5330   6477   2919    555   -346    574       C
ATOM    229  C   GLY A 113      46.698  29.484  -3.226  1.00 39.29           C
ANISOU  229  C   GLY A 113     5189   6403   3337    652   -461    454       C
ATOM    230  O   GLY A 113      45.755  30.278  -3.282  1.00 41.00           O
ANISOU  230  O   GLY A 113     5316   6532   3731    755   -667    588       O
ATOM    231  N   SER A 114      46.696  28.426  -2.418  1.00 37.00           N
ANISOU  231  N   SER A 114     4816   6091   3152    624   -329    203       N
ATOM    232  CA  SER A 114      45.666  28.218  -1.411  1.00 37.53           C
ANISOU  232  CA  SER A 114     4680   6048   3532    650   -346     82       C
ATOM    233  C   SER A 114      46.165  28.537  -0.007  1.00 36.03           C
ANISOU  233  C   SER A 114     4451   5689   3550    667   -118     42       C
ATOM    234  O   SER A 114      45.503  28.187   0.975  1.00 36.54           O
ANISOU  234  O   SER A 114     4381   5695   3809    645    -51    -88       O
ATOM    235  CB  SER A 114      45.139  26.783  -1.481  1.00 37.87           C
ANISOU  235  CB  SER A 114     4698   6166   3525    542   -380   -144       C
ATOM    236  OG  SER A 114      46.195  25.840  -1.431  1.00 35.37           O
ANISOU  236  OG  SER A 114     4562   5837   3040    495   -222   -267       O
ATOM    237  N   LEU A 115      47.316  29.197   0.104  1.00 36.85           N
ANISOU  237  N   LEU A 115     4666   5742   3592    672      6    145       N
ATOM    238  CA  LEU A 115      47.853  29.626   1.386  1.00 35.24           C
ANISOU  238  CA  LEU A 115     4435   5400   3555    675    181    101       C
ATOM    239  C   LEU A 115      47.431  31.060   1.673  1.00 37.62           C
ANISOU  239  C   LEU A 115     4685   5531   4080    753    135    214       C
ATOM    240  O   LEU A 115      47.473  31.921   0.790  1.00 39.31           O
ANISOU  240  O   LEU A 115     4981   5702   4254    780     12    414       O
ATOM    241  CB  LEU A 115      49.378  29.521   1.393  1.00 32.20           C
ANISOU  241  CB  LEU A 115     4155   5072   3006    620    324    107       C
ATOM    242  CG  LEU A 115      49.972  28.131   1.159  1.00 29.19           C
ANISOU  242  CG  LEU A 115     3831   4820   2441    613    373    -40       C
ATOM    243  CD1 LEU A 115      51.474  28.224   0.942  1.00 27.97           C
ANISOU  243  CD1 LEU A 115     3700   4785   2144    597    500    -40       C
ATOM    244  CD2 LEU A 115      49.656  27.213   2.327  1.00 26.38           C
ANISOU  244  CD2 LEU A 115     3462   4363   2198    620    415   -188       C
ATOM    245  N   CYS A 116      47.025  31.311   2.914  1.00 34.86           N
ANISOU  245  N   CYS A 116     4227   5067   3950    787    235     83       N
ATOM    246  CA  CYS A 116      46.592  32.633   3.348  1.00 35.56           C
ANISOU  246  CA  CYS A 116     4263   4953   4295    897    212    107       C
ATOM    247  C   CYS A 116      47.692  33.272   4.185  1.00 34.79           C
ANISOU  247  C   CYS A 116     4274   4728   4218    821    368     76       C
ATOM    248  O   CYS A 116      48.104  32.715   5.208  1.00 31.40           O
ANISOU  248  O   CYS A 116     3833   4359   3739    747    518    -82       O
ATOM    249  CB  CYS A 116      45.294  32.547   4.147  1.00 34.32           C
ANISOU  249  CB  CYS A 116     3872   4798   4369    991    240    -84       C
ATOM    250  SG  CYS A 116      44.679  34.142   4.711  1.00 35.89           S
ANISOU  250  SG  CYS A 116     3979   4729   4929   1204    221   -141       S
ATOM    251  N   ILE A 117      48.161  34.437   3.751  1.00 34.19           N
ANISOU  251  N   ILE A 117     4320   4468   4203    817    310    237       N
ATOM    252  CA  ILE A 117      49.211  35.177   4.438  1.00 35.24           C
ANISOU  252  CA  ILE A 117     4551   4464   4375    697    430    204       C
ATOM    253  C   ILE A 117      48.563  36.348   5.159  1.00 35.81           C
ANISOU  253  C   ILE A 117     4617   4230   4760    820    415    104       C
ATOM    254  O   ILE A 117      47.948  37.212   4.523  1.00 38.26           O
ANISOU  254  O   ILE A 117     4979   4316   5242    955    256    248       O
ATOM    255  CB  ILE A 117      50.289  35.662   3.457  1.00 39.87           C
ANISOU  255  CB  ILE A 117     5294   5045   4809    531    410    441       C
ATOM    256  CG1 ILE A 117      50.646  34.549   2.469  1.00 38.98           C
ANISOU  256  CG1 ILE A 117     5172   5246   4392    479    409    517       C
ATOM    257  CG2 ILE A 117      51.526  36.126   4.210  1.00 42.11           C
ANISOU  257  CG2 ILE A 117     5612   5286   5102    340    549    359       C
ATOM    258  CD1 ILE A 117      51.234  35.055   1.173  1.00 40.41           C
ANISOU  258  CD1 ILE A 117     5505   5467   4382    343    372    787       C
ATOM    259  N   ARG A 118      48.694  36.379   6.482  1.00 44.58           N
ANISOU  259  N   ARG A 118     5681   5325   5933    791    565   -152       N
ATOM    260  CA  ARG A 118      48.127  37.440   7.302  1.00 44.83           C
ANISOU  260  CA  ARG A 118     5705   5083   6244    913    595   -340       C
ATOM    261  C   ARG A 118      49.214  38.028   8.188  1.00 45.85           C
ANISOU  261  C   ARG A 118     5963   5103   6356    728    700   -474       C
ATOM    262  O   ARG A 118      50.050  37.298   8.730  1.00 44.50           O
ANISOU  262  O   ARG A 118     5782   5168   5959    563    789   -543       O
ATOM    263  CB  ARG A 118      46.965  36.920   8.158  1.00 41.34           C
ANISOU  263  CB  ARG A 118     5048   4781   5877   1053    703   -602       C
ATOM    264  CG  ARG A 118      45.830  36.324   7.342  1.00 41.07           C
ANISOU  264  CG  ARG A 118     4828   4888   5889   1202    587   -513       C
ATOM    265  CD  ARG A 118      44.910  35.448   8.184  1.00 38.17           C
ANISOU  265  CD  ARG A 118     4230   4768   5503   1204    749   -752       C
ATOM    266  NE  ARG A 118      43.816  36.202   8.790  1.00 38.92           N
ANISOU  266  NE  ARG A 118     4118   4775   5896   1416    816  -1002       N
ATOM    267  CZ  ARG A 118      42.677  36.491   8.169  1.00 41.04           C
ANISOU  267  CZ  ARG A 118     4149   5026   6417   1656    668  -1000       C
ATOM    268  NH1 ARG A 118      42.487  36.096   6.917  1.00 41.86           N
ANISOU  268  NH1 ARG A 118     4237   5199   6471   1680    426   -741       N
ATOM    269  NH2 ARG A 118      41.730  37.177   8.795  1.00 44.33           N
ANISOU  269  NH2 ARG A 118     4332   5380   7131   1885    752  -1281       N
ATOM    270  N   MET A 119      49.202  39.352   8.328  1.00 41.56           N
ANISOU  270  N   MET A 119     5546   4182   6063    762    658   -518       N
ATOM    271  CA  MET A 119      50.179  40.043   9.154  1.00 42.97           C
ANISOU  271  CA  MET A 119     5853   4217   6255    555    731   -681       C
ATOM    272  C   MET A 119      49.583  41.361   9.626  1.00 44.49           C
ANISOU  272  C   MET A 119     6151   3961   6792    706    710   -879       C
ATOM    273  O   MET A 119      48.689  41.920   8.985  1.00 46.17           O
ANISOU  273  O   MET A 119     6381   3907   7255    956    585   -771       O
ATOM    274  CB  MET A 119      51.485  40.296   8.394  1.00 46.71           C
ANISOU  274  CB  MET A 119     6455   4676   6618    268    682   -427       C
ATOM    275  CG  MET A 119      51.392  41.434   7.394  1.00 50.03           C
ANISOU  275  CG  MET A 119     7084   4684   7242    259    547   -157       C
ATOM    276  SD  MET A 119      52.945  41.788   6.556  1.00 53.83           S
ANISOU  276  SD  MET A 119     7704   5188   7562   -176    561    134       S
ATOM    277  CE  MET A 119      52.567  43.374   5.817  1.00 55.97           C
ANISOU  277  CE  MET A 119     8324   4804   8138   -178    397    402       C
ATOM    278  N   ASP A 120      50.089  41.852  10.753  1.00 44.78           N
ANISOU  278  N   ASP A 120     6263   3911   6842    571    810  -1186       N
ATOM    279  CA  ASP A 120      49.641  43.117  11.323  1.00 48.80           C
ANISOU  279  CA  ASP A 120     6901   3963   7677    702    810  -1459       C
ATOM    280  C   ASP A 120      50.586  44.216  10.853  1.00 51.54           C
ANISOU  280  C   ASP A 120     7527   3884   8172    456    693  -1299       C
ATOM    281  O   ASP A 120      51.774  44.210  11.190  1.00 51.29           O
ANISOU  281  O   ASP A 120     7551   3966   7972    101    729  -1332       O
ATOM    282  CB  ASP A 120      49.594  43.033  12.848  1.00 49.33           C
ANISOU  282  CB  ASP A 120     6920   4189   7635    670    994  -1933       C
ATOM    283  CG  ASP A 120      48.924  44.239  13.482  1.00 54.14           C
ANISOU  283  CG  ASP A 120     7627   4360   8583    879   1032  -2310       C
ATOM    284  OD1 ASP A 120      48.460  45.130  12.739  1.00 57.12           O
ANISOU  284  OD1 ASP A 120     8111   4268   9324   1087    887  -2184       O
ATOM    285  OD2 ASP A 120      48.857  44.295  14.728  1.00 55.43           O
ANISOU  285  OD2 ASP A 120     7779   4642   8638    848   1199  -2741       O
ATOM    286  N   GLN A 121      50.059  45.160  10.070  1.00 54.97           N
ANISOU  286  N   GLN A 121     8134   3826   8927    633    538  -1112       N
ATOM    287  CA  GLN A 121      50.876  46.255   9.559  1.00 58.44           C
ANISOU  287  CA  GLN A 121     8897   3788   9521    364    425   -907       C
ATOM    288  C   GLN A 121      51.297  47.236  10.643  1.00 62.00           C
ANISOU  288  C   GLN A 121     9527   3870  10160    212    480  -1313       C
ATOM    289  O   GLN A 121      52.187  48.057  10.398  1.00 64.89           O
ANISOU  289  O   GLN A 121    10151   3888  10617   -138    419  -1192       O
ATOM    290  CB  GLN A 121      50.125  47.007   8.458  1.00 61.97           C
ANISOU  290  CB  GLN A 121     9541   3752  10253    623    202   -564       C
ATOM    291  CG  GLN A 121      49.710  46.147   7.276  1.00 59.36           C
ANISOU  291  CG  GLN A 121     9076   3763   9716    747    102   -155       C
ATOM    292  CD  GLN A 121      49.022  46.950   6.190  1.00 63.65           C
ANISOU  292  CD  GLN A 121     9853   3829  10501    992   -179    216       C
ATOM    293  OE1 GLN A 121      47.909  46.630   5.774  1.00 63.73           O
ANISOU  293  OE1 GLN A 121     9694   3931  10590   1390   -319    275       O
ATOM    294  NE2 GLN A 121      49.686  48.002   5.722  1.00 67.77           N
ANISOU  294  NE2 GLN A 121    10771   3839  11139    736   -282    482       N
ATOM    295  N   ALA A 122      50.689  47.174  11.824  1.00 62.35           N
ANISOU  295  N   ALA A 122     9450   3994  10246    428    605  -1804       N
ATOM    296  CA  ALA A 122      51.006  48.086  12.915  1.00 66.20           C
ANISOU  296  CA  ALA A 122    10118   4155  10881    305    661  -2268       C
ATOM    297  C   ALA A 122      52.226  47.656  13.721  1.00 64.37           C
ANISOU  297  C   ALA A 122     9835   4322  10300   -143    749  -2447       C
ATOM    298  O   ALA A 122      52.526  48.285  14.742  1.00 67.47           O
ANISOU  298  O   ALA A 122    10355   4546  10734   -281    792  -2884       O
ATOM    299  CB  ALA A 122      49.795  48.232  13.840  1.00 68.21           C
ANISOU  299  CB  ALA A 122    10258   4366  11294    737    784  -2763       C
ATOM    300  N   ILE A 123      52.925  46.610  13.299  1.00 59.96           N
ANISOU  300  N   ILE A 123     9089   4289   9405   -350    757  -2148       N
ATOM    301  CA  ILE A 123      54.117  46.138  13.992  1.00 58.61           C
ANISOU  301  CA  ILE A 123     8821   4530   8918   -726    787  -2284       C
ATOM    302  C   ILE A 123      55.338  46.773  13.341  1.00 60.70           C
ANISOU  302  C   ILE A 123     9202   4601   9259  -1176    694  -2053       C
ATOM    303  O   ILE A 123      55.453  46.796  12.110  1.00 60.29           O
ANISOU  303  O   ILE A 123     9185   4456   9267  -1226    650  -1612       O
ATOM    304  CB  ILE A 123      54.205  44.604  13.955  1.00 53.39           C
ANISOU  304  CB  ILE A 123     7876   4534   7878   -658    839  -2125       C
ATOM    305  CG1 ILE A 123      52.869  43.981  14.368  1.00 51.80           C
ANISOU  305  CG1 ILE A 123     7564   4486   7630   -257    949  -2267       C
ATOM    306  CG2 ILE A 123      55.324  44.113  14.859  1.00 52.79           C
ANISOU  306  CG2 ILE A 123     7694   4876   7488   -953    825  -2315       C
ATOM    307  CD1 ILE A 123      52.432  44.340  15.771  1.00 54.36           C
ANISOU  307  CD1 ILE A 123     7946   4789   7922   -190   1064  -2786       C
ATOM    308  N   MET A 124      56.250  47.290  14.162  1.00 63.43           N
ANISOU  308  N   MET A 124     9605   4916   9579  -1537    670  -2357       N
ATOM    309  CA  MET A 124      57.404  48.013  13.650  1.00 66.51           C
ANISOU  309  CA  MET A 124    10089   5103  10078  -2037    602  -2195       C
ATOM    310  C   MET A 124      58.554  47.933  14.641  1.00 67.70           C
ANISOU  310  C   MET A 124    10093   5597  10031  -2428    564  -2529       C
ATOM    311  O   MET A 124      58.341  47.963  15.855  1.00 68.60           O
ANISOU  311  O   MET A 124    10235   5782  10047  -2347    558  -2980       O
ATOM    312  CB  MET A 124      57.055  49.480  13.371  1.00 72.06           C
ANISOU  312  CB  MET A 124    11195   4972  11211  -2096    541  -2208       C
ATOM    313  CG  MET A 124      56.092  50.079  14.381  1.00 74.69           C
ANISOU  313  CG  MET A 124    11711   4923  11744  -1765    552  -2704       C
ATOM    314  SD  MET A 124      55.811  51.842  14.137  1.00 82.35           S
ANISOU  314  SD  MET A 124    13164   4904  13220  -1787    401  -2727       S
ATOM    315  CE  MET A 124      57.343  52.517  14.765  1.00 86.52           C
ANISOU  315  CE  MET A 124    13732   5472  13669  -2462    299  -2919       C
ATOM    316  N   ASP A 125      59.771  47.830  14.103  1.00 68.19           N
ANISOU  316  N   ASP A 125     9981   5910  10018  -2855    537  -2314       N
ATOM    317  CA  ASP A 125      61.015  47.916  14.869  1.00 70.56           C
ANISOU  317  CA  ASP A 125    10100   6515  10193  -3299    454  -2597       C
ATOM    318  C   ASP A 125      61.060  46.882  15.995  1.00 67.77           C
ANISOU  318  C   ASP A 125     9516   6754   9482  -3085    397  -2886       C
ATOM    319  O   ASP A 125      61.107  47.212  17.182  1.00 70.22           O
ANISOU  319  O   ASP A 125     9916   7052   9712  -3158    320  -3329       O
ATOM    320  CB  ASP A 125      61.224  49.331  15.417  1.00 76.73           C
ANISOU  320  CB  ASP A 125    11196   6702  11256  -3654    388  -2930       C
ATOM    321  CG  ASP A 125      61.122  50.390  14.342  1.00 80.29           C
ANISOU  321  CG  ASP A 125    11963   6472  12070  -3864    419  -2605       C
ATOM    322  OD1 ASP A 125      60.155  51.178  14.374  1.00 82.52           O
ANISOU  322  OD1 ASP A 125    12602   6134  12618  -3573    390  -2654       O
ATOM    323  OD2 ASP A 125      61.999  50.427  13.455  1.00 81.31           O
ANISOU  323  OD2 ASP A 125    11966   6731  12197  -4270    454  -2262       O
ATOM    324  N   LYS A 126      61.050  45.613  15.597  1.00 64.65           N
ANISOU  324  N   LYS A 126     8854   6862   8847  -2831    426  -2624       N
ATOM    325  CA  LYS A 126      61.242  44.528  16.548  1.00 62.62           C
ANISOU  325  CA  LYS A 126     8394   7168   8232  -2660    339  -2799       C
ATOM    326  C   LYS A 126      61.752  43.304  15.807  1.00 61.41           C
ANISOU  326  C   LYS A 126     7910   7512   7909  -2541    336  -2464       C
ATOM    327  O   LYS A 126      61.640  43.203  14.582  1.00 61.82           O
ANISOU  327  O   LYS A 126     7927   7483   8080  -2502    445  -2119       O
ATOM    328  CB  LYS A 126      59.957  44.205  17.319  1.00 60.65           C
ANISOU  328  CB  LYS A 126     8340   6849   7856  -2254    411  -2979       C
ATOM    329  CG  LYS A 126      58.666  44.485  16.573  1.00 59.76           C
ANISOU  329  CG  LYS A 126     8415   6306   7986  -1942    566  -2801       C
ATOM    330  CD  LYS A 126      57.701  45.250  17.467  1.00 60.40           C
ANISOU  330  CD  LYS A 126     8757   6022   8169  -1790    636  -3202       C
ATOM    331  CE  LYS A 126      57.580  44.602  18.840  1.00 60.23           C
ANISOU  331  CE  LYS A 126     8709   6419   7758  -1713    637  -3538       C
ATOM    332  NZ  LYS A 126      56.808  45.447  19.794  1.00 63.96           N
ANISOU  332  NZ  LYS A 126     9418   6594   8291  -1620    730  -3998       N
ATOM    333  N   ASN A 127      62.326  42.382  16.572  1.00 61.05           N
ANISOU  333  N   ASN A 127     7646   7977   7574  -2474    191  -2581       N
ATOM    334  CA  ASN A 127      62.882  41.149  16.032  1.00 60.35           C
ANISOU  334  CA  ASN A 127     7239   8359   7332  -2309    152  -2336       C
ATOM    335  C   ASN A 127      61.784  40.095  15.975  1.00 58.10           C
ANISOU  335  C   ASN A 127     7075   8108   6893  -1852    226  -2173       C
ATOM    336  O   ASN A 127      61.177  39.766  17.001  1.00 56.26           O
ANISOU  336  O   ASN A 127     7004   7912   6461  -1685    185  -2338       O
ATOM    337  CB  ASN A 127      64.055  40.673  16.887  1.00 60.46           C
ANISOU  337  CB  ASN A 127     6962   8869   7141  -2423    -95  -2530       C
ATOM    338  CG  ASN A 127      65.099  41.753  17.092  1.00 62.46           C
ANISOU  338  CG  ASN A 127     7075   9111   7546  -2930   -188  -2756       C
ATOM    339  OD1 ASN A 127      66.034  41.888  16.302  1.00 63.52           O
ANISOU  339  OD1 ASN A 127     6894   9418   7822  -3185   -157  -2645       O
ATOM    340  ND2 ASN A 127      64.939  42.535  18.153  1.00 64.14           N
ANISOU  340  ND2 ASN A 127     7516   9131   7722  -3109   -284  -3100       N
ATOM    341  N   ILE A 128      61.528  39.572  14.780  1.00 53.21           N
ANISOU  341  N   ILE A 128     6384   7490   6342  -1690    345  -1861       N
ATOM    342  CA  ILE A 128      60.456  38.614  14.549  1.00 50.98           C
ANISOU  342  CA  ILE A 128     6208   7203   5958  -1311    421  -1698       C
ATOM    343  C   ILE A 128      61.060  37.312  14.044  1.00 50.43           C
ANISOU  343  C   ILE A 128     5894   7523   5745  -1138    363  -1524       C
ATOM    344  O   ILE A 128      61.947  37.319  13.183  1.00 51.93           O
ANISOU  344  O   ILE A 128     5846   7876   6007  -1265    386  -1421       O
ATOM    345  CB  ILE A 128      59.415  39.162  13.551  1.00 51.47           C
ANISOU  345  CB  ILE A 128     6450   6871   6236  -1231    584  -1512       C
ATOM    346  CG1 ILE A 128      58.891  40.520  14.024  1.00 52.08           C
ANISOU  346  CG1 ILE A 128     6767   6503   6517  -1360    618  -1709       C
ATOM    347  CG2 ILE A 128      58.268  38.184  13.387  1.00 48.09           C
ANISOU  347  CG2 ILE A 128     6092   6468   5710   -879    645  -1389       C
ATOM    348  CD1 ILE A 128      57.852  41.129  13.109  1.00 52.57           C
ANISOU  348  CD1 ILE A 128     7012   6142   6822  -1230    717  -1526       C
ATOM    349  N   ILE A 129      60.579  36.196  14.586  1.00 50.55           N
ANISOU  349  N   ILE A 129     5975   7675   5555   -858    303  -1505       N
ATOM    350  CA  ILE A 129      61.024  34.864  14.194  1.00 49.01           C
ANISOU  350  CA  ILE A 129     5615   7765   5242   -629    225  -1362       C
ATOM    351  C   ILE A 129      59.864  34.144  13.523  1.00 44.57           C
ANISOU  351  C   ILE A 129     5210   7048   4675   -390    355  -1175       C
ATOM    352  O   ILE A 129      58.719  34.220  13.985  1.00 41.95           O
ANISOU  352  O   ILE A 129     5104   6522   4315   -329    429  -1198       O
ATOM    353  CB  ILE A 129      61.553  34.067  15.404  1.00 48.18           C
ANISOU  353  CB  ILE A 129     5489   7923   4894   -519    -16  -1464       C
ATOM    354  CG1 ILE A 129      61.948  32.647  14.990  1.00 47.00           C
ANISOU  354  CG1 ILE A 129     5213   7978   4667   -220   -120  -1315       C
ATOM    355  CG2 ILE A 129      60.530  34.043  16.532  1.00 45.49           C
ANISOU  355  CG2 ILE A 129     5472   7447   4365   -484     -5  -1545       C
ATOM    356  CD1 ILE A 129      63.140  32.595  14.064  1.00 49.43           C
ANISOU  356  CD1 ILE A 129     5133   8532   5118   -237   -132  -1315       C
ATOM    357  N   LEU A 130      60.156  33.464  12.417  1.00 46.44           N
ANISOU  357  N   LEU A 130     5307   7397   4942   -270    393  -1024       N
ATOM    358  CA  LEU A 130      59.163  32.684  11.686  1.00 41.57           C
ANISOU  358  CA  LEU A 130     4817   6669   4310    -65    482   -869       C
ATOM    359  C   LEU A 130      59.294  31.226  12.111  1.00 38.99           C
ANISOU  359  C   LEU A 130     4511   6482   3820    181    351   -850       C
ATOM    360  O   LEU A 130      60.283  30.562  11.781  1.00 39.83           O
ANISOU  360  O   LEU A 130     4424   6803   3907    298    260   -858       O
ATOM    361  CB  LEU A 130      59.347  32.833  10.178  1.00 41.49           C
ANISOU  361  CB  LEU A 130     4697   6680   4388    -98    603   -735       C
ATOM    362  CG  LEU A 130      59.268  34.242   9.589  1.00 45.93           C
ANISOU  362  CG  LEU A 130     5293   7058   5102   -353    712   -674       C
ATOM    363  CD1 LEU A 130      59.349  34.184   8.074  1.00 45.62           C
ANISOU  363  CD1 LEU A 130     5205   7077   5053   -376    826   -493       C
ATOM    364  CD2 LEU A 130      57.997  34.939  10.030  1.00 46.90           C
ANISOU  364  CD2 LEU A 130     5656   6838   5325   -340    738   -685       C
ATOM    365  N   LYS A 131      58.302  30.733  12.845  1.00 38.65           N
ANISOU  365  N   LYS A 131     4704   6311   3670    257    345   -831       N
ATOM    366  CA  LYS A 131      58.258  29.348  13.291  1.00 37.76           C
ANISOU  366  CA  LYS A 131     4711   6238   3398    452    219   -763       C
ATOM    367  C   LYS A 131      57.134  28.621  12.567  1.00 34.44           C
ANISOU  367  C   LYS A 131     4429   5650   3008    542    332   -648       C
ATOM    368  O   LYS A 131      56.036  29.163  12.404  1.00 32.71           O
ANISOU  368  O   LYS A 131     4279   5291   2857    447    483   -643       O
ATOM    369  CB  LYS A 131      58.066  29.270  14.808  1.00 39.05           C
ANISOU  369  CB  LYS A 131     5069   6418   3350    396    121   -813       C
ATOM    370  CG  LYS A 131      59.271  29.780  15.592  1.00 42.72           C
ANISOU  370  CG  LYS A 131     5399   7092   3740    322    -69   -942       C
ATOM    371  CD  LYS A 131      58.900  30.249  16.992  1.00 43.18           C
ANISOU  371  CD  LYS A 131     5663   7163   3579    167    -95  -1055       C
ATOM    372  CE  LYS A 131      58.523  29.094  17.898  1.00 42.97           C
ANISOU  372  CE  LYS A 131     5921   7149   3255    266   -209   -924       C
ATOM    373  NZ  LYS A 131      58.262  29.564  19.288  1.00 43.73           N
ANISOU  373  NZ  LYS A 131     6224   7332   3059     87   -223  -1050       N
ATOM    374  N   ALA A 132      57.411  27.395  12.126  1.00 38.09           N
ANISOU  374  N   ALA A 132     4914   6121   3437    734    242   -581       N
ATOM    375  CA  ALA A 132      56.483  26.671  11.272  1.00 35.78           C
ANISOU  375  CA  ALA A 132     4730   5682   3184    794    327   -507       C
ATOM    376  C   ALA A 132      56.467  25.190  11.623  1.00 37.79           C
ANISOU  376  C   ALA A 132     5189   5831   3340    953    189   -440       C
ATOM    377  O   ALA A 132      57.450  24.638  12.123  1.00 41.11           O
ANISOU  377  O   ALA A 132     5607   6314   3700   1114      0   -443       O
ATOM    378  CB  ALA A 132      56.839  26.840   9.789  1.00 34.35           C
ANISOU  378  CB  ALA A 132     4367   5576   3108    842    401   -523       C
ATOM    379  N   ASN A 133      55.326  24.559  11.355  1.00 33.74           N
ANISOU  379  N   ASN A 133     4853   5139   2827    903    265   -377       N
ATOM    380  CA  ASN A 133      55.172  23.112  11.406  1.00 36.49           C
ANISOU  380  CA  ASN A 133     5439   5301   3124   1013    154   -306       C
ATOM    381  C   ASN A 133      54.909  22.613   9.994  1.00 35.04           C
ANISOU  381  C   ASN A 133     5211   5051   3050   1090    201   -364       C
ATOM    382  O   ASN A 133      53.999  23.106   9.320  1.00 32.55           O
ANISOU  382  O   ASN A 133     4826   4749   2793    947    338   -379       O
ATOM    383  CB  ASN A 133      54.023  22.706  12.332  1.00 37.83           C
ANISOU  383  CB  ASN A 133     5877   5320   3177    808    214   -197       C
ATOM    384  CG  ASN A 133      54.287  23.055  13.780  1.00 39.32           C
ANISOU  384  CG  ASN A 133     6173   5595   3172    724    164   -147       C
ATOM    385  OD1 ASN A 133      55.259  23.740  14.100  1.00 39.30           O
ANISOU  385  OD1 ASN A 133     6020   5765   3149    801     73   -214       O
ATOM    386  ND2 ASN A 133      53.416  22.588  14.669  1.00 40.94           N
ANISOU  386  ND2 ASN A 133     6640   5705   3209    528    231    -40       N
ATOM    387  N   PHE A 134      55.703  21.646   9.544  1.00 41.23           N
ANISOU  387  N   PHE A 134     6031   5774   3859   1335     71   -418       N
ATOM    388  CA  PHE A 134      55.589  21.177   8.171  1.00 39.62           C
ANISOU  388  CA  PHE A 134     5789   5546   3721   1419    121   -532       C
ATOM    389  C   PHE A 134      56.189  19.785   8.056  1.00 42.57           C
ANISOU  389  C   PHE A 134     6332   5717   4125   1698    -46   -602       C
ATOM    390  O   PHE A 134      57.039  19.383   8.855  1.00 45.18           O
ANISOU  390  O   PHE A 134     6706   6007   4453   1900   -220   -568       O
ATOM    391  CB  PHE A 134      56.273  22.139   7.191  1.00 36.66           C
ANISOU  391  CB  PHE A 134     5092   5469   3367   1445    235   -635       C
ATOM    392  CG  PHE A 134      57.738  22.349   7.464  1.00 37.62           C
ANISOU  392  CG  PHE A 134     4987   5800   3507   1628    169   -710       C
ATOM    393  CD1 PHE A 134      58.695  21.575   6.827  1.00 38.51           C
ANISOU  393  CD1 PHE A 134     4989   5986   3656   1912    121   -876       C
ATOM    394  CD2 PHE A 134      58.157  23.322   8.355  1.00 38.06           C
ANISOU  394  CD2 PHE A 134     4910   5996   3555   1516    153   -655       C
ATOM    395  CE1 PHE A 134      60.042  21.768   7.078  1.00 39.71           C
ANISOU  395  CE1 PHE A 134     4850   6385   3854   2088     57   -974       C
ATOM    396  CE2 PHE A 134      59.501  23.518   8.610  1.00 39.77           C
ANISOU  396  CE2 PHE A 134     4868   6442   3800   1652     69   -745       C
ATOM    397  CZ  PHE A 134      60.444  22.740   7.970  1.00 40.45           C
ANISOU  397  CZ  PHE A 134     4793   6637   3941   1941     20   -898       C
ATOM    398  N   SER A 135      55.732  19.058   7.042  1.00 41.25           N
ANISOU  398  N   SER A 135     6268   5413   3990   1723    -16   -714       N
ATOM    399  CA  SER A 135      56.260  17.746   6.710  1.00 43.24           C
ANISOU  399  CA  SER A 135     6693   5430   4307   2013   -157   -847       C
ATOM    400  C   SER A 135      57.296  17.869   5.600  1.00 41.37           C
ANISOU  400  C   SER A 135     6164   5463   4093   2268    -86  -1102       C
ATOM    401  O   SER A 135      57.200  18.736   4.727  1.00 38.94           O
ANISOU  401  O   SER A 135     5631   5451   3713   2126     96  -1161       O
ATOM    402  CB  SER A 135      55.141  16.799   6.272  1.00 44.79           C
ANISOU  402  CB  SER A 135     7205   5292   4521   1859   -167   -873       C
ATOM    403  OG  SER A 135      54.549  17.239   5.062  1.00 42.59           O
ANISOU  403  OG  SER A 135     6782   5199   4199   1706    -20  -1002       O
ATOM    404  N   VAL A 136      58.296  16.992   5.643  1.00 48.19           N
ANISOU  404  N   VAL A 136     7034   6226   5048   2653   -230  -1249       N
ATOM    405  CA  VAL A 136      59.328  16.957   4.619  1.00 47.36           C
ANISOU  405  CA  VAL A 136     6620   6402   4974   2905   -135  -1535       C
ATOM    406  C   VAL A 136      59.269  15.609   3.916  1.00 49.08           C
ANISOU  406  C   VAL A 136     7055   6309   5282   3057   -209  -1719       C
ATOM    407  O   VAL A 136      58.731  14.628   4.436  1.00 51.11           O
ANISOU  407  O   VAL A 136     7724   6091   5605   3147   -388  -1674       O
ATOM    408  CB  VAL A 136      60.741  17.210   5.187  1.00 48.01           C
ANISOU  408  CB  VAL A 136     6359   6735   5147   3144   -233  -1560       C
ATOM    409  CG1 VAL A 136      60.770  18.495   5.997  1.00 47.01           C
ANISOU  409  CG1 VAL A 136     6050   6865   4945   2935   -193  -1375       C
ATOM    410  CG2 VAL A 136      61.199  16.030   6.024  1.00 51.16           C
ANISOU  410  CG2 VAL A 136     6979   6776   5685   3516   -546  -1548       C
ATOM    411  N   ILE A 137      59.824  15.578   2.708  1.00 53.87           N
ANISOU  411  N   ILE A 137     7011   5800   7658   2840   1090  -1474       N
ATOM    412  CA  ILE A 137      59.949  14.346   1.939  1.00 59.25           C
ANISOU  412  CA  ILE A 137     8069   6110   8335   3119   1227  -1883       C
ATOM    413  C   ILE A 137      61.041  14.562   0.903  1.00 63.39           C
ANISOU  413  C   ILE A 137     8368   6949   8767   3377   1715  -2135       C
ATOM    414  O   ILE A 137      61.134  15.630   0.290  1.00 61.96           O
ANISOU  414  O   ILE A 137     8028   7236   8277   3225   1961  -2085       O
ATOM    415  CB  ILE A 137      58.600  13.935   1.300  1.00 59.18           C
ANISOU  415  CB  ILE A 137     8613   5886   7987   2754   1053  -2082       C
ATOM    416  CG1 ILE A 137      58.662  12.497   0.790  1.00 65.28           C
ANISOU  416  CG1 ILE A 137     9854   6109   8840   3005   1096  -2517       C
ATOM    417  CG2 ILE A 137      58.204  14.881   0.173  1.00 58.20           C
ANISOU  417  CG2 ILE A 137     8542   6232   7341   2500   1216  -2169       C
ATOM    418  CD1 ILE A 137      57.356  12.020   0.205  1.00 66.23           C
ANISOU  418  CD1 ILE A 137    10496   5991   8676   2591    858  -2753       C
ATOM    419  N   PHE A 138      61.887  13.544   0.733  1.00 69.20           N
ANISOU  419  N   PHE A 138     9051   7424   9816   3664   1856  -2344       N
ATOM    420  CA  PHE A 138      63.073  13.644  -0.120  1.00 74.36           C
ANISOU  420  CA  PHE A 138     9367   8369  10517   3843   2312  -2565       C
ATOM    421  C   PHE A 138      63.920  14.856   0.263  1.00 72.31           C
ANISOU  421  C   PHE A 138     8446   8617  10412   3769   2421  -2278       C
ATOM    422  O   PHE A 138      64.502  15.529  -0.590  1.00 74.50           O
ANISOU  422  O   PHE A 138     8494   9317  10493   3694   2797  -2385       O
ATOM    423  CB  PHE A 138      62.685  13.689  -1.602  1.00 77.10           C
ANISOU  423  CB  PHE A 138    10119   8885  10289   3716   2620  -2936       C
ATOM    424  CG  PHE A 138      61.739  12.597  -2.014  1.00 79.36           C
ANISOU  424  CG  PHE A 138    11079   8690  10383   3672   2437  -3263       C
ATOM    425  CD1 PHE A 138      62.186  11.295  -2.163  1.00 85.80           C
ANISOU  425  CD1 PHE A 138    12036   9053  11509   3944   2507  -3580       C
ATOM    426  CD2 PHE A 138      60.404  12.874  -2.257  1.00 75.82           C
ANISOU  426  CD2 PHE A 138    11103   8228   9478   3332   2171  -3271       C
ATOM    427  CE1 PHE A 138      61.318  10.289  -2.541  1.00 88.61           C
ANISOU  427  CE1 PHE A 138    13009   8933  11727   3830   2324  -3899       C
ATOM    428  CE2 PHE A 138      59.531  11.872  -2.637  1.00 78.67           C
ANISOU  428  CE2 PHE A 138    12042   8147   9703   3195   1944  -3600       C
ATOM    429  CZ  PHE A 138      59.988  10.578  -2.779  1.00 85.06           C
ANISOU  429  CZ  PHE A 138    13002   8489  10828   3422   2028  -3914       C
ATOM    430  N   ASP A 139      63.975  15.141   1.565  1.00 68.70           N
ANISOU  430  N   ASP A 139     7707   8116  10279   3743   2067  -1913       N
ATOM    431  CA  ASP A 139      64.717  16.269   2.131  1.00 66.95           C
ANISOU  431  CA  ASP A 139     6878   8313  10249   3606   2046  -1657       C
ATOM    432  C   ASP A 139      64.265  17.616   1.569  1.00 63.22           C
ANISOU  432  C   ASP A 139     6412   8265   9342   3241   2233  -1550       C
ATOM    433  O   ASP A 139      65.019  18.594   1.609  1.00 63.62           O
ANISOU  433  O   ASP A 139     5996   8699   9476   3082   2355  -1438       O
ATOM    434  CB  ASP A 139      66.227  16.092   1.940  1.00 73.40           C
ANISOU  434  CB  ASP A 139     7158   9315  11414   3817   2238  -1798       C
ATOM    435  CG  ASP A 139      66.765  14.880   2.674  1.00 77.55           C
ANISOU  435  CG  ASP A 139     7638   9389  12438   4168   2059  -1712       C
ATOM    436  OD1 ASP A 139      66.209  14.540   3.740  1.00 74.57           O
ANISOU  436  OD1 ASP A 139     7477   8722  12135   4197   1687  -1382       O
ATOM    437  OD2 ASP A 139      67.736  14.264   2.185  1.00 84.41           O
ANISOU  437  OD2 ASP A 139     8277  10228  13565   4447   2302  -1947       O
ATOM    438  N   ARG A 140      63.041  17.687   1.049  1.00 60.26           N
ANISOU  438  N   ARG A 140     6576   7814   8507   3095   2233  -1572       N
ATOM    439  CA  ARG A 140      62.422  18.933   0.627  1.00 56.74           C
ANISOU  439  CA  ARG A 140     6211   7685   7664   2765   2351  -1382       C
ATOM    440  C   ARG A 140      61.170  19.174   1.459  1.00 51.02           C
ANISOU  440  C   ARG A 140     5725   6782   6877   2469   1864  -1146       C
ATOM    441  O   ARG A 140      60.557  18.232   1.967  1.00 50.88           O
ANISOU  441  O   ARG A 140     5979   6400   6952   2526   1550  -1206       O
ATOM    442  CB  ARG A 140      62.049  18.908  -0.864  1.00 59.54           C
ANISOU  442  CB  ARG A 140     7001   8161   7462   2700   2674  -1617       C
ATOM    443  CG  ARG A 140      63.227  18.835  -1.821  1.00 65.87           C
ANISOU  443  CG  ARG A 140     7583   9193   8252   2779   3128  -1835       C
ATOM    444  CD  ARG A 140      62.748  18.805  -3.266  1.00 69.07           C
ANISOU  444  CD  ARG A 140     8506   9730   8007   2685   3387  -2049       C
ATOM    445  NE  ARG A 140      63.853  18.878  -4.218  1.00 75.65           N
ANISOU  445  NE  ARG A 140     9124  10865   8754   2734   3866  -2228       N
ATOM    446  CZ  ARG A 140      64.500  17.820  -4.696  1.00 81.79           C
ANISOU  446  CZ  ARG A 140     9901  11550   9625   3034   4066  -2640       C
ATOM    447  NH1 ARG A 140      64.157  16.598  -4.309  1.00 82.14           N
ANISOU  447  NH1 ARG A 140    10186  11133   9889   3281   3813  -2893       N
ATOM    448  NH2 ARG A 140      65.494  17.982  -5.559  1.00 88.25           N
ANISOU  448  NH2 ARG A 140    10483  12726  10323   3088   4527  -2793       N
ATOM    449  N   LEU A 141      60.791  20.441   1.598  1.00 47.52           N
ANISOU  449  N   LEU A 141     5183   6568   6305   2125   1819   -872       N
ATOM    450  CA  LEU A 141      59.537  20.763   2.268  1.00 44.93           C
ANISOU  450  CA  LEU A 141     5063   6111   5897   1838   1420   -673       C
ATOM    451  C   LEU A 141      58.378  20.244   1.429  1.00 47.86           C
ANISOU  451  C   LEU A 141     5923   6365   5895   1737   1316   -831       C
ATOM    452  O   LEU A 141      58.223  20.627   0.264  1.00 49.48           O
ANISOU  452  O   LEU A 141     6318   6770   5710   1674   1516   -905       O
ATOM    453  CB  LEU A 141      59.414  22.270   2.494  1.00 42.43           C
ANISOU  453  CB  LEU A 141     4562   6024   5538   1549   1437   -385       C
ATOM    454  CG  LEU A 141      58.246  22.753   3.366  1.00 40.62           C
ANISOU  454  CG  LEU A 141     4445   5688   5303   1311   1082   -178       C
ATOM    455  CD1 LEU A 141      58.629  24.018   4.115  1.00 37.47           C
ANISOU  455  CD1 LEU A 141     3758   5403   5074   1143   1080     40       C
ATOM    456  CD2 LEU A 141      56.982  23.000   2.552  1.00 42.76           C
ANISOU  456  CD2 LEU A 141     5051   5984   5213   1148   1004   -154       C
ATOM    457  N   GLU A 142      57.566  19.368   2.017  1.00 42.13           N
ANISOU  457  N   GLU A 142     5409   5324   5275   1695    990   -873       N
ATOM    458  CA  GLU A 142      56.424  18.783   1.305  1.00 43.19           C
ANISOU  458  CA  GLU A 142     5957   5327   5128   1538    818  -1055       C
ATOM    459  C   GLU A 142      55.180  19.643   1.497  1.00 41.78           C
ANISOU  459  C   GLU A 142     5772   5289   4814   1206    568   -810       C
ATOM    460  O   GLU A 142      54.717  20.305   0.563  1.00 43.02           O
ANISOU  460  O   GLU A 142     6041   5687   4617   1094    584   -794       O
ATOM    461  CB  GLU A 142      56.177  17.350   1.781  1.00 45.03           C
ANISOU  461  CB  GLU A 142     6415   5097   5597   1614    625  -1230       C
ATOM    462  CG  GLU A 142      55.047  16.649   1.047  1.00 47.56           C
ANISOU  462  CG  GLU A 142     7145   5240   5685   1391    420  -1477       C
ATOM    463  CD  GLU A 142      54.581  15.394   1.756  1.00 48.67           C
ANISOU  463  CD  GLU A 142     7495   4862   6133   1327    191  -1542       C
ATOM    464  OE1 GLU A 142      54.791  15.292   2.983  1.00 46.74           O
ANISOU  464  OE1 GLU A 142     7082   4460   6219   1379    123  -1269       O
ATOM    465  OE2 GLU A 142      54.003  14.511   1.087  1.00 52.35           O
ANISOU  465  OE2 GLU A 142     8334   5065   6493   1203     71  -1863       O
ATOM    466  N   THR A 143      54.634  19.640   2.711  1.00 38.33           N
ANISOU  466  N   THR A 143     5210   4710   4643   1079    346   -604       N
ATOM    467  CA  THR A 143      53.383  20.314   3.021  1.00 38.90           C
ANISOU  467  CA  THR A 143     5231   4883   4665    812    136   -401       C
ATOM    468  C   THR A 143      53.550  21.147   4.283  1.00 34.03           C
ANISOU  468  C   THR A 143     4345   4319   4264    790    145   -121       C
ATOM    469  O   THR A 143      54.137  20.690   5.268  1.00 31.83           O
ANISOU  469  O   THR A 143     3999   3883   4212    887    134    -76       O
ATOM    470  CB  THR A 143      52.245  19.300   3.212  1.00 41.96           C
ANISOU  470  CB  THR A 143     5787   5026   5129    607   -125   -492       C
ATOM    471  OG1 THR A 143      52.099  18.513   2.024  1.00 44.73           O
ANISOU  471  OG1 THR A 143     6437   5301   5259    596   -176   -821       O
ATOM    472  CG2 THR A 143      50.934  20.010   3.512  1.00 43.62           C
ANISOU  472  CG2 THR A 143     5837   5398   5338    357   -307   -289       C
ATOM    473  N   LEU A 144      53.032  22.371   4.245  1.00 37.38           N
ANISOU  473  N   LEU A 144     4653   4948   4599    684    143     61       N
ATOM    474  CA  LEU A 144      53.022  23.248   5.405  1.00 31.75           C
ANISOU  474  CA  LEU A 144     3750   4264   4050    640    148    268       C
ATOM    475  C   LEU A 144      51.755  23.017   6.219  1.00 31.19           C
ANISOU  475  C   LEU A 144     3670   4115   4065    486    -13    359       C
ATOM    476  O   LEU A 144      50.645  23.049   5.676  1.00 33.79           O
ANISOU  476  O   LEU A 144     4007   4512   4320    373   -125    361       O
ATOM    477  CB  LEU A 144      53.107  24.712   4.975  1.00 29.96           C
ANISOU  477  CB  LEU A 144     3441   4216   3727    624    266    408       C
ATOM    478  CG  LEU A 144      52.896  25.740   6.091  1.00 25.32           C
ANISOU  478  CG  LEU A 144     2722   3613   3288    566    263    566       C
ATOM    479  CD1 LEU A 144      54.092  25.767   7.032  1.00 24.17           C
ANISOU  479  CD1 LEU A 144     2456   3424   3305    600    313    540       C
ATOM    480  CD2 LEU A 144      52.616  27.122   5.518  1.00 25.35           C
ANISOU  480  CD2 LEU A 144     2728   3691   3214    550    342    715       C
ATOM    481  N   ILE A 145      51.923  22.786   7.516  1.00 31.67           N
ANISOU  481  N   ILE A 145     3697   4066   4268    478    -23    442       N
ATOM    482  CA  ILE A 145      50.786  22.716   8.428  1.00 31.12           C
ANISOU  482  CA  ILE A 145     3601   3964   4258    322    -70    561       C
ATOM    483  C   ILE A 145      50.419  24.100   8.950  1.00 27.30           C
ANISOU  483  C   ILE A 145     2977   3633   3764    322     18    673       C
ATOM    484  O   ILE A 145      49.253  24.502   8.909  1.00 27.34           O
ANISOU  484  O   ILE A 145     2873   3722   3793    248     21    732       O
ATOM    485  CB  ILE A 145      51.083  21.731   9.582  1.00 31.40           C
ANISOU  485  CB  ILE A 145     3763   3795   4373    312   -102    628       C
ATOM    486  CG1 ILE A 145      50.730  20.295   9.180  1.00 35.80           C
ANISOU  486  CG1 ILE A 145     4497   4101   5006    223   -191    551       C
ATOM    487  CG2 ILE A 145      50.316  22.116  10.836  1.00 30.11           C
ANISOU  487  CG2 ILE A 145     3566   3680   4193    192    -35    792       C
ATOM    488  CD1 ILE A 145      51.635  19.693   8.123  1.00 38.14           C
ANISOU  488  CD1 ILE A 145     4906   4291   5296    399   -215    338       C
ATOM    489  N   LEU A 146      51.407  24.858   9.422  1.00 31.68           N
ANISOU  489  N   LEU A 146     3512   4211   4314    409     82    683       N
ATOM    490  CA  LEU A 146      51.165  26.198   9.933  1.00 29.91           C
ANISOU  490  CA  LEU A 146     3224   4048   4093    409    170    736       C
ATOM    491  C   LEU A 146      52.492  26.932  10.038  1.00 29.62           C
ANISOU  491  C   LEU A 146     3164   4011   4080    447    201    692       C
ATOM    492  O   LEU A 146      53.533  26.322  10.296  1.00 30.00           O
ANISOU  492  O   LEU A 146     3194   4047   4158    484    134    643       O
ATOM    493  CB  LEU A 146      50.469  26.162  11.299  1.00 30.74           C
ANISOU  493  CB  LEU A 146     3363   4138   4179    352    217    784       C
ATOM    494  CG  LEU A 146      50.028  27.499  11.902  1.00 30.60           C
ANISOU  494  CG  LEU A 146     3321   4146   4158    384    349    778       C
ATOM    495  CD1 LEU A 146      49.007  28.192  11.004  1.00 29.47           C
ANISOU  495  CD1 LEU A 146     3040   4049   4109    450    396    829       C
ATOM    496  CD2 LEU A 146      49.473  27.296  13.307  1.00 32.63           C
ANISOU  496  CD2 LEU A 146     3664   4421   4314    336    452    793       C
ATOM    497  N   LEU A 147      52.442  28.245   9.822  1.00 29.54           N
ANISOU  497  N   LEU A 147     3131   3996   4097    437    293    718       N
ATOM    498  CA  LEU A 147      53.572  29.129  10.064  1.00 30.69           C
ANISOU  498  CA  LEU A 147     3239   4104   4316    382    333    672       C
ATOM    499  C   LEU A 147      53.059  30.371  10.774  1.00 32.66           C
ANISOU  499  C   LEU A 147     3572   4242   4596    351    396    657       C
ATOM    500  O   LEU A 147      52.023  30.925  10.397  1.00 32.32           O
ANISOU  500  O   LEU A 147     3567   4150   4564    427    473    735       O
ATOM    501  CB  LEU A 147      54.289  29.515   8.758  1.00 30.99           C
ANISOU  501  CB  LEU A 147     3218   4172   4385    367    448    718       C
ATOM    502  CG  LEU A 147      55.652  30.220   8.834  1.00 32.38           C
ANISOU  502  CG  LEU A 147     3263   4335   4704    242    520    676       C
ATOM    503  CD1 LEU A 147      56.436  29.993   7.550  1.00 32.38           C
ANISOU  503  CD1 LEU A 147     3164   4444   4695    248    693    717       C
ATOM    504  CD2 LEU A 147      55.524  31.717   9.098  1.00 34.49           C
ANISOU  504  CD2 LEU A 147     3620   4422   5064    116    596    709       C
ATOM    505  N   ARG A 148      53.784  30.805  11.801  1.00 30.90           N
ANISOU  505  N   ARG A 148     3378   3973   4390    260    340    536       N
ATOM    506  CA  ARG A 148      53.409  31.994  12.550  1.00 35.01           C
ANISOU  506  CA  ARG A 148     4042   4338   4923    226    409    443       C
ATOM    507  C   ARG A 148      54.653  32.804  12.884  1.00 39.06           C
ANISOU  507  C   ARG A 148     4543   4756   5543     35    341    308       C
ATOM    508  O   ARG A 148      55.745  32.257  13.061  1.00 39.08           O
ANISOU  508  O   ARG A 148     4389   4889   5571    -53    182    261       O
ATOM    509  CB  ARG A 148      52.640  31.638  13.830  1.00 37.16           C
ANISOU  509  CB  ARG A 148     4448   4660   5011    280    407    363       C
ATOM    510  CG  ARG A 148      51.208  31.208  13.571  1.00 33.20           C
ANISOU  510  CG  ARG A 148     3905   4217   4492    416    540    481       C
ATOM    511  CD  ARG A 148      50.422  31.040  14.859  1.00 35.55           C
ANISOU  511  CD  ARG A 148     4324   4569   4614    443    654    413       C
ATOM    512  NE  ARG A 148      48.983  31.031  14.606  1.00 32.94           N
ANISOU  512  NE  ARG A 148     3861   4288   4368    564    843    499       N
ATOM    513  CZ  ARG A 148      48.058  30.909  15.550  1.00 34.28           C
ANISOU  513  CZ  ARG A 148     4055   4539   4431    602   1052    468       C
ATOM    514  NH1 ARG A 148      48.416  30.778  16.820  1.00 37.75           N
ANISOU  514  NH1 ARG A 148     4740   5012   4590    531   1094    361       N
ATOM    515  NH2 ARG A 148      46.772  30.916  15.225  1.00 32.60           N
ANISOU  515  NH2 ARG A 148     3605   4406   4377    709   1219    550       N
ATOM    516  N   ALA A 149      54.470  34.119  12.966  1.00 34.29           N
ANISOU  516  N   ALA A 149     4085   3901   5042    -26    449    240       N
ATOM    517  CA  ALA A 149      55.551  35.058  13.229  1.00 37.10           C
ANISOU  517  CA  ALA A 149     4449   4093   5556   -285    393     92       C
ATOM    518  C   ALA A 149      55.454  35.540  14.671  1.00 42.22           C
ANISOU  518  C   ALA A 149     5327   4644   6069   -348    285   -195       C
ATOM    519  O   ALA A 149      54.423  36.085  15.078  1.00 43.22           O
ANISOU  519  O   ALA A 149     5696   4602   6122   -198    437   -270       O
ATOM    520  CB  ALA A 149      55.486  36.237  12.260  1.00 35.66           C
ANISOU  520  CB  ALA A 149     4352   3603   5593   -350    597    222       C
ATOM    521  N   PHE A 150      56.525  35.344  15.437  1.00 39.39           N
ANISOU  521  N   PHE A 150     4887   4413   5666   -549     18   -372       N
ATOM    522  CA  PHE A 150      56.562  35.704  16.848  1.00 43.54           C
ANISOU  522  CA  PHE A 150     5675   4908   5960   -634   -155   -676       C
ATOM    523  C   PHE A 150      57.596  36.795  17.085  1.00 44.68           C
ANISOU  523  C   PHE A 150     5822   4842   6312   -994   -311   -927       C
ATOM    524  O   PHE A 150      58.678  36.778  16.489  1.00 44.68           O
ANISOU  524  O   PHE A 150     5475   4910   6590  -1213   -416   -858       O
ATOM    525  CB  PHE A 150      56.897  34.493  17.726  1.00 44.46           C
ANISOU  525  CB  PHE A 150     5748   5378   5767   -570   -444   -673       C
ATOM    526  CG  PHE A 150      55.892  33.381  17.642  1.00 43.87           C
ANISOU  526  CG  PHE A 150     5711   5458   5498   -292   -295   -441       C
ATOM    527  CD1 PHE A 150      55.951  32.452  16.617  1.00 39.82           C
ANISOU  527  CD1 PHE A 150     4929   5056   5145   -181   -253   -182       C
ATOM    528  CD2 PHE A 150      54.896  33.258  18.595  1.00 45.65           C
ANISOU  528  CD2 PHE A 150     6250   5715   5381   -171   -173   -502       C
ATOM    529  CE1 PHE A 150      55.031  31.429  16.540  1.00 37.77           C
ANISOU  529  CE1 PHE A 150     4714   4892   4746      5   -143      2       C
ATOM    530  CE2 PHE A 150      53.974  32.234  18.523  1.00 43.47           C
ANISOU  530  CE2 PHE A 150     5968   5570   4979      9    -16   -275       C
ATOM    531  CZ  PHE A 150      54.041  31.319  17.494  1.00 39.86           C
ANISOU  531  CZ  PHE A 150     5243   5180   4723     77    -28    -27       C
ATOM    532  N   THR A 151      57.260  37.741  17.958  1.00 48.47           N
ANISOU  532  N   THR A 151     6684   5060   6671  -1070   -304  -1243       N
ATOM    533  CA  THR A 151      58.235  38.711  18.428  1.00 52.37           C
ANISOU  533  CA  THR A 151     7240   5341   7316  -1472   -532  -1569       C
ATOM    534  C   THR A 151      59.064  38.095  19.554  1.00 54.91           C
ANISOU  534  C   THR A 151     7496   6028   7339  -1613  -1014  -1780       C
ATOM    535  O   THR A 151      58.840  36.957  19.975  1.00 52.74           O
ANISOU  535  O   THR A 151     7191   6116   6731  -1370  -1131  -1638       O
ATOM    536  CB  THR A 151      57.541  39.990  18.892  1.00 55.88           C
ANISOU  536  CB  THR A 151     8187   5294   7752  -1482   -335  -1875       C
ATOM    537  OG1 THR A 151      56.617  39.681  19.943  1.00 56.10           O
ANISOU  537  OG1 THR A 151     8565   5450   7299  -1201   -275  -2054       O
ATOM    538  CG2 THR A 151      56.793  40.641  17.738  1.00 54.34           C
ANISOU  538  CG2 THR A 151     8040   4715   7891  -1306     76  -1611       C
ATOM    539  N   GLU A 152      60.042  38.857  20.051  1.00 60.31           N
ANISOU  539  N   GLU A 152     8167   6600   8146  -2026  -1332  -2109       N
ATOM    540  CA  GLU A 152      60.882  38.354  21.134  1.00 63.92           C
ANISOU  540  CA  GLU A 152     8552   7428   8307  -2167  -1891  -2319       C
ATOM    541  C   GLU A 152      60.073  38.090  22.397  1.00 65.08           C
ANISOU  541  C   GLU A 152     9255   7689   7782  -1938  -1956  -2514       C
ATOM    542  O   GLU A 152      60.392  37.167  23.156  1.00 66.05           O
ANISOU  542  O   GLU A 152     9362   8221   7512  -1839  -2327  -2464       O
ATOM    543  CB  GLU A 152      62.016  39.337  21.429  1.00 70.53           C
ANISOU  543  CB  GLU A 152     9266   8106   9426  -2713  -2249  -2688       C
ATOM    544  CG  GLU A 152      63.232  39.175  20.531  1.00 71.20           C
ANISOU  544  CG  GLU A 152     8620   8350  10083  -2985  -2365  -2487       C
ATOM    545  CD  GLU A 152      64.370  40.101  20.920  1.00 78.79           C
ANISOU  545  CD  GLU A 152     9387   9195  11354  -3595  -2761  -2867       C
ATOM    546  OE1 GLU A 152      64.119  41.078  21.657  1.00 83.16           O
ANISOU  546  OE1 GLU A 152    10463   9385  11749  -3836  -2853  -3295       O
ATOM    547  OE2 GLU A 152      65.516  39.849  20.493  1.00 81.03           O
ANISOU  547  OE2 GLU A 152     9005   9764  12018  -3821  -2936  -2726       O
ATOM    548  N   GLU A 153      59.026  38.879  22.638  1.00 65.66           N
ANISOU  548  N   GLU A 153     9832   7407   7710  -1825  -1575  -2716       N
ATOM    549  CA  GLU A 153      58.186  38.691  23.813  1.00 67.51           C
ANISOU  549  CA  GLU A 153    10605   7757   7288  -1601  -1507  -2915       C
ATOM    550  C   GLU A 153      57.155  37.583  23.638  1.00 62.32           C
ANISOU  550  C   GLU A 153     9917   7353   6409  -1175  -1171  -2505       C
ATOM    551  O   GLU A 153      56.478  37.235  24.611  1.00 64.02           O
ANISOU  551  O   GLU A 153    10527   7741   6057   -998  -1071  -2586       O
ATOM    552  CB  GLU A 153      57.480  40.001  24.175  1.00 71.35           C
ANISOU  552  CB  GLU A 153    11622   7749   7738  -1613  -1183  -3347       C
ATOM    553  CG  GLU A 153      57.245  40.946  23.003  1.00 69.88           C
ANISOU  553  CG  GLU A 153    11309   7033   8208  -1641   -826  -3257       C
ATOM    554  CD  GLU A 153      58.418  41.882  22.761  1.00 74.24           C
ANISOU  554  CD  GLU A 153    11753   7261   9193  -2163  -1126  -3496       C
ATOM    555  OE1 GLU A 153      59.462  41.713  23.426  1.00 77.98           O
ANISOU  555  OE1 GLU A 153    12125   7991   9512  -2507  -1659  -3723       O
ATOM    556  OE2 GLU A 153      58.294  42.789  21.910  1.00 74.58           O
ANISOU  556  OE2 GLU A 153    11804   6792   9742  -2243   -843  -3437       O
ATOM    557  N   GLY A 154      57.016  37.025  22.437  1.00 56.79           N
ANISOU  557  N   GLY A 154     8780   6678   6119  -1037   -981  -2083       N
ATOM    558  CA  GLY A 154      56.128  35.904  22.209  1.00 52.42           C
ANISOU  558  CA  GLY A 154     8152   6351   5417   -710   -730  -1709       C
ATOM    559  C   GLY A 154      54.812  36.234  21.541  1.00 49.69           C
ANISOU  559  C   GLY A 154     7836   5785   5261   -460   -191  -1589       C
ATOM    560  O   GLY A 154      53.992  35.328  21.355  1.00 48.02           O
ANISOU  560  O   GLY A 154     7533   5757   4956   -237     19  -1303       O
ATOM    561  N   ALA A 155      54.582  37.491  21.174  1.00 51.30           N
ANISOU  561  N   ALA A 155     8152   5583   5754   -493     14  -1786       N
ATOM    562  CA  ALA A 155      53.337  37.883  20.534  1.00 49.70           C
ANISOU  562  CA  ALA A 155     7948   5167   5768   -198    470  -1659       C
ATOM    563  C   ALA A 155      53.302  37.414  19.084  1.00 44.93           C
ANISOU  563  C   ALA A 155     6918   4601   5550   -131    513  -1234       C
ATOM    564  O   ALA A 155      54.322  37.390  18.392  1.00 43.94           O
ANISOU  564  O   ALA A 155     6563   4466   5667   -349    301  -1129       O
ATOM    565  CB  ALA A 155      53.160  39.399  20.594  1.00 53.87           C
ANISOU  565  CB  ALA A 155     8782   5179   6509   -211    643  -1983       C
ATOM    566  N   ILE A 156      52.111  37.045  18.625  1.00 45.42           N
ANISOU  566  N   ILE A 156     6865   4732   5659    164    799  -1009       N
ATOM    567  CA  ILE A 156      51.911  36.615  17.245  1.00 42.04           C
ANISOU  567  CA  ILE A 156     6099   4354   5520    249    829   -641       C
ATOM    568  C   ILE A 156      51.554  37.832  16.400  1.00 40.34           C
ANISOU  568  C   ILE A 156     5931   3740   5655    358    999   -596       C
ATOM    569  O   ILE A 156      50.638  38.590  16.740  1.00 43.01           O
ANISOU  569  O   ILE A 156     6445   3856   6041    594   1237   -726       O
ATOM    570  CB  ILE A 156      50.820  35.536  17.157  1.00 39.06           C
ANISOU  570  CB  ILE A 156     5545   4270   5027    461    971   -422       C
ATOM    571  CG1 ILE A 156      51.172  34.355  18.064  1.00 40.79           C
ANISOU  571  CG1 ILE A 156     5808   4800   4891    352    818   -421       C
ATOM    572  CG2 ILE A 156      50.653  35.070  15.720  1.00 34.51           C
ANISOU  572  CG2 ILE A 156     4665   3756   4693    519    934   -100       C
ATOM    573  CD1 ILE A 156      50.067  33.330  18.198  1.00 37.11           C
ANISOU  573  CD1 ILE A 156     5230   4565   4305    483   1004   -228       C
ATOM    574  N   VAL A 157      52.279  38.021  15.295  1.00 45.05           N
ANISOU  574  N   VAL A 157     6388   4236   6494    211    904   -394       N
ATOM    575  CA  VAL A 157      52.106  39.197  14.447  1.00 43.74           C
ANISOU  575  CA  VAL A 157     6334   3648   6638    272   1039   -279       C
ATOM    576  C   VAL A 157      51.935  38.798  12.987  1.00 39.80           C
ANISOU  576  C   VAL A 157     5608   3272   6242    365   1045    131       C
ATOM    577  O   VAL A 157      51.661  39.649  12.133  1.00 40.79           O
ANISOU  577  O   VAL A 157     5838   3092   6570    471   1143    335       O
ATOM    578  CB  VAL A 157      53.290  40.171  14.599  1.00 46.11           C
ANISOU  578  CB  VAL A 157     6812   3592   7116    -96    959   -462       C
ATOM    579  CG1 VAL A 157      53.382  40.693  16.024  1.00 49.90           C
ANISOU  579  CG1 VAL A 157     7599   3908   7452   -188    918   -929       C
ATOM    580  CG2 VAL A 157      54.588  39.495  14.175  1.00 45.59           C
ANISOU  580  CG2 VAL A 157     6454   3804   7065   -432    764   -360       C
ATOM    581  N   GLY A 158      52.104  37.514  12.682  1.00 40.35           N
ANISOU  581  N   GLY A 158     5420   3761   6149    334    931    254       N
ATOM    582  CA  GLY A 158      51.963  37.051  11.314  1.00 36.75           C
ANISOU  582  CA  GLY A 158     4800   3454   5710    409    922    576       C
ATOM    583  C   GLY A 158      51.613  35.583  11.266  1.00 34.30           C
ANISOU  583  C   GLY A 158     4274   3549   5211    477    823    622       C
ATOM    584  O   GLY A 158      51.796  34.849  12.242  1.00 35.46           O
ANISOU  584  O   GLY A 158     4388   3862   5224    412    752    457       O
ATOM    585  N   GLU A 159      51.110  35.154  10.110  1.00 39.69           N
ANISOU  585  N   GLU A 159     4851   4368   5863    598    798    854       N
ATOM    586  CA  GLU A 159      50.681  33.771   9.954  1.00 37.05           C
ANISOU  586  CA  GLU A 159     4344   4348   5386    636    696    879       C
ATOM    587  C   GLU A 159      50.622  33.408   8.478  1.00 35.36           C
ANISOU  587  C   GLU A 159     4084   4256   5095    673    632   1081       C
ATOM    588  O   GLU A 159      50.297  34.243   7.630  1.00 35.77           O
ANISOU  588  O   GLU A 159     4224   4192   5175    779    655   1268       O
ATOM    589  CB  GLU A 159      49.314  33.536  10.609  1.00 36.19           C
ANISOU  589  CB  GLU A 159     4148   4318   5284    804    730    845       C
ATOM    590  CG  GLU A 159      48.891  32.074  10.689  1.00 33.62           C
ANISOU  590  CG  GLU A 159     3667   4255   4851    752    642    850       C
ATOM    591  CD  GLU A 159      47.429  31.909  11.057  1.00 33.31           C
ANISOU  591  CD  GLU A 159     3451   4322   4882    879    714    874       C
ATOM    592  OE1 GLU A 159      46.570  32.509  10.376  1.00 33.43           O
ANISOU  592  OE1 GLU A 159     3340   4332   5030   1066    697    989       O
ATOM    593  OE2 GLU A 159      47.142  31.182  12.031  1.00 33.61           O
ANISOU  593  OE2 GLU A 159     3461   4459   4848    797    793    801       O
ATOM    594  N   ILE A 160      50.950  32.150   8.185  1.00 32.15           N
ANISOU  594  N   ILE A 160     3590   4063   4564    602    546   1039       N
ATOM    595  CA  ILE A 160      50.706  31.540   6.884  1.00 31.96           C
ANISOU  595  CA  ILE A 160     3559   4197   4389    643    463   1146       C
ATOM    596  C   ILE A 160      50.030  30.201   7.129  1.00 30.58           C
ANISOU  596  C   ILE A 160     3275   4177   4167    633    328   1049       C
ATOM    597  O   ILE A 160      50.534  29.381   7.904  1.00 29.50           O
ANISOU  597  O   ILE A 160     3118   4044   4047    551    328    924       O
ATOM    598  CB  ILE A 160      52.001  31.347   6.071  1.00 33.32           C
ANISOU  598  CB  ILE A 160     3785   4416   4458    541    556   1150       C
ATOM    599  CG1 ILE A 160      52.721  32.681   5.873  1.00 33.86           C
ANISOU  599  CG1 ILE A 160     3946   4300   4618    462    730   1271       C
ATOM    600  CG2 ILE A 160      51.685  30.713   4.724  1.00 34.55           C
ANISOU  600  CG2 ILE A 160     4016   4746   4365    598    485   1212       C
ATOM    601  CD1 ILE A 160      54.035  32.558   5.136  1.00 34.18           C
ANISOU  601  CD1 ILE A 160     3964   4420   4601    326    907   1286       C
ATOM    602  N   SER A 161      48.889  29.980   6.482  1.00 31.13           N
ANISOU  602  N   SER A 161     3275   4359   4195    704    188   1123       N
ATOM    603  CA  SER A 161      48.137  28.754   6.694  1.00 31.08           C
ANISOU  603  CA  SER A 161     3147   4462   4200    622     61   1034       C
ATOM    604  C   SER A 161      47.387  28.401   5.422  1.00 33.71           C
ANISOU  604  C   SER A 161     3451   4952   4405    635   -168   1074       C
ATOM    605  O   SER A 161      47.011  29.298   4.657  1.00 34.44           O
ANISOU  605  O   SER A 161     3559   5094   4434    775   -247   1231       O
ATOM    606  CB  SER A 161      47.153  28.897   7.864  1.00 29.93           C
ANISOU  606  CB  SER A 161     2821   4314   4238    635    134   1036       C
ATOM    607  OG  SER A 161      46.219  29.931   7.615  1.00 30.41           O
ANISOU  607  OG  SER A 161     2744   4402   4410    818    122   1155       O
ATOM    608  N   PRO A 162      47.157  27.114   5.164  1.00 28.66           N
ANISOU  608  N   PRO A 162     2806   4369   3714    489   -308    937       N
ATOM    609  CA  PRO A 162      46.341  26.733   4.009  1.00 31.95           C
ANISOU  609  CA  PRO A 162     3196   4953   3990    454   -597    918       C
ATOM    610  C   PRO A 162      44.877  27.065   4.249  1.00 32.98           C
ANISOU  610  C   PRO A 162     2978   5219   4335    475   -756   1020       C
ATOM    611  O   PRO A 162      44.362  26.910   5.359  1.00 32.49           O
ANISOU  611  O   PRO A 162     2693   5121   4532    410   -621   1016       O
ATOM    612  CB  PRO A 162      46.567  25.222   3.900  1.00 35.36           C
ANISOU  612  CB  PRO A 162     3744   5315   4378    254   -671    686       C
ATOM    613  CG  PRO A 162      46.880  24.802   5.284  1.00 33.06           C
ANISOU  613  CG  PRO A 162     3403   4847   4311    185   -470    674       C
ATOM    614  CD  PRO A 162      47.646  25.937   5.905  1.00 28.85           C
ANISOU  614  CD  PRO A 162     2888   4273   3802    348   -244    791       C
ATOM    615  N   LEU A 163      44.213  27.533   3.197  1.00 33.40           N
ANISOU  615  N   LEU A 163     3242   4315   5134     15   -881   -737       N
ATOM    616  CA  LEU A 163      42.813  27.911   3.320  1.00 33.98           C
ANISOU  616  CA  LEU A 163     2934   4550   5429      9  -1110  -1142       C
ATOM    617  C   LEU A 163      41.953  26.671   3.553  1.00 35.05           C
ANISOU  617  C   LEU A 163     3023   4921   5372   -299   -900  -1326       C
ATOM    618  O   LEU A 163      42.131  25.653   2.877  1.00 36.40           O
ANISOU  618  O   LEU A 163     3558   4977   5297   -438   -775  -1117       O
ATOM    619  CB  LEU A 163      42.343  28.657   2.072  1.00 35.98           C
ANISOU  619  CB  LEU A 163     3247   4577   5845    186  -1583  -1112       C
ATOM    620  CG  LEU A 163      42.837  30.104   1.982  1.00 36.56           C
ANISOU  620  CG  LEU A 163     3313   4389   6190    444  -1895  -1024       C
ATOM    621  CD1 LEU A 163      42.468  30.734   0.652  1.00 39.37           C
ANISOU  621  CD1 LEU A 163     3888   4452   6621    544  -2439   -854       C
ATOM    622  CD2 LEU A 163      42.276  30.922   3.132  1.00 38.17           C
ANISOU  622  CD2 LEU A 163     3019   4718   6766    582  -1913  -1461       C
ATOM    623  N   PRO A 164      41.017  26.723   4.505  1.00 37.06           N
ANISOU  623  N   PRO A 164     2838   5519   5723   -464   -826  -1764       N
ATOM    624  CA  PRO A 164      40.262  25.508   4.851  1.00 38.59           C
ANISOU  624  CA  PRO A 164     3036   5972   5656   -889   -571  -1932       C
ATOM    625  C   PRO A 164      39.331  25.023   3.753  1.00 40.51           C
ANISOU  625  C   PRO A 164     3303   6215   5874   -967   -742  -2056       C
ATOM    626  O   PRO A 164      39.057  23.818   3.683  1.00 41.19           O
ANISOU  626  O   PRO A 164     3632   6353   5666  -1327   -513  -2021       O
ATOM    627  CB  PRO A 164      39.485  25.929   6.108  1.00 41.14           C
ANISOU  627  CB  PRO A 164     2952   6657   6024  -1020   -399  -2344       C
ATOM    628  CG  PRO A 164      39.422  27.419   6.042  1.00 41.85           C
ANISOU  628  CG  PRO A 164     2828   6588   6483   -559   -636  -2468       C
ATOM    629  CD  PRO A 164      40.698  27.853   5.393  1.00 38.55           C
ANISOU  629  CD  PRO A 164     2610   5852   6186   -322   -867  -2100       C
ATOM    630  N   SER A 165      38.837  25.910   2.892  1.00 42.01           N
ANISOU  630  N   SER A 165     3282   6327   6354   -668  -1176  -2182       N
ATOM    631  CA  SER A 165      37.870  25.518   1.876  1.00 44.66           C
ANISOU  631  CA  SER A 165     3603   6722   6644   -756  -1395  -2297       C
ATOM    632  C   SER A 165      38.504  25.081   0.562  1.00 43.34           C
ANISOU  632  C   SER A 165     3996   6243   6227   -763  -1497  -1866       C
ATOM    633  O   SER A 165      37.784  24.611  -0.326  1.00 45.62           O
ANISOU  633  O   SER A 165     4332   6611   6390   -930  -1656  -1948       O
ATOM    634  CB  SER A 165      36.894  26.669   1.602  1.00 48.46           C
ANISOU  634  CB  SER A 165     3761   7183   7469   -388  -1742  -2460       C
ATOM    635  OG  SER A 165      35.987  26.843   2.678  1.00 51.29           O
ANISOU  635  OG  SER A 165     3741   7813   7933   -407  -1475  -2865       O
ATOM    636  N   LEU A 166      39.816  25.211   0.413  1.00 40.31           N
ANISOU  636  N   LEU A 166     4019   5556   5740   -628  -1373  -1448       N
ATOM    637  CA  LEU A 166      40.486  24.945  -0.849  1.00 39.82           C
ANISOU  637  CA  LEU A 166     4455   5241   5433   -662  -1418  -1107       C
ATOM    638  C   LEU A 166      41.416  23.746  -0.739  1.00 37.85           C
ANISOU  638  C   LEU A 166     4608   4852   4923   -833   -925   -919       C
ATOM    639  O   LEU A 166      41.855  23.383   0.358  1.00 36.37           O
ANISOU  639  O   LEU A 166     4379   4672   4767   -832   -640   -895       O
ATOM    640  CB  LEU A 166      41.284  26.176  -1.299  1.00 39.24           C
ANISOU  640  CB  LEU A 166     4509   4930   5470   -396  -1710   -834       C
ATOM    641  CG  LEU A 166      40.443  27.426  -1.556  1.00 42.30           C
ANISOU  641  CG  LEU A 166     4591   5291   6188   -166  -2322   -957       C
ATOM    642  CD1 LEU A 166      41.311  28.556  -2.084  1.00 42.38           C
ANISOU  642  CD1 LEU A 166     4887   4980   6234     -8  -2614   -607       C
ATOM    643  CD2 LEU A 166      39.307  27.114  -2.520  1.00 45.99           C
ANISOU  643  CD2 LEU A 166     5013   5883   6578   -308  -2683  -1080       C
ATOM    644  N   PRO A 167      41.733  23.091  -1.867  1.00 38.58           N
ANISOU  644  N   PRO A 167     5094   4803   4763   -993   -838   -804       N
ATOM    645  CA  PRO A 167      42.696  21.980  -1.829  1.00 37.68           C
ANISOU  645  CA  PRO A 167     5328   4473   4515  -1071   -398   -691       C
ATOM    646  C   PRO A 167      44.114  22.443  -1.522  1.00 35.54           C
ANISOU  646  C   PRO A 167     5122   4044   4337   -807   -270   -462       C
ATOM    647  O   PRO A 167      44.349  23.627  -1.263  1.00 34.43           O
ANISOU  647  O   PRO A 167     4795   3961   4327   -615   -487   -375       O
ATOM    648  CB  PRO A 167      42.587  21.368  -3.232  1.00 39.89           C
ANISOU  648  CB  PRO A 167     5938   4694   4526  -1327   -359   -743       C
ATOM    649  CG  PRO A 167      42.012  22.449  -4.084  1.00 41.36           C
ANISOU  649  CG  PRO A 167     6033   5031   4650  -1338   -837   -710       C
ATOM    650  CD  PRO A 167      41.100  23.228  -3.191  1.00 41.26           C
ANISOU  650  CD  PRO A 167     5550   5196   4931  -1152  -1151   -834       C
ATOM    651  N   GLY A 168      45.063  21.515  -1.570  1.00 35.60           N
ANISOU  651  N   GLY A 168     5375   3837   4313   -794     67   -402       N
ATOM    652  CA  GLY A 168      46.381  21.727  -1.013  1.00 34.19           C
ANISOU  652  CA  GLY A 168     5162   3553   4274   -535    211   -241       C
ATOM    653  C   GLY A 168      47.244  22.697  -1.803  1.00 33.90           C
ANISOU  653  C   GLY A 168     5153   3554   4173   -468    160   -167       C
ATOM    654  O   GLY A 168      46.809  23.394  -2.721  1.00 34.79           O
ANISOU  654  O   GLY A 168     5344   3751   4122   -621    -65   -167       O
ATOM    655  N   HIS A 169      48.516  22.728  -1.411  1.00 34.46           N
ANISOU  655  N   HIS A 169     5168   3567   4360   -271    348    -91       N
ATOM    656  CA  HIS A 169      49.521  23.638  -1.939  1.00 35.51           C
ANISOU  656  CA  HIS A 169     5291   3780   4422   -260    371    -42       C
ATOM    657  C   HIS A 169      50.761  22.837  -2.317  1.00 36.51           C
ANISOU  657  C   HIS A 169     5458   3822   4593   -197    743   -183       C
ATOM    658  O   HIS A 169      50.819  21.618  -2.133  1.00 36.70           O
ANISOU  658  O   HIS A 169     5533   3646   4764    -96    923   -291       O
ATOM    659  CB  HIS A 169      49.872  24.720  -0.913  1.00 33.64           C
ANISOU  659  CB  HIS A 169     4798   3648   4336    -78    213    107       C
ATOM    660  CG  HIS A 169      50.356  24.167   0.389  1.00 31.03           C
ANISOU  660  CG  HIS A 169     4273   3304   4213    148    327    163       C
ATOM    661  ND1 HIS A 169      49.532  23.999   1.480  1.00 29.59           N
ANISOU  661  ND1 HIS A 169     3971   3167   4106    159    208    198       N
ATOM    662  CD2 HIS A 169      51.576  23.720   0.767  1.00 31.21           C
ANISOU  662  CD2 HIS A 169     4200   3293   4365    336    515    188       C
ATOM    663  CE1 HIS A 169      50.225  23.484   2.479  1.00 29.78           C
ANISOU  663  CE1 HIS A 169     3907   3170   4237    298    290    311       C
ATOM    664  NE2 HIS A 169      51.469  23.305   2.072  1.00 30.77           N
ANISOU  664  NE2 HIS A 169     4029   3226   4437    457    441    317       N
ATOM    665  N   THR A 170      51.769  23.529  -2.835  1.00 36.66           N
ANISOU  665  N   THR A 170     5441   3978   4510   -268    855   -220       N
ATOM    666  CA  THR A 170      52.994  22.887  -3.284  1.00 38.79           C
ANISOU  666  CA  THR A 170     5642   4249   4848   -226   1238   -480       C
ATOM    667  C   THR A 170      54.199  23.493  -2.573  1.00 38.39           C
ANISOU  667  C   THR A 170     5273   4346   4967    -15   1293   -437       C
ATOM    668  O   THR A 170      54.102  24.514  -1.888  1.00 36.17           O
ANISOU  668  O   THR A 170     4897   4171   4677     16   1057   -202       O
ATOM    669  CB  THR A 170      53.159  23.007  -4.806  1.00 41.83           C
ANISOU  669  CB  THR A 170     6261   4779   4852   -674   1434   -706       C
ATOM    670  OG1 THR A 170      54.102  22.034  -5.257  1.00 45.38           O
ANISOU  670  OG1 THR A 170     6603   5202   5436   -626   1871  -1119       O
ATOM    671  CG2 THR A 170      53.672  24.378  -5.185  1.00 42.04           C
ANISOU  671  CG2 THR A 170     6324   5052   4597   -956   1346   -579       C
ATOM    672  N   ASP A 171      55.345  22.828  -2.746  1.00 46.66           N
ANISOU  672  N   ASP A 171     6118   5404   6205    136   1610   -727       N
ATOM    673  CA  ASP A 171      56.604  23.310  -2.183  1.00 45.06           C
ANISOU  673  CA  ASP A 171     5541   5408   6171    318   1688   -769       C
ATOM    674  C   ASP A 171      56.898  24.743  -2.613  1.00 45.88           C
ANISOU  674  C   ASP A 171     5689   5823   5919    -69   1673   -699       C
ATOM    675  O   ASP A 171      57.364  25.560  -1.810  1.00 44.40           O
ANISOU  675  O   ASP A 171     5294   5782   5795     17   1548   -539       O
ATOM    676  CB  ASP A 171      57.741  22.372  -2.606  1.00 47.21           C
ANISOU  676  CB  ASP A 171     5542   5676   6720    502   2050  -1230       C
ATOM    677  CG  ASP A 171      59.116  22.934  -2.299  1.00 48.66           C
ANISOU  677  CG  ASP A 171     5271   6190   7029    598   2180  -1394       C
ATOM    678  OD1 ASP A 171      59.436  23.107  -1.103  1.00 47.28           O
ANISOU  678  OD1 ASP A 171     4847   6019   7097    932   1934  -1145       O
ATOM    679  OD2 ASP A 171      59.883  23.188  -3.252  1.00 52.05           O
ANISOU  679  OD2 ASP A 171     5581   6920   7277    282   2541  -1799       O
ATOM    680  N   GLU A 172      56.623  25.067  -3.879  1.00 45.50           N
ANISOU  680  N   GLU A 172     5958   5865   5466   -553   1774   -800       N
ATOM    681  CA  GLU A 172      56.859  26.418  -4.378  1.00 45.32           C
ANISOU  681  CA  GLU A 172     6106   6056   5056  -1010   1700   -671       C
ATOM    682  C   GLU A 172      55.892  27.427  -3.766  1.00 44.01           C
ANISOU  682  C   GLU A 172     6114   5724   4882   -965   1209   -239       C
ATOM    683  O   GLU A 172      56.265  28.586  -3.553  1.00 42.91           O
ANISOU  683  O   GLU A 172     5989   5668   4646  -1127   1083    -89       O
ATOM    684  CB  GLU A 172      56.749  26.432  -5.903  1.00 47.92           C
ANISOU  684  CB  GLU A 172     6809   6510   4887  -1616   1871   -840       C
ATOM    685  CG  GLU A 172      57.084  27.764  -6.553  1.00 49.43           C
ANISOU  685  CG  GLU A 172     7288   6896   4597  -2219   1788   -680       C
ATOM    686  CD  GLU A 172      56.730  27.795  -8.028  1.00 53.41           C
ANISOU  686  CD  GLU A 172     8280   7504   4511  -2904   1828   -726       C
ATOM    687  OE1 GLU A 172      56.030  26.870  -8.493  1.00 53.79           O
ANISOU  687  OE1 GLU A 172     8441   7456   4541  -2872   1861   -850       O
ATOM    688  OE2 GLU A 172      57.150  28.745  -8.723  1.00 56.68           O
ANISOU  688  OE2 GLU A 172     9000   8102   4435  -3538   1815   -628       O
ATOM    689  N   ASP A 173      54.654  27.011  -3.480  1.00 40.14           N
ANISOU  689  N   ASP A 173     5733   5003   4517   -766    943    -93       N
ATOM    690  CA  ASP A 173      53.677  27.931  -2.903  1.00 38.02           C
ANISOU  690  CA  ASP A 173     5531   4595   4319   -688    493    190       C
ATOM    691  C   ASP A 173      54.109  28.405  -1.521  1.00 36.90           C
ANISOU  691  C   ASP A 173     5049   4506   4464   -390    448    259       C
ATOM    692  O   ASP A 173      53.940  29.582  -1.180  1.00 35.05           O
ANISOU  692  O   ASP A 173     4836   4233   4247   -444    194    398       O
ATOM    693  CB  ASP A 173      52.302  27.264  -2.826  1.00 37.18           C
ANISOU  693  CB  ASP A 173     5497   4325   4306   -557    287    217       C
ATOM    694  CG  ASP A 173      51.707  26.984  -4.191  1.00 39.34           C
ANISOU  694  CG  ASP A 173     6125   4573   4251   -909    232    180       C
ATOM    695  OD1 ASP A 173      51.951  27.772  -5.128  1.00 40.92           O
ANISOU  695  OD1 ASP A 173     6606   4823   4120  -1292    127    275       O
ATOM    696  OD2 ASP A 173      50.989  25.972  -4.326  1.00 39.46           O
ANISOU  696  OD2 ASP A 173     6172   4523   4297   -863    282     68       O
ATOM    697  N   VAL A 174      54.664  27.502  -0.709  1.00 38.57           N
ANISOU  697  N   VAL A 174     4965   4781   4909    -88    656    164       N
ATOM    698  CA  VAL A 174      55.078  27.869   0.643  1.00 34.90           C
ANISOU  698  CA  VAL A 174     4187   4421   4652    139    589    246       C
ATOM    699  C   VAL A 174      56.201  28.897   0.599  1.00 36.82           C
ANISOU  699  C   VAL A 174     4316   4872   4801    -32    682    217       C
ATOM    700  O   VAL A 174      56.209  29.862   1.372  1.00 35.06           O
ANISOU  700  O   VAL A 174     3993   4701   4628    -42    522    309       O
ATOM    701  CB  VAL A 174      55.491  26.614   1.434  1.00 32.18           C
ANISOU  701  CB  VAL A 174     3617   4066   4543    462    705    216       C
ATOM    702  CG1 VAL A 174      55.976  26.996   2.822  1.00 30.82           C
ANISOU  702  CG1 VAL A 174     3144   4064   4504    619    597    334       C
ATOM    703  CG2 VAL A 174      54.330  25.640   1.522  1.00 31.57           C
ANISOU  703  CG2 VAL A 174     3718   3762   4514    529    615    259       C
ATOM    704  N   LYS A 175      57.163  28.709  -0.308  1.00 40.32           N
ANISOU  704  N   LYS A 175     4760   5463   5095   -224    974     29       N
ATOM    705  CA  LYS A 175      58.283  29.640  -0.402  1.00 39.60           C
ANISOU  705  CA  LYS A 175     4549   5633   4864   -486   1117    -50       C
ATOM    706  C   LYS A 175      57.821  31.023  -0.844  1.00 40.13           C
ANISOU  706  C   LYS A 175     4996   5576   4676   -881    877    144       C
ATOM    707  O   LYS A 175      58.297  32.037  -0.323  1.00 39.35           O
ANISOU  707  O   LYS A 175     4824   5558   4570  -1003    817    197       O
ATOM    708  CB  LYS A 175      59.339  29.097  -1.362  1.00 40.86           C
ANISOU  708  CB  LYS A 175     4597   6036   4894   -686   1533   -394       C
ATOM    709  CG  LYS A 175      59.927  27.760  -0.950  1.00 42.12           C
ANISOU  709  CG  LYS A 175     4341   6239   5423   -225   1723   -638       C
ATOM    710  CD  LYS A 175      61.011  27.325  -1.923  1.00 46.99           C
ANISOU  710  CD  LYS A 175     4748   7131   5975   -423   2172  -1122       C
ATOM    711  CE  LYS A 175      61.574  25.964  -1.554  1.00 49.36           C
ANISOU  711  CE  LYS A 175     4620   7365   6771    125   2294  -1409       C
ATOM    712  NZ  LYS A 175      62.694  25.573  -2.455  1.00 55.08           N
ANISOU  712  NZ  LYS A 175     5008   8398   7521    -31   2768  -2026       N
ATOM    713  N   ASN A 176      56.897  31.084  -1.807  1.00 40.56           N
ANISOU  713  N   ASN A 176     5477   5405   4531  -1092    695    259       N
ATOM    714  CA  ASN A 176      56.342  32.371  -2.213  1.00 40.50           C
ANISOU  714  CA  ASN A 176     5874   5159   4354  -1401    321    504       C
ATOM    715  C   ASN A 176      55.621  33.048  -1.055  1.00 38.75           C
ANISOU  715  C   ASN A 176     5510   4726   4487  -1068    -24    619       C
ATOM    716  O   ASN A 176      55.706  34.271  -0.890  1.00 38.92           O
ANISOU  716  O   ASN A 176     5675   4594   4518  -1234   -240    727       O
ATOM    717  CB  ASN A 176      55.392  32.189  -3.397  1.00 41.59           C
ANISOU  717  CB  ASN A 176     6459   5099   4245  -1631     91    630       C
ATOM    718  CG  ASN A 176      56.121  31.872  -4.686  1.00 44.25           C
ANISOU  718  CG  ASN A 176     7041   5670   4103  -2172    419    500       C
ATOM    719  OD1 ASN A 176      57.271  32.268  -4.877  1.00 46.63           O
ANISOU  719  OD1 ASN A 176     7299   6228   4189  -2523    721    372       O
ATOM    720  ND2 ASN A 176      55.451  31.160  -5.584  1.00 45.43           N
ANISOU  720  ND2 ASN A 176     7426   5781   4053  -2305    391    478       N
ATOM    721  N   ALA A 177      54.909  32.266  -0.240  1.00 38.71           N
ANISOU  721  N   ALA A 177     5233   4709   4768   -649    -59    559       N
ATOM    722  CA  ALA A 177      54.197  32.836   0.899  1.00 36.64           C
ANISOU  722  CA  ALA A 177     4771   4336   4814   -397   -311    557       C
ATOM    723  C   ALA A 177      55.164  33.430   1.915  1.00 38.31           C
ANISOU  723  C   ALA A 177     4703   4750   5102   -397   -165    492       C
ATOM    724  O   ALA A 177      54.900  34.495   2.486  1.00 37.85           O
ANISOU  724  O   ALA A 177     4623   4559   5200   -407   -369    471       O
ATOM    725  CB  ALA A 177      53.317  31.772   1.552  1.00 33.94           C
ANISOU  725  CB  ALA A 177     4209   4032   4654    -91   -305    475       C
ATOM    726  N   VAL A 178      56.293  32.758   2.152  1.00 42.47           N
ANISOU  726  N   VAL A 178     4988   5594   5554   -376    169    421       N
ATOM    727  CA  VAL A 178      57.279  33.278   3.094  1.00 40.84           C
ANISOU  727  CA  VAL A 178     4477   5652   5388   -403    287    355       C
ATOM    728  C   VAL A 178      57.894  34.567   2.564  1.00 43.05           C
ANISOU  728  C   VAL A 178     4976   5888   5491   -810    280    366       C
ATOM    729  O   VAL A 178      58.145  35.510   3.324  1.00 42.77           O
ANISOU  729  O   VAL A 178     4840   5881   5529   -897    217    327       O
ATOM    730  CB  VAL A 178      58.350  32.211   3.386  1.00 36.65           C
ANISOU  730  CB  VAL A 178     3596   5458   4873   -240    565    268       C
ATOM    731  CG1 VAL A 178      59.409  32.760   4.327  1.00 33.05           C
ANISOU  731  CG1 VAL A 178     2787   5338   4434   -294    642    200       C
ATOM    732  CG2 VAL A 178      57.709  30.971   3.979  1.00 32.33           C
ANISOU  732  CG2 VAL A 178     2937   4851   4496    113    502    323       C
ATOM    733  N   GLY A 179      58.139  34.633   1.254  1.00 41.39           N
ANISOU  733  N   GLY A 179     5107   5612   5007  -1140    351    410       N
ATOM    734  CA  GLY A 179      58.677  35.852   0.676  1.00 41.97           C
ANISOU  734  CA  GLY A 179     5505   5607   4833  -1649    317    471       C
ATOM    735  C   GLY A 179      57.725  37.024   0.804  1.00 42.78           C
ANISOU  735  C   GLY A 179     5949   5211   5095  -1673   -145    642       C
ATOM    736  O   GLY A 179      58.148  38.158   1.041  1.00 43.57           O
ANISOU  736  O   GLY A 179     6179   5196   5178  -1945   -220    658       O
ATOM    737  N   VAL A 180      56.424  36.767   0.655  1.00 41.95           N
ANISOU  737  N   VAL A 180     5966   4786   5187  -1380   -474    731       N
ATOM    738  CA  VAL A 180      55.436  37.828   0.818  1.00 41.98           C
ANISOU  738  CA  VAL A 180     6188   4285   5477  -1286   -969    811       C
ATOM    739  C   VAL A 180      55.376  38.284   2.270  1.00 41.89           C
ANISOU  739  C   VAL A 180     5760   4330   5828  -1026   -941    576       C
ATOM    740  O   VAL A 180      55.315  39.486   2.555  1.00 42.74           O
ANISOU  740  O   VAL A 180     6003   4112   6122  -1120  -1170    542       O
ATOM    741  CB  VAL A 180      54.060  37.360   0.312  1.00 41.04           C
ANISOU  741  CB  VAL A 180     6184   3903   5508  -1019  -1322    884       C
ATOM    742  CG1 VAL A 180      52.985  38.381   0.661  1.00 41.74           C
ANISOU  742  CG1 VAL A 180     6317   3494   6048   -781  -1854    848       C
ATOM    743  CG2 VAL A 180      54.103  37.121  -1.188  1.00 42.45           C
ANISOU  743  CG2 VAL A 180     6859   4006   5263  -1393  -1412   1132       C
ATOM    744  N   LEU A 181      55.400  37.335   3.209  1.00 44.39           N
ANISOU  744  N   LEU A 181     5597   5041   6228   -743   -674    406       N
ATOM    745  CA  LEU A 181      55.340  37.693   4.623  1.00 43.66           C
ANISOU  745  CA  LEU A 181     5113   5096   6379   -595   -622    168       C
ATOM    746  C   LEU A 181      56.590  38.448   5.058  1.00 45.04           C
ANISOU  746  C   LEU A 181     5221   5473   6420   -897   -423    115       C
ATOM    747  O   LEU A 181      56.495  39.450   5.775  1.00 45.31           O
ANISOU  747  O   LEU A 181     5193   5371   6651   -955   -517    -61       O
ATOM    748  CB  LEU A 181      55.148  36.440   5.475  1.00 38.51           C
ANISOU  748  CB  LEU A 181     4061   4837   5734   -343   -418     82       C
ATOM    749  CG  LEU A 181      55.084  36.672   6.985  1.00 33.04           C
ANISOU  749  CG  LEU A 181     2973   4406   5172   -299   -341   -157       C
ATOM    750  CD1 LEU A 181      53.871  37.515   7.350  1.00 32.74           C
ANISOU  750  CD1 LEU A 181     2892   4062   5487   -199   -591   -434       C
ATOM    751  CD2 LEU A 181      55.071  35.352   7.734  1.00 29.29           C
ANISOU  751  CD2 LEU A 181     2226   4316   4588   -167   -177   -124       C
ATOM    752  N   ILE A 182      57.768  37.985   4.636  1.00 49.99           N
ANISOU  752  N   ILE A 182     5820   6442   6734  -1105   -131    200       N
ATOM    753  CA  ILE A 182      59.010  38.656   5.010  1.00 48.98           C
ANISOU  753  CA  ILE A 182     5569   6592   6451  -1437     79    110       C
ATOM    754  C   ILE A 182      59.080  40.042   4.381  1.00 51.66           C
ANISOU  754  C   ILE A 182     6394   6498   6735  -1850   -102    178       C
ATOM    755  O   ILE A 182      59.388  41.032   5.055  1.00 52.16           O
ANISOU  755  O   ILE A 182     6425   6507   6885  -2036   -116     40       O
ATOM    756  CB  ILE A 182      60.226  37.798   4.618  1.00 46.00           C
ANISOU  756  CB  ILE A 182     4967   6707   5804  -1543    427    100       C
ATOM    757  CG1 ILE A 182      60.319  36.565   5.517  1.00 40.85           C
ANISOU  757  CG1 ILE A 182     3825   6421   5276  -1126    524     51       C
ATOM    758  CG2 ILE A 182      61.505  38.613   4.698  1.00 44.98           C
ANISOU  758  CG2 ILE A 182     4755   6870   5467  -1999    639    -20       C
ATOM    759  CD1 ILE A 182      61.526  35.700   5.242  1.00 38.03           C
ANISOU  759  CD1 ILE A 182     3148   6499   4802  -1110    802    -27       C
ATOM    760  N   GLY A 183      58.795  40.132   3.080  1.00 49.49           N
ANISOU  760  N   GLY A 183     6624   5889   6293  -2047   -268    403       N
ATOM    761  CA  GLY A 183      58.832  41.423   2.413  1.00 50.65           C
ANISOU  761  CA  GLY A 183     7354   5540   6349  -2495   -533    561       C
ATOM    762  C   GLY A 183      57.848  42.416   3.000  1.00 51.55           C
ANISOU  762  C   GLY A 183     7585   5056   6944  -2253   -968    499       C
ATOM    763  O   GLY A 183      58.175  43.590   3.190  1.00 53.15           O
ANISOU  763  O   GLY A 183     8035   4948   7213  -2555  -1081    468       O
ATOM    764  N   GLY A 184      56.631  41.960   3.301  1.00 53.50           N
ANISOU  764  N   GLY A 184     7632   5134   7560  -1722  -1204    422       N
ATOM    765  CA  GLY A 184      55.651  42.843   3.908  1.00 53.85           C
ANISOU  765  CA  GLY A 184     7650   4662   8150  -1433  -1585    221       C
ATOM    766  C   GLY A 184      55.985  43.213   5.338  1.00 54.74           C
ANISOU  766  C   GLY A 184     7291   5051   8457  -1390  -1319   -180       C
ATOM    767  O   GLY A 184      55.683  44.325   5.782  1.00 55.86           O
ANISOU  767  O   GLY A 184     7507   4746   8973  -1386  -1537   -400       O
ATOM    768  N   LEU A 185      56.609  42.295   6.078  1.00 57.30           N
ANISOU  768  N   LEU A 185     7139   6090   8542  -1370   -878   -288       N
ATOM    769  CA  LEU A 185      56.988  42.588   7.456  1.00 56.94           C
ANISOU  769  CA  LEU A 185     6655   6404   8574  -1417   -636   -635       C
ATOM    770  C   LEU A 185      58.189  43.524   7.522  1.00 58.91           C
ANISOU  770  C   LEU A 185     7060   6703   8619  -1910   -482   -651       C
ATOM    771  O   LEU A 185      58.295  44.328   8.455  1.00 58.99           O
ANISOU  771  O   LEU A 185     6907   6706   8800  -2030   -429   -972       O
ATOM    772  CB  LEU A 185      57.282  41.287   8.200  1.00 52.62           C
ANISOU  772  CB  LEU A 185     5616   6571   7808  -1268   -323   -657       C
ATOM    773  CG  LEU A 185      56.550  41.022   9.516  1.00 47.12           C
ANISOU  773  CG  LEU A 185     4472   6134   7296  -1072   -268   -991       C
ATOM    774  CD1 LEU A 185      55.070  41.320   9.380  1.00 47.65           C
ANISOU  774  CD1 LEU A 185     4586   5717   7801   -779   -558  -1206       C
ATOM    775  CD2 LEU A 185      56.764  39.578   9.948  1.00 40.07           C
ANISOU  775  CD2 LEU A 185     3283   5804   6139   -948    -81   -841       C
ATOM    776  N   GLU A 186      59.095  43.443   6.544  1.00 62.34           N
ANISOU  776  N   GLU A 186     7794   7224   8669  -2262   -375   -366       N
ATOM    777  CA  GLU A 186      60.274  44.299   6.530  1.00 62.24           C
ANISOU  777  CA  GLU A 186     7926   7322   8399  -2830   -191   -402       C
ATOM    778  C   GLU A 186      59.977  45.713   6.051  1.00 65.21           C
ANISOU  778  C   GLU A 186     8931   6888   8956  -3126   -535   -343       C
ATOM    779  O   GLU A 186      60.794  46.612   6.281  1.00 66.00           O
ANISOU  779  O   GLU A 186     9166   6983   8927  -3617   -408   -449       O
ATOM    780  CB  GLU A 186      61.367  43.683   5.653  1.00 60.45           C
ANISOU  780  CB  GLU A 186     7736   7554   7678  -3171     99   -213       C
ATOM    781  CG  GLU A 186      62.048  42.471   6.267  1.00 56.27           C
ANISOU  781  CG  GLU A 186     6539   7827   7012  -2944    441   -330       C
ATOM    782  CD  GLU A 186      63.187  41.948   5.413  1.00 54.48           C
ANISOU  782  CD  GLU A 186     6250   8056   6393  -3266    752   -289       C
ATOM    783  OE1 GLU A 186      63.268  42.334   4.228  1.00 56.63           O
ANISOU  783  OE1 GLU A 186     7043   8050   6426  -3675    725   -134       O
ATOM    784  OE2 GLU A 186      64.003  41.153   5.927  1.00 50.25           O
ANISOU  784  OE2 GLU A 186     5136   8165   5790  -3133   1004   -436       O
ATOM    785  N   ARG A 187      58.838  45.935   5.389  1.00 68.98           N
ANISOU  785  N   ARG A 187     9807   6658   9744  -2851  -1009   -170       N
ATOM    786  CA  ARG A 187      58.481  47.285   4.968  1.00 70.72           C
ANISOU  786  CA  ARG A 187    10656   5979  10235  -3054  -1467    -80       C
ATOM    787  C   ARG A 187      58.200  48.200   6.151  1.00 72.65           C
ANISOU  787  C   ARG A 187    10665   5950  10988  -2914  -1508   -551       C
ATOM    788  O   ARG A 187      58.199  49.424   5.986  1.00 74.52           O
ANISOU  788  O   ARG A 187    11363   5516  11435  -3121  -1770   -551       O
ATOM    789  CB  ARG A 187      57.269  47.249   4.036  1.00 69.91           C
ANISOU  789  CB  ARG A 187    10956   5197  10409  -2707  -2059    207       C
ATOM    790  CG  ARG A 187      57.564  46.659   2.665  1.00 68.29           C
ANISOU  790  CG  ARG A 187    11159   5158   9628  -2993  -2063    684       C
ATOM    791  CD  ARG A 187      56.290  46.424   1.865  1.00 67.68           C
ANISOU  791  CD  ARG A 187    11264   4703   9749  -2519  -2572    911       C
ATOM    792  NE  ARG A 187      56.541  45.649   0.651  1.00 67.01           N
ANISOU  792  NE  ARG A 187    11461   4924   9078  -2800  -2503   1267       N
ATOM    793  CZ  ARG A 187      55.588  45.190  -0.154  1.00 67.06           C
ANISOU  793  CZ  ARG A 187    11590   4801   9089  -2518  -2865   1465       C
ATOM    794  NH1 ARG A 187      54.313  45.424   0.125  1.00 67.95           N
ANISOU  794  NH1 ARG A 187    11520   4524   9775  -1922  -3326   1345       N
ATOM    795  NH2 ARG A 187      55.908  44.494  -1.236  1.00 67.08           N
ANISOU  795  NH2 ARG A 187    11838   5136   8514  -2856  -2738   1708       N
ATOM    796  N   ASN A 188      57.965  47.636   7.335  1.00 67.72           N
ANISOU  796  N   ASN A 188     9329   5876  10524  -2569  -1217   -962       N
ATOM    797  CA  ASN A 188      57.764  48.405   8.556  1.00 68.91           C
ANISOU  797  CA  ASN A 188     9167   5942  11074  -2521  -1143  -1511       C
ATOM    798  C   ASN A 188      58.984  48.337   9.471  1.00 68.65           C
ANISOU  798  C   ASN A 188     8756   6709  10619  -2953   -619  -1712       C
ATOM    799  O   ASN A 188      58.860  48.462  10.692  1.00 66.61           O
ANISOU  799  O   ASN A 188     8024   6771  10514  -2904   -416  -2186       O
ATOM    800  CB  ASN A 188      56.514  47.924   9.290  1.00 66.79           C
ANISOU  800  CB  ASN A 188     8376   5741  11262  -1928  -1212  -1904       C
ATOM    801  CG  ASN A 188      55.254  48.085   8.459  1.00 66.37           C
ANISOU  801  CG  ASN A 188     8601   4906  11713  -1467  -1782  -1796       C
ATOM    802  OD1 ASN A 188      54.598  47.102   8.106  1.00 64.22           O
ANISOU  802  OD1 ASN A 188     8162   4840  11400  -1130  -1851  -1644       O
ATOM    803  ND2 ASN A 188      54.908  49.329   8.144  1.00 69.55           N
ANISOU  803  ND2 ASN A 188     9419   4557  12451  -1401  -2136  -1800       N
ATOM    804  N   ASP A 189      60.164  48.124   8.885  1.00 78.89           N
ANISOU  804  N   ASP A 189    13641   6386   9946  -4366    915  -1006       N
ATOM    805  CA  ASP A 189      61.438  48.150   9.607  1.00 82.12           C
ANISOU  805  CA  ASP A 189    13636   7012  10553  -4881    742  -1466       C
ATOM    806  C   ASP A 189      61.498  47.073  10.689  1.00 77.48           C
ANISOU  806  C   ASP A 189    12533   7056   9851  -4414    552  -1836       C
ATOM    807  O   ASP A 189      62.004  47.300  11.789  1.00 80.46           O
ANISOU  807  O   ASP A 189    12892   7430  10249  -4431    241  -2320       O
ATOM    808  CB  ASP A 189      61.709  49.534  10.202  1.00 89.94           C
ANISOU  808  CB  ASP A 189    15111   7323  11738  -5041    471  -1695       C
ATOM    809  CG  ASP A 189      61.573  50.644   9.179  1.00 95.52           C
ANISOU  809  CG  ASP A 189    16282   7440  12570  -5279    644  -1229       C
ATOM    810  OD1 ASP A 189      61.754  50.370   7.974  1.00 94.84           O
ANISOU  810  OD1 ASP A 189    15977   7628  12429  -5507    971   -780       O
ATOM    811  OD2 ASP A 189      61.283  51.791   9.579  1.00101.27           O
ANISOU  811  OD2 ASP A 189    17607   7445  13428  -5191    447  -1327       O
ATOM    812  N   ASN A 190      60.984  45.888  10.376  1.00 70.98           N
ANISOU  812  N   ASN A 190    11282   6785   8901  -3942    715  -1599       N
ATOM    813  CA  ASN A 190      61.060  44.747  11.277  1.00 67.05           C
ANISOU  813  CA  ASN A 190    10260   6897   8318  -3469    600  -1809       C
ATOM    814  C   ASN A 190      62.208  43.835  10.870  1.00 66.20           C
ANISOU  814  C   ASN A 190     9377   7439   8335  -3874    669  -1911       C
ATOM    815  O   ASN A 190      62.461  43.625   9.681  1.00 65.70           O
ANISOU  815  O   ASN A 190     9099   7522   8343  -4229    923  -1674       O
ATOM    816  CB  ASN A 190      59.751  43.954  11.286  1.00 61.47           C
ANISOU  816  CB  ASN A 190     9533   6325   7497  -2693    731  -1493       C
ATOM    817  CG  ASN A 190      58.649  44.652  12.057  1.00 62.62           C
ANISOU  817  CG  ASN A 190    10282   6025   7487  -2104    652  -1481       C
ATOM    818  OD1 ASN A 190      58.704  44.758  13.282  1.00 64.37           O
ANISOU  818  OD1 ASN A 190    10619   6291   7549  -1775    474  -1774       O
ATOM    819  ND2 ASN A 190      57.631  45.117  11.342  1.00 62.27           N
ANISOU  819  ND2 ASN A 190    10618   5599   7444  -1896    774  -1157       N
ATOM    820  N   THR A 191      62.898  43.292  11.869  1.00 66.70           N
ANISOU  820  N   THR A 191     9038   7928   8377  -3746    434  -2275       N
ATOM    821  CA  THR A 191      63.989  42.344  11.651  1.00 66.37           C
ANISOU  821  CA  THR A 191     8215   8554   8449  -3979    448  -2426       C
ATOM    822  C   THR A 191      63.401  40.939  11.704  1.00 60.47           C
ANISOU  822  C   THR A 191     7143   8200   7633  -3307    547  -2210       C
ATOM    823  O   THR A 191      63.203  40.374  12.782  1.00 59.41           O
ANISOU  823  O   THR A 191     6955   8249   7368  -2748    380  -2294       O
ATOM    824  CB  THR A 191      65.086  42.542  12.691  1.00 71.29           C
ANISOU  824  CB  THR A 191     8565   9423   9099  -4170     72  -2957       C
ATOM    825  OG1 THR A 191      65.648  43.850  12.541  1.00 77.76           O
ANISOU  825  OG1 THR A 191     9646   9791  10107  -4826    -21  -3116       O
ATOM    826  CG2 THR A 191      66.184  41.504  12.526  1.00 71.38           C
ANISOU  826  CG2 THR A 191     7723  10175   9222  -4267     59  -3114       C
ATOM    827  N   VAL A 192      63.113  40.375  10.536  1.00 58.34           N
ANISOU  827  N   VAL A 192     6685   8036   7446  -3350    819  -1926       N
ATOM    828  CA  VAL A 192      62.458  39.077  10.428  1.00 53.51           C
ANISOU  828  CA  VAL A 192     5799   7657   6878  -2787    905  -1728       C
ATOM    829  C   VAL A 192      63.516  38.000  10.249  1.00 53.68           C
ANISOU  829  C   VAL A 192     5121   8264   7011  -2840    890  -1927       C
ATOM    830  O   VAL A 192      64.460  38.159   9.464  1.00 56.29           O
ANISOU  830  O   VAL A 192     5170   8837   7380  -3309    983  -2046       O
ATOM    831  CB  VAL A 192      61.446  39.059   9.266  1.00 50.97           C
ANISOU  831  CB  VAL A 192     5688   7095   6582  -2722   1116  -1395       C
ATOM    832  CG1 VAL A 192      60.698  37.735   9.227  1.00 46.95           C
ANISOU  832  CG1 VAL A 192     4878   6733   6226  -2181   1151  -1245       C
ATOM    833  CG2 VAL A 192      60.476  40.218   9.395  1.00 52.07           C
ANISOU  833  CG2 VAL A 192     6509   6662   6611  -2643   1111  -1214       C
ATOM    834  N   ARG A 193      63.358  36.898  10.977  1.00 54.88           N
ANISOU  834  N   ARG A 193     5023   8622   7208  -2282    796  -1910       N
ATOM    835  CA  ARG A 193      64.266  35.765  10.901  1.00 53.86           C
ANISOU  835  CA  ARG A 193     4271   8994   7200  -2170    746  -2086       C
ATOM    836  C   ARG A 193      63.458  34.482  10.769  1.00 50.33           C
ANISOU  836  C   ARG A 193     3706   8479   6938  -1630    832  -1839       C
ATOM    837  O   ARG A 193      62.298  34.413  11.186  1.00 49.39           O
ANISOU  837  O   ARG A 193     3910   8009   6847  -1283    888  -1543       O
ATOM    838  CB  ARG A 193      65.171  35.701  12.137  1.00 57.81           C
ANISOU  838  CB  ARG A 193     4562   9813   7589  -2018    447  -2370       C
ATOM    839  CG  ARG A 193      66.469  34.940  11.933  1.00 59.76           C
ANISOU  839  CG  ARG A 193     4193  10586   7926  -2030    351  -2626       C
ATOM    840  CD  ARG A 193      67.333  35.001  13.184  1.00 63.94           C
ANISOU  840  CD  ARG A 193     4449  11514   8332  -1896    -32  -2985       C
ATOM    841  NE  ARG A 193      67.568  36.376  13.621  1.00 67.43           N
ANISOU  841  NE  ARG A 193     5178  11791   8652  -2357   -207  -3226       N
ATOM    842  CZ  ARG A 193      68.648  37.088  13.315  1.00 72.33           C
ANISOU  842  CZ  ARG A 193     5684  12444   9355  -2822   -243  -3396       C
ATOM    843  NH1 ARG A 193      69.607  36.559  12.566  1.00 74.22           N
ANISOU  843  NH1 ARG A 193     5570  12920   9710  -2833    -96  -3337       N
ATOM    844  NH2 ARG A 193      68.772  38.331  13.760  1.00 76.14           N
ANISOU  844  NH2 ARG A 193     6456  12661   9813  -3228   -430  -3607       N
ATOM    845  N   VAL A 194      64.075  33.467  10.172  1.00 54.20           N
ANISOU  845  N   VAL A 194     3871   9178   7545  -1492    813  -1902       N
ATOM    846  CA  VAL A 194      63.451  32.159  10.020  1.00 51.84           C
ANISOU  846  CA  VAL A 194     3515   8695   7486  -1018    820  -1694       C
ATOM    847  C   VAL A 194      64.111  31.194  10.992  1.00 54.95           C
ANISOU  847  C   VAL A 194     3620   9311   7947   -605    667  -1746       C
ATOM    848  O   VAL A 194      65.258  31.387  11.410  1.00 58.32           O
ANISOU  848  O   VAL A 194     3838  10111   8210   -677    513  -2007       O
ATOM    849  CB  VAL A 194      63.545  31.634   8.571  1.00 50.89           C
ANISOU  849  CB  VAL A 194     3438   8500   7400  -1056    847  -1701       C
ATOM    850  CG1 VAL A 194      62.837  32.580   7.617  1.00 50.08           C
ANISOU  850  CG1 VAL A 194     3602   8244   7184  -1373    983  -1632       C
ATOM    851  CG2 VAL A 194      64.997  31.451   8.164  1.00 53.93           C
ANISOU  851  CG2 VAL A 194     3608   9243   7639  -1157    799  -1954       C
ATOM    852  N   SER A 195      63.372  30.152  11.360  1.00 53.64           N
ANISOU  852  N   SER A 195     3441   8897   8045   -158    703  -1473       N
ATOM    853  CA  SER A 195      63.892  29.165  12.291  1.00 57.90           C
ANISOU  853  CA  SER A 195     3766   9580   8654    324    581  -1424       C
ATOM    854  C   SER A 195      64.943  28.290  11.608  1.00 58.14           C
ANISOU  854  C   SER A 195     3633   9717   8740    356    450  -1604       C
ATOM    855  O   SER A 195      65.165  28.360  10.396  1.00 54.92           O
ANISOU  855  O   SER A 195     3276   9283   8309     70    489  -1751       O
ATOM    856  CB  SER A 195      62.760  28.300  12.847  1.00 59.23           C
ANISOU  856  CB  SER A 195     4005   9355   9145    772    733   -986       C
ATOM    857  OG  SER A 195      62.162  27.524  11.825  1.00 54.80           O
ANISOU  857  OG  SER A 195     3520   8409   8892    691    776   -858       O
ATOM    858  N   GLU A 196      65.597  27.452  12.413  1.00 71.65           N
ANISOU  858  N   GLU A 196     7577   8725  10921  -1506  -4505    253       N
ATOM    859  CA  GLU A 196      66.639  26.583  11.878  1.00 79.85           C
ANISOU  859  CA  GLU A 196     7111  10058  13172  -1256  -4100     -6       C
ATOM    860  C   GLU A 196      66.057  25.546  10.924  1.00 77.54           C
ANISOU  860  C   GLU A 196     6499   9920  13043   -813  -2915   -703       C
ATOM    861  O   GLU A 196      66.671  25.222   9.902  1.00 82.45           O
ANISOU  861  O   GLU A 196     6037  11051  14238   -837  -2150  -1069       O
ATOM    862  CB  GLU A 196      67.391  25.908  13.025  1.00 85.94           C
ANISOU  862  CB  GLU A 196     7509  10297  14846   -833  -4960    398       C
ATOM    863  CG  GLU A 196      68.713  25.273  12.627  1.00 96.10           C
ANISOU  863  CG  GLU A 196     7191  11923  17401   -674  -4733    396       C
ATOM    864  CD  GLU A 196      69.438  24.663  13.811  1.00101.99           C
ANISOU  864  CD  GLU A 196     7698  12165  18890   -305  -5490    879       C
ATOM    865  OE1 GLU A 196      70.629  24.982  14.015  1.00110.12           O
ANISOU  865  OE1 GLU A 196     8154  13416  20271   -586  -5766   1341       O
ATOM    866  OE2 GLU A 196      68.811  23.871  14.544  1.00 98.50           O
ANISOU  866  OE2 GLU A 196     7848  11117  18460    253  -5614    789       O
ATOM    867  N   THR A 197      64.868  25.024  11.234  1.00 70.34           N
ANISOU  867  N   THR A 197     6558   8570  11598   -416  -2754   -857       N
ATOM    868  CA  THR A 197      64.239  24.048  10.350  1.00 68.60           C
ANISOU  868  CA  THR A 197     6184   8456  11424    -72  -1689  -1475       C
ATOM    869  C   THR A 197      63.760  24.697   9.058  1.00 64.99           C
ANISOU  869  C   THR A 197     5780   8667  10248   -640   -787  -1816       C
ATOM    870  O   THR A 197      63.900  24.115   7.977  1.00 66.62           O
ANISOU  870  O   THR A 197     5292   9234  10786   -595    166  -2351       O
ATOM    871  CB  THR A 197      63.078  23.357  11.065  1.00 64.66           C
ANISOU  871  CB  THR A 197     6727   7336  10505    454  -1853  -1437       C
ATOM    872  OG1 THR A 197      62.262  24.341  11.712  1.00 54.30           O
ANISOU  872  OG1 THR A 197     6657   5838   8138    187  -2425   -963       O
ATOM    873  CG2 THR A 197      63.597  22.372  12.100  1.00 65.98           C
ANISOU  873  CG2 THR A 197     6563   6902  11604   1121  -2480  -1283       C
ATOM    874  N   LEU A 198      63.186  25.900   9.147  1.00 83.60           N
ANISOU  874  N   LEU A 198     8985  11181  11599  -1174  -1043  -1504       N
ATOM    875  CA  LEU A 198      62.784  26.610   7.937  1.00 75.16           C
ANISOU  875  CA  LEU A 198     7896  10797   9864  -1771   -216  -1773       C
ATOM    876  C   LEU A 198      63.987  26.966   7.077  1.00 75.32           C
ANISOU  876  C   LEU A 198     6636  11460  10522  -2151     81  -1971       C
ATOM    877  O   LEU A 198      63.896  26.954   5.843  1.00 66.00           O
ANISOU  877  O   LEU A 198     4969  10851   9259  -2414   1038  -2430       O
ATOM    878  CB  LEU A 198      62.000  27.872   8.297  1.00 60.73           C
ANISOU  878  CB  LEU A 198     7234   8983   6858  -2233   -589  -1313       C
ATOM    879  CG  LEU A 198      60.489  27.715   8.467  1.00 41.04           C
ANISOU  879  CG  LEU A 198     5966   6226   3402  -2048   -313  -1196       C
ATOM    880  CD1 LEU A 198      59.863  29.019   8.944  1.00 32.52           C
ANISOU  880  CD1 LEU A 198     5465   4762   2129  -1826   -450   -363       C
ATOM    881  CD2 LEU A 198      59.854  27.255   7.161  1.00 35.41           C
ANISOU  881  CD2 LEU A 198     4860   5844   2748  -2043    813  -1494       C
ATOM    882  N   GLN A 199      65.122  27.277   7.706  1.00 68.72           N
ANISOU  882  N   GLN A 199     5233  10555  10323  -2196   -738  -1582       N
ATOM    883  CA  GLN A 199      66.328  27.613   6.962  1.00 76.21           C
ANISOU  883  CA  GLN A 199     4904  12130  11924  -2522   -544  -1634       C
ATOM    884  C   GLN A 199      66.895  26.413   6.217  1.00 82.51           C
ANISOU  884  C   GLN A 199     4579  13075  13697  -2028    287  -2118       C
ATOM    885  O   GLN A 199      67.706  26.591   5.301  1.00 87.88           O
ANISOU  885  O   GLN A 199     4747  14109  14533  -2062    694  -1990       O
ATOM    886  CB  GLN A 199      67.376  28.194   7.912  1.00 82.27           C
ANISOU  886  CB  GLN A 199     5397  12752  13110  -2708  -1716   -968       C
ATOM    887  CG  GLN A 199      68.470  29.003   7.236  1.00 88.34           C
ANISOU  887  CG  GLN A 199     5291  14079  14197  -3161  -1719   -737       C
ATOM    888  CD  GLN A 199      69.322  29.765   8.230  1.00 93.19           C
ANISOU  888  CD  GLN A 199     6089  14523  14796  -3361  -2784   -207       C
ATOM    889  OE1 GLN A 199      69.010  29.816   9.421  1.00 91.23           O
ANISOU  889  OE1 GLN A 199     6714  13694  14253  -3286  -3611    217       O
ATOM    890  NE2 GLN A 199      70.406  30.364   7.747  1.00 99.76           N
ANISOU  890  NE2 GLN A 199     6294  15710  15901  -3530  -2731   -136       N
ATOM    891  N   ARG A 200      66.475  25.202   6.575  1.00 82.07           N
ANISOU  891  N   ARG A 200     4765  12468  13947  -1356    479  -2345       N
ATOM    892  CA  ARG A 200      67.005  23.987   5.976  1.00 88.56           C
ANISOU  892  CA  ARG A 200     4723  13287  15639   -803   1242  -2751       C
ATOM    893  C   ARG A 200      66.231  23.537   4.746  1.00 84.99           C
ANISOU  893  C   ARG A 200     4982  12882  14430   -772   2240  -3161       C
ATOM    894  O   ARG A 200      66.787  22.807   3.917  1.00 91.10           O
ANISOU  894  O   ARG A 200     5482  13663  15467   -485   2759  -3260       O
ATOM    895  CB  ARG A 200      67.009  22.862   7.016  1.00 90.56           C
ANISOU  895  CB  ARG A 200     5075  12804  16530    -60    817  -2663       C
ATOM    896  CG  ARG A 200      67.959  21.716   6.723  1.00 99.94           C
ANISOU  896  CG  ARG A 200     5359  13908  18706    538   1290  -2778       C
ATOM    897  CD  ARG A 200      67.916  20.704   7.857  1.00101.18           C
ANISOU  897  CD  ARG A 200     5575  13344  19523   1238    790  -2666       C
ATOM    898  NE  ARG A 200      68.078  21.349   9.158  1.00 99.96           N
ANISOU  898  NE  ARG A 200     5729  12896  19357   1089   -486  -2008       N
ATOM    899  CZ  ARG A 200      67.841  20.757  10.325  1.00 98.76           C
ANISOU  899  CZ  ARG A 200     6019  12080  19427   1556  -1176  -1764       C
ATOM    900  NH1 ARG A 200      67.425  19.498  10.362  1.00 98.44           N
ANISOU  900  NH1 ARG A 200     6071  11619  19714   2225   -722  -2143       N
ATOM    901  NH2 ARG A 200      68.015  21.426  11.457  1.00 97.99           N
ANISOU  901  NH2 ARG A 200     6308  11722  19200   1339  -2332  -1137       N
ATOM    902  N   PHE A 201      64.972  23.954   4.600  1.00 75.66           N
ANISOU  902  N   PHE A 201     4798  11687  12262  -1089   2373  -3276       N
ATOM    903  CA  PHE A 201      64.120  23.452   3.528  1.00 71.93           C
ANISOU  903  CA  PHE A 201     5178  11050  11101  -1083   2902  -3439       C
ATOM    904  C   PHE A 201      63.423  24.528   2.706  1.00 65.19           C
ANISOU  904  C   PHE A 201     5098  10377   9293  -1580   2819  -3224       C
ATOM    905  O   PHE A 201      63.017  24.231   1.575  1.00 64.03           O
ANISOU  905  O   PHE A 201     5343  10102   8884  -1599   2990  -3206       O
ATOM    906  CB  PHE A 201      63.058  22.498   4.097  1.00 67.06           C
ANISOU  906  CB  PHE A 201     5224   9941  10315   -764   2921  -3553       C
ATOM    907  CG  PHE A 201      63.625  21.404   4.964  1.00 72.81           C
ANISOU  907  CG  PHE A 201     5369  10272  12022    -79   2834  -3729       C
ATOM    908  CD1 PHE A 201      64.122  20.240   4.402  1.00 79.56           C
ANISOU  908  CD1 PHE A 201     5998  10934  13297    287   3188  -3833       C
ATOM    909  CD2 PHE A 201      63.658  21.539   6.343  1.00 71.60           C
ANISOU  909  CD2 PHE A 201     5082   9815  12309    249   2146  -3602       C
ATOM    910  CE1 PHE A 201      64.642  19.235   5.197  1.00 84.88           C
ANISOU  910  CE1 PHE A 201     6273  11179  14799    939   3012  -3855       C
ATOM    911  CE2 PHE A 201      64.177  20.537   7.143  1.00 76.73           C
ANISOU  911  CE2 PHE A 201     5395   9913  13846    948   1760  -3528       C
ATOM    912  CZ  PHE A 201      64.669  19.385   6.569  1.00 83.30           C
ANISOU  912  CZ  PHE A 201     5899  10635  15115   1286   2305  -3717       C
ATOM    913  N   ALA A 202      63.274  25.755   3.214  1.00132.57           N
ANISOU  913  N   ALA A 202    18770  16608  14991  -6108  -5652    338       N
ATOM    914  CA  ALA A 202      62.612  26.825   2.471  1.00128.71           C
ANISOU  914  CA  ALA A 202    17946  16785  14175  -5932  -5123    124       C
ATOM    915  C   ALA A 202      62.766  28.173   3.166  1.00124.97           C
ANISOU  915  C   ALA A 202    17237  16792  13455  -5807  -4736    240       C
ATOM    916  O   ALA A 202      61.811  28.674   3.768  1.00124.51           O
ANISOU  916  O   ALA A 202    17075  17231  13005  -6155  -4504    464       O
ATOM    917  CB  ALA A 202      61.124  26.513   2.285  1.00130.35           C
ANISOU  917  CB  ALA A 202    18117  17354  14058  -6428  -5093    249       C
ATOM    918  N   TRP A 203      63.948  28.779   3.078  1.00122.70           N
ANISOU  918  N   TRP A 203    16851  16350  13419  -5316  -4641     79       N
ATOM    919  CA  TRP A 203      64.232  30.025   3.773  1.00119.73           C
ANISOU  919  CA  TRP A 203    16290  16332  12871  -5201  -4328    156       C
ATOM    920  C   TRP A 203      64.237  31.201   2.797  1.00115.64           C
ANISOU  920  C   TRP A 203    15378  16220  12341  -4729  -3795   -132       C
ATOM    921  O   TRP A 203      64.018  31.046   1.594  1.00115.20           O
ANISOU  921  O   TRP A 203    15205  16213  12354  -4506  -3678   -367       O
ATOM    922  CB  TRP A 203      65.563  29.929   4.521  1.00120.65           C
ANISOU  922  CB  TRP A 203    16553  15992  13296  -5055  -4653    258       C
ATOM    923  CG  TRP A 203      66.771  29.875   3.636  1.00119.88           C
ANISOU  923  CG  TRP A 203    16341  15481  13728  -4461  -4690    -17       C
ATOM    924  CD1 TRP A 203      66.989  29.022   2.594  1.00121.49           C
ANISOU  924  CD1 TRP A 203    16602  15302  14257  -4228  -4805   -255       C
ATOM    925  CD2 TRP A 203      67.941  30.697   3.734  1.00117.93           C
ANISOU  925  CD2 TRP A 203    15901  15147  13761  -4037  -4591    -87       C
ATOM    926  NE1 TRP A 203      68.216  29.270   2.028  1.00120.68           N
ANISOU  926  NE1 TRP A 203    16341  14899  14612  -3660  -4732   -466       N
ATOM    927  CE2 TRP A 203      68.821  30.293   2.710  1.00118.41           C
ANISOU  927  CE2 TRP A 203    15876  14786  14329  -3538  -4618   -341       C
ATOM    928  CE3 TRP A 203      68.327  31.738   4.584  1.00116.27           C
ANISOU  928  CE3 TRP A 203    15586  15165  13426  -4046  -4475     26       C
ATOM    929  CZ2 TRP A 203      70.064  30.894   2.514  1.00117.17           C
ANISOU  929  CZ2 TRP A 203    15486  14444  14591  -3043  -4526   -433       C
ATOM    930  CZ3 TRP A 203      69.561  32.334   4.387  1.00115.00           C
ANISOU  930  CZ3 TRP A 203    15210  14802  13681  -3580  -4436    -78       C
ATOM    931  CH2 TRP A 203      70.415  31.910   3.360  1.00115.39           C
ANISOU  931  CH2 TRP A 203    15132  14445  14267  -3081  -4459   -280       C
ATOM    932  N   ARG A 204      64.502  32.389   3.333  1.00113.10           N
ANISOU  932  N   ARG A 204    14866  16184  11922  -4594  -3481   -106       N
ATOM    933  CA  ARG A 204      64.481  33.629   2.566  1.00109.45           C
ANISOU  933  CA  ARG A 204    14002  16114  11471  -4177  -2957   -304       C
ATOM    934  C   ARG A 204      65.272  34.690   3.336  1.00107.72           C
ANISOU  934  C   ARG A 204    13683  15923  11324  -4007  -2796   -292       C
ATOM    935  O   ARG A 204      66.082  34.359   4.208  1.00109.35           O
ANISOU  935  O   ARG A 204    14128  15776  11644  -4112  -3158   -180       O
ATOM    936  CB  ARG A 204      63.031  34.065   2.292  1.00108.85           C
ANISOU  936  CB  ARG A 204    13702  16614  11043  -4406  -2586   -235       C
ATOM    937  CG  ARG A 204      62.482  33.678   0.927  1.00109.03           C
ANISOU  937  CG  ARG A 204    13594  16758  11074  -4290  -2550   -377       C
ATOM    938  CD  ARG A 204      63.003  34.590  -0.176  1.00106.18           C
ANISOU  938  CD  ARG A 204    12893  16565  10885  -3720  -2196   -599       C
ATOM    939  NE  ARG A 204      64.330  34.205  -0.648  1.00106.28           N
ANISOU  939  NE  ARG A 204    13030  16100  11251  -3316  -2386   -815       N
ATOM    940  CZ  ARG A 204      64.966  34.799  -1.653  1.00104.56           C
ANISOU  940  CZ  ARG A 204    12567  15943  11217  -2806  -2120  -1010       C
ATOM    941  NH1 ARG A 204      64.396  35.808  -2.297  1.00102.53           N
ANISOU  941  NH1 ARG A 204    11937  16202  10818  -2648  -1693   -991       N
ATOM    942  NH2 ARG A 204      66.172  34.383  -2.016  1.00105.28           N
ANISOU  942  NH2 ARG A 204    12764  15578  11662  -2452  -2267  -1191       N
TER
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.