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***  FPC_apoabpbp3  ***

elNémo ID: 220606212815147285

Job options:

ID        	=	 220606212815147285
JOBID     	=	 FPC_apoabpbp3
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER FPC_apoabpbp3

ATOM      1  N   THR A  69     -27.174  -8.553  -0.221  1.00 77.02           N  
ANISOU    1  N   THR A  69    11543  11539   6181  -1874   2797   2798       N  
ATOM      2  CA  THR A  69     -27.188  -8.186  -1.642  1.00 74.48           C  
ANISOU    2  CA  THR A  69    10990  11179   6130  -1805   2714   2698       C  
ATOM      3  C   THR A  69     -25.929  -7.449  -2.158  1.00 75.29           C  
ANISOU    3  C   THR A  69    11124  11286   6198  -1770   2495   2558       C  
ATOM      4  O   THR A  69     -25.426  -6.541  -1.496  1.00 75.42           O  
ANISOU    4  O   THR A  69    11321  11342   5991  -1773   2505   2467       O  
ATOM      5  CB  THR A  69     -28.532  -7.542  -2.053  1.00 85.68           C  
ANISOU    5  CB  THR A  69    12259  12593   7704  -1755   2969   2647       C  
ATOM      6  OG1 THR A  69     -28.548  -7.363  -3.467  1.00 84.33           O  
ANISOU    6  OG1 THR A  69    11862  12379   7799  -1698   2865   2571       O  
ATOM      7  CG2 THR A  69     -28.805  -6.204  -1.351  1.00 86.51           C  
ANISOU    7  CG2 THR A  69    12512  12744   7615  -1726   3172   2527       C  
ATOM      8  N   GLU A  70     -25.446  -7.839  -3.358  1.00 68.95           N  
ANISOU    8  N   GLU A  70    10142  10435   5620  -1738   2302   2541       N  
ATOM      9  CA  GLU A  70     -24.266  -7.257  -4.021  1.00 66.54           C  
ANISOU    9  CA  GLU A  70     9827  10126   5330  -1701   2090   2422       C  
ATOM     10  C   GLU A  70     -24.480  -6.979  -5.516  1.00 66.55           C  
ANISOU   10  C   GLU A  70     9595  10083   5607  -1632   2050   2335       C  
ATOM     11  O   GLU A  70     -25.205  -7.716  -6.185  1.00 65.21           O  
ANISOU   11  O   GLU A  70     9257   9870   5648  -1626   2080   2404       O  
ATOM     12  CB  GLU A  70     -23.003  -8.118  -3.801  1.00 67.79           C  
ANISOU   12  CB  GLU A  70    10062  10274   5423  -1740   1832   2504       C  
ATOM     13  CG  GLU A  70     -23.109  -9.560  -4.281  1.00 76.33           C  
ANISOU   13  CG  GLU A  70    11015  11297   6690  -1757   1738   2644       C  
ATOM     14  CD  GLU A  70     -21.805 -10.284  -4.559  1.00 95.13           C  
ANISOU   14  CD  GLU A  70    13399  13646   9098  -1763   1463   2692       C  
ATOM     15  OE1 GLU A  70     -20.725  -9.759  -4.198  1.00 82.43           O  
ANISOU   15  OE1 GLU A  70    11910  12069   7340  -1767   1329   2639       O  
ATOM     16  OE2 GLU A  70     -21.868 -11.386  -5.150  1.00 91.82           O  
ANISOU   16  OE2 GLU A  70    12860  13167   8861  -1763   1382   2785       O  
ATOM     17  N   ARG A  71     -23.835  -5.927  -6.037  1.00 61.33           N  
ANISOU   17  N   ARG A  71     8930   9431   4942  -1584   1975   2187       N  
ATOM     18  CA  ARG A  71     -23.958  -5.568  -7.444  1.00 58.79           C  
ANISOU   18  CA  ARG A  71     8407   9071   4858  -1519   1931   2098       C  
ATOM     19  C   ARG A  71     -23.139  -6.483  -8.362  1.00 61.13           C  
ANISOU   19  C   ARG A  71     8596   9318   5314  -1510   1696   2140       C  
ATOM     20  O   ARG A  71     -22.100  -7.013  -7.951  1.00 61.13           O  
ANISOU   20  O   ARG A  71     8691   9320   5217  -1541   1529   2193       O  
ATOM     21  CB  ARG A  71     -23.648  -4.076  -7.679  1.00 57.75           C  
ANISOU   21  CB  ARG A  71     8309   8963   4670  -1470   1957   1928       C  
ATOM     22  CG  ARG A  71     -22.196  -3.750  -8.022  1.00 63.80           C  
ANISOU   22  CG  ARG A  71     9120   9731   5391  -1460   1726   1855       C  
ATOM     23  CD  ARG A  71     -22.102  -2.786  -9.182  1.00 71.19           C  
ANISOU   23  CD  ARG A  71     9929  10647   6473  -1391   1703   1717       C  
ATOM     24  NE  ARG A  71     -22.223  -1.400  -8.736  1.00 84.65           N  
ANISOU   24  NE  ARG A  71    11738  12384   8040  -1374   1822   1592       N  
ATOM     25  CZ  ARG A  71     -21.827  -0.346  -9.441  1.00103.36           C  
ANISOU   25  CZ  ARG A  71    14063  14746  10463  -1326   1782   1460       C  
ATOM     26  NH1 ARG A  71     -21.277  -0.507 -10.640  1.00 90.20           N  
ANISOU   26  NH1 ARG A  71    12250  13045   8979  -1288   1629   1435       N  
ATOM     27  NH2 ARG A  71     -21.971   0.879  -8.951  1.00 92.94           N  
ANISOU   27  NH2 ARG A  71    12853  13448   9011  -1315   1897   1352       N  
ATOM     28  N   LEU A  72     -23.631  -6.676  -9.595  1.00 55.89           N  
ANISOU   28  N   LEU A  72     7736   8605   4895  -1468   1688   2119       N  
ATOM     29  CA  LEU A  72     -22.976  -7.456 -10.645  1.00 54.29           C  
ANISOU   29  CA  LEU A  72     7419   8343   4864  -1448   1489   2139       C  
ATOM     30  C   LEU A  72     -22.598  -6.466 -11.761  1.00 56.03           C  
ANISOU   30  C   LEU A  72     7548   8555   5188  -1381   1433   1991       C  
ATOM     31  O   LEU A  72     -23.471  -6.051 -12.529  1.00 54.74           O  
ANISOU   31  O   LEU A  72     7255   8373   5170  -1346   1530   1939       O  
ATOM     32  CB  LEU A  72     -23.914  -8.559 -11.185  1.00 54.30           C  
ANISOU   32  CB  LEU A  72     7282   8287   5064  -1464   1524   2242       C  
ATOM     33  CG  LEU A  72     -24.303  -9.687 -10.237  1.00 60.61           C  
ANISOU   33  CG  LEU A  72     8149   9081   5798  -1533   1570   2403       C  
ATOM     34  CD1 LEU A  72     -25.626 -10.307 -10.657  1.00 61.25           C  
ANISOU   34  CD1 LEU A  72     8086   9119   6065  -1550   1688   2478       C  
ATOM     35  CD2 LEU A  72     -23.220 -10.753 -10.167  1.00 62.32           C  
ANISOU   35  CD2 LEU A  72     8418   9262   5999  -1555   1364   2489       C  
ATOM     36  N   GLU A  73     -21.319  -6.031 -11.798  1.00 52.11           N  
ANISOU   36  N   GLU A  73     7120   8073   4608  -1365   1281   1926       N  
ATOM     37  CA  GLU A  73     -20.816  -5.059 -12.774  1.00 50.79           C  
ANISOU   37  CA  GLU A  73     6883   7899   4516  -1305   1220   1789       C  
ATOM     38  C   GLU A  73     -20.920  -5.581 -14.215  1.00 52.07           C  
ANISOU   38  C   GLU A  73     6868   7994   4920  -1262   1141   1783       C  
ATOM     39  O   GLU A  73     -20.458  -6.687 -14.506  1.00 52.01           O  
ANISOU   39  O   GLU A  73     6830   7942   4988  -1271   1014   1863       O  
ATOM     40  CB  GLU A  73     -19.366  -4.651 -12.450  1.00 52.61           C  
ANISOU   40  CB  GLU A  73     7220   8154   4615  -1308   1059   1747       C  
ATOM     41  CG  GLU A  73     -19.200  -3.191 -12.041  1.00 67.95           C  
ANISOU   41  CG  GLU A  73     9258  10146   6414  -1300   1125   1625       C  
ATOM     42  CD  GLU A  73     -18.155  -2.356 -12.771  1.00 89.38           C  
ANISOU   42  CD  GLU A  73    11942  12856   9164  -1259    997   1514       C  
ATOM     43  OE1 GLU A  73     -17.489  -2.878 -13.695  1.00 79.33           O  
ANISOU   43  OE1 GLU A  73    10567  11543   8031  -1230    851   1527       O  
ATOM     44  OE2 GLU A  73     -18.016  -1.160 -12.422  1.00 83.87           O  
ANISOU   44  OE2 GLU A  73    11323  12190   8353  -1256   1049   1412       O  
ATOM     45  N   ALA A  74     -21.558  -4.795 -15.101  1.00 46.00           N  
ANISOU   45  N   ALA A  74     5992   7216   4270  -1216   1219   1689       N  
ATOM     46  CA  ALA A  74     -21.733  -5.148 -16.511  1.00 43.46           C  
ANISOU   46  CA  ALA A  74     5515   6832   4166  -1176   1153   1669       C  
ATOM     47  C   ALA A  74     -20.428  -4.973 -17.261  1.00 44.03           C  
ANISOU   47  C   ALA A  74     5578   6885   4266  -1135    980   1604       C  
ATOM     48  O   ALA A  74     -19.785  -3.925 -17.130  1.00 42.93           O  
ANISOU   48  O   ALA A  74     5493   6784   4036  -1115    966   1513       O  
ATOM     49  CB  ALA A  74     -22.807  -4.273 -17.143  1.00 43.56           C  
ANISOU   49  CB  ALA A  74     5426   6845   4280  -1142   1288   1594       C  
ATOM     50  N   MET A  75     -20.030  -5.988 -18.049  1.00 38.74           N  
ANISOU   50  N   MET A  75     4842   6153   3724  -1123    853   1651       N  
ATOM     51  CA  MET A  75     -18.825  -5.866 -18.863  1.00 37.36           C  
ANISOU   51  CA  MET A  75     4645   5954   3597  -1077    703   1593       C  
ATOM     52  C   MET A  75     -19.087  -4.813 -19.956  1.00 37.65           C  
ANISOU   52  C   MET A  75     4594   5985   3727  -1024    740   1470       C  
ATOM     53  O   MET A  75     -20.095  -4.903 -20.664  1.00 36.60           O  
ANISOU   53  O   MET A  75     4368   5820   3719  -1015    805   1464       O  
ATOM     54  CB  MET A  75     -18.423  -7.209 -19.483  1.00 39.87           C  
ANISOU   54  CB  MET A  75     4916   6196   4036  -1070    580   1669       C  
ATOM     55  CG  MET A  75     -17.087  -7.154 -20.183  1.00 43.24           C  
ANISOU   55  CG  MET A  75     5330   6598   4502  -1020    435   1623       C  
ATOM     56  SD  MET A  75     -16.639  -8.765 -20.822  1.00 48.29           S  
ANISOU   56  SD  MET A  75     5929   7139   5279  -1006    309   1714       S  
ATOM     57  CE  MET A  75     -15.886  -8.295 -22.367  1.00 43.57           C  
ANISOU   57  CE  MET A  75     5247   6496   4810   -925    237   1601       C  
ATOM     58  N   ARG A  76     -18.227  -3.775 -20.018  1.00 32.04           N  
ANISOU   58  N   ARG A  76     3917   5306   2949   -995    700   1379       N  
ATOM     59  CA  ARG A  76     -18.337  -2.697 -20.994  1.00 30.58           C  
ANISOU   59  CA  ARG A  76     3664   5119   2838   -945    727   1263       C  
ATOM     60  C   ARG A  76     -18.053  -3.281 -22.392  1.00 32.39           C  
ANISOU   60  C   ARG A  76     3794   5278   3234   -902    629   1254       C  
ATOM     61  O   ARG A  76     -17.193  -4.161 -22.536  1.00 31.53           O  
ANISOU   61  O   ARG A  76     3696   5136   3148   -897    511   1305       O  
ATOM     62  CB  ARG A  76     -17.375  -1.539 -20.644  1.00 29.78           C  
ANISOU   62  CB  ARG A  76     3633   5062   2618   -933    695   1179       C  
ATOM     63  CG  ARG A  76     -17.573  -0.271 -21.474  1.00 30.81           C  
ANISOU   63  CG  ARG A  76     3708   5195   2803   -887    745   1060       C  
ATOM     64  CD  ARG A  76     -16.720   0.876 -20.947  1.00 34.75           C  
ANISOU   64  CD  ARG A  76     4292   5738   3174   -889    727    983       C  
ATOM     65  NE  ARG A  76     -16.814   2.070 -21.791  1.00 39.18           N  
ANISOU   65  NE  ARG A  76     4800   6293   3794   -844    765    873       N  
ATOM     66  CZ  ARG A  76     -17.702   3.049 -21.623  1.00 50.32           C  
ANISOU   66  CZ  ARG A  76     6216   7721   5184   -836    901    812       C  
ATOM     67  NH1 ARG A  76     -18.596   2.986 -20.643  1.00 42.26           N  
ANISOU   67  NH1 ARG A  76     5249   6725   4083   -869   1026    847       N  
ATOM     68  NH2 ARG A  76     -17.710   4.094 -22.444  1.00 26.95           N  
ANISOU   68  NH2 ARG A  76     3204   4748   2286   -793    921    718       N  
ATOM     69  N   GLY A  77     -18.825  -2.825 -23.375  1.00 27.18           N  
ANISOU   69  N   GLY A  77     3046   4595   2688   -872    682   1197       N  
ATOM     70  CA  GLY A  77     -18.743  -3.290 -24.753  1.00 25.58           C  
ANISOU   70  CA  GLY A  77     2760   4323   2635   -834    605   1180       C  
ATOM     71  C   GLY A  77     -17.394  -3.092 -25.420  1.00 28.84           C  
ANISOU   71  C   GLY A  77     3179   4720   3058   -788    492   1128       C  
ATOM     72  O   GLY A  77     -16.635  -2.183 -25.063  1.00 27.78           O  
ANISOU   72  O   GLY A  77     3086   4631   2836   -777    482   1074       O  
ATOM     73  N   VAL A  78     -17.096  -3.951 -26.405  1.00 24.43           N  
ANISOU   73  N   VAL A  78     2579   4091   2611   -761    407   1144       N  
ATOM     74  CA  VAL A  78     -15.858  -3.874 -27.168  1.00 23.48           C  
ANISOU   74  CA  VAL A  78     2454   3945   2523   -709    312   1102       C  
ATOM     75  C   VAL A  78     -16.041  -2.882 -28.310  1.00 26.14           C  
ANISOU   75  C   VAL A  78     2737   4273   2921   -666    337   1001       C  
ATOM     76  O   VAL A  78     -17.038  -2.957 -29.029  1.00 25.09           O  
ANISOU   76  O   VAL A  78     2553   4107   2872   -665    373    987       O  
ATOM     77  CB  VAL A  78     -15.397  -5.280 -27.669  1.00 26.51           C  
ANISOU   77  CB  VAL A  78     2833   4250   2990   -695    220   1166       C  
ATOM     78  CG1 VAL A  78     -14.228  -5.189 -28.657  1.00 24.97           C  
ANISOU   78  CG1 VAL A  78     2621   4018   2850   -630    142   1118       C  
ATOM     79  CG2 VAL A  78     -15.039  -6.189 -26.504  1.00 26.81           C  
ANISOU   79  CG2 VAL A  78     2929   4296   2963   -734    184   1271       C  
ATOM     80  N   ILE A  79     -15.086  -1.951 -28.474  1.00 23.07           N  
ANISOU   80  N   ILE A  79     2358   3914   2495   -633    312    935       N  
ATOM     81  CA  ILE A  79     -15.094  -1.036 -29.621  1.00 21.85           C  
ANISOU   81  CA  ILE A  79     2157   3746   2400   -588    326    844       C  
ATOM     82  C   ILE A  79     -14.069  -1.644 -30.556  1.00 26.06           C  
ANISOU   82  C   ILE A  79     2678   4222   3002   -541    236    844       C  
ATOM     83  O   ILE A  79     -12.910  -1.804 -30.164  1.00 25.44           O  
ANISOU   83  O   ILE A  79     2623   4154   2889   -530    176    867       O  
ATOM     84  CB  ILE A  79     -14.782   0.464 -29.327  1.00 24.24           C  
ANISOU   84  CB  ILE A  79     2473   4107   2630   -580    368    766       C  
ATOM     85  CG1 ILE A  79     -15.761   1.084 -28.317  1.00 24.63           C  
ANISOU   85  CG1 ILE A  79     2548   4209   2601   -621    472    762       C  
ATOM     86  CG2 ILE A  79     -14.794   1.268 -30.643  1.00 25.11           C  
ANISOU   86  CG2 ILE A  79     2532   4191   2817   -532    374    684       C  
ATOM     87  CD1 ILE A  79     -15.194   2.288 -27.558  1.00 32.59           C  
ANISOU   87  CD1 ILE A  79     3610   5274   3499   -630    496    706       C  
ATOM     88  N   SER A  80     -14.486  -2.029 -31.763  1.00 22.81           N  
ANISOU   88  N   SER A  80     2231   3747   2689   -513    225    824       N  
ATOM     89  CA  SER A  80     -13.531  -2.614 -32.695  1.00 22.33           C  
ANISOU   89  CA  SER A  80     2170   3625   2691   -463    155    819       C  
ATOM     90  C   SER A  80     -13.510  -1.880 -34.034  1.00 24.31           C  
ANISOU   90  C   SER A  80     2393   3849   2994   -416    165    736       C  
ATOM     91  O   SER A  80     -14.373  -1.048 -34.285  1.00 24.52           O  
ANISOU   91  O   SER A  80     2395   3896   3023   -427    216    691       O  
ATOM     92  CB  SER A  80     -13.754  -4.120 -32.829  1.00 27.54           C  
ANISOU   92  CB  SER A  80     2844   4211   3407   -472    112    890       C  
ATOM     93  OG  SER A  80     -14.580  -4.469 -33.927  1.00 42.36           O  
ANISOU   93  OG  SER A  80     4706   6023   5364   -466    113    866       O  
ATOM     94  N   ASP A  81     -12.495  -2.143 -34.863  1.00 20.13           N  
ANISOU   94  N   ASP A  81     1867   3274   2506   -363    120    720       N  
ATOM     95  CA  ASP A  81     -12.355  -1.582 -36.209  1.00 18.08           C  
ANISOU   95  CA  ASP A  81     1596   2982   2293   -315    127    648       C  
ATOM     96  C   ASP A  81     -13.251  -2.392 -37.167  1.00 20.33           C  
ANISOU   96  C   ASP A  81     1892   3189   2643   -317    113    649       C  
ATOM     97  O   ASP A  81     -13.813  -3.408 -36.747  1.00 20.40           O  
ANISOU   97  O   ASP A  81     1914   3169   2668   -353     95    707       O  
ATOM     98  CB  ASP A  81     -10.863  -1.592 -36.624  1.00 19.82           C  
ANISOU   98  CB  ASP A  81     1817   3183   2530   -257     95    640       C  
ATOM     99  CG  ASP A  81     -10.328  -2.739 -37.495  1.00 25.35           C  
ANISOU   99  CG  ASP A  81     2542   3793   3298   -209     60    659       C  
ATOM    100  OD1 ASP A  81     -10.899  -3.843 -37.450  1.00 26.32           O  
ANISOU  100  OD1 ASP A  81     2691   3864   3447   -229     38    702       O  
ATOM    101  OD2 ASP A  81      -9.314  -2.534 -38.182  1.00 30.01           O  
ANISOU  101  OD2 ASP A  81     3127   4361   3915   -152     59    633       O  
ATOM    102  N   ARG A  82     -13.339  -1.980 -38.455  1.00 17.15           N  
ANISOU  102  N   ARG A  82     1492   2748   2275   -282    115    587       N  
ATOM    103  CA  ARG A  82     -14.131  -2.632 -39.521  1.00 15.94           C  
ANISOU  103  CA  ARG A  82     1363   2516   2178   -285     89    577       C  
ATOM    104  C   ARG A  82     -13.923  -4.146 -39.762  1.00 21.27           C  
ANISOU  104  C   ARG A  82     2085   3103   2892   -279     39    620       C  
ATOM    105  O   ARG A  82     -14.861  -4.824 -40.216  1.00 20.98           O  
ANISOU  105  O   ARG A  82     2068   3008   2896   -312     11    631       O  
ATOM    106  CB  ARG A  82     -14.115  -1.804 -40.821  1.00 11.14           C  
ANISOU  106  CB  ARG A  82      761   1889   1581   -247     97    502       C  
ATOM    107  CG  ARG A  82     -12.827  -1.785 -41.666  1.00 13.28           C  
ANISOU  107  CG  ARG A  82     1067   2124   1855   -177     94    467       C  
ATOM    108  CD  ARG A  82     -12.954  -0.889 -42.929  1.00  7.65           C  
ANISOU  108  CD  ARG A  82      437   1361   1109   -123     83    392       C  
ATOM    109  NE  ARG A  82     -14.085  -1.322 -43.769  1.00 18.64           N  
ANISOU  109  NE  ARG A  82     1790   2728   2563   -175     73    388       N  
ATOM    110  CZ  ARG A  82     -15.277  -0.715 -43.825  1.00 36.26           C  
ANISOU  110  CZ  ARG A  82     3986   4985   4806   -217     72    381       C  
ATOM    111  NH1 ARG A  82     -15.492   0.410 -43.154  1.00 15.66           N  
ANISOU  111  NH1 ARG A  82     1316   2456   2177   -228    118    372       N  
ATOM    112  NH2 ARG A  82     -16.251  -1.221 -44.571  1.00 28.72           N  
ANISOU  112  NH2 ARG A  82     3057   3969   3884   -247     23    382       N  
ATOM    113  N   HIS A  83     -12.710  -4.668 -39.436  1.00 18.42           N  
ANISOU  113  N   HIS A  83     1742   2729   2528   -240     26    648       N  
ATOM    114  CA  HIS A  83     -12.326  -6.074 -39.600  1.00 19.32           C  
ANISOU  114  CA  HIS A  83     1903   2755   2684   -223    -14    691       C  
ATOM    115  C   HIS A  83     -12.350  -6.876 -38.287  1.00 25.22           C  
ANISOU  115  C   HIS A  83     2643   3518   3423   -263    -34    779       C  
ATOM    116  O   HIS A  83     -11.931  -8.039 -38.251  1.00 27.34           O  
ANISOU  116  O   HIS A  83     2945   3715   3727   -247    -68    826       O  
ATOM    117  CB  HIS A  83     -10.967  -6.188 -40.313  1.00 20.84           C  
ANISOU  117  CB  HIS A  83     2118   2904   2897   -140    -12    666       C  
ATOM    118  CG  HIS A  83     -10.897  -5.444 -41.616  1.00 24.51           C  
ANISOU  118  CG  HIS A  83     2601   3349   3361   -100     14    584       C  
ATOM    119  ND1 HIS A  83     -11.756  -5.741 -42.678  1.00 26.80           N  
ANISOU  119  ND1 HIS A  83     2944   3570   3668   -112     -3    546       N  
ATOM    120  CD2 HIS A  83     -10.060  -4.451 -42.000  1.00 26.00           C  
ANISOU  120  CD2 HIS A  83     2766   3577   3534    -54     50    541       C  
ATOM    121  CE1 HIS A  83     -11.414  -4.920 -43.659  1.00 25.62           C  
ANISOU  121  CE1 HIS A  83     2807   3422   3505    -70     25    481       C  
ATOM    122  NE2 HIS A  83     -10.396  -4.129 -43.303  1.00 25.90           N  
ANISOU  122  NE2 HIS A  83     2795   3521   3524    -33     62    477       N  
ATOM    123  N   GLY A  84     -12.859  -6.256 -37.230  1.00 21.62           N  
ANISOU  123  N   GLY A  84     2148   3150   2917   -314     -9    803       N  
ATOM    124  CA  GLY A  84     -13.008  -6.874 -35.918  1.00 21.89           C  
ANISOU  124  CA  GLY A  84     2181   3211   2924   -362    -19    887       C  
ATOM    125  C   GLY A  84     -11.809  -6.794 -34.996  1.00 26.62           C  
ANISOU  125  C   GLY A  84     2777   3857   3480   -342    -35    928       C  
ATOM    126  O   GLY A  84     -11.797  -7.474 -33.963  1.00 28.55           O  
ANISOU  126  O   GLY A  84     3035   4111   3703   -376    -57   1007       O  
ATOM    127  N   VAL A  85     -10.798  -5.968 -35.344  1.00 22.13           N  
ANISOU  127  N   VAL A  85     2190   3318   2902   -292    -30    880       N  
ATOM    128  CA  VAL A  85      -9.586  -5.766 -34.535  1.00 22.28           C  
ANISOU  128  CA  VAL A  85     2195   3383   2889   -276    -58    917       C  
ATOM    129  C   VAL A  85      -9.988  -4.984 -33.276  1.00 25.58           C  
ANISOU  129  C   VAL A  85     2609   3899   3211   -339    -38    931       C  
ATOM    130  O   VAL A  85     -10.502  -3.874 -33.404  1.00 24.87           O  
ANISOU  130  O   VAL A  85     2504   3858   3086   -354     10    867       O  
ATOM    131  CB  VAL A  85      -8.465  -5.025 -35.328  1.00 25.99           C  
ANISOU  131  CB  VAL A  85     2636   3854   3385   -209    -53    862       C  
ATOM    132  CG1 VAL A  85      -7.302  -4.592 -34.424  1.00 25.13           C  
ANISOU  132  CG1 VAL A  85     2499   3805   3243   -208    -88    900       C  
ATOM    133  CG2 VAL A  85      -7.973  -5.854 -36.509  1.00 25.90           C  
ANISOU  133  CG2 VAL A  85     2641   3741   3459   -141    -60    852       C  
ATOM    134  N   PRO A  86      -9.740  -5.513 -32.063  1.00 23.80           N  
ANISOU  134  N   PRO A  86     2402   3700   2940   -375    -73   1012       N  
ATOM    135  CA  PRO A  86     -10.145  -4.772 -30.851  1.00 24.23           C  
ANISOU  135  CA  PRO A  86     2473   3845   2887   -437    -47   1021       C  
ATOM    136  C   PRO A  86      -9.390  -3.459 -30.650  1.00 28.49           C  
ANISOU  136  C   PRO A  86     3000   4452   3374   -429    -46    967       C  
ATOM    137  O   PRO A  86      -8.161  -3.425 -30.741  1.00 28.22           O  
ANISOU  137  O   PRO A  86     2946   4413   3362   -394   -101    980       O  
ATOM    138  CB  PRO A  86      -9.899  -5.775 -29.717  1.00 26.71           C  
ANISOU  138  CB  PRO A  86     2822   4159   3166   -471    -97   1129       C  
ATOM    139  CG  PRO A  86      -8.906  -6.742 -30.258  1.00 30.90           C  
ANISOU  139  CG  PRO A  86     3339   4614   3786   -414   -162   1171       C  
ATOM    140  CD  PRO A  86      -9.151  -6.831 -31.728  1.00 25.72           C  
ANISOU  140  CD  PRO A  86     2662   3888   3221   -362   -134   1103       C  
ATOM    141  N   LEU A  87     -10.141  -2.374 -30.403  1.00 24.66           N  
ANISOU  141  N   LEU A  87     2521   4023   2827   -461     18    908       N  
ATOM    142  CA  LEU A  87      -9.597  -1.024 -30.209  1.00 23.94           C  
ANISOU  142  CA  LEU A  87     2426   3990   2681   -462     28    847       C  
ATOM    143  C   LEU A  87      -9.791  -0.530 -28.780  1.00 29.19           C  
ANISOU  143  C   LEU A  87     3145   4727   3220   -525     41    865       C  
ATOM    144  O   LEU A  87      -8.997   0.270 -28.300  1.00 28.70           O  
ANISOU  144  O   LEU A  87     3098   4709   3100   -537     10    844       O  
ATOM    145  CB  LEU A  87     -10.171  -0.024 -31.237  1.00 22.68           C  
ANISOU  145  CB  LEU A  87     2235   3826   2557   -436     93    752       C  
ATOM    146  CG  LEU A  87      -9.797  -0.254 -32.713  1.00 26.64           C  
ANISOU  146  CG  LEU A  87     2698   4262   3164   -371     79    720       C  
ATOM    147  CD1 LEU A  87     -10.590   0.653 -33.631  1.00 26.49           C  
ANISOU  147  CD1 LEU A  87     2659   4238   3169   -357    141    639       C  
ATOM    148  CD2 LEU A  87      -8.304  -0.058 -32.963  1.00 28.30           C  
ANISOU  148  CD2 LEU A  87     2885   4468   3400   -330     27    721       C  
ATOM    149  N   ALA A  88     -10.832  -1.031 -28.100  1.00 27.58           N  
ANISOU  149  N   ALA A  88     2974   4532   2972   -569     86    906       N  
ATOM    150  CA  ALA A  88     -11.143  -0.750 -26.700  1.00 28.31           C  
ANISOU  150  CA  ALA A  88     3135   4687   2935   -631    113    933       C  
ATOM    151  C   ALA A  88     -11.776  -2.011 -26.130  1.00 35.10           C  
ANISOU  151  C   ALA A  88     4019   5527   3789   -663    116   1028       C  
ATOM    152  O   ALA A  88     -12.835  -2.446 -26.598  1.00 34.42           O  
ANISOU  152  O   ALA A  88     3905   5407   3766   -663    173   1033       O  
ATOM    153  CB  ALA A  88     -12.089   0.436 -26.581  1.00 28.57           C  
ANISOU  153  CB  ALA A  88     3179   4758   2918   -646    219    855       C  
ATOM    154  N   ILE A  89     -11.079  -2.646 -25.176  1.00 34.92           N  
ANISOU  154  N   ILE A  89     4047   5520   3703   -692     44   1109       N  
ATOM    155  CA  ILE A  89     -11.505  -3.894 -24.518  1.00 36.67           C  
ANISOU  155  CA  ILE A  89     4301   5721   3912   -727     34   1214       C  
ATOM    156  C   ILE A  89     -11.548  -3.772 -23.001  1.00 42.81           C  
ANISOU  156  C   ILE A  89     5172   6562   4534   -793     41   1266       C  
ATOM    157  O   ILE A  89     -10.828  -2.951 -22.428  1.00 41.89           O  
ANISOU  157  O   ILE A  89     5098   6494   4322   -809      6   1237       O  
ATOM    158  CB  ILE A  89     -10.644  -5.122 -24.957  1.00 40.38           C  
ANISOU  158  CB  ILE A  89     4742   6123   4479   -690    -68   1287       C  
ATOM    159  CG1 ILE A  89      -9.131  -4.894 -24.748  1.00 41.34           C  
ANISOU  159  CG1 ILE A  89     4861   6260   4588   -669   -173   1300       C  
ATOM    160  CG2 ILE A  89     -10.941  -5.541 -26.387  1.00 40.44           C  
ANISOU  160  CG2 ILE A  89     4682   6054   4630   -636    -54   1249       C  
ATOM    161  CD1 ILE A  89      -8.536  -5.719 -23.705  1.00 47.41           C  
ANISOU  161  CD1 ILE A  89     5677   7035   5302   -702   -258   1412       C  
ATOM    162  N   SER A  90     -12.361  -4.630 -22.350  1.00 42.37           N  
ANISOU  162  N   SER A  90     5151   6499   4448   -834     81   1347       N  
ATOM    163  CA  SER A  90     -12.472  -4.694 -20.890  1.00 43.86           C  
ANISOU  163  CA  SER A  90     5441   6742   4481   -899     94   1411       C  
ATOM    164  C   SER A  90     -12.016  -6.054 -20.360  1.00 49.76           C  
ANISOU  164  C   SER A  90     6218   7458   5232   -919      3   1541       C  
ATOM    165  O   SER A  90     -12.399  -7.095 -20.899  1.00 50.19           O  
ANISOU  165  O   SER A  90     6225   7447   5397   -904      0   1592       O  
ATOM    166  CB  SER A  90     -13.889  -4.371 -20.430  1.00 47.65           C  
ANISOU  166  CB  SER A  90     5948   7251   4905   -936    243   1397       C  
ATOM    167  OG  SER A  90     -14.186  -3.008 -20.680  1.00 55.64           O  
ANISOU  167  OG  SER A  90     6953   8299   5888   -921    323   1283       O  
ATOM    168  N   THR A  91     -11.174  -6.038 -19.324  1.00 47.78           N  
ANISOU  168  N   THR A  91     6045   7246   4861   -954    -79   1594       N  
ATOM    169  CA  THR A  91     -10.640  -7.252 -18.697  1.00 49.11           C  
ANISOU  169  CA  THR A  91     6250   7390   5022   -975   -178   1726       C  
ATOM    170  C   THR A  91     -11.040  -7.387 -17.199  1.00 54.30           C  
ANISOU  170  C   THR A  91     7032   8101   5497  -1054   -149   1802       C  
ATOM    171  O   THR A  91     -10.940  -6.407 -16.451  1.00 52.85           O  
ANISOU  171  O   THR A  91     6931   7985   5165  -1091   -128   1756       O  
ATOM    172  CB  THR A  91      -9.131  -7.392 -18.969  1.00 59.88           C  
ANISOU  172  CB  THR A  91     7576   8732   6441   -936   -330   1749       C  
ATOM    173  OG1 THR A  91      -8.455  -6.206 -18.538  1.00 60.48           O  
ANISOU  173  OG1 THR A  91     7692   8874   6414   -956   -367   1689       O  
ATOM    174  CG2 THR A  91      -8.821  -7.667 -20.452  1.00 57.54           C  
ANISOU  174  CG2 THR A  91     7163   8364   6336   -855   -346   1704       C  
ATOM    175  N   PRO A  92     -11.508  -8.586 -16.756  1.00 53.22           N  
ANISOU  175  N   PRO A  92     6922   7933   5368  -1083   -144   1918       N  
ATOM    176  CA  PRO A  92     -11.909  -8.755 -15.342  1.00 54.63           C  
ANISOU  176  CA  PRO A  92     7227   8161   5369  -1159   -108   1998       C  
ATOM    177  C   PRO A  92     -10.797  -8.493 -14.333  1.00 59.32           C  
ANISOU  177  C   PRO A  92     7921   8803   5814  -1196   -232   2039       C  
ATOM    178  O   PRO A  92      -9.677  -8.993 -14.490  1.00 59.17           O  
ANISOU  178  O   PRO A  92     7869   8754   5858  -1171   -382   2094       O  
ATOM    179  CB  PRO A  92     -12.399 -10.204 -15.278  1.00 57.08           C  
ANISOU  179  CB  PRO A  92     7524   8409   5754  -1172   -109   2122       C  
ATOM    180  CG  PRO A  92     -11.740 -10.880 -16.439  1.00 60.79           C  
ANISOU  180  CG  PRO A  92     7884   8796   6416  -1104   -206   2126       C  
ATOM    181  CD  PRO A  92     -11.709  -9.837 -17.514  1.00 54.84           C  
ANISOU  181  CD  PRO A  92     7051   8050   5738  -1050   -168   1981       C  
ATOM    182  N   ILE A  93     -11.119  -7.682 -13.308  1.00 55.83           N  
ANISOU  182  N   ILE A  93     7603   8434   5177  -1254   -167   2012       N  
ATOM    183  CA  ILE A  93     -10.211  -7.269 -12.242  1.00 56.15           C  
ANISOU  183  CA  ILE A  93     7765   8526   5042  -1305   -277   2039       C  
ATOM    184  C   ILE A  93     -10.845  -7.495 -10.858  1.00 60.94           C  
ANISOU  184  C   ILE A  93     8534   9178   5444  -1385   -209   2116       C  
ATOM    185  O   ILE A  93     -12.042  -7.257 -10.685  1.00 61.17           O  
ANISOU  185  O   ILE A  93     8593   9224   5425  -1399    -33   2082       O  
ATOM    186  CB  ILE A  93      -9.664  -5.834 -12.534  1.00 58.45           C  
ANISOU  186  CB  ILE A  93     8053   8855   5301  -1290   -294   1902       C  
ATOM    187  CG1 ILE A  93      -8.148  -5.841 -12.783  1.00 58.97           C  
ANISOU  187  CG1 ILE A  93     8071   8908   5429  -1271   -492   1925       C  
ATOM    188  CG2 ILE A  93     -10.085  -4.756 -11.531  1.00 59.46           C  
ANISOU  188  CG2 ILE A  93     8333   9051   5210  -1350   -207   1836       C  
ATOM    189  CD1 ILE A  93      -7.744  -6.156 -14.209  1.00 67.36           C  
ANISOU  189  CD1 ILE A  93     8961   9907   6726  -1184   -528   1899       C  
ATOM    190  N   MET A  94     -10.055  -8.015  -9.896  1.00 57.68           N  
ANISOU  190  N   MET A  94     8220   8779   4918  -1434   -348   2228       N  
ATOM    191  CA  MET A  94     -10.533  -8.357  -8.556  1.00 58.08           C  
ANISOU  191  CA  MET A  94     8436   8866   4764  -1512   -304   2320       C  
ATOM    192  C   MET A  94     -10.027  -7.478  -7.432  1.00 61.74           C  
ANISOU  192  C   MET A  94     9076   9398   4985  -1580   -358   2295       C  
ATOM    193  O   MET A  94      -8.850  -7.122  -7.394  1.00 61.94           O  
ANISOU  193  O   MET A  94     9104   9432   4997  -1584   -529   2287       O  
ATOM    194  CB  MET A  94     -10.260  -9.833  -8.247  1.00 61.14           C  
ANISOU  194  CB  MET A  94     8820   9209   5199  -1526   -406   2491       C  
ATOM    195  CG  MET A  94     -11.507 -10.684  -8.217  1.00 65.08           C  
ANISOU  195  CG  MET A  94     9309   9680   5740  -1535   -255   2558       C  
ATOM    196  SD  MET A  94     -12.315 -10.876  -9.827  1.00 67.39           S  
ANISOU  196  SD  MET A  94     9397   9904   6305  -1454   -145   2480       S  
ATOM    197  CE  MET A  94     -13.497 -12.123  -9.422  1.00 65.12           C  
ANISOU  197  CE  MET A  94     9128   9580   6033  -1495    -29   2612       C  
ATOM    198  N   LYS A  95     -10.929  -7.161  -6.496  1.00 58.35           N  
ANISOU  198  N   LYS A  95     8795   9012   4362  -1634   -209   2288       N  
ATOM    199  CA  LYS A  95     -10.689  -6.365  -5.291  1.00 59.15           C  
ANISOU  199  CA  LYS A  95     9104   9176   4195  -1708   -221   2263       C  
ATOM    200  C   LYS A  95     -10.833  -7.322  -4.093  1.00 63.44           C  
ANISOU  200  C   LYS A  95     9795   9732   4576  -1779   -241   2421       C  
ATOM    201  O   LYS A  95     -11.943  -7.779  -3.804  1.00 63.10           O  
ANISOU  201  O   LYS A  95     9781   9688   4505  -1790    -67   2464       O  
ATOM    202  CB  LYS A  95     -11.746  -5.248  -5.213  1.00 61.84           C  
ANISOU  202  CB  LYS A  95     9502   9548   4447  -1705      5   2126       C  
ATOM    203  CG  LYS A  95     -11.276  -3.923  -4.647  1.00 78.57           C  
ANISOU  203  CG  LYS A  95    11763  11710   6381  -1742    -19   2010       C  
ATOM    204  CD  LYS A  95     -12.429  -2.925  -4.702  1.00 90.71           C  
ANISOU  204  CD  LYS A  95    13335  13264   7867  -1722    228   1880       C  
ATOM    205  CE  LYS A  95     -12.027  -1.512  -4.357  1.00103.27           C  
ANISOU  205  CE  LYS A  95    15046  14881   9310  -1745    220   1741       C  
ATOM    206  NZ  LYS A  95     -13.192  -0.585  -4.391  1.00110.95           N  
ANISOU  206  NZ  LYS A  95    16056  15863  10238  -1720    472   1623       N  
ATOM    207  N   ILE A  96      -9.710  -7.668  -3.436  1.00 60.31           N  
ANISOU  207  N   ILE A  96     9482   9346   4090  -1826   -456   2517       N  
ATOM    208  CA  ILE A  96      -9.692  -8.576  -2.278  1.00 66.87           C  
ANISOU  208  CA  ILE A  96    10460  10187   4759  -1896   -510   2678       C  
ATOM    209  C   ILE A  96     -10.186  -7.843  -1.026  1.00 94.05           C  
ANISOU  209  C   ILE A  96    14148  13692   7894  -1976   -401   2644       C  
ATOM    210  O   ILE A  96      -9.599  -6.837  -0.634  1.00 58.37           O  
ANISOU  210  O   ILE A  96     9740   9209   3229  -2011   -471   2557       O  
ATOM    211  CB  ILE A  96      -8.293  -9.245  -2.064  1.00 70.00           C  
ANISOU  211  CB  ILE A  96    10846  10566   5184  -1915   -793   2800       C  
ATOM    212  CG1 ILE A  96      -7.700  -9.878  -3.363  1.00 67.90           C  
ANISOU  212  CG1 ILE A  96    10338  10233   5230  -1825   -896   2819       C  
ATOM    213  CG2 ILE A  96      -8.281 -10.219  -0.867  1.00 72.71           C  
ANISOU  213  CG2 ILE A  96    11346  10918   5361  -1989   -861   2979       C  
ATOM    214  CD1 ILE A  96      -8.539 -10.968  -4.104  1.00 69.22           C  
ANISOU  214  CD1 ILE A  96    10370  10335   5594  -1771   -789   2885       C  
ATOM    215  N   VAL A 186     -13.129 -12.756   4.634  1.00 75.01           N  
ANISOU  215  N   VAL A 186    12537  11326   4636  -2323    -64   3496       N  
ATOM    216  CA  VAL A 186     -12.722 -11.982   3.469  1.00 73.35           C  
ANISOU  216  CA  VAL A 186    12149  11103   4617  -2248   -104   3332       C  
ATOM    217  C   VAL A 186     -13.475 -12.392   2.186  1.00 75.58           C  
ANISOU  217  C   VAL A 186    12174  11330   5214  -2163     21   3299       C  
ATOM    218  O   VAL A 186     -13.874 -13.556   2.047  1.00 75.49           O  
ANISOU  218  O   VAL A 186    12086  11272   5327  -2160     39   3431       O  
ATOM    219  CB  VAL A 186     -11.179 -11.869   3.267  1.00 77.14           C  
ANISOU  219  CB  VAL A 186    12596  11576   5137  -2244   -409   3330       C  
ATOM    220  CG1 VAL A 186     -10.483 -11.363   4.531  1.00 78.77           C  
ANISOU  220  CG1 VAL A 186    13064  11840   5027  -2336   -535   3346       C  
ATOM    221  CG2 VAL A 186     -10.561 -13.182   2.786  1.00 76.66           C  
ANISOU  221  CG2 VAL A 186    12388  11451   5288  -2215   -595   3482       C  
ATOM    222  N   TYR A 187     -13.680 -11.421   1.269  1.00 69.77           N  
ANISOU  222  N   TYR A 187    11316  10596   4599  -2101    103   3125       N  
ATOM    223  CA  TYR A 187     -14.388 -11.629   0.002  1.00 67.48           C  
ANISOU  223  CA  TYR A 187    10791  10257   4594  -2023    216   3072       C  
ATOM    224  C   TYR A 187     -13.752 -10.874  -1.164  1.00 68.73           C  
ANISOU  224  C   TYR A 187    10791  10399   4926  -1951    123   2927       C  
ATOM    225  O   TYR A 187     -12.877 -10.029  -0.948  1.00 67.52           O  
ANISOU  225  O   TYR A 187    10713  10278   4662  -1963      4   2851       O  
ATOM    226  CB  TYR A 187     -15.896 -11.313   0.142  1.00 69.07           C  
ANISOU  226  CB  TYR A 187    11004  10476   4765  -2023    516   3028       C  
ATOM    227  CG  TYR A 187     -16.233  -9.856   0.386  1.00 71.06           C  
ANISOU  227  CG  TYR A 187    11354  10782   4862  -2021    659   2864       C  
ATOM    228  CD1 TYR A 187     -16.559  -9.011  -0.669  1.00 70.86           C  
ANISOU  228  CD1 TYR A 187    11178  10748   4999  -1950    743   2708       C  
ATOM    229  CD2 TYR A 187     -16.304  -9.343   1.679  1.00 74.12           C  
ANISOU  229  CD2 TYR A 187    11996  11227   4941  -2089    725   2868       C  
ATOM    230  CE1 TYR A 187     -16.893  -7.675  -0.451  1.00 71.85           C  
ANISOU  230  CE1 TYR A 187    11394  10914   4992  -1944    880   2560       C  
ATOM    231  CE2 TYR A 187     -16.638  -8.009   1.911  1.00 75.48           C  
ANISOU  231  CE2 TYR A 187    12269  11439   4971  -2085    867   2713       C  
ATOM    232  CZ  TYR A 187     -16.933  -7.178   0.841  1.00 82.05           C  
ANISOU  232  CZ  TYR A 187    12940  12257   5980  -2010    945   2560       C  
ATOM    233  OH  TYR A 187     -17.266  -5.862   1.051  1.00 84.25           O  
ANISOU  233  OH  TYR A 187    13316  12566   6129  -2001   1087   2409       O  
ATOM    234  N   THR A 188     -14.192 -11.192  -2.405  1.00 64.42           N  
ANISOU  234  N   THR A 188    10029   9798   4650  -1879    176   2892       N  
ATOM    235  CA  THR A 188     -13.702 -10.561  -3.642  1.00 61.80           C  
ANISOU  235  CA  THR A 188     9531   9444   4506  -1805    109   2760       C  
ATOM    236  C   THR A 188     -14.772  -9.676  -4.291  1.00 64.68           C  
ANISOU  236  C   THR A 188     9814   9817   4943  -1762    325   2618       C  
ATOM    237  O   THR A 188     -15.968  -9.897  -4.081  1.00 64.87           O  
ANISOU  237  O   THR A 188     9840   9842   4967  -1774    518   2647       O  
ATOM    238  CB  THR A 188     -13.145 -11.605  -4.644  1.00 64.81           C  
ANISOU  238  CB  THR A 188     9734   9748   5143  -1751    -37   2829       C  
ATOM    239  OG1 THR A 188     -14.201 -12.431  -5.137  1.00 62.02           O  
ANISOU  239  OG1 THR A 188     9281   9344   4939  -1735     92   2884       O  
ATOM    240  CG2 THR A 188     -12.033 -12.463  -4.058  1.00 63.82           C  
ANISOU  240  CG2 THR A 188     9670   9607   4972  -1781   -260   2969       C  
ATOM    241  N   GLU A 189     -14.335  -8.676  -5.080  1.00 59.76           N  
ANISOU  241  N   GLU A 189     9116   9200   4392  -1712    289   2472       N  
ATOM    242  CA  GLU A 189     -15.208  -7.777  -5.841  1.00 57.98           C  
ANISOU  242  CA  GLU A 189     8796   8976   4259  -1663    464   2332       C  
ATOM    243  C   GLU A 189     -14.693  -7.734  -7.265  1.00 59.79           C  
ANISOU  243  C   GLU A 189     8830   9157   4729  -1588    362   2264       C  
ATOM    244  O   GLU A 189     -13.522  -7.421  -7.485  1.00 58.93           O  
ANISOU  244  O   GLU A 189     8715   9049   4627  -1575    192   2230       O  
ATOM    245  CB  GLU A 189     -15.279  -6.362  -5.234  1.00 59.88           C  
ANISOU  245  CB  GLU A 189     9176   9275   4301  -1683    554   2207       C  
ATOM    246  CG  GLU A 189     -16.041  -6.297  -3.919  1.00 73.51           C  
ANISOU  246  CG  GLU A 189    11095  11045   5791  -1746    713   2252       C  
ATOM    247  CD  GLU A 189     -16.640  -4.952  -3.556  1.00 93.40           C  
ANISOU  247  CD  GLU A 189    13714  13604   8172  -1744    894   2114       C  
ATOM    248  OE1 GLU A 189     -15.931  -3.925  -3.669  1.00 79.33           O  
ANISOU  248  OE1 GLU A 189    11973  11836   6333  -1736    814   1997       O  
ATOM    249  OE2 GLU A 189     -17.809  -4.933  -3.108  1.00 91.37           O  
ANISOU  249  OE2 GLU A 189    13498  13359   7861  -1752   1119   2127       O  
ATOM    250  N   LYS A 190     -15.552  -8.099  -8.224  1.00 55.24           N  
ANISOU  250  N   LYS A 190     8099   8536   4354  -1542    462   2253       N  
ATOM    251  CA  LYS A 190     -15.213  -8.137  -9.640  1.00 53.24           C  
ANISOU  251  CA  LYS A 190     7667   8231   4332  -1471    387   2191       C  
ATOM    252  C   LYS A 190     -15.627  -6.854 -10.334  1.00 56.03           C  
ANISOU  252  C   LYS A 190     7960   8601   4729  -1426    493   2032       C  
ATOM    253  O   LYS A 190     -16.809  -6.500 -10.349  1.00 55.55           O  
ANISOU  253  O   LYS A 190     7881   8551   4675  -1424    678   1995       O  
ATOM    254  CB  LYS A 190     -15.868  -9.354 -10.317  1.00 55.60           C  
ANISOU  254  CB  LYS A 190     7842   8461   4824  -1453    413   2277       C  
ATOM    255  CG  LYS A 190     -15.394  -9.626 -11.739  1.00 70.99           C  
ANISOU  255  CG  LYS A 190     9629  10344   7001  -1383    312   2233       C  
ATOM    256  CD  LYS A 190     -16.206 -10.750 -12.362  1.00 83.76           C  
ANISOU  256  CD  LYS A 190    11144  11890   8792  -1375    354   2307       C  
ATOM    257  CE  LYS A 190     -15.755 -11.109 -13.753  1.00 95.24           C  
ANISOU  257  CE  LYS A 190    12459  13271  10459  -1308    257   2266       C  
ATOM    258  NZ  LYS A 190     -16.557 -12.231 -14.308  1.00105.30           N  
ANISOU  258  NZ  LYS A 190    13651  14468  11892  -1310    289   2338       N  
ATOM    259  N   SER A 191     -14.636  -6.164 -10.910  1.00 52.23           N  
ANISOU  259  N   SER A 191     7440   8120   4283  -1390    375   1943       N  
ATOM    260  CA  SER A 191     -14.798  -4.954 -11.714  1.00 50.71           C  
ANISOU  260  CA  SER A 191     7180   7935   4153  -1342    440   1793       C  
ATOM    261  C   SER A 191     -14.051  -5.150 -13.051  1.00 53.90           C  
ANISOU  261  C   SER A 191     7431   8287   4761  -1277    312   1760       C  
ATOM    262  O   SER A 191     -13.356  -6.159 -13.219  1.00 53.26           O  
ANISOU  262  O   SER A 191     7316   8169   4753  -1272    178   1851       O  
ATOM    263  CB  SER A 191     -14.325  -3.719 -10.948  1.00 53.45           C  
ANISOU  263  CB  SER A 191     7664   8339   4307  -1372    437   1707       C  
ATOM    264  OG  SER A 191     -13.072  -3.217 -11.379  1.00 59.43           O  
ANISOU  264  OG  SER A 191     8394   9094   5094  -1352    273   1654       O  
ATOM    265  N   TYR A 192     -14.212  -4.216 -14.004  1.00 49.78           N  
ANISOU  265  N   TYR A 192     6823   7759   4334  -1226    361   1636       N  
ATOM    266  CA  TYR A 192     -13.546  -4.319 -15.305  1.00 47.94           C  
ANISOU  266  CA  TYR A 192     6455   7477   4283  -1163    258   1599       C  
ATOM    267  C   TYR A 192     -12.586  -3.163 -15.568  1.00 51.50           C  
ANISOU  267  C   TYR A 192     6911   7952   4706  -1143    186   1496       C  
ATOM    268  O   TYR A 192     -12.870  -2.021 -15.193  1.00 51.43           O  
ANISOU  268  O   TYR A 192     6967   7983   4590  -1159    268   1408       O  
ATOM    269  CB  TYR A 192     -14.568  -4.484 -16.443  1.00 47.80           C  
ANISOU  269  CB  TYR A 192     6307   7414   4441  -1117    358   1563       C  
ATOM    270  CG  TYR A 192     -15.329  -5.790 -16.377  1.00 49.38           C  
ANISOU  270  CG  TYR A 192     6479   7574   4709  -1136    392   1674       C  
ATOM    271  CD1 TYR A 192     -16.515  -5.893 -15.655  1.00 52.15           C  
ANISOU  271  CD1 TYR A 192     6874   7947   4991  -1179    539   1714       C  
ATOM    272  CD2 TYR A 192     -14.865  -6.924 -17.035  1.00 49.68           C  
ANISOU  272  CD2 TYR A 192     6447   7545   4884  -1111    282   1742       C  
ATOM    273  CE1 TYR A 192     -17.217  -7.094 -15.585  1.00 53.41           C  
ANISOU  273  CE1 TYR A 192     7005   8068   5221  -1203    569   1823       C  
ATOM    274  CE2 TYR A 192     -15.557  -8.134 -16.970  1.00 51.21           C  
ANISOU  274  CE2 TYR A 192     6621   7694   5144  -1134    308   1845       C  
ATOM    275  CZ  TYR A 192     -16.733  -8.214 -16.243  1.00 60.04           C  
ANISOU  275  CZ  TYR A 192     7779   8839   6195  -1183    448   1888       C  
ATOM    276  OH  TYR A 192     -17.418  -9.401 -16.170  1.00 63.64           O  
ANISOU  276  OH  TYR A 192     8210   9247   6722  -1212    471   1995       O  
ATOM    277  N   LYS A 193     -11.433  -3.477 -16.191  1.00 46.91           N  
ANISOU  277  N   LYS A 193     6259   7339   4224  -1109     34   1511       N  
ATOM    278  CA  LYS A 193     -10.382  -2.521 -16.536  1.00 45.26           C  
ANISOU  278  CA  LYS A 193     6033   7144   4020  -1090    -54   1432       C  
ATOM    279  C   LYS A 193     -10.341  -2.322 -18.061  1.00 45.48           C  
ANISOU  279  C   LYS A 193     5916   7125   4239  -1013    -43   1359       C  
ATOM    280  O   LYS A 193     -10.183  -3.299 -18.802  1.00 44.10           O  
ANISOU  280  O   LYS A 193     5656   6895   4205   -973    -88   1411       O  
ATOM    281  CB  LYS A 193      -9.026  -3.016 -15.977  1.00 48.80           C  
ANISOU  281  CB  LYS A 193     6515   7596   4431  -1114   -238   1520       C  
ATOM    282  CG  LYS A 193      -7.791  -2.259 -16.468  1.00 63.37           C  
ANISOU  282  CG  LYS A 193     8309   9443   6325  -1090   -354   1464       C  
ATOM    283  CD  LYS A 193      -7.134  -1.429 -15.386  1.00 71.56           C  
ANISOU  283  CD  LYS A 193     9470  10535   7184  -1158   -431   1450       C  
ATOM    284  CE  LYS A 193      -5.993  -0.620 -15.952  1.00 80.77           C  
ANISOU  284  CE  LYS A 193    10572  11700   8418  -1137   -536   1392       C  
ATOM    285  NZ  LYS A 193      -5.328   0.200 -14.908  1.00 92.87           N  
ANISOU  285  NZ  LYS A 193    12228  13281   9780  -1213   -626   1377       N  
ATOM    286  N   ARG A 194     -10.502  -1.052 -18.518  1.00 39.77           N  
ANISOU  286  N   ARG A 194     5177   6420   3515   -994     21   1238       N  
ATOM    287  CA  ARG A 194     -10.452  -0.661 -19.931  1.00 36.99           C  
ANISOU  287  CA  ARG A 194     4705   6029   3322   -926     35   1160       C  
ATOM    288  C   ARG A 194      -9.000  -0.662 -20.412  1.00 40.67           C  
ANISOU  288  C   ARG A 194     5117   6478   3858   -898   -110   1167       C  
ATOM    289  O   ARG A 194      -8.120  -0.142 -19.722  1.00 42.04           O  
ANISOU  289  O   ARG A 194     5348   6686   3938   -933   -195   1168       O  
ATOM    290  CB  ARG A 194     -11.050   0.750 -20.152  1.00 34.40           C  
ANISOU  290  CB  ARG A 194     4384   5724   2961   -919    147   1036       C  
ATOM    291  CG  ARG A 194     -12.417   0.809 -20.831  1.00 32.97           C  
ANISOU  291  CG  ARG A 194     4143   5522   2864   -889    289    998       C  
ATOM    292  CD  ARG A 194     -12.507  -0.014 -22.093  1.00 30.76           C  
ANISOU  292  CD  ARG A 194     3746   5182   2761   -836    259   1020       C  
ATOM    293  NE  ARG A 194     -13.571   0.443 -22.985  1.00 32.63           N  
ANISOU  293  NE  ARG A 194     3912   5397   3088   -802    367    955       N  
ATOM    294  CZ  ARG A 194     -14.442  -0.354 -23.600  1.00 40.86           C  
ANISOU  294  CZ  ARG A 194     4892   6398   4235   -789    406    991       C  
ATOM    295  NH1 ARG A 194     -14.416  -1.665 -23.393  1.00 27.87           N  
ANISOU  295  NH1 ARG A 194     3249   4724   2616   -806    357   1089       N  
ATOM    296  NH2 ARG A 194     -15.346   0.154 -24.428  1.00 27.07           N  
ANISOU  296  NH2 ARG A 194     3079   4634   2573   -761    487    932       N  
ATOM    297  N   TYR A 195      -8.759  -1.247 -21.591  1.00 34.59           N  
ANISOU  297  N   TYR A 195     4240   5651   3252   -835   -137   1175       N  
ATOM    298  CA  TYR A 195      -7.446  -1.327 -22.216  1.00 32.71           C  
ANISOU  298  CA  TYR A 195     3932   5387   3110   -793   -251   1185       C  
ATOM    299  C   TYR A 195      -7.550  -0.940 -23.694  1.00 32.68           C  
ANISOU  299  C   TYR A 195     3831   5342   3245   -724   -202   1103       C  
ATOM    300  O   TYR A 195      -8.502  -1.328 -24.369  1.00 31.11           O  
ANISOU  300  O   TYR A 195     3600   5109   3113   -699   -122   1087       O  
ATOM    301  CB  TYR A 195      -6.807  -2.721 -22.014  1.00 33.87           C  
ANISOU  301  CB  TYR A 195     4063   5496   3311   -784   -353   1309       C  
ATOM    302  CG  TYR A 195      -5.495  -2.919 -22.746  1.00 35.96           C  
ANISOU  302  CG  TYR A 195     4240   5724   3700   -728   -455   1328       C  
ATOM    303  CD1 TYR A 195      -4.341  -2.246 -22.350  1.00 38.56           C  
ANISOU  303  CD1 TYR A 195     4568   6088   3996   -746   -553   1330       C  
ATOM    304  CD2 TYR A 195      -5.406  -3.779 -23.836  1.00 36.60           C  
ANISOU  304  CD2 TYR A 195     4241   5732   3935   -658   -450   1346       C  
ATOM    305  CE1 TYR A 195      -3.134  -2.414 -23.033  1.00 39.85           C  
ANISOU  305  CE1 TYR A 195     4636   6216   4288   -692   -636   1355       C  
ATOM    306  CE2 TYR A 195      -4.209  -3.946 -24.535  1.00 37.39           C  
ANISOU  306  CE2 TYR A 195     4260   5793   4153   -599   -523   1363       C  
ATOM    307  CZ  TYR A 195      -3.073  -3.266 -24.128  1.00 46.68           C  
ANISOU  307  CZ  TYR A 195     5422   7009   5307   -614   -613   1371       C  
ATOM    308  OH  TYR A 195      -1.890  -3.465 -24.808  1.00 48.35           O  
ANISOU  308  OH  TYR A 195     5541   7182   5650   -553   -678   1398       O  
ATOM    309  N   TYR A 196      -6.577  -0.163 -24.186  1.00 26.99           N  
ANISOU  309  N   TYR A 196     3066   4625   2566   -698   -253   1055       N  
ATOM    310  CA  TYR A 196      -6.576   0.281 -25.580  1.00 25.06           C  
ANISOU  310  CA  TYR A 196     2737   4343   2440   -634   -209    978       C  
ATOM    311  C   TYR A 196      -5.384  -0.328 -26.356  1.00 30.49           C  
ANISOU  311  C   TYR A 196     3345   4983   3256   -575   -292   1021       C  
ATOM    312  O   TYR A 196      -4.249   0.138 -26.182  1.00 30.43           O  
ANISOU  312  O   TYR A 196     3316   4994   3253   -578   -370   1029       O  
ATOM    313  CB  TYR A 196      -6.635   1.813 -25.661  1.00 23.85           C  
ANISOU  313  CB  TYR A 196     2596   4227   2237   -647   -163    874       C  
ATOM    314  CG  TYR A 196      -7.802   2.405 -24.900  1.00 23.87           C  
ANISOU  314  CG  TYR A 196     2678   4270   2121   -695    -67    832       C  
ATOM    315  CD1 TYR A 196      -9.096   2.323 -25.397  1.00 24.50           C  
ANISOU  315  CD1 TYR A 196     2741   4332   2236   -677     44    800       C  
ATOM    316  CD2 TYR A 196      -7.611   3.043 -23.675  1.00 25.35           C  
ANISOU  316  CD2 TYR A 196     2960   4510   2162   -759    -87    827       C  
ATOM    317  CE1 TYR A 196     -10.176   2.849 -24.692  1.00 25.86           C  
ANISOU  317  CE1 TYR A 196     2976   4538   2313   -715    145    769       C  
ATOM    318  CE2 TYR A 196      -8.686   3.594 -22.970  1.00 26.31           C  
ANISOU  318  CE2 TYR A 196     3161   4663   2173   -797     19    785       C  
ATOM    319  CZ  TYR A 196      -9.968   3.486 -23.481  1.00 29.17           C  
ANISOU  319  CZ  TYR A 196     3492   5006   2583   -771    140    759       C  
ATOM    320  OH  TYR A 196     -11.042   4.023 -22.820  1.00 25.25           O  
ANISOU  320  OH  TYR A 196     3062   4537   1994   -800    257    724       O  
ATOM    321  N   PRO A 197      -5.633  -1.396 -27.173  1.00 26.84           N  
ANISOU  321  N   PRO A 197     2842   4455   2899   -524   -276   1052       N  
ATOM    322  CA  PRO A 197      -4.526  -2.087 -27.859  1.00 27.21           C  
ANISOU  322  CA  PRO A 197     2823   4448   3068   -462   -341   1098       C  
ATOM    323  C   PRO A 197      -3.756  -1.329 -28.947  1.00 33.78           C  
ANISOU  323  C   PRO A 197     3583   5264   3986   -406   -332   1034       C  
ATOM    324  O   PRO A 197      -2.560  -1.584 -29.095  1.00 33.66           O  
ANISOU  324  O   PRO A 197     3515   5230   4045   -371   -400   1082       O  
ATOM    325  CB  PRO A 197      -5.155  -3.397 -28.345  1.00 28.48           C  
ANISOU  325  CB  PRO A 197     2984   4539   3299   -431   -315   1139       C  
ATOM    326  CG  PRO A 197      -6.476  -3.502 -27.645  1.00 32.23           C  
ANISOU  326  CG  PRO A 197     3523   5041   3682   -492   -259   1143       C  
ATOM    327  CD  PRO A 197      -6.909  -2.096 -27.413  1.00 27.67           C  
ANISOU  327  CD  PRO A 197     2966   4529   3018   -526   -203   1056       C  
ATOM    328  N   GLN A 198      -4.406  -0.400 -29.688  1.00 31.69           N  
ANISOU  328  N   GLN A 198     3315   5007   3719   -396   -249    935       N  
ATOM    329  CA  GLN A 198      -3.740   0.434 -30.716  1.00 31.85           C  
ANISOU  329  CA  GLN A 198     3276   5015   3810   -348   -231    872       C  
ATOM    330  C   GLN A 198      -3.841   1.907 -30.185  1.00 34.87           C  
ANISOU  330  C   GLN A 198     3684   5464   4101   -401   -218    805       C  
ATOM    331  O   GLN A 198      -4.710   2.650 -30.657  1.00 33.33           O  
ANISOU  331  O   GLN A 198     3502   5274   3887   -400   -138    726       O  
ATOM    332  CB  GLN A 198      -4.444   0.256 -32.086  1.00 32.83           C  
ANISOU  332  CB  GLN A 198     3385   5082   4006   -293   -152    815       C  
ATOM    333  CG  GLN A 198      -4.741  -1.195 -32.521  1.00 47.64           C  
ANISOU  333  CG  GLN A 198     5267   6886   5947   -257   -153    865       C  
ATOM    334  CD  GLN A 198      -3.531  -2.016 -32.925  1.00 74.87           C  
ANISOU  334  CD  GLN A 198     8672  10281   9495   -195   -200    924       C  
ATOM    335  OE1 GLN A 198      -2.470  -1.492 -33.300  1.00 72.89           O  
ANISOU  335  OE1 GLN A 198     8368  10034   9293   -160   -215    917       O  
ATOM    336  NE2 GLN A 198      -3.678  -3.338 -32.882  1.00 67.58           N  
ANISOU  336  NE2 GLN A 198     7767   9301   8611   -178   -221    988       N  
ATOM    337  N   PRO A 199      -3.046   2.297 -29.128  1.00 31.50           N  
ANISOU  337  N   PRO A 199     3274   5084   3611   -451   -298    840       N  
ATOM    338  CA  PRO A 199      -3.318   3.556 -28.408  1.00 31.15           C  
ANISOU  338  CA  PRO A 199     3284   5096   3454   -513   -285    779       C  
ATOM    339  C   PRO A 199      -3.336   4.916 -29.084  1.00 32.49           C  
ANISOU  339  C   PRO A 199     3433   5272   3639   -503   -233    681       C  
ATOM    340  O   PRO A 199      -4.414   5.491 -29.257  1.00 31.00           O  
ANISOU  340  O   PRO A 199     3279   5089   3411   -508   -143    612       O  
ATOM    341  CB  PRO A 199      -2.395   3.486 -27.182  1.00 34.42           C  
ANISOU  341  CB  PRO A 199     3728   5548   3801   -571   -402    848       C  
ATOM    342  CG  PRO A 199      -1.331   2.537 -27.557  1.00 39.12           C  
ANISOU  342  CG  PRO A 199     4244   6105   4512   -524   -478    935       C  
ATOM    343  CD  PRO A 199      -2.016   1.516 -28.410  1.00 34.18           C  
ANISOU  343  CD  PRO A 199     3598   5425   3965   -462   -409    944       C  
ATOM    344  N   GLN A 200      -2.155   5.452 -29.384  1.00 28.05           N  
ANISOU  344  N   GLN A 200     2815   4709   3135   -493   -290    683       N  
ATOM    345  CA  GLN A 200      -1.926   6.752 -30.003  1.00 27.19           C  
ANISOU  345  CA  GLN A 200     2680   4602   3050   -487   -256    603       C  
ATOM    346  C   GLN A 200      -2.728   6.964 -31.315  1.00 30.10           C  
ANISOU  346  C   GLN A 200     3023   4934   3480   -427   -147    537       C  
ATOM    347  O   GLN A 200      -3.393   7.998 -31.412  1.00 30.02           O  
ANISOU  347  O   GLN A 200     3044   4936   3427   -443    -86    459       O  
ATOM    348  CB  GLN A 200      -0.404   6.996 -30.216  1.00 28.99           C  
ANISOU  348  CB  GLN A 200     2828   4825   3362   -478   -340    643       C  
ATOM    349  CG  GLN A 200       0.496   6.389 -29.139  1.00 38.93           C  
ANISOU  349  CG  GLN A 200     4086   6106   4600   -521   -466    738       C  
ATOM    350  CD  GLN A 200       1.360   7.423 -28.485  1.00 70.26           C  
ANISOU  350  CD  GLN A 200     8057  10107   8531   -587   -552    731       C  
ATOM    351  OE1 GLN A 200       1.009   7.985 -27.451  1.00 69.20           O  
ANISOU  351  OE1 GLN A 200     8018  10010   8265   -662   -579    702       O  
ATOM    352  NE2 GLN A 200       2.518   7.696 -29.069  1.00 71.57           N  
ANISOU  352  NE2 GLN A 200     8122  10256   8814   -563   -595    757       N  
ATOM    353  N   PRO A 201      -2.731   6.041 -32.322  1.00 25.39           N  
ANISOU  353  N   PRO A 201     2380   4289   2979   -360   -122    563       N  
ATOM    354  CA  PRO A 201      -3.492   6.336 -33.555  1.00 23.92           C  
ANISOU  354  CA  PRO A 201     2183   4068   2837   -312    -32    497       C  
ATOM    355  C   PRO A 201      -4.999   6.501 -33.386  1.00 27.52           C  
ANISOU  355  C   PRO A 201     2693   4533   3229   -334     37    452       C  
ATOM    356  O   PRO A 201      -5.586   7.311 -34.095  1.00 27.33           O  
ANISOU  356  O   PRO A 201     2667   4500   3218   -318     99    386       O  
ATOM    357  CB  PRO A 201      -3.136   5.175 -34.502  1.00 25.12           C  
ANISOU  357  CB  PRO A 201     2295   4161   3087   -244    -31    541       C  
ATOM    358  CG  PRO A 201      -1.900   4.543 -33.925  1.00 29.56           C  
ANISOU  358  CG  PRO A 201     2821   4727   3685   -243   -116    625       C  
ATOM    359  CD  PRO A 201      -2.000   4.754 -32.443  1.00 26.27           C  
ANISOU  359  CD  PRO A 201     2451   4367   3164   -322   -175    649       C  
ATOM    360  N   ASN A 202      -5.610   5.804 -32.417  1.00 24.44           N  
ANISOU  360  N   ASN A 202     2350   4162   2775   -373     26    493       N  
ATOM    361  CA  ASN A 202      -7.061   5.809 -32.214  1.00 23.90           C  
ANISOU  361  CA  ASN A 202     2321   4100   2660   -392     98    466       C  
ATOM    362  C   ASN A 202      -7.644   6.633 -31.047  1.00 29.99           C  
ANISOU  362  C   ASN A 202     3154   4923   3318   -452    130    436       C  
ATOM    363  O   ASN A 202      -8.866   6.861 -31.015  1.00 28.34           O  
ANISOU  363  O   ASN A 202     2964   4717   3087   -459    209    404       O  
ATOM    364  CB  ASN A 202      -7.570   4.365 -32.196  1.00 21.30           C  
ANISOU  364  CB  ASN A 202     1997   3741   2355   -384     90    531       C  
ATOM    365  CG  ASN A 202      -7.215   3.623 -33.458  1.00 31.59           C  
ANISOU  365  CG  ASN A 202     3258   4982   3765   -321     78    544       C  
ATOM    366  OD1 ASN A 202      -7.823   3.818 -34.507  1.00 23.24           O  
ANISOU  366  OD1 ASN A 202     2186   3891   2753   -290    125    498       O  
ATOM    367  ND2 ASN A 202      -6.187   2.796 -33.403  1.00 20.01           N  
ANISOU  367  ND2 ASN A 202     1772   3494   2338   -300     14    606       N  
ATOM    368  N   ALA A 203      -6.772   7.088 -30.119  1.00 28.53           N  
ANISOU  368  N   ALA A 203     3002   4775   3066   -495     70    445       N  
ATOM    369  CA  ALA A 203      -7.090   7.843 -28.898  1.00 29.85           C  
ANISOU  369  CA  ALA A 203     3249   4986   3106   -557     87    417       C  
ATOM    370  C   ALA A 203      -8.006   9.054 -29.031  1.00 33.14           C  
ANISOU  370  C   ALA A 203     3690   5407   3494   -558    187    328       C  
ATOM    371  O   ALA A 203      -8.850   9.251 -28.166  1.00 32.02           O  
ANISOU  371  O   ALA A 203     3615   5290   3262   -593    247    313       O  
ATOM    372  CB  ALA A 203      -5.805   8.254 -28.188  1.00 31.67           C  
ANISOU  372  CB  ALA A 203     3500   5242   3289   -599    -13    434       C  
ATOM    373  N   GLN A 204      -7.795   9.907 -30.048  1.00 31.40           N  
ANISOU  373  N   GLN A 204     3421   5163   3346   -522    207    270       N  
ATOM    374  CA  GLN A 204      -8.608  11.123 -30.217  1.00 31.61           C  
ANISOU  374  CA  GLN A 204     3466   5187   3357   -518    297    187       C  
ATOM    375  C   GLN A 204     -10.056  10.859 -30.615  1.00 34.16           C  
ANISOU  375  C   GLN A 204     3773   5495   3712   -491    392    179       C  
ATOM    376  O   GLN A 204     -10.921  11.661 -30.278  1.00 32.87           O  
ANISOU  376  O   GLN A 204     3642   5338   3509   -500    476    130       O  
ATOM    377  CB  GLN A 204      -7.928  12.153 -31.135  1.00 32.57           C  
ANISOU  377  CB  GLN A 204     3545   5285   3543   -492    285    135       C  
ATOM    378  CG  GLN A 204      -6.644  12.718 -30.522  1.00 39.61           C  
ANISOU  378  CG  GLN A 204     4461   6196   4393   -536    202    132       C  
ATOM    379  CD  GLN A 204      -5.588  13.094 -31.527  1.00 47.07           C  
ANISOU  379  CD  GLN A 204     5333   7116   5434   -507    157    129       C  
ATOM    380  OE1 GLN A 204      -5.453  12.492 -32.603  1.00 37.28           O  
ANISOU  380  OE1 GLN A 204     4026   5849   4289   -452    160    157       O  
ATOM    381  NE2 GLN A 204      -4.764  14.063 -31.162  1.00 44.07           N  
ANISOU  381  NE2 GLN A 204     4972   6744   5031   -546    112    100       N  
ATOM    382  N   ILE A 205     -10.312   9.732 -31.313  1.00 32.14           N  
ANISOU  382  N   ILE A 205     3468   5215   3530   -460    377    230       N  
ATOM    383  CA  ILE A 205     -11.640   9.273 -31.748  1.00 31.90           C  
ANISOU  383  CA  ILE A 205     3411   5165   3545   -441    445    239       C  
ATOM    384  C   ILE A 205     -12.303   8.406 -30.668  1.00 33.32           C  
ANISOU  384  C   ILE A 205     3631   5368   3663   -480    467    296       C  
ATOM    385  O   ILE A 205     -13.472   8.621 -30.355  1.00 33.82           O  
ANISOU  385  O   ILE A 205     3700   5438   3713   -488    553    285       O  
ATOM    386  CB  ILE A 205     -11.571   8.596 -33.168  1.00 34.98           C  
ANISOU  386  CB  ILE A 205     3738   5506   4047   -391    414    256       C  
ATOM    387  CG1 ILE A 205     -11.868   9.603 -34.287  1.00 35.25           C  
ANISOU  387  CG1 ILE A 205     3737   5514   4141   -353    452    192       C  
ATOM    388  CG2 ILE A 205     -12.474   7.366 -33.325  1.00 35.69           C  
ANISOU  388  CG2 ILE A 205     3812   5573   4175   -391    421    310       C  
ATOM    389  CD1 ILE A 205     -10.713  10.289 -34.812  1.00 44.39           C  
ANISOU  389  CD1 ILE A 205     4884   6665   5316   -333    415    161       C  
ATOM    390  N   ILE A 206     -11.559   7.449 -30.092  1.00 28.73           N  
ANISOU  390  N   ILE A 206     3072   4797   3047   -502    392    361       N  
ATOM    391  CA  ILE A 206     -12.084   6.529 -29.069  1.00 28.46           C  
ANISOU  391  CA  ILE A 206     3080   4782   2952   -542    405    427       C  
ATOM    392  C   ILE A 206     -12.345   7.192 -27.724  1.00 32.26           C  
ANISOU  392  C   ILE A 206     3644   5310   3301   -591    456    408       C  
ATOM    393  O   ILE A 206     -13.379   6.929 -27.103  1.00 31.28           O  
ANISOU  393  O   ILE A 206     3547   5199   3139   -613    535    430       O  
ATOM    394  CB  ILE A 206     -11.301   5.181 -29.022  1.00 31.03           C  
ANISOU  394  CB  ILE A 206     3398   5092   3302   -542    309    511       C  
ATOM    395  CG1 ILE A 206     -11.740   4.304 -30.217  1.00 30.41           C  
ANISOU  395  CG1 ILE A 206     3255   4957   3342   -500    307    532       C  
ATOM    396  CG2 ILE A 206     -11.473   4.424 -27.682  1.00 31.73           C  
ANISOU  396  CG2 ILE A 206     3551   5211   3294   -595    300    583       C  
ATOM    397  CD1 ILE A 206     -10.751   3.469 -30.743  1.00 34.29           C  
ANISOU  397  CD1 ILE A 206     3723   5414   3893   -471    223    573       C  
ATOM    398  N   GLY A 207     -11.447   8.084 -27.326  1.00 29.03           N  
ANISOU  398  N   GLY A 207     3279   4922   2828   -609    417    366       N  
ATOM    399  CA  GLY A 207     -11.566   8.792 -26.061  1.00 30.22           C  
ANISOU  399  CA  GLY A 207     3531   5111   2839   -659    455    337       C  
ATOM    400  C   GLY A 207     -11.058   7.990 -24.885  1.00 36.07           C  
ANISOU  400  C   GLY A 207     4347   5883   3476   -713    387    410       C  
ATOM    401  O   GLY A 207     -10.170   7.145 -25.051  1.00 36.22           O  
ANISOU  401  O   GLY A 207     4334   5894   3533   -711    279    474       O  
ATOM    402  N   LEU A 208     -11.617   8.258 -23.684  1.00 34.41           N  
ANISOU  402  N   LEU A 208     4239   5704   3130   -759    454    404       N  
ATOM    403  CA  LEU A 208     -11.200   7.660 -22.410  1.00 35.63           C  
ANISOU  403  CA  LEU A 208     4493   5893   3152   -819    396    469       C  
ATOM    404  C   LEU A 208     -12.358   7.454 -21.422  1.00 41.42           C  
ANISOU  404  C   LEU A 208     5309   6649   3781   -849    518    488       C  
ATOM    405  O   LEU A 208     -13.363   8.156 -21.501  1.00 40.72           O  
ANISOU  405  O   LEU A 208     5223   6556   3694   -830    652    428       O  
ATOM    406  CB  LEU A 208     -10.167   8.602 -21.751  1.00 36.42           C  
ANISOU  406  CB  LEU A 208     4679   6013   3145   -864    318    423       C  
ATOM    407  CG  LEU A 208      -8.806   8.014 -21.390  1.00 42.72           C  
ANISOU  407  CG  LEU A 208     5487   6822   3921   -899    149    494       C  
ATOM    408  CD1 LEU A 208      -7.771   9.111 -21.229  1.00 43.51           C  
ANISOU  408  CD1 LEU A 208     5624   6929   3980   -930     65    435       C  
ATOM    409  CD2 LEU A 208      -8.857   7.210 -20.089  1.00 47.60           C  
ANISOU  409  CD2 LEU A 208     6212   7473   4401   -958    119    575       C  
ATOM    410  N   THR A 209     -12.176   6.529 -20.450  1.00 40.06           N  
ANISOU  410  N   THR A 209     5207   6501   3514   -896    472    575       N  
ATOM    411  CA  THR A 209     -13.131   6.276 -19.368  1.00 42.01           C  
ANISOU  411  CA  THR A 209     5549   6772   3639   -933    582    605       C  
ATOM    412  C   THR A 209     -12.637   6.846 -18.020  1.00 49.00           C  
ANISOU  412  C   THR A 209     6603   7696   4320  -1000    558    587       C  
ATOM    413  O   THR A 209     -11.461   7.203 -17.881  1.00 49.53           O  
ANISOU  413  O   THR A 209     6704   7769   4347  -1026    424    573       O  
ATOM    414  CB  THR A 209     -13.506   4.781 -19.235  1.00 49.71           C  
ANISOU  414  CB  THR A 209     6492   7743   4653   -941    571    723       C  
ATOM    415  OG1 THR A 209     -12.358   4.018 -18.853  1.00 47.65           O  
ANISOU  415  OG1 THR A 209     6259   7489   4357   -971    413    800       O  
ATOM    416  CG2 THR A 209     -14.179   4.211 -20.493  1.00 47.05           C  
ANISOU  416  CG2 THR A 209     6009   7365   4505   -884    607    738       C  
ATOM    417  N   ASN A 210     -13.556   6.923 -17.041  1.00 46.52           N  
ANISOU  417  N   ASN A 210     6394   7403   3879  -1028    689    589       N  
ATOM    418  CA  ASN A 210     -13.364   7.359 -15.650  1.00 47.89           C  
ANISOU  418  CA  ASN A 210     6755   7610   3832  -1095    700    576       C  
ATOM    419  C   ASN A 210     -12.720   6.212 -14.866  1.00 53.33           C  
ANISOU  419  C   ASN A 210     7506   8323   4436  -1150    574    694       C  
ATOM    420  O   ASN A 210     -12.509   5.125 -15.409  1.00 51.78           O  
ANISOU  420  O   ASN A 210     7203   8112   4359  -1130    498    781       O  
ATOM    421  CB  ASN A 210     -14.763   7.595 -15.011  1.00 46.45           C  
ANISOU  421  CB  ASN A 210     6641   7436   3570  -1093    915    557       C  
ATOM    422  CG  ASN A 210     -15.223   9.025 -14.877  1.00 64.58           C  
ANISOU  422  CG  ASN A 210     9005   9723   5811  -1076   1044    432       C  
ATOM    423  OD1 ASN A 210     -14.432   9.973 -14.802  1.00 67.02           O  
ANISOU  423  OD1 ASN A 210     9379  10025   6060  -1094    972    351       O  
ATOM    424  ND2 ASN A 210     -16.528   9.202 -14.770  1.00 49.96           N  
ANISOU  424  ND2 ASN A 210     7142   7865   3975  -1045   1243    417       N  
ATOM    425  N   SER A 211     -12.492   6.426 -13.559  1.00 53.16           N  
ANISOU  425  N   SER A 211     7666   8333   4201  -1219    563    700       N  
ATOM    426  CA  SER A 211     -12.033   5.382 -12.644  1.00 54.68           C  
ANISOU  426  CA  SER A 211     7942   8550   4284  -1277    461    818       C  
ATOM    427  C   SER A 211     -13.259   4.484 -12.374  1.00 59.98           C  
ANISOU  427  C   SER A 211     8603   9224   4960  -1269    611    894       C  
ATOM    428  O   SER A 211     -13.116   3.282 -12.129  1.00 59.72           O  
ANISOU  428  O   SER A 211     8558   9195   4937  -1288    543   1014       O  
ATOM    429  CB  SER A 211     -11.546   6.001 -11.337  1.00 60.40           C  
ANISOU  429  CB  SER A 211     8880   9304   4765  -1357    416    792       C  
ATOM    430  OG  SER A 211     -12.562   6.771 -10.716  1.00 71.16           O  
ANISOU  430  OG  SER A 211    10366  10675   5997  -1363    613    716       O  
ATOM    431  N   GLU A 212     -14.471   5.095 -12.465  1.00 57.18           N  
ANISOU  431  N   GLU A 212     8245   8865   4617  -1236    817    827       N  
ATOM    432  CA  GLU A 212     -15.786   4.470 -12.278  1.00 57.83           C  
ANISOU  432  CA  GLU A 212     8302   8948   4723  -1223    990    885       C  
ATOM    433  C   GLU A 212     -16.211   3.652 -13.503  1.00 60.80           C  
ANISOU  433  C   GLU A 212     8474   9290   5338  -1168    984    934       C  
ATOM    434  O   GLU A 212     -17.113   2.822 -13.393  1.00 61.72           O  
ANISOU  434  O   GLU A 212     8550   9402   5497  -1169   1076   1014       O  
ATOM    435  CB  GLU A 212     -16.856   5.533 -11.952  1.00 59.94           C  
ANISOU  435  CB  GLU A 212     8630   9218   4927  -1204   1210    791       C  
ATOM    436  CG  GLU A 212     -16.630   6.291 -10.647  1.00 73.96           C  
ANISOU  436  CG  GLU A 212    10634  11021   6447  -1260   1250    740       C  
ATOM    437  CD  GLU A 212     -15.878   7.610 -10.732  1.00 98.23           C  
ANISOU  437  CD  GLU A 212    13776  14085   9464  -1262   1188    611       C  
ATOM    438  OE1 GLU A 212     -16.202   8.518  -9.931  1.00 96.98           O  
ANISOU  438  OE1 GLU A 212    13775  13929   9142  -1280   1307    531       O  
ATOM    439  OE2 GLU A 212     -14.961   7.740 -11.578  1.00 87.77           O  
ANISOU  439  OE2 GLU A 212    12351  12744   8253  -1247   1025    591       O  
ATOM    440  N   GLY A 213     -15.562   3.892 -14.642  1.00 55.13           N  
ANISOU  440  N   GLY A 213     7635   8545   4767  -1125    876    888       N  
ATOM    441  CA  GLY A 213     -15.824   3.185 -15.891  1.00 53.64           C  
ANISOU  441  CA  GLY A 213     7267   8316   4796  -1073    851    922       C  
ATOM    442  C   GLY A 213     -16.634   3.945 -16.928  1.00 55.50           C  
ANISOU  442  C   GLY A 213     7389   8527   5173  -1012    962    836       C  
ATOM    443  O   GLY A 213     -16.932   3.393 -17.993  1.00 54.22           O  
ANISOU  443  O   GLY A 213     7086   8329   5184   -973    944    860       O  
ATOM    444  N   ARG A 214     -16.988   5.212 -16.634  1.00 50.91           N  
ANISOU  444  N   ARG A 214     6870   7957   4516  -1004   1072    736       N  
ATOM    445  CA  ARG A 214     -17.781   6.064 -17.519  1.00 49.59           C  
ANISOU  445  CA  ARG A 214     6604   7765   4474   -946   1183    655       C  
ATOM    446  C   ARG A 214     -16.914   6.779 -18.549  1.00 52.29           C  
ANISOU  446  C   ARG A 214     6879   8083   4904   -909   1074    576       C  
ATOM    447  O   ARG A 214     -15.868   7.320 -18.195  1.00 51.64           O  
ANISOU  447  O   ARG A 214     6881   8014   4726   -935    979    534       O  
ATOM    448  CB  ARG A 214     -18.550   7.106 -16.692  1.00 50.91           C  
ANISOU  448  CB  ARG A 214     6875   7947   4521   -949   1362    586       C  
ATOM    449  CG  ARG A 214     -19.634   7.843 -17.466  1.00 62.14           C  
ANISOU  449  CG  ARG A 214     8187   9342   6081   -887   1507    527       C  
ATOM    450  CD  ARG A 214     -20.324   8.883 -16.610  1.00 76.51           C  
ANISOU  450  CD  ARG A 214    10116  11170   7784   -883   1688    456       C  
ATOM    451  NE  ARG A 214     -21.460   9.484 -17.310  1.00 84.83           N  
ANISOU  451  NE  ARG A 214    11050  12194   8986   -819   1833    418       N  
ATOM    452  CZ  ARG A 214     -22.715   9.056 -17.210  1.00 97.77           C  
ANISOU  452  CZ  ARG A 214    12616  13831  10700   -803   1982    478       C  
ATOM    453  NH1 ARG A 214     -23.013   8.023 -16.430  1.00 82.17           N  
ANISOU  453  NH1 ARG A 214    10680  11880   8659   -848   2014    579       N  
ATOM    454  NH2 ARG A 214     -23.683   9.662 -17.885  1.00 85.51           N  
ANISOU  454  NH2 ARG A 214    10946  12250   9295   -745   2097    446       N  
ATOM    455  N   GLY A 215     -17.396   6.830 -19.793  1.00 47.33           N  
ANISOU  455  N   GLY A 215     6106   7421   4457   -854   1093    557       N  
ATOM    456  CA  GLY A 215     -16.740   7.541 -20.881  1.00 45.59           C  
ANISOU  456  CA  GLY A 215     5814   7175   4333   -813   1014    484       C  
ATOM    457  C   GLY A 215     -16.716   9.028 -20.598  1.00 49.44           C  
ANISOU  457  C   GLY A 215     6372   7666   4746   -806   1083    374       C  
ATOM    458  O   GLY A 215     -17.758   9.610 -20.284  1.00 49.24           O  
ANISOU  458  O   GLY A 215     6365   7640   4706   -791   1240    339       O  
ATOM    459  N   ILE A 216     -15.512   9.633 -20.647  1.00 46.05           N  
ANISOU  459  N   ILE A 216     5988   7238   4272   -820    968    324       N  
ATOM    460  CA  ILE A 216     -15.289  11.054 -20.358  1.00 46.21           C  
ANISOU  460  CA  ILE A 216     6089   7253   4214   -823   1007    218       C  
ATOM    461  C   ILE A 216     -14.767  11.866 -21.576  1.00 47.41           C  
ANISOU  461  C   ILE A 216     6151   7373   4491   -779    951    149       C  
ATOM    462  O   ILE A 216     -14.693  13.100 -21.525  1.00 47.33           O  
ANISOU  462  O   ILE A 216     6189   7347   4446   -774    992     58       O  
ATOM    463  CB  ILE A 216     -14.462  11.217 -19.035  1.00 50.86           C  
ANISOU  463  CB  ILE A 216     6849   7875   4602   -896    942    215       C  
ATOM    464  CG1 ILE A 216     -14.800  12.517 -18.265  1.00 52.84           C  
ANISOU  464  CG1 ILE A 216     7235   8120   4720   -911   1055    114       C  
ATOM    465  CG2 ILE A 216     -12.955  11.034 -19.236  1.00 50.71           C  
ANISOU  465  CG2 ILE A 216     6821   7859   4586   -924    742    235       C  
ATOM    466  CD1 ILE A 216     -16.223  12.599 -17.633  1.00 61.49           C  
ANISOU  466  CD1 ILE A 216     8381   9220   5763   -896   1265    110       C  
ATOM    467  N   GLU A 217     -14.449  11.164 -22.678  1.00 40.72           N  
ANISOU  467  N   GLU A 217     5177   6509   3787   -747    865    194       N  
ATOM    468  CA  GLU A 217     -13.958  11.760 -23.919  1.00 38.51           C  
ANISOU  468  CA  GLU A 217     4806   6197   3628   -704    812    145       C  
ATOM    469  C   GLU A 217     -14.305  10.865 -25.112  1.00 37.62           C  
ANISOU  469  C   GLU A 217     4561   6061   3673   -658    791    198       C  
ATOM    470  O   GLU A 217     -14.533   9.665 -24.929  1.00 36.06           O  
ANISOU  470  O   GLU A 217     4346   5870   3485   -670    770    280       O  
ATOM    471  CB  GLU A 217     -12.429  11.968 -23.841  1.00 40.25           C  
ANISOU  471  CB  GLU A 217     5059   6425   3811   -734    663    138       C  
ATOM    472  CG  GLU A 217     -11.961  13.317 -24.357  1.00 53.31           C  
ANISOU  472  CG  GLU A 217     6709   8054   5492   -720    656     47       C  
ATOM    473  CD  GLU A 217     -11.781  14.374 -23.283  1.00 80.29           C  
ANISOU  473  CD  GLU A 217    10264  11479   8762   -768    682    -23       C  
ATOM    474  OE1 GLU A 217     -12.797  14.960 -22.845  1.00 88.51           O  
ANISOU  474  OE1 GLU A 217    11361  12514   9756   -759    821    -72       O  
ATOM    475  OE2 GLU A 217     -10.620  14.633 -22.895  1.00 72.04           O  
ANISOU  475  OE2 GLU A 217     9273  10444   7656   -816    564    -28       O  
ATOM    476  N   GLY A 218     -14.334  11.467 -26.306  1.00 32.08           N  
ANISOU  476  N   GLY A 218     3776   5326   3087   -609    793    151       N  
ATOM    477  CA  GLY A 218     -14.575  10.815 -27.595  1.00 30.55           C  
ANISOU  477  CA  GLY A 218     3468   5101   3038   -564    764    184       C  
ATOM    478  C   GLY A 218     -15.790   9.911 -27.670  1.00 34.22           C  
ANISOU  478  C   GLY A 218     3885   5559   3557   -558    828    243       C  
ATOM    479  O   GLY A 218     -16.843  10.223 -27.098  1.00 34.94           O  
ANISOU  479  O   GLY A 218     3994   5660   3621   -563    944    235       O  
ATOM    480  N   LEU A 219     -15.636   8.771 -28.371  1.00 29.57           N  
ANISOU  480  N   LEU A 219     3237   4949   3049   -547    754    304       N  
ATOM    481  CA  LEU A 219     -16.694   7.768 -28.555  1.00 29.06           C  
ANISOU  481  CA  LEU A 219     3122   4870   3052   -547    789    368       C  
ATOM    482  C   LEU A 219     -17.066   7.019 -27.278  1.00 34.53           C  
ANISOU  482  C   LEU A 219     3872   5593   3654   -595    827    434       C  
ATOM    483  O   LEU A 219     -18.192   6.530 -27.168  1.00 35.82           O  
ANISOU  483  O   LEU A 219     4000   5750   3858   -603    900    477       O  
ATOM    484  CB  LEU A 219     -16.354   6.786 -29.679  1.00 28.29           C  
ANISOU  484  CB  LEU A 219     2961   4730   3057   -524    695    407       C  
ATOM    485  CG  LEU A 219     -16.490   7.306 -31.112  1.00 31.77           C  
ANISOU  485  CG  LEU A 219     3333   5131   3606   -476    682    358       C  
ATOM    486  CD1 LEU A 219     -15.892   6.325 -32.080  1.00 30.72           C  
ANISOU  486  CD1 LEU A 219     3171   4958   3543   -455    585    390       C  
ATOM    487  CD2 LEU A 219     -17.953   7.563 -31.488  1.00 33.82           C  
ANISOU  487  CD2 LEU A 219     3533   5375   3942   -465    767    356       C  
ATOM    488  N   GLU A 220     -16.136   6.929 -26.315  1.00 31.26           N  
ANISOU  488  N   GLU A 220     3547   5211   3121   -631    776    447       N  
ATOM    489  CA  GLU A 220     -16.403   6.302 -25.020  1.00 32.19           C  
ANISOU  489  CA  GLU A 220     3741   5360   3129   -681    809    509       C  
ATOM    490  C   GLU A 220     -17.488   7.117 -24.328  1.00 39.12           C  
ANISOU  490  C   GLU A 220     4655   6258   3949   -688    964    472       C  
ATOM    491  O   GLU A 220     -18.393   6.537 -23.738  1.00 39.34           O  
ANISOU  491  O   GLU A 220     4690   6296   3961   -709   1046    529       O  
ATOM    492  CB  GLU A 220     -15.135   6.227 -24.141  1.00 33.29           C  
ANISOU  492  CB  GLU A 220     3976   5530   3144   -719    712    523       C  
ATOM    493  CG  GLU A 220     -14.116   5.184 -24.574  1.00 35.36           C  
ANISOU  493  CG  GLU A 220     4203   5772   3458   -715    571    586       C  
ATOM    494  CD  GLU A 220     -14.334   3.760 -24.103  1.00 48.05           C  
ANISOU  494  CD  GLU A 220     5821   7376   5059   -742    546    692       C  
ATOM    495  OE1 GLU A 220     -15.492   3.282 -24.120  1.00 52.51           O  
ANISOU  495  OE1 GLU A 220     6358   7931   5662   -746    632    726       O  
ATOM    496  OE2 GLU A 220     -13.329   3.105 -23.745  1.00 36.01           O  
ANISOU  496  OE2 GLU A 220     4326   5855   3502   -760    435    748       O  
ATOM    497  N   MET A 221     -17.412   8.461 -24.448  1.00 38.01           N  
ANISOU  497  N   MET A 221     4534   6117   3789   -666   1008    378       N  
ATOM    498  CA  MET A 221     -18.379   9.403 -23.886  1.00 39.63           C  
ANISOU  498  CA  MET A 221     4776   6331   3951   -660   1163    329       C  
ATOM    499  C   MET A 221     -19.664   9.374 -24.696  1.00 42.82           C  
ANISOU  499  C   MET A 221     5059   6706   4502   -619   1253    342       C  
ATOM    500  O   MET A 221     -20.711   9.048 -24.149  1.00 43.89           O  
ANISOU  500  O   MET A 221     5187   6852   4639   -629   1364    387       O  
ATOM    501  CB  MET A 221     -17.806  10.829 -23.853  1.00 42.34           C  
ANISOU  501  CB  MET A 221     5176   6671   4238   -649   1169    225       C  
ATOM    502  CG  MET A 221     -18.752  11.835 -23.234  1.00 47.75           C  
ANISOU  502  CG  MET A 221     5913   7356   4872   -637   1335    168       C  
ATOM    503  SD  MET A 221     -18.146  13.526 -23.373  1.00 53.09           S  
ANISOU  503  SD  MET A 221     6647   8011   5513   -619   1340     42       S  
ATOM    504  CE  MET A 221     -18.993  14.280 -21.970  1.00 51.85           C  
ANISOU  504  CE  MET A 221     6624   7864   5214   -631   1529     -4       C  
ATOM    505  N   GLN A 222     -19.581   9.713 -25.997  1.00 37.11           N  
ANISOU  505  N   GLN A 222     4244   5950   3908   -576   1201    308       N  
ATOM    506  CA  GLN A 222     -20.727   9.774 -26.896  1.00 35.96           C  
ANISOU  506  CA  GLN A 222     3981   5773   3910   -538   1261    318       C  
ATOM    507  C   GLN A 222     -21.643   8.527 -26.813  1.00 37.89           C  
ANISOU  507  C   GLN A 222     4164   6013   4218   -560   1284    416       C  
ATOM    508  O   GLN A 222     -22.828   8.669 -26.527  1.00 36.88           O  
ANISOU  508  O   GLN A 222     3993   5885   4134   -554   1407    438       O  
ATOM    509  CB  GLN A 222     -20.289  10.097 -28.344  1.00 35.66           C  
ANISOU  509  CB  GLN A 222     3869   5698   3982   -498   1168    281       C  
ATOM    510  CG  GLN A 222     -21.445  10.603 -29.208  1.00 46.97           C  
ANISOU  510  CG  GLN A 222     5198   7098   5550   -457   1235    271       C  
ATOM    511  CD  GLN A 222     -21.086  10.867 -30.649  1.00 61.72           C  
ANISOU  511  CD  GLN A 222     7004   8929   7517   -420   1143    241       C  
ATOM    512  OE1 GLN A 222     -20.997  12.019 -31.078  1.00 57.28           O  
ANISOU  512  OE1 GLN A 222     6437   8353   6975   -387   1166    175       O  
ATOM    513  NE2 GLN A 222     -20.985   9.816 -31.456  1.00 52.87           N  
ANISOU  513  NE2 GLN A 222     5837   7785   6465   -425   1047    290       N  
ATOM    514  N   LEU A 223     -21.069   7.327 -26.998  1.00 32.90           N  
ANISOU  514  N   LEU A 223     3533   5376   3591   -585   1171    477       N  
ATOM    515  CA  LEU A 223     -21.786   6.052 -26.979  1.00 32.20           C  
ANISOU  515  CA  LEU A 223     3394   5275   3566   -612   1170    573       C  
ATOM    516  C   LEU A 223     -21.752   5.343 -25.614  1.00 37.92           C  
ANISOU  516  C   LEU A 223     4202   6035   4170   -663   1208    638       C  
ATOM    517  O   LEU A 223     -21.804   4.113 -25.565  1.00 39.12           O  
ANISOU  517  O   LEU A 223     4341   6175   4350   -692   1157    720       O  
ATOM    518  CB  LEU A 223     -21.206   5.130 -28.075  1.00 30.84           C  
ANISOU  518  CB  LEU A 223     3176   5062   3481   -605   1025    600       C  
ATOM    519  CG  LEU A 223     -21.038   5.713 -29.484  1.00 33.23           C  
ANISOU  519  CG  LEU A 223     3415   5327   3882   -558    969    540       C  
ATOM    520  CD1 LEU A 223     -20.337   4.731 -30.384  1.00 32.36           C  
ANISOU  520  CD1 LEU A 223     3292   5177   3824   -553    836    565       C  
ATOM    521  CD2 LEU A 223     -22.368   6.132 -30.085  1.00 34.04           C  
ANISOU  521  CD2 LEU A 223     3422   5408   4104   -539   1041    540       C  
ATOM    522  N   ASN A 224     -21.687   6.102 -24.510  1.00 34.73           N  
ANISOU  522  N   ASN A 224     3894   5669   3631   -675   1298    602       N  
ATOM    523  CA  ASN A 224     -21.622   5.528 -23.164  1.00 35.22           C  
ANISOU  523  CA  ASN A 224     4057   5769   3557   -725   1336    660       C  
ATOM    524  C   ASN A 224     -22.823   4.684 -22.740  1.00 40.70           C  
ANISOU  524  C   ASN A 224     4707   6462   4296   -751   1435    754       C  
ATOM    525  O   ASN A 224     -22.619   3.673 -22.076  1.00 42.73           O  
ANISOU  525  O   ASN A 224     5011   6729   4494   -795   1399    835       O  
ATOM    526  CB  ASN A 224     -21.307   6.584 -22.113  1.00 34.18           C  
ANISOU  526  CB  ASN A 224     4053   5673   3261   -735   1412    593       C  
ATOM    527  CG  ASN A 224     -20.971   5.994 -20.773  1.00 50.76           C  
ANISOU  527  CG  ASN A 224     6281   7810   5197   -792   1416    650       C  
ATOM    528  OD1 ASN A 224     -19.894   5.425 -20.566  1.00 46.87           O  
ANISOU  528  OD1 ASN A 224     5841   7326   4641   -820   1280    681       O  
ATOM    529  ND2 ASN A 224     -21.920   6.054 -19.856  1.00 41.47           N  
ANISOU  529  ND2 ASN A 224     5150   6654   3954   -808   1575    676       N  
ATOM    530  N   THR A 225     -24.055   5.091 -23.075  1.00 35.73           N  
ANISOU  530  N   THR A 225     3984   5818   3774   -726   1557    752       N  
ATOM    531  CA  THR A 225     -25.251   4.334 -22.667  1.00 35.54           C  
ANISOU  531  CA  THR A 225     3903   5793   3809   -753   1660    848       C  
ATOM    532  C   THR A 225     -25.283   2.969 -23.357  1.00 38.06           C  
ANISOU  532  C   THR A 225     4145   6076   4241   -779   1540    933       C  
ATOM    533  O   THR A 225     -25.561   1.970 -22.707  1.00 39.17           O  
ANISOU  533  O   THR A 225     4305   6222   4358   -825   1558   1026       O  
ATOM    534  CB  THR A 225     -26.538   5.171 -22.845  1.00 42.89           C  
ANISOU  534  CB  THR A 225     4740   6715   4842   -716   1819    828       C  
ATOM    535  OG1 THR A 225     -26.358   6.453 -22.225  1.00 44.52           O  
ANISOU  535  OG1 THR A 225     5036   6945   4934   -687   1922    737       O  
ATOM    536  CG2 THR A 225     -27.778   4.492 -22.251  1.00 39.93           C  
ANISOU  536  CG2 THR A 225     4308   6344   4518   -745   1952    931       C  
ATOM    537  N   ARG A 226     -24.956   2.922 -24.654  1.00 33.08           N  
ANISOU  537  N   ARG A 226     3441   5404   3723   -751   1417    901       N  
ATOM    538  CA  ARG A 226     -24.923   1.674 -25.413  1.00 31.99           C  
ANISOU  538  CA  ARG A 226     3245   5221   3691   -772   1296    967       C  
ATOM    539  C   ARG A 226     -23.783   0.751 -24.946  1.00 33.70           C  
ANISOU  539  C   ARG A 226     3556   5440   3807   -801   1186   1006       C  
ATOM    540  O   ARG A 226     -23.999  -0.454 -24.785  1.00 33.02           O  
ANISOU  540  O   ARG A 226     3461   5332   3754   -840   1152   1097       O  
ATOM    541  CB  ARG A 226     -24.825   1.958 -26.924  1.00 31.87           C  
ANISOU  541  CB  ARG A 226     3147   5159   3803   -731   1200    913       C  
ATOM    542  CG  ARG A 226     -26.154   2.427 -27.545  1.00 33.44           C  
ANISOU  542  CG  ARG A 226     3222   5337   4145   -715   1275    917       C  
ATOM    543  CD  ARG A 226     -25.947   3.084 -28.891  1.00 36.25           C  
ANISOU  543  CD  ARG A 226     3526   5659   4587   -669   1196    844       C  
ATOM    544  NE  ARG A 226     -25.628   2.107 -29.931  1.00 44.51           N  
ANISOU  544  NE  ARG A 226     4551   6652   5710   -679   1048    868       N  
ATOM    545  CZ  ARG A 226     -25.141   2.407 -31.131  1.00 61.19           C  
ANISOU  545  CZ  ARG A 226     6650   8731   7870   -644    952    809       C  
ATOM    546  NH1 ARG A 226     -24.896   3.671 -31.460  1.00 50.41           N  
ANISOU  546  NH1 ARG A 226     5283   7381   6489   -598    981    727       N  
ATOM    547  NH2 ARG A 226     -24.883   1.445 -32.007  1.00 47.82           N  
ANISOU  547  NH2 ARG A 226     4952   6984   6235   -655    830    832       N  
ATOM    548  N   LEU A 227     -22.593   1.325 -24.697  1.00 28.45           N  
ANISOU  548  N   LEU A 227     2980   4803   3029   -784   1133    942       N  
ATOM    549  CA  LEU A 227     -21.388   0.604 -24.260  1.00 27.30           C  
ANISOU  549  CA  LEU A 227     2919   4661   2791   -805   1020    975       C  
ATOM    550  C   LEU A 227     -21.388   0.144 -22.789  1.00 31.28           C  
ANISOU  550  C   LEU A 227     3522   5207   3156   -857   1072   1046       C  
ATOM    551  O   LEU A 227     -20.754  -0.865 -22.488  1.00 32.15           O  
ANISOU  551  O   LEU A 227     3674   5306   3235   -883    980   1115       O  
ATOM    552  CB  LEU A 227     -20.119   1.434 -24.544  1.00 25.97           C  
ANISOU  552  CB  LEU A 227     2797   4507   2565   -772    939    887       C  
ATOM    553  CG  LEU A 227     -19.674   1.613 -25.997  1.00 28.81           C  
ANISOU  553  CG  LEU A 227     3085   4822   3041   -724    848    833       C  
ATOM    554  CD1 LEU A 227     -18.696   2.757 -26.109  1.00 28.60           C  
ANISOU  554  CD1 LEU A 227     3096   4817   2952   -695    817    742       C  
ATOM    555  CD2 LEU A 227     -19.007   0.359 -26.543  1.00 30.74           C  
ANISOU  555  CD2 LEU A 227     3317   5020   3344   -724    720    889       C  
ATOM    556  N   ALA A 228     -22.033   0.888 -21.873  1.00 27.52           N  
ANISOU  556  N   ALA A 228     3094   4774   2590   -869   1217   1029       N  
ATOM    557  CA  ALA A 228     -22.037   0.550 -20.437  1.00 28.37           C  
ANISOU  557  CA  ALA A 228     3316   4923   2541   -919   1277   1091       C  
ATOM    558  C   ALA A 228     -22.900  -0.651 -20.065  1.00 35.70           C  
ANISOU  558  C   ALA A 228     4212   5836   3515   -961   1325   1212       C  
ATOM    559  O   ALA A 228     -22.540  -1.413 -19.164  1.00 35.24           O  
ANISOU  559  O   ALA A 228     4242   5794   3354  -1006   1298   1289       O  
ATOM    560  CB  ALA A 228     -22.438   1.751 -19.600  1.00 29.32           C  
ANISOU  560  CB  ALA A 228     3512   5087   2542   -915   1428   1027       C  
ATOM    561  N   GLY A 229     -24.043  -0.789 -20.731  1.00 34.45           N  
ANISOU  561  N   GLY A 229     3929   5647   3513   -951   1393   1233       N  
ATOM    562  CA  GLY A 229     -24.981  -1.864 -20.440  1.00 35.82           C  
ANISOU  562  CA  GLY A 229     4054   5801   3753   -995   1447   1349       C  
ATOM    563  C   GLY A 229     -25.691  -1.620 -19.127  1.00 42.36           C  
ANISOU  563  C   GLY A 229     4952   6678   4465  -1025   1624   1391       C  
ATOM    564  O   GLY A 229     -25.725  -0.483 -18.644  1.00 42.78           O  
ANISOU  564  O   GLY A 229     5065   6771   4420  -1002   1727   1314       O  
ATOM    565  N   VAL A 230     -26.259  -2.687 -18.531  1.00 40.00           N  
ANISOU  565  N   VAL A 230     4653   6372   4173  -1078   1667   1512       N  
ATOM    566  CA  VAL A 230     -27.012  -2.574 -17.277  1.00 40.73           C  
ANISOU  566  CA  VAL A 230     4810   6508   4158  -1109   1851   1567       C  
ATOM    567  C   VAL A 230     -26.432  -3.508 -16.200  1.00 45.80           C  
ANISOU  567  C   VAL A 230     5586   7168   4647  -1167   1809   1660       C  
ATOM    568  O   VAL A 230     -26.263  -4.711 -16.441  1.00 44.54           O  
ANISOU  568  O   VAL A 230     5395   6969   4558  -1200   1700   1749       O  
ATOM    569  CB  VAL A 230     -28.539  -2.794 -17.496  1.00 44.78           C  
ANISOU  569  CB  VAL A 230     5180   7000   4835  -1118   1994   1635       C  
ATOM    570  CG1 VAL A 230     -29.332  -2.587 -16.204  1.00 46.25           C  
ANISOU  570  CG1 VAL A 230     5431   7231   4911  -1141   2212   1686       C  
ATOM    571  CG2 VAL A 230     -29.087  -1.890 -18.602  1.00 43.32           C  
ANISOU  571  CG2 VAL A 230     4857   6793   4810  -1061   2014   1551       C  
ATOM    572  N   ASP A 231     -26.139  -2.944 -15.011  1.00 44.10           N  
ANISOU  572  N   ASP A 231     5527   7008   4222  -1181   1894   1640       N  
ATOM    573  CA  ASP A 231     -25.626  -3.699 -13.866  1.00 45.40           C  
ANISOU  573  CA  ASP A 231     5837   7197   4215  -1239   1866   1729       C  
ATOM    574  C   ASP A 231     -26.714  -4.609 -13.304  1.00 51.97           C  
ANISOU  574  C   ASP A 231     6639   8023   5086  -1287   1994   1864       C  
ATOM    575  O   ASP A 231     -27.892  -4.231 -13.256  1.00 51.68           O  
ANISOU  575  O   ASP A 231     6527   7991   5116  -1277   2177   1870       O  
ATOM    576  CB  ASP A 231     -25.136  -2.753 -12.745  1.00 48.23           C  
ANISOU  576  CB  ASP A 231     6381   7615   4330  -1245   1934   1665       C  
ATOM    577  CG  ASP A 231     -23.841  -1.981 -12.987  1.00 58.75           C  
ANISOU  577  CG  ASP A 231     7786   8960   5578  -1220   1786   1555       C  
ATOM    578  OD1 ASP A 231     -23.073  -2.365 -13.903  1.00 58.13           O  
ANISOU  578  OD1 ASP A 231     7635   8847   5604  -1202   1606   1546       O  
ATOM    579  OD2 ASP A 231     -23.566  -1.031 -12.219  1.00 65.40           O  
ANISOU  579  OD2 ASP A 231     8765   9842   6243  -1222   1849   1483       O  
ATOM    580  N   GLY A 232     -26.297  -5.793 -12.872  1.00 50.29           N  
ANISOU  580  N   GLY A 232     6480   7796   4833  -1338   1898   1976       N  
ATOM    581  CA  GLY A 232     -27.173  -6.775 -12.249  1.00 51.71           C  
ANISOU  581  CA  GLY A 232     6649   7966   5031  -1394   2001   2119       C  
ATOM    582  C   GLY A 232     -27.130  -6.715 -10.732  1.00 57.27           C  
ANISOU  582  C   GLY A 232     7538   8727   5494  -1438   2114   2170       C  
ATOM    583  O   GLY A 232     -26.328  -5.969 -10.159  1.00 56.07           O  
ANISOU  583  O   GLY A 232     7534   8619   5153  -1429   2090   2094       O  
ATOM    584  N   GLU A 233     -28.008  -7.502 -10.074  1.00 56.24           N  
ANISOU  584  N   GLU A 233     7406   8595   5368  -1489   2239   2303       N  
ATOM    585  CA  GLU A 233     -28.138  -7.602  -8.613  1.00 58.77           C  
ANISOU  585  CA  GLU A 233     7902   8964   5464  -1538   2369   2376       C  
ATOM    586  C   GLU A 233     -28.182  -9.070  -8.181  1.00 62.79           C  
ANISOU  586  C   GLU A 233     8430   9445   5984  -1606   2314   2545       C  
ATOM    587  O   GLU A 233     -28.894  -9.873  -8.790  1.00 62.27           O  
ANISOU  587  O   GLU A 233     8210   9327   6122  -1622   2318   2626       O  
ATOM    588  CB  GLU A 233     -29.397  -6.866  -8.107  1.00 62.03           C  
ANISOU  588  CB  GLU A 233     8299   9409   5862  -1525   2652   2366       C  
ATOM    589  CG  GLU A 233     -29.345  -5.351  -8.252  1.00 77.77           C  
ANISOU  589  CG  GLU A 233    10318  11432   7799  -1460   2734   2204       C  
ATOM    590  CD  GLU A 233     -30.236  -4.764  -9.331  1.00104.00           C  
ANISOU  590  CD  GLU A 233    13432  14726  11360  -1402   2811   2142       C  
ATOM    591  OE1 GLU A 233     -31.475  -4.780  -9.150  1.00111.03           O  
ANISOU  591  OE1 GLU A 233    14230  15614  12343  -1403   3014   2203       O  
ATOM    592  OE2 GLU A 233     -29.695  -4.253 -10.339  1.00 92.18           O  
ANISOU  592  OE2 GLU A 233    11863  13209   9954  -1356   2674   2037       O  
ATOM    593  N   GLN A 234     -27.420  -9.418  -7.134  1.00 59.49           N  
ANISOU  593  N   GLN A 234     8202   9057   5346  -1650   2256   2602       N  
ATOM    594  CA  GLN A 234     -27.329 -10.786  -6.621  1.00 59.64           C  
ANISOU  594  CA  GLN A 234     8264   9049   5348  -1716   2191   2767       C  
ATOM    595  C   GLN A 234     -27.334 -10.784  -5.101  1.00 64.46           C  
ANISOU  595  C   GLN A 234     9087   9716   5689  -1769   2307   2839       C  
ATOM    596  O   GLN A 234     -26.633  -9.975  -4.493  1.00 63.99           O  
ANISOU  596  O   GLN A 234     9191   9707   5416  -1761   2288   2759       O  
ATOM    597  CB  GLN A 234     -26.042 -11.443  -7.141  1.00 59.54           C  
ANISOU  597  CB  GLN A 234     8257   8995   5370  -1711   1914   2773       C  
ATOM    598  CG  GLN A 234     -26.000 -12.956  -7.030  1.00 71.02           C  
ANISOU  598  CG  GLN A 234     9695  10393   6898  -1764   1821   2936       C  
ATOM    599  CD  GLN A 234     -24.723 -13.497  -7.613  1.00 85.60           C  
ANISOU  599  CD  GLN A 234    11537  12193   8793  -1744   1561   2929       C  
ATOM    600  OE1 GLN A 234     -23.635 -13.342  -7.048  1.00 80.57           O  
ANISOU  600  OE1 GLN A 234    11037  11587   7988  -1747   1442   2919       O  
ATOM    601  NE2 GLN A 234     -24.827 -14.142  -8.763  1.00 76.87           N  
ANISOU  601  NE2 GLN A 234    10274  11010   7923  -1722   1466   2935       N  
ATOM    602  N   LYS A 235     -28.117 -11.699  -4.494  1.00 62.25           N  
ANISOU  602  N   LYS A 235     8810   9424   5417  -1826   2421   2994       N  
ATOM    603  CA  LYS A 235     -28.227 -11.882  -3.040  1.00 63.83           C  
ANISOU  603  CA  LYS A 235     9214   9672   5367  -1885   2541   3090       C  
ATOM    604  C   LYS A 235     -26.954 -12.524  -2.481  1.00 67.25           C  
ANISOU  604  C   LYS A 235     9808  10106   5639  -1925   2320   3154       C  
ATOM    605  O   LYS A 235     -26.371 -13.401  -3.129  1.00 65.37           O  
ANISOU  605  O   LYS A 235     9486   9811   5542  -1927   2118   3204       O  
ATOM    606  CB  LYS A 235     -29.447 -12.753  -2.694  1.00 67.65           C  
ANISOU  606  CB  LYS A 235     9626  10134   5943  -1935   2720   3247       C  
ATOM    607  CG  LYS A 235     -30.628 -11.992  -2.088  1.00 87.25           C  
ANISOU  607  CG  LYS A 235    12124  12662   8366  -1927   3032   3233       C  
ATOM    608  CD  LYS A 235     -30.480 -11.746  -0.576  1.00101.07           C  
ANISOU  608  CD  LYS A 235    14140  14476   9787  -1967   3161   3272       C  
ATOM    609  CE  LYS A 235     -31.768 -11.308   0.088  1.00114.43           C  
ANISOU  609  CE  LYS A 235    15841  16199  11438  -1968   3495   3303       C  
ATOM    610  NZ  LYS A 235     -32.165  -9.926  -0.297  1.00122.40           N  
ANISOU  610  NZ  LYS A 235    16799  17232  12477  -1891   3637   3137       N  
ATOM    611  N   ILE A 236     -26.526 -12.083  -1.279  1.00 65.05           N  
ANISOU  611  N   ILE A 236     9763   9887   5065  -1956   2358   3152       N  
ATOM    612  CA  ILE A 236     -25.320 -12.591  -0.608  1.00 80.95           C  
ANISOU  612  CA  ILE A 236    11949  11910   6898  -2000   2152   3217       C  
ATOM    613  C   ILE A 236     -25.594 -13.928   0.089  1.00 94.62           C  
ANISOU  613  C   ILE A 236    13731  13617   8602  -2071   2158   3421       C  
ATOM    614  O   ILE A 236     -26.601 -14.079   0.774  1.00 55.15           O  
ANISOU  614  O   ILE A 236     8776   8637   3541  -2108   2380   3502       O  
ATOM    615  CB  ILE A 236     -24.661 -11.527   0.328  1.00 84.56           C  
ANISOU  615  CB  ILE A 236    12643  12437   7048  -2009   2158   3125       C  
ATOM    616  CG1 ILE A 236     -24.115 -10.326  -0.497  1.00 82.90           C  
ANISOU  616  CG1 ILE A 236    12371  12236   6890  -1940   2083   2929       C  
ATOM    617  CG2 ILE A 236     -23.552 -12.152   1.199  1.00 85.46           C  
ANISOU  617  CG2 ILE A 236    12949  12564   6960  -2070   1957   3225       C  
ATOM    618  CD1 ILE A 236     -23.746  -9.058   0.318  1.00 89.27           C  
ANISOU  618  CD1 ILE A 236    13392  13105   7421  -1944   2142   2809       C  
ATOM    619  N   LYS A 246     -21.675 -17.779   1.196  1.00 70.77           N  
ANISOU  619  N   LYS A 246    10982  10471   5435  -2204   1267   3888       N  
ATOM    620  CA  LYS A 246     -22.600 -18.531   0.341  1.00 70.77           C  
ANISOU  620  CA  LYS A 246    10780  10399   5711  -2191   1350   3934       C  
ATOM    621  C   LYS A 246     -22.692 -18.033  -1.141  1.00 74.43           C  
ANISOU  621  C   LYS A 246    11024  10827   6429  -2111   1326   3778       C  
ATOM    622  O   LYS A 246     -22.243 -16.926  -1.451  1.00 71.72           O  
ANISOU  622  O   LYS A 246    10684  10527   6038  -2063   1306   3621       O  
ATOM    623  CB  LYS A 246     -23.992 -18.680   1.004  1.00 74.59           C  
ANISOU  623  CB  LYS A 246    11293  10905   6145  -2243   1624   4018       C  
ATOM    624  CG  LYS A 246     -24.765 -17.369   1.216  1.00 85.34           C  
ANISOU  624  CG  LYS A 246    12683  12340   7403  -2223   1863   3888       C  
ATOM    625  CD  LYS A 246     -26.264 -17.491   0.882  1.00 90.66           C  
ANISOU  625  CD  LYS A 246    13201  12993   8252  -2225   2107   3915       C  
ATOM    626  CE  LYS A 246     -26.562 -17.234  -0.585  1.00 87.66           C  
ANISOU  626  CE  LYS A 246    12577  12565   8164  -2158   2077   3799       C  
ATOM    627  NZ  LYS A 246     -27.981 -16.854  -0.815  1.00 85.01           N  
ANISOU  627  NZ  LYS A 246    12111  12236   7952  -2151   2333   3782       N  
ATOM    628  N   VAL A 247     -23.280 -18.875  -2.037  1.00 73.05           N  
ANISOU  628  N   VAL A 247    10668  10568   6519  -2101   1324   3828       N  
ATOM    629  CA  VAL A 247     -23.508 -18.669  -3.490  1.00 71.29           C  
ANISOU  629  CA  VAL A 247    10234  10293   6560  -2036   1298   3712       C  
ATOM    630  C   VAL A 247     -24.826 -19.383  -3.939  1.00 78.14           C  
ANISOU  630  C   VAL A 247    10954  11101   7635  -2064   1434   3790       C  
ATOM    631  O   VAL A 247     -25.126 -20.439  -3.372  1.00 79.71           O  
ANISOU  631  O   VAL A 247    11193  11262   7832  -2125   1447   3954       O  
ATOM    632  CB  VAL A 247     -22.305 -19.153  -4.347  1.00 73.31           C  
ANISOU  632  CB  VAL A 247    10428  10482   6945  -1988   1038   3689       C  
ATOM    633  CG1 VAL A 247     -21.192 -18.113  -4.394  1.00 72.40           C  
ANISOU  633  CG1 VAL A 247    10376  10424   6709  -1941    925   3556       C  
ATOM    634  CG2 VAL A 247     -21.778 -20.518  -3.896  1.00 73.99           C  
ANISOU  634  CG2 VAL A 247    10573  10505   7034  -2029    898   3864       C  
ATOM    635  N   SER A 248     -25.613 -18.891  -4.943  1.00 74.83           N  
ANISOU  635  N   SER A 248    10363  10665   7403  -2026   1525   3688       N  
ATOM    636  CA  SER A 248     -25.571 -17.672  -5.767  1.00 73.68           C  
ANISOU  636  CA  SER A 248    10135  10551   7307  -1955   1544   3501       C  
ATOM    637  C   SER A 248     -26.984 -17.498  -6.377  1.00 78.13           C  
ANISOU  637  C   SER A 248    10530  11098   8058  -1955   1723   3483       C  
ATOM    638  O   SER A 248     -27.432 -18.381  -7.111  1.00 77.61           O  
ANISOU  638  O   SER A 248    10333  10950   8208  -1971   1678   3544       O  
ATOM    639  CB  SER A 248     -24.552 -17.819  -6.897  1.00 76.74           C  
ANISOU  639  CB  SER A 248    10443  10881   7833  -1896   1318   3420       C  
ATOM    640  OG  SER A 248     -24.482 -16.658  -7.710  1.00 84.33           O  
ANISOU  640  OG  SER A 248    11326  11871   8844  -1830   1331   3247       O  
ATOM    641  N   GLU A 249     -27.697 -16.397  -6.053  1.00 75.44           N  
ANISOU  641  N   GLU A 249    10196  10829   7639  -1941   1924   3407       N  
ATOM    642  CA  GLU A 249     -29.051 -16.158  -6.579  1.00 75.43           C  
ANISOU  642  CA  GLU A 249    10028  10816   7817  -1938   2100   3396       C  
ATOM    643  C   GLU A 249     -29.304 -14.720  -7.043  1.00 79.21           C  
ANISOU  643  C   GLU A 249    10451  11343   8301  -1870   2197   3227       C  
ATOM    644  O   GLU A 249     -29.204 -13.784  -6.245  1.00 79.27           O  
ANISOU  644  O   GLU A 249    10586  11426   8106  -1857   2313   3168       O  
ATOM    645  CB  GLU A 249     -30.164 -16.700  -5.651  1.00 78.90           C  
ANISOU  645  CB  GLU A 249    10485  11265   8230  -2008   2307   3550       C  
ATOM    646  CG  GLU A 249     -30.205 -16.134  -4.241  1.00 90.96           C  
ANISOU  646  CG  GLU A 249    12208  12880   9474  -2029   2476   3572       C  
ATOM    647  CD  GLU A 249     -31.307 -16.705  -3.367  1.00115.26           C  
ANISOU  647  CD  GLU A 249    15295  15964  12533  -2096   2693   3730       C  
ATOM    648  OE1 GLU A 249     -32.415 -16.121  -3.350  1.00116.10           O  
ANISOU  648  OE1 GLU A 249    15309  16095  12708  -2083   2916   3711       O  
ATOM    649  OE2 GLU A 249     -31.063 -17.733  -2.695  1.00104.26           O  
ANISOU  649  OE2 GLU A 249    14000  14551  11062  -2159   2645   3877       O  
ATOM    650  N   VAL A 250     -29.627 -14.552  -8.345  1.00 74.96           N  
ANISOU  650  N   VAL A 250     9729  10758   7995  -1829   2145   3151       N  
ATOM    651  CA  VAL A 250     -29.847 -13.235  -8.962  1.00 73.70           C  
ANISOU  651  CA  VAL A 250     9497  10633   7875  -1761   2212   2993       C  
ATOM    652  C   VAL A 250     -31.217 -12.581  -8.719  1.00 77.56           C  
ANISOU  652  C   VAL A 250     9903  11154   8413  -1759   2472   2996       C  
ATOM    653  O   VAL A 250     -32.253 -13.241  -8.827  1.00 77.84           O  
ANISOU  653  O   VAL A 250     9818  11153   8605  -1800   2561   3105       O  
ATOM    654  CB  VAL A 250     -29.377 -13.123 -10.444  1.00 75.94           C  
ANISOU  654  CB  VAL A 250     9650  10861   8344  -1708   2028   2887       C  
ATOM    655  CG1 VAL A 250     -27.888 -13.432 -10.580  1.00 74.76           C  
ANISOU  655  CG1 VAL A 250     9600  10695   8112  -1691   1801   2856       C  
ATOM    656  CG2 VAL A 250     -30.204 -14.005 -11.378  1.00 75.71           C  
ANISOU  656  CG2 VAL A 250     9441  10748   8579  -1734   1996   2956       C  
ATOM    657  N   ILE A 251     -31.200 -11.272  -8.393  1.00 73.51           N  
ANISOU  657  N   ILE A 251     9454  10706   7770  -1710   2592   2878       N  
ATOM    658  CA  ILE A 251     -32.377 -10.416  -8.196  1.00 73.80           C  
ANISOU  658  CA  ILE A 251     9420  10776   7845  -1686   2844   2853       C  
ATOM    659  C   ILE A 251     -32.692  -9.782  -9.570  1.00 75.06           C  
ANISOU  659  C   ILE A 251     9388  10903   8228  -1625   2796   2743       C  
ATOM    660  O   ILE A 251     -33.849  -9.785 -10.001  1.00 75.58           O  
ANISOU  660  O   ILE A 251     9282  10945   8489  -1625   2911   2784       O  
ATOM    661  CB  ILE A 251     -32.120  -9.356  -7.081  1.00 77.95           C  
ANISOU  661  CB  ILE A 251    10142  11378   8096  -1665   2994   2780       C  
ATOM    662  CG1 ILE A 251     -31.973 -10.030  -5.694  1.00 80.17           C  
ANISOU  662  CG1 ILE A 251    10614  11690   8156  -1733   3059   2905       C  
ATOM    663  CG2 ILE A 251     -33.217  -8.274  -7.055  1.00 79.66           C  
ANISOU  663  CG2 ILE A 251    10280  11621   8366  -1616   3247   2720       C  
ATOM    664  CD1 ILE A 251     -31.054  -9.305  -4.718  1.00 86.31           C  
ANISOU  664  CD1 ILE A 251    11641  12528   8623  -1728   3054   2829       C  
ATOM    665  N   LYS A 252     -31.649  -9.266 -10.254  1.00 67.85           N  
ANISOU  665  N   LYS A 252     8504   9987   7290  -1577   2618   2614       N  
ATOM    666  CA  LYS A 252     -31.732  -8.674 -11.589  1.00 65.54           C  
ANISOU  666  CA  LYS A 252     8056   9662   7183  -1519   2539   2505       C  
ATOM    667  C   LYS A 252     -30.555  -9.178 -12.416  1.00 67.13           C  
ANISOU  667  C   LYS A 252     8266   9820   7420  -1510   2272   2465       C  
ATOM    668  O   LYS A 252     -29.401  -9.023 -12.010  1.00 66.54           O  
ANISOU  668  O   LYS A 252     8339   9772   7171  -1502   2168   2421       O  
ATOM    669  CB  LYS A 252     -31.743  -7.135 -11.537  1.00 67.49           C  
ANISOU  669  CB  LYS A 252     8334   9958   7349  -1451   2653   2361       C  
ATOM    670  CG  LYS A 252     -32.136  -6.479 -12.863  1.00 79.21           C  
ANISOU  670  CG  LYS A 252     9640  11411   9045  -1393   2620   2269       C  
ATOM    671  CD  LYS A 252     -31.272  -5.268 -13.209  1.00 87.61           C  
ANISOU  671  CD  LYS A 252    10770  12500  10019  -1327   2556   2104       C  
ATOM    672  CE  LYS A 252     -31.958  -3.962 -12.887  1.00 98.05           C  
ANISOU  672  CE  LYS A 252    12088  13858  11306  -1277   2769   2027       C  
ATOM    673  NZ  LYS A 252     -31.130  -2.791 -13.270  1.00102.64           N  
ANISOU  673  NZ  LYS A 252    12732  14456  11811  -1217   2700   1869       N  
ATOM    674  N   GLU A 253     -30.852  -9.790 -13.571  1.00 61.70           N  
ANISOU  674  N   GLU A 253     7422   9063   6958  -1512   2161   2484       N  
ATOM    675  CA  GLU A 253     -29.850 -10.333 -14.483  1.00 59.54           C  
ANISOU  675  CA  GLU A 253     7141   8735   6746  -1499   1923   2448       C  
ATOM    676  C   GLU A 253     -28.912  -9.251 -15.013  1.00 59.78           C  
ANISOU  676  C   GLU A 253     7209   8791   6712  -1428   1839   2291       C  
ATOM    677  O   GLU A 253     -29.315  -8.091 -15.123  1.00 58.39           O  
ANISOU  677  O   GLU A 253     7003   8653   6530  -1386   1951   2201       O  
ATOM    678  CB  GLU A 253     -30.536 -11.065 -15.645  1.00 60.61           C  
ANISOU  678  CB  GLU A 253     7104   8789   7137  -1515   1849   2488       C  
ATOM    679  CG  GLU A 253     -30.667 -12.562 -15.433  1.00 72.91           C  
ANISOU  679  CG  GLU A 253     8662  10285   8757  -1586   1783   2634       C  
ATOM    680  CD  GLU A 253     -29.425 -13.360 -15.785  1.00 94.73           C  
ANISOU  680  CD  GLU A 253    11501  12997  11494  -1582   1568   2632       C  
ATOM    681  OE1 GLU A 253     -29.032 -13.366 -16.976  1.00 86.53           O  
ANISOU  681  OE1 GLU A 253    10400  11906  10571  -1544   1427   2553       O  
ATOM    682  OE2 GLU A 253     -28.857 -13.999 -14.870  1.00 88.60           O  
ANISOU  682  OE2 GLU A 253    10848  12231  10587  -1615   1542   2713       O  
ATOM    683  N   VAL A 254     -27.654  -9.632 -15.314  1.00 54.53           N  
ANISOU  683  N   VAL A 254     6612   8103   6004  -1416   1646   2264       N  
ATOM    684  CA  VAL A 254     -26.639  -8.721 -15.858  1.00 52.21           C  
ANISOU  684  CA  VAL A 254     6349   7827   5660  -1354   1546   2127       C  
ATOM    685  C   VAL A 254     -26.836  -8.592 -17.362  1.00 53.72           C  
ANISOU  685  C   VAL A 254     6395   7963   6054  -1313   1465   2057       C  
ATOM    686  O   VAL A 254     -27.166  -9.578 -18.027  1.00 53.22           O  
ANISOU  686  O   VAL A 254     6249   7829   6143  -1336   1390   2120       O  
ATOM    687  CB  VAL A 254     -25.171  -9.124 -15.557  1.00 55.49           C  
ANISOU  687  CB  VAL A 254     6889   8243   5953  -1353   1378   2130       C  
ATOM    688  CG1 VAL A 254     -24.320  -7.892 -15.289  1.00 54.60           C  
ANISOU  688  CG1 VAL A 254     6867   8190   5687  -1313   1368   2011       C  
ATOM    689  CG2 VAL A 254     -25.064 -10.122 -14.409  1.00 57.00           C  
ANISOU  689  CG2 VAL A 254     7185   8439   6032  -1416   1381   2267       C  
ATOM    690  N   GLU A 255     -26.611  -7.383 -17.896  1.00 48.09           N  
ANISOU  690  N   GLU A 255     5661   7276   5337  -1254   1475   1928       N  
ATOM    691  CA  GLU A 255     -26.715  -7.090 -19.326  1.00 45.85           C  
ANISOU  691  CA  GLU A 255     5255   6945   5220  -1211   1399   1850       C  
ATOM    692  C   GLU A 255     -25.406  -6.465 -19.789  1.00 44.06           C  
ANISOU  692  C   GLU A 255     5086   6728   4926  -1158   1276   1740       C  
ATOM    693  O   GLU A 255     -25.100  -5.333 -19.405  1.00 42.29           O  
ANISOU  693  O   GLU A 255     4920   6559   4588  -1129   1335   1657       O  
ATOM    694  CB  GLU A 255     -27.901  -6.143 -19.620  1.00 47.89           C  
ANISOU  694  CB  GLU A 255     5408   7223   5566  -1189   1550   1807       C  
ATOM    695  CG  GLU A 255     -29.272  -6.705 -19.279  1.00 62.11           C  
ANISOU  695  CG  GLU A 255     7120   9010   7469  -1238   1676   1919       C  
ATOM    696  CD  GLU A 255     -30.422  -5.765 -19.586  1.00 94.76           C  
ANISOU  696  CD  GLU A 255    11136  13160  11711  -1211   1820   1884       C  
ATOM    697  OE1 GLU A 255     -30.884  -5.063 -18.657  1.00 88.70           O  
ANISOU  697  OE1 GLU A 255    10406  12446  10848  -1203   1999   1880       O  
ATOM    698  OE2 GLU A 255     -30.862  -5.730 -20.758  1.00 98.04           O  
ANISOU  698  OE2 GLU A 255    11422  13527  12303  -1197   1755   1863       O  
ATOM    699  N   SER A 256     -24.615  -7.211 -20.580  1.00 39.12           N  
ANISOU  699  N   SER A 256     4450   6045   4369  -1146   1108   1742       N  
ATOM    700  CA  SER A 256     -23.342  -6.722 -21.128  1.00 37.77           C  
ANISOU  700  CA  SER A 256     4317   5874   4160  -1094    987   1649       C  
ATOM    701  C   SER A 256     -23.576  -5.542 -22.072  1.00 39.88           C  
ANISOU  701  C   SER A 256     4510   6147   4494  -1041   1014   1530       C  
ATOM    702  O   SER A 256     -24.633  -5.456 -22.706  1.00 39.42           O  
ANISOU  702  O   SER A 256     4348   6064   4567  -1041   1068   1529       O  
ATOM    703  CB  SER A 256     -22.616  -7.829 -21.889  1.00 40.83           C  
ANISOU  703  CB  SER A 256     4693   6186   4635  -1087    825   1681       C  
ATOM    704  OG  SER A 256     -21.890  -8.690 -21.032  1.00 51.18           O  
ANISOU  704  OG  SER A 256     6095   7496   5855  -1116    762   1767       O  
ATOM    705  N   GLY A 257     -22.595  -4.646 -22.141  1.00 35.50           N  
ANISOU  705  N   GLY A 257     4007   5625   3856  -1000    971   1438       N  
ATOM    706  CA  GLY A 257     -22.628  -3.489 -23.023  1.00 33.91           C  
ANISOU  706  CA  GLY A 257     3751   5429   3706   -948    984   1324       C  
ATOM    707  C   GLY A 257     -22.562  -3.907 -24.478  1.00 37.05           C  
ANISOU  707  C   GLY A 257     4061   5756   4261   -919    880   1302       C  
ATOM    708  O   GLY A 257     -22.052  -4.988 -24.796  1.00 37.02           O  
ANISOU  708  O   GLY A 257     4066   5700   4299   -927    771   1351       O  
ATOM    709  N   GLU A 258     -23.110  -3.071 -25.367  1.00 32.29           N  
ANISOU  709  N   GLU A 258     3379   5144   3744   -885    913   1229       N  
ATOM    710  CA  GLU A 258     -23.166  -3.327 -26.803  1.00 30.37           C  
ANISOU  710  CA  GLU A 258     3062   4837   3642   -859    822   1200       C  
ATOM    711  C   GLU A 258     -21.786  -3.197 -27.445  1.00 33.29           C  
ANISOU  711  C   GLU A 258     3475   5189   3983   -813    705   1135       C  
ATOM    712  O   GLU A 258     -21.096  -2.198 -27.237  1.00 32.47           O  
ANISOU  712  O   GLU A 258     3412   5131   3795   -783    718   1066       O  
ATOM    713  CB  GLU A 258     -24.165  -2.356 -27.463  1.00 31.52           C  
ANISOU  713  CB  GLU A 258     3117   4985   3874   -836    897   1146       C  
ATOM    714  CG  GLU A 258     -24.388  -2.548 -28.956  1.00 38.79           C  
ANISOU  714  CG  GLU A 258     3964   5839   4934   -816    806   1117       C  
ATOM    715  CD  GLU A 258     -24.932  -1.336 -29.684  1.00 54.77           C  
ANISOU  715  CD  GLU A 258     5921   7873   7018   -778    850   1043       C  
ATOM    716  OE1 GLU A 258     -25.675  -0.551 -29.055  1.00 45.41           O  
ANISOU  716  OE1 GLU A 258     4704   6731   5820   -778    976   1042       O  
ATOM    717  OE2 GLU A 258     -24.626  -1.176 -30.888  1.00 51.83           O  
ANISOU  717  OE2 GLU A 258     5529   7459   6705   -746    762    989       O  
ATOM    718  N   ASN A 259     -21.403  -4.202 -28.241  1.00 30.15           N  
ANISOU  718  N   ASN A 259     3070   4722   3663   -808    595   1159       N  
ATOM    719  CA  ASN A 259     -20.161  -4.200 -29.006  1.00 29.97           C  
ANISOU  719  CA  ASN A 259     3076   4671   3640   -759    492   1106       C  
ATOM    720  C   ASN A 259     -20.331  -3.270 -30.227  1.00 35.19           C  
ANISOU  720  C   ASN A 259     3684   5318   4368   -715    489   1013       C  
ATOM    721  O   ASN A 259     -21.342  -3.357 -30.926  1.00 34.15           O  
ANISOU  721  O   ASN A 259     3490   5151   4335   -725    501   1015       O  
ATOM    722  CB  ASN A 259     -19.774  -5.627 -29.418  1.00 28.58           C  
ANISOU  722  CB  ASN A 259     2917   4417   3525   -765    392   1165       C  
ATOM    723  CG  ASN A 259     -19.343  -6.478 -28.248  1.00 43.52           C  
ANISOU  723  CG  ASN A 259     4870   6321   5345   -799    378   1255       C  
ATOM    724  OD1 ASN A 259     -18.751  -5.992 -27.287  1.00 35.00           O  
ANISOU  724  OD1 ASN A 259     3841   5307   4151   -802    399   1257       O  
ATOM    725  ND2 ASN A 259     -19.620  -7.775 -28.297  1.00 38.12           N  
ANISOU  725  ND2 ASN A 259     4188   5571   4724   -830    335   1335       N  
ATOM    726  N   ILE A 260     -19.369  -2.348 -30.440  1.00 32.99           N  
ANISOU  726  N   ILE A 260     3430   5068   4035   -669    473    937       N  
ATOM    727  CA  ILE A 260     -19.411  -1.363 -31.527  1.00 32.46           C  
ANISOU  727  CA  ILE A 260     3323   4993   4016   -626    474    850       C  
ATOM    728  C   ILE A 260     -18.291  -1.527 -32.572  1.00 35.00           C  
ANISOU  728  C   ILE A 260     3663   5270   4364   -577    382    807       C  
ATOM    729  O   ILE A 260     -17.115  -1.526 -32.230  1.00 34.60           O  
ANISOU  729  O   ILE A 260     3656   5237   4255   -558    345    803       O  
ATOM    730  CB  ILE A 260     -19.606   0.082 -30.965  1.00 35.80           C  
ANISOU  730  CB  ILE A 260     3744   5485   4372   -618    568    793       C  
ATOM    731  CG1 ILE A 260     -21.095   0.270 -30.534  1.00 37.13           C  
ANISOU  731  CG1 ILE A 260     3860   5670   4577   -650    672    824       C  
ATOM    732  CG2 ILE A 260     -19.181   1.170 -31.968  1.00 35.38           C  
ANISOU  732  CG2 ILE A 260     3673   5429   4343   -567    552    701       C  
ATOM    733  CD1 ILE A 260     -21.362   1.236 -29.435  1.00 42.87           C  
ANISOU  733  CD1 ILE A 260     4613   6464   5212   -659    786    805       C  
ATOM    734  N   THR A 261     -18.680  -1.707 -33.846  1.00 30.87           N  
ANISOU  734  N   THR A 261     3109   4687   3932   -558    345    780       N  
ATOM    735  CA  THR A 261     -17.748  -1.849 -34.966  1.00 29.33           C  
ANISOU  735  CA  THR A 261     2936   4442   3766   -508    273    736       C  
ATOM    736  C   THR A 261     -17.673  -0.532 -35.729  1.00 31.01           C  
ANISOU  736  C   THR A 261     3125   4674   3981   -470    297    653       C  
ATOM    737  O   THR A 261     -18.682  -0.044 -36.233  1.00 30.53           O  
ANISOU  737  O   THR A 261     3022   4609   3969   -478    324    633       O  
ATOM    738  CB  THR A 261     -17.971  -3.145 -35.810  1.00 36.55           C  
ANISOU  738  CB  THR A 261     3864   5264   4759   -514    203    769       C  
ATOM    739  OG1 THR A 261     -17.653  -2.919 -37.191  1.00 30.96           O  
ANISOU  739  OG1 THR A 261     3167   4505   4090   -468    162    706       O  
ATOM    740  CG2 THR A 261     -19.363  -3.734 -35.678  1.00 39.76           C  
ANISOU  740  CG2 THR A 261     4234   5647   5227   -572    214    821       C  
ATOM    741  N   LEU A 262     -16.485   0.068 -35.755  1.00 26.08           N  
ANISOU  741  N   LEU A 262     2524   4073   3310   -431    287    611       N  
ATOM    742  CA  LEU A 262     -16.257   1.343 -36.439  1.00 23.85           C  
ANISOU  742  CA  LEU A 262     2226   3809   3027   -394    310    534       C  
ATOM    743  C   LEU A 262     -15.922   1.161 -37.919  1.00 22.97           C  
ANISOU  743  C   LEU A 262     2124   3632   2971   -351    260    499       C  
ATOM    744  O   LEU A 262     -15.552   0.070 -38.343  1.00 20.80           O  
ANISOU  744  O   LEU A 262     1879   3300   2724   -341    208    525       O  
ATOM    745  CB  LEU A 262     -15.167   2.169 -35.728  1.00 23.55           C  
ANISOU  745  CB  LEU A 262     2207   3827   2913   -381    324    508       C  
ATOM    746  CG  LEU A 262     -15.360   2.491 -34.229  1.00 27.94           C  
ANISOU  746  CG  LEU A 262     2778   4450   3388   -423    373    532       C  
ATOM    747  CD1 LEU A 262     -14.190   3.334 -33.723  1.00 27.47           C  
ANISOU  747  CD1 LEU A 262     2744   4434   3258   -413    365    498       C  
ATOM    748  CD2 LEU A 262     -16.665   3.235 -33.974  1.00 27.96           C  
ANISOU  748  CD2 LEU A 262     2751   4478   3395   -444    457    514       C  
ATOM    749  N   SER A 263     -16.054   2.245 -38.696  1.00 18.22           N  
ANISOU  749  N   SER A 263     1505   3037   2383   -326    281    439       N  
ATOM    750  CA  SER A 263     -15.753   2.296 -40.127  1.00 17.92           C  
ANISOU  750  CA  SER A 263     1484   2942   2381   -285    245    398       C  
ATOM    751  C   SER A 263     -14.244   2.278 -40.354  1.00 23.88           C  
ANISOU  751  C   SER A 263     2270   3691   3111   -238    229    381       C  
ATOM    752  O   SER A 263     -13.803   1.981 -41.459  1.00 23.44           O  
ANISOU  752  O   SER A 263     2245   3580   3080   -201    202    359       O  
ATOM    753  CB  SER A 263     -16.321   3.580 -40.725  1.00 19.59           C  
ANISOU  753  CB  SER A 263     1666   3171   2606   -273    276    347       C  
ATOM    754  OG  SER A 263     -15.743   4.691 -40.058  1.00 20.90           O  
ANISOU  754  OG  SER A 263     1820   3398   2725   -263    325    317       O  
ATOM    755  N   ILE A 264     -13.479   2.695 -39.325  1.00 20.67           N  
ANISOU  755  N   ILE A 264     1855   3343   2656   -242    248    388       N  
ATOM    756  CA  ILE A 264     -12.025   2.800 -39.253  1.00 20.69           C  
ANISOU  756  CA  ILE A 264     1866   3353   2641   -208    233    385       C  
ATOM    757  C   ILE A 264     -11.352   1.461 -39.534  1.00 23.83           C  
ANISOU  757  C   ILE A 264     2290   3693   3070   -183    188    426       C  
ATOM    758  O   ILE A 264     -11.791   0.436 -39.005  1.00 23.31           O  
ANISOU  758  O   ILE A 264     2238   3609   3010   -211    166    478       O  
ATOM    759  CB  ILE A 264     -11.605   3.363 -37.837  1.00 24.29           C  
ANISOU  759  CB  ILE A 264     2312   3884   3034   -240    247    399       C  
ATOM    760  CG1 ILE A 264     -12.006   4.854 -37.636  1.00 24.25           C  
ANISOU  760  CG1 ILE A 264     2290   3927   2996   -253    298    344       C  
ATOM    761  CG2 ILE A 264     -10.122   3.103 -37.483  1.00 24.54           C  
ANISOU  761  CG2 ILE A 264     2346   3923   3057   -220    207    427       C  
ATOM    762  CD1 ILE A 264     -11.078   5.940 -38.278  1.00 24.77           C  
ANISOU  762  CD1 ILE A 264     2345   3998   3068   -218    304    292       C  
ATOM    763  N   ASP A 265     -10.252   1.497 -40.331  1.00 18.27           N  
ANISOU  763  N   ASP A 265     1593   2958   2390   -128    182    407       N  
ATOM    764  CA  ASP A 265      -9.390   0.348 -40.625  1.00 17.61           C  
ANISOU  764  CA  ASP A 265     1533   2816   2343    -88    153    443       C  
ATOM    765  C   ASP A 265      -8.128   0.620 -39.815  1.00 22.69           C  
ANISOU  765  C   ASP A 265     2142   3505   2975    -77    143    473       C  
ATOM    766  O   ASP A 265      -7.395   1.551 -40.146  1.00 22.25           O  
ANISOU  766  O   ASP A 265     2060   3473   2921    -52    164    440       O  
ATOM    767  CB  ASP A 265      -9.070   0.275 -42.136  1.00 18.05           C  
ANISOU  767  CB  ASP A 265     1622   2803   2434    -30    167    401       C  
ATOM    768  CG  ASP A 265      -8.475  -1.032 -42.616  1.00 28.10           C  
ANISOU  768  CG  ASP A 265     2935   3994   3748     15    150    429       C  
ATOM    769  OD1 ASP A 265      -7.591  -1.584 -41.912  1.00 30.35           O  
ANISOU  769  OD1 ASP A 265     3199   4283   4051     29    134    481       O  
ATOM    770  OD2 ASP A 265      -8.814  -1.459 -43.748  1.00 34.15           O  
ANISOU  770  OD2 ASP A 265     3758   4687   4530     39    153    398       O  
ATOM    771  N   SER A 266      -7.910  -0.125 -38.708  1.00 20.67           N  
ANISOU  771  N   SER A 266     1883   3264   2707   -103    107    539       N  
ATOM    772  CA  SER A 266      -6.732   0.075 -37.843  1.00 21.00           C  
ANISOU  772  CA  SER A 266     1892   3350   2738   -102     78    578       C  
ATOM    773  C   SER A 266      -5.358   0.087 -38.587  1.00 24.16           C  
ANISOU  773  C   SER A 266     2262   3717   3201    -34     78    580       C  
ATOM    774  O   SER A 266      -4.449   0.784 -38.152  1.00 23.10           O  
ANISOU  774  O   SER A 266     2086   3628   3064    -35     64    589       O  
ATOM    775  CB  SER A 266      -6.736  -0.901 -36.667  1.00 24.50           C  
ANISOU  775  CB  SER A 266     2347   3802   3161   -137     31    658       C  
ATOM    776  OG  SER A 266      -6.674  -2.253 -37.086  1.00 29.89           O  
ANISOU  776  OG  SER A 266     3052   4405   3901   -105     12    699       O  
ATOM    777  N   ARG A 267      -5.231  -0.640 -39.720  1.00 22.05           N  
ANISOU  777  N   ARG A 267     2019   3370   2991     25     99    569       N  
ATOM    778  CA  ARG A 267      -3.998  -0.663 -40.528  1.00 21.97           C  
ANISOU  778  CA  ARG A 267     1984   3321   3045     98    121    570       C  
ATOM    779  C   ARG A 267      -3.782   0.693 -41.190  1.00 24.99           C  
ANISOU  779  C   ARG A 267     2343   3735   3417    109    166    508       C  
ATOM    780  O   ARG A 267      -2.659   1.189 -41.182  1.00 23.87           O  
ANISOU  780  O   ARG A 267     2147   3612   3310    135    171    522       O  
ATOM    781  CB  ARG A 267      -4.038  -1.747 -41.605  1.00 20.07           C  
ANISOU  781  CB  ARG A 267     1795   2978   2852    157    144    564       C  
ATOM    782  CG  ARG A 267      -4.169  -3.168 -41.094  1.00 25.93           C  
ANISOU  782  CG  ARG A 267     2565   3670   3619    155    103    626       C  
ATOM    783  CD  ARG A 267      -4.612  -4.103 -42.209  1.00 30.17           C  
ANISOU  783  CD  ARG A 267     3180   4103   4181    193    125    598       C  
ATOM    784  NE  ARG A 267      -5.759  -3.571 -42.956  1.00 33.90           N  
ANISOU  784  NE  ARG A 267     3698   4573   4608    162    143    527       N  
ATOM    785  CZ  ARG A 267      -5.993  -3.804 -44.244  1.00 48.29           C  
ANISOU  785  CZ  ARG A 267     5590   6322   6438    199    172    476       C  
ATOM    786  NH1 ARG A 267      -5.173  -4.576 -44.947  1.00 48.62           N  
ANISOU  786  NH1 ARG A 267     5669   6279   6525    272    201    480       N  
ATOM    787  NH2 ARG A 267      -7.037  -3.252 -44.844  1.00 21.52           N  
ANISOU  787  NH2 ARG A 267     2233   2936   3006    164    173    421       N  
ATOM    788  N   LEU A 268      -4.856   1.282 -41.773  1.00 21.96           N  
ANISOU  788  N   LEU A 268     1996   3354   2994     87    194    445       N  
ATOM    789  CA  LEU A 268      -4.834   2.606 -42.414  1.00 20.98           C  
ANISOU  789  CA  LEU A 268     1859   3257   2857     92    235    386       C  
ATOM    790  C   LEU A 268      -4.565   3.676 -41.346  1.00 23.51           C  
ANISOU  790  C   LEU A 268     2130   3660   3143     44    217    389       C  
ATOM    791  O   LEU A 268      -3.823   4.648 -41.594  1.00 22.77           O  
ANISOU  791  O   LEU A 268     2000   3589   3064     56    237    370       O  
ATOM    792  CB  LEU A 268      -6.174   2.891 -43.107  1.00 20.99           C  
ANISOU  792  CB  LEU A 268     1907   3241   2825     73    253    333       C  
ATOM    793  CG  LEU A 268      -6.225   2.671 -44.627  1.00 26.37           C  
ANISOU  793  CG  LEU A 268     2643   3851   3527    125    285    296       C  
ATOM    794  CD1 LEU A 268      -6.625   1.242 -44.971  1.00 27.04           C  
ANISOU  794  CD1 LEU A 268     2787   3860   3626    138    263    314       C  
ATOM    795  CD2 LEU A 268      -7.207   3.638 -45.283  1.00 25.61           C  
ANISOU  795  CD2 LEU A 268     2566   3765   3399    105    302    240       C  
ATOM    796  N   GLN A 269      -5.188   3.492 -40.160  1.00 17.93           N  
ANISOU  796  N   GLN A 269     1429   2994   2389    -15    182    413       N  
ATOM    797  CA  GLN A 269      -4.998   4.341 -38.986  1.00 17.61           C  
ANISOU  797  CA  GLN A 269     1365   3026   2299    -68    160    417       C  
ATOM    798  C   GLN A 269      -3.520   4.356 -38.537  1.00 21.52           C  
ANISOU  798  C   GLN A 269     1811   3538   2828    -57    119    465       C  
ATOM    799  O   GLN A 269      -2.959   5.436 -38.357  1.00 21.69           O  
ANISOU  799  O   GLN A 269     1803   3597   2842    -74    116    444       O  
ATOM    800  CB  GLN A 269      -5.936   3.921 -37.833  1.00 18.69           C  
ANISOU  800  CB  GLN A 269     1533   3195   2376   -127    139    443       C  
ATOM    801  CG  GLN A 269      -6.128   5.014 -36.801  1.00 25.21           C  
ANISOU  801  CG  GLN A 269     2361   4089   3129   -184    139    420       C  
ATOM    802  CD  GLN A 269      -7.150   6.051 -37.179  1.00 26.52           C  
ANISOU  802  CD  GLN A 269     2539   4267   3271   -196    198    351       C  
ATOM    803  OE1 GLN A 269      -7.105   6.642 -38.251  1.00 19.41           O  
ANISOU  803  OE1 GLN A 269     1625   3343   2408   -161    228    307       O  
ATOM    804  NE2 GLN A 269      -8.034   6.380 -36.255  1.00 20.37           N  
ANISOU  804  NE2 GLN A 269     1785   3526   2428   -245    217    343       N  
ATOM    805  N   TYR A 270      -2.890   3.168 -38.401  1.00 18.20           N  
ANISOU  805  N   TYR A 270     1379   3083   2454    -27     85    531       N  
ATOM    806  CA  TYR A 270      -1.483   3.010 -38.034  1.00 18.22           C  
ANISOU  806  CA  TYR A 270     1322   3092   2509     -9     40    592       C  
ATOM    807  C   TYR A 270      -0.561   3.736 -39.028  1.00 24.52           C  
ANISOU  807  C   TYR A 270     2069   3874   3374     40     82    567       C  
ATOM    808  O   TYR A 270       0.333   4.458 -38.604  1.00 27.38           O  
ANISOU  808  O   TYR A 270     2376   4274   3754     21     51    586       O  
ATOM    809  CB  TYR A 270      -1.125   1.510 -37.939  1.00 20.31           C  
ANISOU  809  CB  TYR A 270     1587   3305   2827     29     10    665       C  
ATOM    810  CG  TYR A 270       0.345   1.238 -37.689  1.00 23.28           C  
ANISOU  810  CG  TYR A 270     1888   3676   3282     61    -33    738       C  
ATOM    811  CD1 TYR A 270       0.849   1.150 -36.394  1.00 26.52           C  
ANISOU  811  CD1 TYR A 270     2273   4133   3671     11   -121    806       C  
ATOM    812  CD2 TYR A 270       1.243   1.117 -38.748  1.00 23.61           C  
ANISOU  812  CD2 TYR A 270     1883   3666   3420    140     15    742       C  
ATOM    813  CE1 TYR A 270       2.215   0.968 -36.160  1.00 28.16           C  
ANISOU  813  CE1 TYR A 270     2400   4338   3963     37   -172    881       C  
ATOM    814  CE2 TYR A 270       2.607   0.939 -38.525  1.00 24.91           C  
ANISOU  814  CE2 TYR A 270     1962   3827   3674    171    -19    816       C  
ATOM    815  CZ  TYR A 270       3.086   0.839 -37.232  1.00 34.20           C  
ANISOU  815  CZ  TYR A 270     3104   5051   4840    119   -119    888       C  
ATOM    816  OH  TYR A 270       4.427   0.599 -37.030  1.00 40.09           O  
ANISOU  816  OH  TYR A 270     3754   5788   5688    151   -163    972       O  
ATOM    817  N   ILE A 271      -0.782   3.542 -40.333  1.00 20.75           N  
ANISOU  817  N   ILE A 271     1615   3339   2930     99    150    529       N  
ATOM    818  CA  ILE A 271      -0.032   4.144 -41.440  1.00 21.07           C  
ANISOU  818  CA  ILE A 271     1622   3355   3027    153    209    505       C  
ATOM    819  C   ILE A 271      -0.145   5.676 -41.431  1.00 21.49           C  
ANISOU  819  C   ILE A 271     1661   3460   3045    111    222    453       C  
ATOM    820  O   ILE A 271       0.878   6.353 -41.568  1.00 20.15           O  
ANISOU  820  O   ILE A 271     1429   3303   2924    120    228    467       O  
ATOM    821  CB  ILE A 271      -0.450   3.502 -42.800  1.00 24.88           C  
ANISOU  821  CB  ILE A 271     2164   3761   3527    218    276    472       C  
ATOM    822  CG1 ILE A 271       0.176   2.098 -42.914  1.00 27.09           C  
ANISOU  822  CG1 ILE A 271     2442   3978   3873    277    274    530       C  
ATOM    823  CG2 ILE A 271      -0.042   4.386 -43.998  1.00 27.42           C  
ANISOU  823  CG2 ILE A 271     2479   4067   3872    259    350    428       C  
ATOM    824  CD1 ILE A 271      -0.009   1.383 -44.279  1.00 41.90           C  
ANISOU  824  CD1 ILE A 271     4387   5765   5769    348    343    498       C  
ATOM    825  N   MET A 272      -1.388   6.204 -41.263  1.00 15.55           N  
ANISOU  825  N   MET A 272      962   2732   2216     65    228    398       N  
ATOM    826  CA  MET A 272      -1.664   7.636 -41.194  1.00 14.53           C  
ANISOU  826  CA  MET A 272      829   2643   2049     25    243    345       C  
ATOM    827  C   MET A 272      -0.930   8.265 -40.014  1.00 19.28           C  
ANISOU  827  C   MET A 272     1388   3300   2638    -29    185    371       C  
ATOM    828  O   MET A 272      -0.231   9.257 -40.219  1.00 18.50           O  
ANISOU  828  O   MET A 272     1250   3213   2567    -35    192    358       O  
ATOM    829  CB  MET A 272      -3.178   7.934 -41.144  1.00 15.70           C  
ANISOU  829  CB  MET A 272     1036   2801   2129     -8    261    292       C  
ATOM    830  CG  MET A 272      -3.514   9.424 -41.184  1.00 18.17           C  
ANISOU  830  CG  MET A 272     1349   3143   2412    -37    288    235       C  
ATOM    831  SD  MET A 272      -5.297   9.761 -41.302  1.00 20.90           S  
ANISOU  831  SD  MET A 272     1748   3490   2705    -61    320    181       S  
ATOM    832  CE  MET A 272      -5.532   9.616 -43.103  1.00 16.42           C  
ANISOU  832  CE  MET A 272     1203   2858   2179      3    365    156       C  
ATOM    833  N   TYR A 273      -1.050   7.673 -38.794  1.00 17.58           N  
ANISOU  833  N   TYR A 273     1186   3114   2381    -72    122    411       N  
ATOM    834  CA  TYR A 273      -0.386   8.217 -37.610  1.00 17.54           C  
ANISOU  834  CA  TYR A 273     1158   3159   2349   -133     53    436       C  
ATOM    835  C   TYR A 273       1.132   8.224 -37.714  1.00 24.60           C  
ANISOU  835  C   TYR A 273     1968   4047   3331   -112     14    493       C  
ATOM    836  O   TYR A 273       1.752   9.205 -37.283  1.00 26.60           O  
ANISOU  836  O   TYR A 273     2192   4332   3585   -156    -22    489       O  
ATOM    837  CB  TYR A 273      -0.868   7.579 -36.289  1.00 18.06           C  
ANISOU  837  CB  TYR A 273     1268   3257   2338   -186     -5    470       C  
ATOM    838  CG  TYR A 273      -0.318   8.301 -35.064  1.00 20.54           C  
ANISOU  838  CG  TYR A 273     1584   3624   2598   -259    -79    483       C  
ATOM    839  CD1 TYR A 273      -0.861   9.515 -34.642  1.00 22.67           C  
ANISOU  839  CD1 TYR A 273     1899   3925   2791   -311    -60    414       C  
ATOM    840  CD2 TYR A 273       0.812   7.827 -34.397  1.00 21.86           C  
ANISOU  840  CD2 TYR A 273     1706   3802   2797   -274   -169    562       C  
ATOM    841  CE1 TYR A 273      -0.302  10.232 -33.579  1.00 24.83           C  
ANISOU  841  CE1 TYR A 273     2187   4237   3010   -381   -131    418       C  
ATOM    842  CE2 TYR A 273       1.374   8.532 -33.327  1.00 23.72           C  
ANISOU  842  CE2 TYR A 273     1950   4082   2982   -348   -251    574       C  
ATOM    843  CZ  TYR A 273       0.799   9.723 -32.906  1.00 34.37           C  
ANISOU  843  CZ  TYR A 273     3359   5460   4242   -404   -233    498       C  
ATOM    844  OH  TYR A 273       1.324  10.408 -31.831  1.00 38.05           O  
ANISOU  844  OH  TYR A 273     3851   5962   4645   -483   -318    503       O  
ATOM    845  N   ARG A 274       1.725   7.134 -38.269  1.00 21.05           N  
ANISOU  845  N   ARG A 274     1481   3554   2964    -46     23    549       N  
ATOM    846  CA  ARG A 274       3.162   6.968 -38.435  1.00 21.44           C  
ANISOU  846  CA  ARG A 274     1437   3590   3119    -13     -1    617       C  
ATOM    847  C   ARG A 274       3.750   8.071 -39.319  1.00 27.79           C  
ANISOU  847  C   ARG A 274     2192   4388   3978      5     53    585       C  
ATOM    848  O   ARG A 274       4.777   8.648 -38.954  1.00 28.94           O  
ANISOU  848  O   ARG A 274     2264   4556   4177    -22      5    623       O  
ATOM    849  CB  ARG A 274       3.503   5.561 -38.967  1.00 20.44           C  
ANISOU  849  CB  ARG A 274     1292   3405   3069     66     22    673       C  
ATOM    850  CG  ARG A 274       5.013   5.266 -39.050  1.00 25.70           C  
ANISOU  850  CG  ARG A 274     1849   4054   3861    109     -1    757       C  
ATOM    851  CD  ARG A 274       5.344   4.094 -39.960  1.00 27.38           C  
ANISOU  851  CD  ARG A 274     2050   4193   4161    208     65    790       C  
ATOM    852  NE  ARG A 274       4.999   4.384 -41.355  1.00 33.54           N  
ANISOU  852  NE  ARG A 274     2868   4930   4944    264    180    721       N  
ATOM    853  CZ  ARG A 274       4.651   3.472 -42.259  1.00 43.38           C  
ANISOU  853  CZ  ARG A 274     4172   6109   6203    335    251    704       C  
ATOM    854  NH1 ARG A 274       4.584   2.189 -41.929  1.00 29.70           N  
ANISOU  854  NH1 ARG A 274     2459   4338   4489    361    223    749       N  
ATOM    855  NH2 ARG A 274       4.349   3.838 -43.492  1.00 30.40           N  
ANISOU  855  NH2 ARG A 274     2573   4431   4548    376    346    641       N  
ATOM    856  N   GLU A 275       3.079   8.382 -40.451  1.00 22.66           N  
ANISOU  856  N   GLU A 275     1586   3708   3315     44    145    519       N  
ATOM    857  CA  GLU A 275       3.500   9.407 -41.413  1.00 21.00           C  
ANISOU  857  CA  GLU A 275     1344   3486   3147     64    210    487       C  
ATOM    858  C   GLU A 275       3.249  10.828 -40.907  1.00 22.51           C  
ANISOU  858  C   GLU A 275     1546   3721   3285    -11    183    438       C  
ATOM    859  O   GLU A 275       4.007  11.736 -41.245  1.00 21.63           O  
ANISOU  859  O   GLU A 275     1380   3612   3227    -18    196    441       O  
ATOM    860  CB  GLU A 275       2.782   9.229 -42.765  1.00 21.53           C  
ANISOU  860  CB  GLU A 275     1472   3505   3203    126    307    435       C  
ATOM    861  CG  GLU A 275       3.009   7.906 -43.467  1.00 30.92           C  
ANISOU  861  CG  GLU A 275     2671   4636   4441    206    350    468       C  
ATOM    862  CD  GLU A 275       4.439   7.488 -43.739  1.00 54.22           C  
ANISOU  862  CD  GLU A 275     5532   7561   7507    263    371    540       C  
ATOM    863  OE1 GLU A 275       5.343   8.354 -43.764  1.00 44.81           O  
ANISOU  863  OE1 GLU A 275     4261   6390   6374    249    373    563       O  
ATOM    864  OE2 GLU A 275       4.646   6.275 -43.958  1.00 56.70           O  
ANISOU  864  OE2 GLU A 275     5854   7828   7862    322    390    576       O  
ATOM    865  N   LEU A 276       2.159  11.028 -40.139  1.00 16.53           N  
ANISOU  865  N   LEU A 276      861   2993   2427    -64    155    393       N  
ATOM    866  CA  LEU A 276       1.801  12.308 -39.535  1.00 14.70           C  
ANISOU  866  CA  LEU A 276      657   2796   2133   -135    134    341       C  
ATOM    867  C   LEU A 276       2.883  12.705 -38.511  1.00 20.74           C  
ANISOU  867  C   LEU A 276     1370   3594   2917   -196     41    386       C  
ATOM    868  O   LEU A 276       3.262  13.865 -38.446  1.00 20.48           O  
ANISOU  868  O   LEU A 276     1321   3570   2891   -237     31    360       O  
ATOM    869  CB  LEU A 276       0.409  12.169 -38.896  1.00 13.48           C  
ANISOU  869  CB  LEU A 276      588   2660   1873   -167    135    296       C  
ATOM    870  CG  LEU A 276      -0.814  12.911 -39.487  1.00 15.38           C  
ANISOU  870  CG  LEU A 276      884   2889   2070   -161    207    218       C  
ATOM    871  CD1 LEU A 276      -0.719  13.223 -40.973  1.00 14.20           C  
ANISOU  871  CD1 LEU A 276      717   2698   1980   -101    277    199       C  
ATOM    872  CD2 LEU A 276      -2.089  12.228 -39.124  1.00 13.97           C  
ANISOU  872  CD2 LEU A 276      765   2715   1828   -166    218    204       C  
ATOM    873  N   THR A 277       3.451  11.720 -37.788  1.00 20.15           N  
ANISOU  873  N   THR A 277     1265   3530   2860   -200    -31    459       N  
ATOM    874  CA  THR A 277       4.566  11.919 -36.846  1.00 21.01           C  
ANISOU  874  CA  THR A 277     1317   3667   2998   -257   -137    519       C  
ATOM    875  C   THR A 277       5.841  12.277 -37.631  1.00 27.12           C  
ANISOU  875  C   THR A 277     1979   4419   3907   -225   -123    563       C  
ATOM    876  O   THR A 277       6.540  13.230 -37.266  1.00 27.75           O  
ANISOU  876  O   THR A 277     2019   4515   4010   -283   -178    569       O  
ATOM    877  CB  THR A 277       4.793  10.658 -36.004  1.00 22.93           C  
ANISOU  877  CB  THR A 277     1556   3922   3237   -259   -214    597       C  
ATOM    878  OG1 THR A 277       3.558  10.249 -35.414  1.00 24.27           O  
ANISOU  878  OG1 THR A 277     1826   4106   3288   -281   -207    560       O  
ATOM    879  CG2 THR A 277       5.837  10.858 -34.931  1.00 20.25           C  
ANISOU  879  CG2 THR A 277     1167   3613   2914   -326   -343    663       C  
ATOM    880  N   ALA A 278       6.145  11.507 -38.704  1.00 23.07           N  
ANISOU  880  N   ALA A 278     1419   3864   3481   -133    -46    595       N  
ATOM    881  CA  ALA A 278       7.311  11.745 -39.554  1.00 22.71           C  
ANISOU  881  CA  ALA A 278     1267   3793   3568    -88     -5    641       C  
ATOM    882  C   ALA A 278       7.251  13.187 -40.124  1.00 26.47           C  
ANISOU  882  C   ALA A 278     1748   4268   4040   -116     43    580       C  
ATOM    883  O   ALA A 278       8.228  13.927 -39.985  1.00 28.51           O  
ANISOU  883  O   ALA A 278     1926   4535   4372   -154      4    615       O  
ATOM    884  CB  ALA A 278       7.355  10.719 -40.672  1.00 22.93           C  
ANISOU  884  CB  ALA A 278     1285   3770   3658     19     95    661       C  
ATOM    885  N   ALA A 279       6.088  13.605 -40.667  1.00 20.41           N  
ANISOU  885  N   ALA A 279     1074   3491   3189   -106    115    493       N  
ATOM    886  CA  ALA A 279       5.880  14.959 -41.199  1.00 21.01           C  
ANISOU  886  CA  ALA A 279     1168   3562   3253   -130    162    433       C  
ATOM    887  C   ALA A 279       5.979  16.039 -40.124  1.00 25.67           C  
ANISOU  887  C   ALA A 279     1770   4185   3800   -230     74    409       C  
ATOM    888  O   ALA A 279       6.522  17.097 -40.400  1.00 25.74           O  
ANISOU  888  O   ALA A 279     1739   4185   3855   -259     80    402       O  
ATOM    889  CB  ALA A 279       4.536  15.061 -41.890  1.00 20.92           C  
ANISOU  889  CB  ALA A 279     1254   3533   3162    -99    241    355       C  
ATOM    890  N   GLY A 280       5.412  15.787 -38.945  1.00 22.23           N  
ANISOU  890  N   GLY A 280     1397   3781   3270   -283      0    394       N  
ATOM    891  CA  GLY A 280       5.456  16.715 -37.827  1.00 22.81           C  
ANISOU  891  CA  GLY A 280     1504   3881   3281   -381    -86    366       C  
ATOM    892  C   GLY A 280       6.857  16.905 -37.270  1.00 29.27           C  
ANISOU  892  C   GLY A 280     2232   4711   4180   -433   -190    440       C  
ATOM    893  O   GLY A 280       7.228  18.029 -36.922  1.00 30.65           O  
ANISOU  893  O   GLY A 280     2406   4887   4352   -504   -237    417       O  
ATOM    894  N   VAL A 281       7.650  15.808 -37.186  1.00 25.52           N  
ANISOU  894  N   VAL A 281     1676   4240   3782   -398   -230    532       N  
ATOM    895  CA  VAL A 281       9.034  15.850 -36.705  1.00 26.95           C  
ANISOU  895  CA  VAL A 281     1747   4429   4063   -440   -335    621       C  
ATOM    896  C   VAL A 281       9.937  16.575 -37.740  1.00 32.25           C  
ANISOU  896  C   VAL A 281     2311   5071   4870   -417   -277    646       C  
ATOM    897  O   VAL A 281      10.703  17.463 -37.352  1.00 32.75           O  
ANISOU  897  O   VAL A 281     2325   5140   4979   -492   -354    666       O  
ATOM    898  CB  VAL A 281       9.582  14.448 -36.295  1.00 31.09           C  
ANISOU  898  CB  VAL A 281     2213   4962   4639   -406   -395    720       C  
ATOM    899  CG1 VAL A 281      11.085  14.489 -36.002  1.00 31.67           C  
ANISOU  899  CG1 VAL A 281     2146   5038   4849   -436   -494    826       C  
ATOM    900  CG2 VAL A 281       8.824  13.896 -35.092  1.00 31.05           C  
ANISOU  900  CG2 VAL A 281     2313   4990   4496   -453   -473    706       C  
ATOM    901  N   ALA A 282       9.819  16.210 -39.046  1.00 28.21           N  
ANISOU  901  N   ALA A 282     1774   4527   4417   -317   -142    644       N  
ATOM    902  CA  ALA A 282      10.601  16.797 -40.161  1.00 28.17           C  
ANISOU  902  CA  ALA A 282     1677   4492   4535   -281    -59    670       C  
ATOM    903  C   ALA A 282      10.333  18.275 -40.356  1.00 30.85           C  
ANISOU  903  C   ALA A 282     2056   4824   4840   -339    -42    601       C  
ATOM    904  O   ALA A 282      11.227  19.024 -40.740  1.00 29.66           O  
ANISOU  904  O   ALA A 282     1818   4658   4792   -361    -36    637       O  
ATOM    905  CB  ALA A 282      10.308  16.064 -41.464  1.00 28.24           C  
ANISOU  905  CB  ALA A 282     1692   4466   4572   -164     86    667       C  
ATOM    906  N   ASN A 283       9.096  18.693 -40.121  1.00 27.43           N  
ANISOU  906  N   ASN A 283     1753   4397   4273   -362    -27    505       N  
ATOM    907  CA  ASN A 283       8.700  20.079 -40.321  1.00 26.88           C  
ANISOU  907  CA  ASN A 283     1734   4312   4167   -409     -2    433       C  
ATOM    908  C   ASN A 283       8.740  20.932 -39.066  1.00 30.12           C  
ANISOU  908  C   ASN A 283     2188   4741   4517   -522   -122    401       C  
ATOM    909  O   ASN A 283       8.350  22.101 -39.134  1.00 29.23           O  
ANISOU  909  O   ASN A 283     2130   4609   4368   -563   -103    334       O  
ATOM    910  CB  ASN A 283       7.309  20.116 -40.965  1.00 24.56           C  
ANISOU  910  CB  ASN A 283     1549   4005   3780   -357     99    348       C  
ATOM    911  CG  ASN A 283       7.369  19.804 -42.426  1.00 36.23           C  
ANISOU  911  CG  ASN A 283     2996   5451   5319   -263    221    366       C  
ATOM    912  OD1 ASN A 283       7.879  20.587 -43.213  1.00 38.25           O  
ANISOU  912  OD1 ASN A 283     3208   5681   5643   -257    275    376       O  
ATOM    913  ND2 ASN A 283       6.914  18.637 -42.815  1.00 25.41           N  
ANISOU  913  ND2 ASN A 283     1651   4078   3927   -191    266    374       N  
ATOM    914  N   ASN A 284       9.190  20.356 -37.913  1.00 27.54           N  
ANISOU  914  N   ASN A 284     1848   4445   4172   -574   -245    447       N  
ATOM    915  CA  ASN A 284       9.170  21.002 -36.589  1.00 27.24           C  
ANISOU  915  CA  ASN A 284     1878   4425   4048   -686   -370    416       C  
ATOM    916  C   ASN A 284       7.816  21.752 -36.439  1.00 27.78           C  
ANISOU  916  C   ASN A 284     2092   4484   3980   -700   -311    296       C  
ATOM    917  O   ASN A 284       7.774  22.948 -36.142  1.00 26.88           O  
ANISOU  917  O   ASN A 284     2027   4351   3835   -769   -337    241       O  
ATOM    918  CB  ASN A 284      10.385  21.926 -36.393  1.00 29.09           C  
ANISOU  918  CB  ASN A 284     2028   4646   4380   -767   -460    459       C  
ATOM    919  CG  ASN A 284      10.577  22.384 -34.965  1.00 55.90           C  
ANISOU  919  CG  ASN A 284     5490   8058   7693   -887   -615    444       C  
ATOM    920  OD1 ASN A 284      10.370  21.636 -34.000  1.00 51.04           O  
ANISOU  920  OD1 ASN A 284     4926   7475   6990   -910   -693    458       O  
ATOM    921  ND2 ASN A 284      10.959  23.637 -34.796  1.00 51.44           N  
ANISOU  921  ND2 ASN A 284     4935   7467   7145   -971   -663    413       N  
ATOM    922  N   ALA A 285       6.721  21.039 -36.778  1.00 21.69           N  
ANISOU  922  N   ALA A 285     1379   3718   3143   -627   -223    262       N  
ATOM    923  CA  ALA A 285       5.364  21.571 -36.807  1.00 20.57           C  
ANISOU  923  CA  ALA A 285     1353   3566   2895   -619   -148    163       C  
ATOM    924  C   ALA A 285       4.713  21.539 -35.433  1.00 27.13           C  
ANISOU  924  C   ALA A 285     2296   4424   3589   -682   -211    120       C  
ATOM    925  O   ALA A 285       5.212  20.865 -34.524  1.00 27.05           O  
ANISOU  925  O   ALA A 285     2279   4444   3554   -722   -310    171       O  
ATOM    926  CB  ALA A 285       4.519  20.796 -37.817  1.00 19.39           C  
ANISOU  926  CB  ALA A 285     1208   3410   2750   -518    -35    156       C  
ATOM    927  N   ARG A 286       3.599  22.273 -35.281  1.00 24.62           N  
ANISOU  927  N   ARG A 286     2081   4092   3182   -690   -149     28       N  
ATOM    928  CA  ARG A 286       2.863  22.305 -34.030  1.00 25.37           C  
ANISOU  928  CA  ARG A 286     2294   4207   3138   -741   -180    -21       C  
ATOM    929  C   ARG A 286       1.916  21.090 -33.967  1.00 27.08           C  
ANISOU  929  C   ARG A 286     2537   4451   3302   -683   -129     -9       C  
ATOM    930  O   ARG A 286       1.643  20.579 -32.882  1.00 26.84           O  
ANISOU  930  O   ARG A 286     2573   4451   3175   -721   -176     -4       O  
ATOM    931  CB  ARG A 286       2.109  23.632 -33.882  1.00 26.93           C  
ANISOU  931  CB  ARG A 286     2585   4370   3276   -769   -125   -121       C  
ATOM    932  CG  ARG A 286       1.605  23.888 -32.461  1.00 30.55           C  
ANISOU  932  CG  ARG A 286     3176   4842   3589   -838   -163   -176       C  
ATOM    933  CD  ARG A 286       0.597  25.004 -32.424  1.00 36.81           C  
ANISOU  933  CD  ARG A 286     4064   5597   4326   -838    -74   -277       C  
ATOM    934  NE  ARG A 286      -0.070  25.052 -31.122  1.00 55.23           N  
ANISOU  934  NE  ARG A 286     6530   7943   6511   -885    -78   -329       N  
ATOM    935  CZ  ARG A 286      -1.341  24.720 -30.911  1.00 67.24           C  
ANISOU  935  CZ  ARG A 286     8112   9474   7962   -841     19   -364       C  
ATOM    936  NH1 ARG A 286      -2.116  24.344 -31.925  1.00 53.34           N  
ANISOU  936  NH1 ARG A 286     6289   7710   6269   -754    117   -355       N  
ATOM    937  NH2 ARG A 286      -1.853  24.780 -29.690  1.00 50.62           N  
ANISOU  937  NH2 ARG A 286     6132   7382   5721   -886     21   -406       N  
ATOM    938  N   SER A 287       1.441  20.631 -35.139  1.00 20.98           N  
ANISOU  938  N   SER A 287     1715   3664   2591   -597    -37      0       N  
ATOM    939  CA  SER A 287       0.549  19.479 -35.315  1.00 19.50           C  
ANISOU  939  CA  SER A 287     1541   3491   2376   -538     14     15       C  
ATOM    940  C   SER A 287       0.418  19.112 -36.787  1.00 22.25           C  
ANISOU  940  C   SER A 287     1826   3813   2815   -452     91     32       C  
ATOM    941  O   SER A 287       0.802  19.892 -37.665  1.00 21.34           O  
ANISOU  941  O   SER A 287     1672   3668   2767   -436    125     19       O  
ATOM    942  CB  SER A 287      -0.822  19.707 -34.672  1.00 21.55           C  
ANISOU  942  CB  SER A 287     1904   3758   2527   -550     67    -52       C  
ATOM    943  OG  SER A 287      -1.660  20.552 -35.438  1.00 27.34           O  
ANISOU  943  OG  SER A 287     2654   4459   3277   -515    160   -115       O  
ATOM    944  N   ALA A 288      -0.050  17.887 -37.050  1.00 18.77           N  
ANISOU  944  N   ALA A 288     1379   3379   2375   -401    114     65       N  
ATOM    945  CA  ALA A 288      -0.236  17.334 -38.396  1.00 17.47           C  
ANISOU  945  CA  ALA A 288     1174   3187   2278   -321    181     81       C  
ATOM    946  C   ALA A 288      -1.443  16.421 -38.292  1.00 21.29           C  
ANISOU  946  C   ALA A 288     1706   3676   2708   -295    213     73       C  
ATOM    947  O   ALA A 288      -1.446  15.494 -37.481  1.00 22.53           O  
ANISOU  947  O   ALA A 288     1875   3857   2829   -311    168    111       O  
ATOM    948  CB  ALA A 288       1.012  16.564 -38.841  1.00 17.94           C  
ANISOU  948  CB  ALA A 288     1150   3240   2427   -289    151    158       C  
ATOM    949  N   THR A 289      -2.504  16.746 -39.036  1.00 15.76           N  
ANISOU  949  N   THR A 289     1033   2953   2001   -261    286     27       N  
ATOM    950  CA  THR A 289      -3.770  16.044 -38.968  1.00 14.60           C  
ANISOU  950  CA  THR A 289      927   2808   1813   -244    318     17       C  
ATOM    951  C   THR A 289      -4.172  15.553 -40.339  1.00 18.43           C  
ANISOU  951  C   THR A 289     1397   3256   2349   -179    363     23       C  
ATOM    952  O   THR A 289      -3.852  16.213 -41.325  1.00 19.12           O  
ANISOU  952  O   THR A 289     1467   3318   2482   -151    394      8       O  
ATOM    953  CB  THR A 289      -4.804  17.019 -38.370  1.00 25.14           C  
ANISOU  953  CB  THR A 289     2315   4151   3088   -276    355    -45       C  
ATOM    954  OG1 THR A 289      -4.291  17.540 -37.153  1.00 21.14           O  
ANISOU  954  OG1 THR A 289     1836   3671   2526   -340    310    -56       O  
ATOM    955  CG2 THR A 289      -6.150  16.387 -38.091  1.00 27.81           C  
ANISOU  955  CG2 THR A 289     2685   4495   3386   -268    390    -50       C  
ATOM    956  N   ALA A 290      -4.860  14.384 -40.416  1.00 13.39           N  
ANISOU  956  N   ALA A 290      775   2613   1700   -157    365     46       N  
ATOM    957  CA  ALA A 290      -5.372  13.877 -41.691  1.00 11.75           C  
ANISOU  957  CA  ALA A 290      572   2365   1528   -103    399     46       C  
ATOM    958  C   ALA A 290      -6.667  13.082 -41.553  1.00 15.80           C  
ANISOU  958  C   ALA A 290     1115   2873   2014   -104    404     48       C  
ATOM    959  O   ALA A 290      -7.100  12.783 -40.434  1.00 15.35           O  
ANISOU  959  O   ALA A 290     1072   2848   1914   -142    389     58       O  
ATOM    960  CB  ALA A 290      -4.315  13.087 -42.439  1.00 11.96           C  
ANISOU  960  CB  ALA A 290      572   2366   1608    -59    390     89       C  
ATOM    961  N   ILE A 291      -7.323  12.816 -42.691  1.00 12.47           N  
ANISOU  961  N   ILE A 291      707   2412   1617    -67    427     40       N  
ATOM    962  CA  ILE A 291      -8.559  12.029 -42.777  1.00 11.71           C  
ANISOU  962  CA  ILE A 291      634   2303   1514    -68    425     47       C  
ATOM    963  C   ILE A 291      -8.593  11.347 -44.115  1.00 16.00           C  
ANISOU  963  C   ILE A 291     1198   2793   2088    -24    422     55       C  
ATOM    964  O   ILE A 291      -8.166  11.946 -45.104  1.00 15.62           O  
ANISOU  964  O   ILE A 291     1155   2722   2059      7    444     36       O  
ATOM    965  CB  ILE A 291      -9.867  12.848 -42.534  1.00 13.95           C  
ANISOU  965  CB  ILE A 291      918   2597   1784    -91    455     14       C  
ATOM    966  CG1 ILE A 291     -11.096  11.890 -42.417  1.00 13.03           C  
ANISOU  966  CG1 ILE A 291      809   2471   1670   -102    446     38       C  
ATOM    967  CG2 ILE A 291     -10.088  13.931 -43.627  1.00 14.02           C  
ANISOU  967  CG2 ILE A 291      927   2579   1821    -65    483    -21       C  
ATOM    968  CD1 ILE A 291     -12.313  12.496 -41.900  1.00 14.48           C  
ANISOU  968  CD1 ILE A 291      981   2672   1850   -125    481     21       C  
ATOM    969  N   ALA A 292      -9.097  10.104 -44.152  1.00 12.28           N  
ANISOU  969  N   ALA A 292      747   2299   1619    -23    397     82       N  
ATOM    970  CA  ALA A 292      -9.256   9.325 -45.379  1.00 11.44           C  
ANISOU  970  CA  ALA A 292      680   2134   1531     13    388     86       C  
ATOM    971  C   ALA A 292     -10.679   8.818 -45.354  1.00 16.54           C  
ANISOU  971  C   ALA A 292     1341   2766   2177    -14    366     91       C  
ATOM    972  O   ALA A 292     -11.177   8.335 -44.322  1.00 15.56           O  
ANISOU  972  O   ALA A 292     1200   2667   2044    -50    353    116       O  
ATOM    973  CB  ALA A 292      -8.274   8.162 -45.412  1.00 12.21           C  
ANISOU  973  CB  ALA A 292      790   2205   1643     41    374    120       C  
ATOM    974  N   VAL A 293     -11.354   8.979 -46.480  1.00 12.47           N  
ANISOU  974  N   VAL A 293      855   2211   1672     -1    360     72       N  
ATOM    975  CA  VAL A 293     -12.745   8.625 -46.623  1.00 11.23           C  
ANISOU  975  CA  VAL A 293      702   2035   1529    -29    330     81       C  
ATOM    976  C   VAL A 293     -12.897   7.801 -47.903  1.00 15.10           C  
ANISOU  976  C   VAL A 293     1259   2456   2023     -9    292     80       C  
ATOM    977  O   VAL A 293     -12.255   8.105 -48.925  1.00 11.39           O  
ANISOU  977  O   VAL A 293      831   1956   1539     30    305     58       O  
ATOM    978  CB  VAL A 293     -13.631   9.932 -46.633  1.00 15.17           C  
ANISOU  978  CB  VAL A 293     1165   2559   2041    -42    352     58       C  
ATOM    979  CG1 VAL A 293     -15.075   9.654 -47.021  1.00 15.19           C  
ANISOU  979  CG1 VAL A 293     1161   2535   2076    -66    316     73       C  
ATOM    980  CG2 VAL A 293     -13.584  10.658 -45.291  1.00 14.59           C  
ANISOU  980  CG2 VAL A 293     1042   2546   1956    -66    393     54       C  
ATOM    981  N   ASP A 294     -13.773   6.756 -47.830  1.00 14.09           N  
ANISOU  981  N   ASP A 294     1145   2297   1910    -39    246    106       N  
ATOM    982  CA  ASP A 294     -14.214   5.898 -48.928  1.00 14.11           C  
ANISOU  982  CA  ASP A 294     1219   2227   1915    -37    193    105       C  
ATOM    983  C   ASP A 294     -15.275   6.772 -49.618  1.00 18.27           C  
ANISOU  983  C   ASP A 294     1735   2750   2457    -54    170     93       C  
ATOM    984  O   ASP A 294     -16.310   7.040 -49.023  1.00 19.14           O  
ANISOU  984  O   ASP A 294     1782   2887   2601    -91    160    113       O  
ATOM    985  CB  ASP A 294     -14.842   4.619 -48.328  1.00 16.10           C  
ANISOU  985  CB  ASP A 294     1470   2457   2189    -77    150    144       C  
ATOM    986  CG  ASP A 294     -15.184   3.503 -49.289  1.00 31.39           C  
ANISOU  986  CG  ASP A 294     3491   4309   4128    -83     88    145       C  
ATOM    987  OD1 ASP A 294     -15.840   3.780 -50.319  1.00 35.14           O  
ANISOU  987  OD1 ASP A 294     4003   4748   4601    -91     48    128       O  
ATOM    988  OD2 ASP A 294     -14.911   2.337 -48.955  1.00 39.17           O  
ANISOU  988  OD2 ASP A 294     4505   5261   5118    -86     72    167       O  
ATOM    989  N   VAL A 295     -14.969   7.319 -50.806  1.00 15.71           N  
ANISOU  989  N   VAL A 295     1465   2396   2108    -22    170     64       N  
ATOM    990  CA  VAL A 295     -15.841   8.278 -51.530  1.00 15.82           C  
ANISOU  990  CA  VAL A 295     1471   2405   2133    -31    145     56       C  
ATOM    991  C   VAL A 295     -17.190   7.678 -51.972  1.00 21.92           C  
ANISOU  991  C   VAL A 295     2256   3135   2936    -76     59     81       C  
ATOM    992  O   VAL A 295     -18.157   8.417 -52.211  1.00 21.73           O  
ANISOU  992  O   VAL A 295     2190   3118   2948    -95     31     92       O  
ATOM    993  CB  VAL A 295     -15.132   8.960 -52.741  1.00 18.12           C  
ANISOU  993  CB  VAL A 295     1831   2671   2383     12    165     26       C  
ATOM    994  CG1 VAL A 295     -13.710   9.407 -52.397  1.00 16.11           C  
ANISOU  994  CG1 VAL A 295     1564   2449   2109     53    245      9       C  
ATOM    995  CG2 VAL A 295     -15.138   8.041 -53.954  1.00 18.69           C  
ANISOU  995  CG2 VAL A 295     2020   2666   2415     19    113     17       C  
ATOM    996  N   LYS A 296     -17.213   6.351 -52.138  1.00 19.31           N  
ANISOU  996  N   LYS A 296     1984   2755   2598    -92     13     91       N  
ATOM    997  CA  LYS A 296     -18.357   5.589 -52.603  1.00 20.44           C  
ANISOU  997  CA  LYS A 296     2151   2846   2769   -141    -81    115       C  
ATOM    998  C   LYS A 296     -19.339   5.278 -51.475  1.00 26.18           C  
ANISOU  998  C   LYS A 296     2777   3606   3565   -192    -92    161       C  
ATOM    999  O   LYS A 296     -20.519   5.070 -51.759  1.00 26.37           O  
ANISOU  999  O   LYS A 296     2779   3604   3638   -239   -165    191       O  
ATOM   1000  CB  LYS A 296     -17.872   4.287 -53.273  1.00 22.07           C  
ANISOU 1000  CB  LYS A 296     2478   2974   2933   -136   -120    101       C  
ATOM   1001  CG  LYS A 296     -17.236   4.482 -54.660  1.00 23.31           C  
ANISOU 1001  CG  LYS A 296     2758   3081   3020    -95   -122     59       C  
ATOM   1002  CD  LYS A 296     -16.493   3.227 -55.103  1.00 26.28           C  
ANISOU 1002  CD  LYS A 296     3251   3382   3351    -72   -124     38       C  
ATOM   1003  CE  LYS A 296     -15.417   3.459 -56.143  1.00 27.75           C  
ANISOU 1003  CE  LYS A 296     3545   3535   3464     -9    -71     -5       C  
ATOM   1004  NZ  LYS A 296     -15.948   3.544 -57.536  1.00 27.11           N  
ANISOU 1004  NZ  LYS A 296     3584   3389   3328    -24   -141    -26       N  
ATOM   1005  N   THR A 297     -18.849   5.227 -50.200  1.00 22.43           N  
ANISOU 1005  N   THR A 297     2243   3186   3093   -186    -21    171       N  
ATOM   1006  CA  THR A 297     -19.651   4.828 -49.038  1.00 21.90           C  
ANISOU 1006  CA  THR A 297     2093   3151   3079   -231    -15    217       C  
ATOM   1007  C   THR A 297     -19.823   5.889 -47.954  1.00 24.52           C  
ANISOU 1007  C   THR A 297     2328   3561   3426   -227     65    222       C  
ATOM   1008  O   THR A 297     -20.750   5.757 -47.153  1.00 23.55           O  
ANISOU 1008  O   THR A 297     2133   3461   3352   -265     77    262       O  
ATOM   1009  CB  THR A 297     -19.182   3.462 -48.445  1.00 25.49           C  
ANISOU 1009  CB  THR A 297     2583   3583   3521   -244    -22    239       C  
ATOM   1010  OG1 THR A 297     -17.954   3.619 -47.726  1.00 26.40           O  
ANISOU 1010  OG1 THR A 297     2698   3740   3592   -205     47    223       O  
ATOM   1011  CG2 THR A 297     -19.046   2.375 -49.481  1.00 20.94           C  
ANISOU 1011  CG2 THR A 297     2111   2917   2929   -247    -96    230       C  
ATOM   1012  N   GLY A 298     -18.909   6.873 -47.898  1.00 19.51           N  
ANISOU 1012  N   GLY A 298     1699   2962   2751   -183    125    183       N  
ATOM   1013  CA  GLY A 298     -18.916   7.924 -46.887  1.00 18.19           C  
ANISOU 1013  CA  GLY A 298     1463   2862   2585   -177    202    175       C  
ATOM   1014  C   GLY A 298     -18.252   7.541 -45.569  1.00 21.91           C  
ANISOU 1014  C   GLY A 298     1924   3378   3023   -184    251    185       C  
ATOM   1015  O   GLY A 298     -18.228   8.345 -44.629  1.00 23.49           O  
ANISOU 1015  O   GLY A 298     2082   3631   3212   -186    314    177       O  
ATOM   1016  N   GLU A 299     -17.718   6.319 -45.485  1.00 15.71           N  
ANISOU 1016  N   GLU A 299     1184   2567   2219   -190    219    204       N  
ATOM   1017  CA  GLU A 299     -17.017   5.762 -44.319  1.00 15.57           C  
ANISOU 1017  CA  GLU A 299     1166   2583   2168   -197    246    224       C  
ATOM   1018  C   GLU A 299     -15.633   6.410 -44.099  1.00 19.25           C  
ANISOU 1018  C   GLU A 299     1646   3080   2586   -160    282    191       C  
ATOM   1019  O   GLU A 299     -14.836   6.536 -45.038  1.00 17.98           O  
ANISOU 1019  O   GLU A 299     1525   2889   2416   -121    271    164       O  
ATOM   1020  CB  GLU A 299     -16.859   4.219 -44.465  1.00 16.74           C  
ANISOU 1020  CB  GLU A 299     1360   2679   2323   -210    192    258       C  
ATOM   1021  CG  GLU A 299     -18.187   3.471 -44.344  1.00 30.41           C  
ANISOU 1021  CG  GLU A 299     3065   4384   4104   -261    157    303       C  
ATOM   1022  CD  GLU A 299     -18.171   1.972 -44.579  1.00 48.74           C  
ANISOU 1022  CD  GLU A 299     5437   6640   6440   -280     96    335       C  
ATOM   1023  OE1 GLU A 299     -18.121   1.556 -45.759  1.00 47.72           O  
ANISOU 1023  OE1 GLU A 299     5371   6444   6318   -266     42    314       O  
ATOM   1024  OE2 GLU A 299     -18.295   1.216 -43.588  1.00 37.71           O  
ANISOU 1024  OE2 GLU A 299     4025   5256   5049   -311    103    382       O  
ATOM   1025  N   ILE A 300     -15.348   6.800 -42.856  1.00 15.97           N  
ANISOU 1025  N   ILE A 300     1203   2723   2141   -175    324    197       N  
ATOM   1026  CA  ILE A 300     -14.052   7.354 -42.486  1.00 15.15           C  
ANISOU 1026  CA  ILE A 300     1107   2651   1998   -153    345    175       C  
ATOM   1027  C   ILE A 300     -13.140   6.138 -42.190  1.00 18.90           C  
ANISOU 1027  C   ILE A 300     1610   3111   2462   -147    311    212       C  
ATOM   1028  O   ILE A 300     -13.405   5.405 -41.255  1.00 19.21           O  
ANISOU 1028  O   ILE A 300     1645   3165   2490   -179    303    253       O  
ATOM   1029  CB  ILE A 300     -14.192   8.352 -41.296  1.00 17.58           C  
ANISOU 1029  CB  ILE A 300     1387   3022   2272   -177    396    162       C  
ATOM   1030  CG1 ILE A 300     -15.035   9.590 -41.701  1.00 18.28           C  
ANISOU 1030  CG1 ILE A 300     1448   3113   2384   -171    435    125       C  
ATOM   1031  CG2 ILE A 300     -12.827   8.759 -40.730  1.00 14.68           C  
ANISOU 1031  CG2 ILE A 300     1030   2687   1862   -170    399    150       C  
ATOM   1032  CD1 ILE A 300     -15.595  10.481 -40.511  1.00 19.28           C  
ANISOU 1032  CD1 ILE A 300     1552   3288   2486   -196    500    112       C  
ATOM   1033  N   LEU A 301     -12.118   5.897 -43.017  1.00 16.56           N  
ANISOU 1033  N   LEU A 301     1340   2778   2173   -104    296    202       N  
ATOM   1034  CA  LEU A 301     -11.211   4.760 -42.844  1.00 16.86           C  
ANISOU 1034  CA  LEU A 301     1400   2792   2216    -87    269    238       C  
ATOM   1035  C   LEU A 301     -10.010   5.063 -41.954  1.00 20.25           C  
ANISOU 1035  C   LEU A 301     1803   3267   2624    -83    274    253       C  
ATOM   1036  O   LEU A 301      -9.373   4.141 -41.443  1.00 20.26           O  
ANISOU 1036  O   LEU A 301     1808   3261   2630    -80    248    298       O  
ATOM   1037  CB  LEU A 301     -10.733   4.243 -44.208  1.00 17.17           C  
ANISOU 1037  CB  LEU A 301     1485   2760   2280    -37    258    224       C  
ATOM   1038  CG  LEU A 301     -11.792   3.805 -45.221  1.00 21.75           C  
ANISOU 1038  CG  LEU A 301     2107   3281   2875    -44    233    210       C  
ATOM   1039  CD1 LEU A 301     -11.132   3.321 -46.499  1.00 21.40           C  
ANISOU 1039  CD1 LEU A 301     2128   3165   2836      8    231    190       C  
ATOM   1040  CD2 LEU A 301     -12.765   2.746 -44.643  1.00 21.83           C  
ANISOU 1040  CD2 LEU A 301     2120   3274   2900    -91    196    251       C  
ATOM   1041  N   ALA A 302      -9.668   6.348 -41.815  1.00 16.84           N  
ANISOU 1041  N   ALA A 302     1347   2877   2175    -84    302    218       N  
ATOM   1042  CA  ALA A 302      -8.549   6.833 -41.003  1.00 16.18           C  
ANISOU 1042  CA  ALA A 302     1238   2837   2072    -91    298    228       C  
ATOM   1043  C   ALA A 302      -8.761   8.304 -40.678  1.00 17.91           C  
ANISOU 1043  C   ALA A 302     1442   3100   2264   -114    329    183       C  
ATOM   1044  O   ALA A 302      -9.208   9.065 -41.525  1.00 17.67           O  
ANISOU 1044  O   ALA A 302     1412   3054   2249    -97    358    142       O  
ATOM   1045  CB  ALA A 302      -7.215   6.616 -41.734  1.00 16.59           C  
ANISOU 1045  CB  ALA A 302     1281   2859   2165    -39    292    239       C  
ATOM   1046  N   MET A 303      -8.538   8.677 -39.435  1.00 14.74           N  
ANISOU 1046  N   MET A 303     1035   2748   1816   -154    321    191       N  
ATOM   1047  CA  MET A 303      -8.691  10.041 -38.929  1.00 15.30           C  
ANISOU 1047  CA  MET A 303     1105   2856   1851   -182    351    146       C  
ATOM   1048  C   MET A 303      -7.868  10.078 -37.672  1.00 20.97           C  
ANISOU 1048  C   MET A 303     1830   3617   2522   -221    314    170       C  
ATOM   1049  O   MET A 303      -8.218   9.411 -36.679  1.00 20.27           O  
ANISOU 1049  O   MET A 303     1764   3551   2388   -254    299    204       O  
ATOM   1050  CB  MET A 303     -10.166  10.411 -38.617  1.00 17.83           C  
ANISOU 1050  CB  MET A 303     1437   3187   2151   -204    397    122       C  
ATOM   1051  CG  MET A 303     -10.344  11.883 -38.290  1.00 21.53           C  
ANISOU 1051  CG  MET A 303     1910   3678   2594   -219    439     68       C  
ATOM   1052  SD  MET A 303     -12.049  12.383 -37.940  1.00 25.80           S  
ANISOU 1052  SD  MET A 303     2453   4225   3125   -235    510     44       S  
ATOM   1053  CE  MET A 303     -11.879  14.139 -37.973  1.00 21.83           C  
ANISOU 1053  CE  MET A 303     1955   3725   2615   -231    553    -25       C  
ATOM   1054  N   THR A 304      -6.744  10.826 -37.733  1.00 16.74           N  
ANISOU 1054  N   THR A 304     1274   3089   1996   -219    294    158       N  
ATOM   1055  CA  THR A 304      -5.790  10.937 -36.640  1.00 16.74           C  
ANISOU 1055  CA  THR A 304     1276   3125   1958   -260    240    184       C  
ATOM   1056  C   THR A 304      -5.011  12.280 -36.671  1.00 21.14           C  
ANISOU 1056  C   THR A 304     1820   3693   2520   -276    236    145       C  
ATOM   1057  O   THR A 304      -5.065  13.028 -37.653  1.00 18.05           O  
ANISOU 1057  O   THR A 304     1411   3276   2170   -247    277    106       O  
ATOM   1058  CB  THR A 304      -4.968   9.608 -36.481  1.00 18.96           C  
ANISOU 1058  CB  THR A 304     1536   3398   2270   -245    180    260       C  
ATOM   1059  OG1 THR A 304      -4.278   9.570 -35.244  1.00 20.90           O  
ANISOU 1059  OG1 THR A 304     1792   3683   2468   -295    116    296       O  
ATOM   1060  CG2 THR A 304      -4.017   9.365 -37.585  1.00 15.54           C  
ANISOU 1060  CG2 THR A 304     1053   2927   1924   -189    177    277       C  
ATOM   1061  N   SER A 305      -4.323  12.591 -35.563  1.00 18.71           N  
ANISOU 1061  N   SER A 305     1527   3419   2163   -329    180    158       N  
ATOM   1062  CA  SER A 305      -3.610  13.841 -35.427  1.00 18.86           C  
ANISOU 1062  CA  SER A 305     1541   3445   2182   -358    164    123       C  
ATOM   1063  C   SER A 305      -2.341  13.606 -34.635  1.00 23.34           C  
ANISOU 1063  C   SER A 305     2088   4035   2746   -398     68    176       C  
ATOM   1064  O   SER A 305      -2.327  12.788 -33.722  1.00 24.20           O  
ANISOU 1064  O   SER A 305     2223   4168   2806   -425     19    222       O  
ATOM   1065  CB  SER A 305      -4.503  14.852 -34.706  1.00 22.95           C  
ANISOU 1065  CB  SER A 305     2125   3977   2616   -400    206     56       C  
ATOM   1066  OG  SER A 305      -4.063  16.193 -34.829  1.00 36.74           O  
ANISOU 1066  OG  SER A 305     3874   5714   4371   -421    209      6       O  
ATOM   1067  N   TRP A 306      -1.272  14.277 -35.012  1.00 19.27           N  
ANISOU 1067  N   TRP A 306     1523   3510   2289   -402     38    179       N  
ATOM   1068  CA  TRP A 306      -0.030  14.229 -34.264  1.00 20.39           C  
ANISOU 1068  CA  TRP A 306     1635   3671   2440   -448    -64    232       C  
ATOM   1069  C   TRP A 306       0.116  15.634 -33.692  1.00 23.95           C  
ANISOU 1069  C   TRP A 306     2128   4132   2840   -514    -84    174       C  
ATOM   1070  O   TRP A 306      -0.118  16.587 -34.419  1.00 22.98           O  
ANISOU 1070  O   TRP A 306     2001   3985   2747   -498    -24    118       O  
ATOM   1071  CB  TRP A 306       1.178  13.798 -35.124  1.00 19.57           C  
ANISOU 1071  CB  TRP A 306     1427   3546   2463   -400    -86    295       C  
ATOM   1072  CG  TRP A 306       2.508  14.047 -34.468  1.00 21.71           C  
ANISOU 1072  CG  TRP A 306     1648   3834   2768   -452   -192    348       C  
ATOM   1073  CD1 TRP A 306       3.213  13.177 -33.687  1.00 25.49           C  
ANISOU 1073  CD1 TRP A 306     2101   4332   3254   -472   -287    430       C  
ATOM   1074  CD2 TRP A 306       3.263  15.274 -34.487  1.00 21.82           C  
ANISOU 1074  CD2 TRP A 306     1633   3845   2813   -497   -224    328       C  
ATOM   1075  NE1 TRP A 306       4.364  13.775 -33.233  1.00 26.03           N  
ANISOU 1075  NE1 TRP A 306     2120   4411   3360   -527   -382    465       N  
ATOM   1076  CE2 TRP A 306       4.420  15.064 -33.706  1.00 27.09           C  
ANISOU 1076  CE2 TRP A 306     2252   4531   3510   -546   -345    402       C  
ATOM   1077  CE3 TRP A 306       3.049  16.546 -35.055  1.00 22.34           C  
ANISOU 1077  CE3 TRP A 306     1710   3891   2887   -504   -167    257       C  
ATOM   1078  CZ2 TRP A 306       5.373  16.073 -33.489  1.00 27.05           C  
ANISOU 1078  CZ2 TRP A 306     2207   4526   3545   -607   -414    407       C  
ATOM   1079  CZ3 TRP A 306       3.977  17.550 -34.814  1.00 24.76           C  
ANISOU 1079  CZ3 TRP A 306     1984   4194   3227   -564   -229    259       C  
ATOM   1080  CH2 TRP A 306       5.133  17.306 -34.060  1.00 26.45           C  
ANISOU 1080  CH2 TRP A 306     2148   4428   3476   -616   -352    333       C  
ATOM   1081  N   PRO A 307       0.434  15.810 -32.401  1.00 23.10           N  
ANISOU 1081  N   PRO A 307     2074   4054   2649   -591   -168    182       N  
ATOM   1082  CA  PRO A 307       0.687  14.770 -31.386  1.00 24.03           C  
ANISOU 1082  CA  PRO A 307     2214   4202   2715   -622   -251    251       C  
ATOM   1083  C   PRO A 307      -0.593  14.165 -30.806  1.00 28.16           C  
ANISOU 1083  C   PRO A 307     2822   4741   3135   -620   -197    234       C  
ATOM   1084  O   PRO A 307      -1.601  14.850 -30.657  1.00 26.95           O  
ANISOU 1084  O   PRO A 307     2740   4587   2913   -630   -121    159       O  
ATOM   1085  CB  PRO A 307       1.493  15.514 -30.299  1.00 27.01           C  
ANISOU 1085  CB  PRO A 307     2632   4600   3032   -716   -362    251       C  
ATOM   1086  CG  PRO A 307       1.616  16.987 -30.764  1.00 31.37           C  
ANISOU 1086  CG  PRO A 307     3184   5126   3608   -734   -329    175       C  
ATOM   1087  CD  PRO A 307       0.572  17.165 -31.830  1.00 25.64           C  
ANISOU 1087  CD  PRO A 307     2452   4374   2914   -660   -192    119       C  
ATOM   1088  N   SER A 308      -0.542  12.874 -30.481  1.00 25.67           N  
ANISOU 1088  N   SER A 308     2496   4438   2818   -607   -234    309       N  
ATOM   1089  CA  SER A 308      -1.638  12.166 -29.832  1.00 26.05           C  
ANISOU 1089  CA  SER A 308     2619   4503   2775   -613   -195    313       C  
ATOM   1090  C   SER A 308      -1.163  11.838 -28.396  1.00 32.47           C  
ANISOU 1090  C   SER A 308     3498   5353   3487   -688   -300    364       C  
ATOM   1091  O   SER A 308      -0.241  12.486 -27.902  1.00 33.93           O  
ANISOU 1091  O   SER A 308     3689   5549   3653   -743   -390    367       O  
ATOM   1092  CB  SER A 308      -2.008  10.906 -30.613  1.00 27.81           C  
ANISOU 1092  CB  SER A 308     2789   4703   3074   -543   -155    360       C  
ATOM   1093  OG  SER A 308      -3.278  10.405 -30.234  1.00 34.96           O  
ANISOU 1093  OG  SER A 308     3756   5616   3909   -545    -92    351       O  
ATOM   1094  N   TYR A 309      -1.766  10.854 -27.730  1.00 29.23           N  
ANISOU 1094  N   TYR A 309     3137   4959   3010   -695   -296    408       N  
ATOM   1095  CA  TYR A 309      -1.385  10.489 -26.364  1.00 30.18           C  
ANISOU 1095  CA  TYR A 309     3332   5115   3022   -767   -395    463       C  
ATOM   1096  C   TYR A 309      -1.712   9.024 -26.112  1.00 36.09           C  
ANISOU 1096  C   TYR A 309     4078   5865   3769   -745   -402    548       C  
ATOM   1097  O   TYR A 309      -2.493   8.434 -26.862  1.00 35.40           O  
ANISOU 1097  O   TYR A 309     3957   5754   3738   -686   -314    544       O  
ATOM   1098  CB  TYR A 309      -2.120  11.401 -25.335  1.00 30.83           C  
ANISOU 1098  CB  TYR A 309     3552   5222   2942   -834   -355    390       C  
ATOM   1099  CG  TYR A 309      -3.595  11.088 -25.168  1.00 30.54           C  
ANISOU 1099  CG  TYR A 309     3575   5189   2840   -814   -226    360       C  
ATOM   1100  CD1 TYR A 309      -4.508  11.383 -26.174  1.00 30.89           C  
ANISOU 1100  CD1 TYR A 309     3574   5207   2956   -753   -104    302       C  
ATOM   1101  CD2 TYR A 309      -4.077  10.495 -24.003  1.00 31.71           C  
ANISOU 1101  CD2 TYR A 309     3823   5367   2859   -860   -229    398       C  
ATOM   1102  CE1 TYR A 309      -5.860  11.080 -26.035  1.00 31.86           C  
ANISOU 1102  CE1 TYR A 309     3736   5333   3038   -737      9    286       C  
ATOM   1103  CE2 TYR A 309      -5.430  10.187 -23.852  1.00 31.70           C  
ANISOU 1103  CE2 TYR A 309     3865   5369   2812   -843   -104    381       C  
ATOM   1104  CZ  TYR A 309      -6.317  10.486 -24.870  1.00 37.83           C  
ANISOU 1104  CZ  TYR A 309     4582   6118   3674   -781     13    325       C  
ATOM   1105  OH  TYR A 309      -7.655  10.219 -24.734  1.00 39.77           O  
ANISOU 1105  OH  TYR A 309     4856   6365   3890   -767    133    314       O  
ATOM   1106  N   ASN A 310      -1.150   8.453 -25.037  1.00 34.69           N  
ANISOU 1106  N   ASN A 310     3944   5713   3522   -799   -512    626       N  
ATOM   1107  CA  ASN A 310      -1.442   7.083 -24.653  1.00 35.39           C  
ANISOU 1107  CA  ASN A 310     4046   5804   3599   -788   -528    713       C  
ATOM   1108  C   ASN A 310      -2.514   7.069 -23.540  1.00 40.19           C  
ANISOU 1108  C   ASN A 310     4788   6443   4038   -843   -475    696       C  
ATOM   1109  O   ASN A 310      -2.204   7.449 -22.407  1.00 40.37           O  
ANISOU 1109  O   ASN A 310     4907   6499   3931   -919   -546    703       O  
ATOM   1110  CB  ASN A 310      -0.181   6.351 -24.221  1.00 37.09           C  
ANISOU 1110  CB  ASN A 310     4215   6021   3855   -804   -679    824       C  
ATOM   1111  CG  ASN A 310      -0.357   4.856 -24.093  1.00 59.21           C  
ANISOU 1111  CG  ASN A 310     7004   8807   6687   -775   -694    922       C  
ATOM   1112  OD1 ASN A 310      -1.458   4.345 -23.858  1.00 46.96           O  
ANISOU 1112  OD1 ASN A 310     5513   7257   5073   -774   -614    918       O  
ATOM   1113  ND2 ASN A 310       0.736   4.117 -24.239  1.00 54.85           N  
ANISOU 1113  ND2 ASN A 310     6367   8235   6238   -750   -798   1017       N  
ATOM   1114  N   PRO A 311      -3.772   6.634 -23.843  1.00 36.84           N  
ANISOU 1114  N   PRO A 311     4376   6007   3614   -809   -351    677       N  
ATOM   1115  CA  PRO A 311      -4.828   6.621 -22.805  1.00 37.63           C  
ANISOU 1115  CA  PRO A 311     4596   6137   3564   -856   -281    666       C  
ATOM   1116  C   PRO A 311      -4.673   5.539 -21.737  1.00 44.70           C  
ANISOU 1116  C   PRO A 311     5554   7052   4378   -899   -356    773       C  
ATOM   1117  O   PRO A 311      -5.346   5.613 -20.715  1.00 45.85           O  
ANISOU 1117  O   PRO A 311     5815   7227   4377   -951   -312    771       O  
ATOM   1118  CB  PRO A 311      -6.120   6.408 -23.602  1.00 38.10           C  
ANISOU 1118  CB  PRO A 311     4618   6173   3687   -801   -138    630       C  
ATOM   1119  CG  PRO A 311      -5.736   6.480 -25.032  1.00 40.90           C  
ANISOU 1119  CG  PRO A 311     4852   6487   4202   -732   -138    606       C  
ATOM   1120  CD  PRO A 311      -4.300   6.152 -25.133  1.00 36.71           C  
ANISOU 1120  CD  PRO A 311     4267   5950   3733   -729   -271    666       C  
ATOM   1121  N   ASN A 312      -3.808   4.534 -21.970  1.00 42.42           N  
ANISOU 1121  N   ASN A 312     5190   6744   4182   -876   -461    868       N  
ATOM   1122  CA  ASN A 312      -3.549   3.461 -21.017  1.00 44.13           C  
ANISOU 1122  CA  ASN A 312     5456   6973   4337   -913   -547    981       C  
ATOM   1123  C   ASN A 312      -2.720   3.966 -19.825  1.00 54.26           C  
ANISOU 1123  C   ASN A 312     6832   8297   5485   -997   -672   1005       C  
ATOM   1124  O   ASN A 312      -2.818   3.393 -18.739  1.00 55.00           O  
ANISOU 1124  O   ASN A 312     7023   8416   5460  -1050   -718   1076       O  
ATOM   1125  CB  ASN A 312      -2.877   2.264 -21.706  1.00 42.47           C  
ANISOU 1125  CB  ASN A 312     5135   6720   4283   -853   -615   1074       C  
ATOM   1126  CG  ASN A 312      -3.711   1.599 -22.790  1.00 50.50           C  
ANISOU 1126  CG  ASN A 312     6084   7690   5415   -781   -506   1059       C  
ATOM   1127  OD1 ASN A 312      -4.884   1.254 -22.599  1.00 44.97           O  
ANISOU 1127  OD1 ASN A 312     5432   6990   4664   -789   -411   1052       O  
ATOM   1128  ND2 ASN A 312      -3.103   1.347 -23.937  1.00 33.29           N  
ANISOU 1128  ND2 ASN A 312     3793   5465   3392   -710   -520   1060       N  
ATOM   1129  N   ASP A 313      -1.930   5.051 -20.022  1.00 54.92           N  
ANISOU 1129  N   ASP A 313     6895   8387   5585  -1013   -728    946       N  
ATOM   1130  CA  ASP A 313      -1.084   5.687 -18.997  1.00 58.01           C  
ANISOU 1130  CA  ASP A 313     7372   8811   5859  -1100   -860    956       C  
ATOM   1131  C   ASP A 313      -1.870   6.716 -18.166  1.00 65.88           C  
ANISOU 1131  C   ASP A 313     8529   9837   6667  -1163   -782    860       C  
ATOM   1132  O   ASP A 313      -2.557   7.566 -18.735  1.00 64.78           O  
ANISOU 1132  O   ASP A 313     8385   9686   6543  -1135   -656    752       O  
ATOM   1133  CB  ASP A 313       0.154   6.343 -19.646  1.00 59.98           C  
ANISOU 1133  CB  ASP A 313     7513   9046   6232  -1090   -960    946       C  
ATOM   1134  CG  ASP A 313       1.024   5.400 -20.461  1.00 72.73           C  
ANISOU 1134  CG  ASP A 313     8969  10628   8036  -1023  -1030   1041       C  
ATOM   1135  OD1 ASP A 313       1.146   4.212 -20.072  1.00 74.54           O  
ANISOU 1135  OD1 ASP A 313     9197  10855   8271  -1019  -1090   1150       O  
ATOM   1136  OD2 ASP A 313       1.619   5.859 -21.459  1.00 77.71           O  
ANISOU 1136  OD2 ASP A 313     9482  11233   8809   -976  -1025   1011       O  
ATOM   1137  N   LYS A 314      -1.750   6.650 -16.825  1.00 66.93           N  
ANISOU 1137  N   LYS A 314     8808  10003   6620  -1248   -857    899       N  
ATOM   1138  CA  LYS A 314      -2.472   7.532 -15.892  1.00 68.93           C  
ANISOU 1138  CA  LYS A 314     9240  10280   6671  -1312   -781    814       C  
ATOM   1139  C   LYS A 314      -1.832   8.887 -15.536  1.00 75.49           C  
ANISOU 1139  C   LYS A 314    10146  11114   7423  -1377   -855    730       C  
ATOM   1140  O   LYS A 314      -2.561   9.817 -15.180  1.00 75.03           O  
ANISOU 1140  O   LYS A 314    10205  11057   7244  -1400   -745    624       O  
ATOM   1141  CB  LYS A 314      -2.891   6.771 -14.615  1.00 73.12           C  
ANISOU 1141  CB  LYS A 314     9918  10841   7022  -1369   -792    889       C  
ATOM   1142  CG  LYS A 314      -4.091   5.840 -14.804  1.00 88.82           C  
ANISOU 1142  CG  LYS A 314    11888  12826   9036  -1317   -640    922       C  
ATOM   1143  CD  LYS A 314      -5.431   6.574 -14.727  1.00100.49           C  
ANISOU 1143  CD  LYS A 314    13443  14307  10433  -1305   -434    814       C  
ATOM   1144  CE  LYS A 314      -6.582   5.685 -15.135  1.00112.68           C  
ANISOU 1144  CE  LYS A 314    14926  15839  12048  -1248   -290    849       C  
ATOM   1145  NZ  LYS A 314      -7.876   6.419 -15.156  1.00121.23           N  
ANISOU 1145  NZ  LYS A 314    16056  16921  13084  -1228    -88    750       N  
ATOM   1146  N   GLY A 315      -0.505   8.987 -15.622  1.00 74.49           N  
ANISOU 1146  N   GLY A 315     9952  10984   7368  -1406  -1035    779       N  
ATOM   1147  CA  GLY A 315       0.231  10.199 -15.262  1.00 76.23           C  
ANISOU 1147  CA  GLY A 315    10236  11203   7526  -1480  -1135    715       C  
ATOM   1148  C   GLY A 315       0.469  11.234 -16.348  1.00 81.58           C  
ANISOU 1148  C   GLY A 315    10806  11848   8342  -1440  -1090    622       C  
ATOM   1149  O   GLY A 315       0.179  10.995 -17.527  1.00 79.45           O  
ANISOU 1149  O   GLY A 315    10391  11557   8239  -1347   -993    614       O  
ATOM   1150  N   GLY A 316       1.001  12.388 -15.921  1.00 81.09           N  
ANISOU 1150  N   GLY A 316    10828  11780   8204  -1516  -1167    555       N  
ATOM   1151  CA  GLY A 316       1.365  13.533 -16.759  1.00 81.07           C  
ANISOU 1151  CA  GLY A 316    10750  11745   8310  -1502  -1150    468       C  
ATOM   1152  C   GLY A 316       0.224  14.210 -17.495  1.00 85.34           C  
ANISOU 1152  C   GLY A 316    11290  12260   8875  -1433   -939    350       C  
ATOM   1153  O   GLY A 316      -0.479  15.049 -16.921  1.00 85.94           O  
ANISOU 1153  O   GLY A 316    11519  12330   8805  -1468   -853    251       O  
ATOM   1154  N   LEU A 317       0.072  13.870 -18.796  1.00 80.47           N  
ANISOU 1154  N   LEU A 317    10501  11626   8448  -1334   -857    361       N  
ATOM   1155  CA  LEU A 317      -0.957  14.346 -19.737  1.00 78.90           C  
ANISOU 1155  CA  LEU A 317    10261  11402   8316  -1255   -669    272       C  
ATOM   1156  C   LEU A 317      -0.917  15.822 -20.171  1.00 82.00           C  
ANISOU 1156  C   LEU A 317    10666  11759   8731  -1263   -626    158       C  
ATOM   1157  O   LEU A 317      -0.416  16.688 -19.447  1.00 82.41           O  
ANISOU 1157  O   LEU A 317    10825  11805   8683  -1346   -708    113       O  
ATOM   1158  CB  LEU A 317      -2.395  13.897 -19.356  1.00 78.84           C  
ANISOU 1158  CB  LEU A 317    10340  11408   8209  -1225   -510    250       C  
ATOM   1159  CG  LEU A 317      -2.720  12.391 -19.439  1.00 83.23           C  
ANISOU 1159  CG  LEU A 317    10836  11983   8806  -1182   -499    356       C  
ATOM   1160  CD1 LEU A 317      -4.114  12.101 -18.895  1.00 83.44           C  
ANISOU 1160  CD1 LEU A 317    10963  12023   8718  -1173   -348    334       C  
ATOM   1161  CD2 LEU A 317      -2.606  11.861 -20.869  1.00 83.94           C  
ANISOU 1161  CD2 LEU A 317    10740  12048   9105  -1090   -470    388       C  
ATOM   1162  N   SER A 318      -1.446  16.079 -21.384  1.00 76.83           N  
ANISOU 1162  N   SER A 318     9905  11078   8210  -1178   -503    114       N  
ATOM   1163  CA  SER A 318      -1.586  17.393 -22.010  1.00 76.09           C  
ANISOU 1163  CA  SER A 318     9803  10944   8163  -1165   -436     12       C  
ATOM   1164  C   SER A 318      -2.898  17.421 -22.821  1.00 78.62           C  
ANISOU 1164  C   SER A 318    10086  11247   8538  -1075   -249    -40       C  
ATOM   1165  O   SER A 318      -2.974  16.851 -23.914  1.00 76.66           O  
ANISOU 1165  O   SER A 318     9703  10992   8434  -1001   -214     -3       O  
ATOM   1166  CB  SER A 318      -0.375  17.724 -22.882  1.00 78.87           C  
ANISOU 1166  CB  SER A 318    10018  11276   8671  -1161   -536     40       C  
ATOM   1167  OG  SER A 318      -0.236  16.843 -23.985  1.00 84.30           O  
ANISOU 1167  OG  SER A 318    10548  11964   9519  -1077   -514    108       O  
ATOM   1168  N   ASN A 319      -3.945  18.033 -22.239  1.00 75.63           N  
ANISOU 1168  N   ASN A 319     9834  10862   8041  -1084   -130   -120       N  
ATOM   1169  CA  ASN A 319      -5.275  18.146 -22.846  1.00 74.56           C  
ANISOU 1169  CA  ASN A 319     9671  10709   7948  -1007     47   -167       C  
ATOM   1170  C   ASN A 319      -5.279  19.177 -23.965  1.00 77.80           C  
ANISOU 1170  C   ASN A 319    10004  11074   8481   -962     96   -233       C  
ATOM   1171  O   ASN A 319      -5.871  18.934 -25.021  1.00 75.71           O  
ANISOU 1171  O   ASN A 319     9633  10796   8335   -885    177   -225       O  
ATOM   1172  CB  ASN A 319      -6.334  18.485 -21.783  1.00 75.92           C  
ANISOU 1172  CB  ASN A 319    10001  10886   7960  -1030    163   -226       C  
ATOM   1173  CG  ASN A 319      -6.019  19.673 -20.892  1.00104.84           C  
ANISOU 1173  CG  ASN A 319    13821  14527  11488  -1103    138   -312       C  
ATOM   1174  OD1 ASN A 319      -4.931  20.268 -20.939  1.00 99.89           O  
ANISOU 1174  OD1 ASN A 319    13192  13883  10877  -1153     12   -324       O  
ATOM   1175  ND2 ASN A 319      -6.969  20.036 -20.041  1.00 99.05           N  
ANISOU 1175  ND2 ASN A 319    13228  13788  10618  -1113    261   -371       N  
ATOM   1176  N   LYS A 320      -4.572  20.312 -23.723  1.00 75.46           N  
ANISOU 1176  N   LYS A 320     9766  10751   8155  -1017     36   -292       N  
ATOM   1177  CA  LYS A 320      -4.355  21.514 -24.547  1.00 74.52           C  
ANISOU 1177  CA  LYS A 320     9604  10582   8127  -1000     59   -360       C  
ATOM   1178  C   LYS A 320      -4.203  21.268 -26.066  1.00 75.57           C  
ANISOU 1178  C   LYS A 320     9565  10702   8445   -922     76   -322       C  
ATOM   1179  O   LYS A 320      -4.480  22.170 -26.867  1.00 75.00           O  
ANISOU 1179  O   LYS A 320     9459  10588   8448   -884    147   -378       O  
ATOM   1180  CB  LYS A 320      -3.123  22.271 -23.999  1.00 77.95           C  
ANISOU 1180  CB  LYS A 320    10096  11002   8519  -1092    -84   -378       C  
ATOM   1181  CG  LYS A 320      -3.033  23.746 -24.382  1.00 91.24           C  
ANISOU 1181  CG  LYS A 320    11804  12625  10238  -1101    -51   -470       C  
ATOM   1182  CD  LYS A 320      -1.796  24.025 -25.231  1.00 96.89           C  
ANISOU 1182  CD  LYS A 320    12396  13325  11094  -1115   -162   -431       C  
ATOM   1183  CE  LYS A 320      -1.663  25.486 -25.584  1.00101.58           C  
ANISOU 1183  CE  LYS A 320    13015  13855  11725  -1132   -138   -515       C  
ATOM   1184  NZ  LYS A 320      -0.396  25.765 -26.306  1.00107.64           N  
ANISOU 1184  NZ  LYS A 320    13665  14609  12625  -1156   -249   -469       N  
ATOM   1185  N   ASP A 321      -3.754  20.066 -26.456  1.00 69.44           N  
ANISOU 1185  N   ASP A 321     8691   9957   7738   -898     14   -228       N  
ATOM   1186  CA  ASP A 321      -3.544  19.735 -27.861  1.00 66.83           C  
ANISOU 1186  CA  ASP A 321     8213   9612   7566   -826     28   -190       C  
ATOM   1187  C   ASP A 321      -3.842  18.267 -28.199  1.00 64.79           C  
ANISOU 1187  C   ASP A 321     7886   9380   7352   -775     38   -110       C  
ATOM   1188  O   ASP A 321      -4.536  17.992 -29.179  1.00 63.40           O  
ANISOU 1188  O   ASP A 321     7644   9188   7257   -704    121   -111       O  
ATOM   1189  CB  ASP A 321      -2.086  20.085 -28.268  1.00 69.34           C  
ANISOU 1189  CB  ASP A 321     8458   9919   7970   -855    -89   -159       C  
ATOM   1190  CG  ASP A 321      -1.896  21.293 -29.180  1.00 83.11           C  
ANISOU 1190  CG  ASP A 321    10160  11616   9801   -838    -52   -216       C  
ATOM   1191  OD1 ASP A 321      -2.727  21.483 -30.102  1.00 83.60           O  
ANISOU 1191  OD1 ASP A 321    10186  11656   9923   -769     58   -246       O  
ATOM   1192  OD2 ASP A 321      -0.860  21.986 -29.041  1.00 89.80           O  
ANISOU 1192  OD2 ASP A 321    11002  12449  10669   -895   -141   -218       O  
ATOM   1193  N   ALA A 322      -3.287  17.333 -27.410  1.00 57.90           N  
ANISOU 1193  N   ALA A 322     7031   8542   6427   -813    -56    -38       N  
ATOM   1194  CA  ALA A 322      -3.311  15.899 -27.680  1.00 55.46           C  
ANISOU 1194  CA  ALA A 322     6655   8250   6167   -773    -73     49       C  
ATOM   1195  C   ALA A 322      -4.572  15.067 -27.459  1.00 54.71           C  
ANISOU 1195  C   ALA A 322     6593   8168   6026   -744     17     61       C  
ATOM   1196  O   ALA A 322      -4.722  14.051 -28.129  1.00 52.03           O  
ANISOU 1196  O   ALA A 322     6179   7824   5767   -693     27    117       O  
ATOM   1197  CB  ALA A 322      -2.108  15.231 -27.023  1.00 56.85           C  
ANISOU 1197  CB  ALA A 322     6820   8451   6332   -820   -219    133       C  
ATOM   1198  N   MET A 323      -5.467  15.484 -26.560  1.00 51.55           N  
ANISOU 1198  N   MET A 323     6303   7779   5506   -775     87     12       N  
ATOM   1199  CA  MET A 323      -6.627  14.699 -26.117  1.00 51.42           C  
ANISOU 1199  CA  MET A 323     6324   7779   5433   -762    171     34       C  
ATOM   1200  C   MET A 323      -7.863  14.277 -27.002  1.00 56.00           C  
ANISOU 1200  C   MET A 323     6838   8342   6099   -691    288     33       C  
ATOM   1201  O   MET A 323      -8.295  13.144 -26.777  1.00 57.42           O  
ANISOU 1201  O   MET A 323     7010   8536   6272   -685    294     97       O  
ATOM   1202  CB  MET A 323      -7.038  15.063 -24.691  1.00 54.71           C  
ANISOU 1202  CB  MET A 323     6888   8220   5681   -825    200      3       C  
ATOM   1203  CG  MET A 323      -6.037  14.519 -23.669  1.00 59.11           C  
ANISOU 1203  CG  MET A 323     7506   8807   6144   -895     63     66       C  
ATOM   1204  SD  MET A 323      -6.677  14.119 -22.031  1.00 64.33           S  
ANISOU 1204  SD  MET A 323     8333   9506   6604   -957     97     83       S  
ATOM   1205  CE  MET A 323      -7.770  12.770 -22.409  1.00 60.11           C  
ANISOU 1205  CE  MET A 323     7727   8980   6134   -899    186    156       C  
ATOM   1206  N   ARG A 324      -8.541  15.056 -27.882  1.00 50.55           N  
ANISOU 1206  N   ARG A 324     6106   7620   5480   -644    378    -28       N  
ATOM   1207  CA  ARG A 324      -8.500  16.360 -28.555  1.00 49.14           C  
ANISOU 1207  CA  ARG A 324     5912   7409   5351   -624    414   -105       C  
ATOM   1208  C   ARG A 324      -8.418  16.165 -30.076  1.00 47.86           C  
ANISOU 1208  C   ARG A 324     5634   7217   5332   -560    414    -91       C  
ATOM   1209  O   ARG A 324      -7.347  16.274 -30.680  1.00 48.09           O  
ANISOU 1209  O   ARG A 324     5613   7236   5423   -555    340    -78       O  
ATOM   1210  CB  ARG A 324      -7.569  17.437 -27.973  1.00 51.48           C  
ANISOU 1210  CB  ARG A 324     6275   7703   5584   -680    354   -154       C  
ATOM   1211  CG  ARG A 324      -8.193  18.829 -28.041  1.00 64.10           C  
ANISOU 1211  CG  ARG A 324     7917   9266   7170   -671    449   -249       C  
ATOM   1212  CD  ARG A 324      -7.219  19.868 -28.550  1.00 78.67           C  
ANISOU 1212  CD  ARG A 324     9742  11082   9066   -685    390   -289       C  
ATOM   1213  NE  ARG A 324      -7.880  20.884 -29.371  1.00 87.98           N  
ANISOU 1213  NE  ARG A 324    10896  12216  10315   -637    484   -352       N  
ATOM   1214  CZ  ARG A 324      -7.252  21.709 -30.206  1.00100.23           C  
ANISOU 1214  CZ  ARG A 324    12401  13735  11948   -627    457   -377       C  
ATOM   1215  NH1 ARG A 324      -5.933  21.648 -30.347  1.00 87.03           N  
ANISOU 1215  NH1 ARG A 324    10694  12068  10306   -661    344   -343       N  
ATOM   1216  NH2 ARG A 324      -7.941  22.596 -30.911  1.00 84.92           N  
ANISOU 1216  NH2 ARG A 324    10445  11753  10068   -583    544   -428       N  
ATOM   1217  N   ASN A 325      -9.574  15.785 -30.667  1.00 39.86           N  
ANISOU 1217  N   ASN A 325     4581   6192   4372   -513    495    -85       N  
ATOM   1218  CA  ASN A 325      -9.769  15.523 -32.096  1.00 36.85           C  
ANISOU 1218  CA  ASN A 325     4109   5780   4113   -453    504    -72       C  
ATOM   1219  C   ASN A 325      -9.729  16.844 -32.841  1.00 36.23           C  
ANISOU 1219  C   ASN A 325     4014   5669   4083   -430    538   -137       C  
ATOM   1220  O   ASN A 325     -10.770  17.473 -33.037  1.00 34.43           O  
ANISOU 1220  O   ASN A 325     3787   5422   3871   -407    624   -177       O  
ATOM   1221  CB  ASN A 325     -11.106  14.783 -32.340  1.00 34.48           C  
ANISOU 1221  CB  ASN A 325     3782   5475   3844   -424    572    -46       C  
ATOM   1222  CG  ASN A 325     -11.328  14.261 -33.744  1.00 46.00           C  
ANISOU 1222  CG  ASN A 325     5164   6902   5413   -372    561    -22       C  
ATOM   1223  OD1 ASN A 325     -10.888  14.827 -34.742  1.00 40.22           O  
ANISOU 1223  OD1 ASN A 325     4397   6143   4742   -342    547    -46       O  
ATOM   1224  ND2 ASN A 325     -12.089  13.199 -33.864  1.00 39.97           N  
ANISOU 1224  ND2 ASN A 325     4378   6135   4673   -363    572     25       N  
ATOM   1225  N   ARG A 326      -8.509  17.257 -33.252  1.00 31.90           N  
ANISOU 1225  N   ARG A 326     3443   5111   3566   -436    470   -140       N  
ATOM   1226  CA  ARG A 326      -8.221  18.515 -33.960  1.00 30.51           C  
ANISOU 1226  CA  ARG A 326     3252   4902   3438   -422    487   -193       C  
ATOM   1227  C   ARG A 326      -8.970  18.639 -35.268  1.00 30.21           C  
ANISOU 1227  C   ARG A 326     3158   4830   3490   -360    542   -200       C  
ATOM   1228  O   ARG A 326      -9.522  19.698 -35.544  1.00 29.59           O  
ANISOU 1228  O   ARG A 326     3088   4724   3431   -346    600   -251       O  
ATOM   1229  CB  ARG A 326      -6.709  18.698 -34.177  1.00 30.55           C  
ANISOU 1229  CB  ARG A 326     3230   4906   3472   -443    399   -174       C  
ATOM   1230  CG  ARG A 326      -6.064  19.697 -33.224  1.00 38.88           C  
ANISOU 1230  CG  ARG A 326     4348   5966   4460   -507    363   -215       C  
ATOM   1231  CD  ARG A 326      -4.559  19.765 -33.423  1.00 43.96           C  
ANISOU 1231  CD  ARG A 326     4947   6610   5148   -533    266   -181       C  
ATOM   1232  NE  ARG A 326      -3.969  18.441 -33.230  1.00 48.51           N  
ANISOU 1232  NE  ARG A 326     5486   7215   5731   -533    197   -102       N  
ATOM   1233  CZ  ARG A 326      -3.266  18.078 -32.169  1.00 49.81           C  
ANISOU 1233  CZ  ARG A 326     5682   7410   5835   -590    109    -67       C  
ATOM   1234  NH1 ARG A 326      -2.964  18.962 -31.232  1.00 43.61           N  
ANISOU 1234  NH1 ARG A 326     4970   6628   4971   -658     72   -108       N  
ATOM   1235  NH2 ARG A 326      -2.814  16.843 -32.061  1.00 27.11           N  
ANISOU 1235  NH2 ARG A 326     2768   4555   2979   -581     52     10       N  
ATOM   1236  N   GLY A 327      -9.023  17.550 -36.029  1.00 25.80           N  
ANISOU 1236  N   GLY A 327     2550   4269   2983   -326    522   -148       N  
ATOM   1237  CA  GLY A 327      -9.735  17.470 -37.305  1.00 24.58           C  
ANISOU 1237  CA  GLY A 327     2352   4083   2906   -272    557   -146       C  
ATOM   1238  C   GLY A 327     -11.193  17.887 -37.231  1.00 28.91           C  
ANISOU 1238  C   GLY A 327     2906   4620   3459   -259    634   -173       C  
ATOM   1239  O   GLY A 327     -11.689  18.583 -38.126  1.00 28.60           O  
ANISOU 1239  O   GLY A 327     2843   4548   3476   -225    667   -196       O  
ATOM   1240  N   ALA A 328     -11.891  17.453 -36.164  1.00 25.24           N  
ANISOU 1240  N   ALA A 328     2471   4181   2938   -284    665   -164       N  
ATOM   1241  CA  ALA A 328     -13.286  17.774 -35.947  1.00 25.50           C  
ANISOU 1241  CA  ALA A 328     2501   4206   2980   -272    749   -181       C  
ATOM   1242  C   ALA A 328     -13.474  19.134 -35.324  1.00 29.55           C  
ANISOU 1242  C   ALA A 328     3059   4711   3458   -282    813   -246       C  
ATOM   1243  O   ALA A 328     -14.444  19.800 -35.665  1.00 30.41           O  
ANISOU 1243  O   ALA A 328     3146   4793   3616   -251    882   -268       O  
ATOM   1244  CB  ALA A 328     -13.957  16.707 -35.080  1.00 27.01           C  
ANISOU 1244  CB  ALA A 328     2703   4428   3131   -294    767   -138       C  
ATOM   1245  N   ILE A 329     -12.587  19.550 -34.399  1.00 26.58           N  
ANISOU 1245  N   ILE A 329     2749   4352   2999   -326    788   -274       N  
ATOM   1246  CA  ILE A 329     -12.774  20.822 -33.698  1.00 27.82           C  
ANISOU 1246  CA  ILE A 329     2968   4492   3108   -341    851   -343       C  
ATOM   1247  C   ILE A 329     -12.124  22.069 -34.342  1.00 33.33           C  
ANISOU 1247  C   ILE A 329     3666   5150   3848   -333    836   -392       C  
ATOM   1248  O   ILE A 329     -12.690  23.157 -34.220  1.00 34.49           O  
ANISOU 1248  O   ILE A 329     3840   5263   4001   -319    909   -446       O  
ATOM   1249  CB  ILE A 329     -12.643  20.739 -32.131  1.00 31.97           C  
ANISOU 1249  CB  ILE A 329     3593   5051   3505   -396    863   -360       C  
ATOM   1250  CG1 ILE A 329     -11.226  21.107 -31.624  1.00 33.03           C  
ANISOU 1250  CG1 ILE A 329     3782   5193   3573   -451    771   -379       C  
ATOM   1251  CG2 ILE A 329     -13.180  19.395 -31.534  1.00 30.67           C  
ANISOU 1251  CG2 ILE A 329     3426   4926   3300   -407    870   -298       C  
ATOM   1252  CD1 ILE A 329     -11.133  21.287 -30.103  1.00 42.71           C  
ANISOU 1252  CD1 ILE A 329     5127   6440   4660   -511    781   -408       C  
ATOM   1253  N   ASP A 330     -10.969  21.921 -35.024  1.00 28.75           N  
ANISOU 1253  N   ASP A 330     3053   4570   3300   -339    749   -369       N  
ATOM   1254  CA  ASP A 330     -10.292  23.056 -35.656  1.00 28.76           C  
ANISOU 1254  CA  ASP A 330     3048   4533   3345   -337    733   -405       C  
ATOM   1255  C   ASP A 330     -10.957  23.493 -36.957  1.00 31.32           C  
ANISOU 1255  C   ASP A 330     3315   4817   3767   -277    775   -405       C  
ATOM   1256  O   ASP A 330     -11.195  22.674 -37.851  1.00 30.19           O  
ANISOU 1256  O   ASP A 330     3116   4678   3676   -243    758   -357       O  
ATOM   1257  CB  ASP A 330      -8.803  22.749 -35.980  1.00 30.46           C  
ANISOU 1257  CB  ASP A 330     3237   4761   3575   -362    635   -371       C  
ATOM   1258  CG  ASP A 330      -7.805  22.694 -34.833  1.00 38.00           C  
ANISOU 1258  CG  ASP A 330     4245   5744   4450   -430    566   -372       C  
ATOM   1259  OD1 ASP A 330      -8.227  22.872 -33.661  1.00 35.26           O  
ANISOU 1259  OD1 ASP A 330     3976   5409   4012   -465    592   -405       O  
ATOM   1260  OD2 ASP A 330      -6.581  22.513 -35.116  1.00 44.70           O  
ANISOU 1260  OD2 ASP A 330     5056   6599   5328   -448    486   -338       O  
ATOM   1261  N   MET A 331     -11.192  24.801 -37.082  1.00 26.82           N  
ANISOU 1261  N   MET A 331     2767   4204   3220   -268    822   -457       N  
ATOM   1262  CA  MET A 331     -11.676  25.409 -38.314  1.00 24.73           C  
ANISOU 1262  CA  MET A 331     2454   3895   3047   -217    850   -456       C  
ATOM   1263  C   MET A 331     -10.594  26.384 -38.806  1.00 26.49           C  
ANISOU 1263  C   MET A 331     2684   4085   3296   -233    816   -476       C  
ATOM   1264  O   MET A 331      -9.798  26.868 -38.002  1.00 26.56           O  
ANISOU 1264  O   MET A 331     2742   4095   3254   -283    790   -509       O  
ATOM   1265  CB  MET A 331     -13.085  26.017 -38.186  1.00 27.08           C  
ANISOU 1265  CB  MET A 331     2753   4162   3373   -181    944   -483       C  
ATOM   1266  CG  MET A 331     -13.169  27.262 -37.331  1.00 31.48           C  
ANISOU 1266  CG  MET A 331     3381   4685   3894   -198   1002   -554       C  
ATOM   1267  SD  MET A 331     -14.807  28.025 -37.460  1.00 36.15           S  
ANISOU 1267  SD  MET A 331     3952   5229   4555   -136   1121   -575       S  
ATOM   1268  CE  MET A 331     -14.596  29.445 -36.422  1.00 33.99           C  
ANISOU 1268  CE  MET A 331     3783   4906   4225   -161   1184   -667       C  
ATOM   1269  N   PHE A 332     -10.489  26.569 -40.124  1.00 20.92           N  
ANISOU 1269  N   PHE A 332     1930   3353   2665   -196    805   -450       N  
ATOM   1270  CA  PHE A 332      -9.484  27.428 -40.741  1.00 20.82           C  
ANISOU 1270  CA  PHE A 332     1913   3308   2689   -207    779   -456       C  
ATOM   1271  C   PHE A 332      -9.985  27.880 -42.117  1.00 23.05           C  
ANISOU 1271  C   PHE A 332     2161   3549   3048   -153    803   -437       C  
ATOM   1272  O   PHE A 332     -10.894  27.264 -42.684  1.00 21.60           O  
ANISOU 1272  O   PHE A 332     1949   3370   2888   -113    816   -408       O  
ATOM   1273  CB  PHE A 332      -8.124  26.659 -40.881  1.00 22.93           C  
ANISOU 1273  CB  PHE A 332     2155   3610   2948   -234    705   -413       C  
ATOM   1274  CG  PHE A 332      -8.270  25.252 -41.437  1.00 24.88           C  
ANISOU 1274  CG  PHE A 332     2363   3890   3202   -203    684   -358       C  
ATOM   1275  CD1 PHE A 332      -8.290  25.028 -42.811  1.00 27.47           C  
ANISOU 1275  CD1 PHE A 332     2656   4198   3583   -157    686   -323       C  
ATOM   1276  CD2 PHE A 332      -8.483  24.168 -40.588  1.00 27.43           C  
ANISOU 1276  CD2 PHE A 332     2694   4256   3471   -218    666   -342       C  
ATOM   1277  CE1 PHE A 332      -8.521  23.753 -43.326  1.00 28.16           C  
ANISOU 1277  CE1 PHE A 332     2724   4306   3672   -129    668   -279       C  
ATOM   1278  CE2 PHE A 332      -8.690  22.886 -41.105  1.00 30.14           C  
ANISOU 1278  CE2 PHE A 332     3008   4619   3825   -189    648   -293       C  
ATOM   1279  CZ  PHE A 332      -8.698  22.686 -42.472  1.00 27.98           C  
ANISOU 1279  CZ  PHE A 332     2705   4322   3606   -145    648   -265       C  
ATOM   1280  N   GLU A 333      -9.329  28.901 -42.692  1.00 19.12           N  
ANISOU 1280  N   GLU A 333     1666   3010   2590   -159    800   -447       N  
ATOM   1281  CA  GLU A 333      -9.643  29.397 -44.031  1.00 16.74           C  
ANISOU 1281  CA  GLU A 333     1340   2667   2355   -114    817   -423       C  
ATOM   1282  C   GLU A 333      -9.121  28.375 -45.050  1.00 19.99           C  
ANISOU 1282  C   GLU A 333     1718   3103   2775    -93    779   -364       C  
ATOM   1283  O   GLU A 333      -7.960  27.994 -45.010  1.00 18.82           O  
ANISOU 1283  O   GLU A 333     1558   2977   2615   -119    745   -345       O  
ATOM   1284  CB  GLU A 333      -9.099  30.807 -44.258  1.00 17.83           C  
ANISOU 1284  CB  GLU A 333     1496   2748   2529   -129    830   -449       C  
ATOM   1285  CG  GLU A 333      -9.225  31.671 -43.012  1.00 26.10           C  
ANISOU 1285  CG  GLU A 333     2595   3773   3549   -165    856   -515       C  
ATOM   1286  CD  GLU A 333      -8.785  33.115 -43.114  1.00 46.64           C  
ANISOU 1286  CD  GLU A 333     5226   6309   6187   -186    869   -548       C  
ATOM   1287  OE1 GLU A 333      -7.602  33.411 -42.821  1.00 49.06           O  
ANISOU 1287  OE1 GLU A 333     5543   6615   6484   -241    827   -554       O  
ATOM   1288  OE2 GLU A 333      -9.657  33.967 -43.392  1.00 34.59           O  
ANISOU 1288  OE2 GLU A 333     3711   4727   4704   -150    920   -568       O  
ATOM   1289  N   PRO A 334     -10.018  27.795 -45.866  1.00 16.78           N  
ANISOU 1289  N   PRO A 334     1295   2694   2386    -49    782   -334       N  
ATOM   1290  CA  PRO A 334      -9.596  26.744 -46.808  1.00 15.84           C  
ANISOU 1290  CA  PRO A 334     1163   2593   2263    -29    750   -285       C  
ATOM   1291  C   PRO A 334      -8.543  27.118 -47.848  1.00 19.82           C  
ANISOU 1291  C   PRO A 334     1666   3074   2790    -22    747   -260       C  
ATOM   1292  O   PRO A 334      -7.835  26.221 -48.337  1.00 20.49           O  
ANISOU 1292  O   PRO A 334     1745   3178   2864    -13    730   -226       O  
ATOM   1293  CB  PRO A 334     -10.902  26.362 -47.490  1.00 17.28           C  
ANISOU 1293  CB  PRO A 334     1341   2761   2464     10    750   -265       C  
ATOM   1294  CG  PRO A 334     -11.804  27.573 -47.308  1.00 20.61           C  
ANISOU 1294  CG  PRO A 334     1761   3144   2924     21    787   -293       C  
ATOM   1295  CD  PRO A 334     -11.473  28.045 -45.955  1.00 17.00           C  
ANISOU 1295  CD  PRO A 334     1317   2699   2441    -16    812   -340       C  
ATOM   1296  N   GLY A 335      -8.459  28.405 -48.195  1.00 14.18           N  
ANISOU 1296  N   GLY A 335      961   2316   2112    -22    771   -272       N  
ATOM   1297  CA  GLY A 335      -7.521  28.909 -49.197  1.00 12.85           C  
ANISOU 1297  CA  GLY A 335      808   2110   1966    -19    765   -243       C  
ATOM   1298  C   GLY A 335      -7.810  28.316 -50.565  1.00 16.67           C  
ANISOU 1298  C   GLY A 335     1290   2594   2449     28    777   -201       C  
ATOM   1299  O   GLY A 335      -8.972  28.113 -50.920  1.00 15.63           O  
ANISOU 1299  O   GLY A 335     1172   2453   2316     55    767   -197       O  
ATOM   1300  N   SER A 336      -6.759  27.947 -51.308  1.00 14.75           N  
ANISOU 1300  N   SER A 336     1047   2354   2203     36    785   -166       N  
ATOM   1301  CA  SER A 336      -6.886  27.315 -52.633  1.00 13.51           C  
ANISOU 1301  CA  SER A 336      924   2183   2025     77    788   -128       C  
ATOM   1302  C   SER A 336      -7.656  25.987 -52.664  1.00 13.34           C  
ANISOU 1302  C   SER A 336      919   2185   1966     97    755   -124       C  
ATOM   1303  O   SER A 336      -8.129  25.598 -53.728  1.00 11.99           O  
ANISOU 1303  O   SER A 336      839   1957   1761    117    699    -97       O  
ATOM   1304  CB  SER A 336      -5.525  27.183 -53.300  1.00 17.88           C  
ANISOU 1304  CB  SER A 336     1475   2735   2585     83    821    -93       C  
ATOM   1305  OG  SER A 336      -4.885  28.440 -53.402  1.00 25.35           O  
ANISOU 1305  OG  SER A 336     2405   3654   3573     62    849    -89       O  
ATOM   1306  N   THR A 337      -7.871  25.333 -51.505  1.00 10.71           N  
ANISOU 1306  N   THR A 337      719   1774   1578     52    591   -133       N  
ATOM   1307  CA  THR A 337      -8.664  24.098 -51.483  1.00 10.69           C  
ANISOU 1307  CA  THR A 337      717   1796   1550     65    570   -127       C  
ATOM   1308  C   THR A 337     -10.142  24.372 -51.908  1.00 17.26           C  
ANISOU 1308  C   THR A 337     1414   2709   2433    103    682   -139       C  
ATOM   1309  O   THR A 337     -10.832  23.443 -52.337  1.00 14.49           O  
ANISOU 1309  O   THR A 337     1084   2358   2065    116    648   -123       O  
ATOM   1310  CB  THR A 337      -8.527  23.343 -50.141  1.00 17.45           C  
ANISOU 1310  CB  THR A 337     1395   2804   2433     61    686   -153       C  
ATOM   1311  OG1 THR A 337      -8.842  24.213 -49.053  1.00 21.11           O  
ANISOU 1311  OG1 THR A 337     1837   3277   2908     31    697   -187       O  
ATOM   1312  CG2 THR A 337      -7.148  22.704 -49.938  1.00 12.48           C  
ANISOU 1312  CG2 THR A 337      749   2195   1796     56    688   -135       C  
ATOM   1313  N   MET A 338     -10.595  25.675 -51.820  1.00 17.76           N  
ANISOU 1313  N   MET A 338     1466   2749   2534    101    700   -154       N  
ATOM   1314  CA  MET A 338     -11.932  26.165 -52.209  1.00 17.89           C  
ANISOU 1314  CA  MET A 338     1481   2735   2581    118    685   -146       C  
ATOM   1315  C   MET A 338     -12.062  26.331 -53.717  1.00 19.19           C  
ANISOU 1315  C   MET A 338     1690   2861   2740    144    663   -110       C  
ATOM   1316  O   MET A 338     -13.162  26.214 -54.242  1.00 20.33           O  
ANISOU 1316  O   MET A 338     1840   2986   2898    158    624    -88       O  
ATOM   1317  CB  MET A 338     -12.244  27.528 -51.562  1.00 20.48           C  
ANISOU 1317  CB  MET A 338     1784   3043   2956    111    721   -174       C  
ATOM   1318  CG  MET A 338     -13.126  27.491 -50.337  1.00 25.39           C  
ANISOU 1318  CG  MET A 338     2371   3682   3595    101    735   -202       C  
ATOM   1319  SD  MET A 338     -14.455  26.251 -50.130  1.00 29.74           S  
ANISOU 1319  SD  MET A 338     2895   4257   4148    108    701   -180       S  
ATOM   1320  CE  MET A 338     -13.562  25.018 -49.390  1.00 24.77           C  
ANISOU 1320  CE  MET A 338     2274   3680   3457     80    693   -189       C  
ATOM   1321  N   LYS A 339     -10.971  26.692 -54.395  1.00 14.41           N  
ANISOU 1321  N   LYS A 339     1115   2241   2117    149    690    -98       N  
ATOM   1322  CA  LYS A 339     -10.992  26.928 -55.841  1.00 14.39           C  
ANISOU 1322  CA  LYS A 339     1171   2201   2097    173    679    -62       C  
ATOM   1323  C   LYS A 339     -11.807  25.916 -56.665  1.00 18.44           C  
ANISOU 1323  C   LYS A 339     1731   2705   2571    187    621    -38       C  
ATOM   1324  O   LYS A 339     -12.646  26.390 -57.437  1.00 18.21           O  
ANISOU 1324  O   LYS A 339     1725   2642   2552    198    584    -13       O  
ATOM   1325  CB  LYS A 339      -9.610  27.224 -56.424  1.00 15.58           C  
ANISOU 1325  CB  LYS A 339     1348   2343   2229    176    728    -49       C  
ATOM   1326  CG  LYS A 339      -9.031  28.533 -55.908  1.00 11.27           C  
ANISOU 1326  CG  LYS A 339      841   1726   1714    139    694    -52       C  
ATOM   1327  CD  LYS A 339      -7.553  28.741 -56.303  1.00  8.00           C  
ANISOU 1327  CD  LYS A 339      679   1116   1244     83    486     -4       C  
ATOM   1328  CE  LYS A 339      -7.059  29.974 -55.580  1.00 10.57           C  
ANISOU 1328  CE  LYS A 339      790   1564   1660     93    696    -45       C  
ATOM   1329  NZ  LYS A 339      -5.653  30.326 -55.839  1.00 18.48           N  
ANISOU 1329  NZ  LYS A 339     1625   2679   2716    107    892    -38       N  
ATOM   1330  N   PRO A 340     -11.682  24.560 -56.483  1.00 15.80           N  
ANISOU 1330  N   PRO A 340     1410   2396   2198    184    602    -44       N  
ATOM   1331  CA  PRO A 340     -12.515  23.640 -57.285  1.00 15.46           C  
ANISOU 1331  CA  PRO A 340     1420   2334   2119    190    536    -24       C  
ATOM   1332  C   PRO A 340     -14.025  23.794 -57.103  1.00 17.39           C  
ANISOU 1332  C   PRO A 340     1627   2571   2411    181    476    -11       C  
ATOM   1333  O   PRO A 340     -14.764  23.487 -58.031  1.00 15.74           O  
ANISOU 1333  O   PRO A 340     1465   2332   2184    183    410     17       O  
ATOM   1334  CB  PRO A 340     -11.990  22.246 -56.911  1.00 16.79           C  
ANISOU 1334  CB  PRO A 340     1600   2527   2250    187    538    -36       C  
ATOM   1335  CG  PRO A 340     -10.622  22.494 -56.351  1.00 21.21           C  
ANISOU 1335  CG  PRO A 340     2131   3111   2815    188    608    -51       C  
ATOM   1336  CD  PRO A 340     -10.742  23.794 -55.633  1.00 16.67           C  
ANISOU 1336  CD  PRO A 340     1494   2544   2294    174    632    -64       C  
ATOM   1337  N   PHE A 341     -14.481  24.291 -55.932  1.00 15.94           N  
ANISOU 1337  N   PHE A 341     1361   2408   2287    170    498    -30       N  
ATOM   1338  CA  PHE A 341     -15.920  24.536 -55.660  1.00 15.78           C  
ANISOU 1338  CA  PHE A 341     1287   2379   2331    168    459    -14       C  
ATOM   1339  C   PHE A 341     -16.423  25.827 -56.329  1.00 20.68           C  
ANISOU 1339  C   PHE A 341     1904   2957   2997    186    451     11       C  
ATOM   1340  O   PHE A 341     -17.555  25.862 -56.812  1.00 22.09           O  
ANISOU 1340  O   PHE A 341     2068   3111   3214    190    389     47       O  
ATOM   1341  CB  PHE A 341     -16.248  24.490 -54.162  1.00 16.31           C  
ANISOU 1341  CB  PHE A 341     1277   2481   2438    154    499    -42       C  
ATOM   1342  CG  PHE A 341     -15.715  23.254 -53.476  1.00 16.41           C  
ANISOU 1342  CG  PHE A 341     1295   2535   2407    135    503    -59       C  
ATOM   1343  CD1 PHE A 341     -16.421  22.050 -53.524  1.00 18.95           C  
ANISOU 1343  CD1 PHE A 341     1616   2862   2723    122    449    -39       C  
ATOM   1344  CD2 PHE A 341     -14.516  23.294 -52.765  1.00 15.05           C  
ANISOU 1344  CD2 PHE A 341     1124   2391   2205    126    555    -90       C  
ATOM   1345  CE1 PHE A 341     -15.910  20.895 -52.918  1.00 18.75           C  
ANISOU 1345  CE1 PHE A 341     1598   2866   2658    105    452    -50       C  
ATOM   1346  CE2 PHE A 341     -14.008  22.139 -52.157  1.00 17.78           C  
ANISOU 1346  CE2 PHE A 341     1472   2770   2514    111    553    -97       C  
ATOM   1347  CZ  PHE A 341     -14.706  20.946 -52.240  1.00 16.47           C  
ANISOU 1347  CZ  PHE A 341     1312   2607   2341    103    504    -78       C  
ATOM   1348  N   THR A 342     -15.565  26.865 -56.379  1.00 16.21           N  
ANISOU 1348  N   THR A 342     1350   2378   2430    195    508     -4       N  
ATOM   1349  CA  THR A 342     -15.801  28.156 -57.046  1.00 16.00           C  
ANISOU 1349  CA  THR A 342     1331   2305   2442    213    509     21       C  
ATOM   1350  C   THR A 342     -16.051  27.894 -58.544  1.00 17.92           C  
ANISOU 1350  C   THR A 342     1650   2517   2641    221    440     70       C  
ATOM   1351  O   THR A 342     -17.022  28.411 -59.114  1.00 16.41           O  
ANISOU 1351  O   THR A 342     1452   2291   2493    232    386    110       O  
ATOM   1352  CB  THR A 342     -14.565  29.098 -56.810  1.00 20.00           C  
ANISOU 1352  CB  THR A 342     1848   2807   2945    211    584     -5       C  
ATOM   1353  OG1 THR A 342     -14.464  29.482 -55.429  1.00 15.15           O  
ANISOU 1353  OG1 THR A 342     1173   2211   2370    199    636    -50       O  
ATOM   1354  CG2 THR A 342     -14.575  30.325 -57.682  1.00 13.67           C  
ANISOU 1354  CG2 THR A 342     1073   1952   2169    228    587     27       C  
ATOM   1355  N   VAL A 343     -15.151  27.090 -59.166  1.00 14.17           N  
ANISOU 1355  N   VAL A 343     1253   2052   2079    218    443     67       N  
ATOM   1356  CA  VAL A 343     -15.176  26.675 -60.577  1.00 14.34           C  
ANISOU 1356  CA  VAL A 343     1376   2044   2029    223    388    103       C  
ATOM   1357  C   VAL A 343     -16.405  25.789 -60.834  1.00 19.98           C  
ANISOU 1357  C   VAL A 343     2094   2752   2746    209    287    125       C  
ATOM   1358  O   VAL A 343     -17.075  25.967 -61.847  1.00 21.01           O  
ANISOU 1358  O   VAL A 343     2275   2846   2863    210    211    168       O  
ATOM   1359  CB  VAL A 343     -13.818  26.020 -61.013  1.00 17.57           C  
ANISOU 1359  CB  VAL A 343     1862   2463   2349    228    442     87       C  
ATOM   1360  CG1 VAL A 343     -13.959  25.172 -62.285  1.00 17.45           C  
ANISOU 1360  CG1 VAL A 343     1966   2420   2243    230    384    110       C  
ATOM   1361  CG2 VAL A 343     -12.732  27.075 -61.180  1.00 16.62           C  
ANISOU 1361  CG2 VAL A 343     1748   2334   2233    238    524     89       C  
ATOM   1362  N   ALA A 344     -16.735  24.882 -59.907  1.00 18.77           N  
ANISOU 1362  N   ALA A 344     1886   2632   2614    194    279    102       N  
ATOM   1363  CA  ALA A 344     -17.959  24.056 -60.021  1.00 19.88           C  
ANISOU 1363  CA  ALA A 344     2012   2766   2776    174    182    127       C  
ATOM   1364  C   ALA A 344     -19.219  24.968 -60.022  1.00 22.28           C  
ANISOU 1364  C   ALA A 344     2241   3047   3179    179    134    169       C  
ATOM   1365  O   ALA A 344     -20.127  24.706 -60.809  1.00 22.59           O  
ANISOU 1365  O   ALA A 344     2303   3057   3224    166     31    214       O  
ATOM   1366  CB  ALA A 344     -18.041  23.044 -58.885  1.00 20.28           C  
ANISOU 1366  CB  ALA A 344     2005   2857   2844    157    199     98       C  
ATOM   1367  N   ALA A 345     -19.237  26.069 -59.206  1.00 17.17           N  
ANISOU 1367  N   ALA A 345     1511   2405   2607    198    206    156       N  
ATOM   1368  CA  ALA A 345     -20.364  27.042 -59.196  1.00 16.94           C  
ANISOU 1368  CA  ALA A 345     1406   2346   2684    213    179    196       C  
ATOM   1369  C   ALA A 345     -20.490  27.816 -60.521  1.00 22.01           C  
ANISOU 1369  C   ALA A 345     2112   2938   3314    226    121    247       C  
ATOM   1370  O   ALA A 345     -21.597  28.079 -60.975  1.00 24.12           O  
ANISOU 1370  O   ALA A 345     2343   3174   3646    229     40    303       O  
ATOM   1371  CB  ALA A 345     -20.241  28.019 -58.027  1.00 16.83           C  
ANISOU 1371  CB  ALA A 345     1312   2341   2742    233    282    161       C  
ATOM   1372  N   ALA A 346     -19.357  28.143 -61.144  1.00 18.89           N  
ANISOU 1372  N   ALA A 346     1808   2535   2836    232    161    234       N  
ATOM   1373  CA  ALA A 346     -19.262  28.867 -62.408  1.00 19.29           C  
ANISOU 1373  CA  ALA A 346     1937   2539   2853    243    122    281       C  
ATOM   1374  C   ALA A 346     -19.690  27.981 -63.560  1.00 23.52           C  
ANISOU 1374  C   ALA A 346     2567   3058   3311    222      7    319       C  
ATOM   1375  O   ALA A 346     -20.273  28.489 -64.515  1.00 24.90           O  
ANISOU 1375  O   ALA A 346     2780   3191   3489    224    -74    378       O  
ATOM   1376  CB  ALA A 346     -17.827  29.351 -62.624  1.00 19.76           C  
ANISOU 1376  CB  ALA A 346     2063   2600   2845    251    215    254       C  
ATOM   1377  N   LEU A 347     -19.382  26.664 -63.491  1.00 19.23           N  
ANISOU 1377  N   LEU A 347     2070   2540   2695    201     -5    287       N  
ATOM   1378  CA  LEU A 347     -19.762  25.708 -64.531  1.00 18.95           C  
ANISOU 1378  CA  LEU A 347     2140   2483   2576    176   -114    312       C  
ATOM   1379  C   LEU A 347     -21.278  25.501 -64.515  1.00 24.63           C  
ANISOU 1379  C   LEU A 347     2788   3187   3382    153   -239    362       C  
ATOM   1380  O   LEU A 347     -21.908  25.556 -65.577  1.00 25.12           O  
ANISOU 1380  O   LEU A 347     2914   3210   3419    138   -354    416       O  
ATOM   1381  CB  LEU A 347     -18.994  24.366 -64.425  1.00 17.62           C  
ANISOU 1381  CB  LEU A 347     2043   2337   2315    163    -84    261       C  
ATOM   1382  CG  LEU A 347     -17.479  24.353 -64.831  1.00 20.61           C  
ANISOU 1382  CG  LEU A 347     2522   2719   2590    184     19    228       C  
ATOM   1383  CD1 LEU A 347     -16.774  23.055 -64.382  1.00 19.93           C  
ANISOU 1383  CD1 LEU A 347     2461   2658   2452    180     65    177       C  
ATOM   1384  CD2 LEU A 347     -17.287  24.512 -66.310  1.00 20.31           C  
ANISOU 1384  CD2 LEU A 347     2635   2637   2446    186    -22    260       C  
ATOM   1385  N   GLU A 348     -21.873  25.333 -63.315  1.00 21.24           N  
ANISOU 1385  N   GLU A 348     2222   2787   3059    151   -214    349       N  
ATOM   1386  CA  GLU A 348     -23.317  25.137 -63.208  1.00 22.42           C  
ANISOU 1386  CA  GLU A 348     2281   2926   3313    132   -319    402       C  
ATOM   1387  C   GLU A 348     -24.198  26.321 -63.587  1.00 27.33           C  
ANISOU 1387  C   GLU A 348     2838   3511   4036    151   -369    470       C  
ATOM   1388  O   GLU A 348     -25.340  26.108 -63.969  1.00 28.59           O  
ANISOU 1388  O   GLU A 348     2955   3647   4260    130   -491    533       O  
ATOM   1389  CB  GLU A 348     -23.747  24.431 -61.916  1.00 24.11           C  
ANISOU 1389  CB  GLU A 348     2380   3179   3602    120   -280    377       C  
ATOM   1390  CG  GLU A 348     -23.500  25.168 -60.610  1.00 39.87           C  
ANISOU 1390  CG  GLU A 348     4269   5206   5673    152   -144    340       C  
ATOM   1391  CD  GLU A 348     -24.536  24.883 -59.531  1.00 55.96           C  
ANISOU 1391  CD  GLU A 348     6167   7264   7829    146   -133    353       C  
ATOM   1392  OE1 GLU A 348     -24.957  23.709 -59.378  1.00 36.08           O  
ANISOU 1392  OE1 GLU A 348     3640   4761   5308    109   -189    361       O  
ATOM   1393  OE2 GLU A 348     -24.928  25.849 -58.834  1.00 43.90           O  
ANISOU 1393  OE2 GLU A 348     4543   5736   6401    178    -62    356       O  
ATOM   1394  N   SER A 349     -23.648  27.552 -63.558  1.00 24.16           N  
ANISOU 1394  N   SER A 349     2434   3098   3649    189   -285    463       N  
ATOM   1395  CA  SER A 349     -24.338  28.780 -63.938  1.00 24.62           C  
ANISOU 1395  CA  SER A 349     2440   3113   3800    216   -319    527       C  
ATOM   1396  C   SER A 349     -24.637  28.817 -65.442  1.00 33.95           C  
ANISOU 1396  C   SER A 349     3732   4251   4918    197   -458    595       C  
ATOM   1397  O   SER A 349     -25.455  29.630 -65.877  1.00 35.98           O  
ANISOU 1397  O   SER A 349     3942   4468   5261    211   -529    667       O  
ATOM   1398  CB  SER A 349     -23.504  29.996 -63.560  1.00 24.90           C  
ANISOU 1398  CB  SER A 349     2470   3143   3850    255   -191    494       C  
ATOM   1399  OG  SER A 349     -22.359  30.111 -64.390  1.00 28.91           O  
ANISOU 1399  OG  SER A 349     3115   3643   4228    252   -167    479       O  
ATOM   1400  N   GLY A 350     -23.945  27.973 -66.216  1.00 31.08           N  
ANISOU 1400  N   GLY A 350     3517   3891   4401    169   -490    572       N  
ATOM   1401  CA  GLY A 350     -24.075  27.907 -67.664  1.00 31.15           C  
ANISOU 1401  CA  GLY A 350     3667   3859   4311    146   -613    625       C  
ATOM   1402  C   GLY A 350     -23.443  29.101 -68.349  1.00 35.25           C  
ANISOU 1402  C   GLY A 350     4257   4349   4789    175   -567    649       C  
ATOM   1403  O   GLY A 350     -23.656  29.319 -69.544  1.00 37.50           O  
ANISOU 1403  O   GLY A 350     4651   4594   5003    161   -668    707       O  
ATOM   1404  N   GLN A 351     -22.683  29.898 -67.593  1.00 28.67           N  
ANISOU 1404  N   GLN A 351     3366   3531   3997    212   -420    607       N  
ATOM   1405  CA  GLN A 351     -21.977  31.066 -68.109  1.00 27.51           C  
ANISOU 1405  CA  GLN A 351     3274   3355   3822    238   -357    626       C  
ATOM   1406  C   GLN A 351     -20.615  30.616 -68.603  1.00 31.92           C  
ANISOU 1406  C   GLN A 351     3976   3929   4223    231   -279    580       C  
ATOM   1407  O   GLN A 351     -19.968  31.354 -69.352  1.00 32.99           O  
ANISOU 1407  O   GLN A 351     4199   4038   4297    243   -243    605       O  
ATOM   1408  CB  GLN A 351     -21.752  32.107 -66.994  1.00 27.53           C  
ANISOU 1408  CB  GLN A 351     3150   3363   3948    275   -234    597       C  
ATOM   1409  CG  GLN A 351     -22.956  32.958 -66.619  1.00 32.54           C  
ANISOU 1409  CG  GLN A 351     3651   3965   4747    299   -278    650       C  
ATOM   1410  CD  GLN A 351     -22.564  34.074 -65.684  1.00 44.48           C  
ANISOU 1410  CD  GLN A 351     5079   5467   6353    336   -147    615       C  
ATOM   1411  OE1 GLN A 351     -21.590  34.805 -65.909  1.00 38.22           O  
ANISOU 1411  OE1 GLN A 351     4347   4658   5515    345    -70    601       O  
ATOM   1412  NE2 GLN A 351     -23.339  34.257 -64.627  1.00 37.05           N  
ANISOU 1412  NE2 GLN A 351     4000   4531   5547    356   -118    603       N  
ATOM   1413  N   TYR A 352     -20.135  29.439 -68.120  1.00 26.90           N  
ANISOU 1413  N   TYR A 352     3355   3335   3532    217   -239    515       N  
ATOM   1414  CA  TYR A 352     -18.794  28.958 -68.449  1.00 24.79           C  
ANISOU 1414  CA  TYR A 352     3203   3083   3135    219   -146    468       C  
ATOM   1415  C   TYR A 352     -18.713  27.509 -68.805  1.00 27.54           C  
ANISOU 1415  C   TYR A 352     3648   3440   3376    194   -193    439       C  
ATOM   1416  O   TYR A 352     -19.555  26.694 -68.425  1.00 28.46           O  
ANISOU 1416  O   TYR A 352     3716   3566   3531    171   -276    435       O  
ATOM   1417  CB  TYR A 352     -17.827  29.211 -67.289  1.00 23.77           C  
ANISOU 1417  CB  TYR A 352     2985   2992   3055    238      2    407       C  
ATOM   1418  CG  TYR A 352     -17.641  30.661 -66.924  1.00 24.77           C  
ANISOU 1418  CG  TYR A 352     3037   3103   3272    261     69    422       C  
ATOM   1419  CD1 TYR A 352     -18.441  31.263 -65.956  1.00 25.68           C  
ANISOU 1419  CD1 TYR A 352     3014   3218   3526    271     65    422       C  
ATOM   1420  CD2 TYR A 352     -16.605  31.410 -67.475  1.00 25.25           C  
ANISOU 1420  CD2 TYR A 352     3166   3145   3281    272    149    433       C  
ATOM   1421  CE1 TYR A 352     -18.256  32.585 -65.591  1.00 25.70           C  
ANISOU 1421  CE1 TYR A 352     2958   3196   3611    292    130    429       C  
ATOM   1422  CE2 TYR A 352     -16.380  32.723 -67.082  1.00 25.57           C  
ANISOU 1422  CE2 TYR A 352     3141   3165   3410    288    211    443       C  
ATOM   1423  CZ  TYR A 352     -17.218  33.310 -66.150  1.00 33.09           C  
ANISOU 1423  CZ  TYR A 352     3966   4112   4496    298    198    439       C  
ATOM   1424  OH  TYR A 352     -17.016  34.607 -65.778  1.00 31.95           O  
ANISOU 1424  OH  TYR A 352     3768   3937   4436    314    259    444       O  
ATOM   1425  N   THR A 353     -17.626  27.192 -69.475  1.00 23.94           N  
ANISOU 1425  N   THR A 353     3325   2980   2792    201   -124    418       N  
ATOM   1426  CA  THR A 353     -17.224  25.873 -69.932  1.00 24.66           C  
ANISOU 1426  CA  THR A 353     3541   3070   2760    189   -131    381       C  
ATOM   1427  C   THR A 353     -15.760  25.696 -69.423  1.00 26.85           C  
ANISOU 1427  C   THR A 353     3811   3379   3013    217     37    326       C  
ATOM   1428  O   THR A 353     -15.113  26.708 -69.136  1.00 23.75           O  
ANISOU 1428  O   THR A 353     3361   2996   2668    238    131    332       O  
ATOM   1429  CB  THR A 353     -17.450  25.848 -71.466  1.00 36.41           C  
ANISOU 1429  CB  THR A 353     5214   4507   4113    173   -219    427       C  
ATOM   1430  OG1 THR A 353     -18.203  24.699 -71.838  1.00 41.72           O  
ANISOU 1430  OG1 THR A 353     5961   5160   4729    137   -346    421       O  
ATOM   1431  CG2 THR A 353     -16.174  26.007 -72.293  1.00 33.37           C  
ANISOU 1431  CG2 THR A 353     4973   4108   3599    198   -101    418       C  
ATOM   1432  N   PRO A 354     -15.197  24.467 -69.311  1.00 25.08           N  
ANISOU 1432  N   PRO A 354     3641   3166   2722    218     75    277       N  
ATOM   1433  CA  PRO A 354     -13.807  24.342 -68.814  1.00 24.11           C  
ANISOU 1433  CA  PRO A 354     3494   3071   2594    248    229    236       C  
ATOM   1434  C   PRO A 354     -12.773  25.099 -69.641  1.00 27.36           C  
ANISOU 1434  C   PRO A 354     3989   3466   2942    273    331    259       C  
ATOM   1435  O   PRO A 354     -11.806  25.636 -69.093  1.00 25.56           O  
ANISOU 1435  O   PRO A 354     3685   3262   2766    292    447    249       O  
ATOM   1436  CB  PRO A 354     -13.576  22.825 -68.820  1.00 25.50           C  
ANISOU 1436  CB  PRO A 354     3742   3246   2701    246    227    192       C  
ATOM   1437  CG  PRO A 354     -14.950  22.266 -68.630  1.00 29.39           C  
ANISOU 1437  CG  PRO A 354     4210   3730   3225    208     78    199       C  
ATOM   1438  CD  PRO A 354     -15.787  23.129 -69.532  1.00 26.40           C  
ANISOU 1438  CD  PRO A 354     3881   3318   2832    192    -21    257       C  
ATOM   1439  N   ASN A 355     -13.045  25.233 -70.943  1.00 26.37           N  
ANISOU 1439  N   ASN A 355     4016   3295   2708    268    279    297       N  
ATOM   1440  CA  ASN A 355     -12.185  25.923 -71.903  1.00 26.99           C  
ANISOU 1440  CA  ASN A 355     4198   3350   2708    289    369    329       C  
ATOM   1441  C   ASN A 355     -12.415  27.437 -71.976  1.00 33.16           C  
ANISOU 1441  C   ASN A 355     4919   4122   3559    287    363    384       C  
ATOM   1442  O   ASN A 355     -11.620  28.123 -72.630  1.00 33.98           O  
ANISOU 1442  O   ASN A 355     5086   4209   3616    302    452    416       O  
ATOM   1443  CB  ASN A 355     -12.302  25.271 -73.274  1.00 28.88           C  
ANISOU 1443  CB  ASN A 355     4652   3542   2777    284    326    340       C  
ATOM   1444  CG  ASN A 355     -11.956  23.803 -73.293  1.00 48.98           C  
ANISOU 1444  CG  ASN A 355     7278   6084   5247    292    349    282       C  
ATOM   1445  OD1 ASN A 355     -10.993  23.345 -72.662  1.00 35.25           O  
ANISOU 1445  OD1 ASN A 355     5480   4372   3541    320    470    243       O  
ATOM   1446  ND2 ASN A 355     -12.734  23.032 -74.038  1.00 46.25           N  
ANISOU 1446  ND2 ASN A 355     7075   5700   4799    266    229    279       N  
ATOM   1447  N   SER A 356     -13.479  27.967 -71.294  1.00 28.95           N  
ANISOU 1447  N   SER A 356     4260   3596   3143    270    267    399       N  
ATOM   1448  CA  SER A 356     -13.801  29.407 -71.249  1.00 28.50           C  
ANISOU 1448  CA  SER A 356     4133   3523   3173    271    257    449       C  
ATOM   1449  C   SER A 356     -12.604  30.213 -70.733  1.00 30.82           C  
ANISOU 1449  C   SER A 356     4356   3832   3523    289    406    438       C  
ATOM   1450  O   SER A 356     -11.955  29.784 -69.788  1.00 26.75           O  
ANISOU 1450  O   SER A 356     3756   3354   3052    295    481    386       O  
ATOM   1451  CB  SER A 356     -15.022  29.667 -70.365  1.00 30.93           C  
ANISOU 1451  CB  SER A 356     4299   3840   3616    260    159    452       C  
ATOM   1452  OG  SER A 356     -16.221  29.200 -70.962  1.00 38.43           O  
ANISOU 1452  OG  SER A 356     5300   4765   4535    238      6    486       O  
ATOM   1453  N   ILE A 357     -12.315  31.374 -71.352  1.00 30.89           N  
ANISOU 1453  N   ILE A 357     4398   3808   3529    295    440    492       N  
ATOM   1454  CA  ILE A 357     -11.155  32.211 -70.989  1.00 30.80           C  
ANISOU 1454  CA  ILE A 357     4329   3803   3571    304    575    492       C  
ATOM   1455  C   ILE A 357     -11.454  33.382 -70.039  1.00 34.53           C  
ANISOU 1455  C   ILE A 357     4657   4270   4194    300    574    494       C  
ATOM   1456  O   ILE A 357     -12.459  34.079 -70.194  1.00 35.07           O  
ANISOU 1456  O   ILE A 357     4710   4306   4311    298    487    533       O  
ATOM   1457  CB  ILE A 357     -10.370  32.662 -72.271  1.00 34.26           C  
ANISOU 1457  CB  ILE A 357     4906   4206   3904    312    646    548       C  
ATOM   1458  CG1 ILE A 357      -9.825  31.451 -73.066  1.00 35.47           C  
ANISOU 1458  CG1 ILE A 357     5204   4365   3908    324    687    530       C  
ATOM   1459  CG2 ILE A 357      -9.265  33.708 -71.981  1.00 33.38           C  
ANISOU 1459  CG2 ILE A 357     4728   4092   3865    315    775    565       C  
ATOM   1460  CD1 ILE A 357      -8.386  30.926 -72.679  1.00 45.00           C  
ANISOU 1460  CD1 ILE A 357     6380   5603   5115    342    844    492       C  
ATOM   1461  N   VAL A 358     -10.543  33.597 -69.069  1.00 30.10           N  
ANISOU 1461  N   VAL A 358     3996   3735   3706    297    673    454       N  
ATOM   1462  CA  VAL A 358     -10.549  34.732 -68.140  1.00 29.32           C  
ANISOU 1462  CA  VAL A 358     3778   3625   3738    290    696    446       C  
ATOM   1463  C   VAL A 358      -9.161  35.420 -68.108  1.00 32.84           C  
ANISOU 1463  C   VAL A 358     4208   4065   4206    282    818    456       C  
ATOM   1464  O   VAL A 358      -8.150  34.751 -67.904  1.00 34.09           O  
ANISOU 1464  O   VAL A 358     4359   4258   4336    281    895    430       O  
ATOM   1465  CB  VAL A 358     -11.277  34.550 -66.757  1.00 32.28           C  
ANISOU 1465  CB  VAL A 358     4027   4027   4212    285    652    390       C  
ATOM   1466  CG1 VAL A 358     -11.919  33.167 -66.584  1.00 31.26           C  
ANISOU 1466  CG1 VAL A 358     3907   3935   4035    286    586    358       C  
ATOM   1467  CG2 VAL A 358     -10.412  34.937 -65.556  1.00 31.50           C  
ANISOU 1467  CG2 VAL A 358     3826   3950   4194    271    736    341       C  
ATOM   1468  N   ASN A 359      -9.119  36.730 -68.385  1.00 28.80           N  
ANISOU 1468  N   ASN A 359     3692   3504   3746    277    833    502       N  
ATOM   1469  CA  ASN A 359      -7.883  37.511 -68.387  1.00 29.00           C  
ANISOU 1469  CA  ASN A 359     3697   3514   3806    262    940    521       C  
ATOM   1470  C   ASN A 359      -7.412  37.785 -66.950  1.00 30.35           C  
ANISOU 1470  C   ASN A 359     3737   3706   4087    240    975    461       C  
ATOM   1471  O   ASN A 359      -8.154  38.370 -66.167  1.00 28.65           O  
ANISOU 1471  O   ASN A 359     3457   3473   3956    235    928    435       O  
ATOM   1472  CB  ASN A 359      -8.050  38.818 -69.199  1.00 33.53           C  
ANISOU 1472  CB  ASN A 359     4320   4021   4399    260    938    595       C  
ATOM   1473  CG  ASN A 359      -6.866  39.173 -70.099  1.00 58.47           C  
ANISOU 1473  CG  ASN A 359     7546   7162   7507    253   1042    652       C  
ATOM   1474  OD1 ASN A 359      -5.880  38.426 -70.230  1.00 46.22           O  
ANISOU 1474  OD1 ASN A 359     6010   5647   5905    254   1125    641       O  
ATOM   1475  ND2 ASN A 359      -6.939  40.337 -70.745  1.00 51.06           N  
ANISOU 1475  ND2 ASN A 359     6648   6164   6589    248   1045    720       N  
ATOM   1476  N   THR A 360      -6.195  37.312 -66.600  1.00 26.19           N  
ANISOU 1476  N   THR A 360     3177   3216   3559    227   1057    440       N  
ATOM   1477  CA  THR A 360      -5.605  37.467 -65.260  1.00 25.07           C  
ANISOU 1477  CA  THR A 360     2921   3098   3508    198   1083    387       C  
ATOM   1478  C   THR A 360      -4.413  38.464 -65.248  1.00 29.21           C  
ANISOU 1478  C   THR A 360     3409   3593   4097    166   1164    419       C  
ATOM   1479  O   THR A 360      -3.837  38.721 -64.186  1.00 27.44           O  
ANISOU 1479  O   THR A 360     3096   3380   3950    133   1179    381       O  
ATOM   1480  CB  THR A 360      -5.326  36.093 -64.581  1.00 33.43           C  
ANISOU 1480  CB  THR A 360     3944   4223   4537    202   1084    335       C  
ATOM   1481  OG1 THR A 360      -4.153  35.473 -65.131  1.00 28.74           O  
ANISOU 1481  OG1 THR A 360     3374   3650   3896    209   1166    361       O  
ATOM   1482  CG2 THR A 360      -6.542  35.126 -64.620  1.00 33.10           C  
ANISOU 1482  CG2 THR A 360     3938   4203   4437    227   1000    309       C  
ATOM   1483  N   ALA A 361      -4.076  39.039 -66.428  1.00 27.08           N  
ANISOU 1483  N   ALA A 361     3211   3283   3794    172   1211    492       N  
ATOM   1484  CA  ALA A 361      -3.007  40.037 -66.606  1.00 27.75           C  
ANISOU 1484  CA  ALA A 361     3270   3333   3942    140   1290    539       C  
ATOM   1485  C   ALA A 361      -3.264  41.302 -65.769  1.00 29.76           C  
ANISOU 1485  C   ALA A 361     3461   3537   4310    106   1256    518       C  
ATOM   1486  O   ALA A 361      -4.416  41.739 -65.694  1.00 29.28           O  
ANISOU 1486  O   ALA A 361     3420   3445   4262    122   1186    506       O  
ATOM   1487  CB  ALA A 361      -2.883  40.420 -68.081  1.00 29.22           C  
ANISOU 1487  CB  ALA A 361     3564   3479   4058    158   1335    624       C  
ATOM   1488  N   PRO A 362      -2.241  41.917 -65.129  1.00 25.16           N  
ANISOU 1488  N   PRO A 362     2803   2942   3816     59   1302    515       N  
ATOM   1489  CA  PRO A 362      -0.802  41.580 -65.120  1.00 24.96           C  
ANISOU 1489  CA  PRO A 362     2727   2947   3810     33   1384    539       C  
ATOM   1490  C   PRO A 362      -0.363  40.638 -63.988  1.00 28.92           C  
ANISOU 1490  C   PRO A 362     3144   3513   4330     19   1369    475       C  
ATOM   1491  O   PRO A 362       0.809  40.620 -63.610  1.00 27.35           O  
ANISOU 1491  O   PRO A 362     2872   3330   4190    -16   1415    489       O  
ATOM   1492  CB  PRO A 362      -0.160  42.962 -65.002  1.00 26.71           C  
ANISOU 1492  CB  PRO A 362     2911   3104   4134    -19   1414    575       C  
ATOM   1493  CG  PRO A 362      -1.121  43.721 -64.121  1.00 29.83           C  
ANISOU 1493  CG  PRO A 362     3292   3458   4585    -32   1332    515       C  
ATOM   1494  CD  PRO A 362      -2.493  43.152 -64.357  1.00 25.18           C  
ANISOU 1494  CD  PRO A 362     2762   2885   3920     24   1270    489       C  
ATOM   1495  N   GLY A 363      -1.309  39.859 -63.471  1.00 27.48           N  
ANISOU 1495  N   GLY A 363     2971   3366   4103     46   1301    414       N  
ATOM   1496  CA  GLY A 363      -1.082  38.936 -62.361  1.00 27.55           C  
ANISOU 1496  CA  GLY A 363     2912   3435   4120     35   1275    353       C  
ATOM   1497  C   GLY A 363      -1.558  39.512 -61.044  1.00 31.74           C  
ANISOU 1497  C   GLY A 363     3392   3954   4714     -1   1211    285       C  
ATOM   1498  O   GLY A 363      -1.304  38.934 -59.982  1.00 32.15           O  
ANISOU 1498  O   GLY A 363     3386   4050   4780    -22   1186    236       O  
ATOM   1499  N   THR A 364      -2.211  40.695 -61.114  1.00 27.58           N  
ANISOU 1499  N   THR A 364     2892   3362   4227     -7   1190    286       N  
ATOM   1500  CA  THR A 364      -2.798  41.451 -59.999  1.00 26.72           C  
ANISOU 1500  CA  THR A 364     2757   3220   4177    -33   1143    222       C  
ATOM   1501  C   THR A 364      -4.201  41.939 -60.345  1.00 27.20           C  
ANISOU 1501  C   THR A 364     2869   3235   4231      9   1107    220       C  
ATOM   1502  O   THR A 364      -4.580  41.913 -61.511  1.00 26.49           O  
ANISOU 1502  O   THR A 364     2836   3130   4100     45   1112    278       O  
ATOM   1503  CB  THR A 364      -1.890  42.587 -59.495  1.00 35.34           C  
ANISOU 1503  CB  THR A 364     3809   4260   5357    -98   1161    224       C  
ATOM   1504  OG1 THR A 364      -1.459  43.390 -60.590  1.00 31.01           O  
ANISOU 1504  OG1 THR A 364     3291   3659   4834   -101   1208    301       O  
ATOM   1505  CG2 THR A 364      -0.710  42.079 -58.658  1.00 33.65           C  
ANISOU 1505  CG2 THR A 364     3523   4095   5169   -149   1164    205       C  
ATOM   1506  N   MET A 365      -4.976  42.361 -59.329  1.00 22.27           N  
ANISOU 1506  N   MET A 365     2227   2589   3646      5   1071    156       N  
ATOM   1507  CA  MET A 365      -6.367  42.800 -59.462  1.00 21.92           C  
ANISOU 1507  CA  MET A 365     2211   2501   3616     48   1038    150       C  
ATOM   1508  C   MET A 365      -6.804  43.551 -58.193  1.00 26.59           C  
ANISOU 1508  C   MET A 365     2778   3052   4272     31   1029     76       C  
ATOM   1509  O   MET A 365      -6.428  43.158 -57.084  1.00 23.15           O  
ANISOU 1509  O   MET A 365     2310   2654   3830     -2   1026     13       O  
ATOM   1510  CB  MET A 365      -7.270  41.553 -59.665  1.00 23.70           C  
ANISOU 1510  CB  MET A 365     2446   2788   3771     94    999    146       C  
ATOM   1511  CG  MET A 365      -8.751  41.832 -59.622  1.00 27.93           C  
ANISOU 1511  CG  MET A 365     2988   3291   4333    138    958    139       C  
ATOM   1512  SD  MET A 365      -9.704  40.323 -59.432  1.00 32.07           S  
ANISOU 1512  SD  MET A 365     3499   3891   4794    171    909    117       S  
ATOM   1513  CE  MET A 365     -11.331  41.003 -59.415  1.00 28.88           C  
ANISOU 1513  CE  MET A 365     3083   3430   4459    216    871    125       C  
ATOM   1514  N   ARG A 366      -7.645  44.600 -58.353  1.00 25.82           N  
ANISOU 1514  N   ARG A 366     2702   2874   4234     56   1025     84       N  
ATOM   1515  CA  ARG A 366      -8.155  45.310 -57.195  1.00 26.72           C  
ANISOU 1515  CA  ARG A 366     2805   2939   4407     49   1029     11       C  
ATOM   1516  C   ARG A 366      -9.602  45.001 -56.791  1.00 32.85           C  
ANISOU 1516  C   ARG A 366     3571   3721   5190    106   1010    -20       C  
ATOM   1517  O   ARG A 366     -10.526  45.032 -57.618  1.00 32.69           O  
ANISOU 1517  O   ARG A 366     3557   3680   5182    158    988     33       O  
ATOM   1518  CB  ARG A 366      -7.791  46.796 -57.193  1.00 29.10           C  
ANISOU 1518  CB  ARG A 366     3129   3136   4790     22   1052     17       C  
ATOM   1519  CG  ARG A 366      -8.713  47.749 -57.943  1.00 41.57           C  
ANISOU 1519  CG  ARG A 366     4737   4630   6430     72   1050     65       C  
ATOM   1520  CD  ARG A 366      -8.429  49.190 -57.563  1.00 42.48           C  
ANISOU 1520  CD  ARG A 366     4874   4635   6633     42   1076     44       C  
ATOM   1521  NE  ARG A 366      -8.203  49.312 -56.124  1.00 51.95           N  
ANISOU 1521  NE  ARG A 366     6068   5829   7842      3   1088    -58       N  
ATOM   1522  CZ  ARG A 366      -7.020  49.529 -55.553  1.00 56.77           C  
ANISOU 1522  CZ  ARG A 366     6679   6437   8454    -75   1092    -91       C  
ATOM   1523  NH1 ARG A 366      -5.933  49.689 -56.300  1.00 40.28           N  
ANISOU 1523  NH1 ARG A 366     4584   4349   6371   -119   1095    -26       N  
ATOM   1524  NH2 ARG A 366      -6.917  49.589 -54.235  1.00 37.01           N  
ANISOU 1524  NH2 ARG A 366     4184   3931   5947   -110   1092   -185       N  
ATOM   1525  N   LEU A 367      -9.763  44.646 -55.512  1.00 29.70           N  
ANISOU 1525  N   LEU A 367     3151   3353   4781     92   1018   -101       N  
ATOM   1526  CA  LEU A 367     -11.041  44.376 -54.879  1.00 29.75           C  
ANISOU 1526  CA  LEU A 367     3138   3365   4799    138   1018   -139       C  
ATOM   1527  C   LEU A 367     -11.182  45.408 -53.767  1.00 31.79           C  
ANISOU 1527  C   LEU A 367     3413   3551   5114    126   1058   -214       C  
ATOM   1528  O   LEU A 367     -10.881  45.105 -52.610  1.00 30.85           O  
ANISOU 1528  O   LEU A 367     3297   3463   4961     91   1071   -288       O  
ATOM   1529  CB  LEU A 367     -11.079  42.942 -54.306  1.00 29.99           C  
ANISOU 1529  CB  LEU A 367     3141   3498   4754    132   1000   -169       C  
ATOM   1530  CG  LEU A 367     -11.362  41.768 -55.264  1.00 35.07           C  
ANISOU 1530  CG  LEU A 367     3774   4208   5343    160    959   -108       C  
ATOM   1531  CD1 LEU A 367     -11.432  40.472 -54.491  1.00 35.05           C  
ANISOU 1531  CD1 LEU A 367     3746   4292   5280    150    948   -147       C  
ATOM   1532  CD2 LEU A 367     -12.686  41.956 -56.037  1.00 38.07           C  
ANISOU 1532  CD2 LEU A 367     4147   4553   5766    220    933    -56       C  
ATOM   1533  N   GLY A 368     -11.583  46.631 -54.148  1.00 27.23           N  
ANISOU 1533  N   GLY A 368     2856   2872   4618    151   1076   -193       N  
ATOM   1534  CA  GLY A 368     -11.741  47.770 -53.253  1.00 27.17           C  
ANISOU 1534  CA  GLY A 368     2879   2772   4673    145   1120   -261       C  
ATOM   1535  C   GLY A 368     -10.382  48.338 -52.904  1.00 31.73           C  
ANISOU 1535  C   GLY A 368     3493   3322   5242     63   1121   -291       C  
ATOM   1536  O   GLY A 368      -9.601  48.679 -53.801  1.00 29.69           O  
ANISOU 1536  O   GLY A 368     3239   3045   4998     36   1106   -228       O  
ATOM   1537  N   TRP A 369     -10.058  48.388 -51.606  1.00 29.96           N  
ANISOU 1537  N   TRP A 369     3293   3099   4991     19   1137   -383       N  
ATOM   1538  CA  TRP A 369      -8.722  48.818 -51.209  1.00 31.03           C  
ANISOU 1538  CA  TRP A 369     3457   3216   5118    -71   1120   -411       C  
ATOM   1539  C   TRP A 369      -7.789  47.607 -50.998  1.00 34.51           C  
ANISOU 1539  C   TRP A 369     3864   3772   5476   -122   1081   -405       C  
ATOM   1540  O   TRP A 369      -6.622  47.758 -50.631  1.00 33.46           O  
ANISOU 1540  O   TRP A 369     3737   3642   5335   -200   1057   -420       O  
ATOM   1541  CB  TRP A 369      -8.739  49.810 -50.041  1.00 30.89           C  
ANISOU 1541  CB  TRP A 369     3504   3107   5125   -103   1148   -507       C  
ATOM   1542  CG  TRP A 369      -8.645  51.255 -50.472  1.00 32.81           C  
ANISOU 1542  CG  TRP A 369     3788   3219   5461   -108   1166   -493       C  
ATOM   1543  CD1 TRP A 369      -9.594  52.218 -50.299  1.00 36.54           C  
ANISOU 1543  CD1 TRP A 369     4298   3584   6002    -53   1214   -524       C  
ATOM   1544  CD2 TRP A 369      -7.554  51.885 -51.174  1.00 32.93           C  
ANISOU 1544  CD2 TRP A 369     3804   3192   5517   -168   1140   -437       C  
ATOM   1545  NE1 TRP A 369      -9.157  53.414 -50.823  1.00 37.47           N  
ANISOU 1545  NE1 TRP A 369     4447   3592   6199    -77   1215   -494       N  
ATOM   1546  CE2 TRP A 369      -7.896  53.247 -51.339  1.00 38.09           C  
ANISOU 1546  CE2 TRP A 369     4504   3708   6260   -152   1170   -442       C  
ATOM   1547  CE3 TRP A 369      -6.303  51.439 -51.652  1.00 33.79           C  
ANISOU 1547  CE3 TRP A 369     3875   3361   5602   -233   1101   -382       C  
ATOM   1548  CZ2 TRP A 369      -7.043  54.164 -51.970  1.00 37.57           C  
ANISOU 1548  CZ2 TRP A 369     4452   3565   6257   -204   1157   -392       C  
ATOM   1549  CZ3 TRP A 369      -5.450  52.355 -52.265  1.00 35.75           C  
ANISOU 1549  CZ3 TRP A 369     4132   3537   5916   -284   1095   -331       C  
ATOM   1550  CH2 TRP A 369      -5.839  53.690 -52.453  1.00 37.35           C  
ANISOU 1550  CH2 TRP A 369     4383   3605   6204   -270   1121   -333       C  
ATOM   1551  N   HIS A 370      -8.316  46.399 -51.266  1.00 30.91           N  
ANISOU 1551  N   HIS A 370     3367   3407   4968    -76   1072   -378       N  
ATOM   1552  CA  HIS A 370      -7.542  45.164 -51.192  1.00 30.38           C  
ANISOU 1552  CA  HIS A 370     3266   3447   4830   -109   1039   -363       C  
ATOM   1553  C   HIS A 370      -7.052  44.787 -52.601  1.00 29.68           C  
ANISOU 1553  C   HIS A 370     3148   3388   4742    -95   1028   -267       C  
ATOM   1554  O   HIS A 370      -7.822  44.864 -53.565  1.00 27.45           O  
ANISOU 1554  O   HIS A 370     2866   3086   4476    -36   1034   -214       O  
ATOM   1555  CB  HIS A 370      -8.368  44.039 -50.531  1.00 31.60           C  
ANISOU 1555  CB  HIS A 370     3404   3678   4924    -74   1037   -398       C  
ATOM   1556  CG  HIS A 370      -7.632  42.745 -50.348  1.00 35.49           C  
ANISOU 1556  CG  HIS A 370     3864   4274   5347   -104   1003   -386       C  
ATOM   1557  ND1 HIS A 370      -6.307  42.708 -49.912  1.00 38.36           N  
ANISOU 1557  ND1 HIS A 370     4222   4656   5695   -179    977   -395       N  
ATOM   1558  CD2 HIS A 370      -8.070  41.475 -50.509  1.00 36.79           C  
ANISOU 1558  CD2 HIS A 370     3999   4520   5461    -70    990   -365       C  
ATOM   1559  CE1 HIS A 370      -5.984  41.424 -49.861  1.00 36.99           C  
ANISOU 1559  CE1 HIS A 370     4013   4575   5466   -180    953   -376       C  
ATOM   1560  NE2 HIS A 370      -7.016  40.647 -50.200  1.00 36.68           N  
ANISOU 1560  NE2 HIS A 370     3963   4573   5400   -116    961   -361       N  
ATOM   1561  N   THR A 371      -5.756  44.441 -52.725  1.00 25.49           N  
ANISOU 1561  N   THR A 371     2593   2896   4194   -150   1012   -240       N  
ATOM   1562  CA  THR A 371      -5.150  44.033 -53.995  1.00 24.68           C  
ANISOU 1562  CA  THR A 371     2469   2823   4084   -139   1017   -152       C  
ATOM   1563  C   THR A 371      -4.681  42.568 -53.963  1.00 28.85           C  
ANISOU 1563  C   THR A 371     2961   3456   4545   -139   1002   -139       C  
ATOM   1564  O   THR A 371      -3.982  42.123 -53.049  1.00 27.84           O  
ANISOU 1564  O   THR A 371     2808   3370   4400   -186    982   -174       O  
ATOM   1565  CB  THR A 371      -4.271  45.124 -54.661  1.00 37.84           C  
ANISOU 1565  CB  THR A 371     4143   4420   5815   -178   1036   -101       C  
ATOM   1566  OG1 THR A 371      -3.407  44.566 -55.654  1.00 33.10           O  
ANISOU 1566  OG1 THR A 371     3517   3864   5196   -181   1052    -24       O  
ATOM   1567  CG2 THR A 371      -3.468  45.921 -53.682  1.00 42.27           C  
ANISOU 1567  CG2 THR A 371     4704   4934   6421   -257   1023   -150       C  
ATOM   1568  N   ILE A 372      -5.177  41.809 -54.937  1.00 25.58           N  
ANISOU 1568  N   ILE A 372     2551   3078   4091    -83   1006    -90       N  
ATOM   1569  CA  ILE A 372      -4.975  40.373 -55.107  1.00 24.63           C  
ANISOU 1569  CA  ILE A 372     2410   3044   3906    -65    996    -75       C  
ATOM   1570  C   ILE A 372      -3.831  40.097 -56.063  1.00 27.55           C  
ANISOU 1570  C   ILE A 372     2768   3431   4270    -75   1023     -5       C  
ATOM   1571  O   ILE A 372      -3.716  40.763 -57.088  1.00 26.20           O  
ANISOU 1571  O   ILE A 372     2623   3214   4120    -64   1051     50       O  
ATOM   1572  CB  ILE A 372      -6.350  39.719 -55.505  1.00 26.80           C  
ANISOU 1572  CB  ILE A 372     2706   3338   4140     -1    978    -72       C  
ATOM   1573  CG1 ILE A 372      -7.176  39.416 -54.254  1.00 27.50           C  
ANISOU 1573  CG1 ILE A 372     2781   3448   4220      1    960   -143       C  
ATOM   1574  CG2 ILE A 372      -6.249  38.486 -56.359  1.00 25.55           C  
ANISOU 1574  CG2 ILE A 372     2554   3238   3918     30    972    -28       C  
ATOM   1575  CD1 ILE A 372      -7.992  40.542 -53.783  1.00 36.87           C  
ANISOU 1575  CD1 ILE A 372     3984   4565   5461     10    971   -180       C  
ATOM   1576  N   ARG A 373      -2.977  39.127 -55.706  1.00 24.26           N  
ANISOU 1576  N   ARG A 373     2311   3078   3829    -95   1021     -5       N  
ATOM   1577  CA  ARG A 373      -1.850  38.737 -56.550  1.00 24.89           C  
ANISOU 1577  CA  ARG A 373     2370   3178   3908    -97   1061     61       C  
ATOM   1578  C   ARG A 373      -1.787  37.233 -56.795  1.00 30.07           C  
ANISOU 1578  C   ARG A 373     3022   3904   4500    -60   1064     72       C  
ATOM   1579  O   ARG A 373      -2.206  36.427 -55.954  1.00 29.68           O  
ANISOU 1579  O   ARG A 373     2959   3900   4419    -57   1026     26       O  
ATOM   1580  CB  ARG A 373      -0.512  39.273 -55.993  1.00 24.02           C  
ANISOU 1580  CB  ARG A 373     2202   3058   3867   -167   1067     70       C  
ATOM   1581  CG  ARG A 373      -0.160  38.824 -54.559  1.00 29.57           C  
ANISOU 1581  CG  ARG A 373     2859   3803   4572   -213   1016     15       C  
ATOM   1582  CD  ARG A 373       1.159  39.380 -54.037  1.00 26.77           C  
ANISOU 1582  CD  ARG A 373     2445   3434   4291   -289   1005     31       C  
ATOM   1583  NE  ARG A 373       2.169  39.488 -55.091  1.00 29.71           N  
ANISOU 1583  NE  ARG A 373     2781   3798   4709   -289   1063    116       N  
ATOM   1584  CZ  ARG A 373       3.030  38.534 -55.428  1.00 44.60           C  
ANISOU 1584  CZ  ARG A 373     4613   5735   6597   -274   1093    166       C  
ATOM   1585  NH1 ARG A 373       3.033  37.377 -54.782  1.00 30.30           N  
ANISOU 1585  NH1 ARG A 373     2777   3987   4747   -261   1060    142       N  
ATOM   1586  NH2 ARG A 373       3.904  38.736 -56.408  1.00 37.63           N  
ANISOU 1586  NH2 ARG A 373     3702   4837   5760   -270   1162    245       N  
ATOM   1587  N   ASP A 374      -1.284  36.875 -57.973  1.00 27.03           N  
ANISOU 1587  N   ASP A 374     2656   3523   4092    -30   1114    135       N  
ATOM   1588  CA  ASP A 374      -0.982  35.511 -58.385  1.00 26.16           C  
ANISOU 1588  CA  ASP A 374     2548   3466   3927      6   1134    154       C  
ATOM   1589  C   ASP A 374       0.542  35.322 -58.201  1.00 32.71           C  
ANISOU 1589  C   ASP A 374     3304   4316   4809    -24   1176    189       C  
ATOM   1590  O   ASP A 374       1.268  36.313 -58.044  1.00 30.60           O  
ANISOU 1590  O   ASP A 374     2996   4016   4614    -71   1191    210       O  
ATOM   1591  CB  ASP A 374      -1.412  35.272 -59.847  1.00 26.87           C  
ANISOU 1591  CB  ASP A 374     2721   3538   3951     60   1169    199       C  
ATOM   1592  CG  ASP A 374      -2.879  34.902 -60.003  1.00 30.99           C  
ANISOU 1592  CG  ASP A 374     3302   4059   4413     95   1112    169       C  
ATOM   1593  OD1 ASP A 374      -3.594  34.845 -58.977  1.00 31.49           O  
ANISOU 1593  OD1 ASP A 374     3337   4136   4491     83   1057    115       O  
ATOM   1594  OD2 ASP A 374      -3.310  34.663 -61.142  1.00 33.41           O  
ANISOU 1594  OD2 ASP A 374     3685   4350   4658    133   1121    203       O  
ATOM   1595  N   THR A 375       1.013  34.053 -58.170  1.00 32.52           N  
ANISOU 1595  N   THR A 375     3257   4341   4758      2   1191    198       N  
ATOM   1596  CA  THR A 375       2.433  33.703 -58.006  1.00 33.65           C  
ANISOU 1596  CA  THR A 375     3318   4507   4960    -16   1232    240       C  
ATOM   1597  C   THR A 375       3.235  34.242 -59.189  1.00 40.18           C  
ANISOU 1597  C   THR A 375     4151   5300   5817     -6   1325    314       C  
ATOM   1598  O   THR A 375       4.377  34.671 -59.009  1.00 41.83           O  
ANISOU 1598  O   THR A 375     4278   5502   6112    -45   1355    356       O  
ATOM   1599  CB  THR A 375       2.592  32.189 -57.695  1.00 41.58           C  
ANISOU 1599  CB  THR A 375     4304   5566   5930     18   1224    230       C  
ATOM   1600  OG1 THR A 375       1.899  31.900 -56.473  1.00 39.36           O  
ANISOU 1600  OG1 THR A 375     4013   5313   5631     -6   1137    167       O  
ATOM   1601  CG2 THR A 375       4.055  31.750 -57.538  1.00 42.54           C  
ANISOU 1601  CG2 THR A 375     4329   5709   6124      8   1267    282       C  
ATOM   1602  N   HIS A 376       2.611  34.256 -60.389  1.00 36.94           N  
ANISOU 1602  N   HIS A 376     3838   4864   5333     43   1367    333       N  
ATOM   1603  CA  HIS A 376       3.180  34.776 -61.641  1.00 37.10           C  
ANISOU 1603  CA  HIS A 376     3892   4847   5355     59   1461    404       C  
ATOM   1604  C   HIS A 376       2.054  35.394 -62.506  1.00 36.41           C  
ANISOU 1604  C   HIS A 376     3917   4717   5198     81   1446    403       C  
ATOM   1605  O   HIS A 376       0.870  35.180 -62.231  1.00 34.13           O  
ANISOU 1605  O   HIS A 376     3676   4435   4859     95   1371    353       O  
ATOM   1606  CB  HIS A 376       3.872  33.654 -62.452  1.00 39.02           C  
ANISOU 1606  CB  HIS A 376     4155   5114   5559    115   1553    445       C  
ATOM   1607  CG  HIS A 376       4.751  32.737 -61.654  1.00 43.73           C  
ANISOU 1607  CG  HIS A 376     4650   5755   6210    114   1557    444       C  
ATOM   1608  ND1 HIS A 376       6.019  33.122 -61.242  1.00 46.95           N  
ANISOU 1608  ND1 HIS A 376     4939   6165   6734     73   1592    491       N  
ATOM   1609  CD2 HIS A 376       4.521  31.472 -61.230  1.00 45.58           C  
ANISOU 1609  CD2 HIS A 376     4886   6027   6403    146   1527    407       C  
ATOM   1610  CE1 HIS A 376       6.511  32.085 -60.579  1.00 46.32           C  
ANISOU 1610  CE1 HIS A 376     4790   6128   6681     85   1578    484       C  
ATOM   1611  NE2 HIS A 376       5.645  31.071 -60.543  1.00 45.82           N  
ANISOU 1611  NE2 HIS A 376     4799   6087   6525    130   1542    433       N  
ATOM   1612  N   ASN A 377       2.431  36.130 -63.570  1.00 31.18           N  
ANISOU 1612  N   ASN A 377     3298   4013   4536     85   1519    468       N  
ATOM   1613  CA  ASN A 377       1.487  36.666 -64.540  1.00 30.09           C  
ANISOU 1613  CA  ASN A 377     3272   3833   4328    108   1509    485       C  
ATOM   1614  C   ASN A 377       1.147  35.461 -65.425  1.00 32.42           C  
ANISOU 1614  C   ASN A 377     3665   4150   4503    169   1534    487       C  
ATOM   1615  O   ASN A 377       1.980  35.034 -66.236  1.00 32.85           O  
ANISOU 1615  O   ASN A 377     3748   4207   4527    197   1634    535       O  
ATOM   1616  CB  ASN A 377       2.130  37.805 -65.363  1.00 27.72           C  
ANISOU 1616  CB  ASN A 377     2985   3481   4066     88   1584    561       C  
ATOM   1617  CG  ASN A 377       1.247  38.443 -66.428  1.00 35.97           C  
ANISOU 1617  CG  ASN A 377     4149   4477   5041    109   1574    594       C  
ATOM   1618  OD1 ASN A 377       1.696  39.286 -67.217  1.00 32.79           O  
ANISOU 1618  OD1 ASN A 377     3775   4031   4654     98   1638    662       O  
ATOM   1619  ND2 ASN A 377      -0.034  38.130 -66.446  1.00 15.24           N  
ANISOU 1619  ND2 ASN A 377     1590   1855   2348    136   1488    553       N  
ATOM   1620  N   TYR A 378      -0.049  34.869 -65.221  1.00 26.59           N  
ANISOU 1620  N   TYR A 378     2976   3426   3701    190   1445    435       N  
ATOM   1621  CA  TYR A 378      -0.471  33.671 -65.970  1.00 25.31           C  
ANISOU 1621  CA  TYR A 378     2913   3279   3423    240   1447    428       C  
ATOM   1622  C   TYR A 378      -1.268  34.031 -67.200  1.00 28.88           C  
ANISOU 1622  C   TYR A 378     3498   3690   3785    260   1432    462       C  
ATOM   1623  O   TYR A 378      -1.744  33.128 -67.889  1.00 29.68           O  
ANISOU 1623  O   TYR A 378     3702   3795   3781    295   1418    455       O  
ATOM   1624  CB  TYR A 378      -1.270  32.687 -65.088  1.00 24.05           C  
ANISOU 1624  CB  TYR A 378     2733   3159   3248    246   1357    359       C  
ATOM   1625  CG  TYR A 378      -0.503  32.116 -63.918  1.00 23.73           C  
ANISOU 1625  CG  TYR A 378     2577   3162   3276    230   1365    329       C  
ATOM   1626  CD1 TYR A 378      -0.938  32.312 -62.616  1.00 24.30           C  
ANISOU 1626  CD1 TYR A 378     2570   3255   3408    195   1287    278       C  
ATOM   1627  CD2 TYR A 378       0.636  31.334 -64.117  1.00 25.21           C  
ANISOU 1627  CD2 TYR A 378     2742   3369   3467    252   1452    353       C  
ATOM   1628  CE1 TYR A 378      -0.239  31.788 -61.532  1.00 25.46           C  
ANISOU 1628  CE1 TYR A 378     2621   3442   3609    176   1284    255       C  
ATOM   1629  CE2 TYR A 378       1.330  30.777 -63.040  1.00 25.33           C  
ANISOU 1629  CE2 TYR A 378     2649   3423   3551    238   1447    333       C  
ATOM   1630  CZ  TYR A 378       0.886  31.004 -61.747  1.00 31.13           C  
ANISOU 1630  CZ  TYR A 378     3311   4180   4336    196   1357    285       C  
ATOM   1631  OH  TYR A 378       1.536  30.437 -60.670  1.00 28.60           O  
ANISOU 1631  OH  TYR A 378     2894   3900   4073    178   1341    269       O  
ATOM   1632  N   GLY A 379      -1.422  35.336 -67.439  1.00 23.79           N  
ANISOU 1632  N   GLY A 379     2855   3003   3183    236   1427    498       N  
ATOM   1633  CA  GLY A 379      -2.157  35.908 -68.560  1.00 23.62           C  
ANISOU 1633  CA  GLY A 379     2950   2936   3090    249   1403    543       C  
ATOM   1634  C   GLY A 379      -3.581  35.407 -68.679  1.00 26.68           C  
ANISOU 1634  C   GLY A 379     3403   3324   3410    266   1286    511       C  
ATOM   1635  O   GLY A 379      -4.305  35.320 -67.683  1.00 23.88           O  
ANISOU 1635  O   GLY A 379     2976   2987   3109    255   1205    459       O  
ATOM   1636  N   ALA A 380      -3.981  35.063 -69.909  1.00 26.30           N  
ANISOU 1636  N   ALA A 380     3495   3257   3242    292   1279    546       N  
ATOM   1637  CA  ALA A 380      -5.307  34.532 -70.191  1.00 26.82           C  
ANISOU 1637  CA  ALA A 380     3633   3318   3238    304   1160    528       C  
ATOM   1638  C   ALA A 380      -5.308  33.034 -69.834  1.00 31.71           C  
ANISOU 1638  C   ALA A 380     4258   3982   3809    320   1149    471       C  
ATOM   1639  O   ALA A 380      -4.458  32.274 -70.326  1.00 33.02           O  
ANISOU 1639  O   ALA A 380     4481   4158   3907    342   1236    474       O  
ATOM   1640  CB  ALA A 380      -5.646  34.739 -71.659  1.00 28.41           C  
ANISOU 1640  CB  ALA A 380     3994   3478   3322    316   1149    590       C  
ATOM   1641  N   LEU A 381      -6.232  32.631 -68.937  1.00 25.25           N  
ANISOU 1641  N   LEU A 381     3374   3187   3034    312   1050    421       N  
ATOM   1642  CA  LEU A 381      -6.385  31.249 -68.474  1.00 22.56           C  
ANISOU 1642  CA  LEU A 381     3027   2883   2660    322   1022    367       C  
ATOM   1643  C   LEU A 381      -7.775  30.711 -68.753  1.00 28.07           C  
ANISOU 1643  C   LEU A 381     3788   3573   3306    322    894    357       C  
ATOM   1644  O   LEU A 381      -8.764  31.439 -68.632  1.00 29.16           O  
ANISOU 1644  O   LEU A 381     3897   3691   3490    309    810    373       O  
ATOM   1645  CB  LEU A 381      -6.181  31.156 -66.948  1.00 20.21           C  
ANISOU 1645  CB  LEU A 381     2580   2628   2473    305   1022    316       C  
ATOM   1646  CG  LEU A 381      -4.800  31.343 -66.369  1.00 23.28           C  
ANISOU 1646  CG  LEU A 381     2883   3037   2926    298   1125    315       C  
ATOM   1647  CD1 LEU A 381      -4.875  31.293 -64.854  1.00 21.41           C  
ANISOU 1647  CD1 LEU A 381     2516   2836   2783    273   1091    264       C  
ATOM   1648  CD2 LEU A 381      -3.815  30.272 -66.871  1.00 24.00           C  
ANISOU 1648  CD2 LEU A 381     3023   3143   2954    326   1212    319       C  
ATOM   1649  N   THR A 382      -7.861  29.402 -69.003  1.00 24.42           N  
ANISOU 1649  N   THR A 382     3394   3122   2762    334    877    330       N  
ATOM   1650  CA  THR A 382      -9.137  28.709 -69.124  1.00 24.19           C  
ANISOU 1650  CA  THR A 382     3409   3087   2695    326    748    316       C  
ATOM   1651  C   THR A 382      -9.597  28.400 -67.679  1.00 28.32           C  
ANISOU 1651  C   THR A 382     3787   3650   3321    311    706    268       C  
ATOM   1652  O   THR A 382      -8.795  28.548 -66.755  1.00 26.95           O  
ANISOU 1652  O   THR A 382     3514   3507   3219    310    780    244       O  
ATOM   1653  CB  THR A 382      -8.959  27.392 -69.884  1.00 30.57           C  
ANISOU 1653  CB  THR A 382     4351   3886   3377    341    753    299       C  
ATOM   1654  OG1 THR A 382      -7.996  26.590 -69.189  1.00 29.50           O  
ANISOU 1654  OG1 THR A 382     4159   3783   3265    357    841    258       O  
ATOM   1655  CG2 THR A 382      -8.558  27.594 -71.344  1.00 23.94           C  
ANISOU 1655  CG2 THR A 382     3678   3005   2412    356    799    342       C  
ATOM   1656  N   LEU A 383     -10.852  27.913 -67.482  1.00 25.36           N  
ANISOU 1656  N   LEU A 383     3406   3276   2954    298    589    258       N  
ATOM   1657  CA  LEU A 383     -11.319  27.531 -66.152  1.00 24.56           C  
ANISOU 1657  CA  LEU A 383     3180   3212   2940    285    557    217       C  
ATOM   1658  C   LEU A 383     -10.442  26.444 -65.595  1.00 25.13           C  
ANISOU 1658  C   LEU A 383     3237   3318   2994    292    620    174       C  
ATOM   1659  O   LEU A 383     -10.134  26.468 -64.404  1.00 23.05           O  
ANISOU 1659  O   LEU A 383     2861   3090   2806    285    653    145       O  
ATOM   1660  CB  LEU A 383     -12.797  27.122 -66.131  1.00 25.10           C  
ANISOU 1660  CB  LEU A 383     3243   3272   3021    269    427    223       C  
ATOM   1661  CG  LEU A 383     -13.753  28.182 -65.567  1.00 29.86           C  
ANISOU 1661  CG  LEU A 383     3742   3869   3735    262    379    242       C  
ATOM   1662  CD1 LEU A 383     -13.785  29.427 -66.446  1.00 29.95           C  
ANISOU 1662  CD1 LEU A 383     3798   3837   3745    270    377    295       C  
ATOM   1663  CD2 LEU A 383     -15.151  27.610 -65.390  1.00 32.23           C  
ANISOU 1663  CD2 LEU A 383     4012   4168   4066    246    261    250       C  
ATOM   1664  N   THR A 384      -9.977  25.526 -66.465  1.00 22.68           N  
ANISOU 1664  N   THR A 384     3045   2992   2581    308    643    173       N  
ATOM   1665  CA  THR A 384      -9.043  24.477 -66.047  1.00 21.61           C  
ANISOU 1665  CA  THR A 384     2902   2880   2431    324    713    140       C  
ATOM   1666  C   THR A 384      -7.709  25.081 -65.551  1.00 24.12           C  
ANISOU 1666  C   THR A 384     3138   3221   2807    335    833    143       C  
ATOM   1667  O   THR A 384      -7.212  24.638 -64.514  1.00 25.05           O  
ANISOU 1667  O   THR A 384     3163   3373   2981    333    860    116       O  
ATOM   1668  CB  THR A 384      -9.035  23.234 -66.965  1.00 29.43           C  
ANISOU 1668  CB  THR A 384     4038   3840   3306    340    702    130       C  
ATOM   1669  OG1 THR A 384      -7.712  22.692 -67.126  1.00 33.81           O  
ANISOU 1669  OG1 THR A 384     4618   4396   3831    374    823    119       O  
ATOM   1670  CG2 THR A 384      -9.677  23.464 -68.275  1.00 28.82           C  
ANISOU 1670  CG2 THR A 384     4102   3716   3132    337    645    160       C  
ATOM   1671  N   GLY A 385      -7.230  26.141 -66.223  1.00 18.23           N  
ANISOU 1671  N   GLY A 385     2419   2452   2055    341    889    180       N  
ATOM   1672  CA  GLY A 385      -6.004  26.882 -65.901  1.00 17.09           C  
ANISOU 1672  CA  GLY A 385     2201   2320   1973    343    994    196       C  
ATOM   1673  C   GLY A 385      -6.050  27.600 -64.560  1.00 20.00           C  
ANISOU 1673  C   GLY A 385     2424   2718   2456    314    975    177       C  
ATOM   1674  O   GLY A 385      -5.022  27.744 -63.891  1.00 18.36           O  
ANISOU 1674  O   GLY A 385     2133   2533   2309    308   1041    173       O  
ATOM   1675  N   ILE A 386      -7.255  28.045 -64.149  1.00 17.07           N  
ANISOU 1675  N   ILE A 386     2024   2344   2119    295    885    166       N  
ATOM   1676  CA  ILE A 386      -7.497  28.699 -62.867  1.00 16.08           C  
ANISOU 1676  CA  ILE A 386     1780   2240   2090    269    865    141       C  
ATOM   1677  C   ILE A 386      -7.152  27.707 -61.746  1.00 19.95           C  
ANISOU 1677  C   ILE A 386     2203   2776   2601    262    868    100       C  
ATOM   1678  O   ILE A 386      -6.477  28.071 -60.782  1.00 19.50           O  
ANISOU 1678  O   ILE A 386     2060   2742   2606    243    902     84       O  
ATOM   1679  CB  ILE A 386      -8.949  29.308 -62.750  1.00 17.69           C  
ANISOU 1679  CB  ILE A 386     1970   2423   2326    260    778    142       C  
ATOM   1680  CG1 ILE A 386      -9.108  30.512 -63.719  1.00 18.31           C  
ANISOU 1680  CG1 ILE A 386     2099   2453   2405    265    781    190       C  
ATOM   1681  CG2 ILE A 386      -9.266  29.757 -61.282  1.00 14.26           C  
ANISOU 1681  CG2 ILE A 386     1422   2012   1982    238    768    103       C  
ATOM   1682  CD1 ILE A 386     -10.535  30.987 -63.973  1.00 20.61           C  
ANISOU 1682  CD1 ILE A 386     2399   2715   2717    267    690    210       C  
ATOM   1683  N   ILE A 387      -7.555  26.446 -61.926  1.00 17.16           N  
ANISOU 1683  N   ILE A 387     1897   2432   2192    275    831     87       N  
ATOM   1684  CA  ILE A 387      -7.309  25.343 -60.995  1.00 16.13           C  
ANISOU 1684  CA  ILE A 387     1718   2339   2071    271    827     56       C  
ATOM   1685  C   ILE A 387      -5.853  24.878 -61.015  1.00 17.32           C  
ANISOU 1685  C   ILE A 387     1859   2503   2221    288    913     63       C  
ATOM   1686  O   ILE A 387      -5.230  24.780 -59.953  1.00 16.29           O  
ANISOU 1686  O   ILE A 387     1639   2406   2145    273    930     50       O  
ATOM   1687  CB  ILE A 387      -8.364  24.200 -61.204  1.00 19.91           C  
ANISOU 1687  CB  ILE A 387     2252   2814   2500    275    749     44       C  
ATOM   1688  CG1 ILE A 387      -9.774  24.708 -60.830  1.00 19.89           C  
ANISOU 1688  CG1 ILE A 387     2213   2809   2536    254    668     40       C  
ATOM   1689  CG2 ILE A 387      -8.021  22.917 -60.412  1.00 22.24           C  
ANISOU 1689  CG2 ILE A 387     2516   3139   2795    276    752     19       C  
ATOM   1690  CD1 ILE A 387     -10.854  23.615 -60.617  1.00 30.67           C  
ANISOU 1690  CD1 ILE A 387     3586   4179   3887    244    586     29       C  
ATOM   1691  N   VAL A 388      -5.312  24.618 -62.213  1.00 14.16           N  
ANISOU 1691  N   VAL A 388     1549   2073   1759    319    968     89       N  
ATOM   1692  CA  VAL A 388      -3.959  24.098 -62.430  1.00 14.85           C  
ANISOU 1692  CA  VAL A 388     1633   2163   1846    347   1064    104       C  
ATOM   1693  C   VAL A 388      -2.876  25.066 -61.967  1.00 20.20           C  
ANISOU 1693  C   VAL A 388     2213   2856   2607    331   1129    127       C  
ATOM   1694  O   VAL A 388      -1.921  24.658 -61.284  1.00 18.00           O  
ANISOU 1694  O   VAL A 388     1855   2604   2382    332   1167    129       O  
ATOM   1695  CB  VAL A 388      -3.780  23.590 -63.893  1.00 19.32           C  
ANISOU 1695  CB  VAL A 388     2340   2688   2315    388   1115    123       C  
ATOM   1696  CG1 VAL A 388      -2.337  23.171 -64.197  1.00 18.85           C  
ANISOU 1696  CG1 VAL A 388     2273   2625   2265    425   1238    145       C  
ATOM   1697  CG2 VAL A 388      -4.744  22.445 -64.187  1.00 18.77           C  
ANISOU 1697  CG2 VAL A 388     2362   2602   2169    395   1039     95       C  
ATOM   1698  N   LYS A 389      -3.051  26.359 -62.299  1.00 18.66           N  
ANISOU 1698  N   LYS A 389     2020   2641   2431    312   1133    146       N  
ATOM   1699  CA  LYS A 389      -2.099  27.388 -61.889  1.00 18.53           C  
ANISOU 1699  CA  LYS A 389     1915   2628   2496    288   1185    169       C  
ATOM   1700  C   LYS A 389      -2.478  27.967 -60.536  1.00 21.85           C  
ANISOU 1700  C   LYS A 389     2241   3073   2987    242   1119    136       C  
ATOM   1701  O   LYS A 389      -1.672  28.686 -59.959  1.00 21.97           O  
ANISOU 1701  O   LYS A 389     2179   3094   3075    212   1145    145       O  
ATOM   1702  CB  LYS A 389      -1.970  28.493 -62.953  1.00 20.64           C  
ANISOU 1702  CB  LYS A 389     2237   2854   2750    290   1231    212       C  
ATOM   1703  CG  LYS A 389      -1.532  27.979 -64.313  1.00 21.53           C  
ANISOU 1703  CG  LYS A 389     2459   2941   2781    334   1310    246       C  
ATOM   1704  CD  LYS A 389      -0.048  27.681 -64.354  1.00 19.75           C  
ANISOU 1704  CD  LYS A 389     2180   2726   2600    352   1422    278       C  
ATOM   1705  CE  LYS A 389       0.390  27.088 -65.668  1.00 17.44           C  
ANISOU 1705  CE  LYS A 389     2002   2404   2221    404   1518    307       C  
ATOM   1706  NZ  LYS A 389       1.817  26.705 -65.598  1.00 31.41           N  
ANISOU 1706  NZ  LYS A 389     3700   4184   4052    428   1633    340       N  
ATOM   1707  N   SER A 390      -3.681  27.630 -60.013  1.00 17.69           N  
ANISOU 1707  N   SER A 390     1724   2558   2440    235   1037     97       N  
ATOM   1708  CA  SER A 390      -4.180  28.139 -58.721  1.00 18.08           C  
ANISOU 1708  CA  SER A 390     1700   2626   2543    197    984     60       C  
ATOM   1709  C   SER A 390      -4.215  29.715 -58.685  1.00 23.88           C  
ANISOU 1709  C   SER A 390     2414   3329   3330    170    992     67       C  
ATOM   1710  O   SER A 390      -3.672  30.369 -57.772  1.00 22.07           O  
ANISOU 1710  O   SER A 390     2118   3107   3161    133    998     53       O  
ATOM   1711  CB  SER A 390      -3.402  27.538 -57.553  1.00 19.73           C  
ANISOU 1711  CB  SER A 390     1831   2879   2788    176    984     43       C  
ATOM   1712  OG  SER A 390      -4.147  27.710 -56.361  1.00 26.02           O  
ANISOU 1712  OG  SER A 390     2588   3696   3604    146    926      1       O  
ATOM   1713  N   SER A 391      -4.885  30.298 -59.705  1.00 20.00           N  
ANISOU 1713  N   SER A 391     1990   2797   2813    188    987     90       N  
ATOM   1714  CA  SER A 391      -5.024  31.740 -59.839  1.00 19.05           C  
ANISOU 1714  CA  SER A 391     1864   2635   2738    171    994    103       C  
ATOM   1715  C   SER A 391      -6.062  32.298 -58.853  1.00 20.55           C  
ANISOU 1715  C   SER A 391     2016   2820   2972    154    939     61       C  
ATOM   1716  O   SER A 391      -7.218  31.852 -58.847  1.00 18.95           O  
ANISOU 1716  O   SER A 391     1832   2621   2745    171    887     48       O  
ATOM   1717  CB  SER A 391      -5.397  32.101 -61.274  1.00 21.07           C  
ANISOU 1717  CB  SER A 391     2209   2849   2948    198   1001    150       C  
ATOM   1718  OG  SER A 391      -5.518  33.501 -61.471  1.00 27.59           O  
ANISOU 1718  OG  SER A 391     3032   3628   3823    184   1009    171       O  
ATOM   1719  N   ASN A 392      -5.646  33.290 -58.043  1.00 16.48           N  
ANISOU 1719  N   ASN A 392     1449   2291   2521    119    954     41       N  
ATOM   1720  CA  ASN A 392      -6.523  33.981 -57.095  1.00 17.32           C  
ANISOU 1720  CA  ASN A 392     1528   2382   2671    104    922     -3       C  
ATOM   1721  C   ASN A 392      -7.278  35.042 -57.868  1.00 20.79           C  
ANISOU 1721  C   ASN A 392     2003   2760   3135    123    917     24       C  
ATOM   1722  O   ASN A 392      -8.370  35.431 -57.475  1.00 21.28           O  
ANISOU 1722  O   ASN A 392     2059   2803   3225    134    888      3       O  
ATOM   1723  CB  ASN A 392      -5.708  34.668 -55.973  1.00 21.28           C  
ANISOU 1723  CB  ASN A 392     1980   2883   3225     55    939    -37       C  
ATOM   1724  CG  ASN A 392      -4.882  33.745 -55.122  1.00 38.06           C  
ANISOU 1724  CG  ASN A 392     4062   5064   5335     30    934    -56       C  
ATOM   1725  OD1 ASN A 392      -5.359  32.733 -54.612  1.00 35.44           O  
ANISOU 1725  OD1 ASN A 392     3724   4774   4966     40    906    -79       O  
ATOM   1726  ND2 ASN A 392      -3.618  34.078 -54.950  1.00 34.46           N  
ANISOU 1726  ND2 ASN A 392     3571   4608   4915     -7    956    -41       N  
ATOM   1727  N   VAL A 393      -6.670  35.519 -58.959  1.00 17.37           N  
ANISOU 1727  N   VAL A 393     1608   2297   2697    127    950     77       N  
ATOM   1728  CA  VAL A 393      -7.200  36.573 -59.824  1.00 17.14           C  
ANISOU 1728  CA  VAL A 393     1620   2205   2689    143    948    117       C  
ATOM   1729  C   VAL A 393      -8.320  35.987 -60.651  1.00 19.80           C  
ANISOU 1729  C   VAL A 393     2008   2541   2974    182    896    143       C  
ATOM   1730  O   VAL A 393      -9.378  36.601 -60.747  1.00 19.44           O  
ANISOU 1730  O   VAL A 393     1966   2458   2963    198    858    151       O  
ATOM   1731  CB  VAL A 393      -6.084  37.255 -60.691  1.00 18.72           C  
ANISOU 1731  CB  VAL A 393     1845   2373   2895    130   1006    171       C  
ATOM   1732  CG1 VAL A 393      -6.672  38.242 -61.695  1.00 17.47           C  
ANISOU 1732  CG1 VAL A 393     1742   2150   2747    148    998    223       C  
ATOM   1733  CG2 VAL A 393      -5.057  37.934 -59.807  1.00 18.33           C  
ANISOU 1733  CG2 VAL A 393     1735   2316   2913     81   1041    148       C  
ATOM   1734  N   GLY A 394      -8.067  34.826 -61.257  1.00 15.54           N  
ANISOU 1734  N   GLY A 394     1510   2038   2356    196    894    158       N  
ATOM   1735  CA  GLY A 394      -9.075  34.136 -62.048  1.00 14.73           C  
ANISOU 1735  CA  GLY A 394     1466   1936   2195    224    834    180       C  
ATOM   1736  C   GLY A 394     -10.287  33.794 -61.208  1.00 15.82           C  
ANISOU 1736  C   GLY A 394     1554   2089   2366    228    772    144       C  
ATOM   1737  O   GLY A 394     -11.410  33.964 -61.650  1.00 14.01           O  
ANISOU 1737  O   GLY A 394     1342   1834   2146    245    713    169       O  
ATOM   1738  N   SER A 395     -10.052  33.332 -59.974  1.00 16.11           N  
ANISOU 1738  N   SER A 395     1527   2167   2425    211    787     90       N  
ATOM   1739  CA  SER A 395     -11.083  32.919 -59.028  1.00 16.49           C  
ANISOU 1739  CA  SER A 395     1524   2237   2503    212    747     54       C  
ATOM   1740  C   SER A 395     -11.983  34.083 -58.640  1.00 20.65           C  
ANISOU 1740  C   SER A 395     2016   2721   3111    220    740     50       C  
ATOM   1741  O   SER A 395     -13.202  33.953 -58.732  1.00 21.42           O  
ANISOU 1741  O   SER A 395     2099   2808   3232    240    690     64       O  
ATOM   1742  CB  SER A 395     -10.450  32.272 -57.796  1.00 20.47           C  
ANISOU 1742  CB  SER A 395     1980   2793   3005    188    774      3       C  
ATOM   1743  OG  SER A 395      -9.896  31.011 -58.120  1.00 23.57           O  
ANISOU 1743  OG  SER A 395     2400   3223   3332    190    772      9       O  
ATOM   1744  N   ALA A 396     -11.384  35.221 -58.259  1.00 16.95           N  
ANISOU 1744  N   ALA A 396     1530   2219   2690    205    788     36       N  
ATOM   1745  CA  ALA A 396     -12.097  36.440 -57.898  1.00 18.59           C  
ANISOU 1745  CA  ALA A 396     1713   2371   2979    216    794     29       C  
ATOM   1746  C   ALA A 396     -12.944  36.955 -59.074  1.00 24.23           C  
ANISOU 1746  C   ALA A 396     2458   3034   3712    249    751     94       C  
ATOM   1747  O   ALA A 396     -14.111  37.299 -58.869  1.00 24.62           O  
ANISOU 1747  O   ALA A 396     2474   3057   3824    274    725    100       O  
ATOM   1748  CB  ALA A 396     -11.117  37.508 -57.441  1.00 19.65           C  
ANISOU 1748  CB  ALA A 396     1842   2472   3150    187    848      5       C  
ATOM   1749  N   LYS A 397     -12.376  36.961 -60.303  1.00 19.65           N  
ANISOU 1749  N   LYS A 397     1943   2442   3080    249    745    147       N  
ATOM   1750  CA  LYS A 397     -13.080  37.383 -61.522  1.00 19.06           C  
ANISOU 1750  CA  LYS A 397     1916   2321   3004    274    694    217       C  
ATOM   1751  C   LYS A 397     -14.306  36.517 -61.809  1.00 22.43           C  
ANISOU 1751  C   LYS A 397     2340   2766   3416    294    611    237       C  
ATOM   1752  O   LYS A 397     -15.324  37.056 -62.229  1.00 22.50           O  
ANISOU 1752  O   LYS A 397     2341   2732   3477    316    558    282       O  
ATOM   1753  CB  LYS A 397     -12.128  37.437 -62.726  1.00 20.22           C  
ANISOU 1753  CB  LYS A 397     2147   2458   3079    267    714    266       C  
ATOM   1754  CG  LYS A 397     -11.185  38.613 -62.611  1.00 16.21           C  
ANISOU 1754  CG  LYS A 397     1633   1909   2615    249    784    270       C  
ATOM   1755  CD  LYS A 397     -10.599  39.052 -63.911  1.00 12.84           C  
ANISOU 1755  CD  LYS A 397     1287   1450   2143    249    801    339       C  
ATOM   1756  CE  LYS A 397      -9.627  40.167 -63.654  1.00 16.07           C  
ANISOU 1756  CE  LYS A 397     1676   1819   2609    223    872    341       C  
ATOM   1757  NZ  LYS A 397     -10.073  41.436 -64.277  1.00 34.03           N  
ANISOU 1757  NZ  LYS A 397     3979   4015   4936    235    858    397       N  
ATOM   1758  N   LEU A 398     -14.232  35.192 -61.537  1.00 19.09           N  
ANISOU 1758  N   LEU A 398     1917   2403   2934    283    595    209       N  
ATOM   1759  CA  LEU A 398     -15.387  34.291 -61.691  1.00 19.23           C  
ANISOU 1759  CA  LEU A 398     1925   2438   2945    292    512    225       C  
ATOM   1760  C   LEU A 398     -16.514  34.725 -60.760  1.00 23.95           C  
ANISOU 1760  C   LEU A 398     2427   3022   3650    307    503    211       C  
ATOM   1761  O   LEU A 398     -17.652  34.852 -61.211  1.00 23.23           O  
ANISOU 1761  O   LEU A 398     2317   2903   3605    325    433    259       O  
ATOM   1762  CB  LEU A 398     -15.033  32.813 -61.416  1.00 18.23           C  
ANISOU 1762  CB  LEU A 398     1812   2371   2743    275    507    190       C  
ATOM   1763  CG  LEU A 398     -14.154  32.098 -62.436  1.00 22.36           C  
ANISOU 1763  CG  LEU A 398     2435   2905   3154    269    509    207       C  
ATOM   1764  CD1 LEU A 398     -13.822  30.694 -61.965  1.00 21.49           C  
ANISOU 1764  CD1 LEU A 398     2326   2847   2992    257    512    168       C  
ATOM   1765  CD2 LEU A 398     -14.816  32.046 -63.810  1.00 24.05           C  
ANISOU 1765  CD2 LEU A 398     2735   3083   3319    277    427    270       C  
ATOM   1766  N   ALA A 399     -16.174  35.011 -59.472  1.00 21.16           N  
ANISOU 1766  N   ALA A 399     2016   2685   3339    300    576    148       N  
ATOM   1767  CA  ALA A 399     -17.102  35.479 -58.441  1.00 20.11           C  
ANISOU 1767  CA  ALA A 399     1801   2537   3303    317    597    123       C  
ATOM   1768  C   ALA A 399     -17.796  36.726 -58.891  1.00 22.52           C  
ANISOU 1768  C   ALA A 399     2091   2769   3696    349    587    168       C  
ATOM   1769  O   ALA A 399     -19.017  36.789 -58.813  1.00 23.01           O  
ANISOU 1769  O   ALA A 399     2096   2813   3834    376    551    197       O  
ATOM   1770  CB  ALA A 399     -16.362  35.739 -57.138  1.00 20.77           C  
ANISOU 1770  CB  ALA A 399     1860   2639   3391    298    681     48       C  
ATOM   1771  N   LEU A 400     -17.031  37.688 -59.447  1.00 18.93           N  
ANISOU 1771  N   LEU A 400     1686   2271   3237    347    613    183       N  
ATOM   1772  CA  LEU A 400     -17.547  38.967 -59.934  1.00 18.59           C  
ANISOU 1772  CA  LEU A 400     1638   2149   3276    377    606    230       C  
ATOM   1773  C   LEU A 400     -18.557  38.897 -61.068  1.00 22.80           C  
ANISOU 1773  C   LEU A 400     2179   2655   3828    401    507    317       C  
ATOM   1774  O   LEU A 400     -19.492  39.714 -61.107  1.00 22.48           O  
ANISOU 1774  O   LEU A 400     2092   2558   3893    436    490    355       O  
ATOM   1775  CB  LEU A 400     -16.422  39.936 -60.262  1.00 18.51           C  
ANISOU 1775  CB  LEU A 400     1682   2098   3252    361    656    231       C  
ATOM   1776  CG  LEU A 400     -15.615  40.486 -59.077  1.00 23.87           C  
ANISOU 1776  CG  LEU A 400     2343   2772   3954    338    744    153       C  
ATOM   1777  CD1 LEU A 400     -14.972  41.815 -59.457  1.00 24.44           C  
ANISOU 1777  CD1 LEU A 400     2450   2771   4063    332    779    172       C  
ATOM   1778  CD2 LEU A 400     -16.492  40.671 -57.779  1.00 25.02           C  
ANISOU 1778  CD2 LEU A 400     2419   2910   4177    358    780     95       C  
ATOM   1779  N   SER A 401     -18.378  37.918 -61.972  1.00 19.06           N  
ANISOU 1779  N   SER A 401     1768   2219   3253    381    442    350       N  
ATOM   1780  CA  SER A 401     -19.233  37.691 -63.145  1.00 19.32           C  
ANISOU 1780  CA  SER A 401     1832   2232   3276    391    329    433       C  
ATOM   1781  C   SER A 401     -20.554  36.971 -62.835  1.00 22.44           C  
ANISOU 1781  C   SER A 401     2149   2646   3731    400    257    449       C  
ATOM   1782  O   SER A 401     -21.545  37.126 -63.554  1.00 20.30           O  
ANISOU 1782  O   SER A 401     1864   2340   3508    415    161    525       O  
ATOM   1783  CB  SER A 401     -18.468  36.896 -64.190  1.00 22.06           C  
ANISOU 1783  CB  SER A 401     2294   2607   3480    363    295    451       C  
ATOM   1784  OG  SER A 401     -18.277  35.556 -63.760  1.00 32.77           O  
ANISOU 1784  OG  SER A 401     3651   4029   4772    342    294    403       O  
ATOM   1785  N   LEU A 402     -20.546  36.166 -61.782  1.00 20.08           N  
ANISOU 1785  N   LEU A 402     1799   2401   3431    389    298    386       N  
ATOM   1786  CA  LEU A 402     -21.690  35.359 -61.373  1.00 20.02           C  
ANISOU 1786  CA  LEU A 402     1712   2418   3477    390    244    398       C  
ATOM   1787  C   LEU A 402     -22.693  36.145 -60.534  1.00 26.64           C  
ANISOU 1787  C   LEU A 402     2433   3221   4467    430    282    403       C  
ATOM   1788  O   LEU A 402     -22.304  37.152 -59.921  1.00 27.53           O  
ANISOU 1788  O   LEU A 402     2532   3303   4625    450    376    365       O  
ATOM   1789  CB  LEU A 402     -21.193  34.160 -60.553  1.00 18.73           C  
ANISOU 1789  CB  LEU A 402     1547   2324   3244    361    282    330       C  
ATOM   1790  CG  LEU A 402     -20.321  33.148 -61.258  1.00 23.17           C  
ANISOU 1790  CG  LEU A 402     2213   2923   3668    328    250    321       C  
ATOM   1791  CD1 LEU A 402     -19.559  32.308 -60.258  1.00 22.48           C  
ANISOU 1791  CD1 LEU A 402     2117   2894   3529    307    319    247       C  
ATOM   1792  CD2 LEU A 402     -21.108  32.315 -62.219  1.00 26.85           C  
ANISOU 1792  CD2 LEU A 402     2712   3387   4104    314    123    379       C  
ATOM   1793  N   PRO A 403     -23.972  35.664 -60.422  1.00 23.67           N  
ANISOU 1793  N   PRO A 403     1970   2849   4174    440    219    447       N  
ATOM   1794  CA  PRO A 403     -24.933  36.314 -59.502  1.00 23.95           C  
ANISOU 1794  CA  PRO A 403     1884   2854   4361    483    279    448       C  
ATOM   1795  C   PRO A 403     -24.390  36.302 -58.060  1.00 28.52           C  
ANISOU 1795  C   PRO A 403     2443   3465   4928    482    416    350       C  
ATOM   1796  O   PRO A 403     -23.647  35.390 -57.687  1.00 27.39           O  
ANISOU 1796  O   PRO A 403     2343   3382   4681    444    434    296       O  
ATOM   1797  CB  PRO A 403     -26.173  35.423 -59.616  1.00 25.49           C  
ANISOU 1797  CB  PRO A 403     1996   3069   4620    477    187    507       C  
ATOM   1798  CG  PRO A 403     -26.049  34.788 -60.955  1.00 29.93           C  
ANISOU 1798  CG  PRO A 403     2645   3637   5089    440     49    562       C  
ATOM   1799  CD  PRO A 403     -24.588  34.488 -61.066  1.00 24.52           C  
ANISOU 1799  CD  PRO A 403     2083   2985   4248    410     97    495       C  
ATOM   1800  N   LYS A 404     -24.713  37.345 -57.282  1.00 26.89           N  
ANISOU 1800  N   LYS A 404     2181   3212   4825    525    510    326       N  
ATOM   1801  CA  LYS A 404     -24.277  37.566 -55.896  1.00 27.13           C  
ANISOU 1801  CA  LYS A 404     2205   3256   4847    527    641    233       C  
ATOM   1802  C   LYS A 404     -24.461  36.335 -54.991  1.00 31.95           C  
ANISOU 1802  C   LYS A 404     2780   3941   5417    501    664    195       C  
ATOM   1803  O   LYS A 404     -23.611  36.044 -54.146  1.00 30.54           O  
ANISOU 1803  O   LYS A 404     2646   3803   5156    472    730    118       O  
ATOM   1804  CB  LYS A 404     -25.056  38.766 -55.313  1.00 31.36           C  
ANISOU 1804  CB  LYS A 404     2672   3718   5524    588    725    232       C  
ATOM   1805  CG  LYS A 404     -24.192  39.741 -54.536  1.00 44.73           C  
ANISOU 1805  CG  LYS A 404     4424   5377   7195    590    837    146       C  
ATOM   1806  CD  LYS A 404     -24.711  39.951 -53.128  1.00 54.91           C  
ANISOU 1806  CD  LYS A 404     5663   6656   8544    620    960     85       C  
ATOM   1807  CE  LYS A 404     -23.863  40.936 -52.364  1.00 72.60           C  
ANISOU 1807  CE  LYS A 404     7977   8854  10754    615   1059     -4       C  
ATOM   1808  NZ  LYS A 404     -22.595  40.320 -51.895  1.00 87.97           N  
ANISOU 1808  NZ  LYS A 404    10002  10867  12555    548   1064    -74       N  
ATOM   1809  N   GLU A 405     -25.580  35.626 -55.168  1.00 30.90           N  
ANISOU 1809  N   GLU A 405     2567   3824   5350    507    603    256       N  
ATOM   1810  CA  GLU A 405     -25.922  34.441 -54.380  1.00 31.32           C  
ANISOU 1810  CA  GLU A 405     2577   3941   5382    481    617    237       C  
ATOM   1811  C   GLU A 405     -25.080  33.226 -54.722  1.00 35.34           C  
ANISOU 1811  C   GLU A 405     3164   4514   5752    424    552    219       C  
ATOM   1812  O   GLU A 405     -24.952  32.363 -53.861  1.00 37.26           O  
ANISOU 1812  O   GLU A 405     3397   4809   5951    399    590    179       O  
ATOM   1813  CB  GLU A 405     -27.414  34.081 -54.534  1.00 33.36           C  
ANISOU 1813  CB  GLU A 405     2715   4190   5769    502    565    319       C  
ATOM   1814  CG  GLU A 405     -28.376  35.197 -54.177  1.00 45.61           C  
ANISOU 1814  CG  GLU A 405     4171   5678   7481    568    636    347       C  
ATOM   1815  CD  GLU A 405     -29.164  35.688 -55.374  1.00 72.97           C  
ANISOU 1815  CD  GLU A 405     7587   9087  11051    594    526    451       C  
ATOM   1816  OE1 GLU A 405     -30.393  35.442 -55.414  1.00 65.56           O  
ANISOU 1816  OE1 GLU A 405     6528   8138  10242    613    489    525       O  
ATOM   1817  OE2 GLU A 405     -28.545  36.275 -56.294  1.00 64.87           O  
ANISOU 1817  OE2 GLU A 405     6642   8027   9977    592    469    464       O  
ATOM   1818  N   ALA A 406     -24.538  33.132 -55.967  1.00 29.27           N  
ANISOU 1818  N   ALA A 406     2472   3735   4914    406    459    251       N  
ATOM   1819  CA  ALA A 406     -23.782  31.976 -56.466  1.00 27.94           C  
ANISOU 1819  CA  ALA A 406     2384   3614   4618    359    396    241       C  
ATOM   1820  C   ALA A 406     -22.905  31.163 -55.498  1.00 27.38           C  
ANISOU 1820  C   ALA A 406     2342   3603   4457    328    461    167       C  
ATOM   1821  O   ALA A 406     -23.203  29.989 -55.241  1.00 28.16           O  
ANISOU 1821  O   ALA A 406     2422   3744   4534    303    429    171       O  
ATOM   1822  CB  ALA A 406     -23.026  32.314 -57.742  1.00 28.79           C  
ANISOU 1822  CB  ALA A 406     2592   3696   4651    353    338    264       C  
ATOM   1823  N   LEU A 407     -21.857  31.770 -54.965  1.00 19.84           N  
ANISOU 1823  N   LEU A 407     1431   2651   3456    328    544    105       N  
ATOM   1824  CA  LEU A 407     -20.915  31.079 -54.080  1.00 18.65           C  
ANISOU 1824  CA  LEU A 407     1311   2554   3219    296    595     41       C  
ATOM   1825  C   LEU A 407     -21.439  30.687 -52.708  1.00 22.83           C  
ANISOU 1825  C   LEU A 407     1780   3117   3779    293    659      8       C  
ATOM   1826  O   LEU A 407     -21.313  29.500 -52.402  1.00 23.54           O  
ANISOU 1826  O   LEU A 407     1873   3255   3814    264    638      2       O  
ATOM   1827  CB  LEU A 407     -19.537  31.766 -53.973  1.00 18.16           C  
ANISOU 1827  CB  LEU A 407     1315   2486   3097    286    648     -7       C  
ATOM   1828  CG  LEU A 407     -18.829  32.132 -55.266  1.00 22.60           C  
ANISOU 1828  CG  LEU A 407     1946   3020   3619    286    605     24       C  
ATOM   1829  CD1 LEU A 407     -17.485  32.706 -54.964  1.00 23.74           C  
ANISOU 1829  CD1 LEU A 407     2136   3166   3720    270    666    -22       C  
ATOM   1830  CD2 LEU A 407     -18.663  30.928 -56.162  1.00 24.54           C  
ANISOU 1830  CD2 LEU A 407     2239   3294   3790    268    528     56       C  
ATOM   1831  N   PRO A 408     -22.008  31.601 -51.858  1.00 18.46           N  
ANISOU 1831  N   PRO A 408     1176   2535   3302    322    743    -14       N  
ATOM   1832  CA  PRO A 408     -22.503  31.158 -50.542  1.00 17.99           C  
ANISOU 1832  CA  PRO A 408     1070   2509   3255    318    814    -45       C  
ATOM   1833  C   PRO A 408     -23.563  30.072 -50.649  1.00 22.52           C  
ANISOU 1833  C   PRO A 408     1575   3108   3872    312    762     11       C  
ATOM   1834  O   PRO A 408     -23.694  29.278 -49.729  1.00 22.85           O  
ANISOU 1834  O   PRO A 408     1599   3195   3887    291    798     -7       O  
ATOM   1835  CB  PRO A 408     -23.103  32.442 -49.933  1.00 20.01           C  
ANISOU 1835  CB  PRO A 408     1289   2711   3602    363    908    -66       C  
ATOM   1836  CG  PRO A 408     -22.460  33.562 -50.651  1.00 23.61           C  
ANISOU 1836  CG  PRO A 408     1795   3113   4061    376    898    -72       C  
ATOM   1837  CD  PRO A 408     -22.258  33.052 -52.046  1.00 19.26           C  
ANISOU 1837  CD  PRO A 408     1266   2568   3482    362    782    -11       C  
ATOM   1838  N   SER A 409     -24.337  30.073 -51.750  1.00 19.76           N  
ANISOU 1838  N   SER A 409     1189   2729   3592    326    675     84       N  
ATOM   1839  CA  SER A 409     -25.398  29.111 -52.012  1.00 20.01           C  
ANISOU 1839  CA  SER A 409     1150   2774   3677    314    604    148       C  
ATOM   1840  C   SER A 409     -24.820  27.789 -52.499  1.00 20.84           C  
ANISOU 1840  C   SER A 409     1318   2920   3679    266    518    151       C  
ATOM   1841  O   SER A 409     -25.296  26.744 -52.051  1.00 19.58           O  
ANISOU 1841  O   SER A 409     1121   2794   3525    240    505    165       O  
ATOM   1842  CB  SER A 409     -26.408  29.657 -53.013  1.00 26.65           C  
ANISOU 1842  CB  SER A 409     1932   3562   4630    342    528    228       C  
ATOM   1843  OG  SER A 409     -27.472  28.732 -53.170  1.00 40.50           O  
ANISOU 1843  OG  SER A 409     3611   5330   6449    323    455    293       O  
ATOM   1844  N   PHE A 410     -23.809  27.816 -53.407  1.00 15.19           N  
ANISOU 1844  N   PHE A 410      699   2198   2875    255    467    139       N  
ATOM   1845  CA  PHE A 410     -23.224  26.546 -53.819  1.00 15.16           C  
ANISOU 1845  CA  PHE A 410      761   2226   2773    216    401    136       C  
ATOM   1846  C   PHE A 410     -22.412  25.934 -52.665  1.00 20.26           C  
ANISOU 1846  C   PHE A 410     1426   2923   3348    195    475     76       C  
ATOM   1847  O   PHE A 410     -22.497  24.732 -52.460  1.00 22.60           O  
ANISOU 1847  O   PHE A 410     1724   3249   3613    166    442     83       O  
ATOM   1848  CB  PHE A 410     -22.402  26.621 -55.131  1.00 15.79           C  
ANISOU 1848  CB  PHE A 410      942   2284   2774    212    336    144       C  
ATOM   1849  CG  PHE A 410     -21.872  25.255 -55.493  1.00 15.84           C  
ANISOU 1849  CG  PHE A 410     1017   2316   2687    178    281    138       C  
ATOM   1850  CD1 PHE A 410     -22.746  24.208 -55.793  1.00 17.57           C  
ANISOU 1850  CD1 PHE A 410     1217   2534   2925    153    192    180       C  
ATOM   1851  CD2 PHE A 410     -20.506  24.968 -55.390  1.00 16.32           C  
ANISOU 1851  CD2 PHE A 410     1151   2399   2649    171    324     91       C  
ATOM   1852  CE1 PHE A 410     -22.266  22.917 -56.022  1.00 17.33           C  
ANISOU 1852  CE1 PHE A 410     1254   2520   2810    123    149    168       C  
ATOM   1853  CE2 PHE A 410     -20.028  23.679 -55.632  1.00 17.68           C  
ANISOU 1853  CE2 PHE A 410     1382   2591   2745    147    285     84       C  
ATOM   1854  CZ  PHE A 410     -20.910  22.662 -55.947  1.00 16.30           C  
ANISOU 1854  CZ  PHE A 410     1200   2410   2584    124    200    120       C  
ATOM   1855  N   PHE A 411     -21.698  26.763 -51.881  1.00 15.15           N  
ANISOU 1855  N   PHE A 411      793   2282   2683    207    568     21       N  
ATOM   1856  CA  PHE A 411     -20.897  26.317 -50.734  1.00 14.16           C  
ANISOU 1856  CA  PHE A 411      688   2202   2489    184    631    -33       C  
ATOM   1857  C   PHE A 411     -21.749  25.702 -49.609  1.00 19.63           C  
ANISOU 1857  C   PHE A 411     1317   2925   3215    174    672    -30       C  
ATOM   1858  O   PHE A 411     -21.291  24.771 -48.938  1.00 21.17           O  
ANISOU 1858  O   PHE A 411     1533   3164   3348    145    680    -48       O  
ATOM   1859  CB  PHE A 411     -19.975  27.438 -50.210  1.00 15.17           C  
ANISOU 1859  CB  PHE A 411      851   2321   2593    192    706    -89       C  
ATOM   1860  CG  PHE A 411     -18.858  27.936 -51.114  1.00 16.11           C  
ANISOU 1860  CG  PHE A 411     1036   2420   2666    192    683    -96       C  
ATOM   1861  CD1 PHE A 411     -17.971  28.909 -50.675  1.00 17.32           C  
ANISOU 1861  CD1 PHE A 411     1218   2562   2803    190    740   -142       C  
ATOM   1862  CD2 PHE A 411     -18.660  27.393 -52.385  1.00 17.63           C  
ANISOU 1862  CD2 PHE A 411     1267   2603   2828    191    605    -57       C  
ATOM   1863  CE1 PHE A 411     -16.948  29.380 -51.511  1.00 17.41           C  
ANISOU 1863  CE1 PHE A 411     1280   2553   2783    189    725   -140       C  
ATOM   1864  CE2 PHE A 411     -17.662  27.886 -53.229  1.00 19.41           C  
ANISOU 1864  CE2 PHE A 411     1553   2809   3014    195    599    -58       C  
ATOM   1865  CZ  PHE A 411     -16.797  28.861 -52.778  1.00 17.12           C  
ANISOU 1865  CZ  PHE A 411     1276   2509   2719    193    661    -96       C  
ATOM   1866  N   ARG A 412     -22.994  26.175 -49.451  1.00 15.71           N  
ANISOU 1866  N   ARG A 412      742   2404   2822    199    696      2       N  
ATOM   1867  CA  ARG A 412     -23.962  25.669 -48.482  1.00 15.54           C  
ANISOU 1867  CA  ARG A 412      648   2405   2852    194    745     18       C  
ATOM   1868  C   ARG A 412     -24.454  24.276 -48.921  1.00 20.36           C  
ANISOU 1868  C   ARG A 412     1235   3035   3466    161    653     72       C  
ATOM   1869  O   ARG A 412     -24.568  23.395 -48.090  1.00 20.39           O  
ANISOU 1869  O   ARG A 412     1226   3076   3446    135    679     71       O  
ATOM   1870  CB  ARG A 412     -25.155  26.642 -48.370  1.00 16.08           C  
ANISOU 1870  CB  ARG A 412      656   2417   3036    234    784     48       C  
ATOM   1871  CG  ARG A 412     -26.057  26.410 -47.163  1.00 17.24           C  
ANISOU 1871  CG  ARG A 412      702   2599   3249    244    892     53       C  
ATOM   1872  CD  ARG A 412     -27.290  27.285 -47.196  1.00 26.90           C  
ANISOU 1872  CD  ARG A 412     1827   3776   4619    294    941     94       C  
ATOM   1873  NE  ARG A 412     -28.256  26.867 -46.175  1.00 30.64           N  
ANISOU 1873  NE  ARG A 412     2219   4270   5154    298   1029    116       N  
ATOM   1874  CZ  ARG A 412     -29.049  27.695 -45.502  1.00 38.86           C  
ANISOU 1874  CZ  ARG A 412     3196   5282   6287    347   1149    115       C  
ATOM   1875  NH1 ARG A 412     -29.018  28.999 -45.746  1.00 27.03           N  
ANISOU 1875  NH1 ARG A 412     1706   3729   4836    396   1190     93       N  
ATOM   1876  NH2 ARG A 412     -29.865  27.227 -44.567  1.00 23.23           N  
ANISOU 1876  NH2 ARG A 412     1148   3324   4353    348   1238    138       N  
ATOM   1877  N   ARG A 413     -24.753  24.085 -50.215  1.00 18.77           N  
ANISOU 1877  N   ARG A 413     1036   2803   3291    159    544    121       N  
ATOM   1878  CA  ARG A 413     -25.211  22.811 -50.764  1.00 19.88           C  
ANISOU 1878  CA  ARG A 413     1172   2950   3433    122    442    169       C  
ATOM   1879  C   ARG A 413     -24.073  21.747 -50.712  1.00 24.92           C  
ANISOU 1879  C   ARG A 413     1901   3619   3948     90    419    133       C  
ATOM   1880  O   ARG A 413     -24.349  20.554 -50.571  1.00 25.02           O  
ANISOU 1880  O   ARG A 413     1907   3647   3951     56    377    156       O  
ATOM   1881  CB  ARG A 413     -25.770  23.025 -52.190  1.00 23.35           C  
ANISOU 1881  CB  ARG A 413     1610   3342   3920    127    326    225       C  
ATOM   1882  CG  ARG A 413     -26.155  21.727 -52.925  1.00 41.97           C  
ANISOU 1882  CG  ARG A 413     3987   5694   6265     82    201    270       C  
ATOM   1883  CD  ARG A 413     -27.018  21.883 -54.172  1.00 49.79           C  
ANISOU 1883  CD  ARG A 413     4961   6638   7320     77     76    338       C  
ATOM   1884  NE  ARG A 413     -26.408  22.667 -55.256  1.00 47.94           N  
ANISOU 1884  NE  ARG A 413     4812   6372   7033     99     38    329       N  
ATOM   1885  CZ  ARG A 413     -26.651  23.956 -55.459  1.00 60.72           C  
ANISOU 1885  CZ  ARG A 413     6394   7964   8714    140     67    343       C  
ATOM   1886  NH1 ARG A 413     -27.447  24.628 -54.633  1.00 58.55           N  
ANISOU 1886  NH1 ARG A 413     6002   7687   8556    169    143    359       N  
ATOM   1887  NH2 ARG A 413     -26.091  24.588 -56.475  1.00 41.15           N  
ANISOU 1887  NH2 ARG A 413     3998   5456   6182    155     29    341       N  
ATOM   1888  N   ALA A 414     -22.801  22.204 -50.814  1.00 20.90           N  
ANISOU 1888  N   ALA A 414     1471   3115   3354    101    450     81       N  
ATOM   1889  CA  ALA A 414     -21.586  21.395 -50.757  1.00 19.70           C  
ANISOU 1889  CA  ALA A 414     1398   2989   3098     81    442     48       C  
ATOM   1890  C   ALA A 414     -21.235  20.947 -49.317  1.00 22.83           C  
ANISOU 1890  C   ALA A 414     1781   3433   3461     64    516     17       C  
ATOM   1891  O   ALA A 414     -20.393  20.061 -49.140  1.00 23.15           O  
ANISOU 1891  O   ALA A 414     1871   3496   3431     44    502      3       O  
ATOM   1892  CB  ALA A 414     -20.427  22.156 -51.390  1.00 20.20           C  
ANISOU 1892  CB  ALA A 414     1532   3037   3104    100    453     16       C  
ATOM   1893  N   GLY A 415     -21.877  21.550 -48.313  1.00 19.83           N  
ANISOU 1893  N   GLY A 415     1339   3063   3130     72    595     10       N  
ATOM   1894  CA  GLY A 415     -21.699  21.166 -46.911  1.00 19.20           C  
ANISOU 1894  CA  GLY A 415     1255   3027   3014     54    666    -14       C  
ATOM   1895  C   GLY A 415     -21.015  22.121 -45.953  1.00 19.76           C  
ANISOU 1895  C   GLY A 415     1353   3112   3043     62    755    -73       C  
ATOM   1896  O   GLY A 415     -20.969  21.857 -44.745  1.00 18.50           O  
ANISOU 1896  O   GLY A 415     1196   2987   2847     44    814    -92       O  
ATOM   1897  N   PHE A 416     -20.469  23.219 -46.478  1.00 14.45           N  
ANISOU 1897  N   PHE A 416      709   2412   2372     85    762   -101       N  
ATOM   1898  CA  PHE A 416     -19.792  24.260 -45.716  1.00 13.89           C  
ANISOU 1898  CA  PHE A 416      743   2294   2242     79    783   -155       C  
ATOM   1899  C   PHE A 416     -20.766  25.113 -44.885  1.00 20.32           C  
ANISOU 1899  C   PHE A 416     1443   3138   3138    111    927   -174       C  
ATOM   1900  O   PHE A 416     -21.891  25.377 -45.328  1.00 20.36           O  
ANISOU 1900  O   PHE A 416     1383   3114   3237    139    931   -135       O  
ATOM   1901  CB  PHE A 416     -18.941  25.123 -46.669  1.00 14.28           C  
ANISOU 1901  CB  PHE A 416      758   2356   2309    103    807   -174       C  
ATOM   1902  CG  PHE A 416     -17.864  24.279 -47.321  1.00 15.26           C  
ANISOU 1902  CG  PHE A 416      928   2498   2371     85    741   -165       C  
ATOM   1903  CD1 PHE A 416     -18.111  23.604 -48.513  1.00 17.40           C  
ANISOU 1903  CD1 PHE A 416     1203   2754   2654     92    667   -121       C  
ATOM   1904  CD2 PHE A 416     -16.633  24.089 -46.699  1.00 15.00           C  
ANISOU 1904  CD2 PHE A 416      936   2495   2268     60    752   -197       C  
ATOM   1905  CE1 PHE A 416     -17.130  22.790 -49.081  1.00 17.49           C  
ANISOU 1905  CE1 PHE A 416     1264   2776   2606     82    622   -116       C  
ATOM   1906  CE2 PHE A 416     -15.666  23.263 -47.265  1.00 15.80           C  
ANISOU 1906  CE2 PHE A 416     1070   2610   2324     51    701   -183       C  
ATOM   1907  CZ  PHE A 416     -15.913  22.633 -48.453  1.00 14.03           C  
ANISOU 1907  CZ  PHE A 416      855   2366   2111     65    645   -145       C  
ATOM   1908  N   GLY A 417     -20.335  25.490 -43.676  1.00 18.28           N  
ANISOU 1908  N   GLY A 417     1224   2897   2823     97   1001   -227       N  
ATOM   1909  CA  GLY A 417     -21.108  26.315 -42.748  1.00 19.66           C  
ANISOU 1909  CA  GLY A 417     1383   3054   3032    119   1108   -255       C  
ATOM   1910  C   GLY A 417     -21.966  25.503 -41.806  1.00 26.94           C  
ANISOU 1910  C   GLY A 417     2270   4010   3955    109   1162   -232       C  
ATOM   1911  O   GLY A 417     -22.728  26.051 -41.001  1.00 27.91           O  
ANISOU 1911  O   GLY A 417     2377   4120   4109    131   1266   -249       O  
ATOM   1912  N   GLN A 418     -21.829  24.176 -41.900  1.00 23.65           N  
ANISOU 1912  N   GLN A 418     1846   3634   3505     76   1097   -193       N  
ATOM   1913  CA  GLN A 418     -22.573  23.214 -41.095  1.00 23.16           C  
ANISOU 1913  CA  GLN A 418     1751   3607   3442     58   1134   -160       C  
ATOM   1914  C   GLN A 418     -21.677  22.017 -40.748  1.00 25.13           C  
ANISOU 1914  C   GLN A 418     2050   3903   3593     10   1075   -154       C  
ATOM   1915  O   GLN A 418     -20.839  21.617 -41.561  1.00 21.09           O  
ANISOU 1915  O   GLN A 418     1564   3392   3056      0    984   -149       O  
ATOM   1916  CB  GLN A 418     -23.885  22.796 -41.813  1.00 24.63           C  
ANISOU 1916  CB  GLN A 418     1834   3774   3749     76   1110    -86       C  
ATOM   1917  CG  GLN A 418     -23.684  22.259 -43.232  1.00 45.34           C  
ANISOU 1917  CG  GLN A 418     4446   6382   6399     70    979    -47       C  
ATOM   1918  CD  GLN A 418     -24.632  22.792 -44.289  1.00 43.56           C  
ANISOU 1918  CD  GLN A 418     4148   6110   6293    104    944     -3       C  
ATOM   1919  OE1 GLN A 418     -24.251  23.552 -45.200  1.00 29.87           O  
ANISOU 1919  OE1 GLN A 418     2437   4343   4571    126    903    -15       O  
ATOM   1920  NE2 GLN A 418     -25.821  22.242 -44.305  1.00 21.48           N  
ANISOU 1920  NE2 GLN A 418     1264   3311   3587    102    940     60       N  
ATOM   1921  N   SER A 419     -21.817  21.478 -39.517  1.00 24.13           N  
ANISOU 1921  N   SER A 419     1944   3815   3410    -16   1133   -155       N  
ATOM   1922  CA  SER A 419     -21.072  20.287 -39.072  1.00 23.61           C  
ANISOU 1922  CA  SER A 419     1921   3792   3259    -60   1081   -140       C  
ATOM   1923  C   SER A 419     -21.563  19.096 -39.911  1.00 28.91           C  
ANISOU 1923  C   SER A 419     2536   4461   3988    -68   1001    -72       C  
ATOM   1924  O   SER A 419     -22.701  19.124 -40.403  1.00 30.02           O  
ANISOU 1924  O   SER A 419     2600   4577   4227    -50   1009    -32       O  
ATOM   1925  CB  SER A 419     -21.336  20.016 -37.595  1.00 26.63           C  
ANISOU 1925  CB  SER A 419     2334   4209   3573    -85   1167   -146       C  
ATOM   1926  OG  SER A 419     -22.729  19.858 -37.376  1.00 32.08           O  
ANISOU 1926  OG  SER A 419     2952   4894   4342    -70   1239   -103       O  
ATOM   1927  N   SER A 420     -20.726  18.055 -40.049  1.00 24.03           N  
ANISOU 1927  N   SER A 420     1954   3862   3314    -96    923    -56       N  
ATOM   1928  CA  SER A 420     -21.000  16.851 -40.833  1.00 23.37           C  
ANISOU 1928  CA  SER A 420     1842   3769   3269   -109    840     -1       C  
ATOM   1929  C   SER A 420     -21.958  15.883 -40.122  1.00 27.77           C  
ANISOU 1929  C   SER A 420     2358   4344   3850   -136    867     53       C  
ATOM   1930  O   SER A 420     -22.312  16.132 -38.980  1.00 27.37           O  
ANISOU 1930  O   SER A 420     2308   4319   3773   -144    959     47       O  
ATOM   1931  CB  SER A 420     -19.680  16.162 -41.202  1.00 24.31           C  
ANISOU 1931  CB  SER A 420     2020   3895   3323   -121    760     -8       C  
ATOM   1932  OG  SER A 420     -19.034  15.640 -40.052  1.00 30.34           O  
ANISOU 1932  OG  SER A 420     2826   4697   4004   -151    778    -11       O  
ATOM   1933  N   ASP A 421     -22.344  14.764 -40.789  1.00 25.64           N  
ANISOU 1933  N   ASP A 421     2061   4057   3624   -154    789    106       N  
ATOM   1934  CA  ASP A 421     -23.247  13.718 -40.269  1.00 26.33           C  
ANISOU 1934  CA  ASP A 421     2104   4154   3746   -187    799    168       C  
ATOM   1935  C   ASP A 421     -22.674  12.919 -39.099  1.00 31.74           C  
ANISOU 1935  C   ASP A 421     2840   4878   4341   -220    823    176       C  
ATOM   1936  O   ASP A 421     -23.421  12.250 -38.378  1.00 31.14           O  
ANISOU 1936  O   ASP A 421     2733   4816   4282   -248    861    225       O  
ATOM   1937  CB  ASP A 421     -23.700  12.759 -41.385  1.00 28.25           C  
ANISOU 1937  CB  ASP A 421     2319   4359   4057   -203    692    217       C  
ATOM   1938  CG  ASP A 421     -24.477  13.440 -42.497  1.00 40.89           C  
ANISOU 1938  CG  ASP A 421     3863   5920   5754   -179    657    227       C  
ATOM   1939  OD1 ASP A 421     -25.557  14.024 -42.205  1.00 40.41           O  
ANISOU 1939  OD1 ASP A 421     3721   5858   5774   -169    720    251       O  
ATOM   1940  OD2 ASP A 421     -24.017  13.379 -43.662  1.00 46.63           O  
ANISOU 1940  OD2 ASP A 421     4627   6615   6476   -169    568    214       O  
ATOM   1941  N   VAL A 422     -21.353  12.984 -38.915  1.00 29.87           N  
ANISOU 1941  N   VAL A 422     2678   4657   4012   -219    798    135       N  
ATOM   1942  CA  VAL A 422     -20.666  12.311 -37.817  1.00 30.21           C  
ANISOU 1942  CA  VAL A 422     2776   4738   3965   -250    806    144       C  
ATOM   1943  C   VAL A 422     -21.149  12.907 -36.485  1.00 34.15           C  
ANISOU 1943  C   VAL A 422     3284   5271   4420   -260    921    132       C  
ATOM   1944  O   VAL A 422     -21.417  12.156 -35.551  1.00 33.87           O  
ANISOU 1944  O   VAL A 422     3259   5261   4348   -292    952    172       O  
ATOM   1945  CB  VAL A 422     -19.130  12.399 -38.014  1.00 33.46           C  
ANISOU 1945  CB  VAL A 422     3252   5154   4306   -243    748    107       C  
ATOM   1946  CG1 VAL A 422     -18.357  11.882 -36.796  1.00 33.14           C  
ANISOU 1946  CG1 VAL A 422     3269   5154   4170   -275    751    117       C  
ATOM   1947  CG2 VAL A 422     -18.723  11.643 -39.269  1.00 32.92           C  
ANISOU 1947  CG2 VAL A 422     3184   5048   4277   -230    653    124       C  
ATOM   1948  N   LYS A 423     -21.310  14.252 -36.434  1.00 31.89           N  
ANISOU 1948  N   LYS A 423     2996   4981   4141   -231    988     80       N  
ATOM   1949  CA  LYS A 423     -21.729  15.024 -35.254  1.00 33.04           C  
ANISOU 1949  CA  LYS A 423     3165   5148   4241   -232   1109     52       C  
ATOM   1950  C   LYS A 423     -20.847  14.638 -34.054  1.00 39.45           C  
ANISOU 1950  C   LYS A 423     4069   6001   4919   -270   1112     43       C  
ATOM   1951  O   LYS A 423     -21.361  14.321 -32.983  1.00 40.53           O  
ANISOU 1951  O   LYS A 423     4226   6164   5010   -294   1188     66       O  
ATOM   1952  CB  LYS A 423     -23.247  14.874 -34.947  1.00 35.43           C  
ANISOU 1952  CB  LYS A 423     3390   5446   4624   -227   1200    101       C  
ATOM   1953  CG  LYS A 423     -24.198  15.226 -36.103  1.00 38.57           C  
ANISOU 1953  CG  LYS A 423     3688   5803   5165   -193   1185    122       C  
ATOM   1954  CD  LYS A 423     -24.453  16.734 -36.247  1.00 40.23           C  
ANISOU 1954  CD  LYS A 423     3886   5989   5410   -146   1259     68       C  
ATOM   1955  CE  LYS A 423     -25.584  17.040 -37.205  1.00 31.85           C  
ANISOU 1955  CE  LYS A 423     2715   4889   4499   -114   1254    106       C  
ATOM   1956  NZ  LYS A 423     -25.086  17.314 -38.574  1.00 33.70           N  
ANISOU 1956  NZ  LYS A 423     2946   5091   4768    -97   1139     92       N  
ATOM   1957  N   PHE A 424     -19.507  14.640 -34.260  1.00 36.49           N  
ANISOU 1957  N   PHE A 424     3746   5631   4485   -279   1026     15       N  
ATOM   1958  CA  PHE A 424     -18.514  14.308 -33.234  1.00 37.26           C  
ANISOU 1958  CA  PHE A 424     3928   5765   4464   -317   1000     11       C  
ATOM   1959  C   PHE A 424     -18.653  15.299 -32.061  1.00 41.89           C  
ANISOU 1959  C   PHE A 424     4584   6369   4964   -329   1099    -40       C  
ATOM   1960  O   PHE A 424     -19.020  16.446 -32.314  1.00 41.19           O  
ANISOU 1960  O   PHE A 424     4485   6256   4910   -298   1159    -92       O  
ATOM   1961  CB  PHE A 424     -17.074  14.332 -33.828  1.00 38.71           C  
ANISOU 1961  CB  PHE A 424     4135   5943   4630   -316    894     -8       C  
ATOM   1962  CG  PHE A 424     -16.071  13.486 -33.068  1.00 41.58           C  
ANISOU 1962  CG  PHE A 424     4553   6338   4909   -355    828     22       C  
ATOM   1963  CD1 PHE A 424     -15.183  14.069 -32.163  1.00 45.98           C  
ANISOU 1963  CD1 PHE A 424     5184   6919   5366   -384    818    -13       C  
ATOM   1964  CD2 PHE A 424     -16.050  12.099 -33.211  1.00 44.24           C  
ANISOU 1964  CD2 PHE A 424     4869   6675   5266   -365    772     90       C  
ATOM   1965  CE1 PHE A 424     -14.303  13.277 -31.403  1.00 46.82           C  
ANISOU 1965  CE1 PHE A 424     5338   7055   5397   -423    750     26       C  
ATOM   1966  CE2 PHE A 424     -15.171  11.309 -32.447  1.00 47.54           C  
ANISOU 1966  CE2 PHE A 424     5334   7119   5611   -399    713    127       C  
ATOM   1967  CZ  PHE A 424     -14.299  11.905 -31.556  1.00 45.68           C  
ANISOU 1967  CZ  PHE A 424     5165   6911   5279   -427    699     98       C  
ATOM   1968  N   PRO A 425     -18.454  14.902 -30.777  1.00 39.64           N  
ANISOU 1968  N   PRO A 425     4375   6121   4566   -371   1123    -27       N  
ATOM   1969  CA  PRO A 425     -18.576  15.894 -29.688  1.00 40.21           C  
ANISOU 1969  CA  PRO A 425     4533   6202   4542   -382   1220    -85       C  
ATOM   1970  C   PRO A 425     -17.591  17.059 -29.868  1.00 42.90           C  
ANISOU 1970  C   PRO A 425     4923   6526   4850   -379   1181   -162       C  
ATOM   1971  O   PRO A 425     -16.395  16.833 -30.091  1.00 41.45           O  
ANISOU 1971  O   PRO A 425     4756   6350   4643   -400   1067   -160       O  
ATOM   1972  CB  PRO A 425     -18.271  15.080 -28.421  1.00 42.70           C  
ANISOU 1972  CB  PRO A 425     4933   6560   4729   -436   1213    -48       C  
ATOM   1973  CG  PRO A 425     -18.493  13.656 -28.812  1.00 47.09           C  
ANISOU 1973  CG  PRO A 425     5424   7125   5345   -443   1157     40       C  
ATOM   1974  CD  PRO A 425     -18.077  13.576 -30.247  1.00 41.49           C  
ANISOU 1974  CD  PRO A 425     4633   6384   4747   -410   1063     40       C  
ATOM   1975  N   GLY A 426     -18.121  18.287 -29.840  1.00 39.19           N  
ANISOU 1975  N   GLY A 426     4466   6027   4396   -351   1275   -225       N  
ATOM   1976  CA  GLY A 426     -17.332  19.510 -29.995  1.00 38.03           C  
ANISOU 1976  CA  GLY A 426     4368   5854   4228   -349   1253   -301       C  
ATOM   1977  C   GLY A 426     -16.998  19.913 -31.420  1.00 38.30           C  
ANISOU 1977  C   GLY A 426     4321   5854   4376   -313   1187   -308       C  
ATOM   1978  O   GLY A 426     -16.218  20.848 -31.624  1.00 38.91           O  
ANISOU 1978  O   GLY A 426     4432   5909   4442   -317   1152   -361       O  
ATOM   1979  N   GLU A 427     -17.585  19.215 -32.415  1.00 31.27           N  
ANISOU 1979  N   GLU A 427     3330   4957   3595   -281   1166   -252       N  
ATOM   1980  CA  GLU A 427     -17.388  19.454 -33.847  1.00 28.61           C  
ANISOU 1980  CA  GLU A 427     2922   4587   3361   -245   1105   -249       C  
ATOM   1981  C   GLU A 427     -17.764  20.876 -34.265  1.00 31.95           C  
ANISOU 1981  C   GLU A 427     3336   4965   3839   -207   1167   -306       C  
ATOM   1982  O   GLU A 427     -18.839  21.372 -33.927  1.00 33.84           O  
ANISOU 1982  O   GLU A 427     3562   5187   4107   -182   1272   -318       O  
ATOM   1983  CB  GLU A 427     -18.168  18.440 -34.696  1.00 28.86           C  
ANISOU 1983  CB  GLU A 427     2864   4614   3487   -224   1080   -181       C  
ATOM   1984  CG  GLU A 427     -17.622  18.325 -36.109  1.00 37.80           C  
ANISOU 1984  CG  GLU A 427     3952   5722   4688   -201    988   -170       C  
ATOM   1985  CD  GLU A 427     -18.384  17.434 -37.067  1.00 52.06           C  
ANISOU 1985  CD  GLU A 427     5684   7512   6582   -184    952   -112       C  
ATOM   1986  OE1 GLU A 427     -18.606  16.244 -36.744  1.00 38.05           O  
ANISOU 1986  OE1 GLU A 427     3902   5758   4796   -207    930    -61       O  
ATOM   1987  OE2 GLU A 427     -18.691  17.910 -38.182  1.00 47.22           O  
ANISOU 1987  OE2 GLU A 427     5028   6864   6049   -150    936   -115       O  
ATOM   1988  N   SER A 428     -16.885  21.504 -35.034  1.00 24.63           N  
ANISOU 1988  N   SER A 428     2412   4014   2933   -201   1104   -334       N  
ATOM   1989  CA  SER A 428     -17.063  22.850 -35.545  1.00 22.60           C  
ANISOU 1989  CA  SER A 428     2149   3708   2730   -167   1145   -383       C  
ATOM   1990  C   SER A 428     -17.915  22.819 -36.818  1.00 23.46           C  
ANISOU 1990  C   SER A 428     2163   3787   2963   -117   1142   -344       C  
ATOM   1991  O   SER A 428     -17.812  21.892 -37.619  1.00 21.65           O  
ANISOU 1991  O   SER A 428     1888   3568   2769   -115   1069   -293       O  
ATOM   1992  CB  SER A 428     -15.697  23.474 -35.824  1.00 25.08           C  
ANISOU 1992  CB  SER A 428     2504   4011   3016   -189   1073   -418       C  
ATOM   1993  OG  SER A 428     -15.795  24.787 -36.345  1.00 35.81           O  
ANISOU 1993  OG  SER A 428     3862   5316   4426   -161   1108   -463       O  
ATOM   1994  N   ALA A 429     -18.746  23.846 -37.001  1.00 19.57           N  
ANISOU 1994  N   ALA A 429     1649   3252   2536    -77   1219   -369       N  
ATOM   1995  CA  ALA A 429     -19.595  23.985 -38.169  1.00 19.16           C  
ANISOU 1995  CA  ALA A 429     1510   3166   2605    -31   1213   -332       C  
ATOM   1996  C   ALA A 429     -18.925  24.874 -39.215  1.00 25.34           C  
ANISOU 1996  C   ALA A 429     2296   3909   3424    -13   1161   -353       C  
ATOM   1997  O   ALA A 429     -19.465  25.048 -40.303  1.00 25.18           O  
ANISOU 1997  O   ALA A 429     2215   3857   3494     22   1137   -321       O  
ATOM   1998  CB  ALA A 429     -20.947  24.572 -37.763  1.00 20.24           C  
ANISOU 1998  CB  ALA A 429     1607   3276   2807      7   1329   -334       C  
ATOM   1999  N   GLY A 430     -17.748  25.414 -38.895  1.00 23.22           N  
ANISOU 1999  N   GLY A 430     2097   3640   3087    -41   1140   -402       N  
ATOM   2000  CA  GLY A 430     -17.069  26.344 -39.782  1.00 22.79           C  
ANISOU 2000  CA  GLY A 430     2048   3544   3066    -28   1103   -422       C  
ATOM   2001  C   GLY A 430     -17.821  27.668 -39.776  1.00 27.51           C  
ANISOU 2001  C   GLY A 430     2644   4085   3726     11   1185   -457       C  
ATOM   2002  O   GLY A 430     -18.672  27.902 -38.907  1.00 28.97           O  
ANISOU 2002  O   GLY A 430     2834   4263   3910     24   1277   -477       O  
ATOM   2003  N   LEU A 431     -17.501  28.547 -40.723  1.00 22.66           N  
ANISOU 2003  N   LEU A 431     2022   3423   3164     31   1160   -463       N  
ATOM   2004  CA  LEU A 431     -18.146  29.845 -40.876  1.00 23.22           C  
ANISOU 2004  CA  LEU A 431     2087   3428   3306     73   1228   -490       C  
ATOM   2005  C   LEU A 431     -18.428  30.076 -42.359  1.00 25.04           C  
ANISOU 2005  C   LEU A 431     2258   3625   3629    111   1178   -440       C  
ATOM   2006  O   LEU A 431     -17.525  29.952 -43.180  1.00 22.99           O  
ANISOU 2006  O   LEU A 431     2009   3371   3356     95   1102   -423       O  
ATOM   2007  CB  LEU A 431     -17.266  30.995 -40.320  1.00 24.23           C  
ANISOU 2007  CB  LEU A 431     2299   3520   3388     48   1251   -563       C  
ATOM   2008  CG  LEU A 431     -17.570  31.524 -38.899  1.00 31.07           C  
ANISOU 2008  CG  LEU A 431     3236   4372   4197     37   1348   -631       C  
ATOM   2009  CD1 LEU A 431     -16.476  32.480 -38.440  1.00 31.34           C  
ANISOU 2009  CD1 LEU A 431     3362   4372   4173     -6   1335   -699       C  
ATOM   2010  CD2 LEU A 431     -18.934  32.232 -38.821  1.00 32.78           C  
ANISOU 2010  CD2 LEU A 431     3419   4535   4500    102   1459   -637       C  
ATOM   2011  N   LEU A 432     -19.681  30.378 -42.696  1.00 21.71           N  
ANISOU 2011  N   LEU A 432     1776   3171   3304    160   1219   -410       N  
ATOM   2012  CA  LEU A 432     -20.109  30.662 -44.059  1.00 20.88           C  
ANISOU 2012  CA  LEU A 432     1617   3028   3290    196   1168   -357       C  
ATOM   2013  C   LEU A 432     -21.239  31.676 -44.010  1.00 27.53           C  
ANISOU 2013  C   LEU A 432     2415   3809   4236    252   1246   -356       C  
ATOM   2014  O   LEU A 432     -22.294  31.399 -43.440  1.00 28.87           O  
ANISOU 2014  O   LEU A 432     2535   3986   4450    274   1308   -340       O  
ATOM   2015  CB  LEU A 432     -20.561  29.385 -44.779  1.00 19.91           C  
ANISOU 2015  CB  LEU A 432     1438   2943   3183    192   1091   -287       C  
ATOM   2016  CG  LEU A 432     -21.017  29.541 -46.251  1.00 23.75           C  
ANISOU 2016  CG  LEU A 432     1881   3394   3749    222   1019   -226       C  
ATOM   2017  CD1 LEU A 432     -19.852  29.961 -47.194  1.00 21.34           C  
ANISOU 2017  CD1 LEU A 432     1631   3070   3405    212    961   -233       C  
ATOM   2018  CD2 LEU A 432     -21.678  28.282 -46.738  1.00 23.22           C  
ANISOU 2018  CD2 LEU A 432     1764   3359   3701    213    951   -164       C  
ATOM   2019  N   TYR A 433     -21.020  32.845 -44.602  1.00 23.87           N  
ANISOU 2019  N   TYR A 433     1968   3283   3818    276   1247   -367       N  
ATOM   2020  CA  TYR A 433     -22.033  33.903 -44.629  1.00 24.77           C  
ANISOU 2020  CA  TYR A 433     2041   3327   4044    335   1319   -363       C  
ATOM   2021  C   TYR A 433     -22.882  33.873 -45.892  1.00 30.14           C  
ANISOU 2021  C   TYR A 433     2636   3981   4833    374   1255   -277       C  
ATOM   2022  O   TYR A 433     -22.448  33.366 -46.931  1.00 27.62           O  
ANISOU 2022  O   TYR A 433     2319   3682   4492    354   1151   -234       O  
ATOM   2023  CB  TYR A 433     -21.355  35.268 -44.474  1.00 25.93           C  
ANISOU 2023  CB  TYR A 433     2259   3408   4184    339   1360   -424       C  
ATOM   2024  CG  TYR A 433     -20.621  35.423 -43.160  1.00 27.74           C  
ANISOU 2024  CG  TYR A 433     2579   3651   4310    297   1421   -511       C  
ATOM   2025  CD1 TYR A 433     -19.233  35.520 -43.121  1.00 28.16           C  
ANISOU 2025  CD1 TYR A 433     2708   3718   4275    240   1367   -550       C  
ATOM   2026  CD2 TYR A 433     -21.317  35.464 -41.951  1.00 29.93           C  
ANISOU 2026  CD2 TYR A 433     2868   3926   4577    313   1531   -552       C  
ATOM   2027  CE1 TYR A 433     -18.557  35.703 -41.915  1.00 29.30           C  
ANISOU 2027  CE1 TYR A 433     2938   3870   4324    196   1407   -626       C  
ATOM   2028  CE2 TYR A 433     -20.653  35.643 -40.741  1.00 31.77           C  
ANISOU 2028  CE2 TYR A 433     3202   4168   4703    271   1580   -634       C  
ATOM   2029  CZ  TYR A 433     -19.272  35.767 -40.726  1.00 41.61           C  
ANISOU 2029  CZ  TYR A 433     4523   5424   5861    210   1510   -671       C  
ATOM   2030  OH  TYR A 433     -18.628  35.929 -39.521  1.00 47.06           O  
ANISOU 2030  OH  TYR A 433     5316   6122   6444    161   1543   -747       O  
ATOM   2031  N   SER A 434     -24.105  34.400 -45.794  1.00 31.38           N  
ANISOU 2031  N   SER A 434     2721   4093   5108    430   1318   -249       N  
ATOM   2032  CA  SER A 434     -25.024  34.479 -46.936  1.00 31.77           C  
ANISOU 2032  CA  SER A 434     2682   4111   5277    469   1252   -161       C  
ATOM   2033  C   SER A 434     -24.757  35.758 -47.721  1.00 35.40           C  
ANISOU 2033  C   SER A 434     3167   4494   5787    499   1237   -158       C  
ATOM   2034  O   SER A 434     -24.163  36.680 -47.188  1.00 34.67           O  
ANISOU 2034  O   SER A 434     3142   4362   5668    502   1306   -226       O  
ATOM   2035  CB  SER A 434     -26.477  34.406 -46.477  1.00 35.36           C  
ANISOU 2035  CB  SER A 434     3029   4553   5854    516   1323   -118       C  
ATOM   2036  OG  SER A 434     -26.745  35.411 -45.515  1.00 47.23           O  
ANISOU 2036  OG  SER A 434     4547   6004   7394    559   1464   -175       O  
ATOM   2037  N   ALA A 435     -25.181  35.799 -48.992  1.00 34.06           N  
ANISOU 2037  N   ALA A 435     2952   4302   5687    516   1139    -77       N  
ATOM   2038  CA  ALA A 435     -25.002  36.924 -49.901  1.00 34.76           C  
ANISOU 2038  CA  ALA A 435     3061   4318   5828    544   1108    -54       C  
ATOM   2039  C   ALA A 435     -25.588  38.241 -49.384  1.00 42.89           C  
ANISOU 2039  C   ALA A 435     4066   5263   6967    606   1216    -75       C  
ATOM   2040  O   ALA A 435     -25.121  39.300 -49.802  1.00 43.33           O  
ANISOU 2040  O   ALA A 435     4169   5255   7041    621   1218    -86       O  
ATOM   2041  CB  ALA A 435     -25.556  36.583 -51.273  1.00 35.46           C  
ANISOU 2041  CB  ALA A 435     3101   4402   5969    550    981     46       C  
ATOM   2042  N   ASP A 436     -26.560  38.184 -48.444  1.00 42.37           N  
ANISOU 2042  N   ASP A 436     3933   5193   6972    644   1316    -83       N  
ATOM   2043  CA  ASP A 436     -27.161  39.376 -47.832  1.00 44.36           C  
ANISOU 2043  CA  ASP A 436     4165   5361   7329    711   1442   -110       C  
ATOM   2044  C   ASP A 436     -26.164  40.060 -46.891  1.00 47.36           C  
ANISOU 2044  C   ASP A 436     4667   5717   7612    689   1533   -226       C  
ATOM   2045  O   ASP A 436     -26.212  41.277 -46.755  1.00 47.28           O  
ANISOU 2045  O   ASP A 436     4685   5618   7662    731   1602   -256       O  
ATOM   2046  CB  ASP A 436     -28.506  39.071 -47.145  1.00 48.06           C  
ANISOU 2046  CB  ASP A 436     4522   5832   7906    760   1531    -78       C  
ATOM   2047  CG  ASP A 436     -28.403  38.415 -45.777  1.00 66.50           C  
ANISOU 2047  CG  ASP A 436     6893   8225  10151    734   1637   -150       C  
ATOM   2048  OD1 ASP A 436     -28.113  39.138 -44.788  1.00 68.26           O  
ANISOU 2048  OD1 ASP A 436     7192   8407  10336    749   1761   -240       O  
ATOM   2049  OD2 ASP A 436     -28.673  37.195 -45.682  1.00 74.85           O  
ANISOU 2049  OD2 ASP A 436     7903   9359  11178    700   1597   -115       O  
ATOM   2050  N   LYS A 437     -25.229  39.280 -46.284  1.00 43.18           N  
ANISOU 2050  N   LYS A 437     4212   5262   6931    620   1522   -285       N  
ATOM   2051  CA  LYS A 437     -24.147  39.796 -45.431  1.00 42.78           C  
ANISOU 2051  CA  LYS A 437     4283   5199   6773    582   1577   -389       C  
ATOM   2052  C   LYS A 437     -23.082  40.491 -46.300  1.00 47.71           C  
ANISOU 2052  C   LYS A 437     4970   5786   7371    553   1499   -391       C  
ATOM   2053  O   LYS A 437     -21.942  40.708 -45.892  1.00 46.47           O  
ANISOU 2053  O   LYS A 437     4906   5634   7115    500   1496   -458       O  
ATOM   2054  CB  LYS A 437     -23.587  38.710 -44.498  1.00 44.16           C  
ANISOU 2054  CB  LYS A 437     4505   5465   6810    520   1583   -437       C  
ATOM   2055  CG  LYS A 437     -24.376  38.626 -43.195  1.00 58.73           C  
ANISOU 2055  CG  LYS A 437     6347   7310   8659    546   1719   -481       C  
ATOM   2056  CD  LYS A 437     -24.157  37.324 -42.447  1.00 64.27           C  
ANISOU 2056  CD  LYS A 437     7061   8110   9250    494   1712   -492       C  
ATOM   2057  CE  LYS A 437     -25.285  36.338 -42.637  1.00 65.79           C  
ANISOU 2057  CE  LYS A 437     7135   8347   9516    518   1705   -409       C  
ATOM   2058  NZ  LYS A 437     -24.815  34.928 -42.568  1.00 63.68           N  
ANISOU 2058  NZ  LYS A 437     6872   8176   9149    455   1627   -390       N  
ATOM   2059  N   LEU A 438     -23.519  40.798 -47.536  1.00 46.98           N  
ANISOU 2059  N   LEU A 438     4820   5657   7375    589   1430   -308       N  
ATOM   2060  CA  LEU A 438     -23.012  41.608 -48.647  1.00 47.38           C  
ANISOU 2060  CA  LEU A 438     4896   5651   7454    590   1363   -272       C  
ATOM   2061  C   LEU A 438     -21.563  41.560 -49.077  1.00 48.15           C  
ANISOU 2061  C   LEU A 438     5077   5774   7443    523   1296   -294       C  
ATOM   2062  O   LEU A 438     -20.808  40.668 -48.705  1.00 47.83           O  
ANISOU 2062  O   LEU A 438     5069   5812   7292    467   1270   -324       O  
ATOM   2063  CB  LEU A 438     -23.477  43.081 -48.460  1.00 48.97           C  
ANISOU 2063  CB  LEU A 438     5104   5735   7768    651   1449   -292       C  
ATOM   2064  CG  LEU A 438     -24.840  43.453 -49.036  1.00 54.64           C  
ANISOU 2064  CG  LEU A 438     5716   6397   8647    732   1452   -206       C  
ATOM   2065  CD1 LEU A 438     -25.540  44.415 -48.135  1.00 57.90           C  
ANISOU 2065  CD1 LEU A 438     6122   6723   9154    797   1593   -254       C  
ATOM   2066  CD2 LEU A 438     -24.700  44.103 -50.409  1.00 55.35           C  
ANISOU 2066  CD2 LEU A 438     5804   6433   8794    744   1359   -129       C  
ATOM   2067  N   ASN A 439     -21.244  42.513 -49.975  1.00 43.05           N  
ANISOU 2067  N   ASN A 439     4455   5059   6843    534   1263   -262       N  
ATOM   2068  CA  ASN A 439     -19.967  42.913 -50.561  1.00 40.68           C  
ANISOU 2068  CA  ASN A 439     4226   4747   6483    485   1216   -267       C  
ATOM   2069  C   ASN A 439     -19.384  42.023 -51.639  1.00 37.84           C  
ANISOU 2069  C   ASN A 439     3868   4454   6054    449   1114   -206       C  
ATOM   2070  O   ASN A 439     -19.084  40.860 -51.389  1.00 36.11           O  
ANISOU 2070  O   ASN A 439     3646   4322   5754    415   1087   -216       O  
ATOM   2071  CB  ASN A 439     -18.960  43.291 -49.481  1.00 42.38           C  
ANISOU 2071  CB  ASN A 439     4521   4955   6626    433   1272   -367       C  
ATOM   2072  CG  ASN A 439     -17.918  44.293 -49.869  1.00 51.30           C  
ANISOU 2072  CG  ASN A 439     5716   6023   7753    400   1260   -379       C  
ATOM   2073  OD1 ASN A 439     -17.257  44.193 -50.914  1.00 35.78           O  
ANISOU 2073  OD1 ASN A 439     3757   4071   5767    376   1191   -323       O  
ATOM   2074  ND2 ASN A 439     -17.669  45.216 -48.958  1.00 45.60           N  
ANISOU 2074  ND2 ASN A 439     5051   5234   7040    389   1329   -459       N  
ATOM   2075  N   SER A 440     -19.217  42.602 -52.843  1.00 32.29           N  
ANISOU 2075  N   SER A 440     3178   3706   5386    460   1061   -140       N  
ATOM   2076  CA  SER A 440     -18.648  41.978 -54.046  1.00 30.70           C  
ANISOU 2076  CA  SER A 440     2997   3547   5119    433    973    -77       C  
ATOM   2077  C   SER A 440     -17.180  41.603 -53.824  1.00 31.79           C  
ANISOU 2077  C   SER A 440     3193   3735   5152    367    976   -122       C  
ATOM   2078  O   SER A 440     -16.742  40.554 -54.300  1.00 30.25           O  
ANISOU 2078  O   SER A 440     3006   3610   4879    342    926    -98       O  
ATOM   2079  CB  SER A 440     -18.749  42.932 -55.237  1.00 33.70           C  
ANISOU 2079  CB  SER A 440     3393   3853   5559    458    936     -4       C  
ATOM   2080  OG  SER A 440     -20.101  43.212 -55.554  1.00 41.60           O  
ANISOU 2080  OG  SER A 440     4332   4810   6666    519    916     54       O  
ATOM   2081  N   SER A 441     -16.426  42.469 -53.111  1.00 27.54           N  
ANISOU 2081  N   SER A 441     2694   3154   4616    340   1032   -184       N  
ATOM   2082  CA  SER A 441     -15.013  42.242 -52.825  1.00 26.62           C  
ANISOU 2082  CA  SER A 441     2620   3075   4417    275   1031   -222       C  
ATOM   2083  C   SER A 441     -14.827  41.164 -51.769  1.00 28.69           C  
ANISOU 2083  C   SER A 441     2873   3420   4607    245   1040   -278       C  
ATOM   2084  O   SER A 441     -13.860  40.423 -51.862  1.00 27.79           O  
ANISOU 2084  O   SER A 441     2772   3366   4420    202   1012   -277       O  
ATOM   2085  CB  SER A 441     -14.263  43.542 -52.524  1.00 30.48           C  
ANISOU 2085  CB  SER A 441     3155   3485   4940    247   1070   -260       C  
ATOM   2086  OG  SER A 441     -14.599  44.111 -51.271  1.00 40.82           O  
ANISOU 2086  OG  SER A 441     4480   4754   6274    248   1131   -341       O  
ATOM   2087  N   GLN A 442     -15.806  40.996 -50.846  1.00 26.14           N  
ANISOU 2087  N   GLN A 442     2524   3102   4308    273   1081   -315       N  
ATOM   2088  CA  GLN A 442     -15.819  39.905 -49.857  1.00 25.39           C  
ANISOU 2088  CA  GLN A 442     2418   3085   4143    250   1090   -357       C  
ATOM   2089  C   GLN A 442     -16.176  38.602 -50.569  1.00 27.75           C  
ANISOU 2089  C   GLN A 442     2676   3454   4412    261   1029   -296       C  
ATOM   2090  O   GLN A 442     -15.632  37.548 -50.248  1.00 27.05           O  
ANISOU 2090  O   GLN A 442     2592   3438   4247    226   1006   -308       O  
ATOM   2091  CB  GLN A 442     -16.825  40.162 -48.737  1.00 27.62           C  
ANISOU 2091  CB  GLN A 442     2688   3345   4461    281   1164   -408       C  
ATOM   2092  CG  GLN A 442     -16.387  41.196 -47.706  1.00 38.72           C  
ANISOU 2092  CG  GLN A 442     4158   4692   5863    258   1229   -492       C  
ATOM   2093  CD  GLN A 442     -17.499  41.478 -46.702  1.00 49.96           C  
ANISOU 2093  CD  GLN A 442     5575   6084   7324    301   1319   -538       C  
ATOM   2094  OE1 GLN A 442     -18.688  41.474 -47.024  1.00 36.63           O  
ANISOU 2094  OE1 GLN A 442     3824   4376   5717    364   1342   -495       O  
ATOM   2095  NE2 GLN A 442     -17.139  41.724 -45.452  1.00 46.18           N  
ANISOU 2095  NE2 GLN A 442     5162   5597   6786    267   1373   -624       N  
ATOM   2096  N   LEU A 443     -17.072  38.682 -51.561  1.00 25.33           N  
ANISOU 2096  N   LEU A 443     2336   3122   4167    306    996   -229       N  
ATOM   2097  CA  LEU A 443     -17.460  37.534 -52.375  1.00 24.85           C  
ANISOU 2097  CA  LEU A 443     2248   3113   4080    313    925   -168       C  
ATOM   2098  C   LEU A 443     -16.314  37.170 -53.296  1.00 26.88           C  
ANISOU 2098  C   LEU A 443     2553   3396   4266    281    877   -141       C  
ATOM   2099  O   LEU A 443     -16.138  35.999 -53.609  1.00 25.54           O  
ANISOU 2099  O   LEU A 443     2386   3285   4034    266    834   -122       O  
ATOM   2100  CB  LEU A 443     -18.752  37.819 -53.166  1.00 25.68           C  
ANISOU 2100  CB  LEU A 443     2306   3175   4276    365    892   -100       C  
ATOM   2101  CG  LEU A 443     -19.969  36.875 -52.922  1.00 29.91           C  
ANISOU 2101  CG  LEU A 443     2772   3748   4843    385    871    -74       C  
ATOM   2102  CD1 LEU A 443     -19.628  35.442 -53.264  1.00 30.88           C  
ANISOU 2102  CD1 LEU A 443     2910   3947   4877    351    806    -57       C  
ATOM   2103  CD2 LEU A 443     -20.473  36.937 -51.501  1.00 26.55           C  
ANISOU 2103  CD2 LEU A 443     2311   3329   4446    396    958   -132       C  
ATOM   2104  N   GLY A 444     -15.514  38.175 -53.673  1.00 22.62           N  
ANISOU 2104  N   GLY A 444     2052   2808   3736    269    894   -142       N  
ATOM   2105  CA  GLY A 444     -14.311  37.993 -54.471  1.00 21.63           C  
ANISOU 2105  CA  GLY A 444     1970   2699   3551    239    871   -117       C  
ATOM   2106  C   GLY A 444     -13.269  37.226 -53.675  1.00 25.64           C  
ANISOU 2106  C   GLY A 444     2483   3269   3989    193    885   -163       C  
ATOM   2107  O   GLY A 444     -12.583  36.360 -54.227  1.00 25.70           O  
ANISOU 2107  O   GLY A 444     2506   3322   3937    178    859   -138       O  
ATOM   2108  N   THR A 445     -13.185  37.499 -52.348  1.00 21.97           N  
ANISOU 2108  N   THR A 445     2010   2806   3530    172    926   -230       N  
ATOM   2109  CA  THR A 445     -12.245  36.811 -51.453  1.00 20.48           C  
ANISOU 2109  CA  THR A 445     1826   2676   3279    124    929   -273       C  
ATOM   2110  C   THR A 445     -12.622  35.393 -51.157  1.00 20.51           C  
ANISOU 2110  C   THR A 445     1808   2752   3234    128    905   -270       C  
ATOM   2111  O   THR A 445     -11.718  34.584 -51.005  1.00 18.65           O  
ANISOU 2111  O   THR A 445     1576   2567   2943     98    887   -271       O  
ATOM   2112  CB  THR A 445     -11.794  37.631 -50.206  1.00 31.13           C  
ANISOU 2112  CB  THR A 445     3195   3998   4635     87    968   -344       C  
ATOM   2113  OG1 THR A 445     -12.800  37.652 -49.200  1.00 35.35           O  
ANISOU 2113  OG1 THR A 445     3723   4528   5179    105   1004   -389       O  
ATOM   2114  CG2 THR A 445     -11.321  39.028 -50.540  1.00 28.95           C  
ANISOU 2114  CG2 THR A 445     2946   3642   4411     76    987   -345       C  
ATOM   2115  N   MET A 446     -13.949  35.068 -51.070  1.00 18.54           N  
ANISOU 2115  N   MET A 446     1529   2504   3012    165    903   -260       N  
ATOM   2116  CA  MET A 446     -14.455  33.694 -50.809  1.00 16.96           C  
ANISOU 2116  CA  MET A 446     1304   2367   2774    167    876   -250       C  
ATOM   2117  C   MET A 446     -14.050  32.737 -51.933  1.00 17.98           C  
ANISOU 2117  C   MET A 446     1447   2525   2860    167    820   -199       C  
ATOM   2118  O   MET A 446     -13.707  31.581 -51.678  1.00 17.87           O  
ANISOU 2118  O   MET A 446     1432   2564   2792    150    800   -201       O  
ATOM   2119  CB  MET A 446     -15.980  33.666 -50.635  1.00 19.94           C  
ANISOU 2119  CB  MET A 446     1638   2730   3209    205    885   -237       C  
ATOM   2120  CG  MET A 446     -16.476  34.302 -49.359  1.00 24.63           C  
ANISOU 2120  CG  MET A 446     2221   3306   3833    209    957   -293       C  
ATOM   2121  SD  MET A 446     -18.289  34.222 -49.240  1.00 30.00           S  
ANISOU 2121  SD  MET A 446     2830   3967   4600    261    979   -262       S  
ATOM   2122  CE  MET A 446     -18.530  35.343 -48.022  1.00 28.56           C  
ANISOU 2122  CE  MET A 446     2662   3739   4450    272   1081   -331       C  
ATOM   2123  N   ALA A 447     -14.053  33.239 -53.170  1.00 14.55           N  
ANISOU 2123  N   ALA A 447     1034   2050   2446    188    798   -154       N  
ATOM   2124  CA  ALA A 447     -13.660  32.537 -54.389  1.00 14.32           C  
ANISOU 2124  CA  ALA A 447     1039   2033   2368    192    754   -106       C  
ATOM   2125  C   ALA A 447     -12.274  31.843 -54.287  1.00 20.62           C  
ANISOU 2125  C   ALA A 447     1859   2873   3103    164    766   -118       C  
ATOM   2126  O   ALA A 447     -12.086  30.787 -54.886  1.00 21.45           O  
ANISOU 2126  O   ALA A 447     1987   3005   3158    168    737    -94       O  
ATOM   2127  CB  ALA A 447     -13.684  33.506 -55.558  1.00 15.16           C  
ANISOU 2127  CB  ALA A 447     1177   2082   2502    212    745    -62       C  
ATOM   2128  N   TYR A 448     -11.308  32.437 -53.554  1.00 18.31           N  
ANISOU 2128  N   TYR A 448     1559   2581   2817    134    805   -152       N  
ATOM   2129  CA  TYR A 448      -9.981  31.836 -53.374  1.00 18.27           C  
ANISOU 2129  CA  TYR A 448     1557   2614   2771    107    814   -156       C  
ATOM   2130  C   TYR A 448      -9.775  31.353 -51.933  1.00 23.44           C  
ANISOU 2130  C   TYR A 448     2185   3313   3410     75    817   -202       C  
ATOM   2131  O   TYR A 448      -8.647  31.209 -51.485  1.00 23.25           O  
ANISOU 2131  O   TYR A 448     2152   3312   3372     44    822   -211       O  
ATOM   2132  CB  TYR A 448      -8.838  32.727 -53.924  1.00 19.65           C  
ANISOU 2132  CB  TYR A 448     1745   2756   2963     91    843   -138       C  
ATOM   2133  CG  TYR A 448      -8.659  34.064 -53.230  1.00 22.26           C  
ANISOU 2133  CG  TYR A 448     2066   3046   3345     65    868   -171       C  
ATOM   2134  CD1 TYR A 448      -9.280  35.210 -53.711  1.00 24.28           C  
ANISOU 2134  CD1 TYR A 448     2337   3238   3649     84    879   -161       C  
ATOM   2135  CD2 TYR A 448      -7.789  34.201 -52.151  1.00 23.54           C  
ANISOU 2135  CD2 TYR A 448     2209   3226   3508     18    875   -209       C  
ATOM   2136  CE1 TYR A 448      -9.110  36.445 -53.080  1.00 25.43           C  
ANISOU 2136  CE1 TYR A 448     2483   3335   3843     60    904   -195       C  
ATOM   2137  CE2 TYR A 448      -7.624  35.420 -51.504  1.00 25.35           C  
ANISOU 2137  CE2 TYR A 448     2444   3410   3778    -13    892   -245       C  
ATOM   2138  CZ  TYR A 448      -8.291  36.543 -51.969  1.00 33.66           C  
ANISOU 2138  CZ  TYR A 448     3515   4394   4879     10    911   -241       C  
ATOM   2139  OH  TYR A 448      -8.111  37.744 -51.327  1.00 33.22           O  
ANISOU 2139  OH  TYR A 448     3474   4285   4865    -20    930   -281       O  
ATOM   2140  N   GLY A 449     -10.893  31.117 -51.233  1.00 22.42           N  
ANISOU 2140  N   GLY A 449     2039   3194   3285     84    812   -225       N  
ATOM   2141  CA  GLY A 449     -10.985  30.553 -49.888  1.00 22.31           C  
ANISOU 2141  CA  GLY A 449     2009   3222   3245     59    815   -264       C  
ATOM   2142  C   GLY A 449     -10.628  31.396 -48.682  1.00 27.23           C  
ANISOU 2142  C   GLY A 449     2638   3836   3872     24    844   -317       C  
ATOM   2143  O   GLY A 449     -10.087  30.846 -47.716  1.00 27.20           O  
ANISOU 2143  O   GLY A 449     2633   3874   3826    -11    835   -340       O  
ATOM   2144  N   TYR A 450     -10.993  32.696 -48.661  1.00 24.88           N  
ANISOU 2144  N   TYR A 450     2352   3482   3620     31    876   -340       N  
ATOM   2145  CA  TYR A 450     -10.641  33.499 -47.494  1.00 26.27           C  
ANISOU 2145  CA  TYR A 450     2550   3640   3791     -8    902   -398       C  
ATOM   2146  C   TYR A 450     -11.701  34.084 -46.556  1.00 32.72           C  
ANISOU 2146  C   TYR A 450     3381   4430   4621      4    950   -448       C  
ATOM   2147  O   TYR A 450     -11.474  34.098 -45.343  1.00 35.42           O  
ANISOU 2147  O   TYR A 450     3751   4787   4919    -32    964   -499       O  
ATOM   2148  CB  TYR A 450      -9.491  34.466 -47.771  1.00 28.27           C  
ANISOU 2148  CB  TYR A 450     2819   3855   4066    -41    898   -401       C  
ATOM   2149  CG  TYR A 450      -8.157  33.882 -47.355  1.00 31.42           C  
ANISOU 2149  CG  TYR A 450     3211   4300   4427    -92    863   -397       C  
ATOM   2150  CD1 TYR A 450      -7.520  34.304 -46.193  1.00 34.29           C  
ANISOU 2150  CD1 TYR A 450     3598   4663   4770   -149    853   -444       C  
ATOM   2151  CD2 TYR A 450      -7.564  32.853 -48.084  1.00 31.81           C  
ANISOU 2151  CD2 TYR A 450     3233   4392   4462    -81    838   -344       C  
ATOM   2152  CE1 TYR A 450      -6.286  33.774 -45.809  1.00 35.08           C  
ANISOU 2152  CE1 TYR A 450     3680   4803   4845   -198    809   -431       C  
ATOM   2153  CE2 TYR A 450      -6.356  32.285 -47.683  1.00 32.73           C  
ANISOU 2153  CE2 TYR A 450     3330   4548   4557   -122    808   -333       C  
ATOM   2154  CZ  TYR A 450      -5.713  32.756 -46.551  1.00 39.00           C  
ANISOU 2154  CZ  TYR A 450     4135   5343   5342   -181    789   -372       C  
ATOM   2155  OH  TYR A 450      -4.503  32.220 -46.165  1.00 38.13           O  
ANISOU 2155  OH  TYR A 450     3996   5270   5222   -224    748   -351       O  
ATOM   2156  N   GLY A 451     -12.835  34.542 -47.040  1.00 28.23           N  
ANISOU 2156  N   GLY A 451     2796   3820   4109     54    977   -434       N  
ATOM   2157  CA  GLY A 451     -13.808  35.096 -46.085  1.00 27.60           C  
ANISOU 2157  CA  GLY A 451     2726   3711   4050     72   1040   -481       C  
ATOM   2158  C   GLY A 451     -14.740  34.071 -45.458  1.00 28.82           C  
ANISOU 2158  C   GLY A 451     2853   3916   4182     87   1057   -478       C  
ATOM   2159  O   GLY A 451     -15.911  34.371 -45.201  1.00 28.40           O  
ANISOU 2159  O   GLY A 451     2778   3835   4177    127   1110   -483       O  
ATOM   2160  N   LEU A 452     -14.221  32.843 -45.228  1.00 23.28           N  
ANISOU 2160  N   LEU A 452     2147   3284   3414     57   1014   -463       N  
ATOM   2161  CA  LEU A 452     -14.923  31.668 -44.694  1.00 21.88           C  
ANISOU 2161  CA  LEU A 452     1944   3162   3209     61   1017   -450       C  
ATOM   2162  C   LEU A 452     -13.953  30.692 -43.968  1.00 23.29           C  
ANISOU 2162  C   LEU A 452     2146   3404   3300     10    981   -459       C  
ATOM   2163  O   LEU A 452     -12.749  30.673 -44.247  1.00 20.40           O  
ANISOU 2163  O   LEU A 452     1796   3047   2910    -20    937   -455       O  
ATOM   2164  CB  LEU A 452     -15.666  30.932 -45.839  1.00 21.11           C  
ANISOU 2164  CB  LEU A 452     1793   3073   3156     98    976   -382       C  
ATOM   2165  CG  LEU A 452     -14.842  29.999 -46.763  1.00 24.13           C  
ANISOU 2165  CG  LEU A 452     2176   3487   3505     85    903   -339       C  
ATOM   2166  CD1 LEU A 452     -15.730  28.952 -47.410  1.00 24.48           C  
ANISOU 2166  CD1 LEU A 452     2183   3550   3567    107    864   -287       C  
ATOM   2167  CD2 LEU A 452     -14.068  30.771 -47.817  1.00 23.30           C  
ANISOU 2167  CD2 LEU A 452     2090   3343   3421     90    883   -325       C  
ATOM   2168  N   ASN A 453     -14.502  29.910 -43.031  1.00 19.62           N  
ANISOU 2168  N   ASN A 453     1680   2980   2795      1   1003   -466       N  
ATOM   2169  CA  ASN A 453     -13.786  28.910 -42.243  1.00 19.47           C  
ANISOU 2169  CA  ASN A 453     1682   3021   2696    -44    969   -467       C  
ATOM   2170  C   ASN A 453     -14.361  27.506 -42.518  1.00 23.32           C  
ANISOU 2170  C   ASN A 453     2127   3552   3183    -30    942   -414       C  
ATOM   2171  O   ASN A 453     -15.580  27.349 -42.614  1.00 22.39           O  
ANISOU 2171  O   ASN A 453     1973   3426   3109      2    975   -395       O  
ATOM   2172  CB  ASN A 453     -13.892  29.244 -40.751  1.00 20.87           C  
ANISOU 2172  CB  ASN A 453     1914   3204   2811    -74   1020   -524       C  
ATOM   2173  CG  ASN A 453     -12.796  30.129 -40.207  1.00 40.86           C  
ANISOU 2173  CG  ASN A 453     4508   5715   5301   -121   1005   -574       C  
ATOM   2174  OD1 ASN A 453     -12.419  30.012 -39.046  1.00 41.85           O  
ANISOU 2174  OD1 ASN A 453     4689   5865   5347   -167   1004   -608       O  
ATOM   2175  ND2 ASN A 453     -12.231  31.018 -41.014  1.00 26.63           N  
ANISOU 2175  ND2 ASN A 453     2701   3868   3549   -117    987   -577       N  
ATOM   2176  N   ALA A 454     -13.481  26.495 -42.644  1.00 19.79           N  
ANISOU 2176  N   ALA A 454     1679   3144   2695    -54    881   -386       N  
ATOM   2177  CA  ALA A 454     -13.870  25.114 -42.907  1.00 19.91           C  
ANISOU 2177  CA  ALA A 454     1666   3194   2706    -46    847   -338       C  
ATOM   2178  C   ALA A 454     -13.150  24.113 -41.996  1.00 23.73           C  
ANISOU 2178  C   ALA A 454     2169   3728   3118    -86    817   -331       C  
ATOM   2179  O   ALA A 454     -12.132  24.437 -41.383  1.00 22.47           O  
ANISOU 2179  O   ALA A 454     2041   3580   2916   -120    802   -356       O  
ATOM   2180  CB  ALA A 454     -13.584  24.767 -44.368  1.00 20.23           C  
ANISOU 2180  CB  ALA A 454     1687   3217   2783    -20    797   -297       C  
ATOM   2181  N   THR A 455     -13.659  22.872 -41.956  1.00 20.03           N  
ANISOU 2181  N   THR A 455     1681   3287   2644    -83    798   -292       N  
ATOM   2182  CA  THR A 455     -13.012  21.786 -41.231  1.00 19.29           C  
ANISOU 2182  CA  THR A 455     1601   3236   2490   -115    762   -273       C  
ATOM   2183  C   THR A 455     -12.526  20.774 -42.256  1.00 23.29           C  
ANISOU 2183  C   THR A 455     2089   3742   3017    -98    703   -227       C  
ATOM   2184  O   THR A 455     -12.964  20.786 -43.416  1.00 21.78           O  
ANISOU 2184  O   THR A 455     1881   3521   2875    -66    694   -211       O  
ATOM   2185  CB  THR A 455     -13.920  21.171 -40.172  1.00 23.40           C  
ANISOU 2185  CB  THR A 455     2126   3785   2980   -131    796   -265       C  
ATOM   2186  OG1 THR A 455     -15.049  20.574 -40.800  1.00 20.20           O  
ANISOU 2186  OG1 THR A 455     1677   3369   2630   -105    800   -228       O  
ATOM   2187  CG2 THR A 455     -14.359  22.175 -39.119  1.00 23.97           C  
ANISOU 2187  CG2 THR A 455     2232   3855   3022   -144    869   -315       C  
ATOM   2188  N   ILE A 456     -11.615  19.910 -41.831  1.00 21.16           N  
ANISOU 2188  N   ILE A 456     1829   3501   2709   -120    662   -207       N  
ATOM   2189  CA  ILE A 456     -11.064  18.824 -42.631  1.00 22.05           C  
ANISOU 2189  CA  ILE A 456     1932   3610   2836   -102    616   -165       C  
ATOM   2190  C   ILE A 456     -12.210  17.852 -43.051  1.00 20.11           C  
ANISOU 2190  C   ILE A 456     1675   3354   2610    -86    608   -135       C  
ATOM   2191  O   ILE A 456     -12.171  17.298 -44.146  1.00 17.73           O  
ANISOU 2191  O   ILE A 456     1375   3027   2335    -60    581   -114       O  
ATOM   2192  CB  ILE A 456      -9.902  18.170 -41.823  1.00 28.55           C  
ANISOU 2192  CB  ILE A 456     2761   4466   3619   -130    578   -146       C  
ATOM   2193  CG1 ILE A 456      -8.756  19.193 -41.617  1.00 32.02           C  
ANISOU 2193  CG1 ILE A 456     3203   4906   4056   -149    572   -169       C  
ATOM   2194  CG2 ILE A 456      -9.310  16.979 -42.522  1.00 30.97           C  
ANISOU 2194  CG2 ILE A 456     3059   4764   3943   -107    539   -103       C  
ATOM   2195  CD1 ILE A 456      -7.944  19.077 -40.223  1.00 52.51           C  
ANISOU 2195  CD1 ILE A 456     5814   7540   6596   -202    536   -168       C  
ATOM   2196  N   LEU A 457     -13.260  17.734 -42.221  1.00 15.44           N  
ANISOU 2196  N   LEU A 457     1077   2780   2011   -103    637   -135       N  
ATOM   2197  CA  LEU A 457     -14.432  16.890 -42.485  1.00 14.55           C  
ANISOU 2197  CA  LEU A 457      943   2658   1929    -98    630   -102       C  
ATOM   2198  C   LEU A 457     -15.287  17.416 -43.654  1.00 17.02           C  
ANISOU 2198  C   LEU A 457     1233   2930   2304    -68    630   -101       C  
ATOM   2199  O   LEU A 457     -15.693  16.634 -44.507  1.00 15.84           O  
ANISOU 2199  O   LEU A 457     1080   2758   2181    -59    586    -71       O  
ATOM   2200  CB  LEU A 457     -15.280  16.744 -41.219  1.00 14.78           C  
ANISOU 2200  CB  LEU A 457      963   2715   1936   -125    675    -97       C  
ATOM   2201  CG  LEU A 457     -14.618  15.989 -40.081  1.00 20.10           C  
ANISOU 2201  CG  LEU A 457     1665   3428   2543   -159    662    -83       C  
ATOM   2202  CD1 LEU A 457     -15.294  16.324 -38.758  1.00 21.12           C  
ANISOU 2202  CD1 LEU A 457     1807   3587   2633   -186    728    -96       C  
ATOM   2203  CD2 LEU A 457     -14.700  14.505 -40.309  1.00 24.68           C  
ANISOU 2203  CD2 LEU A 457     2240   4006   3132   -164    613    -31       C  
ATOM   2204  N   GLN A 458     -15.552  18.743 -43.679  1.00 14.00           N  
ANISOU 2204  N   GLN A 458      841   2535   1943    -55    674   -134       N  
ATOM   2205  CA  GLN A 458     -16.282  19.453 -44.722  1.00 13.55           C  
ANISOU 2205  CA  GLN A 458      763   2438   1947    -26    673   -131       C  
ATOM   2206  C   GLN A 458     -15.468  19.443 -46.002  1.00 18.36           C  
ANISOU 2206  C   GLN A 458     1401   3021   2554     -6    626   -127       C  
ATOM   2207  O   GLN A 458     -16.020  19.406 -47.090  1.00 17.93           O  
ANISOU 2207  O   GLN A 458     1345   2933   2534     13    593   -106       O  
ATOM   2208  CB  GLN A 458     -16.541  20.906 -44.294  1.00 15.06           C  
ANISOU 2208  CB  GLN A 458      945   2619   2158    -16    737   -170       C  
ATOM   2209  CG  GLN A 458     -17.520  21.049 -43.122  1.00 15.80           C  
ANISOU 2209  CG  GLN A 458     1015   2730   2260    -26    803   -177       C  
ATOM   2210  CD  GLN A 458     -17.520  22.449 -42.573  1.00 23.63           C  
ANISOU 2210  CD  GLN A 458     2019   3706   3253    -16    873   -226       C  
ATOM   2211  OE1 GLN A 458     -16.523  23.177 -42.634  1.00 19.20           O  
ANISOU 2211  OE1 GLN A 458     1495   3136   2662    -22    869   -262       O  
ATOM   2212  NE2 GLN A 458     -18.657  22.876 -42.063  1.00 21.34           N  
ANISOU 2212  NE2 GLN A 458     1697   3406   3006     -2    942   -228       N  
ATOM   2213  N   LEU A 459     -14.149  19.504 -45.870  1.00 18.21           N  
ANISOU 2213  N   LEU A 459     1410   3015   2495    -11    625   -143       N  
ATOM   2214  CA  LEU A 459     -13.224  19.447 -46.996  1.00 18.47           C  
ANISOU 2214  CA  LEU A 459     1471   3024   2522      9    599   -136       C  
ATOM   2215  C   LEU A 459     -13.213  18.051 -47.608  1.00 22.01           C  
ANISOU 2215  C   LEU A 459     1940   3463   2958     16    552   -103       C  
ATOM   2216  O   LEU A 459     -13.321  17.924 -48.832  1.00 21.64           O  
ANISOU 2216  O   LEU A 459     1923   3381   2920     38    526    -91       O  
ATOM   2217  CB  LEU A 459     -11.820  19.869 -46.558  1.00 18.18           C  
ANISOU 2217  CB  LEU A 459     1442   3005   2460     -1    614   -154       C  
ATOM   2218  CG  LEU A 459     -11.264  21.179 -47.100  1.00 23.49           C  
ANISOU 2218  CG  LEU A 459     2120   3654   3152     10    638   -174       C  
ATOM   2219  CD1 LEU A 459     -12.261  21.950 -47.959  1.00 23.78           C  
ANISOU 2219  CD1 LEU A 459     2156   3653   3227     33    647   -174       C  
ATOM   2220  CD2 LEU A 459     -10.678  22.004 -46.010  1.00 24.70           C  
ANISOU 2220  CD2 LEU A 459     2267   3826   3292    -21    662   -205       C  
ATOM   2221  N   ALA A 460     -13.100  17.010 -46.757  1.00 18.96           N  
ANISOU 2221  N   ALA A 460     1550   3104   2550     -4    540    -89       N  
ATOM   2222  CA  ALA A 460     -13.105  15.588 -47.155  1.00 18.40           C  
ANISOU 2222  CA  ALA A 460     1502   3020   2470     -2    497    -60       C  
ATOM   2223  C   ALA A 460     -14.403  15.209 -47.845  1.00 21.58           C  
ANISOU 2223  C   ALA A 460     1906   3391   2902     -2    462    -41       C  
ATOM   2224  O   ALA A 460     -14.378  14.473 -48.829  1.00 21.40           O  
ANISOU 2224  O   ALA A 460     1925   3332   2873     11    421    -28       O  
ATOM   2225  CB  ALA A 460     -12.919  14.710 -45.935  1.00 19.20           C  
ANISOU 2225  CB  ALA A 460     1591   3155   2548    -29    494    -44       C  
ATOM   2226  N   GLN A 461     -15.541  15.707 -47.322  1.00 17.97           N  
ANISOU 2226  N   GLN A 461     1405   2945   2478    -17    479    -39       N  
ATOM   2227  CA  GLN A 461     -16.847  15.387 -47.891  1.00 17.71           C  
ANISOU 2227  CA  GLN A 461     1354   2885   2490    -24    439    -11       C  
ATOM   2228  C   GLN A 461     -17.085  16.061 -49.247  1.00 20.85           C  
ANISOU 2228  C   GLN A 461     1774   3240   2907      0    409    -12       C  
ATOM   2229  O   GLN A 461     -17.652  15.416 -50.130  1.00 23.44           O  
ANISOU 2229  O   GLN A 461     2127   3533   3246     -5    345     12       O  
ATOM   2230  CB  GLN A 461     -17.999  15.502 -46.864  1.00 18.21           C  
ANISOU 2230  CB  GLN A 461     1353   2972   2595    -46    471      4       C  
ATOM   2231  CG  GLN A 461     -18.639  16.876 -46.783  1.00 21.58           C  
ANISOU 2231  CG  GLN A 461     1737   3397   3066    -30    518    -11       C  
ATOM   2232  CD  GLN A 461     -19.476  17.131 -45.563  1.00 32.21           C  
ANISOU 2232  CD  GLN A 461     3028   4770   4442    -43    583     -7       C  
ATOM   2233  OE1 GLN A 461     -19.785  18.283 -45.222  1.00 32.30           O  
ANISOU 2233  OE1 GLN A 461     3013   4781   4478    -27    643    -30       O  
ATOM   2234  NE2 GLN A 461     -19.850  16.090 -44.866  1.00 24.14           N  
ANISOU 2234  NE2 GLN A 461     1990   3768   3415    -72    580     22       N  
ATOM   2235  N   GLY A 462     -16.541  17.268 -49.430  1.00 14.17           N  
ANISOU 2235  N   GLY A 462      931   2395   2058     21    448    -39       N  
ATOM   2236  CA  GLY A 462     -16.622  18.035 -50.672  1.00 13.95           C  
ANISOU 2236  CA  GLY A 462      930   2329   2041     45    427    -37       C  
ATOM   2237  C   GLY A 462     -15.786  17.438 -51.792  1.00 18.26           C  
ANISOU 2237  C   GLY A 462     1554   2847   2537     60    395    -35       C  
ATOM   2238  O   GLY A 462     -16.226  17.384 -52.954  1.00 19.21           O  
ANISOU 2238  O   GLY A 462     1717   2927   2654     68    344    -19       O  
ATOM   2239  N   TYR A 463     -14.567  16.979 -51.458  1.00 12.73           N  
ANISOU 2239  N   TYR A 463      877   2164   1796     66    424    -50       N  
ATOM   2240  CA  TYR A 463     -13.697  16.294 -52.432  1.00 11.47           C  
ANISOU 2240  CA  TYR A 463      791   1975   1592     87    412    -48       C  
ATOM   2241  C   TYR A 463     -14.230  14.870 -52.767  1.00 14.79           C  
ANISOU 2241  C   TYR A 463     1254   2369   1999     75    352    -30       C  
ATOM   2242  O   TYR A 463     -14.233  14.481 -53.941  1.00 15.78           O  
ANISOU 2242  O   TYR A 463     1455   2449   2092     89    318    -27       O  
ATOM   2243  CB  TYR A 463     -12.231  16.307 -51.983  1.00 11.65           C  
ANISOU 2243  CB  TYR A 463      810   2021   1595    100    465    -60       C  
ATOM   2244  CG  TYR A 463     -11.523  17.594 -52.355  1.00 13.59           C  
ANISOU 2244  CG  TYR A 463     1052   2266   1845    117    510    -73       C  
ATOM   2245  CD1 TYR A 463     -11.680  18.749 -51.589  1.00 15.43           C  
ANISOU 2245  CD1 TYR A 463     1231   2523   2107    102    538    -88       C  
ATOM   2246  CD2 TYR A 463     -10.696  17.661 -53.473  1.00 14.76           C  
ANISOU 2246  CD2 TYR A 463     1256   2384   1967    147    531    -68       C  
ATOM   2247  CE1 TYR A 463     -11.073  19.949 -51.952  1.00 13.17           C  
ANISOU 2247  CE1 TYR A 463      944   2228   1832    112    574    -98       C  
ATOM   2248  CE2 TYR A 463     -10.042  18.844 -53.818  1.00 16.16           C  
ANISOU 2248  CE2 TYR A 463     1428   2559   2155    159    575    -72       C  
ATOM   2249  CZ  TYR A 463     -10.241  19.988 -53.057  1.00 23.16           C  
ANISOU 2249  CZ  TYR A 463     2256   3466   3076    139    592    -86       C  
ATOM   2250  OH  TYR A 463      -9.605  21.156 -53.382  1.00 26.21           O  
ANISOU 2250  OH  TYR A 463     2639   3843   3478    145    631    -89       O  
ATOM   2251  N   ALA A 464     -14.759  14.140 -51.759  1.00 10.09           N  
ANISOU 2251  N   ALA A 464      614   1796   1424     47    338    -18       N  
ATOM   2252  CA  ALA A 464     -15.405  12.814 -51.950  1.00 10.68           C  
ANISOU 2252  CA  ALA A 464      718   1842   1498     26    276      3       C  
ATOM   2253  C   ALA A 464     -16.567  12.927 -52.935  1.00 19.07           C  
ANISOU 2253  C   ALA A 464     1801   2863   2579     13    207     19       C  
ATOM   2254  O   ALA A 464     -16.779  12.010 -53.728  1.00 19.69           O  
ANISOU 2254  O   ALA A 464     1951   2896   2635      5    147     26       O  
ATOM   2255  CB  ALA A 464     -15.917  12.268 -50.613  1.00 10.64           C  
ANISOU 2255  CB  ALA A 464      648   1873   1523     -7    280     20       C  
ATOM   2256  N   MET A 465     -17.318  14.080 -52.883  1.00 17.18           N  
ANISOU 2256  N   MET A 465     1504   2639   2385     10    213     25       N  
ATOM   2257  CA  MET A 465     -18.433  14.428 -53.762  1.00 16.47           C  
ANISOU 2257  CA  MET A 465     1415   2514   2328     -1    145     49       C  
ATOM   2258  C   MET A 465     -17.898  14.615 -55.186  1.00 21.24           C  
ANISOU 2258  C   MET A 465     2124   3074   2873     23    117     39       C  
ATOM   2259  O   MET A 465     -18.390  13.983 -56.116  1.00 21.76           O  
ANISOU 2259  O   MET A 465     2256   3094   2918      7     36     54       O  
ATOM   2260  CB  MET A 465     -19.101  15.706 -53.232  1.00 18.91           C  
ANISOU 2260  CB  MET A 465     1632   2848   2703      4    182     57       C  
ATOM   2261  CG  MET A 465     -20.260  16.248 -54.076  1.00 23.02           C  
ANISOU 2261  CG  MET A 465     2135   3335   3276     -2    113     91       C  
ATOM   2262  SD  MET A 465     -19.830  17.410 -55.398  1.00 26.93           S  
ANISOU 2262  SD  MET A 465     2697   3796   3738     32    102     85       S  
ATOM   2263  CE  MET A 465     -19.140  18.773 -54.432  1.00 22.59           C  
ANISOU 2263  CE  MET A 465     2087   3288   3209     62    222     52       C  
ATOM   2264  N   LEU A 466     -16.883  15.468 -55.350  1.00 18.77           N  
ANISOU 2264  N   LEU A 466     1828   2773   2529     57    185     16       N  
ATOM   2265  CA  LEU A 466     -16.226  15.765 -56.634  1.00 19.12           C  
ANISOU 2265  CA  LEU A 466     1972   2781   2513     83    184      8       C  
ATOM   2266  C   LEU A 466     -15.702  14.496 -57.334  1.00 22.39           C  
ANISOU 2266  C   LEU A 466     2494   3155   2858     89    160     -2       C  
ATOM   2267  O   LEU A 466     -15.687  14.456 -58.558  1.00 21.88           O  
ANISOU 2267  O   LEU A 466     2530   3045   2738     97    126     -1       O  
ATOM   2268  CB  LEU A 466     -15.035  16.709 -56.361  1.00 18.50           C  
ANISOU 2268  CB  LEU A 466     1874   2729   2425    114    278    -14       C  
ATOM   2269  CG  LEU A 466     -15.065  18.167 -56.756  1.00 22.02           C  
ANISOU 2269  CG  LEU A 466     2304   3172   2889    129    302    -10       C  
ATOM   2270  CD1 LEU A 466     -16.481  18.734 -56.925  1.00 22.46           C  
ANISOU 2270  CD1 LEU A 466     2318   3215   3001    112    239     18       C  
ATOM   2271  CD2 LEU A 466     -14.208  18.993 -55.823  1.00 20.21           C  
ANISOU 2271  CD2 LEU A 466     2011   2982   2684    138    386    -30       C  
ATOM   2272  N   ALA A 467     -15.240  13.485 -56.551  1.00 18.41           N  
ANISOU 2272  N   ALA A 467     1977   2666   2354     85    182    -11       N  
ATOM   2273  CA  ALA A 467     -14.727  12.187 -57.029  1.00 18.22           C  
ANISOU 2273  CA  ALA A 467     2048   2599   2276     95    170    -22       C  
ATOM   2274  C   ALA A 467     -15.801  11.052 -57.109  1.00 24.92           C  
ANISOU 2274  C   ALA A 467     2924   3410   3135     52     72     -6       C  
ATOM   2275  O   ALA A 467     -15.471   9.934 -57.553  1.00 25.71           O  
ANISOU 2275  O   ALA A 467     3116   3462   3190     56     54    -18       O  
ATOM   2276  CB  ALA A 467     -13.585  11.738 -56.142  1.00 18.02           C  
ANISOU 2276  CB  ALA A 467     1989   2602   2255    117    244    -32       C  
ATOM   2277  N   ASN A 468     -17.049  11.319 -56.647  1.00 19.24           N  
ANISOU 2277  N   ASN A 468     2122   2709   2480     11     16     21       N  
ATOM   2278  CA  ASN A 468     -18.141  10.341 -56.685  1.00 20.05           C  
ANISOU 2278  CA  ASN A 468     2231   2778   2609    -38    -80     45       C  
ATOM   2279  C   ASN A 468     -19.280  10.800 -57.601  1.00 25.18           C  
ANISOU 2279  C   ASN A 468     2896   3396   3276    -67   -178     71       C  
ATOM   2280  O   ASN A 468     -20.441  10.692 -57.224  1.00 25.84           O  
ANISOU 2280  O   ASN A 468     2901   3484   3434   -109   -239    108       O  
ATOM   2281  CB  ASN A 468     -18.686  10.012 -55.258  1.00 18.02           C  
ANISOU 2281  CB  ASN A 468     1854   2567   2427    -68    -65     69       C  
ATOM   2282  CG  ASN A 468     -19.359   8.667 -55.184  1.00 24.69           C  
ANISOU 2282  CG  ASN A 468     2719   3372   3289   -113   -142     91       C  
ATOM   2283  OD1 ASN A 468     -18.851   7.677 -55.713  1.00 22.21           O  
ANISOU 2283  OD1 ASN A 468     2510   3007   2922   -109   -166     73       O  
ATOM   2284  ND2 ASN A 468     -20.527   8.599 -54.556  1.00 13.11           N  
ANISOU 2284  ND2 ASN A 468     1157   1923   1903   -157   -180    131       N  
ATOM   2285  N   HIS A 469     -18.952  11.334 -58.782  1.00 23.25           N  
ANISOU 2285  N   HIS A 469     2747   3120   2969    -44   -190     58       N  
ATOM   2286  CA  HIS A 469     -19.913  11.837 -59.777  1.00 24.74           C  
ANISOU 2286  CA  HIS A 469     2965   3274   3160    -69   -291     87       C  
ATOM   2287  C   HIS A 469     -20.942  12.828 -59.208  1.00 28.29           C  
ANISOU 2287  C   HIS A 469     3270   3762   3717    -83   -307    128       C  
ATOM   2288  O   HIS A 469     -22.111  12.784 -59.580  1.00 28.88           O  
ANISOU 2288  O   HIS A 469     3320   3811   3841   -124   -414    170       O  
ATOM   2289  CB  HIS A 469     -20.576  10.692 -60.574  1.00 26.43           C  
ANISOU 2289  CB  HIS A 469     3281   3419   3340   -117   -418     96       C  
ATOM   2290  CG  HIS A 469     -19.574   9.787 -61.194  1.00 30.50           C  
ANISOU 2290  CG  HIS A 469     3952   3886   3748    -95   -392     51       C  
ATOM   2291  ND1 HIS A 469     -19.030  10.063 -62.430  1.00 33.42           N  
ANISOU 2291  ND1 HIS A 469     4468   4216   4016    -70   -391     29       N  
ATOM   2292  CD2 HIS A 469     -18.984   8.681 -60.688  1.00 33.13           C  
ANISOU 2292  CD2 HIS A 469     4313   4208   4067    -88   -351     27       C  
ATOM   2293  CE1 HIS A 469     -18.144   9.105 -62.655  1.00 33.50           C  
ANISOU 2293  CE1 HIS A 469     4588   4187   3953    -46   -344    -11       C  
ATOM   2294  NE2 HIS A 469     -18.069   8.257 -61.626  1.00 33.60           N  
ANISOU 2294  NE2 HIS A 469     4531   4214   4019    -54   -321    -13       N  
ATOM   2295  N   GLY A 470     -20.479  13.691 -58.301  1.00 22.59           N  
ANISOU 2295  N   GLY A 470     2455   3096   3032    -51   -200    117       N  
ATOM   2296  CA  GLY A 470     -21.283  14.732 -57.678  1.00 21.70           C  
ANISOU 2296  CA  GLY A 470     2211   3017   3016    -51   -183    146       C  
ATOM   2297  C   GLY A 470     -22.241  14.244 -56.622  1.00 24.46           C  
ANISOU 2297  C   GLY A 470     2445   3390   3457    -85   -195    175       C  
ATOM   2298  O   GLY A 470     -23.168  14.981 -56.254  1.00 22.64           O  
ANISOU 2298  O   GLY A 470     2108   3174   3319    -88   -195    209       O  
ATOM   2299  N   VAL A 471     -21.998  13.003 -56.113  1.00 20.84           N  
ANISOU 2299  N   VAL A 471     2008   2933   2978   -107   -194    165       N  
ATOM   2300  CA  VAL A 471     -22.797  12.357 -55.060  1.00 20.62           C  
ANISOU 2300  CA  VAL A 471     1882   2926   3026   -143   -196    196       C  
ATOM   2301  C   VAL A 471     -22.018  12.361 -53.748  1.00 23.66           C  
ANISOU 2301  C   VAL A 471     2223   3367   3399   -123    -79    168       C  
ATOM   2302  O   VAL A 471     -21.077  11.585 -53.585  1.00 21.67           O  
ANISOU 2302  O   VAL A 471     2036   3115   3084   -116    -55    140       O  
ATOM   2303  CB  VAL A 471     -23.320  10.926 -55.424  1.00 23.94           C  
ANISOU 2303  CB  VAL A 471     2352   3300   3446   -195   -301    219       C  
ATOM   2304  CG1 VAL A 471     -24.130  10.322 -54.283  1.00 23.73           C  
ANISOU 2304  CG1 VAL A 471     2215   3297   3504   -234   -291    258       C  
ATOM   2305  CG2 VAL A 471     -24.147  10.940 -56.696  1.00 24.42           C  
ANISOU 2305  CG2 VAL A 471     2461   3302   3514   -226   -433    249       C  
ATOM   2306  N   GLU A 472     -22.436  13.222 -52.808  1.00 22.16           N  
ANISOU 2306  N   GLU A 472     1926   3221   3272   -113     -8    177       N  
ATOM   2307  CA  GLU A 472     -21.852  13.307 -51.473  1.00 21.96           C  
ANISOU 2307  CA  GLU A 472     1860   3249   3234   -102     95    153       C  
ATOM   2308  C   GLU A 472     -22.445  12.240 -50.538  1.00 25.71           C  
ANISOU 2308  C   GLU A 472     2286   3738   3744   -142     93    186       C  
ATOM   2309  O   GLU A 472     -23.571  12.376 -50.075  1.00 27.74           O  
ANISOU 2309  O   GLU A 472     2452   4005   4084   -162     97    225       O  
ATOM   2310  CB  GLU A 472     -22.050  14.704 -50.875  1.00 23.99           C  
ANISOU 2310  CB  GLU A 472     2044   3539   3532    -75    177    143       C  
ATOM   2311  CG  GLU A 472     -21.117  14.973 -49.702  1.00 41.78           C  
ANISOU 2311  CG  GLU A 472     4294   5841   5740    -61    277    104       C  
ATOM   2312  CD  GLU A 472     -21.532  16.090 -48.767  1.00 65.30           C  
ANISOU 2312  CD  GLU A 472     7198   8849   8762    -47    364     95       C  
ATOM   2313  OE1 GLU A 472     -21.561  17.262 -49.208  1.00 68.64           O  
ANISOU 2313  OE1 GLU A 472     7614   9260   9208    -19    382     81       O  
ATOM   2314  OE2 GLU A 472     -21.769  15.801 -47.573  1.00 58.78           O  
ANISOU 2314  OE2 GLU A 472     6332   8058   7943    -64    419     99       O  
ATOM   2315  N   MET A 473     -21.673  11.195 -50.254  1.00 21.21           N  
ANISOU 2315  N   MET A 473     1774   3168   3116   -151     92    173       N  
ATOM   2316  CA  MET A 473     -22.040  10.128 -49.328  1.00 20.14           C  
ANISOU 2316  CA  MET A 473     1606   3045   3002   -188     94    204       C  
ATOM   2317  C   MET A 473     -21.910  10.626 -47.877  1.00 25.00           C  
ANISOU 2317  C   MET A 473     2156   3723   3619   -182    200    199       C  
ATOM   2318  O   MET A 473     -20.926  11.303 -47.549  1.00 25.16           O  
ANISOU 2318  O   MET A 473     2200   3773   3586   -151    260    157       O  
ATOM   2319  CB  MET A 473     -21.186   8.874 -49.567  1.00 21.91           C  
ANISOU 2319  CB  MET A 473     1921   3239   3163   -194     58    193       C  
ATOM   2320  CG  MET A 473     -21.533   8.137 -50.851  1.00 25.69           C  
ANISOU 2320  CG  MET A 473     2474   3648   3641   -213    -50    202       C  
ATOM   2321  SD  MET A 473     -23.238   7.482 -50.916  1.00 29.76           S  
ANISOU 2321  SD  MET A 473     2922   4131   4256   -281   -142    269       S  
ATOM   2322  CE  MET A 473     -23.089   6.148 -49.876  1.00 26.32           C  
ANISOU 2322  CE  MET A 473     2482   3699   3820   -314   -125    293       C  
ATOM   2323  N   PRO A 474     -22.910  10.328 -47.006  1.00 22.37           N  
ANISOU 2323  N   PRO A 474     1745   3410   3346   -214    224    242       N  
ATOM   2324  CA  PRO A 474     -22.863  10.815 -45.616  1.00 21.19           C  
ANISOU 2324  CA  PRO A 474     1548   3316   3186   -210    331    235       C  
ATOM   2325  C   PRO A 474     -21.640  10.321 -44.868  1.00 23.63           C  
ANISOU 2325  C   PRO A 474     1917   3654   3407   -208    361    211       C  
ATOM   2326  O   PRO A 474     -21.351   9.129 -44.916  1.00 25.91           O  
ANISOU 2326  O   PRO A 474     2245   3923   3675   -229    312    231       O  
ATOM   2327  CB  PRO A 474     -24.161  10.238 -45.006  1.00 23.34           C  
ANISOU 2327  CB  PRO A 474     1739   3592   3539   -250    339    298       C  
ATOM   2328  CG  PRO A 474     -25.048  10.006 -46.136  1.00 27.13           C  
ANISOU 2328  CG  PRO A 474     2193   4021   4095   -268    242    334       C  
ATOM   2329  CD  PRO A 474     -24.158   9.564 -47.250  1.00 23.16           C  
ANISOU 2329  CD  PRO A 474     1795   3478   3528   -259    157    302       C  
ATOM   2330  N   LEU A 475     -20.913  11.227 -44.208  1.00 18.31           N  
ANISOU 2330  N   LEU A 475     1253   3019   2684   -184    433    170       N  
ATOM   2331  CA  LEU A 475     -19.730  10.873 -43.423  1.00 18.49           C  
ANISOU 2331  CA  LEU A 475     1325   3073   2628   -185    456    152       C  
ATOM   2332  C   LEU A 475     -20.129   9.994 -42.233  1.00 25.06           C  
ANISOU 2332  C   LEU A 475     2140   3932   3451   -223    482    194       C  
ATOM   2333  O   LEU A 475     -21.136  10.287 -41.580  1.00 25.50           O  
ANISOU 2333  O   LEU A 475     2139   4006   3542   -238    538    214       O  
ATOM   2334  CB  LEU A 475     -18.972  12.141 -42.963  1.00 17.80           C  
ANISOU 2334  CB  LEU A 475     1248   3018   2497   -161    518    102       C  
ATOM   2335  CG  LEU A 475     -17.597  12.412 -43.589  1.00 20.98           C  
ANISOU 2335  CG  LEU A 475     1704   3413   2856   -134    493     66       C  
ATOM   2336  CD1 LEU A 475     -17.599  12.277 -45.091  1.00 20.29           C  
ANISOU 2336  CD1 LEU A 475     1639   3274   2795   -112    434     65       C  
ATOM   2337  CD2 LEU A 475     -17.100  13.765 -43.215  1.00 23.47           C  
ANISOU 2337  CD2 LEU A 475     2019   3751   3149   -119    549     21       C  
ATOM   2338  N   SER A 476     -19.380   8.892 -41.984  1.00 22.19           N  
ANISOU 2338  N   SER A 476     1820   3565   3045   -237    444    212       N  
ATOM   2339  CA  SER A 476     -19.714   7.984 -40.883  1.00 23.26           C  
ANISOU 2339  CA  SER A 476     1947   3722   3168   -275    463    259       C  
ATOM   2340  C   SER A 476     -18.501   7.352 -40.207  1.00 26.55           C  
ANISOU 2340  C   SER A 476     2417   4158   3513   -279    451    263       C  
ATOM   2341  O   SER A 476     -17.615   6.852 -40.894  1.00 24.87           O  
ANISOU 2341  O   SER A 476     2245   3914   3289   -258    396    256       O  
ATOM   2342  CB  SER A 476     -20.673   6.891 -41.375  1.00 27.93           C  
ANISOU 2342  CB  SER A 476     2516   4270   3828   -306    407    312       C  
ATOM   2343  OG  SER A 476     -20.729   5.744 -40.535  1.00 33.14           O  
ANISOU 2343  OG  SER A 476     3184   4935   4473   -342    405    363       O  
ATOM   2344  N   LEU A 477     -18.519   7.289 -38.860  1.00 24.64           N  
ANISOU 2344  N   LEU A 477     2176   3963   3223   -305    502    283       N  
ATOM   2345  CA  LEU A 477     -17.485   6.621 -38.055  1.00 24.13           C  
ANISOU 2345  CA  LEU A 477     2157   3919   3091   -317    482    302       C  
ATOM   2346  C   LEU A 477     -17.892   5.160 -37.755  1.00 26.73           C  
ANISOU 2346  C   LEU A 477     2490   4226   3439   -349    448    371       C  
ATOM   2347  O   LEU A 477     -17.118   4.406 -37.168  1.00 26.20           O  
ANISOU 2347  O   LEU A 477     2459   4165   3329   -359    421    401       O  
ATOM   2348  CB  LEU A 477     -17.176   7.381 -36.744  1.00 24.38           C  
ANISOU 2348  CB  LEU A 477     2209   4011   3045   -332    544    286       C  
ATOM   2349  CG  LEU A 477     -16.023   8.411 -36.753  1.00 29.44           C  
ANISOU 2349  CG  LEU A 477     2877   4672   3639   -309    542    230       C  
ATOM   2350  CD1 LEU A 477     -15.836   9.023 -35.362  1.00 30.43           C  
ANISOU 2350  CD1 LEU A 477     3035   4849   3677   -337    593    216       C  
ATOM   2351  CD2 LEU A 477     -14.668   7.798 -37.220  1.00 30.17           C  
ANISOU 2351  CD2 LEU A 477     2992   4745   3725   -290    466    239       C  
ATOM   2352  N   HIS A 478     -19.104   4.765 -38.156  1.00 23.64           N  
ANISOU 2352  N   HIS A 478     2060   3805   3119   -369    445    400       N  
ATOM   2353  CA  HIS A 478     -19.617   3.403 -37.949  1.00 24.19           C  
ANISOU 2353  CA  HIS A 478     2128   3844   3220   -407    411    468       C  
ATOM   2354  C   HIS A 478     -19.581   2.609 -39.242  1.00 27.02           C  
ANISOU 2354  C   HIS A 478     2504   4128   3634   -397    324    469       C  
ATOM   2355  O   HIS A 478     -19.816   3.170 -40.314  1.00 27.08           O  
ANISOU 2355  O   HIS A 478     2502   4109   3678   -375    302    431       O  
ATOM   2356  CB  HIS A 478     -21.053   3.449 -37.425  1.00 26.45           C  
ANISOU 2356  CB  HIS A 478     2351   4145   3555   -445    468    510       C  
ATOM   2357  CG  HIS A 478     -21.193   4.250 -36.175  1.00 31.11           C  
ANISOU 2357  CG  HIS A 478     2935   4801   4085   -452    569    504       C  
ATOM   2358  ND1 HIS A 478     -20.968   3.692 -34.937  1.00 34.08           N  
ANISOU 2358  ND1 HIS A 478     3345   5211   4394   -483    600    547       N  
ATOM   2359  CD2 HIS A 478     -21.484   5.561 -36.019  1.00 33.61           C  
ANISOU 2359  CD2 HIS A 478     3228   5150   4393   -431    643    458       C  
ATOM   2360  CE1 HIS A 478     -21.154   4.667 -34.065  1.00 34.33           C  
ANISOU 2360  CE1 HIS A 478     3379   5294   4370   -482    693    523       C  
ATOM   2361  NE2 HIS A 478     -21.475   5.809 -34.669  1.00 34.28           N  
ANISOU 2361  NE2 HIS A 478     3337   5286   4401   -449    725    467       N  
ATOM   2362  N   LYS A 479     -19.316   1.299 -39.149  1.00 23.89           N  
ANISOU 2362  N   LYS A 479     2143   3694   3243   -415    274    514       N  
ATOM   2363  CA  LYS A 479     -19.353   0.415 -40.312  1.00 23.16           C  
ANISOU 2363  CA  LYS A 479     2084   3519   3199   -412    194    515       C  
ATOM   2364  C   LYS A 479     -20.811   0.350 -40.751  1.00 24.27           C  
ANISOU 2364  C   LYS A 479     2172   3633   3418   -453    176    540       C  
ATOM   2365  O   LYS A 479     -21.705   0.373 -39.914  1.00 25.71           O  
ANISOU 2365  O   LYS A 479     2296   3847   3624   -492    222    586       O  
ATOM   2366  CB  LYS A 479     -18.835  -0.981 -39.962  1.00 26.29           C  
ANISOU 2366  CB  LYS A 479     2527   3875   3588   -424    152    563       C  
ATOM   2367  CG  LYS A 479     -18.711  -1.922 -41.161  1.00 26.83           C  
ANISOU 2367  CG  LYS A 479     2652   3848   3696   -414     73    554       C  
ATOM   2368  CD  LYS A 479     -18.192  -3.278 -40.745  1.00 20.84           C  
ANISOU 2368  CD  LYS A 479     1939   3043   2936   -422     39    602       C  
ATOM   2369  CE  LYS A 479     -18.002  -4.159 -41.942  1.00 24.68           C  
ANISOU 2369  CE  LYS A 479     2496   3426   3455   -407    -30    584       C  
ATOM   2370  NZ  LYS A 479     -17.225  -5.377 -41.610  1.00 44.19           N  
ANISOU 2370  NZ  LYS A 479     5020   5847   5925   -394    -54    622       N  
ATOM   2371  N   LEU A 480     -21.048   0.377 -42.040  1.00 19.97           N  
ANISOU 2371  N   LEU A 480     1645   3032   2909   -442    115    511       N  
ATOM   2372  CA  LEU A 480     -22.397   0.362 -42.590  1.00 20.80           C  
ANISOU 2372  CA  LEU A 480     1699   3107   3097   -483     78    537       C  
ATOM   2373  C   LEU A 480     -23.029  -1.021 -42.643  1.00 25.36           C  
ANISOU 2373  C   LEU A 480     2286   3620   3729   -540     11    596       C  
ATOM   2374  O   LEU A 480     -22.355  -2.009 -42.971  1.00 25.19           O  
ANISOU 2374  O   LEU A 480     2345   3541   3686   -535    -42    593       O  
ATOM   2375  CB  LEU A 480     -22.393   0.895 -44.039  1.00 20.77           C  
ANISOU 2375  CB  LEU A 480     1727   3061   3104   -455     20    485       C  
ATOM   2376  CG  LEU A 480     -21.856   2.265 -44.367  1.00 25.79           C  
ANISOU 2376  CG  LEU A 480     2359   3739   3700   -401     66    425       C  
ATOM   2377  CD1 LEU A 480     -21.959   2.492 -45.847  1.00 25.98           C  
ANISOU 2377  CD1 LEU A 480     2427   3708   3735   -386     -6    390       C  
ATOM   2378  CD2 LEU A 480     -22.615   3.369 -43.623  1.00 29.02           C  
ANISOU 2378  CD2 LEU A 480     2673   4214   4140   -407    144    436       C  
ATOM   2379  N   ASP A 481     -24.353  -1.056 -42.439  1.00 22.57           N  
ANISOU 2379  N   ASP A 481     1850   3269   3458   -593     10    650       N  
ATOM   2380  CA  ASP A 481     -25.222  -2.209 -42.629  1.00 23.22           C  
ANISOU 2380  CA  ASP A 481     1921   3285   3617   -660    -64    712       C  
ATOM   2381  C   ASP A 481     -26.414  -1.889 -43.543  1.00 24.73           C  
ANISOU 2381  C   ASP A 481     2052   3443   3901   -694   -130    726       C  
ATOM   2382  O   ASP A 481     -27.381  -2.627 -43.636  1.00 25.01           O  
ANISOU 2382  O   ASP A 481     2047   3434   4023   -760   -188    787       O  
ATOM   2383  CB  ASP A 481     -25.556  -2.960 -41.330  1.00 27.35           C  
ANISOU 2383  CB  ASP A 481     2405   3831   4154   -704    -12    788       C  
ATOM   2384  CG  ASP A 481     -24.722  -4.236 -41.216  1.00 53.01           C  
ANISOU 2384  CG  ASP A 481     5749   7027   7364   -708    -57    799       C  
ATOM   2385  OD1 ASP A 481     -25.311  -5.340 -41.270  1.00 56.57           O  
ANISOU 2385  OD1 ASP A 481     6206   7412   7875   -766   -119    854       O  
ATOM   2386  OD2 ASP A 481     -23.464  -4.129 -41.148  1.00 63.00           O  
ANISOU 2386  OD2 ASP A 481     7082   8309   8545   -651    -36    753       O  
ATOM   2387  N   GLN A 482     -26.283  -0.788 -44.254  1.00 21.57           N  
ANISOU 2387  N   GLN A 482     1650   3061   3485   -650   -128    671       N  
ATOM   2388  CA  GLN A 482     -27.140  -0.246 -45.308  1.00 21.56           C  
ANISOU 2388  CA  GLN A 482     1611   3031   3551   -664   -200    670       C  
ATOM   2389  C   GLN A 482     -26.198   0.628 -46.125  1.00 23.45           C  
ANISOU 2389  C   GLN A 482     1924   3277   3710   -596   -199    587       C  
ATOM   2390  O   GLN A 482     -25.226   1.134 -45.589  1.00 20.26           O  
ANISOU 2390  O   GLN A 482     1544   2924   3231   -544   -115    546       O  
ATOM   2391  CB  GLN A 482     -28.348   0.570 -44.762  1.00 23.19           C  
ANISOU 2391  CB  GLN A 482     1669   3289   3853   -682   -138    722       C  
ATOM   2392  CG  GLN A 482     -29.474  -0.344 -44.250  1.00 44.85           C  
ANISOU 2392  CG  GLN A 482     4329   6010   6701   -760   -158    816       C  
ATOM   2393  CD  GLN A 482     -30.862   0.240 -44.075  1.00 55.69           C  
ANISOU 2393  CD  GLN A 482     5550   7404   8205   -788   -134    881       C  
ATOM   2394  OE1 GLN A 482     -31.536   0.666 -45.026  1.00 42.94           O  
ANISOU 2394  OE1 GLN A 482     3895   5758   6663   -799   -217    889       O  
ATOM   2395  NE2 GLN A 482     -31.387   0.091 -42.871  1.00 53.43           N  
ANISOU 2395  NE2 GLN A 482     5177   7162   7961   -809    -28    943       N  
ATOM   2396  N   VAL A 483     -26.453   0.771 -47.415  1.00 22.88           N  
ANISOU 2396  N   VAL A 483     1893   3149   3650   -601   -297    565       N  
ATOM   2397  CA  VAL A 483     -25.663   1.641 -48.280  1.00 22.17           C  
ANISOU 2397  CA  VAL A 483     1873   3062   3490   -540   -297    494       C  
ATOM   2398  C   VAL A 483     -26.561   2.876 -48.551  1.00 25.91           C  
ANISOU 2398  C   VAL A 483     2249   3567   4030   -536   -292    509       C  
ATOM   2399  O   VAL A 483     -27.576   2.727 -49.224  1.00 24.22           O  
ANISOU 2399  O   VAL A 483     2002   3309   3891   -582   -388    548       O  
ATOM   2400  CB  VAL A 483     -25.221   0.910 -49.587  1.00 26.38           C  
ANISOU 2400  CB  VAL A 483     2545   3506   3973   -544   -405    457       C  
ATOM   2401  CG1 VAL A 483     -24.645   1.886 -50.613  1.00 26.17           C  
ANISOU 2401  CG1 VAL A 483     2581   3478   3883   -490   -410    396       C  
ATOM   2402  CG2 VAL A 483     -24.219  -0.203 -49.285  1.00 25.87           C  
ANISOU 2402  CG2 VAL A 483     2574   3408   3847   -531   -391    439       C  
ATOM   2403  N   PRO A 484     -26.227   4.089 -48.037  1.00 23.97           N  
ANISOU 2403  N   PRO A 484     1955   3389   3762   -484   -188    482       N  
ATOM   2404  CA  PRO A 484     -27.065   5.269 -48.327  1.00 24.26           C  
ANISOU 2404  CA  PRO A 484     1903   3446   3868   -472   -180    496       C  
ATOM   2405  C   PRO A 484     -27.109   5.642 -49.816  1.00 25.69           C  
ANISOU 2405  C   PRO A 484     2147   3576   4039   -464   -284    472       C  
ATOM   2406  O   PRO A 484     -26.183   5.312 -50.568  1.00 23.68           O  
ANISOU 2406  O   PRO A 484     2018   3287   3694   -445   -324    423       O  
ATOM   2407  CB  PRO A 484     -26.375   6.389 -47.526  1.00 25.38           C  
ANISOU 2407  CB  PRO A 484     2024   3659   3961   -412    -47    453       C  
ATOM   2408  CG  PRO A 484     -25.558   5.681 -46.511  1.00 29.20           C  
ANISOU 2408  CG  PRO A 484     2547   4170   4379   -412     14    444       C  
ATOM   2409  CD  PRO A 484     -25.071   4.466 -47.204  1.00 24.79           C  
ANISOU 2409  CD  PRO A 484     2089   3549   3783   -433    -80    438       C  
ATOM   2410  N   GLU A 485     -28.173   6.346 -50.237  1.00 20.12           N  
ANISOU 2410  N   GLU A 485     1354   2866   3425   -477   -325    512       N  
ATOM   2411  CA  GLU A 485     -28.253   6.819 -51.620  1.00 20.47           C  
ANISOU 2411  CA  GLU A 485     1458   2866   3455   -469   -426    496       C  
ATOM   2412  C   GLU A 485     -27.346   8.052 -51.870  1.00 24.29           C  
ANISOU 2412  C   GLU A 485     1983   3381   3866   -396   -353    435       C  
ATOM   2413  O   GLU A 485     -27.039   8.359 -53.019  1.00 24.95           O  
ANISOU 2413  O   GLU A 485     2153   3429   3899   -382   -420    409       O  
ATOM   2414  CB  GLU A 485     -29.710   7.099 -52.051  1.00 23.02           C  
ANISOU 2414  CB  GLU A 485     1671   3166   3911   -512   -516    570       C  
ATOM   2415  CG  GLU A 485     -30.339   8.337 -51.447  1.00 33.65           C  
ANISOU 2415  CG  GLU A 485     2873   4563   5349   -476   -422    599       C  
ATOM   2416  CD  GLU A 485     -31.023   8.085 -50.129  1.00 56.01           C  
ANISOU 2416  CD  GLU A 485     5576   7435   8269   -495   -328    650       C  
ATOM   2417  OE1 GLU A 485     -30.314   7.969 -49.107  1.00 33.60           O  
ANISOU 2417  OE1 GLU A 485     2758   4641   5366   -471   -210    616       O  
ATOM   2418  OE2 GLU A 485     -32.267   7.958 -50.126  1.00 70.01           O  
ANISOU 2418  OE2 GLU A 485     7230   9193  10178   -538   -375    730       O  
ATOM   2419  N   GLY A 486     -26.971   8.754 -50.802  1.00 20.76           N  
ANISOU 2419  N   GLY A 486     1477   2998   3414   -356   -218    416       N  
ATOM   2420  CA  GLY A 486     -26.151   9.958 -50.872  1.00 21.16           C  
ANISOU 2420  CA  GLY A 486     1553   3079   3408   -293   -142    363       C  
ATOM   2421  C   GLY A 486     -26.909  11.201 -51.303  1.00 28.19           C  
ANISOU 2421  C   GLY A 486     2369   3969   4373   -273   -148    384       C  
ATOM   2422  O   GLY A 486     -28.091  11.129 -51.675  1.00 28.70           O  
ANISOU 2422  O   GLY A 486     2361   4007   4537   -306   -225    445       O  
ATOM   2423  N   ARG A 487     -26.216  12.358 -51.259  1.00 25.75           N  
ANISOU 2423  N   ARG A 487     2075   3685   4023   -218    -70    339       N  
ATOM   2424  CA  ARG A 487     -26.762  13.661 -51.658  1.00 26.09           C  
ANISOU 2424  CA  ARG A 487     2059   3724   4129   -187    -62    352       C  
ATOM   2425  C   ARG A 487     -26.247  14.052 -53.045  1.00 27.31           C  
ANISOU 2425  C   ARG A 487     2315   3839   4221   -170   -140    330       C  
ATOM   2426  O   ARG A 487     -25.028  14.117 -53.240  1.00 24.44           O  
ANISOU 2426  O   ARG A 487     2049   3482   3755   -143   -104    275       O  
ATOM   2427  CB  ARG A 487     -26.343  14.734 -50.646  1.00 27.62           C  
ANISOU 2427  CB  ARG A 487     2210   3966   4319   -141     81    315       C  
ATOM   2428  CG  ARG A 487     -27.285  14.897 -49.484  1.00 37.32           C  
ANISOU 2428  CG  ARG A 487     3315   5223   5642   -145    163    351       C  
ATOM   2429  CD  ARG A 487     -26.798  16.011 -48.585  1.00 45.75           C  
ANISOU 2429  CD  ARG A 487     4369   6327   6687    -99    299    303       C  
ATOM   2430  NE  ARG A 487     -25.875  15.484 -47.586  1.00 56.08           N  
ANISOU 2430  NE  ARG A 487     5731   7676   7901   -108    367    261       N  
ATOM   2431  CZ  ARG A 487     -26.218  15.161 -46.344  1.00 60.13           C  
ANISOU 2431  CZ  ARG A 487     6197   8224   8427   -122    450    273       C  
ATOM   2432  NH1 ARG A 487     -27.458  15.363 -45.915  1.00 50.12           N  
ANISOU 2432  NH1 ARG A 487     4820   6956   7266   -124    493    323       N  
ATOM   2433  NH2 ARG A 487     -25.319  14.658 -45.513  1.00 34.87           N  
ANISOU 2433  NH2 ARG A 487     3056   5058   5133   -133    494    240       N  
ATOM   2434  N   GLN A 488     -27.160  14.315 -54.004  1.00 24.36           N  
ANISOU 2434  N   GLN A 488     1920   3426   3911   -186   -245    379       N  
ATOM   2435  CA  GLN A 488     -26.786  14.753 -55.357  1.00 23.56           C  
ANISOU 2435  CA  GLN A 488     1920   3285   3748   -172   -323    367       C  
ATOM   2436  C   GLN A 488     -26.613  16.277 -55.308  1.00 27.36           C  
ANISOU 2436  C   GLN A 488     2361   3783   4254   -117   -245    354       C  
ATOM   2437  O   GLN A 488     -27.580  17.036 -55.441  1.00 27.84           O  
ANISOU 2437  O   GLN A 488     2327   3832   4419   -109   -268    404       O  
ATOM   2438  CB  GLN A 488     -27.824  14.310 -56.415  1.00 25.66           C  
ANISOU 2438  CB  GLN A 488     2191   3497   4063   -221   -487    428       C  
ATOM   2439  CG  GLN A 488     -27.333  14.468 -57.877  1.00 37.66           C  
ANISOU 2439  CG  GLN A 488     3857   4969   5481   -218   -580    411       C  
ATOM   2440  CD  GLN A 488     -26.389  13.369 -58.361  1.00 51.95           C  
ANISOU 2440  CD  GLN A 488     5827   6754   7159   -234   -605    360       C  
ATOM   2441  OE1 GLN A 488     -26.748  12.176 -58.430  1.00 43.83           O  
ANISOU 2441  OE1 GLN A 488     4827   5696   6130   -286   -683    373       O  
ATOM   2442  NE2 GLN A 488     -25.176  13.763 -58.771  1.00 35.06           N  
ANISOU 2442  NE2 GLN A 488     3795   4618   4909   -189   -540    305       N  
ATOM   2443  N   VAL A 489     -25.387  16.714 -55.011  1.00 23.82           N  
ANISOU 2443  N   VAL A 489     1972   3359   3719    -79   -147    292       N  
ATOM   2444  CA  VAL A 489     -25.051  18.134 -54.873  1.00 22.83           C  
ANISOU 2444  CA  VAL A 489     1822   3247   3607    -30    -65    271       C  
ATOM   2445  C   VAL A 489     -24.724  18.794 -56.210  1.00 26.26           C  
ANISOU 2445  C   VAL A 489     2341   3642   3995    -12   -125    273       C  
ATOM   2446  O   VAL A 489     -25.140  19.917 -56.463  1.00 25.48           O  
ANISOU 2446  O   VAL A 489     2197   3529   3956     15   -119    296       O  
ATOM   2447  CB  VAL A 489     -24.078  18.447 -53.694  1.00 25.65           C  
ANISOU 2447  CB  VAL A 489     2173   3650   3921     -5     72    212       C  
ATOM   2448  CG1 VAL A 489     -23.492  17.183 -53.097  1.00 24.66           C  
ANISOU 2448  CG1 VAL A 489     2086   3549   3733    -31     85    189       C  
ATOM   2449  CG2 VAL A 489     -22.982  19.454 -54.057  1.00 25.08           C  
ANISOU 2449  CG2 VAL A 489     2166   3577   3786     33    125    168       C  
ATOM   2450  N   LEU A 490     -24.056  18.055 -57.086  1.00 24.54           N  
ANISOU 2450  N   LEU A 490     2250   3401   3674    -27   -184    255       N  
ATOM   2451  CA  LEU A 490     -23.653  18.532 -58.400  1.00 24.37           C  
ANISOU 2451  CA  LEU A 490     2334   3343   3584    -13   -236    256       C  
ATOM   2452  C   LEU A 490     -24.040  17.571 -59.484  1.00 28.68           C  
ANISOU 2452  C   LEU A 490     2975   3842   4081    -54   -372    281       C  
ATOM   2453  O   LEU A 490     -24.021  16.353 -59.265  1.00 29.83           O  
ANISOU 2453  O   LEU A 490     3149   3984   4200    -86   -400    270       O  
ATOM   2454  CB  LEU A 490     -22.122  18.653 -58.442  1.00 23.53           C  
ANISOU 2454  CB  LEU A 490     2319   3250   3371     18   -144    196       C  
ATOM   2455  CG  LEU A 490     -21.486  20.032 -58.414  1.00 27.81           C  
ANISOU 2455  CG  LEU A 490     2852   3802   3914     60    -60    179       C  
ATOM   2456  CD1 LEU A 490     -20.004  19.923 -58.755  1.00 26.99           C  
ANISOU 2456  CD1 LEU A 490     2849   3703   3703     80      5    133       C  
ATOM   2457  CD2 LEU A 490     -22.171  21.001 -59.367  1.00 29.57           C  
ANISOU 2457  CD2 LEU A 490     3078   3986   4170     69   -126    225       C  
ATOM   2458  N   ASP A 491     -24.275  18.108 -60.688  1.00 24.81           N  
ANISOU 2458  N   ASP A 491     2551   3311   3564    -53   -454    310       N  
ATOM   2459  CA  ASP A 491     -24.513  17.309 -61.882  1.00 25.83           C  
ANISOU 2459  CA  ASP A 491     2808   3389   3619    -93   -588    326       C  
ATOM   2460  C   ASP A 491     -23.248  16.397 -62.173  1.00 28.62           C  
ANISOU 2460  C   ASP A 491     3311   3733   3831    -85   -540    262       C  
ATOM   2461  O   ASP A 491     -22.117  16.883 -62.026  1.00 26.10           O  
ANISOU 2461  O   ASP A 491     3023   3436   3457    -40   -424    221       O  
ATOM   2462  CB  ASP A 491     -24.809  18.242 -63.066  1.00 28.66           C  
ANISOU 2462  CB  ASP A 491     3221   3710   3959    -86   -666    367       C  
ATOM   2463  CG  ASP A 491     -25.215  17.499 -64.312  1.00 48.12           C  
ANISOU 2463  CG  ASP A 491     5821   6117   6345   -134   -822    390       C  
ATOM   2464  OD1 ASP A 491     -24.312  17.076 -65.070  1.00 50.21           O  
ANISOU 2464  OD1 ASP A 491     6253   6358   6468   -128   -810    348       O  
ATOM   2465  OD2 ASP A 491     -26.427  17.249 -64.483  1.00 58.56           O  
ANISOU 2465  OD2 ASP A 491     7085   7416   7749   -182   -955    449       O  
ATOM   2466  N   PRO A 492     -23.428  15.098 -62.560  1.00 26.80           N  
ANISOU 2466  N   PRO A 492     3166   3467   3551   -128   -625    256       N  
ATOM   2467  CA  PRO A 492     -22.261  14.212 -62.816  1.00 26.85           C  
ANISOU 2467  CA  PRO A 492     3311   3455   3434   -113   -571    197       C  
ATOM   2468  C   PRO A 492     -21.216  14.692 -63.833  1.00 30.52           C  
ANISOU 2468  C   PRO A 492     3920   3899   3777    -73   -522    168       C  
ATOM   2469  O   PRO A 492     -20.040  14.398 -63.642  1.00 29.07           O  
ANISOU 2469  O   PRO A 492     3785   3727   3532    -36   -413    121       O  
ATOM   2470  CB  PRO A 492     -22.897  12.889 -63.264  1.00 29.52           C  
ANISOU 2470  CB  PRO A 492     3728   3741   3749   -172   -700    205       C  
ATOM   2471  CG  PRO A 492     -24.304  12.938 -62.746  1.00 34.66           C  
ANISOU 2471  CG  PRO A 492     4231   4402   4537   -219   -789    266       C  
ATOM   2472  CD  PRO A 492     -24.702  14.377 -62.777  1.00 30.06           C  
ANISOU 2472  CD  PRO A 492     3551   3846   4024   -192   -774    305       C  
ATOM   2473  N   LYS A 493     -21.642  15.424 -64.897  1.00 28.06           N  
ANISOU 2473  N   LYS A 493     3670   3556   3435    -80   -601    201       N  
ATOM   2474  CA  LYS A 493     -20.782  15.980 -65.953  1.00 28.17           C  
ANISOU 2474  CA  LYS A 493     3824   3547   3331    -45   -559    186       C  
ATOM   2475  C   LYS A 493     -19.865  17.090 -65.413  1.00 30.80           C  
ANISOU 2475  C   LYS A 493     4082   3928   3691     11   -409    171       C  
ATOM   2476  O   LYS A 493     -18.705  17.174 -65.812  1.00 31.15           O  
ANISOU 2476  O   LYS A 493     4218   3970   3649     48   -312    139       O  
ATOM   2477  CB  LYS A 493     -21.627  16.526 -67.123  1.00 31.36           C  
ANISOU 2477  CB  LYS A 493     4299   3907   3707    -74   -695    239       C  
ATOM   2478  CG  LYS A 493     -22.301  15.446 -67.975  1.00 52.29           C  
ANISOU 2478  CG  LYS A 493     7081   6497   6291   -134   -851    247       C  
ATOM   2479  CD  LYS A 493     -21.452  15.002 -69.183  1.00 61.67           C  
ANISOU 2479  CD  LYS A 493     8504   7631   7297   -123   -839    207       C  
ATOM   2480  CE  LYS A 493     -21.369  13.496 -69.338  1.00 65.67           C  
ANISOU 2480  CE  LYS A 493     9128   8091   7733   -154   -881    162       C  
ATOM   2481  NZ  LYS A 493     -22.594  12.902 -69.941  1.00 66.68           N  
ANISOU 2481  NZ  LYS A 493     9315   8164   7858   -233  -1085    198       N  
ATOM   2482  N   ILE A 494     -20.397  17.938 -64.514  1.00 25.94           N  
ANISOU 2482  N   ILE A 494     3302   3354   3200     16   -388    197       N  
ATOM   2483  CA  ILE A 494     -19.675  19.032 -63.871  1.00 24.13           C  
ANISOU 2483  CA  ILE A 494     2990   3166   3012     59   -261    184       C  
ATOM   2484  C   ILE A 494     -18.641  18.463 -62.919  1.00 27.10           C  
ANISOU 2484  C   ILE A 494     3338   3580   3380     79   -145    132       C  
ATOM   2485  O   ILE A 494     -17.483  18.866 -62.984  1.00 28.15           O  
ANISOU 2485  O   ILE A 494     3504   3725   3468    114    -44    107       O  
ATOM   2486  CB  ILE A 494     -20.618  20.088 -63.207  1.00 26.39           C  
ANISOU 2486  CB  ILE A 494     3121   3473   3432     60   -273    223       C  
ATOM   2487  CG1 ILE A 494     -21.605  20.663 -64.245  1.00 27.31           C  
ANISOU 2487  CG1 ILE A 494     3265   3547   3564     43   -397    285       C  
ATOM   2488  CG2 ILE A 494     -19.796  21.218 -62.534  1.00 25.64           C  
ANISOU 2488  CG2 ILE A 494     2960   3413   3371    101   -140    200       C  
ATOM   2489  CD1 ILE A 494     -22.827  21.401 -63.674  1.00 33.53           C  
ANISOU 2489  CD1 ILE A 494     3895   4343   4502     40   -437    335       C  
ATOM   2490  N   ALA A 495     -19.051  17.525 -62.048  1.00 22.78           N  
ANISOU 2490  N   ALA A 495     2727   3050   2878     55   -165    124       N  
ATOM   2491  CA  ALA A 495     -18.162  16.873 -61.082  1.00 21.61           C  
ANISOU 2491  CA  ALA A 495     2549   2936   2725     68    -73     83       C  
ATOM   2492  C   ALA A 495     -16.976  16.210 -61.794  1.00 27.41           C  
ANISOU 2492  C   ALA A 495     3419   3645   3350     93    -27     51       C  
ATOM   2493  O   ALA A 495     -15.829  16.442 -61.397  1.00 26.86           O  
ANISOU 2493  O   ALA A 495     3336   3602   3269    126     81     27       O  
ATOM   2494  CB  ALA A 495     -18.930  15.855 -60.271  1.00 21.75           C  
ANISOU 2494  CB  ALA A 495     2504   2963   2796     31   -124     90       C  
ATOM   2495  N   ASP A 496     -17.256  15.438 -62.883  1.00 25.34           N  
ANISOU 2495  N   ASP A 496     3293   3327   3010     76   -108     53       N  
ATOM   2496  CA  ASP A 496     -16.240  14.766 -63.698  1.00 25.32           C  
ANISOU 2496  CA  ASP A 496     3440   3286   2896    102    -63     21       C  
ATOM   2497  C   ASP A 496     -15.267  15.783 -64.318  1.00 27.85           C  
ANISOU 2497  C   ASP A 496     3806   3609   3167    146     32     20       C  
ATOM   2498  O   ASP A 496     -14.060  15.529 -64.324  1.00 27.77           O  
ANISOU 2498  O   ASP A 496     3833   3601   3117    185    138     -6       O  
ATOM   2499  CB  ASP A 496     -16.887  13.877 -64.782  1.00 27.67           C  
ANISOU 2499  CB  ASP A 496     3886   3514   3113     69   -180     23       C  
ATOM   2500  CG  ASP A 496     -17.677  12.685 -64.246  1.00 38.60           C  
ANISOU 2500  CG  ASP A 496     5244   4884   4539     23   -266     22       C  
ATOM   2501  OD1 ASP A 496     -17.605  12.418 -63.022  1.00 39.57           O  
ANISOU 2501  OD1 ASP A 496     5244   5051   4742     24   -221     19       O  
ATOM   2502  OD2 ASP A 496     -18.407  12.053 -65.036  1.00 43.26           O  
ANISOU 2502  OD2 ASP A 496     5937   5417   5083    -18   -385     30       O  
ATOM   2503  N   GLN A 497     -15.791  16.937 -64.801  1.00 22.46           N  
ANISOU 2503  N   GLN A 497     3110   2926   2499    140     -5     53       N  
ATOM   2504  CA  GLN A 497     -14.987  18.012 -65.394  1.00 22.23           C  
ANISOU 2504  CA  GLN A 497     3117   2897   2432    175     78     61       C  
ATOM   2505  C   GLN A 497     -14.001  18.561 -64.372  1.00 25.23           C  
ANISOU 2505  C   GLN A 497     3381   3328   2876    204    203     45       C  
ATOM   2506  O   GLN A 497     -12.809  18.634 -64.656  1.00 25.66           O  
ANISOU 2506  O   GLN A 497     3481   3382   2887    238    305     32       O  
ATOM   2507  CB  GLN A 497     -15.880  19.142 -65.921  1.00 24.05           C  
ANISOU 2507  CB  GLN A 497     3335   3115   2687    159      3    107       C  
ATOM   2508  CG  GLN A 497     -16.359  18.935 -67.353  1.00 25.74           C  
ANISOU 2508  CG  GLN A 497     3713   3271   2796    141    -97    129       C  
ATOM   2509  CD  GLN A 497     -17.335  19.991 -67.829  1.00 39.50           C  
ANISOU 2509  CD  GLN A 497     5431   5002   4577    122   -190    185       C  
ATOM   2510  OE1 GLN A 497     -17.855  20.815 -67.065  1.00 29.65           O  
ANISOU 2510  OE1 GLN A 497     4035   3783   3447    122   -192    208       O  
ATOM   2511  NE2 GLN A 497     -17.580  20.015 -69.134  1.00 37.41           N  
ANISOU 2511  NE2 GLN A 497     5318   4686   4208    108   -268    211       N  
ATOM   2512  N   VAL A 498     -14.492  18.867 -63.157  1.00 21.07           N  
ANISOU 2512  N   VAL A 498     2706   2844   2454    188    195     46       N  
ATOM   2513  CA  VAL A 498     -13.697  19.387 -62.045  1.00 19.16           C  
ANISOU 2513  CA  VAL A 498     2353   2652   2275    204    292     30       C  
ATOM   2514  C   VAL A 498     -12.648  18.346 -61.624  1.00 22.53           C  
ANISOU 2514  C   VAL A 498     2794   3091   2676    221    359      1       C  
ATOM   2515  O   VAL A 498     -11.482  18.699 -61.401  1.00 20.05           O  
ANISOU 2515  O   VAL A 498     2456   2795   2366    246    454     -7       O  
ATOM   2516  CB  VAL A 498     -14.594  19.881 -60.893  1.00 21.17           C  
ANISOU 2516  CB  VAL A 498     2471   2941   2632    181    264     35       C  
ATOM   2517  CG1 VAL A 498     -13.768  20.226 -59.656  1.00 20.61           C  
ANISOU 2517  CG1 VAL A 498     2303   2918   2609    189    354     11       C  
ATOM   2518  CG2 VAL A 498     -15.404  21.087 -61.336  1.00 20.74           C  
ANISOU 2518  CG2 VAL A 498     2394   2870   2616    177    223     68       C  
ATOM   2519  N   LEU A 499     -13.057  17.056 -61.626  1.00 20.20           N  
ANISOU 2519  N   LEU A 499     2542   2777   2355    207    303     -9       N  
ATOM   2520  CA  LEU A 499     -12.191  15.932 -61.319  1.00 20.50           C  
ANISOU 2520  CA  LEU A 499     2606   2815   2371    225    353    -32       C  
ATOM   2521  C   LEU A 499     -11.006  15.945 -62.293  1.00 23.41           C  
ANISOU 2521  C   LEU A 499     3076   3153   2667    270    439    -38       C  
ATOM   2522  O   LEU A 499      -9.852  15.835 -61.857  1.00 22.77           O  
ANISOU 2522  O   LEU A 499     2955   3092   2605    299    532    -44       O  
ATOM   2523  CB  LEU A 499     -12.962  14.615 -61.480  1.00 21.27           C  
ANISOU 2523  CB  LEU A 499     2766   2876   2441    200    265    -38       C  
ATOM   2524  CG  LEU A 499     -12.670  13.419 -60.548  1.00 25.37           C  
ANISOU 2524  CG  LEU A 499     3247   3406   2986    198    278    -52       C  
ATOM   2525  CD1 LEU A 499     -12.894  12.109 -61.270  1.00 25.98           C  
ANISOU 2525  CD1 LEU A 499     3452   3419   2999    193    225    -65       C  
ATOM   2526  CD2 LEU A 499     -11.297  13.476 -59.863  1.00 24.95           C  
ANISOU 2526  CD2 LEU A 499     3136   3388   2956    236    389    -60       C  
ATOM   2527  N   MET A 500     -11.295  16.117 -63.596  1.00 19.46           N  
ANISOU 2527  N   MET A 500     2702   2605   2087    273    410    -30       N  
ATOM   2528  CA  MET A 500     -10.264  16.141 -64.619  1.00 20.46           C  
ANISOU 2528  CA  MET A 500     2942   2698   2133    316    499    -33       C  
ATOM   2529  C   MET A 500      -9.257  17.268 -64.419  1.00 22.99           C  
ANISOU 2529  C   MET A 500     3187   3053   2496    341    606    -17       C  
ATOM   2530  O   MET A 500      -8.056  17.009 -64.546  1.00 21.66           O  
ANISOU 2530  O   MET A 500     3033   2880   2316    381    714    -21       O  
ATOM   2531  CB  MET A 500     -10.844  16.056 -66.050  1.00 24.30           C  
ANISOU 2531  CB  MET A 500     3599   3125   2511    308    438    -28       C  
ATOM   2532  CG  MET A 500     -11.530  14.704 -66.362  1.00 28.90           C  
ANISOU 2532  CG  MET A 500     4284   3658   3037    285    346    -51       C  
ATOM   2533  SD  MET A 500     -10.473  13.218 -66.241  1.00 34.13           S  
ANISOU 2533  SD  MET A 500     5012   4289   3667    329    435    -90       S  
ATOM   2534  CE  MET A 500     -11.095  12.490 -64.771  1.00 29.35           C  
ANISOU 2534  CE  MET A 500     4261   3721   3169    293    365    -94       C  
ATOM   2535  N   MET A 501      -9.743  18.479 -64.003  1.00 19.21           N  
ANISOU 2535  N   MET A 501     2615   2605   2079    317    578      2       N  
ATOM   2536  CA  MET A 501      -8.939  19.681 -63.696  1.00 18.75           C  
ANISOU 2536  CA  MET A 501     2475   2576   2073    328    661     18       C  
ATOM   2537  C   MET A 501      -8.026  19.432 -62.495  1.00 24.41           C  
ANISOU 2537  C   MET A 501     3076   3337   2863    335    725      5       C  
ATOM   2538  O   MET A 501      -6.944  19.987 -62.440  1.00 26.48           O  
ANISOU 2538  O   MET A 501     3300   3611   3151    353    814     17       O  
ATOM   2539  CB  MET A 501      -9.829  20.887 -63.350  1.00 20.45           C  
ANISOU 2539  CB  MET A 501     2615   2807   2348    298    604     34       C  
ATOM   2540  CG  MET A 501     -10.809  21.260 -64.404  1.00 24.30           C  
ANISOU 2540  CG  MET A 501     3192   3255   2785    287    524     58       C  
ATOM   2541  SD  MET A 501     -11.762  22.715 -63.894  1.00 28.53           S  
ANISOU 2541  SD  MET A 501     3621   3805   3416    264    473     81       S  
ATOM   2542  CE  MET A 501     -13.048  22.668 -65.123  1.00 25.58           C  
ANISOU 2542  CE  MET A 501     3356   3381   2981    247    347    116       C  
ATOM   2543  N   LEU A 502      -8.486  18.653 -61.515  1.00 20.72           N  
ANISOU 2543  N   LEU A 502     2549   2893   2431    316    674    -13       N  
ATOM   2544  CA  LEU A 502      -7.713  18.305 -60.324  1.00 20.03           C  
ANISOU 2544  CA  LEU A 502     2360   2846   2405    317    715    -21       C  
ATOM   2545  C   LEU A 502      -6.556  17.353 -60.667  1.00 24.49           C  
ANISOU 2545  C   LEU A 502     2968   3392   2943    359    791    -21       C  
ATOM   2546  O   LEU A 502      -5.451  17.542 -60.153  1.00 24.34           O  
ANISOU 2546  O   LEU A 502     2874   3398   2975    373    860     -9       O  
ATOM   2547  CB  LEU A 502      -8.613  17.743 -59.217  1.00 18.72           C  
ANISOU 2547  CB  LEU A 502     2129   2707   2275    283    640    -35       C  
ATOM   2548  CG  LEU A 502      -9.448  18.773 -58.456  1.00 20.02           C  
ANISOU 2548  CG  LEU A 502     2208   2902   2495    249    601    -36       C  
ATOM   2549  CD1 LEU A 502     -10.489  18.091 -57.649  1.00 19.42           C  
ANISOU 2549  CD1 LEU A 502     2095   2843   2442    220    531    -43       C  
ATOM   2550  CD2 LEU A 502      -8.583  19.588 -57.514  1.00 19.79           C  
ANISOU 2550  CD2 LEU A 502     2084   2913   2522    242    658    -39       C  
ATOM   2551  N   GLU A 503      -6.774  16.395 -61.586  1.00 20.51           N  
ANISOU 2551  N   GLU A 503     2589   2839   2365    380    780    -30       N  
ATOM   2552  CA  GLU A 503      -5.682  15.539 -62.037  1.00 21.02           C  
ANISOU 2552  CA  GLU A 503     2710   2874   2404    430    868    -30       C  
ATOM   2553  C   GLU A 503      -4.518  16.352 -62.649  1.00 25.72           C  
ANISOU 2553  C   GLU A 503     3305   3466   3002    466    984     -6       C  
ATOM   2554  O   GLU A 503      -3.362  16.103 -62.307  1.00 25.21           O  
ANISOU 2554  O   GLU A 503     3180   3412   2986    497   1068      9       O  
ATOM   2555  CB  GLU A 503      -6.153  14.465 -63.016  1.00 22.88           C  
ANISOU 2555  CB  GLU A 503     3102   3046   2546    446    839    -51       C  
ATOM   2556  CG  GLU A 503      -5.021  13.519 -63.417  1.00 27.33           C  
ANISOU 2556  CG  GLU A 503     3726   3571   3088    506    942    -55       C  
ATOM   2557  CD  GLU A 503      -5.337  12.577 -64.554  1.00 52.34           C  
ANISOU 2557  CD  GLU A 503     7078   6662   6147    527    935    -82       C  
ATOM   2558  OE1 GLU A 503      -4.592  11.583 -64.716  1.00 56.45           O  
ANISOU 2558  OE1 GLU A 503     7647   7144   6658    576   1007    -92       O  
ATOM   2559  OE2 GLU A 503      -6.318  12.835 -65.289  1.00 43.20           O  
ANISOU 2559  OE2 GLU A 503     6020   5480   4916    495    855    -90       O  
ATOM   2560  N   GLN A 504      -4.851  17.349 -63.494  1.00 23.79           N  
ANISOU 2560  N   GLN A 504     3116   3207   2714    457    984      5       N  
ATOM   2561  CA  GLN A 504      -3.911  18.244 -64.184  1.00 24.60           C  
ANISOU 2561  CA  GLN A 504     3229   3303   2814    482   1089     35       C  
ATOM   2562  C   GLN A 504      -3.034  19.085 -63.252  1.00 27.52           C  
ANISOU 2562  C   GLN A 504     3442   3720   3292    471   1138     58       C  
ATOM   2563  O   GLN A 504      -1.886  19.370 -63.610  1.00 28.47           O  
ANISOU 2563  O   GLN A 504     3546   3837   3437    501   1246     87       O  
ATOM   2564  CB  GLN A 504      -4.645  19.135 -65.203  1.00 25.92           C  
ANISOU 2564  CB  GLN A 504     3491   3445   2913    466   1054     46       C  
ATOM   2565  CG  GLN A 504      -5.256  18.383 -66.389  1.00 32.98           C  
ANISOU 2565  CG  GLN A 504     4567   4281   3682    478   1020     31       C  
ATOM   2566  CD  GLN A 504      -4.214  17.654 -67.214  1.00 46.79           C  
ANISOU 2566  CD  GLN A 504     6421   5989   5367    536   1143     29       C  
ATOM   2567  OE1 GLN A 504      -3.215  18.233 -67.687  1.00 41.45           O  
ANISOU 2567  OE1 GLN A 504     5746   5310   4695    567   1263     59       O  
ATOM   2568  NE2 GLN A 504      -4.426  16.360 -67.391  1.00 31.84           N  
ANISOU 2568  NE2 GLN A 504     4620   4059   3419    552   1120     -3       N  
ATOM   2569  N   VAL A 505      -3.553  19.452 -62.049  1.00 20.74           N  
ANISOU 2569  N   VAL A 505     2474   2907   2502    426   1060     47       N  
ATOM   2570  CA  VAL A 505      -2.802  20.194 -61.022  1.00 18.74           C  
ANISOU 2570  CA  VAL A 505     2080   2696   2345    404   1084     61       C  
ATOM   2571  C   VAL A 505      -1.475  19.421 -60.621  1.00 20.86           C  
ANISOU 2571  C   VAL A 505     2286   2976   2665    436   1158     80       C  
ATOM   2572  O   VAL A 505      -0.452  20.051 -60.299  1.00 19.92           O  
ANISOU 2572  O   VAL A 505     2076   2874   2617    432   1214    110       O  
ATOM   2573  CB  VAL A 505      -3.691  20.521 -59.784  1.00 21.02           C  
ANISOU 2573  CB  VAL A 505     2287   3023   2676    353    989     38       C  
ATOM   2574  CG1 VAL A 505      -2.933  21.360 -58.769  1.00 21.09           C  
ANISOU 2574  CG1 VAL A 505     2174   3069   2771    324   1008     48       C  
ATOM   2575  CG2 VAL A 505      -4.963  21.252 -60.182  1.00 20.41           C  
ANISOU 2575  CG2 VAL A 505     2257   2932   2568    331    924     28       C  
ATOM   2576  N   THR A 506      -1.520  18.071 -60.638  1.00 16.85           N  
ANISOU 2576  N   THR A 506     1823   2451   2127    465   1152     66       N  
ATOM   2577  CA  THR A 506      -0.386  17.192 -60.271  1.00 17.80           C  
ANISOU 2577  CA  THR A 506     1889   2574   2301    503   1215     87       C  
ATOM   2578  C   THR A 506       0.613  16.980 -61.413  1.00 23.73           C  
ANISOU 2578  C   THR A 506     2701   3281   3033    566   1344    113       C  
ATOM   2579  O   THR A 506       1.709  16.491 -61.163  1.00 25.12           O  
ANISOU 2579  O   THR A 506     2810   3458   3275    602   1415    142       O  
ATOM   2580  CB  THR A 506      -0.881  15.820 -59.718  1.00 25.50           C  
ANISOU 2580  CB  THR A 506     2883   3544   3261    508   1152     63       C  
ATOM   2581  OG1 THR A 506      -1.385  14.992 -60.774  1.00 24.97           O  
ANISOU 2581  OG1 THR A 506     2964   3420   3103    541   1161     40       O  
ATOM   2582  CG2 THR A 506      -1.927  15.960 -58.630  1.00 23.62           C  
ANISOU 2582  CG2 THR A 506     2594   3346   3034    448   1037     41       C  
ATOM   2583  N   LEU A 507       0.231  17.320 -62.661  1.00 20.94           N  
ANISOU 2583  N   LEU A 507     2476   2889   2591    581   1377    106       N  
ATOM   2584  CA  LEU A 507       1.048  17.098 -63.872  1.00 21.71           C  
ANISOU 2584  CA  LEU A 507     2664   2939   2646    643   1510    126       C  
ATOM   2585  C   LEU A 507       2.013  18.251 -64.238  1.00 27.17           C  
ANISOU 2585  C   LEU A 507     3295   3640   3389    648   1612    175       C  
ATOM   2586  O   LEU A 507       1.821  19.361 -63.726  1.00 27.34           O  
ANISOU 2586  O   LEU A 507     3233   3697   3459    595   1561    186       O  
ATOM   2587  CB  LEU A 507       0.130  16.700 -65.059  1.00 21.40           C  
ANISOU 2587  CB  LEU A 507     2821   2846   2466    656   1490     92       C  
ATOM   2588  CG  LEU A 507      -0.755  15.458 -64.826  1.00 25.64           C  
ANISOU 2588  CG  LEU A 507     3427   3360   2954    652   1397     47       C  
ATOM   2589  CD1 LEU A 507      -1.506  15.100 -66.075  1.00 26.90           C  
ANISOU 2589  CD1 LEU A 507     3786   3460   2976    661   1377     19       C  
ATOM   2590  CD2 LEU A 507       0.058  14.253 -64.339  1.00 26.81           C  
ANISOU 2590  CD2 LEU A 507     3535   3496   3157    700   1452     49       C  
ATOM   2591  N   PRO A 508       3.070  18.028 -65.074  1.00 24.85           N  
ANISOU 2591  N   PRO A 508     3036   3312   3094    709   1760    208       N  
ATOM   2592  CA  PRO A 508       3.981  19.148 -65.415  1.00 25.51           C  
ANISOU 2592  CA  PRO A 508     3053   3405   3236    707   1859    264       C  
ATOM   2593  C   PRO A 508       3.221  20.375 -65.911  1.00 30.73           C  
ANISOU 2593  C   PRO A 508     3772   4067   3839    660   1812    263       C  
ATOM   2594  O   PRO A 508       2.363  20.259 -66.787  1.00 31.47           O  
ANISOU 2594  O   PRO A 508     4022   4127   3809    665   1783    236       O  
ATOM   2595  CB  PRO A 508       4.910  18.552 -66.484  1.00 28.08           C  
ANISOU 2595  CB  PRO A 508     3458   3680   3530    788   2028    290       C  
ATOM   2596  CG  PRO A 508       4.881  17.085 -66.225  1.00 31.98           C  
ANISOU 2596  CG  PRO A 508     3987   4152   4012    833   2021    257       C  
ATOM   2597  CD  PRO A 508       3.490  16.777 -65.749  1.00 26.44           C  
ANISOU 2597  CD  PRO A 508     3340   3462   3245    783   1852    198       C  
ATOM   2598  N   GLY A 509       3.516  21.515 -65.289  1.00 27.55           N  
ANISOU 2598  N   GLY A 509     3241   3698   3530    612   1791    292       N  
ATOM   2599  CA  GLY A 509       2.864  22.802 -65.508  1.00 27.13           C  
ANISOU 2599  CA  GLY A 509     3207   3647   3455    562   1739    296       C  
ATOM   2600  C   GLY A 509       1.972  23.156 -64.332  1.00 31.83           C  
ANISOU 2600  C   GLY A 509     3727   4279   4089    502   1593    259       C  
ATOM   2601  O   GLY A 509       1.556  24.306 -64.187  1.00 34.29           O  
ANISOU 2601  O   GLY A 509     4013   4596   4421    457   1547    264       O  
ATOM   2602  N   GLY A 510       1.707  22.161 -63.487  1.00 26.36           N  
ANISOU 2602  N   GLY A 510     3000   3607   3409    503   1529    225       N  
ATOM   2603  CA  GLY A 510       0.864  22.251 -62.306  1.00 24.77           C  
ANISOU 2603  CA  GLY A 510     2734   3441   3237    453   1402    188       C  
ATOM   2604  C   GLY A 510       1.566  22.716 -61.049  1.00 28.75           C  
ANISOU 2604  C   GLY A 510     3081   3987   3855    414   1382    202       C  
ATOM   2605  O   GLY A 510       2.790  22.860 -61.028  1.00 29.19           O  
ANISOU 2605  O   GLY A 510     3059   4046   3984    424   1461    245       O  
ATOM   2606  N   THR A 511       0.766  22.961 -59.992  1.00 24.48           N  
ANISOU 2606  N   THR A 511     2496   3475   3330    365   1276    166       N  
ATOM   2607  CA  THR A 511       1.175  23.494 -58.686  1.00 24.53           C  
ANISOU 2607  CA  THR A 511     2377   3519   3423    314   1232    166       C  
ATOM   2608  C   THR A 511       1.126  22.452 -57.550  1.00 28.59           C  
ANISOU 2608  C   THR A 511     2840   4067   3954    307   1171    147       C  
ATOM   2609  O   THR A 511       1.419  22.789 -56.398  1.00 27.83           O  
ANISOU 2609  O   THR A 511     2654   4004   3916    261   1123    144       O  
ATOM   2610  CB  THR A 511       0.362  24.792 -58.335  1.00 29.80           C  
ANISOU 2610  CB  THR A 511     3041   4186   4095    263   1173    142       C  
ATOM   2611  OG1 THR A 511      -1.044  24.572 -58.504  1.00 26.65           O  
ANISOU 2611  OG1 THR A 511     2721   3778   3625    266   1110    104       O  
ATOM   2612  CG2 THR A 511       0.798  26.004 -59.131  1.00 25.87           C  
ANISOU 2612  CG2 THR A 511     2552   3658   3620    256   1233    176       C  
ATOM   2613  N   ALA A 512       0.743  21.203 -57.865  1.00 26.25           N  
ANISOU 2613  N   ALA A 512     2610   3761   3603    348   1168    134       N  
ATOM   2614  CA  ALA A 512       0.696  20.128 -56.872  1.00 26.26           C  
ANISOU 2614  CA  ALA A 512     2571   3788   3618    344   1115    123       C  
ATOM   2615  C   ALA A 512       1.493  18.884 -57.363  1.00 29.84           C  
ANISOU 2615  C   ALA A 512     3041   4219   4076    407   1181    149       C  
ATOM   2616  O   ALA A 512       1.111  17.754 -57.083  1.00 28.50           O  
ANISOU 2616  O   ALA A 512     2901   4047   3880    423   1146    133       O  
ATOM   2617  CB  ALA A 512      -0.754  19.773 -56.542  1.00 26.31           C  
ANISOU 2617  CB  ALA A 512     2633   3800   3562    324   1028     77       C  
ATOM   2618  N   LYS A 513       2.623  19.115 -58.068  1.00 27.70           N  
ANISOU 2618  N   LYS A 513     2748   3930   3848    442   1284    192       N  
ATOM   2619  CA  LYS A 513       3.486  18.062 -58.623  1.00 28.77           C  
ANISOU 2619  CA  LYS A 513     2896   4036   3999    511   1373    221       C  
ATOM   2620  C   LYS A 513       4.029  17.052 -57.595  1.00 32.25           C  
ANISOU 2620  C   LYS A 513     3248   4497   4507    519   1340    240       C  
ATOM   2621  O   LYS A 513       4.196  15.880 -57.934  1.00 33.03           O  
ANISOU 2621  O   LYS A 513     3394   4565   4592    576   1380    242       O  
ATOM   2622  CB  LYS A 513       4.634  18.656 -59.441  1.00 31.57           C  
ANISOU 2622  CB  LYS A 513     3220   4372   4405    542   1497    273       C  
ATOM   2623  CG  LYS A 513       4.371  18.711 -60.942  1.00 45.42           C  
ANISOU 2623  CG  LYS A 513     5117   6076   6065    588   1585    264       C  
ATOM   2624  CD  LYS A 513       4.455  20.130 -61.518  1.00 51.36           C  
ANISOU 2624  CD  LYS A 513     5871   6826   6816    558   1620    284       C  
ATOM   2625  CE  LYS A 513       5.779  20.853 -61.326  1.00 54.44           C  
ANISOU 2625  CE  LYS A 513     6128   7230   7327    549   1694    348       C  
ATOM   2626  NZ  LYS A 513       5.706  22.265 -61.802  1.00 63.95           N  
ANISOU 2626  NZ  LYS A 513     7342   8428   8528    512   1713    364       N  
ATOM   2627  N   GLN A 514       4.285  17.490 -56.352  1.00 26.53           N  
ANISOU 2627  N   GLN A 514     2408   3820   3850    462   1266    253       N  
ATOM   2628  CA  GLN A 514       4.780  16.594 -55.295  1.00 25.25           C  
ANISOU 2628  CA  GLN A 514     2163   3682   3750    462   1218    278       C  
ATOM   2629  C   GLN A 514       3.728  15.646 -54.687  1.00 24.07           C  
ANISOU 2629  C   GLN A 514     2070   3539   3536    451   1131    237       C  
ATOM   2630  O   GLN A 514       4.061  14.860 -53.803  1.00 23.90           O  
ANISOU 2630  O   GLN A 514     1990   3535   3557    449   1086    260       O  
ATOM   2631  CB  GLN A 514       5.640  17.312 -54.229  1.00 26.57           C  
ANISOU 2631  CB  GLN A 514     2188   3892   4014    405   1171    318       C  
ATOM   2632  CG  GLN A 514       5.352  18.782 -54.024  1.00 40.62           C  
ANISOU 2632  CG  GLN A 514     3954   5692   5788    337   1136    298       C  
ATOM   2633  CD  GLN A 514       6.158  19.662 -54.951  1.00 56.83           C  
ANISOU 2633  CD  GLN A 514     5980   7722   7892    352   1233    336       C  
ATOM   2634  OE1 GLN A 514       7.354  19.891 -54.748  1.00 53.50           O  
ANISOU 2634  OE1 GLN A 514     5445   7307   7574    347   1262    396       O  
ATOM   2635  NE2 GLN A 514       5.506  20.224 -55.961  1.00 42.41           N  
ANISOU 2635  NE2 GLN A 514     4251   5869   5996    365   1280    307       N  
ATOM   2636  N   ALA A 515       2.478  15.692 -55.179  1.00 17.24           N  
ANISOU 2636  N   ALA A 515     1316   2658   2576    444   1105    185       N  
ATOM   2637  CA  ALA A 515       1.398  14.811 -54.730  1.00 16.35           C  
ANISOU 2637  CA  ALA A 515     1260   2546   2406    431   1028    151       C  
ATOM   2638  C   ALA A 515       1.381  13.547 -55.583  1.00 21.55           C  
ANISOU 2638  C   ALA A 515     2011   3149   3029    497   1076    147       C  
ATOM   2639  O   ALA A 515       0.632  12.606 -55.289  1.00 21.80           O  
ANISOU 2639  O   ALA A 515     2090   3169   3024    494   1019    126       O  
ATOM   2640  CB  ALA A 515       0.062  15.516 -54.854  1.00 16.54           C  
ANISOU 2640  CB  ALA A 515     1346   2577   2361    389    975    104       C  
ATOM   2641  N   VAL A 516       2.194  13.540 -56.656  1.00 18.55           N  
ANISOU 2641  N   VAL A 516     1662   2729   2658    556   1184    166       N  
ATOM   2642  CA  VAL A 516       2.307  12.446 -57.612  1.00 19.59           C  
ANISOU 2642  CA  VAL A 516     1898   2796   2749    626   1252    159       C  
ATOM   2643  C   VAL A 516       2.718  11.116 -56.956  1.00 24.20           C  
ANISOU 2643  C   VAL A 516     2447   3365   3382    657   1239    179       C  
ATOM   2644  O   VAL A 516       3.535  11.101 -56.023  1.00 22.18           O  
ANISOU 2644  O   VAL A 516     2063   3144   3220    650   1227    224       O  
ATOM   2645  CB  VAL A 516       3.142  12.886 -58.855  1.00 24.71           C  
ANISOU 2645  CB  VAL A 516     2586   3408   3396    680   1386    178       C  
ATOM   2646  CG1 VAL A 516       3.817  11.720 -59.575  1.00 25.57           C  
ANISOU 2646  CG1 VAL A 516     2757   3452   3506    767   1489    189       C  
ATOM   2647  CG2 VAL A 516       2.274  13.684 -59.816  1.00 23.63           C  
ANISOU 2647  CG2 VAL A 516     2564   3255   3158    660   1383    142       C  
ATOM   2648  N   ILE A 517       2.014  10.030 -57.360  1.00 22.69           N  
ANISOU 2648  N   ILE A 517     2372   3123   3124    680   1221    145       N  
ATOM   2649  CA  ILE A 517       2.219   8.655 -56.889  1.00 22.86           C  
ANISOU 2649  CA  ILE A 517     2392   3115   3180    713   1207    158       C  
ATOM   2650  C   ILE A 517       2.426   7.752 -58.108  1.00 28.76           C  
ANISOU 2650  C   ILE A 517     3273   3773   3882    792   1302    139       C  
ATOM   2651  O   ILE A 517       1.583   7.775 -59.002  1.00 30.22           O  
ANISOU 2651  O   ILE A 517     3596   3921   3965    785   1295     91       O  
ATOM   2652  CB  ILE A 517       1.026   8.175 -56.024  1.00 24.79           C  
ANISOU 2652  CB  ILE A 517     2653   3379   3388    653   1078    133       C  
ATOM   2653  CG1 ILE A 517       0.941   8.938 -54.689  1.00 24.41           C  
ANISOU 2653  CG1 ILE A 517     2476   3414   3384    582    997    154       C  
ATOM   2654  CG2 ILE A 517       1.074   6.669 -55.776  1.00 25.29           C  
ANISOU 2654  CG2 ILE A 517     2750   3391   3467    688   1066    141       C  
ATOM   2655  CD1 ILE A 517      -0.490   9.059 -54.149  1.00 25.05           C  
ANISOU 2655  CD1 ILE A 517     2590   3523   3406    513    892    118       C  
ATOM   2656  N   PRO A 518       3.513   6.950 -58.181  1.00 25.20           N  
ANISOU 2656  N   PRO A 518     2790   3281   3503    867   1389    176       N  
ATOM   2657  CA  PRO A 518       3.669   6.041 -59.333  1.00 25.30           C  
ANISOU 2657  CA  PRO A 518     2950   3200   3465    945   1488    149       C  
ATOM   2658  C   PRO A 518       2.573   4.966 -59.323  1.00 29.08           C  
ANISOU 2658  C   PRO A 518     3553   3628   3869    926   1400    101       C  
ATOM   2659  O   PRO A 518       2.178   4.470 -58.256  1.00 26.92           O  
ANISOU 2659  O   PRO A 518     3216   3379   3632    887   1299    113       O  
ATOM   2660  CB  PRO A 518       5.068   5.438 -59.132  1.00 27.18           C  
ANISOU 2660  CB  PRO A 518     3091   3412   3825   1026   1591    209       C  
ATOM   2661  CG  PRO A 518       5.322   5.531 -57.674  1.00 31.29           C  
ANISOU 2661  CG  PRO A 518     3439   4003   4446    979   1493    260       C  
ATOM   2662  CD  PRO A 518       4.616   6.786 -57.211  1.00 26.42           C  
ANISOU 2662  CD  PRO A 518     2780   3468   3789    884   1398    244       C  
ATOM   2663  N   GLY A 519       2.059   4.661 -60.508  1.00 26.72           N  
ANISOU 2663  N   GLY A 519     3433   3258   3460    948   1435     48       N  
ATOM   2664  CA  GLY A 519       1.007   3.664 -60.687  1.00 26.31           C  
ANISOU 2664  CA  GLY A 519     3518   3146   3331    926   1352     -1       C  
ATOM   2665  C   GLY A 519      -0.414   4.131 -60.445  1.00 26.42           C  
ANISOU 2665  C   GLY A 519     3558   3201   3280    829   1208    -31       C  
ATOM   2666  O   GLY A 519      -1.353   3.447 -60.850  1.00 24.91           O  
ANISOU 2666  O   GLY A 519     3497   2954   3013    805   1141    -73       O  
ATOM   2667  N   TYR A 520      -0.591   5.308 -59.823  1.00 23.35           N  
ANISOU 2667  N   TYR A 520     3047   2903   2920    774   1162    -10       N  
ATOM   2668  CA  TYR A 520      -1.911   5.849 -59.500  1.00 21.34           C  
ANISOU 2668  CA  TYR A 520     2793   2692   2622    688   1037    -30       C  
ATOM   2669  C   TYR A 520      -2.084   7.257 -59.963  1.00 24.73           C  
ANISOU 2669  C   TYR A 520     3212   3166   3020    662   1048    -34       C  
ATOM   2670  O   TYR A 520      -1.308   8.127 -59.588  1.00 25.15           O  
ANISOU 2670  O   TYR A 520     3151   3272   3134    668   1097     -2       O  
ATOM   2671  CB  TYR A 520      -2.175   5.805 -57.989  1.00 21.73           C  
ANISOU 2671  CB  TYR A 520     2701   2809   2746    636    950     -2       C  
ATOM   2672  CG  TYR A 520      -2.352   4.429 -57.382  1.00 22.27           C  
ANISOU 2672  CG  TYR A 520     2781   2840   2839    639    903      5       C  
ATOM   2673  CD1 TYR A 520      -1.413   3.912 -56.491  1.00 23.98           C  
ANISOU 2673  CD1 TYR A 520     2894   3072   3146    669    929     51       C  
ATOM   2674  CD2 TYR A 520      -3.485   3.665 -57.654  1.00 22.12           C  
ANISOU 2674  CD2 TYR A 520     2871   2770   2762    606    824    -28       C  
ATOM   2675  CE1 TYR A 520      -1.576   2.655 -55.915  1.00 23.10           C  
ANISOU 2675  CE1 TYR A 520     2794   2923   3061    672    884     63       C  
ATOM   2676  CE2 TYR A 520      -3.660   2.405 -57.083  1.00 22.36           C  
ANISOU 2676  CE2 TYR A 520     2913   2762   2822    604    780    -18       C  
ATOM   2677  CZ  TYR A 520      -2.708   1.912 -56.205  1.00 27.33           C  
ANISOU 2677  CZ  TYR A 520     3443   3406   3537    639    813     28       C  
ATOM   2678  OH  TYR A 520      -2.888   0.687 -55.622  1.00 29.18           O  
ANISOU 2678  OH  TYR A 520     3687   3599   3800    637    767     44       O  
ATOM   2679  N   ARG A 521      -3.129   7.492 -60.754  1.00 21.13           N  
ANISOU 2679  N   ARG A 521     2872   2684   2473    629    992    -69       N  
ATOM   2680  CA  ARG A 521      -3.524   8.808 -61.239  1.00 20.20           C  
ANISOU 2680  CA  ARG A 521     2757   2600   2318    598    982    -71       C  
ATOM   2681  C   ARG A 521      -4.101   9.582 -60.054  1.00 21.67           C  
ANISOU 2681  C   ARG A 521     2801   2867   2565    534    898    -55       C  
ATOM   2682  O   ARG A 521      -5.024   9.092 -59.393  1.00 18.93           O  
ANISOU 2682  O   ARG A 521     2437   2530   2226    489    802    -63       O  
ATOM   2683  CB  ARG A 521      -4.555   8.665 -62.366  1.00 19.43           C  
ANISOU 2683  CB  ARG A 521     2828   2446   2110    578    924   -107       C  
ATOM   2684  CG  ARG A 521      -3.947   8.156 -63.677  1.00 17.13           C  
ANISOU 2684  CG  ARG A 521     2699   2073   1734    641   1022   -127       C  
ATOM   2685  CD  ARG A 521      -5.022   7.933 -64.716  1.00 15.21           C  
ANISOU 2685  CD  ARG A 521     2634   1772   1374    610    941   -163       C  
ATOM   2686  NE  ARG A 521      -5.672   9.194 -65.099  1.00 21.03           N  
ANISOU 2686  NE  ARG A 521     3367   2546   2078    565    890   -153       N  
ATOM   2687  CZ  ARG A 521      -6.839   9.274 -65.729  1.00 31.95           C  
ANISOU 2687  CZ  ARG A 521     4854   3902   3385    516    778   -168       C  
ATOM   2688  NH1 ARG A 521      -7.513   8.173 -66.033  1.00 18.96           N  
ANISOU 2688  NH1 ARG A 521     3325   2192   1686    496    699   -198       N  
ATOM   2689  NH2 ARG A 521      -7.360  10.454 -66.023  1.00 19.82           N  
ANISOU 2689  NH2 ARG A 521     3298   2399   1834    482    735   -150       N  
ATOM   2690  N   VAL A 522      -3.520  10.762 -59.747  1.00 18.43           N  
ANISOU 2690  N   VAL A 522     2290   2511   2202    529    942    -32       N  
ATOM   2691  CA  VAL A 522      -3.910  11.565 -58.576  1.00 17.36           C  
ANISOU 2691  CA  VAL A 522     2025   2449   2123    473    880    -21       C  
ATOM   2692  C   VAL A 522      -4.463  12.930 -58.985  1.00 19.38           C  
ANISOU 2692  C   VAL A 522     2283   2725   2356    443    863    -26       C  
ATOM   2693  O   VAL A 522      -4.006  13.539 -59.941  1.00 16.88           O  
ANISOU 2693  O   VAL A 522     2016   2388   2011    469    929    -21       O  
ATOM   2694  CB  VAL A 522      -2.747  11.651 -57.546  1.00 22.11           C  
ANISOU 2694  CB  VAL A 522     2492   3095   2814    484    922     12       C  
ATOM   2695  CG1 VAL A 522      -2.889  12.843 -56.605  1.00 21.98           C  
ANISOU 2695  CG1 VAL A 522     2363   3146   2841    431    885     20       C  
ATOM   2696  CG2 VAL A 522      -2.656  10.375 -56.748  1.00 22.64           C  
ANISOU 2696  CG2 VAL A 522     2536   3156   2912    491    891     21       C  
ATOM   2697  N   GLY A 523      -5.458  13.379 -58.245  1.00 16.10           N  
ANISOU 2697  N   GLY A 523     1814   2346   1956    389    780    -33       N  
ATOM   2698  CA  GLY A 523      -6.123  14.641 -58.488  1.00 15.10           C  
ANISOU 2698  CA  GLY A 523     1678   2236   1822    359    754    -37       C  
ATOM   2699  C   GLY A 523      -6.244  15.365 -57.186  1.00 19.27           C  
ANISOU 2699  C   GLY A 523     2083   2825   2415    319    729    -33       C  
ATOM   2700  O   GLY A 523      -6.794  14.807 -56.233  1.00 19.97           O  
ANISOU 2700  O   GLY A 523     2129   2937   2523    292    675    -38       O  
ATOM   2701  N   GLY A 524      -5.704  16.575 -57.120  1.00 14.90           N  
ANISOU 2701  N   GLY A 524     1476   2293   1891    315    771    -24       N  
ATOM   2702  CA  GLY A 524      -5.779  17.308 -55.869  1.00 14.58           C  
ANISOU 2702  CA  GLY A 524     1331   2303   1904    275    749    -27       C  
ATOM   2703  C   GLY A 524      -5.420  18.760 -55.916  1.00 19.68           C  
ANISOU 2703  C   GLY A 524     1937   2960   2580    263    782    -24       C  
ATOM   2704  O   GLY A 524      -5.043  19.281 -56.967  1.00 20.16           O  
ANISOU 2704  O   GLY A 524     2044   2992   2623    286    829    -12       O  
ATOM   2705  N   LYS A 525      -5.466  19.400 -54.745  1.00 17.17           N  
ANISOU 2705  N   LYS A 525     1539   2681   2304    225    763    -33       N  
ATOM   2706  CA  LYS A 525      -5.210  20.833 -54.640  1.00 17.34           C  
ANISOU 2706  CA  LYS A 525     1523   2708   2358    205    785    -35       C  
ATOM   2707  C   LYS A 525      -4.478  21.199 -53.355  1.00 20.84           C  
ANISOU 2707  C   LYS A 525     1881   3189   2847    170    784    -38       C  
ATOM   2708  O   LYS A 525      -4.830  20.705 -52.281  1.00 19.94           O  
ANISOU 2708  O   LYS A 525     1739   3106   2732    146    743    -51       O  
ATOM   2709  CB  LYS A 525      -6.595  21.532 -54.670  1.00 19.98           C  
ANISOU 2709  CB  LYS A 525     1876   3033   2684    187    744    -55       C  
ATOM   2710  CG  LYS A 525      -6.625  22.973 -55.080  1.00 17.52           C  
ANISOU 2710  CG  LYS A 525     1561   2701   2394    181    767    -54       C  
ATOM   2711  CD  LYS A 525      -6.421  23.172 -56.554  1.00 13.79           C  
ANISOU 2711  CD  LYS A 525     1160   2188   1891    213    798    -29       C  
ATOM   2712  CE  LYS A 525      -6.005  24.604 -56.829  1.00 20.54           C  
ANISOU 2712  CE  LYS A 525     1999   3025   2780    204    835    -18       C  
ATOM   2713  NZ  LYS A 525      -4.851  25.033 -55.983  1.00 31.95           N  
ANISOU 2713  NZ  LYS A 525     3369   4494   4277    180    870    -18       N  
ATOM   2714  N   THR A 526      -3.475  22.087 -53.461  1.00 18.71           N  
ANISOU 2714  N   THR A 526     1575   2916   2617    162    824    -23       N  
ATOM   2715  CA  THR A 526      -2.772  22.607 -52.288  1.00 18.92           C  
ANISOU 2715  CA  THR A 526     1527   2973   2687    118    809    -26       C  
ATOM   2716  C   THR A 526      -3.481  23.869 -51.811  1.00 22.82           C  
ANISOU 2716  C   THR A 526     2019   3463   3188     81    791    -60       C  
ATOM   2717  O   THR A 526      -4.246  24.474 -52.555  1.00 22.96           O  
ANISOU 2717  O   THR A 526     2078   3451   3195     95    803    -68       O  
ATOM   2718  CB  THR A 526      -1.250  22.826 -52.529  1.00 30.71           C  
ANISOU 2718  CB  THR A 526     2969   4464   4235    121    854     15       C  
ATOM   2719  OG1 THR A 526      -1.020  24.008 -53.291  1.00 29.34           O  
ANISOU 2719  OG1 THR A 526     2804   4261   4083    118    896     23       O  
ATOM   2720  CG2 THR A 526      -0.546  21.607 -53.154  1.00 31.01           C  
ANISOU 2720  CG2 THR A 526     3013   4495   4274    172    893     51       C  
ATOM   2721  N   GLY A 527      -3.247  24.232 -50.567  1.00 20.05           N  
ANISOU 2721  N   GLY A 527     1626   3138   2852     34    761    -79       N  
ATOM   2722  CA  GLY A 527      -3.810  25.429 -49.959  1.00 19.56           C  
ANISOU 2722  CA  GLY A 527     1567   3067   2797     -2    751   -117       C  
ATOM   2723  C   GLY A 527      -2.923  25.926 -48.845  1.00 23.18           C  
ANISOU 2723  C   GLY A 527     1984   3543   3279    -58    727   -126       C  
ATOM   2724  O   GLY A 527      -2.051  25.196 -48.364  1.00 22.48           O  
ANISOU 2724  O   GLY A 527     1858   3485   3200    -70    704   -101       O  
ATOM   2725  N   THR A 528      -3.101  27.177 -48.458  1.00 21.41           N  
ANISOU 2725  N   THR A 528     1768   3297   3070    -92    728   -158       N  
ATOM   2726  CA  THR A 528      -2.363  27.757 -47.325  1.00 22.52           C  
ANISOU 2726  CA  THR A 528     1886   3448   3224   -155    693   -176       C  
ATOM   2727  C   THR A 528      -3.377  28.565 -46.525  1.00 26.93           C  
ANISOU 2727  C   THR A 528     2489   3990   3753   -179    691   -238       C  
ATOM   2728  O   THR A 528      -4.160  29.300 -47.120  1.00 27.15           O  
ANISOU 2728  O   THR A 528     2543   3979   3792   -154    726   -255       O  
ATOM   2729  CB  THR A 528      -1.148  28.612 -47.748  1.00 29.43           C  
ANISOU 2729  CB  THR A 528     2722   4296   4163   -182    704   -147       C  
ATOM   2730  OG1 THR A 528      -0.512  28.092 -48.913  1.00 35.70           O  
ANISOU 2730  OG1 THR A 528     3489   5086   4989   -137    744    -91       O  
ATOM   2731  CG2 THR A 528      -0.139  28.722 -46.671  1.00 25.51           C  
ANISOU 2731  CG2 THR A 528     2187   3820   3686   -247    648   -143       C  
ATOM   2732  N   ALA A 529      -3.409  28.380 -45.198  1.00 23.30           N  
ANISOU 2732  N   ALA A 529     2042   3559   3253   -223    653   -268       N  
ATOM   2733  CA  ALA A 529      -4.315  29.110 -44.321  1.00 23.02           C  
ANISOU 2733  CA  ALA A 529     2057   3508   3183   -244    663   -331       C  
ATOM   2734  C   ALA A 529      -3.460  29.937 -43.381  1.00 27.54           C  
ANISOU 2734  C   ALA A 529     2642   4068   3753   -316    625   -359       C  
ATOM   2735  O   ALA A 529      -2.918  29.408 -42.408  1.00 25.58           O  
ANISOU 2735  O   ALA A 529     2395   3858   3467   -361    573   -357       O  
ATOM   2736  CB  ALA A 529      -5.206  28.149 -43.547  1.00 23.00           C  
ANISOU 2736  CB  ALA A 529     2075   3545   3119   -234    659   -345       C  
ATOM   2737  N   HIS A 530      -3.324  31.236 -43.693  1.00 27.36           N  
ANISOU 2737  N   HIS A 530     2635   3990   3772   -332    645   -381       N  
ATOM   2738  CA  HIS A 530      -2.507  32.203 -42.947  1.00 29.32           C  
ANISOU 2738  CA  HIS A 530     2902   4210   4028   -407    606   -410       C  
ATOM   2739  C   HIS A 530      -3.239  32.920 -41.801  1.00 37.22           C  
ANISOU 2739  C   HIS A 530     3986   5184   4971   -439    614   -490       C  
ATOM   2740  O   HIS A 530      -4.350  33.417 -41.997  1.00 37.05           O  
ANISOU 2740  O   HIS A 530     4001   5128   4949   -397    675   -526       O  
ATOM   2741  CB  HIS A 530      -1.937  33.252 -43.910  1.00 29.93           C  
ANISOU 2741  CB  HIS A 530     2955   4231   4185   -410    626   -389       C  
ATOM   2742  CG  HIS A 530      -0.704  32.798 -44.608  1.00 32.91           C  
ANISOU 2742  CG  HIS A 530     3255   4630   4621   -415    605   -315       C  
ATOM   2743  ND1 HIS A 530       0.542  32.897 -44.007  1.00 34.93           N  
ANISOU 2743  ND1 HIS A 530     3473   4895   4903   -486    540   -294       N  
ATOM   2744  CD2 HIS A 530      -0.559  32.256 -45.837  1.00 33.94           C  
ANISOU 2744  CD2 HIS A 530     3341   4769   4786   -357    645   -257       C  
ATOM   2745  CE1 HIS A 530       1.397  32.413 -44.886  1.00 34.34           C  
ANISOU 2745  CE1 HIS A 530     3323   4836   4890   -463    551   -220       C  
ATOM   2746  NE2 HIS A 530       0.782  32.014 -46.003  1.00 34.24           N  
ANISOU 2746  NE2 HIS A 530     3310   4822   4877   -385    619   -199       N  
ATOM   2747  N   LYS A 531      -2.588  33.011 -40.628  1.00 36.61           N  
ANISOU 2747  N   LYS A 531     3942   5119   4848   -513    551   -515       N  
ATOM   2748  CA  LYS A 531      -3.126  33.742 -39.476  1.00 38.63           C  
ANISOU 2748  CA  LYS A 531     4296   5344   5037   -553    558   -597       C  
ATOM   2749  C   LYS A 531      -3.002  35.262 -39.721  1.00 46.96           C  
ANISOU 2749  C   LYS A 531     5387   6313   6142   -576    578   -638       C  
ATOM   2750  O   LYS A 531      -1.956  35.745 -40.194  1.00 45.92           O  
ANISOU 2750  O   LYS A 531     5213   6158   6078   -615    536   -605       O  
ATOM   2751  CB  LYS A 531      -2.397  33.363 -38.181  1.00 41.37           C  
ANISOU 2751  CB  LYS A 531     4681   5728   5310   -633    472   -609       C  
ATOM   2752  CG  LYS A 531      -3.043  32.232 -37.398  1.00 54.51           C  
ANISOU 2752  CG  LYS A 531     6373   7453   6884   -617    476   -611       C  
ATOM   2753  CD  LYS A 531      -2.634  32.295 -35.932  1.00 63.78           C  
ANISOU 2753  CD  LYS A 531     7633   8640   7960   -702    406   -650       C  
ATOM   2754  CE  LYS A 531      -3.194  31.163 -35.111  1.00 77.18           C  
ANISOU 2754  CE  LYS A 531     9364  10399   9563   -692    410   -644       C  
ATOM   2755  NZ  LYS A 531      -2.715  31.218 -33.704  1.00 86.80           N  
ANISOU 2755  NZ  LYS A 531    10675  11630  10675   -780    333   -676       N  
ATOM   2756  N   LEU A 532      -4.076  35.999 -39.364  1.00 46.28           N  
ANISOU 2756  N   LEU A 532     5379   6178   6029   -553    645   -708       N  
ATOM   2757  CA  LEU A 532      -4.247  37.448 -39.512  1.00 47.57           C  
ANISOU 2757  CA  LEU A 532     5592   6248   6234   -562    681   -758       C  
ATOM   2758  C   LEU A 532      -3.114  38.350 -39.000  1.00 51.04           C  
ANISOU 2758  C   LEU A 532     6071   6639   6681   -659    609   -784       C  
ATOM   2759  O   LEU A 532      -2.983  39.464 -39.522  1.00 51.72           O  
ANISOU 2759  O   LEU A 532     6167   6648   6836   -665    628   -796       O  
ATOM   2760  CB  LEU A 532      -5.601  37.906 -38.925  1.00 48.80           C  
ANISOU 2760  CB  LEU A 532     5830   6364   6347   -519    769   -832       C  
ATOM   2761  CG  LEU A 532      -6.881  37.543 -39.710  1.00 53.99           C  
ANISOU 2761  CG  LEU A 532     6441   7029   7044   -418    852   -806       C  
ATOM   2762  CD1 LEU A 532      -8.119  37.750 -38.848  1.00 55.06           C  
ANISOU 2762  CD1 LEU A 532     6647   7144   7130   -385    935   -871       C  
ATOM   2763  CD2 LEU A 532      -7.017  38.377 -40.987  1.00 57.15           C  
ANISOU 2763  CD2 LEU A 532     6801   7365   7548   -376    883   -777       C  
ATOM   2764  N   ARG A 533      -2.328  37.894 -37.972  1.00 45.25           N  
ANISOU 2764  N   ARG A 533     5365   5948   5882   -738    520   -790       N  
ATOM   2765  CA  ARG A 533      -1.194  38.608 -37.343  1.00 44.86           C  
ANISOU 2765  CA  ARG A 533     5354   5860   5832   -846    425   -810       C  
ATOM   2766  C   ARG A 533      -1.639  39.634 -36.287  1.00 47.49           C  
ANISOU 2766  C   ARG A 533     5835   6119   6091   -891    440   -918       C  
ATOM   2767  O   ARG A 533      -2.561  40.423 -36.532  1.00 46.94           O  
ANISOU 2767  O   ARG A 533     5814   5981   6039   -839    534   -969       O  
ATOM   2768  CB  ARG A 533      -0.242  39.206 -38.396  1.00 44.12           C  
ANISOU 2768  CB  ARG A 533     5172   5729   5862   -866    399   -750       C  
ATOM   2769  CG  ARG A 533       1.075  39.767 -37.905  1.00 50.94           C  
ANISOU 2769  CG  ARG A 533     6039   6565   6752   -981    287   -744       C  
ATOM   2770  CD  ARG A 533       1.844  40.294 -39.102  1.00 56.40           C  
ANISOU 2770  CD  ARG A 533     6630   7223   7578   -983    290   -673       C  
ATOM   2771  NE  ARG A 533       3.095  40.941 -38.715  1.00 64.40           N  
ANISOU 2771  NE  ARG A 533     7633   8199   8639  -1097    184   -659       N  
ATOM   2772  CZ  ARG A 533       4.275  40.334 -38.700  1.00 85.32           C  
ANISOU 2772  CZ  ARG A 533    10182  10900  11335  -1148     95   -579       C  
ATOM   2773  NH1 ARG A 533       4.379  39.058 -39.059  1.00 76.02           N  
ANISOU 2773  NH1 ARG A 533     8913   9810  10160  -1090    107   -510       N  
ATOM   2774  NH2 ARG A 533       5.363  40.997 -38.333  1.00 76.23           N  
ANISOU 2774  NH2 ARG A 533     9018   9708  10237  -1258     -7   -565       N  
ATOM   2775  N   ALA A 534      -0.991  39.590 -35.103  1.00 43.05           N  
ANISOU 2775  N   ALA A 534     5348   5565   5443   -986    345   -950       N  
ATOM   2776  CA  ALA A 534      -1.311  40.423 -33.938  1.00 43.29           C  
ANISOU 2776  CA  ALA A 534     5543   5530   5375  -1042    346  -1058       C  
ATOM   2777  C   ALA A 534      -1.197  41.935 -34.147  1.00 45.08           C  
ANISOU 2777  C   ALA A 534     5832   5637   5660  -1074    362  -1115       C  
ATOM   2778  O   ALA A 534      -2.119  42.661 -33.766  1.00 45.66           O  
ANISOU 2778  O   ALA A 534     6017   5640   5691  -1042    452  -1202       O  
ATOM   2779  CB  ALA A 534      -0.507  39.979 -32.721  1.00 44.88           C  
ANISOU 2779  CB  ALA A 534     5809   5772   5472  -1147    219  -1066       C  
ATOM   2780  N   ASP A 535      -0.100  42.416 -34.763  1.00 39.46           N  
ANISOU 2780  N   ASP A 535     5045   4896   5052  -1132    283  -1063       N  
ATOM   2781  CA  ASP A 535       0.066  43.851 -35.004  1.00 39.02           C  
ANISOU 2781  CA  ASP A 535     5042   4721   5061  -1168    292  -1108       C  
ATOM   2782  C   ASP A 535      -0.704  44.363 -36.243  1.00 41.70           C  
ANISOU 2782  C   ASP A 535     5325   5014   5506  -1064    413  -1088       C  
ATOM   2783  O   ASP A 535      -0.517  45.504 -36.665  1.00 43.05           O  
ANISOU 2783  O   ASP A 535     5515   5088   5755  -1085    423  -1104       O  
ATOM   2784  CB  ASP A 535       1.557  44.249 -35.014  1.00 41.12           C  
ANISOU 2784  CB  ASP A 535     5263   4967   5396  -1288    152  -1062       C  
ATOM   2785  CG  ASP A 535       2.413  43.621 -36.101  1.00 44.89           C  
ANISOU 2785  CG  ASP A 535     5555   5509   5993  -1273    120   -935       C  
ATOM   2786  OD1 ASP A 535       1.857  42.883 -36.951  1.00 39.17           O  
ANISOU 2786  OD1 ASP A 535     4744   4842   5298  -1167    206   -883       O  
ATOM   2787  OD2 ASP A 535       3.643  43.885 -36.116  1.00 53.55           O  
ANISOU 2787  OD2 ASP A 535     6596   6594   7157  -1367     11   -886       O  
ATOM   2788  N   ARG A 536      -1.570  43.511 -36.811  1.00 37.06           N  
ANISOU 2788  N   ARG A 536     4670   4493   4918   -956    498  -1050       N  
ATOM   2789  CA  ARG A 536      -2.419  43.741 -37.991  1.00 36.41           C  
ANISOU 2789  CA  ARG A 536     4527   4386   4921   -849    604  -1019       C  
ATOM   2790  C   ARG A 536      -1.661  44.242 -39.247  1.00 39.14           C  
ANISOU 2790  C   ARG A 536     4775   4701   5397   -856    585   -941       C  
ATOM   2791  O   ARG A 536      -2.301  44.735 -40.174  1.00 37.89           O  
ANISOU 2791  O   ARG A 536     4593   4497   5308   -783    663   -923       O  
ATOM   2792  CB  ARG A 536      -3.661  44.617 -37.664  1.00 37.91           C  
ANISOU 2792  CB  ARG A 536     4825   4488   5092   -794    712  -1109       C  
ATOM   2793  CG  ARG A 536      -4.347  44.354 -36.309  1.00 55.30           C  
ANISOU 2793  CG  ARG A 536     7149   6701   7162   -798    744  -1198       C  
ATOM   2794  CD  ARG A 536      -5.041  43.005 -36.195  1.00 75.84           C  
ANISOU 2794  CD  ARG A 536     9701   9411   9705   -734    782  -1165       C  
ATOM   2795  NE  ARG A 536      -6.361  42.998 -36.829  1.00 94.25           N  
ANISOU 2795  NE  ARG A 536    11995  11729  12085   -617    903  -1157       N  
ATOM   2796  CZ  ARG A 536      -6.619  42.492 -38.032  1.00112.57           C  
ANISOU 2796  CZ  ARG A 536    14192  14090  14487   -548    921  -1073       C  
ATOM   2797  NH1 ARG A 536      -5.647  41.945 -38.754  1.00102.58           N  
ANISOU 2797  NH1 ARG A 536    12833  12880  13262   -576    841   -992       N  
ATOM   2798  NH2 ARG A 536      -7.851  42.530 -38.523  1.00 98.76           N  
ANISOU 2798  NH2 ARG A 536    12417  12325  12783   -450   1018  -1066       N  
ATOM   2799  N   LYS A 537      -0.305  44.102 -39.267  1.00 35.96           N  
ANISOU 2799  N   LYS A 537     4313   4322   5029   -943    482   -888       N  
ATOM   2800  CA  LYS A 537       0.607  44.524 -40.351  1.00 35.55           C  
ANISOU 2800  CA  LYS A 537     4164   4245   5098   -964    461   -806       C  
ATOM   2801  C   LYS A 537       0.718  43.417 -41.413  1.00 40.43           C  
ANISOU 2801  C   LYS A 537     4652   4954   5754   -893    489   -705       C  
ATOM   2802  O   LYS A 537       1.818  42.915 -41.702  1.00 39.95           O  
ANISOU 2802  O   LYS A 537     4497   4941   5740   -933    430   -629       O  
ATOM   2803  CB  LYS A 537       2.009  44.864 -39.802  1.00 37.17           C  
ANISOU 2803  CB  LYS A 537     4359   4433   5330  -1094    338   -792       C  
ATOM   2804  CG  LYS A 537       2.153  46.214 -39.135  1.00 33.25           C  
ANISOU 2804  CG  LYS A 537     3980   3820   4835  -1178    304   -873       C  
ATOM   2805  CD  LYS A 537       3.577  46.368 -38.605  1.00 30.62           C  
ANISOU 2805  CD  LYS A 537     3619   3482   4532  -1313    163   -844       C  
ATOM   2806  CE  LYS A 537       3.751  47.616 -37.783  1.00 39.80           C  
ANISOU 2806  CE  LYS A 537     4916   4527   5677  -1412    109   -934       C  
ATOM   2807  NZ  LYS A 537       5.028  47.614 -37.017  1.00 47.28           N  
ANISOU 2807  NZ  LYS A 537     5855   5480   6627  -1553    -50   -916       N  
ATOM   2808  N   GLY A 538      -0.429  43.061 -41.985  1.00 38.19           N  
ANISOU 2808  N   GLY A 538     4366   4688   5455   -787    579   -704       N  
ATOM   2809  CA  GLY A 538      -0.531  42.024 -43.001  1.00 37.99           C  
ANISOU 2809  CA  GLY A 538     4245   4739   5451   -712    612   -622       C  
ATOM   2810  C   GLY A 538      -0.625  40.637 -42.417  1.00 42.89           C  
ANISOU 2810  C   GLY A 538     4844   5460   5992   -699    584   -616       C  
ATOM   2811  O   GLY A 538      -0.840  40.481 -41.212  1.00 43.54           O  
ANISOU 2811  O   GLY A 538     4995   5555   5994   -736    552   -678       O  
ATOM   2812  N   TYR A 539      -0.464  39.626 -43.274  1.00 38.56           N  
ANISOU 2812  N   TYR A 539     4210   4979   5464   -645    600   -540       N  
ATOM   2813  CA  TYR A 539      -0.551  38.222 -42.881  1.00 37.25           C  
ANISOU 2813  CA  TYR A 539     4015   4904   5234   -624    578   -522       C  
ATOM   2814  C   TYR A 539       0.758  37.663 -42.345  1.00 40.05           C  
ANISOU 2814  C   TYR A 539     4317   5305   5595   -696    488   -481       C  
ATOM   2815  O   TYR A 539       1.841  38.057 -42.796  1.00 40.38           O  
ANISOU 2815  O   TYR A 539     4297   5327   5716   -739    458   -430       O  
ATOM   2816  CB  TYR A 539      -1.130  37.369 -44.022  1.00 37.08           C  
ANISOU 2816  CB  TYR A 539     3941   4922   5225   -529    637   -467       C  
ATOM   2817  CG  TYR A 539      -2.632  37.503 -44.133  1.00 38.60           C  
ANISOU 2817  CG  TYR A 539     4186   5095   5386   -460    704   -510       C  
ATOM   2818  CD1 TYR A 539      -3.211  38.546 -44.858  1.00 40.71           C  
ANISOU 2818  CD1 TYR A 539     4475   5289   5704   -426    757   -518       C  
ATOM   2819  CD2 TYR A 539      -3.481  36.618 -43.468  1.00 38.80           C  
ANISOU 2819  CD2 TYR A 539     4235   5170   5338   -431    712   -538       C  
ATOM   2820  CE1 TYR A 539      -4.599  38.679 -44.953  1.00 41.45           C  
ANISOU 2820  CE1 TYR A 539     4604   5361   5784   -360    814   -550       C  
ATOM   2821  CE2 TYR A 539      -4.870  36.746 -43.549  1.00 39.50           C  
ANISOU 2821  CE2 TYR A 539     4358   5239   5413   -369    775   -570       C  
ATOM   2822  CZ  TYR A 539      -5.424  37.778 -44.292  1.00 47.18           C  
ANISOU 2822  CZ  TYR A 539     5343   6139   6444   -332    824   -575       C  
ATOM   2823  OH  TYR A 539      -6.787  37.913 -44.366  1.00 47.24           O  
ANISOU 2823  OH  TYR A 539     5371   6125   6453   -269    882   -598       O  
ATOM   2824  N   SER A 540       0.654  36.768 -41.353  1.00 35.28           N  
ANISOU 2824  N   SER A 540     3734   4760   4910   -712    444   -500       N  
ATOM   2825  CA  SER A 540       1.805  36.142 -40.710  1.00 34.82           C  
ANISOU 2825  CA  SER A 540     3629   4750   4850   -779    347   -459       C  
ATOM   2826  C   SER A 540       2.502  35.171 -41.638  1.00 38.60           C  
ANISOU 2826  C   SER A 540     3990   5281   5396   -736    353   -362       C  
ATOM   2827  O   SER A 540       1.847  34.393 -42.336  1.00 37.39           O  
ANISOU 2827  O   SER A 540     3818   5158   5232   -652    418   -341       O  
ATOM   2828  CB  SER A 540       1.391  35.444 -39.424  1.00 37.86           C  
ANISOU 2828  CB  SER A 540     4080   5182   5122   -801    304   -503       C  
ATOM   2829  OG  SER A 540       2.479  34.727 -38.868  1.00 45.08           O  
ANISOU 2829  OG  SER A 540     4942   6147   6038   -859    203   -451       O  
ATOM   2830  N   ASN A 541       3.838  35.240 -41.661  1.00 36.63           N  
ANISOU 2830  N   ASN A 541     3662   5035   5220   -796    288   -302       N  
ATOM   2831  CA  ASN A 541       4.679  34.370 -42.484  1.00 35.83           C  
ANISOU 2831  CA  ASN A 541     3443   4976   5196   -760    298   -205       C  
ATOM   2832  C   ASN A 541       5.010  33.060 -41.767  1.00 39.46           C  
ANISOU 2832  C   ASN A 541     3868   5507   5617   -763    235   -173       C  
ATOM   2833  O   ASN A 541       5.279  32.056 -42.420  1.00 38.75           O  
ANISOU 2833  O   ASN A 541     3705   5457   5562   -702    267   -109       O  
ATOM   2834  CB  ASN A 541       5.951  35.099 -42.963  1.00 37.89           C  
ANISOU 2834  CB  ASN A 541     3619   5201   5577   -815    275   -143       C  
ATOM   2835  CG  ASN A 541       6.672  35.969 -41.946  1.00 68.85           C  
ANISOU 2835  CG  ASN A 541     7558   9088   9515   -934    165   -166       C  
ATOM   2836  OD1 ASN A 541       6.354  36.014 -40.744  1.00 69.96           O  
ANISOU 2836  OD1 ASN A 541     7783   9233   9566   -987     94   -230       O  
ATOM   2837  ND2 ASN A 541       7.656  36.714 -42.427  1.00 59.79           N  
ANISOU 2837  ND2 ASN A 541     6337   7900   8481   -984    151   -112       N  
ATOM   2838  N   SER A 542       4.948  33.062 -40.424  1.00 36.29           N  
ANISOU 2838  N   SER A 542     3530   5119   5138   -831    148   -219       N  
ATOM   2839  CA  SER A 542       5.248  31.901 -39.595  1.00 35.82           C  
ANISOU 2839  CA  SER A 542     3451   5123   5034   -845     74   -188       C  
ATOM   2840  C   SER A 542       4.002  31.085 -39.242  1.00 39.63           C  
ANISOU 2840  C   SER A 542     4010   5642   5405   -786    118   -233       C  
ATOM   2841  O   SER A 542       3.988  29.873 -39.459  1.00 39.32           O  
ANISOU 2841  O   SER A 542     3923   5651   5365   -732    129   -184       O  
ATOM   2842  CB  SER A 542       5.992  32.332 -38.338  1.00 39.69           C  
ANISOU 2842  CB  SER A 542     3969   5609   5501   -961    -58   -199       C  
ATOM   2843  OG  SER A 542       5.359  33.445 -37.730  1.00 47.53           O  
ANISOU 2843  OG  SER A 542     5085   6548   6424  -1011    -60   -295       O  
ATOM   2844  N   GLU A 543       2.960  31.744 -38.702  1.00 35.81           N  
ANISOU 2844  N   GLU A 543     3641   5129   4835   -795    148   -323       N  
ATOM   2845  CA  GLU A 543       1.717  31.087 -38.310  1.00 33.94           C  
ANISOU 2845  CA  GLU A 543     3474   4921   4499   -745    197   -366       C  
ATOM   2846  C   GLU A 543       0.817  30.815 -39.506  1.00 32.77           C  
ANISOU 2846  C   GLU A 543     3303   4768   4381   -644    306   -359       C  
ATOM   2847  O   GLU A 543       0.198  31.737 -40.038  1.00 34.88           O  
ANISOU 2847  O   GLU A 543     3603   4984   4665   -620    371   -400       O  
ATOM   2848  CB  GLU A 543       0.973  31.874 -37.208  1.00 36.07           C  
ANISOU 2848  CB  GLU A 543     3875   5162   4669   -792    196   -461       C  
ATOM   2849  CG  GLU A 543       1.555  31.679 -35.820  1.00 52.35           C  
ANISOU 2849  CG  GLU A 543     5991   7248   6651   -883     86   -471       C  
ATOM   2850  CD  GLU A 543       0.629  32.054 -34.678  1.00 81.71           C  
ANISOU 2850  CD  GLU A 543     9854  10952  10239   -910    106   -562       C  
ATOM   2851  OE1 GLU A 543       0.314  33.260 -34.536  1.00 83.51           O  
ANISOU 2851  OE1 GLU A 543    10160  11114  10455   -934    137   -635       O  
ATOM   2852  OE2 GLU A 543       0.208  31.140 -33.931  1.00 72.41           O  
ANISOU 2852  OE2 GLU A 543     8716   9826   8972   -904     97   -560       O  
ATOM   2853  N   TYR A 544       0.760  29.553 -39.937  1.00 23.23           N  
ANISOU 2853  N   TYR A 544     2041   3607   3179   -588    319   -304       N  
ATOM   2854  CA  TYR A 544      -0.079  29.086 -41.048  1.00 19.49           C  
ANISOU 2854  CA  TYR A 544     1551   3133   2722   -497    405   -292       C  
ATOM   2855  C   TYR A 544      -0.223  27.558 -41.094  1.00 19.40           C  
ANISOU 2855  C   TYR A 544     1508   3173   2688   -452    400   -247       C  
ATOM   2856  O   TYR A 544       0.662  26.831 -40.602  1.00 16.62           O  
ANISOU 2856  O   TYR A 544     1115   2857   2343   -480    335   -201       O  
ATOM   2857  CB  TYR A 544       0.410  29.618 -42.419  1.00 18.85           C  
ANISOU 2857  CB  TYR A 544     1413   3014   2734   -464    451   -255       C  
ATOM   2858  CG  TYR A 544       1.711  29.006 -42.899  1.00 20.87           C  
ANISOU 2858  CG  TYR A 544     1576   3292   3063   -464    424   -174       C  
ATOM   2859  CD1 TYR A 544       1.717  27.838 -43.662  1.00 22.09           C  
ANISOU 2859  CD1 TYR A 544     1689   3473   3232   -395    458   -124       C  
ATOM   2860  CD2 TYR A 544       2.931  29.618 -42.634  1.00 21.58           C  
ANISOU 2860  CD2 TYR A 544     1617   3369   3215   -530    368   -146       C  
ATOM   2861  CE1 TYR A 544       2.904  27.293 -44.139  1.00 22.38           C  
ANISOU 2861  CE1 TYR A 544     1639   3522   3343   -384    450    -49       C  
ATOM   2862  CE2 TYR A 544       4.126  29.079 -43.106  1.00 22.62           C  
ANISOU 2862  CE2 TYR A 544     1648   3517   3431   -524    354    -64       C  
ATOM   2863  CZ  TYR A 544       4.107  27.910 -43.848  1.00 27.75           C  
ANISOU 2863  CZ  TYR A 544     2259   4193   4093   -447    401    -16       C  
ATOM   2864  OH  TYR A 544       5.275  27.382 -44.327  1.00 26.11           O  
ANISOU 2864  OH  TYR A 544     1953   3996   3973   -431    402     65       O  
ATOM   2865  N   ARG A 545      -1.331  27.096 -41.732  1.00 14.25           N  
ANISOU 2865  N   ARG A 545      875   2522   2019   -384    465   -256       N  
ATOM   2866  CA  ARG A 545      -1.636  25.690 -41.999  1.00 13.57           C  
ANISOU 2866  CA  ARG A 545      768   2472   1918   -334    471   -218       C  
ATOM   2867  C   ARG A 545      -1.324  25.354 -43.465  1.00 19.90           C  
ANISOU 2867  C   ARG A 545     1521   3256   2784   -273    514   -171       C  
ATOM   2868  O   ARG A 545      -1.769  26.063 -44.371  1.00 20.02           O  
ANISOU 2868  O   ARG A 545     1550   3235   2823   -243    566   -186       O  
ATOM   2869  CB  ARG A 545      -3.104  25.345 -41.687  1.00 10.98           C  
ANISOU 2869  CB  ARG A 545      596   2090   1487   -289    444   -263       C  
ATOM   2870  CG  ARG A 545      -3.409  25.242 -40.199  1.00 12.93           C  
ANISOU 2870  CG  ARG A 545      793   2427   1694   -359    474   -288       C  
ATOM   2871  CD  ARG A 545      -4.851  24.857 -39.931  1.00 20.89           C  
ANISOU 2871  CD  ARG A 545     1843   3443   2652   -329    523   -316       C  
ATOM   2872  NE  ARG A 545      -5.408  25.565 -38.773  1.00 32.52           N  
ANISOU 2872  NE  ARG A 545     3387   4912   4059   -371    537   -376       N  
ATOM   2873  CZ  ARG A 545      -5.319  25.143 -37.520  1.00 50.84           C  
ANISOU 2873  CZ  ARG A 545     5750   7266   6301   -417    502   -383       C  
ATOM   2874  NH1 ARG A 545      -4.700  24.006 -37.237  1.00 59.90           N  
ANISOU 2874  NH1 ARG A 545     6870   8455   7434   -429    441   -328       N  
ATOM   2875  NH2 ARG A 545      -5.861  25.846 -36.540  1.00 28.77           N  
ANISOU 2875  NH2 ARG A 545     3033   4460   3438   -450    529   -443       N  
ATOM   2876  N   ALA A 546      -0.533  24.294 -43.694  1.00 16.15           N  
ANISOU 2876  N   ALA A 546      996   2804   2337   -252    495   -112       N  
ATOM   2877  CA  ALA A 546      -0.248  23.803 -45.038  1.00 14.83           C  
ANISOU 2877  CA  ALA A 546      798   2620   2217   -189    545    -70       C  
ATOM   2878  C   ALA A 546      -1.355  22.790 -45.290  1.00 17.81           C  
ANISOU 2878  C   ALA A 546     1217   3006   2546   -141    563    -79       C  
ATOM   2879  O   ALA A 546      -1.553  21.892 -44.488  1.00 17.58           O  
ANISOU 2879  O   ALA A 546     1192   3007   2480   -151    526    -73       O  
ATOM   2880  CB  ALA A 546       1.120  23.116 -45.095  1.00 15.69           C  
ANISOU 2880  CB  ALA A 546      833   2744   2385   -185    522     -4       C  
ATOM   2881  N   LEU A 547      -2.091  22.953 -46.370  1.00 13.91           N  
ANISOU 2881  N   LEU A 547      753   2481   2049    -96    613    -91       N  
ATOM   2882  CA  LEU A 547      -3.194  22.075 -46.679  1.00 13.10           C  
ANISOU 2882  CA  LEU A 547      690   2380   1909    -58    622    -98       C  
ATOM   2883  C   LEU A 547      -3.008  21.346 -47.993  1.00 15.80           C  
ANISOU 2883  C   LEU A 547     1040   2698   2265      1    656    -65       C  
ATOM   2884  O   LEU A 547      -2.489  21.893 -48.978  1.00 13.22           O  
ANISOU 2884  O   LEU A 547      710   2344   1970     22    696    -50       O  
ATOM   2885  CB  LEU A 547      -4.514  22.876 -46.745  1.00 13.35           C  
ANISOU 2885  CB  LEU A 547      762   2394   1918    -59    641   -143       C  
ATOM   2886  CG  LEU A 547      -4.742  24.019 -45.743  1.00 19.41           C  
ANISOU 2886  CG  LEU A 547     1538   3162   2675   -108    635   -188       C  
ATOM   2887  CD1 LEU A 547      -5.892  24.887 -46.183  1.00 18.89           C  
ANISOU 2887  CD1 LEU A 547     1503   3063   2613    -90    670   -220       C  
ATOM   2888  CD2 LEU A 547      -5.003  23.501 -44.360  1.00 22.77           C  
ANISOU 2888  CD2 LEU A 547     1973   3625   3052   -144    601   -203       C  
ATOM   2889  N   PHE A 548      -3.507  20.113 -48.015  1.00 13.07           N  
ANISOU 2889  N   PHE A 548      715   2360   1892     25    642    -55       N  
ATOM   2890  CA  PHE A 548      -3.568  19.302 -49.219  1.00 12.34           C  
ANISOU 2890  CA  PHE A 548      713   2198   1778     75    624    -32       C  
ATOM   2891  C   PHE A 548      -4.844  18.456 -49.242  1.00 20.00           C  
ANISOU 2891  C   PHE A 548     1670   3203   2725     89    644    -48       C  
ATOM   2892  O   PHE A 548      -5.080  17.631 -48.362  1.00 20.17           O  
ANISOU 2892  O   PHE A 548     1683   3249   2732     72    610    -42       O  
ATOM   2893  CB  PHE A 548      -2.304  18.474 -49.522  1.00 12.43           C  
ANISOU 2893  CB  PHE A 548      698   2204   1820    105    642     13       C  
ATOM   2894  CG  PHE A 548      -2.404  17.918 -50.932  1.00 12.29           C  
ANISOU 2894  CG  PHE A 548      743   2137   1789    159    679     24       C  
ATOM   2895  CD1 PHE A 548      -3.031  16.702 -51.176  1.00 13.04           C  
ANISOU 2895  CD1 PHE A 548      821   2262   1869    194    717     18       C  
ATOM   2896  CD2 PHE A 548      -1.996  18.675 -52.028  1.00 12.74           C  
ANISOU 2896  CD2 PHE A 548      800   2177   1865    184    747     30       C  
ATOM   2897  CE1 PHE A 548      -3.232  16.249 -52.486  1.00 14.26           C  
ANISOU 2897  CE1 PHE A 548     1051   2371   1997    241    752     18       C  
ATOM   2898  CE2 PHE A 548      -2.137  18.190 -53.333  1.00 13.95           C  
ANISOU 2898  CE2 PHE A 548      977   2322   2001    243    833     31       C  
ATOM   2899  CZ  PHE A 548      -2.777  16.995 -53.556  1.00 12.87           C  
ANISOU 2899  CZ  PHE A 548      897   2168   1823    266    810     23       C  
ATOM   2900  N   ALA A 549      -5.650  18.668 -50.276  1.00 17.38           N  
ANISOU 2900  N   ALA A 549     1387   2839   2378    112    657    -59       N  
ATOM   2901  CA  ALA A 549      -6.904  17.955 -50.497  1.00 16.18           C  
ANISOU 2901  CA  ALA A 549     1275   2675   2198    118    627    -66       C  
ATOM   2902  C   ALA A 549      -6.750  17.179 -51.785  1.00 20.20           C  
ANISOU 2902  C   ALA A 549     1845   3142   2689    161    639    -51       C  
ATOM   2903  O   ALA A 549      -6.470  17.778 -52.822  1.00 20.18           O  
ANISOU 2903  O   ALA A 549     1873   3111   2682    185    672    -49       O  
ATOM   2904  CB  ALA A 549      -8.026  18.958 -50.619  1.00 16.48           C  
ANISOU 2904  CB  ALA A 549     1319   2704   2237    105    622    -89       C  
ATOM   2905  N   GLY A 550      -6.896  15.859 -51.715  1.00 17.13           N  
ANISOU 2905  N   GLY A 550     1479   2744   2284    172    615    -40       N  
ATOM   2906  CA  GLY A 550      -6.703  15.023 -52.890  1.00 16.88           C  
ANISOU 2906  CA  GLY A 550     1520   2665   2228    213    628    -31       C  
ATOM   2907  C   GLY A 550      -7.572  13.798 -53.003  1.00 20.03           C  
ANISOU 2907  C   GLY A 550     1969   3039   2602    211    580    -32       C  
ATOM   2908  O   GLY A 550      -8.216  13.370 -52.046  1.00 19.98           O  
ANISOU 2908  O   GLY A 550     1929   3058   2605    179    538    -29       O  
ATOM   2909  N   VAL A 551      -7.563  13.225 -54.196  1.00 16.73           N  
ANISOU 2909  N   VAL A 551     1638   2568   2149    244    587    -34       N  
ATOM   2910  CA  VAL A 551      -8.366  12.084 -54.581  1.00 17.07           C  
ANISOU 2910  CA  VAL A 551     1750   2570   2163    240    536    -37       C  
ATOM   2911  C   VAL A 551      -7.571  11.072 -55.452  1.00 20.78           C  
ANISOU 2911  C   VAL A 551     2306   2985   2606    290    573    -36       C  
ATOM   2912  O   VAL A 551      -6.743  11.484 -56.268  1.00 19.07           O  
ANISOU 2912  O   VAL A 551     2122   2749   2373    329    639    -37       O  
ATOM   2913  CB  VAL A 551      -9.627  12.670 -55.274  1.00 21.24           C  
ANISOU 2913  CB  VAL A 551     2319   3082   2670    217    486    -47       C  
ATOM   2914  CG1 VAL A 551     -10.025  11.938 -56.544  1.00 21.05           C  
ANISOU 2914  CG1 VAL A 551     2415   2990   2591    231    454    -55       C  
ATOM   2915  CG2 VAL A 551     -10.782  12.799 -54.292  1.00 21.03           C  
ANISOU 2915  CG2 VAL A 551     2224   3091   2678    169    431    -43       C  
ATOM   2916  N   ALA A 552      -7.870   9.757 -55.307  1.00 17.54           N  
ANISOU 2916  N   ALA A 552     1935   2542   2187    288    536    -34       N  
ATOM   2917  CA  ALA A 552      -7.225   8.695 -56.091  1.00 18.30           C  
ANISOU 2917  CA  ALA A 552     2124   2572   2256    337    571    -39       C  
ATOM   2918  C   ALA A 552      -7.962   7.327 -56.061  1.00 22.72           C  
ANISOU 2918  C   ALA A 552     2747   3083   2802    320    505    -43       C  
ATOM   2919  O   ALA A 552      -8.613   7.008 -55.062  1.00 20.71           O  
ANISOU 2919  O   ALA A 552     2431   2858   2579    276    448    -28       O  
ATOM   2920  CB  ALA A 552      -5.769   8.503 -55.647  1.00 18.88           C  
ANISOU 2920  CB  ALA A 552     2138   2660   2375    382    649    -17       C  
ATOM   2921  N   PRO A 553      -7.800   6.466 -57.107  1.00 21.09           N  
ANISOU 2921  N   PRO A 553     2670   2797   2548    354    519    -62       N  
ATOM   2922  CA  PRO A 553      -7.153   6.742 -58.402  1.00 21.42           C  
ANISOU 2922  CA  PRO A 553     2812   2793   2535    406    591    -82       C  
ATOM   2923  C   PRO A 553      -8.131   7.564 -59.255  1.00 25.77           C  
ANISOU 2923  C   PRO A 553     3425   3338   3028    371    538    -98       C  
ATOM   2924  O   PRO A 553      -9.326   7.342 -59.162  1.00 24.78           O  
ANISOU 2924  O   PRO A 553     3314   3205   2895    318    439   -101       O  
ATOM   2925  CB  PRO A 553      -6.871   5.343 -58.951  1.00 23.61           C  
ANISOU 2925  CB  PRO A 553     3206   2982   2781    444    608    -98       C  
ATOM   2926  CG  PRO A 553      -7.937   4.459 -58.362  1.00 27.50           C  
ANISOU 2926  CG  PRO A 553     3702   3460   3287    389    501    -96       C  
ATOM   2927  CD  PRO A 553      -8.435   5.128 -57.097  1.00 22.77           C  
ANISOU 2927  CD  PRO A 553     2952   2951   2750    336    455    -67       C  
ATOM   2928  N   VAL A 554      -7.645   8.512 -60.049  1.00 23.46           N  
ANISOU 2928  N   VAL A 554     3162   3049   2703    398    600   -102       N  
ATOM   2929  CA  VAL A 554      -8.490   9.413 -60.846  1.00 24.14           C  
ANISOU 2929  CA  VAL A 554     3300   3133   2739    368    551   -108       C  
ATOM   2930  C   VAL A 554      -9.508   8.768 -61.829  1.00 30.27           C  
ANISOU 2930  C   VAL A 554     4226   3839   3438    341    460   -129       C  
ATOM   2931  O   VAL A 554     -10.585   9.334 -62.021  1.00 31.14           O  
ANISOU 2931  O   VAL A 554     4332   3959   3541    293    371   -121       O  
ATOM   2932  CB  VAL A 554      -7.674  10.618 -61.415  1.00 27.08           C  
ANISOU 2932  CB  VAL A 554     3666   3525   3099    402    642    -99       C  
ATOM   2933  CG1 VAL A 554      -8.298  11.210 -62.662  1.00 27.33           C  
ANISOU 2933  CG1 VAL A 554     3816   3521   3048    391    609   -107       C  
ATOM   2934  CG2 VAL A 554      -7.492  11.687 -60.354  1.00 25.57           C  
ANISOU 2934  CG2 VAL A 554     3315   3413   2989    381    654    -78       C  
ATOM   2935  N   SER A 555      -9.197   7.584 -62.389  1.00 27.22           N  
ANISOU 2935  N   SER A 555     3964   3379   3001    369    477   -152       N  
ATOM   2936  CA  SER A 555     -10.060   6.866 -63.342  1.00 27.24           C  
ANISOU 2936  CA  SER A 555     4127   3303   2920    340    388   -177       C  
ATOM   2937  C   SER A 555     -11.333   6.292 -62.721  1.00 34.22           C  
ANISOU 2937  C   SER A 555     4969   4186   3846    269    252   -167       C  
ATOM   2938  O   SER A 555     -12.350   6.161 -63.412  1.00 34.04           O  
ANISOU 2938  O   SER A 555     5037   4121   3776    221    144   -173       O  
ATOM   2939  CB  SER A 555      -9.283   5.757 -64.031  1.00 28.37           C  
ANISOU 2939  CB  SER A 555     4419   3361   3001    394    457   -209       C  
ATOM   2940  OG  SER A 555      -8.731   4.886 -63.061  1.00 33.60           O  
ANISOU 2940  OG  SER A 555     5004   4027   3737    418    494   -202       O  
ATOM   2941  N   ASP A 556     -11.254   5.912 -61.426  1.00 31.17           N  
ANISOU 2941  N   ASP A 556     4448   3844   3549    260    256   -148       N  
ATOM   2942  CA  ASP A 556     -12.348   5.358 -60.618  1.00 30.14           C  
ANISOU 2942  CA  ASP A 556     4252   3723   3475    195    150   -130       C  
ATOM   2943  C   ASP A 556     -11.966   5.602 -59.141  1.00 30.10           C  
ANISOU 2943  C   ASP A 556     4075   3800   3561    199    197   -102       C  
ATOM   2944  O   ASP A 556     -11.397   4.704 -58.495  1.00 27.75           O  
ANISOU 2944  O   ASP A 556     3759   3492   3293    218    229    -97       O  
ATOM   2945  CB  ASP A 556     -12.555   3.853 -60.926  1.00 32.54           C  
ANISOU 2945  CB  ASP A 556     4676   3938   3750    184    100   -149       C  
ATOM   2946  CG  ASP A 556     -13.562   3.177 -60.017  1.00 40.97           C  
ANISOU 2946  CG  ASP A 556     5668   5012   4886    118      3   -122       C  
ATOM   2947  OD1 ASP A 556     -14.708   3.654 -59.943  1.00 42.55           O  
ANISOU 2947  OD1 ASP A 556     5816   5238   5114     58    -87   -100       O  
ATOM   2948  OD2 ASP A 556     -13.188   2.198 -59.352  1.00 49.14           O  
ANISOU 2948  OD2 ASP A 556     6687   6028   5955    129     23   -117       O  
ATOM   2949  N   PRO A 557     -12.199   6.842 -58.621  1.00 24.81           N  
ANISOU 2949  N   PRO A 557     3289   3207   2932    183    206    -84       N  
ATOM   2950  CA  PRO A 557     -11.718   7.170 -57.267  1.00 23.74           C  
ANISOU 2950  CA  PRO A 557     3010   3146   2864    188    256    -64       C  
ATOM   2951  C   PRO A 557     -12.243   6.366 -56.089  1.00 29.12           C  
ANISOU 2951  C   PRO A 557     3620   3845   3599    149    212    -41       C  
ATOM   2952  O   PRO A 557     -13.432   6.097 -55.978  1.00 28.46           O  
ANISOU 2952  O   PRO A 557     3528   3752   3533     96    129    -29       O  
ATOM   2953  CB  PRO A 557     -11.930   8.669 -57.156  1.00 25.03           C  
ANISOU 2953  CB  PRO A 557     3096   3368   3046    178    272    -58       C  
ATOM   2954  CG  PRO A 557     -12.086   9.147 -58.586  1.00 29.82           C  
ANISOU 2954  CG  PRO A 557     3812   3930   3588    191    260    -73       C  
ATOM   2955  CD  PRO A 557     -12.796   8.028 -59.266  1.00 25.29           C  
ANISOU 2955  CD  PRO A 557     3352   3284   2973    167    177    -82       C  
ATOM   2956  N   ARG A 558     -11.308   5.928 -55.241  1.00 26.10           N  
ANISOU 2956  N   ARG A 558     3187   3485   3244    175    267    -30       N  
ATOM   2957  CA  ARG A 558     -11.603   5.131 -54.059  1.00 24.87           C  
ANISOU 2957  CA  ARG A 558     2968   3349   3133    143    237     -3       C  
ATOM   2958  C   ARG A 558     -11.459   5.908 -52.760  1.00 24.76           C  
ANISOU 2958  C   ARG A 558     2825   3423   3159    127    265     17       C  
ATOM   2959  O   ARG A 558     -12.194   5.639 -51.816  1.00 21.63           O  
ANISOU 2959  O   ARG A 558     2371   3055   2792     82    229     40       O  
ATOM   2960  CB  ARG A 558     -10.741   3.856 -54.038  1.00 24.13           C  
ANISOU 2960  CB  ARG A 558     2926   3202   3039    181    262      1       C  
ATOM   2961  CG  ARG A 558     -11.256   2.759 -54.988  1.00 36.16           C  
ANISOU 2961  CG  ARG A 558     4582   4629   4528    175    209    -17       C  
ATOM   2962  CD  ARG A 558     -12.488   2.017 -54.469  1.00 46.88           C  
ANISOU 2962  CD  ARG A 558     5926   5972   5914    107    116      5       C  
ATOM   2963  NE  ARG A 558     -12.379   1.648 -53.049  1.00 54.77           N  
ANISOU 2963  NE  ARG A 558     6823   7020   6966     88    122     45       N  
ATOM   2964  CZ  ARG A 558     -13.038   2.243 -52.052  1.00 64.55           C  
ANISOU 2964  CZ  ARG A 558     7954   8334   8239     43    108     72       C  
ATOM   2965  NH1 ARG A 558     -13.884   3.243 -52.301  1.00 35.20           N  
ANISOU 2965  NH1 ARG A 558     4203   4649   4522     14     85     64       N  
ATOM   2966  NH2 ARG A 558     -12.857   1.840 -50.800  1.00 53.16           N  
ANISOU 2966  NH2 ARG A 558     6439   6930   6829     28    118    108       N  
ATOM   2967  N   LEU A 559     -10.492   6.856 -52.695  1.00 22.30           N  
ANISOU 2967  N   LEU A 559     2474   3151   2848    160    331     10       N  
ATOM   2968  CA  LEU A 559     -10.230   7.609 -51.467  1.00 20.56           C  
ANISOU 2968  CA  LEU A 559     2147   3007   2656    142    356     24       C  
ATOM   2969  C   LEU A 559     -10.088   9.106 -51.644  1.00 21.49           C  
ANISOU 2969  C   LEU A 559     2228   3163   2773    146    391      6       C  
ATOM   2970  O   LEU A 559      -9.457   9.572 -52.584  1.00 19.49           O  
ANISOU 2970  O   LEU A 559     2014   2888   2503    182    429     -8       O  
ATOM   2971  CB  LEU A 559      -8.979   7.075 -50.736  1.00 20.36           C  
ANISOU 2971  CB  LEU A 559     2088   2997   2651    169    391     46       C  
ATOM   2972  CG  LEU A 559      -8.933   5.594 -50.325  1.00 25.38           C  
ANISOU 2972  CG  LEU A 559     2747   3598   3299    169    362     72       C  
ATOM   2973  CD1 LEU A 559      -7.543   5.221 -49.791  1.00 25.83           C  
ANISOU 2973  CD1 LEU A 559     2766   3664   3383    207    400     99       C  
ATOM   2974  CD2 LEU A 559     -10.022   5.256 -49.323  1.00 25.95           C  
ANISOU 2974  CD2 LEU A 559     2781   3698   3381    109    310     93       C  
ATOM   2975  N   ALA A 560     -10.691   9.847 -50.711  1.00 17.71           N  
ANISOU 2975  N   ALA A 560     1677   2738   2313    108    383      9       N  
ATOM   2976  CA  ALA A 560     -10.576  11.289 -50.576  1.00 17.06           C  
ANISOU 2976  CA  ALA A 560     1550   2694   2238    105    417     -7       C  
ATOM   2977  C   ALA A 560      -9.704  11.426 -49.331  1.00 22.11           C  
ANISOU 2977  C   ALA A 560     2128   3385   2889     96    442      3       C  
ATOM   2978  O   ALA A 560      -9.872  10.687 -48.353  1.00 20.74           O  
ANISOU 2978  O   ALA A 560     1932   3232   2718     72    421     22       O  
ATOM   2979  CB  ALA A 560     -11.944  11.941 -50.350  1.00 17.30           C  
ANISOU 2979  CB  ALA A 560     1551   2740   2284     70    391    -12       C  
ATOM   2980  N   MET A 561      -8.738  12.333 -49.392  1.00 20.15           N  
ANISOU 2980  N   MET A 561     1856   3153   2647    112    483     -6       N  
ATOM   2981  CA  MET A 561      -7.808  12.533 -48.301  1.00 20.53           C  
ANISOU 2981  CA  MET A 561     1848   3245   2706     98    494      6       C  
ATOM   2982  C   MET A 561      -7.424  13.995 -48.136  1.00 19.80           C  
ANISOU 2982  C   MET A 561     1721   3179   2623     86    523    -15       C  
ATOM   2983  O   MET A 561      -7.044  14.625 -49.111  1.00 18.75           O  
ANISOU 2983  O   MET A 561     1604   3022   2498    112    553    -24       O  
ATOM   2984  CB  MET A 561      -6.560  11.701 -48.573  1.00 24.14           C  
ANISOU 2984  CB  MET A 561     2310   3683   3180    136    508     32       C  
ATOM   2985  CG  MET A 561      -6.285  10.673 -47.538  1.00 29.24           C  
ANISOU 2985  CG  MET A 561     2933   4345   3832    122    477     64       C  
ATOM   2986  SD  MET A 561      -4.770   9.800 -47.926  1.00 34.25           S  
ANISOU 2986  SD  MET A 561     3561   4948   4505    177    502    101       S  
ATOM   2987  CE  MET A 561      -3.617  11.060 -47.562  1.00 30.31           C  
ANISOU 2987  CE  MET A 561     2989   4491   4037    168    526    107       C  
ATOM   2988  N   ILE A 562      -7.503  14.512 -46.895  1.00 14.59           N  
ANISOU 2988  N   ILE A 562     1022   2564   1958     46    515    -22       N  
ATOM   2989  CA  ILE A 562      -7.081  15.868 -46.533  1.00 14.51           C  
ANISOU 2989  CA  ILE A 562      984   2575   1955     26    536    -44       C  
ATOM   2990  C   ILE A 562      -5.941  15.772 -45.533  1.00 19.37           C  
ANISOU 2990  C   ILE A 562     1562   3223   2574      3    518    -25       C  
ATOM   2991  O   ILE A 562      -6.079  15.064 -44.551  1.00 20.43           O  
ANISOU 2991  O   ILE A 562     1693   3384   2687    -22    488     -9       O  
ATOM   2992  CB  ILE A 562      -8.207  16.822 -45.974  1.00 15.60           C  
ANISOU 2992  CB  ILE A 562     1121   2727   2081     -4    545    -78       C  
ATOM   2993  CG1 ILE A 562      -9.544  16.755 -46.721  1.00 14.65           C  
ANISOU 2993  CG1 ILE A 562     1022   2578   1966     11    545    -84       C  
ATOM   2994  CG2 ILE A 562      -7.697  18.250 -45.833  1.00 14.78           C  
ANISOU 2994  CG2 ILE A 562     1002   2627   1988    -18    569   -104       C  
ATOM   2995  CD1 ILE A 562      -9.559  16.992 -48.205  1.00 17.96           C  
ANISOU 2995  CD1 ILE A 562     1470   2954   2399     47    552    -83       C  
ATOM   2996  N   VAL A 563      -4.853  16.509 -45.770  1.00 15.79           N  
ANISOU 2996  N   VAL A 563     1082   2768   2150      6    533    -21       N  
ATOM   2997  CA  VAL A 563      -3.678  16.613 -44.904  1.00 15.55           C  
ANISOU 2997  CA  VAL A 563     1006   2765   2135    -23    507      2       C  
ATOM   2998  C   VAL A 563      -3.517  18.083 -44.502  1.00 22.16           C  
ANISOU 2998  C   VAL A 563     1834   3613   2974    -63    511    -32       C  
ATOM   2999  O   VAL A 563      -3.568  18.979 -45.357  1.00 21.82           O  
ANISOU 2999  O   VAL A 563     1796   3543   2952    -47    549    -51       O  
ATOM   3000  CB  VAL A 563      -2.382  16.052 -45.553  1.00 17.95           C  
ANISOU 3000  CB  VAL A 563     1274   3052   2493     16    518     48       C  
ATOM   3001  CG1 VAL A 563      -1.190  16.198 -44.613  1.00 18.25           C  
ANISOU 3001  CG1 VAL A 563     1252   3120   2561    -19    476     81       C  
ATOM   3002  CG2 VAL A 563      -2.551  14.600 -45.965  1.00 16.82           C  
ANISOU 3002  CG2 VAL A 563     1154   2887   2349     60    518     74       C  
ATOM   3003  N   VAL A 564      -3.372  18.329 -43.187  1.00 20.08           N  
ANISOU 3003  N   VAL A 564     1566   3384   2681   -117    471    -39       N  
ATOM   3004  CA  VAL A 564      -3.197  19.663 -42.615  1.00 19.40           C  
ANISOU 3004  CA  VAL A 564     1484   3302   2586   -165    466    -76       C  
ATOM   3005  C   VAL A 564      -1.972  19.654 -41.719  1.00 22.34           C  
ANISOU 3005  C   VAL A 564     1822   3700   2967   -211    406    -47       C  
ATOM   3006  O   VAL A 564      -1.906  18.854 -40.786  1.00 22.22           O  
ANISOU 3006  O   VAL A 564     1812   3715   2916   -234    359    -24       O  
ATOM   3007  CB  VAL A 564      -4.468  20.108 -41.854  1.00 24.39           C  
ANISOU 3007  CB  VAL A 564     2166   3943   3158   -190    481   -126       C  
ATOM   3008  CG1 VAL A 564      -4.243  21.433 -41.123  1.00 24.23           C  
ANISOU 3008  CG1 VAL A 564     2166   3921   3120   -241    476   -169       C  
ATOM   3009  CG2 VAL A 564      -5.652  20.218 -42.809  1.00 24.49           C  
ANISOU 3009  CG2 VAL A 564     2197   3927   3182   -145    533   -146       C  
ATOM   3010  N   VAL A 565      -0.982  20.504 -42.032  1.00 18.24           N  
ANISOU 3010  N   VAL A 565     1264   3167   2501   -226    401    -39       N  
ATOM   3011  CA  VAL A 565       0.233  20.642 -41.231  1.00 18.19           C  
ANISOU 3011  CA  VAL A 565     1215   3179   2516   -279    332     -6       C  
ATOM   3012  C   VAL A 565       0.217  22.042 -40.615  1.00 22.64           C  
ANISOU 3012  C   VAL A 565     1811   3735   3056   -343    314    -58       C  
ATOM   3013  O   VAL A 565       0.118  23.029 -41.350  1.00 23.31           O  
ANISOU 3013  O   VAL A 565     1897   3786   3173   -334    361    -85       O  
ATOM   3014  CB  VAL A 565       1.528  20.331 -42.015  1.00 21.82           C  
ANISOU 3014  CB  VAL A 565     1590   3628   3073   -249    335     59       C  
ATOM   3015  CG1 VAL A 565       2.764  20.655 -41.183  1.00 22.42           C  
ANISOU 3015  CG1 VAL A 565     1610   3720   3187   -312    253     97       C  
ATOM   3016  CG2 VAL A 565       1.561  18.869 -42.455  1.00 21.16           C  
ANISOU 3016  CG2 VAL A 565     1489   3546   3006   -186    350    106       C  
ATOM   3017  N   GLU A 566       0.268  22.121 -39.267  1.00 17.06           N  
ANISOU 3017  N   GLU A 566     1141   3055   2286   -409    248    -73       N  
ATOM   3018  CA  GLU A 566       0.223  23.381 -38.540  1.00 16.11           C  
ANISOU 3018  CA  GLU A 566     1073   2922   2127   -475    227   -130       C  
ATOM   3019  C   GLU A 566       1.606  23.972 -38.217  1.00 18.83           C  
ANISOU 3019  C   GLU A 566     1371   3262   2523   -539    148   -100       C  
ATOM   3020  O   GLU A 566       2.419  23.339 -37.546  1.00 15.99           O  
ANISOU 3020  O   GLU A 566      977   2931   2166   -573     64    -48       O  
ATOM   3021  CB  GLU A 566      -0.608  23.199 -37.272  1.00 17.53           C  
ANISOU 3021  CB  GLU A 566     1340   3126   2194   -512    210   -170       C  
ATOM   3022  CG  GLU A 566      -1.224  24.473 -36.728  1.00 20.61           C  
ANISOU 3022  CG  GLU A 566     1814   3490   2528   -552    236   -252       C  
ATOM   3023  CD  GLU A 566      -1.654  24.401 -35.274  1.00 35.60           C  
ANISOU 3023  CD  GLU A 566     3805   5412   4308   -607    205   -288       C  
ATOM   3024  OE1 GLU A 566      -1.548  23.314 -34.659  1.00 35.68           O  
ANISOU 3024  OE1 GLU A 566     3816   5464   4276   -616    160   -244       O  
ATOM   3025  OE2 GLU A 566      -2.066  25.452 -34.735  1.00 28.52           O  
ANISOU 3025  OE2 GLU A 566     2988   4488   3360   -642    229   -359       O  
ATOM   3026  N   ASN A 567       1.830  25.230 -38.637  1.00 18.86           N  
ANISOU 3026  N   ASN A 567     1375   3225   2567   -560    169   -132       N  
ATOM   3027  CA  ASN A 567       3.077  25.992 -38.406  1.00 20.06           C  
ANISOU 3027  CA  ASN A 567     1482   3362   2779   -629     96   -109       C  
ATOM   3028  C   ASN A 567       4.335  25.208 -38.843  1.00 24.13           C  
ANISOU 3028  C   ASN A 567     1877   3895   3395   -614     58    -11       C  
ATOM   3029  O   ASN A 567       5.218  24.980 -38.017  1.00 22.87           O  
ANISOU 3029  O   ASN A 567     1686   3758   3247   -673    -45     32       O  
ATOM   3030  CB  ASN A 567       3.182  26.479 -36.932  1.00 22.17           C  
ANISOU 3030  CB  ASN A 567     1827   3635   2960   -726      4   -150       C  
ATOM   3031  CG  ASN A 567       2.052  27.363 -36.482  1.00 32.40           C  
ANISOU 3031  CG  ASN A 567     3242   4903   4165   -741     53   -248       C  
ATOM   3032  OD1 ASN A 567       1.332  27.957 -37.279  1.00 30.20           O  
ANISOU 3032  OD1 ASN A 567     2977   4589   3908   -692    145   -286       O  
ATOM   3033  ND2 ASN A 567       1.883  27.490 -35.196  1.00 21.41           N  
ANISOU 3033  ND2 ASN A 567     1941   3522   2669   -806     -4   -288       N  
ATOM   3034  N   PRO A 568       4.425  24.763 -40.120  1.00 22.76           N  
ANISOU 3034  N   PRO A 568     1641   3712   3295   -533    138     29       N  
ATOM   3035  CA  PRO A 568       5.619  24.006 -40.533  1.00 23.50           C  
ANISOU 3035  CA  PRO A 568     1622   3818   3491   -509    119    122       C  
ATOM   3036  C   PRO A 568       6.832  24.898 -40.728  1.00 27.61           C  
ANISOU 3036  C   PRO A 568     2060   4315   4115   -559     86    162       C  
ATOM   3037  O   PRO A 568       6.683  26.076 -41.035  1.00 27.19           O  
ANISOU 3037  O   PRO A 568     2034   4227   4070   -586    115    120       O  
ATOM   3038  CB  PRO A 568       5.201  23.368 -41.867  1.00 24.37           C  
ANISOU 3038  CB  PRO A 568     1718   3914   3627   -406    230    136       C  
ATOM   3039  CG  PRO A 568       4.167  24.294 -42.428  1.00 27.86           C  
ANISOU 3039  CG  PRO A 568     2235   4325   4026   -393    302     63       C  
ATOM   3040  CD  PRO A 568       3.481  24.951 -41.252  1.00 23.34           C  
ANISOU 3040  CD  PRO A 568     1747   3758   3364   -460    250     -7       C  
ATOM   3041  N   GLN A 569       8.023  24.317 -40.568  1.00 25.71           N  
ANISOU 3041  N   GLN A 569     1714   4092   3964   -570     28    250       N  
ATOM   3042  CA  GLN A 569       9.320  24.964 -40.779  1.00 27.39           C  
ANISOU 3042  CA  GLN A 569     1818   4287   4303   -615     -6    313       C  
ATOM   3043  C   GLN A 569      10.168  23.995 -41.606  1.00 32.88           C  
ANISOU 3043  C   GLN A 569     2392   4987   5114   -537     47    409       C  
ATOM   3044  O   GLN A 569      11.216  23.534 -41.158  1.00 33.48           O  
ANISOU 3044  O   GLN A 569     2367   5080   5275   -562    -30    491       O  
ATOM   3045  CB  GLN A 569       9.996  25.290 -39.427  1.00 30.16           C  
ANISOU 3045  CB  GLN A 569     2159   4653   4648   -728   -163    329       C  
ATOM   3046  CG  GLN A 569       9.310  26.413 -38.657  1.00 42.73           C  
ANISOU 3046  CG  GLN A 569     3876   6227   6134   -809   -207    231       C  
ATOM   3047  CD  GLN A 569       9.872  26.585 -37.278  1.00 56.82           C  
ANISOU 3047  CD  GLN A 569     5677   8026   7884   -920   -367    241       C  
ATOM   3048  OE1 GLN A 569       9.748  25.716 -36.413  1.00 51.17           O  
ANISOU 3048  OE1 GLN A 569     4992   7351   7101   -930   -437    256       O  
ATOM   3049  NE2 GLN A 569      10.452  27.741 -37.028  1.00 52.41           N  
ANISOU 3049  NE2 GLN A 569     5114   7434   7367  -1010   -432    230       N  
ATOM   3050  N   GLY A 570       9.681  23.661 -42.795  1.00 30.81           N  
ANISOU 3050  N   GLY A 570     2147   4708   4853   -443    178    399       N  
ATOM   3051  CA  GLY A 570      10.353  22.699 -43.663  1.00 30.80           C  
ANISOU 3051  CA  GLY A 570     2055   4702   4944   -356    253    477       C  
ATOM   3052  C   GLY A 570      10.871  23.217 -44.983  1.00 33.76           C  
ANISOU 3052  C   GLY A 570     2375   5041   5410   -311    370    509       C  
ATOM   3053  O   GLY A 570      11.154  24.408 -45.128  1.00 34.17           O  
ANISOU 3053  O   GLY A 570     2412   5072   5500   -365    369    502       O  
ATOM   3054  N   ARG A 571      11.000  22.292 -45.950  1.00 29.00           N  
ANISOU 3054  N   ARG A 571     1751   4428   4841   -210    475    546       N  
ATOM   3055  CA  ARG A 571      11.566  22.473 -47.297  1.00 28.08           C  
ANISOU 3055  CA  ARG A 571     1585   4277   4807   -146    608    589       C  
ATOM   3056  C   ARG A 571      10.853  23.492 -48.163  1.00 31.01           C  
ANISOU 3056  C   ARG A 571     2042   4619   5121   -144    687    530       C  
ATOM   3057  O   ARG A 571      11.501  24.214 -48.912  1.00 28.30           O  
ANISOU 3057  O   ARG A 571     1646   4250   4857   -144    755    569       O  
ATOM   3058  CB  ARG A 571      11.674  21.124 -48.039  1.00 23.19           C  
ANISOU 3058  CB  ARG A 571      959   3649   4203    -35    702    625       C  
ATOM   3059  CG  ARG A 571      12.450  20.049 -47.300  1.00 20.50           C  
ANISOU 3059  CG  ARG A 571      522   3328   3938    -23    638    698       C  
ATOM   3060  CD  ARG A 571      13.934  20.247 -47.443  1.00 27.01           C  
ANISOU 3060  CD  ARG A 571     1182   4145   4935    -29    653    803       C  
ATOM   3061  NE  ARG A 571      14.697  19.253 -46.687  1.00 22.67           N  
ANISOU 3061  NE  ARG A 571      531   3614   4470    -19    579    882       N  
ATOM   3062  CZ  ARG A 571      15.589  18.441 -47.229  1.00 36.46           C  
ANISOU 3062  CZ  ARG A 571     2175   5341   6339     63    660    968       C  
ATOM   3063  NH1 ARG A 571      15.851  18.504 -48.525  1.00 26.97           N  
ANISOU 3063  NH1 ARG A 571      965   4102   5182    141    825    983       N  
ATOM   3064  NH2 ARG A 571      16.239  17.563 -46.475  1.00 30.89           N  
ANISOU 3064  NH2 ARG A 571     1377   4649   5713     70    581   1042       N  
ATOM   3065  N   TYR A 572       9.522  23.528 -48.078  1.00 30.77           N  
ANISOU 3065  N   TYR A 572     2140   4590   4960   -139    678    443       N  
ATOM   3066  CA  TYR A 572       8.698  24.436 -48.868  1.00 31.08           C  
ANISOU 3066  CA  TYR A 572     2268   4600   4940   -132    742    386       C  
ATOM   3067  C   TYR A 572       7.934  25.405 -48.003  1.00 33.71           C  
ANISOU 3067  C   TYR A 572     2665   4937   5208   -211    660    314       C  
ATOM   3068  O   TYR A 572       7.486  25.058 -46.910  1.00 31.83           O  
ANISOU 3068  O   TYR A 572     2456   4727   4911   -247    573    280       O  
ATOM   3069  CB  TYR A 572       7.685  23.643 -49.726  1.00 32.65           C  
ANISOU 3069  CB  TYR A 572     2567   4788   5049    -47    818    349       C  
ATOM   3070  CG  TYR A 572       8.313  22.652 -50.683  1.00 35.39           C  
ANISOU 3070  CG  TYR A 572     2883   5122   5442     40    914    406       C  
ATOM   3071  CD1 TYR A 572       8.500  21.323 -50.316  1.00 37.84           C  
ANISOU 3071  CD1 TYR A 572     3170   5448   5758     81    895    430       C  
ATOM   3072  CD2 TYR A 572       8.701  23.038 -51.964  1.00 36.20           C  
ANISOU 3072  CD2 TYR A 572     2987   5190   5578     85   1031    436       C  
ATOM   3073  CE1 TYR A 572       9.085  20.406 -51.191  1.00 39.48           C  
ANISOU 3073  CE1 TYR A 572     3356   5633   6010    167    993    479       C  
ATOM   3074  CE2 TYR A 572       9.257  22.122 -52.857  1.00 37.34           C  
ANISOU 3074  CE2 TYR A 572     3117   5314   5755    171   1134    483       C  
ATOM   3075  CZ  TYR A 572       9.457  20.809 -52.462  1.00 44.33           C  
ANISOU 3075  CZ  TYR A 572     3980   6213   6652    213   1116    502       C  
ATOM   3076  OH  TYR A 572      10.021  19.903 -53.327  1.00 45.12           O  
ANISOU 3076  OH  TYR A 572     4071   6285   6788    302   1226    545       O  
ATOM   3077  N   TYR A 573       7.750  26.614 -48.516  1.00 32.51           N  
ANISOU 3077  N   TYR A 573     2541   4750   5060   -235    696    291       N  
ATOM   3078  CA  TYR A 573       6.917  27.596 -47.867  1.00 33.79           C  
ANISOU 3078  CA  TYR A 573     2778   4902   5160   -295    641    216       C  
ATOM   3079  C   TYR A 573       5.488  27.375 -48.401  1.00 38.28           C  
ANISOU 3079  C   TYR A 573     3456   5463   5627   -237    691    155       C  
ATOM   3080  O   TYR A 573       5.299  27.250 -49.615  1.00 38.76           O  
ANISOU 3080  O   TYR A 573     3539   5501   5685   -173    778    171       O  
ATOM   3081  CB  TYR A 573       7.393  29.025 -48.138  1.00 36.55           C  
ANISOU 3081  CB  TYR A 573     3105   5210   5573   -350    651    223       C  
ATOM   3082  CG  TYR A 573       6.578  30.026 -47.350  1.00 39.90           C  
ANISOU 3082  CG  TYR A 573     3611   5616   5935   -412    593    142       C  
ATOM   3083  CD1 TYR A 573       6.855  30.276 -46.010  1.00 42.12           C  
ANISOU 3083  CD1 TYR A 573     3887   5909   6207   -497    485    118       C  
ATOM   3084  CD2 TYR A 573       5.469  30.653 -47.916  1.00 40.67           C  
ANISOU 3084  CD2 TYR A 573     3797   5679   5976   -382    647     88       C  
ATOM   3085  CE1 TYR A 573       6.092  31.170 -45.270  1.00 42.12           C  
ANISOU 3085  CE1 TYR A 573     3975   5885   6143   -549    444     37       C  
ATOM   3086  CE2 TYR A 573       4.687  31.540 -47.179  1.00 41.76           C  
ANISOU 3086  CE2 TYR A 573     4009   5794   6063   -429    606     12       C  
ATOM   3087  CZ  TYR A 573       5.007  31.797 -45.857  1.00 50.72           C  
ANISOU 3087  CZ  TYR A 573     5145   6939   7188   -511    511    -16       C  
ATOM   3088  OH  TYR A 573       4.266  32.677 -45.117  1.00 54.20           O  
ANISOU 3088  OH  TYR A 573     5669   7349   7575   -555    482    -94       O  
ATOM   3089  N   GLY A 574       4.518  27.284 -47.494  1.00 33.36           N  
ANISOU 3089  N   GLY A 574     2897   4857   4921   -259    634     92       N  
ATOM   3090  CA  GLY A 574       3.126  27.070 -47.863  1.00 31.98           C  
ANISOU 3090  CA  GLY A 574     2812   4677   4664   -212    669     40       C  
ATOM   3091  C   GLY A 574       2.675  25.621 -47.917  1.00 35.32           C  
ANISOU 3091  C   GLY A 574     3252   5129   5040   -156    672     48       C  
ATOM   3092  O   GLY A 574       3.339  24.722 -47.386  1.00 35.10           O  
ANISOU 3092  O   GLY A 574     3174   5130   5032   -159    636     85       O  
ATOM   3093  N   GLY A 575       1.548  25.416 -48.598  1.00 30.50           N  
ANISOU 3093  N   GLY A 575     2710   4505   4373   -108    712     18       N  
ATOM   3094  CA  GLY A 575       0.857  24.140 -48.748  1.00 29.42           C  
ANISOU 3094  CA  GLY A 575     2609   4385   4185    -59    715     15       C  
ATOM   3095  C   GLY A 575       1.594  22.968 -49.349  1.00 31.37           C  
ANISOU 3095  C   GLY A 575     2826   4635   4459     -7    746     68       C  
ATOM   3096  O   GLY A 575       1.191  21.824 -49.127  1.00 30.53           O  
ANISOU 3096  O   GLY A 575     2739   4543   4316     19    728     68       O  
ATOM   3097  N   LEU A 576       2.648  23.235 -50.138  1.00 28.00           N  
ANISOU 3097  N   LEU A 576     2353   4188   4096     13    801    115       N  
ATOM   3098  CA  LEU A 576       3.454  22.210 -50.796  1.00 27.42           C  
ANISOU 3098  CA  LEU A 576     2250   4109   4060     71    852    168       C  
ATOM   3099  C   LEU A 576       4.026  21.189 -49.826  1.00 31.33           C  
ANISOU 3099  C   LEU A 576     2685   4636   4582     64    798    199       C  
ATOM   3100  O   LEU A 576       4.209  20.039 -50.201  1.00 32.34           O  
ANISOU 3100  O   LEU A 576     2817   4758   4713    120    827    224       O  
ATOM   3101  CB  LEU A 576       4.571  22.843 -51.635  1.00 27.90           C  
ANISOU 3101  CB  LEU A 576     2257   4146   4199     83    926    219       C  
ATOM   3102  CG  LEU A 576       4.242  23.118 -53.106  1.00 31.54           C  
ANISOU 3102  CG  LEU A 576     2789   4566   4627    135   1018    217       C  
ATOM   3103  CD1 LEU A 576       5.502  23.505 -53.869  1.00 30.28           C  
ANISOU 3103  CD1 LEU A 576     2568   4386   4551    153   1104    281       C  
ATOM   3104  CD2 LEU A 576       3.580  21.889 -53.781  1.00 33.69           C  
ANISOU 3104  CD2 LEU A 576     3147   4826   4829    203   1048    203       C  
ATOM   3105  N   VAL A 577       4.262  21.603 -48.569  1.00 26.67           N  
ANISOU 3105  N   VAL A 577     2051   4076   4006     -7    714    194       N  
ATOM   3106  CA  VAL A 577       4.749  20.759 -47.489  1.00 26.54           C  
ANISOU 3106  CA  VAL A 577     1983   4092   4007    -28    641    224       C  
ATOM   3107  C   VAL A 577       3.799  19.555 -47.180  1.00 27.31           C  
ANISOU 3107  C   VAL A 577     2143   4202   4030      1    620    201       C  
ATOM   3108  O   VAL A 577       4.277  18.449 -46.896  1.00 27.03           O  
ANISOU 3108  O   VAL A 577     2073   4176   4020     27    601    244       O  
ATOM   3109  CB  VAL A 577       5.162  21.646 -46.270  1.00 31.09           C  
ANISOU 3109  CB  VAL A 577     2521   4693   4600   -121    550    219       C  
ATOM   3110  CG1 VAL A 577       4.462  21.260 -44.974  1.00 30.45           C  
ANISOU 3110  CG1 VAL A 577     2485   4646   4440   -164    465    184       C  
ATOM   3111  CG2 VAL A 577       6.676  21.659 -46.101  1.00 32.28           C  
ANISOU 3111  CG2 VAL A 577     2555   4848   4862   -140    527    296       C  
ATOM   3112  N   ALA A 578       2.476  19.763 -47.315  1.00 21.78           N  
ANISOU 3112  N   ALA A 578     1529   3496   3249      1    626    140       N  
ATOM   3113  CA  ALA A 578       1.460  18.733 -47.056  1.00 20.17           C  
ANISOU 3113  CA  ALA A 578     1384   3301   2979     21    607    119       C  
ATOM   3114  C   ALA A 578       1.264  17.737 -48.221  1.00 23.75           C  
ANISOU 3114  C   ALA A 578     1876   3721   3428     97    667    131       C  
ATOM   3115  O   ALA A 578       0.817  16.608 -47.987  1.00 24.71           O  
ANISOU 3115  O   ALA A 578     2026   3844   3520    117    646    134       O  
ATOM   3116  CB  ALA A 578       0.143  19.384 -46.643  1.00 19.70           C  
ANISOU 3116  CB  ALA A 578     1387   3249   2850    -13    588     56       C  
ATOM   3117  N   ALA A 579       1.670  18.124 -49.455  1.00 19.63           N  
ANISOU 3117  N   ALA A 579     1360   3164   2933    139    742    142       N  
ATOM   3118  CA  ALA A 579       1.603  17.299 -50.681  1.00 18.60           C  
ANISOU 3118  CA  ALA A 579     1283   2993   2789    211    808    151       C  
ATOM   3119  C   ALA A 579       2.413  15.966 -50.647  1.00 21.10           C  
ANISOU 3119  C   ALA A 579     1569   3300   3148    259    823    198       C  
ATOM   3120  O   ALA A 579       1.809  14.937 -50.940  1.00 20.42           O  
ANISOU 3120  O   ALA A 579     1548   3192   3019    293    824    185       O  
ATOM   3121  CB  ALA A 579       1.928  18.139 -51.922  1.00 19.01           C  
ANISOU 3121  CB  ALA A 579     1355   3013   2854    238    889    155       C  
ATOM   3122  N   PRO A 580       3.713  15.881 -50.241  1.00 18.88           N  
ANISOU 3122  N   PRO A 580     1189   3031   2954    261    827    255       N  
ATOM   3123  CA  PRO A 580       4.382  14.564 -50.214  1.00 19.44           C  
ANISOU 3123  CA  PRO A 580     1232   3086   3070    314    842    302       C  
ATOM   3124  C   PRO A 580       3.879  13.647 -49.086  1.00 24.81           C  
ANISOU 3124  C   PRO A 580     1917   3789   3721    289    752    301       C  
ATOM   3125  O   PRO A 580       3.989  12.430 -49.185  1.00 23.49           O  
ANISOU 3125  O   PRO A 580     1764   3596   3564    337    762    323       O  
ATOM   3126  CB  PRO A 580       5.866  14.922 -50.067  1.00 21.03           C  
ANISOU 3126  CB  PRO A 580     1311   3295   3386    316    865    369       C  
ATOM   3127  CG  PRO A 580       5.948  16.365 -50.384  1.00 24.86           C  
ANISOU 3127  CG  PRO A 580     1782   3787   3876    276    886    354       C  
ATOM   3128  CD  PRO A 580       4.676  16.924 -49.861  1.00 20.30           C  
ANISOU 3128  CD  PRO A 580     1275   3231   3206    218    818    286       C  
ATOM   3129  N   VAL A 581       3.296  14.244 -48.032  1.00 23.69           N  
ANISOU 3129  N   VAL A 581     1772   3691   3539    214    670    275       N  
ATOM   3130  CA  VAL A 581       2.679  13.547 -46.899  1.00 22.90           C  
ANISOU 3130  CA  VAL A 581     1689   3619   3394    179    588    271       C  
ATOM   3131  C   VAL A 581       1.469  12.755 -47.447  1.00 23.72           C  
ANISOU 3131  C   VAL A 581     1890   3692   3429    210    607    232       C  
ATOM   3132  O   VAL A 581       1.386  11.554 -47.215  1.00 24.29           O  
ANISOU 3132  O   VAL A 581     1977   3751   3501    233    587    254       O  
ATOM   3133  CB  VAL A 581       2.300  14.520 -45.747  1.00 25.75           C  
ANISOU 3133  CB  VAL A 581     2040   4027   3715     94    517    243       C  
ATOM   3134  CG1 VAL A 581       1.795  13.757 -44.527  1.00 25.45           C  
ANISOU 3134  CG1 VAL A 581     2020   4020   3630     58    441    249       C  
ATOM   3135  CG2 VAL A 581       3.489  15.397 -45.366  1.00 25.84           C  
ANISOU 3135  CG2 VAL A 581     1965   4058   3794     56    494    276       C  
ATOM   3136  N   PHE A 582       0.603  13.414 -48.231  1.00 18.25           N  
ANISOU 3136  N   PHE A 582     1261   2984   2688    211    641    181       N  
ATOM   3137  CA  PHE A 582      -0.548  12.833 -48.930  1.00 17.06           C  
ANISOU 3137  CA  PHE A 582     1202   2801   2479    235    653    146       C  
ATOM   3138  C   PHE A 582      -0.082  11.696 -49.847  1.00 19.62           C  
ANISOU 3138  C   PHE A 582     1561   3072   2823    306    702    168       C  
ATOM   3139  O   PHE A 582      -0.663  10.617 -49.797  1.00 18.31           O  
ANISOU 3139  O   PHE A 582     1444   2882   2630    318    678    166       O  
ATOM   3140  CB  PHE A 582      -1.253  13.911 -49.787  1.00 18.70           C  
ANISOU 3140  CB  PHE A 582     1457   2996   2651    229    684    103       C  
ATOM   3141  CG  PHE A 582      -2.260  13.369 -50.783  1.00 20.34           C  
ANISOU 3141  CG  PHE A 582     1760   3161   2808    258    696     75       C  
ATOM   3142  CD1 PHE A 582      -1.863  12.981 -52.062  1.00 24.63           C  
ANISOU 3142  CD1 PHE A 582     2359   3653   3348    317    758     80       C  
ATOM   3143  CD2 PHE A 582      -3.604  13.275 -50.455  1.00 22.93           C  
ANISOU 3143  CD2 PHE A 582     2124   3496   3091    225    646     47       C  
ATOM   3144  CE1 PHE A 582      -2.784  12.447 -52.970  1.00 25.91           C  
ANISOU 3144  CE1 PHE A 582     2621   3770   3453    336    755     54       C  
ATOM   3145  CE2 PHE A 582      -4.537  12.793 -51.384  1.00 26.55           C  
ANISOU 3145  CE2 PHE A 582     2666   3913   3509    243    642     27       C  
ATOM   3146  CZ  PHE A 582      -4.122  12.388 -52.638  1.00 25.22           C  
ANISOU 3146  CZ  PHE A 582     2563   3692   3329    295    689     29       C  
ATOM   3147  N   ALA A 583       0.921  11.962 -50.727  1.00 16.94           N  
ANISOU 3147  N   ALA A 583     1205   2706   2527    353    779    189       N  
ATOM   3148  CA  ALA A 583       1.520  10.948 -51.617  1.00 17.82           C  
ANISOU 3148  CA  ALA A 583     1350   2759   2660    430    847    210       C  
ATOM   3149  C   ALA A 583       1.834   9.665 -50.832  1.00 24.90           C  
ANISOU 3149  C   ALA A 583     2217   3651   3594    445    809    247       C  
ATOM   3150  O   ALA A 583       1.379   8.581 -51.221  1.00 23.82           O  
ANISOU 3150  O   ALA A 583     2157   3466   3428    479    814    235       O  
ATOM   3151  CB  ALA A 583       2.788  11.472 -52.276  1.00 17.94           C  
ANISOU 3151  CB  ALA A 583     1311   2763   2742    472    937    244       C  
ATOM   3152  N   LYS A 584       2.518   9.819 -49.674  1.00 22.46           N  
ANISOU 3152  N   LYS A 584     1804   3389   3342    412    758    292       N  
ATOM   3153  CA  LYS A 584       2.907   8.707 -48.810  1.00 23.13           C  
ANISOU 3153  CA  LYS A 584     1848   3473   3468    420    711    340       C  
ATOM   3154  C   LYS A 584       1.752   7.908 -48.260  1.00 24.30           C  
ANISOU 3154  C   LYS A 584     2062   3621   3551    391    645    317       C  
ATOM   3155  O   LYS A 584       1.727   6.694 -48.431  1.00 24.54           O  
ANISOU 3155  O   LYS A 584     2130   3603   3590    433    651    332       O  
ATOM   3156  CB  LYS A 584       3.855   9.175 -47.695  1.00 26.56           C  
ANISOU 3156  CB  LYS A 584     2162   3961   3969    379    655    394       C  
ATOM   3157  CG  LYS A 584       5.313   8.910 -48.004  1.00 30.91           C  
ANISOU 3157  CG  LYS A 584     2621   4488   4633    437    708    462       C  
ATOM   3158  CD  LYS A 584       6.223   9.524 -46.941  1.00 45.94           C  
ANISOU 3158  CD  LYS A 584     4404   6447   6605    382    636    517       C  
ATOM   3159  CE  LYS A 584       7.350   8.604 -46.511  1.00 52.52           C  
ANISOU 3159  CE  LYS A 584     5142   7267   7548    422    619    606       C  
ATOM   3160  NZ  LYS A 584       7.807   8.898 -45.120  1.00 54.30           N  
ANISOU 3160  NZ  LYS A 584     5282   7550   7801    346    497    655       N  
ATOM   3161  N   ILE A 585       0.790   8.581 -47.612  1.00 19.92           N  
ANISOU 3161  N   ILE A 585     1523   3113   2935    320    588    282       N  
ATOM   3162  CA  ILE A 585      -0.382   7.941 -47.020  1.00 17.54           C  
ANISOU 3162  CA  ILE A 585     1274   2817   2575    284    530    265       C  
ATOM   3163  C   ILE A 585      -1.293   7.339 -48.088  1.00 20.67           C  
ANISOU 3163  C   ILE A 585     1770   3154   2930    316    559    226       C  
ATOM   3164  O   ILE A 585      -1.678   6.179 -47.953  1.00 20.71           O  
ANISOU 3164  O   ILE A 585     1815   3125   2928    326    534    239       O  
ATOM   3165  CB  ILE A 585      -1.134   8.877 -46.028  1.00 18.29           C  
ANISOU 3165  CB  ILE A 585     1355   2975   2621    206    477    239       C  
ATOM   3166  CG1 ILE A 585      -0.190   9.421 -44.942  1.00 17.46           C  
ANISOU 3166  CG1 ILE A 585     1167   2922   2546    167    436    276       C  
ATOM   3167  CG2 ILE A 585      -2.318   8.140 -45.397  1.00 16.35           C  
ANISOU 3167  CG2 ILE A 585     1155   2734   2324    172    430    232       C  
ATOM   3168  CD1 ILE A 585      -0.653  10.790 -44.288  1.00 27.49           C  
ANISOU 3168  CD1 ILE A 585     2430   4243   3772     99    413    236       C  
ATOM   3169  N   MET A 586      -1.646   8.119 -49.137  1.00 17.05           N  
ANISOU 3169  N   MET A 586     1357   2679   2442    327    603    183       N  
ATOM   3170  CA  MET A 586      -2.507   7.638 -50.225  1.00 16.39           C  
ANISOU 3170  CA  MET A 586     1377   2537   2311    350    619    146       C  
ATOM   3171  C   MET A 586      -1.979   6.355 -50.887  1.00 21.54           C  
ANISOU 3171  C   MET A 586     2083   3117   2983    416    656    162       C  
ATOM   3172  O   MET A 586      -2.744   5.410 -51.064  1.00 20.73           O  
ANISOU 3172  O   MET A 586     2054   2971   2851    414    625    149       O  
ATOM   3173  CB  MET A 586      -2.759   8.731 -51.280  1.00 17.89           C  
ANISOU 3173  CB  MET A 586     1606   2721   2470    355    661    109       C  
ATOM   3174  CG  MET A 586      -3.785   8.312 -52.345  1.00 20.85           C  
ANISOU 3174  CG  MET A 586     2096   3040   2786    364    654     72       C  
ATOM   3175  SD  MET A 586      -5.404   7.871 -51.644  1.00 22.68           S  
ANISOU 3175  SD  MET A 586     2346   3285   2986    299    559     59       S  
ATOM   3176  CE  MET A 586      -6.158   9.495 -51.593  1.00 18.06           C  
ANISOU 3176  CE  MET A 586     1729   2749   2383    255    549     32       C  
ATOM   3177  N   GLN A 587      -0.682   6.330 -51.251  1.00 19.36           N  
ANISOU 3177  N   GLN A 587     1769   2823   2762    473    726    191       N  
ATOM   3178  CA  GLN A 587      -0.058   5.174 -51.905  1.00 19.13           C  
ANISOU 3178  CA  GLN A 587     1789   2719   2760    548    782    206       C  
ATOM   3179  C   GLN A 587      -0.164   3.902 -51.060  1.00 23.36           C  
ANISOU 3179  C   GLN A 587     2317   3236   3321    545    725    238       C  
ATOM   3180  O   GLN A 587      -0.646   2.896 -51.550  1.00 21.96           O  
ANISOU 3180  O   GLN A 587     2235   2991   3118    567    724    219       O  
ATOM   3181  CB  GLN A 587       1.392   5.456 -52.261  1.00 19.89           C  
ANISOU 3181  CB  GLN A 587     1819   2808   2929    609    872    243       C  
ATOM   3182  CG  GLN A 587       1.994   4.342 -53.124  1.00 27.18           C  
ANISOU 3182  CG  GLN A 587     2809   3642   3876    698    955    249       C  
ATOM   3183  CD  GLN A 587       3.482   4.383 -53.228  1.00 31.73           C  
ANISOU 3183  CD  GLN A 587     3293   4211   4552    764   1042    305       C  
ATOM   3184  OE1 GLN A 587       4.067   3.883 -54.187  1.00 29.74           O  
ANISOU 3184  OE1 GLN A 587     3096   3889   4317    845   1147    304       O  
ATOM   3185  NE2 GLN A 587       4.129   4.875 -52.194  1.00 17.72           N  
ANISOU 3185  NE2 GLN A 587     1379   2502   2851    731    999    359       N  
ATOM   3186  N   GLU A 588       0.256   3.974 -49.794  1.00 21.84           N  
ANISOU 3186  N   GLU A 588     2021   3102   3177    512    673    286       N  
ATOM   3187  CA  GLU A 588       0.203   2.873 -48.858  1.00 23.01           C  
ANISOU 3187  CA  GLU A 588     2152   3241   3349    503    613    328       C  
ATOM   3188  C   GLU A 588      -1.218   2.438 -48.524  1.00 26.43           C  
ANISOU 3188  C   GLU A 588     2654   3672   3716    445    544    300       C  
ATOM   3189  O   GLU A 588      -1.456   1.245 -48.336  1.00 27.41           O  
ANISOU 3189  O   GLU A 588     2819   3747   3849    456    519    318       O  
ATOM   3190  CB  GLU A 588       0.989   3.221 -47.595  1.00 25.46           C  
ANISOU 3190  CB  GLU A 588     2341   3619   3712    472    566    388       C  
ATOM   3191  CG  GLU A 588       2.463   2.872 -47.725  1.00 42.64           C  
ANISOU 3191  CG  GLU A 588     4442   5770   5990    542    615    447       C  
ATOM   3192  CD  GLU A 588       3.256   2.920 -46.435  1.00 62.90           C  
ANISOU 3192  CD  GLU A 588     6892   8390   8617    512    546    521       C  
ATOM   3193  OE1 GLU A 588       4.014   3.898 -46.246  1.00 73.96           O  
ANISOU 3193  OE1 GLU A 588     8206   9838  10057    497    550    541       O  
ATOM   3194  OE2 GLU A 588       3.116   1.988 -45.612  1.00 45.67           O  
ANISOU 3194  OE2 GLU A 588     4707   6201   6443    500    483    562       O  
ATOM   3195  N   SER A 589      -2.155   3.390 -48.467  1.00 21.89           N  
ANISOU 3195  N   SER A 589     2089   3145   3083    387    519    259       N  
ATOM   3196  CA  SER A 589      -3.566   3.137 -48.184  1.00 20.64           C  
ANISOU 3196  CA  SER A 589     1981   2990   2873    329    460    237       C  
ATOM   3197  C   SER A 589      -4.227   2.435 -49.345  1.00 22.01           C  
ANISOU 3197  C   SER A 589     2265   3080   3017    354    472    200       C  
ATOM   3198  O   SER A 589      -5.026   1.544 -49.100  1.00 23.68           O  
ANISOU 3198  O   SER A 589     2519   3261   3217    328    423    206       O  
ATOM   3199  CB  SER A 589      -4.308   4.439 -47.855  1.00 23.41           C  
ANISOU 3199  CB  SER A 589     2301   3409   3183    270    442    207       C  
ATOM   3200  OG  SER A 589      -3.756   5.103 -46.730  1.00 24.52           O  
ANISOU 3200  OG  SER A 589     2356   3622   3340    239    425    233       O  
ATOM   3201  N   LEU A 590      -3.910   2.820 -50.604  1.00 16.36           N  
ANISOU 3201  N   LEU A 590     1604   2327   2285    400    533    165       N  
ATOM   3202  CA  LEU A 590      -4.485   2.197 -51.807  1.00 16.33           C  
ANISOU 3202  CA  LEU A 590     1728   2239   2240    422    541    125       C  
ATOM   3203  C   LEU A 590      -3.943   0.777 -51.974  1.00 22.34           C  
ANISOU 3203  C   LEU A 590     2540   2917   3030    475    560    144       C  
ATOM   3204  O   LEU A 590      -4.681  -0.118 -52.392  1.00 22.26           O  
ANISOU 3204  O   LEU A 590     2627   2840   2993    465    524    124       O  
ATOM   3205  CB  LEU A 590      -4.187   3.014 -53.080  1.00 16.56           C  
ANISOU 3205  CB  LEU A 590     1810   2249   2233    459    608     87       C  
ATOM   3206  CG  LEU A 590      -4.873   4.383 -53.241  1.00 22.06           C  
ANISOU 3206  CG  LEU A 590     2486   3003   2893    412    589     62       C  
ATOM   3207  CD1 LEU A 590      -4.231   5.178 -54.354  1.00 23.05           C  
ANISOU 3207  CD1 LEU A 590     2646   3114   2998    458    669     42       C  
ATOM   3208  CD2 LEU A 590      -6.403   4.273 -53.440  1.00 22.65           C  
ANISOU 3208  CD2 LEU A 590     2621   3064   2921    355    510     36       C  
ATOM   3209  N   ARG A 591      -2.659   0.565 -51.635  1.00 19.37           N  
ANISOU 3209  N   ARG A 591     2098   2543   2719    530    612    185       N  
ATOM   3210  CA  ARG A 591      -2.078  -0.763 -51.751  1.00 20.92           C  
ANISOU 3210  CA  ARG A 591     2334   2657   2958    590    638    208       C  
ATOM   3211  C   ARG A 591      -2.642  -1.700 -50.703  1.00 27.77           C  
ANISOU 3211  C   ARG A 591     3185   3521   3843    545    553    244       C  
ATOM   3212  O   ARG A 591      -2.881  -2.853 -51.006  1.00 29.01           O  
ANISOU 3212  O   ARG A 591     3425   3592   4003    566    544    241       O  
ATOM   3213  CB  ARG A 591      -0.544  -0.736 -51.693  1.00 19.36           C  
ANISOU 3213  CB  ARG A 591     2056   2458   2841    666    719    253       C  
ATOM   3214  CG  ARG A 591       0.127  -0.010 -52.857  1.00 26.89           C  
ANISOU 3214  CG  ARG A 591     3037   3395   3784    723    825    224       C  
ATOM   3215  CD  ARG A 591      -0.178  -0.545 -54.251  1.00 28.31           C  
ANISOU 3215  CD  ARG A 591     3381   3475   3902    769    882    166       C  
ATOM   3216  NE  ARG A 591       0.252  -1.929 -54.448  1.00 47.73           N  
ANISOU 3216  NE  ARG A 591     5903   5835   6398    835    918    177       N  
ATOM   3217  CZ  ARG A 591      -0.574  -2.942 -54.701  1.00 60.22           C  
ANISOU 3217  CZ  ARG A 591     7605   7339   7935    819    869    146       C  
ATOM   3218  NH1 ARG A 591      -1.888  -2.737 -54.788  1.00 37.63           N  
ANISOU 3218  NH1 ARG A 591     4807   4494   4998    738    779    106       N  
ATOM   3219  NH2 ARG A 591      -0.094  -4.166 -54.870  1.00 42.65           N  
ANISOU 3219  NH2 ARG A 591     5437   5017   5752    884    909    156       N  
ATOM   3220  N   LEU A 592      -2.860  -1.208 -49.480  1.00 23.78           N  
ANISOU 3220  N   LEU A 592     2582   3106   3347    483    494    279       N  
ATOM   3221  CA  LEU A 592      -3.370  -1.985 -48.358  1.00 23.07           C  
ANISOU 3221  CA  LEU A 592     2468   3027   3269    435    418    322       C  
ATOM   3222  C   LEU A 592      -4.800  -2.461 -48.645  1.00 29.45           C  
ANISOU 3222  C   LEU A 592     3365   3797   4027    381    365    289       C  
ATOM   3223  O   LEU A 592      -5.157  -3.588 -48.278  1.00 32.32           O  
ANISOU 3223  O   LEU A 592     3760   4111   4407    366    322    317       O  
ATOM   3224  CB  LEU A 592      -3.297  -1.110 -47.104  1.00 22.43           C  
ANISOU 3224  CB  LEU A 592     2278   3056   3189    379    379    356       C  
ATOM   3225  CG  LEU A 592      -3.153  -1.768 -45.742  1.00 26.91           C  
ANISOU 3225  CG  LEU A 592     2790   3651   3784    348    320    425       C  
ATOM   3226  CD1 LEU A 592      -2.270  -2.964 -45.789  1.00 31.65           C  
ANISOU 3226  CD1 LEU A 592     3396   4178   4452    414    333    473       C  
ATOM   3227  CD2 LEU A 592      -2.532  -0.807 -44.776  1.00 25.65           C  
ANISOU 3227  CD2 LEU A 592     2530   3587   3629    320    304    455       C  
ATOM   3228  N   LEU A 593      -5.585  -1.630 -49.361  1.00 23.72           N  
ANISOU 3228  N   LEU A 593     2679   3087   3249    352    365    235       N  
ATOM   3229  CA  LEU A 593      -6.935  -1.958 -49.826  1.00 23.17           C  
ANISOU 3229  CA  LEU A 593     2689   2977   3138    302    311    203       C  
ATOM   3230  C   LEU A 593      -6.883  -2.735 -51.155  1.00 28.63           C  
ANISOU 3230  C   LEU A 593     3514   3554   3809    348    332    163       C  
ATOM   3231  O   LEU A 593      -7.914  -3.208 -51.638  1.00 29.63           O  
ANISOU 3231  O   LEU A 593     3723   3627   3907    307    277    139       O  
ATOM   3232  CB  LEU A 593      -7.800  -0.693 -49.985  1.00 21.97           C  
ANISOU 3232  CB  LEU A 593     2511   2891   2946    251    295    171       C  
ATOM   3233  CG  LEU A 593      -7.950   0.185 -48.752  1.00 25.20           C  
ANISOU 3233  CG  LEU A 593     2807   3405   3362    205    282    199       C  
ATOM   3234  CD1 LEU A 593      -8.614   1.516 -49.115  1.00 24.62           C  
ANISOU 3234  CD1 LEU A 593     2716   3382   3257    176    286    161       C  
ATOM   3235  CD2 LEU A 593      -8.656  -0.562 -47.594  1.00 24.98           C  
ANISOU 3235  CD2 LEU A 593     2748   3393   3349    148    226    244       C  
ATOM   3236  N   ASN A 594      -5.678  -2.861 -51.743  1.00 24.83           N  
ANISOU 3236  N   ASN A 594     3056   3032   3345    432    414    156       N  
ATOM   3237  CA  ASN A 594      -5.428  -3.595 -52.975  1.00 24.76           C  
ANISOU 3237  CA  ASN A 594     3184   2911   3313    490    457    116       C  
ATOM   3238  C   ASN A 594      -6.173  -2.983 -54.164  1.00 27.02           C  
ANISOU 3238  C   ASN A 594     3571   3178   3519    468    449     53       C  
ATOM   3239  O   ASN A 594      -6.817  -3.673 -54.951  1.00 27.59           O  
ANISOU 3239  O   ASN A 594     3775   3163   3547    456    414     17       O  
ATOM   3240  CB  ASN A 594      -5.685  -5.098 -52.764  1.00 28.09           C  
ANISOU 3240  CB  ASN A 594     3672   3239   3760    489    416    132       C  
ATOM   3241  CG  ASN A 594      -5.292  -5.993 -53.904  1.00 49.60           C  
ANISOU 3241  CG  ASN A 594     6546   5836   6465    556    469     90       C  
ATOM   3242  OD1 ASN A 594      -4.194  -5.894 -54.473  1.00 45.45           O  
ANISOU 3242  OD1 ASN A 594     6037   5283   5951    643    572     80       O  
ATOM   3243  ND2 ASN A 594      -6.203  -6.883 -54.256  1.00 38.16           N  
ANISOU 3243  ND2 ASN A 594     5212   4302   4986    515    401     64       N  
ATOM   3244  N   VAL A 595      -6.090  -1.660 -54.272  1.00 22.57           N  
ANISOU 3244  N   VAL A 595     2946   2694   2935    460    474     44       N  
ATOM   3245  CA  VAL A 595      -6.711  -0.916 -55.360  1.00 22.54           C  
ANISOU 3245  CA  VAL A 595     3023   2681   2858    442    467     -5       C  
ATOM   3246  C   VAL A 595      -5.833  -1.135 -56.611  1.00 28.62           C  
ANISOU 3246  C   VAL A 595     3911   3372   3591    525    563    -40       C  
ATOM   3247  O   VAL A 595      -4.618  -0.927 -56.540  1.00 27.23           O  
ANISOU 3247  O   VAL A 595     3680   3210   3455    592    659    -20       O  
ATOM   3248  CB  VAL A 595      -6.930   0.580 -55.005  1.00 24.26           C  
ANISOU 3248  CB  VAL A 595     3136   3006   3074    407    464      2       C  
ATOM   3249  CG1 VAL A 595      -7.516   1.361 -56.182  1.00 23.55           C  
ANISOU 3249  CG1 VAL A 595     3132   2902   2913    394    455    -41       C  
ATOM   3250  CG2 VAL A 595      -7.818   0.721 -53.778  1.00 23.04           C  
ANISOU 3250  CG2 VAL A 595     2880   2920   2952    332    384     33       C  
ATOM   3251  N   PRO A 596      -6.408  -1.647 -57.725  1.00 27.83           N  
ANISOU 3251  N   PRO A 596     3976   3182   3417    520    540    -88       N  
ATOM   3252  CA  PRO A 596      -5.585  -1.884 -58.928  1.00 28.70           C  
ANISOU 3252  CA  PRO A 596     4218   3210   3478    601    643   -125       C  
ATOM   3253  C   PRO A 596      -5.009  -0.604 -59.511  1.00 32.38           C  
ANISOU 3253  C   PRO A 596     4659   3729   3915    633    726   -131       C  
ATOM   3254  O   PRO A 596      -5.675   0.436 -59.473  1.00 31.58           O  
ANISOU 3254  O   PRO A 596     4510   3698   3791    577    673   -131       O  
ATOM   3255  CB  PRO A 596      -6.543  -2.582 -59.904  1.00 30.81           C  
ANISOU 3255  CB  PRO A 596     4672   3377   3656    566    571   -178       C  
ATOM   3256  CG  PRO A 596      -7.887  -2.245 -59.445  1.00 35.11           C  
ANISOU 3256  CG  PRO A 596     5165   3973   4200    464    435   -166       C  
ATOM   3257  CD  PRO A 596      -7.825  -1.993 -57.960  1.00 30.06           C  
ANISOU 3257  CD  PRO A 596     4334   3430   3656    440    418   -109       C  
ATOM   3258  N   LEU A 597      -3.777  -0.679 -60.053  1.00 29.67           N  
ANISOU 3258  N   LEU A 597     4344   3350   3579    724    860   -133       N  
ATOM   3259  CA  LEU A 597      -3.099   0.481 -60.658  1.00 29.07           C  
ANISOU 3259  CA  LEU A 597     4247   3315   3481    760    956   -132       C  
ATOM   3260  C   LEU A 597      -3.878   1.054 -61.854  1.00 32.36           C  
ANISOU 3260  C   LEU A 597     4810   3708   3778    728    927   -180       C  
ATOM   3261  O   LEU A 597      -4.681   0.358 -62.465  1.00 32.78           O  
ANISOU 3261  O   LEU A 597     5013   3685   3756    700    860   -220       O  
ATOM   3262  CB  LEU A 597      -1.632   0.157 -61.043  1.00 29.65           C  
ANISOU 3262  CB  LEU A 597     4325   3344   3596    868   1116   -118       C  
ATOM   3263  CG  LEU A 597      -0.672  -0.374 -59.953  1.00 33.79           C  
ANISOU 3263  CG  LEU A 597     4699   3888   4251    911   1153    -60       C  
ATOM   3264  CD1 LEU A 597       0.762  -0.337 -60.422  1.00 34.19           C  
ANISOU 3264  CD1 LEU A 597     4726   3911   4353   1014   1317    -36       C  
ATOM   3265  CD2 LEU A 597      -0.752   0.412 -58.664  1.00 33.80           C  
ANISOU 3265  CD2 LEU A 597     4508   4008   4326    850   1078    -10       C  
ATOM   3266  N   ASP A 598      -3.683   2.333 -62.157  1.00 28.97           N  
ANISOU 3266  N   ASP A 598     4335   3342   3332    724    965   -170       N  
ATOM   3267  CA  ASP A 598      -4.393   2.970 -63.273  1.00 28.11           C  
ANISOU 3267  CA  ASP A 598     4355   3214   3110    694    934   -204       C  
ATOM   3268  C   ASP A 598      -3.482   3.925 -64.052  1.00 29.71           C  
ANISOU 3268  C   ASP A 598     4571   3433   3285    748   1065   -197       C  
ATOM   3269  O   ASP A 598      -3.936   4.662 -64.929  1.00 27.43           O  
ANISOU 3269  O   ASP A 598     4371   3142   2908    725   1050   -214       O  
ATOM   3270  CB  ASP A 598      -5.698   3.637 -62.781  1.00 28.20           C  
ANISOU 3270  CB  ASP A 598     4301   3291   3124    598    788   -197       C  
ATOM   3271  CG  ASP A 598      -5.566   5.029 -62.198  1.00 32.71           C  
ANISOU 3271  CG  ASP A 598     4713   3966   3749    576    797   -162       C  
ATOM   3272  OD1 ASP A 598      -4.555   5.298 -61.523  1.00 33.93           O  
ANISOU 3272  OD1 ASP A 598     4742   4166   3983    613    876   -131       O  
ATOM   3273  OD2 ASP A 598      -6.509   5.824 -62.353  1.00 32.37           O  
ANISOU 3273  OD2 ASP A 598     4667   3956   3677    519    716   -164       O  
ATOM   3274  N   LYS A 599      -2.190   3.890 -63.723  1.00 27.29           N  
ANISOU 3274  N   LYS A 599     4171   3140   3059    818   1191   -165       N  
ATOM   3275  CA  LYS A 599      -1.172   4.706 -64.371  1.00 28.66           C  
ANISOU 3275  CA  LYS A 599     4334   3325   3229    874   1332   -147       C  
ATOM   3276  C   LYS A 599      -0.008   3.809 -64.866  1.00 34.44           C  
ANISOU 3276  C   LYS A 599     5129   3979   3978    977   1487   -148       C  
ATOM   3277  O   LYS A 599       0.515   2.985 -64.092  1.00 33.04           O  
ANISOU 3277  O   LYS A 599     4867   3791   3897   1011   1504   -125       O  
ATOM   3278  CB  LYS A 599      -0.668   5.790 -63.397  1.00 29.30           C  
ANISOU 3278  CB  LYS A 599     4200   3512   3420    853   1337    -93       C  
ATOM   3279  CG  LYS A 599      -0.147   7.044 -64.063  1.00 29.51           C  
ANISOU 3279  CG  LYS A 599     4215   3570   3429    868   1427    -75       C  
ATOM   3280  CD  LYS A 599       0.215   8.111 -63.016  1.00 33.37           C  
ANISOU 3280  CD  LYS A 599     4498   4156   4024    831   1406    -27       C  
ATOM   3281  CE  LYS A 599       1.700   8.172 -62.712  1.00 34.16           C  
ANISOU 3281  CE  LYS A 599     4473   4271   4234    893   1531     24       C  
ATOM   3282  NZ  LYS A 599       1.984   8.935 -61.476  1.00 36.35           N  
ANISOU 3282  NZ  LYS A 599     4555   4637   4619    846   1478     67       N  
ATOM   3283  N   PRO A 600       0.399   3.941 -66.150  1.00 34.08           N  
ANISOU 3283  N   PRO A 600     5234   3875   3840   1030   1606   -171       N  
ATOM   3284  CA  PRO A 600       1.535   3.144 -66.642  1.00 35.70           C  
ANISOU 3284  CA  PRO A 600     5498   4003   4066   1137   1776   -170       C  
ATOM   3285  C   PRO A 600       2.799   3.451 -65.841  1.00 42.08           C  
ANISOU 3285  C   PRO A 600     6087   4868   5035   1187   1874    -98       C  
ATOM   3286  O   PRO A 600       3.032   4.607 -65.490  1.00 41.19           O  
ANISOU 3286  O   PRO A 600     5835   4841   4972   1154   1869    -57       O  
ATOM   3287  CB  PRO A 600       1.698   3.600 -68.100  1.00 38.05           C  
ANISOU 3287  CB  PRO A 600     5977   4252   4229   1171   1886   -198       C  
ATOM   3288  CG  PRO A 600       0.438   4.256 -68.457  1.00 42.13           C  
ANISOU 3288  CG  PRO A 600     6579   4794   4635   1078   1741   -227       C  
ATOM   3289  CD  PRO A 600      -0.106   4.851 -67.198  1.00 36.59           C  
ANISOU 3289  CD  PRO A 600     5675   4194   4034    999   1600   -192       C  
ATOM   3290  N   LEU A 601       3.584   2.425 -65.518  1.00 41.32           N  
ANISOU 3290  N   LEU A 601     5954   4719   5025   1261   1951    -81       N  
ATOM   3291  CA  LEU A 601       4.831   2.629 -64.782  1.00 42.58           C  
ANISOU 3291  CA  LEU A 601     5903   4925   5348   1311   2038     -4       C  
ATOM   3292  C   LEU A 601       5.973   2.895 -65.767  1.00 48.89           C  
ANISOU 3292  C   LEU A 601     6736   5685   6155   1406   2250     16       C  
ATOM   3293  O   LEU A 601       5.879   2.491 -66.931  1.00 49.98           O  
ANISOU 3293  O   LEU A 601     7082   5735   6174   1454   2341    -35       O  
ATOM   3294  CB  LEU A 601       5.156   1.404 -63.898  1.00 43.09           C  
ANISOU 3294  CB  LEU A 601     5897   4956   5521   1348   2013     18       C  
ATOM   3295  CG  LEU A 601       4.155   1.053 -62.802  1.00 46.69           C  
ANISOU 3295  CG  LEU A 601     6304   5450   5987   1259   1820     11       C  
ATOM   3296  CD1 LEU A 601       4.259  -0.417 -62.438  1.00 47.74           C  
ANISOU 3296  CD1 LEU A 601     6472   5501   6166   1305   1811      8       C  
ATOM   3297  CD2 LEU A 601       4.337   1.941 -61.564  1.00 47.42           C  
ANISOU 3297  CD2 LEU A 601     6171   5664   6185   1198   1737     73       C  
ATOM   3298  N   ASP A 602       7.049   3.568 -65.309  1.00 46.33           N  
ANISOU 3298  N   ASP A 602     6213   5422   5968   1432   2328     93       N  
ATOM   3299  CA  ASP A 602       8.221   3.843 -66.155  1.00 84.86           C  
ANISOU 3299  CA  ASP A 602    11091  10269  10881   1523   2541    129       C  
ATOM   3300  C   ASP A 602       9.549   3.663 -65.419  1.00108.92           C  
ANISOU 3300  C   ASP A 602    13917  13336  14132   1587   2626    219       C  
ATOM   3301  O   ASP A 602       9.704   4.119 -64.288  1.00 70.85           O  
ANISOU 3301  O   ASP A 602     8897   8598   9423   1530   2519    272       O  
ATOM   3302  CB  ASP A 602       8.138   5.231 -66.822  1.00 86.54           C  
ANISOU 3302  CB  ASP A 602    11322  10533  11024   1481   2575    135       C  
ATOM   3303  CG  ASP A 602       8.335   5.231 -68.336  1.00 99.00           C  
ANISOU 3303  CG  ASP A 602    13111  12034  12470   1545   2741    100       C  
ATOM   3304  OD1 ASP A 602       8.971   4.282 -68.860  1.00101.02           O  
ANISOU 3304  OD1 ASP A 602    13451  12201  12733   1647   2892     92       O  
ATOM   3305  OD2 ASP A 602       7.881   6.194 -68.993  1.00104.90           O  
ANISOU 3305  OD2 ASP A 602    13942  12809  13108   1496   2727     84       O  
TER    3306      ASP A 602                                                      
HETATM 3307  O   HOH A   1     -20.332  37.761 -47.103  1.00 35.54           O  
HETATM 3308  O   HOH A   2      -0.919  12.149 -61.014  1.00 28.23           O  
HETATM 3309  O   HOH A   3      -5.266  21.548 -37.854  1.00 37.77           O  
HETATM 3310  O   HOH A   4      -1.740  31.331 -54.090  1.00 49.31           O  
HETATM 3311  O   HOH A   5     -28.932  12.362 -43.447  1.00 53.67           O  
HETATM 3312  O   HOH A   6      10.786  12.084 -40.141  1.00 39.05           O  
HETATM 3313  O   HOH A  10       2.187  39.342 -61.925  1.00 19.95           O  
HETATM 3314  O   HOH A  11     -15.120  36.414 -66.951  1.00 27.36           O  
HETATM 3315  O   HOH A  12       3.477  35.315 -36.599  1.00 31.24           O  
HETATM 3316  O   HOH A  13     -21.561  19.505 -43.571  1.00 16.63           O  
HETATM 3317  O   HOH A  14     -15.513  22.323 -72.846  1.00 40.45           O  
HETATM 3318  O   HOH A  15     -16.104  -6.991 -38.348  1.00 36.77           O  
HETATM 3319  O   HOH A  16      -1.235  27.721 -51.603  1.00 26.06           O  
HETATM 3320  O   HOH A  17     -18.911  35.914 -68.549  1.00 44.35           O  
HETATM 3321  O   HOH A  18     -23.198  -6.450 -29.193  1.00 33.71           O  
HETATM 3322  O   HOH A  19     -17.433  25.521 -43.687  1.00 22.47           O  
HETATM 3323  O   HOH A  20      -6.593   0.354 -64.375  1.00 28.43           O  
HETATM 3324  O   HOH A  21     -20.513  35.330 -57.435  1.00 31.38           O  
HETATM 3325  O   HOH A  22      -7.128  37.599 -48.063  1.00 31.07           O  
HETATM 3326  O   HOH A  23       2.366   2.372 -21.589  1.00 56.77           O  
HETATM 3327  O   HOH A  24       6.260  21.931 -64.512  1.00 32.49           O  
HETATM 3328  O   HOH A  25       1.689  34.956 -69.280  1.00 45.77           O  
HETATM 3329  O   HOH A  27     -25.469   1.612 -41.391  1.00 18.54           O  
HETATM 3330  O   HOH A  29      -4.545  23.726 -67.975  1.00 37.97           O  
HETATM 3331  O   HOH A  33     -10.443  20.730 -39.160  1.00 18.14           O  
HETATM 3332  O   HOH A  34     -24.374   4.409 -34.334  1.00 58.17           O  
HETATM 3333  O   HOH A  35      -2.755  23.332 -56.050  1.00 22.50           O  
HETATM 3334  O   HOH A  36     -18.851  43.465 -43.905  1.00 44.97           O  
HETATM 3335  O   HOH A  37     -19.809  -5.633 -38.865  1.00 50.05           O  
HETATM 3336  O   HOH A  38      -0.587  20.490 -65.658  1.00 23.76           O  
HETATM 3337  O   HOH A  39      -3.724  11.554 -67.859  1.00 29.67           O  
HETATM 3338  O   HOH A  40     -19.861   9.813 -34.543  1.00 39.38           O  
HETATM 3339  O   HOH A  42      11.563  26.306 -50.686  1.00 34.20           O  
HETATM 3340  O   HOH A  44     -18.520  20.192 -46.965  1.00 16.20           O  
HETATM 3341  O   HOH A  45      -1.785  28.230 -37.706  1.00 22.77           O  
HETATM 3342  O   HOH A  46     -15.029  -5.972 -43.367  1.00 38.12           O  
HETATM 3343  O   HOH A  48     -21.822   5.767 -54.160  1.00 34.70           O  
HETATM 3344  O   HOH A  49     -20.996   2.083 -52.311  1.00 52.31           O  
HETATM 3345  O   HOH A  51       5.238  12.605 -54.384  1.00 26.31           O  
HETATM 3346  O   HOH A  52      -4.789  35.944 -48.549  1.00 29.28           O  
HETATM 3347  O   HOH A  53       7.426  20.155 -33.154  1.00 42.13           O  
HETATM 3348  O   HOH A  54       0.002   1.033 -24.467  1.00 33.95           O  
HETATM 3349  O   HOH A  55     -16.192   6.833 -57.444  1.00 22.71           O  
HETATM 3350  O   HOH A 610     -11.768  13.120 -28.279  1.00 22.62           O  
HETATM 3351  O   HOH A 611       3.897  37.079 -69.712  1.00 53.86           O  
HETATM 3352  O   HOH A 612       6.948   7.918 -37.502  1.00 27.32           O  
HETATM 3353  O   HOH A 613      -5.330  25.505 -33.103  1.00 53.96           O  
HETATM 3354  O   HOH A 614      -6.667  46.958 -47.964  1.00 37.93           O  
HETATM 3355  O   HOH A 615      10.604   2.006 -68.916  1.00 67.37           O  
HETATM 3356  O   HOH A 616      -3.297  14.175 -69.137  1.00 66.47           O  
HETATM 3357  O   HOH A 617     -19.113  10.836 -51.695  1.00 14.87           O  
HETATM 3358  O   HOH A 618     -12.266 -10.059 -33.534  1.00 37.41           O  
HETATM 3359  O   HOH A 619     -20.003  18.052 -51.077  1.00 24.82           O  
HETATM 3360  O   HOH A 620       7.480  28.209 -43.436  1.00 33.72           O  
HETATM 3361  O   HOH A 621       5.467  11.851 -44.121  1.00 32.71           O  
HETATM 3362  O   HOH A 622     -23.205  15.945 -30.769  1.00 47.85           O  
HETATM 3363  O   HOH A 623      -5.086  27.941 -69.483  1.00 23.31           O  
HETATM 3364  O   HOH A 624     -22.266  -2.853 -38.678  1.00 30.22           O  
HETATM 3365  O   HOH A 625     -16.674  37.540 -45.668  1.00 37.43           O  
HETATM 3366  O   HOH A 626     -20.214  -2.135 -44.673  1.00 21.02           O  
HETATM 3367  O   HOH A 627     -17.145  19.777 -39.482  1.00 25.98           O  
HETATM 3368  O   HOH A 628     -28.675  10.650 -54.491  1.00 34.53           O  
HETATM 3369  O   HOH A 629      -9.021  42.233 -70.502  1.00 46.81           O  
HETATM 3370  O   HOH A 630       9.073  17.983 -33.497  1.00 27.93           O  
HETATM 3371  O   HOH A 631      -3.776   0.935 -18.273  1.00 51.61           O  
HETATM 3372  O   HOH A 632      -4.549   5.930 -44.125  1.00 29.81           O  
HETATM 3373  O   HOH A 633     -16.712  -4.808 -31.368  1.00 31.76           O  
HETATM 3374  O   HOH A 634       6.238  15.071 -59.898  1.00 27.93           O  
HETATM 3375  O   HOH A 635     -12.915  38.844 -46.746  1.00 46.20           O  
HETATM 3376  O   HOH A 636       3.000   5.912 -25.055  1.00 43.46           O  
HETATM 3377  O   HOH A 637      -4.185   1.184 -35.414  1.00 35.20           O  
HETATM 3378  O   HOH A 638     -18.123  10.745 -48.545  1.00 24.88           O  
HETATM 3379  O   HOH A 639     -13.659  32.479 -73.619  1.00 48.73           O  
HETATM 3380  O   HOH A 640      -1.764  30.366 -30.868  1.00 51.31           O  
HETATM 3381  O   HOH A 641     -21.417  -8.444 -17.959  1.00 32.11           O  
HETATM 3382  O   HOH A 642       6.121  28.276 -39.523  1.00 20.20           O  
HETATM 3383  O   HOH A 643       7.373  25.272 -44.211  1.00 27.32           O  
HETATM 3384  O   HOH A 644     -20.474  -1.407 -17.746  1.00 40.26           O  
HETATM 3385  O   HOH A 645     -15.764   9.984 -60.729  1.00 38.35           O  
HETATM 3386  O   HOH A 646      -0.825   1.198 -17.240  1.00 53.16           O  
HETATM 3387  O   HOH A 647     -21.072  18.162 -32.735  1.00 36.41           O  
HETATM 3388  O   HOH A 648      -6.390  41.342 -63.442  1.00 37.54           O  
HETATM 3389  O   HOH A 649     -19.134  -0.876 -46.530  1.00 39.18           O  
HETATM 3390  O   HOH A 650       4.564  38.923 -67.391  1.00 41.11           O  
HETATM 3391  O   HOH A 651     -14.188  -4.050 -44.988  1.00 50.28           O  
HETATM 3392  O   HOH A 652     -27.539   1.923 -39.647  1.00 51.00           O  
HETATM 3393  O   HOH A 653      -4.181  29.031 -50.219  1.00 14.95           O  
HETATM 3394  O   HOH A 654       4.256  21.677 -57.737  1.00 21.76           O  
HETATM 3395  O   HOH A 655       5.039  34.725 -66.288  1.00 35.92           O  
HETATM 3396  O   HOH A 656     -21.557  14.259 -43.547  1.00 23.13           O  
HETATM 3397  O   HOH A 657     -17.440  -2.211 -17.134  1.00 36.51           O  
HETATM 3398  O   HOH A 658      -7.912  45.347 -38.715  1.00 54.90           O  
HETATM 3399  O   HOH A 659      -6.682  24.302 -70.115  1.00 42.19           O  
HETATM 3400  O   HOH A 660       6.589  28.710 -36.939  1.00 36.06           O  
HETATM 3401  O   HOH A 661       6.571  12.327 -31.378  1.00 43.94           O  
HETATM 3402  O   HOH A 662      -7.192  41.452 -46.314  1.00 59.47           O  
HETATM 3403  O   HOH A 663      -7.161  15.159 -66.277  1.00 30.60           O  
HETATM 3404  O   HOH A 664     -25.614   5.416 -36.475  1.00 78.61           O  
HETATM 3405  O   HOH A 665     -15.720   0.741 -60.573  1.00 40.42           O  
HETATM 3406  O   HOH A 666      -2.937  19.874 -37.728  1.00 25.85           O  
HETATM 3407  O   HOH A 667     -25.357  21.207 -60.330  1.00 38.50           O  
HETATM 3408  O   HOH A 668      -7.875   9.237 -33.721  1.00 27.98           O  
HETATM 3409  O   HOH A 669     -25.409   5.597 -26.388  1.00 35.36           O  
HETATM 3410  O   HOH A 670      -5.832  -5.189 -31.184  1.00 41.55           O  
HETATM 3411  O   HOH A 671     -20.863  10.235 -68.723  1.00 44.31           O  
HETATM 3412  O   HOH A 672       6.160  35.756 -56.149  1.00 44.80           O  
HETATM 3413  O   HOH A 673     -16.383   6.440 -60.214  1.00 31.11           O  
HETATM 3414  O   HOH A 674     -18.355  33.249 -45.735  1.00 25.59           O  
HETATM 3415  O   HOH A 675     -21.030   8.357 -37.652  1.00 34.51           O  
HETATM 3416  O   HOH A 676       8.134  17.155 -59.464  1.00 40.39           O  
HETATM 3417  O   HOH A 677      -9.446  38.835 -47.306  1.00 66.08           O  
HETATM 3418  O   HOH A 678      -4.163  40.806 -41.497  1.00 30.95           O  
HETATM 3419  O   HOH A 679       4.520  26.572 -57.061  1.00 43.66           O  
HETATM 3420  O   HOH A 680       1.791  34.973 -53.046  1.00 42.70           O  
HETATM 3421  O   HOH A 681       9.089  33.936 -39.892  1.00 45.96           O  
HETATM 3422  O   HOH A 682      -7.658  -4.481 -39.845  1.00 39.82           O  
HETATM 3423  O   HOH A 683     -27.955   9.531 -48.179  1.00 32.21           O  
HETATM 3424  O   HOH A 684     -30.143  -0.600 -40.347  1.00 50.70           O  
HETATM 3425  O   HOH A 685     -19.313  -7.642 -10.608  1.00 33.88           O  
HETATM 3426  O   HOH A 686       0.138  30.022 -57.966  1.00 35.94           O  
HETATM 3427  O   HOH A 687      -0.851  35.492 -53.143  1.00 58.77           O  
HETATM 3428  O   HOH A 688       6.058   7.803 -67.725  1.00 62.02           O  
HETATM 3429  O   HOH A 689      12.683  26.114 -42.643  1.00 35.38           O  
HETATM 3430  O   HOH A 690       5.169   5.539 -69.246  1.00 50.31           O  
HETATM 3431  O   HOH A 691       2.586  10.140 -27.227  1.00 65.70           O  
HETATM 3432  O   HOH A 692       6.988  13.225 -61.682  1.00 53.56           O  
HETATM 3433  O   HOH A 693       4.822   2.813 -70.025  1.00 30.09           O  
HETATM 3434  O   HOH A 694     -26.047   6.363 -30.195  1.00 53.29           O  
HETATM 3435  O   HOH A 695      -3.333  38.298 -52.443  1.00 20.75           O  
HETATM 3436  O   HOH A 696      -9.634  43.169 -68.108  1.00 55.58           O  
HETATM 3437  O   HOH A 697     -25.083   1.400 -38.014  1.00 40.20           O  
HETATM 3438  O   HOH A 698       8.829  10.949 -31.916  1.00 45.71           O  
HETATM 3439  O   HOH A 699       2.620  12.027 -29.226  1.00 43.20           O  
HETATM 3440  O   HOH A 700      -8.371  16.904 -68.795  1.00 74.01           O  
HETATM 3441  O   HOH A 701      13.339  26.615 -40.035  1.00 55.37           O  
HETATM 3442  O   HOH A 702      -8.013  -8.324 -38.743  1.00 44.66           O  
HETATM 3443  O   HOH A 703      -7.539  17.111 -72.247  1.00 73.23           O  
HETATM 3444  O   HOH A 704       9.800  10.554 -34.224  1.00 37.09           O  
HETATM 3445  O   HOH A 705      -6.847   1.703 -29.310  1.00 20.29           O  
HETATM 3446  O   HOH A 706      -7.240   4.245 -28.627  1.00 28.74           O  
HETATM 3447  O   HOH A 707       0.206  10.534 -59.418  1.00 16.60           O  
HETATM 3448  O   HOH A 708      -8.273   1.475 -60.022  1.00 38.34           O  
HETATM 3449  O   HOH A 709       3.726  26.749 -51.548  1.00 45.75           O  
HETATM 3450  O   HOH A 710       6.553  17.704 -45.713  1.00 20.10           O  
HETATM 3451  O   HOH A 711       8.311  18.335 -47.567  1.00 24.40           O  
HETATM 3452  O   HOH A 712      -2.695  -3.352 -60.032  1.00 24.64           O  
HETATM 3453  O   HOH A 713      -8.221  36.199 -43.179  1.00 35.42           O  
HETATM 3454  O   HOH A 714      -1.281  32.122 -57.391  1.00 20.93           O  
HETATM 3455  O   HOH A 715       2.711  26.470 -62.140  1.00 36.29           O  
HETATM 3456  O   HOH A 716     -13.961  -1.566 -18.391  1.00 40.38           O  
HETATM 3457  O   HOH A 717      -5.761   9.839 -32.249  1.00 34.10           O  
HETATM 3458  O   HOH A 718      -8.460   5.533 -26.711  1.00 37.57           O  
HETATM 3459  O   HOH A 719     -23.275  -7.381 -25.890  1.00 52.53           O  
HETATM 3460  O   HOH A 720      -1.946  35.809 -63.206  1.00 35.26           O  
HETATM 3461  O   HOH A 721     -21.563  34.727 -55.317  1.00 30.41           O  
HETATM 3462  O   HOH A 722     -14.948  37.456 -47.751  1.00 41.93           O  
HETATM 3463  O   HOH A 723     -16.694  12.811 -60.345  1.00 28.50           O  
HETATM 3464  O   HOH A 724     -20.189  21.870 -67.944  1.00 37.15           O  
HETATM 3465  O   HOH A 725      -1.981  11.452 -63.362  1.00 32.68           O  
HETATM 3466  O   HOH A 726       1.914   2.698 -56.237  1.00 31.99           O  
HETATM 3467  O   HOH A 727      -1.847  27.961 -35.316  1.00 31.51           O  
HETATM 3468  O   HOH A 728       9.880  18.929 -45.191  1.00 35.70           O  
HETATM 3469  O   HOH A 729       3.430   5.406 -62.983  1.00 36.85           O  
HETATM 3470  O   HOH A 730      -3.442  31.337 -48.561  1.00 33.18           O  
HETATM 3471  O   HOH A 731       0.108  40.299 -46.287  1.00 35.17           O  
MASTER      449    0    0   18   18    0    0    6 3470    1    0   43          
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.