CNRS Nantes University UFIP UFIP
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***  hsa_ab1  ***

elNémo ID: 19090919135863860

Job options:

ID        	=	 19090919135863860
JOBID     	=	 hsa_ab1
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER hsa_ab1

ATOM      1  N   LYS A   4     -15.704  18.270  -8.603  1.00 91.28           N  
ANISOU    1  N   LYS A   4    10672  12029  11982      6    -54   1081       N  
ATOM      2  CA  LYS A   4     -16.681  19.416  -8.555  1.00 95.68           C  
ANISOU    2  CA  LYS A   4    11195  12579  12580     32    -20   1148       C  
ATOM      3  C   LYS A   4     -17.787  19.100  -7.538  1.00 94.18           C  
ANISOU    3  C   LYS A   4    10994  12373  12416     40    -11   1166       C  
ATOM      4  O   LYS A   4     -18.898  18.735  -7.903  1.00100.32           O  
ANISOU    4  O   LYS A   4    11740  13183  13195     33    -31   1210       O  
ATOM      5  CB  LYS A   4     -17.260  19.679  -9.957  1.00 98.64           C  
ANISOU    5  CB  LYS A   4    11532  13005  12944     25    -41   1206       C  
ATOM      6  CG  LYS A   4     -16.244  20.195 -10.985  1.00105.12           C  
ANISOU    6  CG  LYS A   4    12359  13839  13743     22    -43   1199       C  
ATOM      7  CD  LYS A   4     -15.270  19.129 -11.515  1.00100.42           C  
ANISOU    7  CD  LYS A   4    11792  13264  13099     -7    -83   1141       C  
ATOM      8  CE  LYS A   4     -13.802  19.532 -11.390  1.00 93.70           C  
ANISOU    8  CE  LYS A   4    10975  12384  12242     -1    -65   1092       C  
ATOM      9  NZ  LYS A   4     -12.889  18.367 -11.533  1.00 88.75           N1+
ANISOU    9  NZ  LYS A   4    10380  11768  11574    -26    -98   1030       N1+
ATOM     10  N   SER A   5     -17.466  19.286  -6.261  1.00 90.14           N  
ANISOU   10  N   SER A   5    10510  11813  11925     55     21   1132       N  
ATOM     11  CA  SER A   5     -18.026  18.500  -5.144  1.00 83.84           C  
ANISOU   11  CA  SER A   5     9721  11000  11136     54     20   1115       C  
ATOM     12  C   SER A   5     -17.305  17.147  -5.031  1.00 91.74           C  
ANISOU   12  C   SER A   5    10751  12009  12098     28    -19   1052       C  
ATOM     13  O   SER A   5     -17.713  16.155  -5.657  1.00 86.58           O  
ANISOU   13  O   SER A   5    10085  11393  11419      4    -61   1056       O  
ATOM     14  CB  SER A   5     -19.511  18.275  -5.244  1.00 77.92           C  
ANISOU   14  CB  SER A   5     8931  10273  10402     56     11   1174       C  
ATOM     15  OG  SER A   5     -19.887  17.292  -4.298  1.00 75.95           O  
ANISOU   15  OG  SER A   5     8694  10013  10152     49      1   1149       O  
ATOM     16  N   GLU A   6     -16.235  17.110  -4.231  1.00 93.37           N  
ANISOU   16  N   GLU A   6    10996  12180  12300     31     -4    994       N  
ATOM     17  CA  GLU A   6     -15.266  16.026  -4.330  1.00 91.09           C  
ANISOU   17  CA  GLU A   6    10736  11900  11973      8    -37    935       C  
ATOM     18  C   GLU A   6     -15.704  14.809  -3.533  1.00 83.82           C  
ANISOU   18  C   GLU A   6     9824  10977  11045     -3    -56    911       C  
ATOM     19  O   GLU A   6     -15.668  13.695  -4.047  1.00 82.94           O  
ANISOU   19  O   GLU A   6     9715  10894  10905    -27    -95    894       O  
ATOM     20  CB  GLU A   6     -13.872  16.497  -3.882  1.00104.31           C  
ANISOU   20  CB  GLU A   6    12447  13542  13644     15    -16    884       C  
ATOM     21  CG  GLU A   6     -12.701  15.694  -4.467  1.00117.26           C  
ANISOU   21  CG  GLU A   6    14110  15199  15245     -8    -48    835       C  
ATOM     22  CD  GLU A   6     -12.498  15.917  -5.974  1.00125.41           C  
ANISOU   22  CD  GLU A   6    15125  16269  16256    -19    -68    858       C  
ATOM     23  OE1 GLU A   6     -12.611  17.070  -6.446  1.00132.00           O  
ANISOU   23  OE1 GLU A   6    15942  17103  17109     -4    -45    896       O  
ATOM     24  OE2 GLU A   6     -12.208  14.936  -6.696  1.00130.39           O1-
ANISOU   24  OE2 GLU A   6    15761  16930  16851    -42   -106    837       O1-
ATOM     25  N   VAL A   7     -16.137  15.020  -2.291  1.00 77.63           N  
ANISOU   25  N   VAL A   7     9047  10159  10290     16    -26    912       N  
ATOM     26  CA  VAL A   7     -16.564  13.915  -1.437  1.00 71.38           C  
ANISOU   26  CA  VAL A   7     8263   9362   9495      8    -39    892       C  
ATOM     27  C   VAL A   7     -17.500  13.004  -2.188  1.00 69.00           C  
ANISOU   27  C   VAL A   7     7934   9102   9181    -13    -79    920       C  
ATOM     28  O   VAL A   7     -17.396  11.803  -2.089  1.00 72.94           O  
ANISOU   28  O   VAL A   7     8444   9611   9658    -32   -108    889       O  
ATOM     29  CB  VAL A   7     -17.243  14.410  -0.135  1.00 76.23           C  
ANISOU   29  CB  VAL A   7     8878   9939  10145     34      1    907       C  
ATOM     30  CG1 VAL A   7     -18.504  15.229  -0.405  1.00 72.80           C  
ANISOU   30  CG1 VAL A   7     8404   9512   9743     50     20    978       C  
ATOM     31  CG2 VAL A   7     -17.571  13.233   0.764  1.00 78.18           C  
ANISOU   31  CG2 VAL A   7     9136  10181  10387     26    -13    883       C  
ATOM     32  N   ALA A   8     -18.405  13.593  -2.954  1.00 74.55           N  
ANISOU   32  N   ALA A   8     8600   9829   9898     -9    -79    980       N  
ATOM     33  CA  ALA A   8     -19.375  12.851  -3.747  1.00 74.19           C  
ANISOU   33  CA  ALA A   8     8523   9826   9841    -30   -116   1015       C  
ATOM     34  C   ALA A   8     -18.661  12.100  -4.848  1.00 69.32           C  
ANISOU   34  C   ALA A   8     7916   9242   9181    -59   -158    985       C  
ATOM     35  O   ALA A   8     -18.891  10.924  -5.032  1.00 65.98           O  
ANISOU   35  O   ALA A   8     7494   8839   8736    -84   -193    969       O  
ATOM     36  CB  ALA A   8     -20.433  13.801  -4.326  1.00 77.73           C  
ANISOU   36  CB  ALA A   8     8928  10292  10315    -17   -103   1089       C  
ATOM     37  N   HIS A   9     -17.780  12.781  -5.568  1.00 74.23           N  
ANISOU   37  N   HIS A   9     8546   9868   9789    -57   -153    977       N  
ATOM     38  CA  HIS A   9     -17.076  12.174  -6.700  1.00 77.39           C  
ANISOU   38  CA  HIS A   9     8956  10302  10149    -83   -190    952       C  
ATOM     39  C   HIS A   9     -16.357  10.903  -6.261  1.00 80.44           C  
ANISOU   39  C   HIS A   9     9376  10679  10509   -101   -211    888       C  
ATOM     40  O   HIS A   9     -16.603   9.833  -6.813  1.00 81.96           O  
ANISOU   40  O   HIS A   9     9567  10900  10676   -128   -249    879       O  
ATOM     41  CB  HIS A   9     -16.099  13.169  -7.350  1.00 78.27           C  
ANISOU   41  CB  HIS A   9     9075  10411  10254    -73   -173    949       C  
ATOM     42  CG  HIS A   9     -15.077  12.519  -8.228  1.00 83.73           C  
ANISOU   42  CG  HIS A   9     9788  11124  10902    -96   -203    908       C  
ATOM     43  CD2 HIS A   9     -13.729  12.486  -8.144  1.00 91.87           C  
ANISOU   43  CD2 HIS A   9    10852  12137  11917    -96   -197    857       C  
ATOM     44  ND1 HIS A   9     -15.402  11.784  -9.346  1.00 88.13           N  
ANISOU   44  ND1 HIS A   9    10332  11726  11428   -123   -244    918       N  
ATOM     45  CE1 HIS A   9     -14.301  11.330  -9.916  1.00 85.68           C  
ANISOU   45  CE1 HIS A   9    10047  11423  11083   -137   -260    874       C  
ATOM     46  NE2 HIS A   9     -13.268  11.751  -9.211  1.00 88.51           N  
ANISOU   46  NE2 HIS A   9    10433  11745  11452   -121   -232    838       N  
ATOM     47  N   ARG A  10     -15.513  11.020  -5.238  1.00 86.90           N  
ANISOU   47  N   ARG A  10    10226  11457  11336    -87   -186    846       N  
ATOM     48  CA  ARG A  10     -14.754   9.877  -4.716  1.00 87.40           C  
ANISOU   48  CA  ARG A  10    10322  11508  11377   -100   -201    786       C  
ATOM     49  C   ARG A  10     -15.652   8.762  -4.120  1.00 76.95           C  
ANISOU   49  C   ARG A  10     8993  10188  10058   -111   -219    786       C  
ATOM     50  O   ARG A  10     -15.365   7.588  -4.263  1.00 73.93           O  
ANISOU   50  O   ARG A  10     8625   9814   9650   -133   -247    752       O  
ATOM     51  CB  ARG A  10     -13.687  10.342  -3.695  1.00 93.64           C  
ANISOU   51  CB  ARG A  10    11144  12257  12178    -81   -169    745       C  
ATOM     52  CG  ARG A  10     -12.727  11.453  -4.169  1.00 99.34           C  
ANISOU   52  CG  ARG A  10    11873  12971  12899    -70   -149    742       C  
ATOM     53  CD  ARG A  10     -11.700  10.996  -5.205  1.00103.64           C  
ANISOU   53  CD  ARG A  10    12433  13539  13407    -89   -175    711       C  
ATOM     54  NE  ARG A  10     -10.983  12.117  -5.819  1.00100.17           N  
ANISOU   54  NE  ARG A  10    11993  13098  12969    -79   -158    720       N  
ATOM     55  CZ  ARG A  10     -10.091  11.988  -6.796  1.00110.10           C  
ANISOU   55  CZ  ARG A  10    13260  14375  14198    -92   -174    702       C  
ATOM     56  NH1 ARG A  10      -9.796  10.794  -7.290  1.00121.15           N1+
ANISOU   56  NH1 ARG A  10    14671  15796  15564   -115   -207    673       N1+
ATOM     57  NH2 ARG A  10      -9.496  13.058  -7.297  1.00118.58           N  
ANISOU   57  NH2 ARG A  10    14332  15446  15278    -81   -155    713       N  
ATOM     58  N   PHE A  11     -16.753   9.122  -3.480  1.00 76.01           N  
ANISOU   58  N   PHE A  11     8852  10059   9971    -97   -201    826       N  
ATOM     59  CA  PHE A  11     -17.753   8.123  -3.084  1.00 74.74           C  
ANISOU   59  CA  PHE A  11     8678   9905   9815   -108   -219    836       C  
ATOM     60  C   PHE A  11     -18.319   7.304  -4.262  1.00 71.53           C  
ANISOU   60  C   PHE A  11     8251   9543   9383   -140   -264    852       C  
ATOM     61  O   PHE A  11     -18.578   6.113  -4.131  1.00 69.65           O  
ANISOU   61  O   PHE A  11     8018   9312   9134   -160   -289    833       O  
ATOM     62  CB  PHE A  11     -18.916   8.798  -2.376  1.00 76.23           C  
ANISOU   62  CB  PHE A  11     8840  10080  10043    -86   -192    886       C  
ATOM     63  CG  PHE A  11     -19.820   7.840  -1.665  1.00 82.50           C  
ANISOU   63  CG  PHE A  11     9626  10872  10848    -93   -202    892       C  
ATOM     64  CD1 PHE A  11     -20.680   7.006  -2.371  1.00 80.59           C  
ANISOU   64  CD1 PHE A  11     9360  10665  10596   -119   -239    915       C  
ATOM     65  CD2 PHE A  11     -19.811   7.776  -0.275  1.00 90.91           C  
ANISOU   65  CD2 PHE A  11    10708  11899  11933    -73   -174    874       C  
ATOM     66  CE1 PHE A  11     -21.496   6.116  -1.709  1.00 84.92           C  
ANISOU   66  CE1 PHE A  11     9900  11210  11156   -125   -248    919       C  
ATOM     67  CE2 PHE A  11     -20.636   6.894   0.400  1.00 92.63           C  
ANISOU   67  CE2 PHE A  11    10919  12114  12162    -78   -181    880       C  
ATOM     68  CZ  PHE A  11     -21.480   6.054  -0.320  1.00 92.42           C  
ANISOU   68  CZ  PHE A  11    10867  12122  12128   -104   -218    903       C  
ATOM     69  N   LYS A  12     -18.549   7.947  -5.393  1.00 72.00           N  
ANISOU   69  N   LYS A  12     8287   9634   9437   -145   -273    889       N  
ATOM     70  CA  LYS A  12     -19.186   7.281  -6.506  1.00 73.82           C  
ANISOU   70  CA  LYS A  12     8496   9909   9644   -175   -314    910       C  
ATOM     71  C   LYS A  12     -18.224   6.327  -7.138  1.00 78.68           C  
ANISOU   71  C   LYS A  12     9141  10538  10218   -201   -344    857       C  
ATOM     72  O   LYS A  12     -18.610   5.215  -7.519  1.00 89.52           O  
ANISOU   72  O   LYS A  12    10512  11932  11571   -229   -378    847       O  
ATOM     73  CB  LYS A  12     -19.659   8.289  -7.554  1.00 78.47           C  
ANISOU   73  CB  LYS A  12     9051  10529  10236   -171   -315    966       C  
ATOM     74  CG  LYS A  12     -20.999   8.908  -7.219  1.00 81.56           C  
ANISOU   74  CG  LYS A  12     9402  10923  10664   -155   -299   1031       C  
ATOM     75  CD  LYS A  12     -21.371  10.019  -8.174  1.00 81.84           C  
ANISOU   75  CD  LYS A  12     9405  10985  10705   -147   -293   1088       C  
ATOM     76  CE  LYS A  12     -21.960  11.191  -7.416  1.00 86.96           C  
ANISOU   76  CE  LYS A  12    10034  11606  11401   -111   -248   1133       C  
ATOM     77  NZ  LYS A  12     -21.335  12.462  -7.871  1.00 97.73           N1+
ANISOU   77  NZ  LYS A  12    11398  12964  12770    -91   -221   1147       N1+
ATOM     78  N   ASP A  13     -16.972   6.752  -7.255  1.00 72.51           N  
ANISOU   78  N   ASP A  13     8385   9741   9423   -191   -330    823       N  
ATOM     79  CA  ASP A  13     -15.968   5.930  -7.905  1.00 72.79           C  
ANISOU   79  CA  ASP A  13     8449   9788   9418   -213   -354    774       C  
ATOM     80  C   ASP A  13     -15.667   4.639  -7.132  1.00 74.15           C  
ANISOU   80  C   ASP A  13     8649   9940   9583   -225   -364    724       C  
ATOM     81  O   ASP A  13     -15.384   3.597  -7.741  1.00 74.38           O  
ANISOU   81  O   ASP A  13     8692   9988   9582   -251   -393    695       O  
ATOM     82  CB  ASP A  13     -14.691   6.730  -8.104  1.00 77.01           C  
ANISOU   82  CB  ASP A  13     9006  10310   9946   -198   -333    751       C  
ATOM     83  CG  ASP A  13     -14.864   7.828  -9.105  1.00 81.87           C  
ANISOU   83  CG  ASP A  13     9596  10949  10561   -192   -329    795       C  
ATOM     84  OD1 ASP A  13     -16.021   8.261  -9.319  1.00 86.42           O  
ANISOU   84  OD1 ASP A  13    10138  11544  11155   -190   -330    850       O  
ATOM     85  OD2 ASP A  13     -13.843   8.252  -9.682  1.00 81.79           O1-
ANISOU   85  OD2 ASP A  13     9602  10941  10534   -189   -324    777       O1-
ATOM     86  N   LEU A  14     -15.772   4.704  -5.805  1.00 68.10           N  
ANISOU   86  N   LEU A  14     7890   9139   8846   -205   -338    717       N  
ATOM     87  CA  LEU A  14     -15.275   3.648  -4.945  1.00 66.38           C  
ANISOU   87  CA  LEU A  14     7702   8898   8623   -209   -340    668       C  
ATOM     88  C   LEU A  14     -16.331   2.763  -4.311  1.00 73.84           C  
ANISOU   88  C   LEU A  14     8633   9839   9582   -218   -351    679       C  
ATOM     89  O   LEU A  14     -16.083   1.585  -4.036  1.00 77.60           O  
ANISOU   89  O   LEU A  14     9130  10310  10045   -233   -366    642       O  
ATOM     90  CB  LEU A  14     -14.468   4.287  -3.839  1.00 66.94           C  
ANISOU   90  CB  LEU A  14     7794   8929   8712   -180   -303    645       C  
ATOM     91  CG  LEU A  14     -13.245   5.012  -4.375  1.00 71.05           C  
ANISOU   91  CG  LEU A  14     8330   9447   9217   -174   -293    625       C  
ATOM     92  CD1 LEU A  14     -12.419   5.595  -3.225  1.00 70.53           C  
ANISOU   92  CD1 LEU A  14     8287   9342   9168   -148   -259    599       C  
ATOM     93  CD2 LEU A  14     -12.397   4.089  -5.240  1.00 75.09           C  
ANISOU   93  CD2 LEU A  14     8863   9977   9690   -198   -321    586       C  
ATOM     94  N   GLY A  15     -17.495   3.333  -4.036  1.00 83.78           N  
ANISOU   94  N   GLY A  15     9861  11101  10870   -207   -340    730       N  
ATOM     95  CA  GLY A  15     -18.560   2.606  -3.359  1.00 86.52           C  
ANISOU   95  CA  GLY A  15    10194  11445  11236   -212   -347    745       C  
ATOM     96  C   GLY A  15     -18.358   2.615  -1.855  1.00 81.01           C  
ANISOU   96  C   GLY A  15     9513  10705  10562   -187   -315    726       C  
ATOM     97  O   GLY A  15     -17.231   2.627  -1.367  1.00 73.12           O  
ANISOU   97  O   GLY A  15     8546   9682   9553   -177   -301    683       O  
ATOM     98  N   GLU A  16     -19.472   2.562  -1.135  1.00 81.88           N  
ANISOU   98  N   GLU A  16     9602  10807  10700   -179   -306    759       N  
ATOM     99  CA  GLU A  16     -19.500   2.751   0.317  1.00 86.78           C  
ANISOU   99  CA  GLU A  16    10235  11391  11348   -152   -272    753       C  
ATOM    100  C   GLU A  16     -18.501   1.945   1.146  1.00 87.45           C  
ANISOU  100  C   GLU A  16    10357  11450  11419   -151   -268    694       C  
ATOM    101  O   GLU A  16     -17.812   2.515   1.988  1.00 99.83           O  
ANISOU  101  O   GLU A  16    11947  12990  12995   -128   -239    674       O  
ATOM    102  CB  GLU A  16     -20.902   2.475   0.838  1.00 98.96           C  
ANISOU  102  CB  GLU A  16    11748  12935  12919   -150   -271    795       C  
ATOM    103  CG  GLU A  16     -21.203   3.044   2.218  1.00102.06           C  
ANISOU  103  CG  GLU A  16    12143  13292  13343   -117   -230    806       C  
ATOM    104  CD  GLU A  16     -22.695   3.203   2.437  1.00103.45           C  
ANISOU  104  CD  GLU A  16    12281  13475  13551   -111   -224    865       C  
ATOM    105  OE1 GLU A  16     -23.415   3.285   1.424  1.00104.20           O  
ANISOU  105  OE1 GLU A  16    12345  13603  13645   -127   -246    904       O  
ATOM    106  OE2 GLU A  16     -23.152   3.244   3.603  1.00101.26           O1-
ANISOU  106  OE2 GLU A  16    12005  13172  13299    -90   -197    873       O1-
ATOM    107  N   GLU A  17     -18.419   0.634   0.940  1.00 84.38           N  
ANISOU  107  N   GLU A  17     9978  11070  11012   -176   -297    667       N  
ATOM    108  CA  GLU A  17     -17.539  -0.187   1.786  1.00 82.66           C  
ANISOU  108  CA  GLU A  17     9795  10829  10785   -173   -292    616       C  
ATOM    109  C   GLU A  17     -16.148   0.381   1.911  1.00 73.37           C  
ANISOU  109  C   GLU A  17     8647   9636   9594   -160   -275    579       C  
ATOM    110  O   GLU A  17     -15.725   0.694   3.011  1.00 73.24           O  
ANISOU  110  O   GLU A  17     8647   9591   9589   -137   -248    563       O  
ATOM    111  CB  GLU A  17     -17.454  -1.627   1.318  1.00 86.66           C  
ANISOU  111  CB  GLU A  17    10310  11348  11270   -203   -325    588       C  
ATOM    112  CG  GLU A  17     -18.155  -2.561   2.281  1.00 92.19           C  
ANISOU  112  CG  GLU A  17    11007  12033  11987   -204   -324    590       C  
ATOM    113  CD  GLU A  17     -18.381  -3.921   1.689  1.00 98.23           C  
ANISOU  113  CD  GLU A  17    11773  12813  12736   -237   -358    574       C  
ATOM    114  OE1 GLU A  17     -17.373  -4.593   1.358  1.00 93.53           O  
ANISOU  114  OE1 GLU A  17    11205  12216  12114   -249   -369    529       O  
ATOM    115  OE2 GLU A  17     -19.573  -4.295   1.555  1.00100.69           O1-
ANISOU  115  OE2 GLU A  17    12058  13138  13062   -251   -372    607       O1-
ATOM    116  N   ASN A  18     -15.455   0.520   0.785  1.00 72.38           N  
ANISOU  116  N   ASN A  18     8527   9530   9444   -174   -292    566       N  
ATOM    117  CA  ASN A  18     -14.151   1.214   0.751  1.00 78.59           C  
ANISOU  117  CA  ASN A  18     9336  10305  10218   -161   -276    537       C  
ATOM    118  C   ASN A  18     -14.210   2.626   1.325  1.00 81.55           C  
ANISOU  118  C   ASN A  18     9705  10662  10617   -133   -241    560       C  
ATOM    119  O   ASN A  18     -13.359   3.022   2.128  1.00 87.49           O  
ANISOU  119  O   ASN A  18    10480  11389  11372   -116   -218    533       O  
ATOM    120  CB  ASN A  18     -13.597   1.347  -0.673  1.00 71.16           C  
ANISOU  120  CB  ASN A  18     8396   9392   9250   -179   -297    532       C  
ATOM    121  CG  ASN A  18     -13.714   0.092  -1.460  1.00 66.81           C  
ANISOU  121  CG  ASN A  18     7848   8863   8675   -209   -332    517       C  
ATOM    122  ND2 ASN A  18     -13.642   0.243  -2.780  1.00 64.00           N  
ANISOU  122  ND2 ASN A  18     7484   8536   8297   -227   -352    526       N  
ATOM    123  OD1 ASN A  18     -13.882  -1.010  -0.898  1.00 64.63           O  
ANISOU  123  OD1 ASN A  18     7580   8576   8398   -218   -340    498       O  
ATOM    124  N   PHE A  19     -15.189   3.393   0.881  1.00 74.01           N  
ANISOU  124  N   PHE A  19     8721   9721   9680   -129   -237    610       N  
ATOM    125  CA  PHE A  19     -15.308   4.737   1.343  1.00 78.17           C  
ANISOU  125  CA  PHE A  19     9240  10230  10230   -102   -202    634       C  
ATOM    126  C   PHE A  19     -15.324   4.709   2.879  1.00 85.67           C  
ANISOU  126  C   PHE A  19    10205  11145  11199    -82   -175    620       C  
ATOM    127  O   PHE A  19     -14.550   5.417   3.528  1.00 97.73           O  
ANISOU  127  O   PHE A  19    11753  12648  12731    -64   -148    599       O  
ATOM    128  CB  PHE A  19     -16.576   5.356   0.779  1.00 77.83           C  
ANISOU  128  CB  PHE A  19     9158  10206  10206   -101   -202    695       C  
ATOM    129  CG  PHE A  19     -16.774   6.774   1.184  1.00 74.07           C  
ANISOU  129  CG  PHE A  19     8674   9711   9758    -73   -164    724       C  
ATOM    130  CD1 PHE A  19     -17.522   7.079   2.305  1.00 76.56           C  
ANISOU  130  CD1 PHE A  19     8983  10002  10104    -52   -136    745       C  
ATOM    131  CD2 PHE A  19     -16.200   7.802   0.447  1.00 73.53           C  
ANISOU  131  CD2 PHE A  19     8605   9648   9686    -67   -155    732       C  
ATOM    132  CE1 PHE A  19     -17.694   8.390   2.702  1.00 80.87           C  
ANISOU  132  CE1 PHE A  19     9523  10527  10675    -26    -97    770       C  
ATOM    133  CE2 PHE A  19     -16.367   9.110   0.825  1.00 70.11           C  
ANISOU  133  CE2 PHE A  19     8164   9194   9279    -42   -117    758       C  
ATOM    134  CZ  PHE A  19     -17.109   9.405   1.955  1.00 76.98           C  
ANISOU  134  CZ  PHE A  19     9030  10039  10179    -21    -88    776       C  
ATOM    135  N   LYS A  20     -16.154   3.834   3.442  1.00 83.52           N  
ANISOU  135  N   LYS A  20     9926  10872  10937    -86   -182    628       N  
ATOM    136  CA  LYS A  20     -16.342   3.708   4.892  1.00 82.40           C  
ANISOU  136  CA  LYS A  20     9796  10700  10813    -67   -157    619       C  
ATOM    137  C   LYS A  20     -15.092   3.221   5.558  1.00 69.77           C  
ANISOU  137  C   LYS A  20     8232   9083   9195    -65   -154    564       C  
ATOM    138  O   LYS A  20     -14.744   3.602   6.662  1.00 68.58           O  
ANISOU  138  O   LYS A  20     8099   8906   9053    -46   -127    549       O  
ATOM    139  CB  LYS A  20     -17.447   2.684   5.158  1.00 96.36           C  
ANISOU  139  CB  LYS A  20    11547  12476  12591    -76   -172    639       C  
ATOM    140  CG  LYS A  20     -18.283   2.965   6.387  1.00104.48           C  
ANISOU  140  CG  LYS A  20    12568  13480  13648    -53   -142    662       C  
ATOM    141  CD  LYS A  20     -19.766   2.782   6.079  1.00101.63           C  
ANISOU  141  CD  LYS A  20    12169  13137  13308    -59   -152    715       C  
ATOM    142  CE  LYS A  20     -20.599   3.322   7.230  1.00102.88           C  
ANISOU  142  CE  LYS A  20    12319  13272  13500    -31   -115    745       C  
ATOM    143  NZ  LYS A  20     -22.040   3.398   6.909  1.00103.07           N1+
ANISOU  143  NZ  LYS A  20    12302  13311  13548    -33   -119    804       N1+
ATOM    144  N   ALA A  21     -14.421   2.336   4.861  1.00 73.98           N  
ANISOU  144  N   ALA A  21     8776   9631   9701    -87   -183    534       N  
ATOM    145  CA  ALA A  21     -13.209   1.735   5.370  1.00 83.87           C  
ANISOU  145  CA  ALA A  21    10060  10870  10934    -88   -185    483       C  
ATOM    146  C   ALA A  21     -12.058   2.730   5.318  1.00 79.48           C  
ANISOU  146  C   ALA A  21     9522  10305  10371    -77   -168    462       C  
ATOM    147  O   ALA A  21     -11.287   2.846   6.271  1.00 76.25           O  
ANISOU  147  O   ALA A  21     9136   9875   9961    -64   -150    433       O  
ATOM    148  CB  ALA A  21     -12.871   0.466   4.577  1.00 89.14           C  
ANISOU  148  CB  ALA A  21    10734  11557  11577   -115   -219    459       C  
ATOM    149  N   LEU A  22     -11.956   3.446   4.202  1.00 78.74           N  
ANISOU  149  N   LEU A  22     9417  10229  10273    -83   -174    479       N  
ATOM    150  CA  LEU A  22     -10.869   4.395   3.988  1.00 76.29           C  
ANISOU  150  CA  LEU A  22     9120   9910   9955    -75   -160    462       C  
ATOM    151  C   LEU A  22     -10.803   5.509   5.026  1.00 68.87           C  
ANISOU  151  C   LEU A  22     8188   8943   9038    -51   -122    466       C  
ATOM    152  O   LEU A  22      -9.739   5.778   5.618  1.00 56.58           O  
ANISOU  152  O   LEU A  22     6655   7369   7475    -43   -109    432       O  
ATOM    153  CB  LEU A  22     -10.964   4.980   2.579  1.00 75.38           C  
ANISOU  153  CB  LEU A  22     8987   9820   9834    -85   -171    487       C  
ATOM    154  CG  LEU A  22     -10.304   4.016   1.598  1.00 73.01           C  
ANISOU  154  CG  LEU A  22     8696   9543   9503   -109   -204    460       C  
ATOM    155  CD1 LEU A  22     -10.359   4.503   0.159  1.00 68.73           C  
ANISOU  155  CD1 LEU A  22     8138   9029   8950   -120   -218    483       C  
ATOM    156  CD2 LEU A  22      -8.857   3.796   2.020  1.00 69.16           C  
ANISOU  156  CD2 LEU A  22     8239   9040   8999   -106   -199    411       C  
ATOM    157  N   VAL A  23     -11.942   6.142   5.256  1.00 62.75           N  
ANISOU  157  N   VAL A  23     7391   8162   8288    -38   -105    508       N  
ATOM    158  CA  VAL A  23     -11.994   7.158   6.263  1.00 63.04           C  
ANISOU  158  CA  VAL A  23     7435   8171   8347    -15    -67    513       C  
ATOM    159  C   VAL A  23     -11.607   6.562   7.604  1.00 62.91           C  
ANISOU  159  C   VAL A  23     7443   8132   8326     -8    -58    479       C  
ATOM    160  O   VAL A  23     -10.870   7.180   8.388  1.00 64.05           O  
ANISOU  160  O   VAL A  23     7610   8255   8472      4    -35    455       O  
ATOM    161  CB  VAL A  23     -13.387   7.747   6.420  1.00 61.93           C  
ANISOU  161  CB  VAL A  23     7268   8027   8235     -1    -49    565       C  
ATOM    162  CG1 VAL A  23     -13.376   8.736   7.580  1.00 64.15           C  
ANISOU  162  CG1 VAL A  23     7562   8274   8537     23     -7    564       C  
ATOM    163  CG2 VAL A  23     -13.870   8.403   5.132  1.00 59.41           C  
ANISOU  163  CG2 VAL A  23     6921   7730   7922     -7    -56    606       C  
ATOM    164  N   LEU A  24     -12.105   5.360   7.870  1.00 64.09           N  
ANISOU  164  N   LEU A  24     7590   8290   8471    -16    -77    477       N  
ATOM    165  CA  LEU A  24     -11.862   4.757   9.170  1.00 75.16           C  
ANISOU  165  CA  LEU A  24     9012   9673   9872     -8    -67    449       C  
ATOM    166  C   LEU A  24     -10.336   4.624   9.457  1.00 78.31           C  
ANISOU  166  C   LEU A  24     9441  10065  10248    -11    -69    399       C  
ATOM    167  O   LEU A  24      -9.852   4.825  10.570  1.00 74.65           O  
ANISOU  167  O   LEU A  24     8998   9581   9784      2    -50    377       O  
ATOM    168  CB  LEU A  24     -12.575   3.421   9.303  1.00 74.50           C  
ANISOU  168  CB  LEU A  24     8920   9600   9787    -18    -88    455       C  
ATOM    169  CG  LEU A  24     -12.243   2.727  10.630  1.00 81.92           C  
ANISOU  169  CG  LEU A  24     9882  10522  10723     -9    -79    426       C  
ATOM    170  CD1 LEU A  24     -12.676   3.579  11.830  1.00 81.47           C  
ANISOU  170  CD1 LEU A  24     9830  10440  10686     16    -42    438       C  
ATOM    171  CD2 LEU A  24     -12.904   1.348  10.627  1.00 90.92           C  
ANISOU  171  CD2 LEU A  24    11012  11671  11861    -21   -101    431       C  
ATOM    172  N   ILE A  25      -9.590   4.311   8.418  1.00 77.88           N  
ANISOU  172  N   ILE A  25     9388  10028  10174    -27    -93    383       N  
ATOM    173  CA  ILE A  25      -8.156   4.241   8.511  1.00 70.62           C  
ANISOU  173  CA  ILE A  25     8493   9105   9234    -31    -96    341       C  
ATOM    174  C   ILE A  25      -7.623   5.641   8.809  1.00 67.14           C  
ANISOU  174  C   ILE A  25     8061   8648   8803    -18    -69    338       C  
ATOM    175  O   ILE A  25      -6.737   5.806   9.628  1.00 68.02           O  
ANISOU  175  O   ILE A  25     8193   8743   8907    -12    -57    307       O  
ATOM    176  CB  ILE A  25      -7.578   3.676   7.192  1.00 67.39           C  
ANISOU  176  CB  ILE A  25     8082   8720   8804    -51   -126    330       C  
ATOM    177  CG1 ILE A  25      -8.026   2.221   7.030  1.00 62.89           C  
ANISOU  177  CG1 ILE A  25     7508   8163   8225    -65   -151    327       C  
ATOM    178  CG2 ILE A  25      -6.061   3.789   7.166  1.00 67.53           C  
ANISOU  178  CG2 ILE A  25     8121   8734   8804    -54   -126    291       C  
ATOM    179  CD1 ILE A  25      -8.219   1.786   5.602  1.00 63.47           C  
ANISOU  179  CD1 ILE A  25     7568   8262   8285    -86   -178    337       C  
ATOM    180  N   ALA A  26      -8.172   6.651   8.151  1.00 60.76           N  
ANISOU  180  N   ALA A  26     7235   7841   8010    -14    -58    371       N  
ATOM    181  CA  ALA A  26      -7.595   7.960   8.260  1.00 63.89           C  
ANISOU  181  CA  ALA A  26     7639   8222   8414     -4    -33    367       C  
ATOM    182  C   ALA A  26      -7.677   8.367   9.692  1.00 67.98           C  
ANISOU  182  C   ALA A  26     8173   8712   8944     13     -4    357       C  
ATOM    183  O   ALA A  26      -6.657   8.651  10.327  1.00 73.88           O  
ANISOU  183  O   ALA A  26     8944   9446   9683     15      5    323       O  
ATOM    184  CB  ALA A  26      -8.336   8.962   7.396  1.00 67.96           C  
ANISOU  184  CB  ALA A  26     8131   8743   8948      0    -23    410       C  
ATOM    185  N   PHE A  27      -8.897   8.385  10.214  1.00 67.20           N  
ANISOU  185  N   PHE A  27     8063   8606   8865     24     10    387       N  
ATOM    186  CA  PHE A  27      -9.088   8.877  11.561  1.00 62.15           C  
ANISOU  186  CA  PHE A  27     7437   7938   8237     42     41    381       C  
ATOM    187  C   PHE A  27      -8.251   8.011  12.438  1.00 61.65           C  
ANISOU  187  C   PHE A  27     7399   7873   8153     38     31    339       C  
ATOM    188  O   PHE A  27      -7.494   8.510  13.232  1.00 63.24           O  
ANISOU  188  O   PHE A  27     7622   8057   8349     43     48    312       O  
ATOM    189  CB  PHE A  27     -10.549   8.843  12.001  1.00 63.57           C  
ANISOU  189  CB  PHE A  27     7601   8113   8440     55     56    421       C  
ATOM    190  CG  PHE A  27     -11.425   9.889  11.348  1.00 65.00           C  
ANISOU  190  CG  PHE A  27     7758   8293   8646     63     74    467       C  
ATOM    191  CD1 PHE A  27     -10.901  11.100  10.934  1.00 65.00           C  
ANISOU  191  CD1 PHE A  27     7761   8283   8652     67     92    467       C  
ATOM    192  CD2 PHE A  27     -12.777   9.665  11.179  1.00 70.26           C  
ANISOU  192  CD2 PHE A  27     8398   8967   9331     69     74    511       C  
ATOM    193  CE1 PHE A  27     -11.678  12.054  10.349  1.00 62.00           C  
ANISOU  193  CE1 PHE A  27     7360   7901   8296     76    110    511       C  
ATOM    194  CE2 PHE A  27     -13.574  10.617  10.599  1.00 70.61           C  
ANISOU  194  CE2 PHE A  27     8419   9011   9399     78     91    556       C  
ATOM    195  CZ  PHE A  27     -13.022  11.815  10.182  1.00 68.84           C  
ANISOU  195  CZ  PHE A  27     8199   8777   9180     82    109    556       C  
ATOM    196  N   ALA A  28      -8.324   6.710  12.215  1.00 68.03           N  
ANISOU  196  N   ALA A  28     8202   8698   8948     27      3    333       N  
ATOM    197  CA  ALA A  28      -7.585   5.763  13.023  1.00 75.52           C  
ANISOU  197  CA  ALA A  28     9171   9645   9877     24     -7    297       C  
ATOM    198  C   ALA A  28      -6.153   6.198  13.101  1.00 70.76           C  
ANISOU  198  C   ALA A  28     8589   9038   9259     19     -6    260       C  
ATOM    199  O   ALA A  28      -5.571   6.190  14.178  1.00 75.98           O  
ANISOU  199  O   ALA A  28     9270   9687   9912     25      5    234       O  
ATOM    200  CB  ALA A  28      -7.651   4.369  12.410  1.00 83.62           C  
ANISOU  200  CB  ALA A  28    10189  10693  10890      8    -40    293       C  
ATOM    201  N   GLN A  29      -5.621   6.611  11.954  1.00 66.08           N  
ANISOU  201  N   GLN A  29     7989   8457   8662      9    -17    260       N  
ATOM    202  CA  GLN A  29      -4.184   6.798  11.768  1.00 70.11           C  
ANISOU  202  CA  GLN A  29     8515   8969   9154      1    -23    226       C  
ATOM    203  C   GLN A  29      -3.653   8.093  12.397  1.00 69.01           C  
ANISOU  203  C   GLN A  29     8390   8808   9023      9      5    215       C  
ATOM    204  O   GLN A  29      -2.542   8.117  12.925  1.00 67.16           O  
ANISOU  204  O   GLN A  29     8174   8568   8774      6      5    181       O  
ATOM    205  CB  GLN A  29      -3.801   6.709  10.270  1.00 74.60           C  
ANISOU  205  CB  GLN A  29     9071   9558   9714    -13    -45    232       C  
ATOM    206  CG  GLN A  29      -3.750   5.276   9.699  1.00 75.24           C  
ANISOU  206  CG  GLN A  29     9149   9660   9779    -26    -76    224       C  
ATOM    207  CD  GLN A  29      -3.175   5.177   8.277  1.00 74.74           C  
ANISOU  207  CD  GLN A  29     9079   9617   9702    -41    -96    223       C  
ATOM    208  NE2 GLN A  29      -2.432   4.105   8.020  1.00 79.14           N  
ANISOU  208  NE2 GLN A  29     9644  10185  10239    -52   -117    198       N  
ATOM    209  OE1 GLN A  29      -3.387   6.041   7.431  1.00 68.48           O  
ANISOU  209  OE1 GLN A  29     8273   8829   8917    -42    -91    244       O  
ATOM    210  N   TYR A  30      -4.458   9.152  12.359  1.00 67.64           N  
ANISOU  210  N   TYR A  30     8208   8621   8872     20     29    243       N  
ATOM    211  CA  TYR A  30      -4.151  10.421  13.042  1.00 68.50           C  
ANISOU  211  CA  TYR A  30     8331   8704   8991     29     61    235       C  
ATOM    212  C   TYR A  30      -4.437  10.400  14.570  1.00 72.59           C  
ANISOU  212  C   TYR A  30     8867   9203   9511     41     82    222       C  
ATOM    213  O   TYR A  30      -3.624  10.803  15.409  1.00 74.27           O  
ANISOU  213  O   TYR A  30     9102   9402   9715     41     94    192       O  
ATOM    214  CB  TYR A  30      -5.020  11.514  12.466  1.00 62.90           C  
ANISOU  214  CB  TYR A  30     7605   7987   8308     38     83    273       C  
ATOM    215  CG  TYR A  30      -4.706  11.980  11.076  1.00 59.27           C  
ANISOU  215  CG  TYR A  30     7130   7541   7850     29     73    287       C  
ATOM    216  CD1 TYR A  30      -4.925  11.185   9.983  1.00 59.13           C  
ANISOU  216  CD1 TYR A  30     7093   7550   7823     19     43    302       C  
ATOM    217  CD2 TYR A  30      -4.283  13.273  10.870  1.00 59.79           C  
ANISOU  217  CD2 TYR A  30     7199   7591   7929     32     95    288       C  
ATOM    218  CE1 TYR A  30      -4.684  11.652   8.712  1.00 65.58           C  
ANISOU  218  CE1 TYR A  30     7896   8380   8640     12     35    316       C  
ATOM    219  CE2 TYR A  30      -4.045  13.765   9.614  1.00 63.82           C  
ANISOU  219  CE2 TYR A  30     7694   8113   8442     26     89    304       C  
ATOM    220  CZ  TYR A  30      -4.240  12.964   8.529  1.00 67.58           C  
ANISOU  220  CZ  TYR A  30     8152   8618   8907     16     59    319       C  
ATOM    221  OH  TYR A  30      -3.955  13.514   7.284  1.00 71.02           O  
ANISOU  221  OH  TYR A  30     8574   9066   9344     11     54    335       O  
ATOM    222  N   LEU A  31      -5.641   9.984  14.925  1.00 78.18           N  
ANISOU  222  N   LEU A  31     9565   9910  10230     51     88    248       N  
ATOM    223  CA  LEU A  31      -6.062   9.944  16.327  1.00 79.53           C  
ANISOU  223  CA  LEU A  31     9752  10063  10404     64    109    242       C  
ATOM    224  C   LEU A  31      -5.864   8.498  16.789  1.00 77.27           C  
ANISOU  224  C   LEU A  31     9470   9791  10098     59     85    225       C  
ATOM    225  O   LEU A  31      -6.768   7.661  16.806  1.00 71.45           O  
ANISOU  225  O   LEU A  31     8720   9062   9366     63     76    246       O  
ATOM    226  CB  LEU A  31      -7.498  10.475  16.484  1.00 82.23           C  
ANISOU  226  CB  LEU A  31    10079  10392  10773     81    136    284       C  
ATOM    227  CG  LEU A  31      -7.663  11.918  15.928  1.00 84.10           C  
ANISOU  227  CG  LEU A  31    10310  10613  11031     86    161    304       C  
ATOM    228  CD1 LEU A  31      -9.094  12.402  15.636  1.00 74.12           C  
ANISOU  228  CD1 LEU A  31     9023   9343   9797    101    182    354       C  
ATOM    229  CD2 LEU A  31      -6.946  12.871  16.877  1.00 88.69           C  
ANISOU  229  CD2 LEU A  31    10920  11169  11610     91    190    273       C  
ATOM    230  N   GLN A  32      -4.621   8.223  17.133  1.00 72.04           N  
ANISOU  230  N   GLN A  32     8825   9132   9413     51     73    187       N  
ATOM    231  CA  GLN A  32      -4.213   6.899  17.479  1.00 68.93           C  
ANISOU  231  CA  GLN A  32     8437   8754   9000     45     49    168       C  
ATOM    232  C   GLN A  32      -4.635   6.600  18.897  1.00 70.49           C  
ANISOU  232  C   GLN A  32     8648   8940   9196     58     65    163       C  
ATOM    233  O   GLN A  32      -5.051   5.476  19.189  1.00 79.13           O  
ANISOU  233  O   GLN A  32     9738  10043  10286     60     53    168       O  
ATOM    234  CB  GLN A  32      -2.699   6.767  17.273  1.00 75.96           C  
ANISOU  234  CB  GLN A  32     9339   9654   9870     32     32    132       C  
ATOM    235  CG  GLN A  32      -2.279   7.132  15.826  1.00 74.82           C  
ANISOU  235  CG  GLN A  32     9181   9520   9727     20     18    138       C  
ATOM    236  CD  GLN A  32      -0.791   7.055  15.550  1.00 63.93           C  
ANISOU  236  CD  GLN A  32     7812   8150   8329      8      3    106       C  
ATOM    237  NE2 GLN A  32      -0.243   5.855  15.584  1.00 63.66           N  
ANISOU  237  NE2 GLN A  32     7780   8131   8277      2    -20     90       N  
ATOM    238  OE1 GLN A  32      -0.149   8.064  15.298  1.00 59.44           O  
ANISOU  238  OE1 GLN A  32     7248   7573   7763      4     13     98       O  
ATOM    239  N   GLN A  33      -4.622   7.596  19.774  1.00 75.27           N  
ANISOU  239  N   GLN A  33     9269   9524   9804     68     94    155       N  
ATOM    240  CA  GLN A  33      -4.958   7.322  21.171  1.00 84.77           C  
ANISOU  240  CA  GLN A  33    10489  10718  11002     80    110    148       C  
ATOM    241  C   GLN A  33      -6.481   7.453  21.352  1.00 89.54           C  
ANISOU  241  C   GLN A  33    11080  11311  11631     96    132    187       C  
ATOM    242  O   GLN A  33      -6.952   7.741  22.444  1.00103.23           O  
ANISOU  242  O   GLN A  33    12828  13029  13367    110    158    188       O  
ATOM    243  CB  GLN A  33      -4.188   8.216  22.176  1.00 89.04           C  
ANISOU  243  CB  GLN A  33    11057  11242  11531     81    131    118       C  
ATOM    244  CG  GLN A  33      -2.831   8.812  21.733  1.00 99.79           C  
ANISOU  244  CG  GLN A  33    12428  12607  12881     66    122     89       C  
ATOM    245  CD  GLN A  33      -1.729   7.819  21.358  1.00105.31           C  
ANISOU  245  CD  GLN A  33    13125  13330  13560     52     87     67       C  
ATOM    246  NE2 GLN A  33      -1.661   6.707  22.073  1.00112.68           N  
ANISOU  246  NE2 GLN A  33    14062  14273  14477     55     75     58       N  
ATOM    247  OE1 GLN A  33      -0.923   8.072  20.455  1.00 93.96           O  
ANISOU  247  OE1 GLN A  33    11682  11900  12119     39     73     58       O  
ATOM    248  N   CYS A  34      -7.241   7.202  20.288  1.00 92.40           N  
ANISOU  248  N   CYS A  34    11416  11682  12008     94    120    219       N  
ATOM    249  CA  CYS A  34      -8.696   7.339  20.296  1.00 93.24           C  
ANISOU  249  CA  CYS A  34    11505  11782  12141    107    138    260       C  
ATOM    250  C   CYS A  34      -9.386   5.974  20.252  1.00 91.14           C  
ANISOU  250  C   CYS A  34    11223  11530  11875    106    117    277       C  
ATOM    251  O   CYS A  34      -9.050   5.142  19.412  1.00 99.44           O  
ANISOU  251  O   CYS A  34    12263  12602  12917     91     85    272       O  
ATOM    252  CB  CYS A  34      -9.123   8.150  19.084  1.00 91.40           C  
ANISOU  252  CB  CYS A  34    11251  11550  11928    104    140    289       C  
ATOM    253  SG  CYS A  34     -10.393   9.353  19.445  1.00 99.18           S  
ANISOU  253  SG  CYS A  34    12230  12510  12944    126    185    328       S  
ATOM    254  N   PRO A  35     -10.352   5.731  21.146  1.00 88.26           N  
ANISOU  254  N   PRO A  35    10858  11156  11521    122    135    295       N  
ATOM    255  CA  PRO A  35     -10.988   4.415  21.211  1.00 85.49           C  
ANISOU  255  CA  PRO A  35    10493  10818  11172    121    117    310       C  
ATOM    256  C   PRO A  35     -12.021   4.194  20.117  1.00 89.55           C  
ANISOU  256  C   PRO A  35    10975  11344  11707    115    105    350       C  
ATOM    257  O   PRO A  35     -12.731   5.122  19.714  1.00 83.91           O  
ANISOU  257  O   PRO A  35    10247  10622  11013    122    122    379       O  
ATOM    258  CB  PRO A  35     -11.669   4.422  22.570  1.00 84.05           C  
ANISOU  258  CB  PRO A  35    10321  10619  10995    141    146    318       C  
ATOM    259  CG  PRO A  35     -12.032   5.840  22.778  1.00 89.51           C  
ANISOU  259  CG  PRO A  35    11018  11290  11702    154    182    330       C  
ATOM    260  CD  PRO A  35     -10.967   6.674  22.090  1.00 93.15           C  
ANISOU  260  CD  PRO A  35    11488  11752  12154    141    176    306       C  
ATOM    261  N   PHE A  36     -12.123   2.941  19.691  1.00 86.71           N  
ANISOU  261  N   PHE A  36    10603  11002  11342    103     75    351       N  
ATOM    262  CA  PHE A  36     -12.807   2.555  18.448  1.00 80.98           C  
ANISOU  262  CA  PHE A  36     9849  10293  10628     89     52    380       C  
ATOM    263  C   PHE A  36     -14.233   3.104  18.118  1.00 82.97           C  
ANISOU  263  C   PHE A  36    10073  10542  10909     98     67    430       C  
ATOM    264  O   PHE A  36     -14.548   3.363  16.948  1.00 74.91           O  
ANISOU  264  O   PHE A  36     9031   9535   9897     87     53    452       O  
ATOM    265  CB  PHE A  36     -12.750   1.041  18.387  1.00 71.21           C  
ANISOU  265  CB  PHE A  36     8608   9069   9380     77     24    370       C  
ATOM    266  CG  PHE A  36     -13.500   0.444  17.252  1.00 73.94           C  
ANISOU  266  CG  PHE A  36     8927   9433   9736     61     -1    396       C  
ATOM    267  CD1 PHE A  36     -13.041   0.570  15.956  1.00 82.49           C  
ANISOU  267  CD1 PHE A  36    10002  10531  10810     43    -23    392       C  
ATOM    268  CD2 PHE A  36     -14.657  -0.272  17.477  1.00 71.43           C  
ANISOU  268  CD2 PHE A  36     8590   9116   9435     63     -2    426       C  
ATOM    269  CE1 PHE A  36     -13.732  -0.019  14.901  1.00 87.04           C  
ANISOU  269  CE1 PHE A  36    10554  11126  11392     26    -48    415       C  
ATOM    270  CE2 PHE A  36     -15.359  -0.838  16.433  1.00 70.98           C  
ANISOU  270  CE2 PHE A  36     8507   9076   9385     45    -27    449       C  
ATOM    271  CZ  PHE A  36     -14.895  -0.723  15.141  1.00 76.43           C  
ANISOU  271  CZ  PHE A  36     9191   9784  10065     26    -51    443       C  
ATOM    272  N   GLU A  37     -15.085   3.286  19.117  1.00 89.96           N  
ANISOU  272  N   GLU A  37    10958  11411  11811    117     95    450       N  
ATOM    273  CA  GLU A  37     -16.479   3.676  18.835  1.00 94.87           C  
ANISOU  273  CA  GLU A  37    11552  12032  12462    126    109    501       C  
ATOM    274  C   GLU A  37     -16.497   5.091  18.270  1.00 89.67           C  
ANISOU  274  C   GLU A  37    10888  11366  11816    132    128    517       C  
ATOM    275  O   GLU A  37     -17.099   5.370  17.241  1.00 86.83           O  
ANISOU  275  O   GLU A  37    10502  11019  11471    125    119    550       O  
ATOM    276  CB  GLU A  37     -17.413   3.534  20.066  1.00 96.12           C  
ANISOU  276  CB  GLU A  37    11710  12173  12637    148    137    521       C  
ATOM    277  CG  GLU A  37     -16.735   3.404  21.431  1.00 96.16           C  
ANISOU  277  CG  GLU A  37    11749  12163  12625    160    155    486       C  
ATOM    278  CD  GLU A  37     -16.027   2.067  21.613  1.00 95.68           C  
ANISOU  278  CD  GLU A  37    11698  12114  12540    147    126    454       C  
ATOM    279  OE1 GLU A  37     -16.639   1.027  21.359  1.00 95.18           O  
ANISOU  279  OE1 GLU A  37    11617  12063  12485    139    107    471       O  
ATOM    280  OE2 GLU A  37     -14.850   2.031  21.990  1.00 97.00           O1-
ANISOU  280  OE2 GLU A  37    11892  12281  12684    143    122    413       O1-
ATOM    281  N   ASP A  38     -15.776   5.963  18.949  1.00 89.69           N  
ANISOU  281  N   ASP A  38    10917  11349  11811    143    153    491       N  
ATOM    282  CA  ASP A  38     -15.641   7.351  18.548  1.00 96.48           C  
ANISOU  282  CA  ASP A  38    11778  12198  12681    149    176    500       C  
ATOM    283  C   ASP A  38     -15.335   7.491  17.058  1.00 85.60           C  
ANISOU  283  C   ASP A  38    10383  10841  11302    130    148    507       C  
ATOM    284  O   ASP A  38     -15.888   8.340  16.372  1.00 82.68           O  
ANISOU  284  O   ASP A  38     9993  10471  10951    135    160    541       O  
ATOM    285  CB  ASP A  38     -14.538   8.007  19.386  1.00105.39           C  
ANISOU  285  CB  ASP A  38    12943  13307  13793    155    196    456       C  
ATOM    286  CG  ASP A  38     -14.793   7.894  20.899  1.00103.67           C  
ANISOU  286  CG  ASP A  38    12747  13070  13574    173    223    447       C  
ATOM    287  OD1 ASP A  38     -15.495   6.957  21.322  1.00102.16           O  
ANISOU  287  OD1 ASP A  38    12546  12884  13387    177    217    462       O  
ATOM    288  OD2 ASP A  38     -14.276   8.730  21.672  1.00108.94           O1-
ANISOU  288  OD2 ASP A  38    13440  13715  14235    182    251    424       O1-
ATOM    289  N   HIS A  39     -14.468   6.632  16.559  1.00 81.71           N  
ANISOU  289  N   HIS A  39     9896  10367  10785    111    113    477       N  
ATOM    290  CA  HIS A  39     -14.113   6.656  15.155  1.00 86.21           C  
ANISOU  290  CA  HIS A  39    10450  10958  11347     92     86    480       C  
ATOM    291  C   HIS A  39     -15.262   6.182  14.290  1.00 80.39           C  
ANISOU  291  C   HIS A  39     9678  10240  10624     84     67    524       C  
ATOM    292  O   HIS A  39     -15.545   6.763  13.252  1.00 81.46           O  
ANISOU  292  O   HIS A  39     9794  10388  10769     79     62    550       O  
ATOM    293  CB  HIS A  39     -12.935   5.743  14.898  1.00 90.77           C  
ANISOU  293  CB  HIS A  39    11043  11549  11895     73     54    437       C  
ATOM    294  CG  HIS A  39     -11.647   6.235  15.473  1.00 93.88           C  
ANISOU  294  CG  HIS A  39    11468  11929  12272     76     65    395       C  
ATOM    295  CD2 HIS A  39     -10.780   5.659  16.338  1.00 95.59           C  
ANISOU  295  CD2 HIS A  39    11709  12141  12469     75     61    355       C  
ATOM    296  ND1 HIS A  39     -11.092   7.442  15.119  1.00100.61           N  
ANISOU  296  ND1 HIS A  39    12326  12773  13127     78     80    390       N  
ATOM    297  CE1 HIS A  39      -9.936   7.588  15.743  1.00106.64           C  
ANISOU  297  CE1 HIS A  39    13118  13528  13874     77     84    348       C  
ATOM    298  NE2 HIS A  39      -9.728   6.524  16.495  1.00100.80           N  
ANISOU  298  NE2 HIS A  39    12390  12791  13120     75     73    328       N  
ATOM    299  N   VAL A  40     -15.903   5.106  14.711  1.00 74.11           N  
ANISOU  299  N   VAL A  40     8875   9450   9831     82     56    531       N  
ATOM    300  CA  VAL A  40     -17.044   4.587  13.970  1.00 79.37           C  
ANISOU  300  CA  VAL A  40     9508  10136  10512     73     38    572       C  
ATOM    301  C   VAL A  40     -18.092   5.703  13.814  1.00 75.54           C  
ANISOU  301  C   VAL A  40     8999   9644  10056     89     65    623       C  
ATOM    302  O   VAL A  40     -18.656   5.905  12.721  1.00 76.31           O  
ANISOU  302  O   VAL A  40     9069   9762  10163     80     50    657       O  
ATOM    303  CB  VAL A  40     -17.650   3.333  14.661  1.00 80.79           C  
ANISOU  303  CB  VAL A  40     9685  10317  10695     72     28    575       C  
ATOM    304  CG1 VAL A  40     -19.028   2.994  14.096  1.00 81.22           C  
ANISOU  304  CG1 VAL A  40     9703  10387  10771     66     17    625       C  
ATOM    305  CG2 VAL A  40     -16.733   2.133  14.504  1.00 80.18           C  
ANISOU  305  CG2 VAL A  40     9623  10251  10590     52     -3    533       C  
ATOM    306  N   LYS A  41     -18.317   6.441  14.897  1.00 69.15           N  
ANISOU  306  N   LYS A  41     8204   8809   9263    114    105    627       N  
ATOM    307  CA  LYS A  41     -19.293   7.514  14.891  1.00 78.60           C  
ANISOU  307  CA  LYS A  41     9380   9994  10489    133    137    674       C  
ATOM    308  C   LYS A  41     -18.914   8.595  13.858  1.00 83.93           C  
ANISOU  308  C   LYS A  41    10048  10675  11167    129    139    684       C  
ATOM    309  O   LYS A  41     -19.702   8.924  12.956  1.00 88.49           O  
ANISOU  309  O   LYS A  41    10594  11268  11761    127    134    728       O  
ATOM    310  CB  LYS A  41     -19.417   8.115  16.286  1.00 87.68           C  
ANISOU  310  CB  LYS A  41    10553  11112  11651    159    182    668       C  
ATOM    311  CG  LYS A  41     -20.541   9.140  16.450  1.00100.54           C  
ANISOU  311  CG  LYS A  41    12162  12725  13314    182    221    719       C  
ATOM    312  CD  LYS A  41     -20.403   9.910  17.756  1.00117.78           C  
ANISOU  312  CD  LYS A  41    14375  14873  15503    207    268    704       C  
ATOM    313  CE  LYS A  41     -19.327  10.993  17.675  1.00131.67           C  
ANISOU  313  CE  LYS A  41    16160  16616  17252    208    284    673       C  
ATOM    314  NZ  LYS A  41     -19.717  12.137  16.799  1.00132.99           N1+
ANISOU  314  NZ  LYS A  41    16307  16782  17443    214    301    711       N1+
ATOM    315  N   LEU A  42     -17.694   9.108  13.973  1.00 73.61           N  
ANISOU  315  N   LEU A  42     8770   9357   9843    128    145    642       N  
ATOM    316  CA  LEU A  42     -17.208  10.109  13.070  1.00 69.87           C  
ANISOU  316  CA  LEU A  42     8292   8885   9369    125    149    646       C  
ATOM    317  C   LEU A  42     -17.305   9.628  11.652  1.00 74.67           C  
ANISOU  317  C   LEU A  42     8874   9527   9969    103    109    663       C  
ATOM    318  O   LEU A  42     -17.907  10.291  10.814  1.00 93.48           O  
ANISOU  318  O   LEU A  42    11230  11920  12367    105    113    705       O  
ATOM    319  CB  LEU A  42     -15.768  10.456  13.389  1.00 74.98           C  
ANISOU  319  CB  LEU A  42     8975   9519   9995    122    153    593       C  
ATOM    320  CG  LEU A  42     -15.552  11.267  14.681  1.00 79.05           C  
ANISOU  320  CG  LEU A  42     9518   9998  10518    142    196    576       C  
ATOM    321  CD1 LEU A  42     -14.058  11.340  14.949  1.00 75.17           C  
ANISOU  321  CD1 LEU A  42     9059   9500  10000    133    190    520       C  
ATOM    322  CD2 LEU A  42     -16.177  12.667  14.632  1.00 79.90           C  
ANISOU  322  CD2 LEU A  42     9616  10086  10656    162    237    612       C  
ATOM    323  N   VAL A  43     -16.749   8.461  11.376  1.00 76.85           N  
ANISOU  323  N   VAL A  43     9158   9822  10219     82     72    632       N  
ATOM    324  CA  VAL A  43     -16.943   7.838  10.054  1.00 87.10           C  
ANISOU  324  CA  VAL A  43    10433  11155  11508     59     33    647       C  
ATOM    325  C   VAL A  43     -18.401   7.916   9.543  1.00 90.19           C  
ANISOU  325  C   VAL A  43    10784  11560  11922     61     31    708       C  
ATOM    326  O   VAL A  43     -18.637   8.338   8.406  1.00 93.21           O  
ANISOU  326  O   VAL A  43    11143  11964  12307     53     19    736       O  
ATOM    327  CB  VAL A  43     -16.508   6.350  10.040  1.00 88.20           C  
ANISOU  327  CB  VAL A  43    10582  11308  11621     39     -3    613       C  
ATOM    328  CG1 VAL A  43     -16.781   5.715   8.661  1.00 89.50           C  
ANISOU  328  CG1 VAL A  43    10723  11507  11774     14    -42    629       C  
ATOM    329  CG2 VAL A  43     -15.037   6.205  10.436  1.00 85.11           C  
ANISOU  329  CG2 VAL A  43    10227  10906  11206     36     -5    556       C  
ATOM    330  N   ASN A  44     -19.364   7.505  10.370  1.00 84.48           N  
ANISOU  330  N   ASN A  44    10053  10829  11218     72     43    729       N  
ATOM    331  CA  ASN A  44     -20.765   7.537   9.963  1.00 86.17           C  
ANISOU  331  CA  ASN A  44    10226  11057  11456     73     41    787       C  
ATOM    332  C   ASN A  44     -21.225   8.914   9.550  1.00 85.43           C  
ANISOU  332  C   ASN A  44    10114  10960  11386     90     69    830       C  
ATOM    333  O   ASN A  44     -21.765   9.085   8.458  1.00 93.60           O  
ANISOU  333  O   ASN A  44    11118  12021  12426     80     52    868       O  
ATOM    334  CB  ASN A  44     -21.643   7.047  11.089  1.00 91.07           C  
ANISOU  334  CB  ASN A  44    10844  11663  12095     87     58    802       C  
ATOM    335  CG  ASN A  44     -21.397   5.605  11.390  1.00 93.50           C  
ANISOU  335  CG  ASN A  44    11163  11978  12383     70     29    770       C  
ATOM    336  ND2 ASN A  44     -21.403   5.252  12.659  1.00 94.69           N  
ANISOU  336  ND2 ASN A  44    11334  12107  12539     84     48    752       N  
ATOM    337  OD1 ASN A  44     -21.182   4.812  10.479  1.00101.22           O  
ANISOU  337  OD1 ASN A  44    12134  12982  13343     44    -11    760       O  
ATOM    338  N   GLU A  45     -20.991   9.891  10.421  1.00 80.60           N  
ANISOU  338  N   GLU A  45     9522  10315  10788    115    112    824       N  
ATOM    339  CA  GLU A  45     -21.313  11.291  10.140  1.00 77.75           C  
ANISOU  339  CA  GLU A  45     9148   9943  10451    134    146    861       C  
ATOM    340  C   GLU A  45     -20.745  11.732   8.784  1.00 70.14           C  
ANISOU  340  C   GLU A  45     8174   9001   9474    119    125    863       C  
ATOM    341  O   GLU A  45     -21.378  12.454   8.014  1.00 56.86           O  
ANISOU  341  O   GLU A  45     6463   7332   7811    124    131    912       O  
ATOM    342  CB  GLU A  45     -20.742  12.173  11.252  1.00 82.68           C  
ANISOU  342  CB  GLU A  45     9806  10527  11083    156    191    834       C  
ATOM    343  CG  GLU A  45     -21.211  11.788  12.650  1.00 89.18           C  
ANISOU  343  CG  GLU A  45    10644  11327  11915    172    214    827       C  
ATOM    344  CD  GLU A  45     -20.738  12.744  13.732  1.00 95.79           C  
ANISOU  344  CD  GLU A  45    11514  12124  12758    195    261    804       C  
ATOM    345  OE1 GLU A  45     -19.685  13.393  13.536  1.00104.84           O  
ANISOU  345  OE1 GLU A  45    12681  13261  13892    191    266    772       O  
ATOM    346  OE2 GLU A  45     -21.408  12.841  14.795  1.00 92.11           O1-
ANISOU  346  OE2 GLU A  45    11053  11636  12310    215    293    816       O1-
ATOM    347  N   VAL A  46     -19.535  11.263   8.515  1.00 70.96           N  
ANISOU  347  N   VAL A  46     8303   9112   9547    101    100    812       N  
ATOM    348  CA  VAL A  46     -18.845  11.545   7.284  1.00 73.22           C  
ANISOU  348  CA  VAL A  46     8585   9419   9816     85     78    807       C  
ATOM    349  C   VAL A  46     -19.493  10.813   6.128  1.00 77.35           C  
ANISOU  349  C   VAL A  46     9075   9983  10330     63     37    836       C  
ATOM    350  O   VAL A  46     -19.554  11.325   5.006  1.00 84.87           O  
ANISOU  350  O   VAL A  46    10007  10957  11282     57     28    863       O  
ATOM    351  CB  VAL A  46     -17.361  11.147   7.399  1.00 72.45           C  
ANISOU  351  CB  VAL A  46     8524   9317   9687     72     64    742       C  
ATOM    352  CG1 VAL A  46     -16.781  10.709   6.050  1.00 77.34           C  
ANISOU  352  CG1 VAL A  46     9135   9969  10279     47     24    732       C  
ATOM    353  CG2 VAL A  46     -16.569  12.298   7.991  1.00 70.65           C  
ANISOU  353  CG2 VAL A  46     8321   9056   9466     90    102    721       C  
ATOM    354  N   THR A  47     -19.969   9.607   6.392  1.00 78.67           N  
ANISOU  354  N   THR A  47     9237  10161  10491     51     13    832       N  
ATOM    355  CA  THR A  47     -20.530   8.797   5.339  1.00 78.57           C  
ANISOU  355  CA  THR A  47     9198  10188  10468     26    -28    854       C  
ATOM    356  C   THR A  47     -21.945   9.199   4.984  1.00 83.90           C  
ANISOU  356  C   THR A  47     9830  10877  11171     33    -23    922       C  
ATOM    357  O   THR A  47     -22.289   9.236   3.808  1.00 82.95           O  
ANISOU  357  O   THR A  47     9683  10790  11044     17    -47    951       O  
ATOM    358  CB  THR A  47     -20.491   7.349   5.721  1.00 75.82           C  
ANISOU  358  CB  THR A  47     8860   9844  10102      8    -56    823       C  
ATOM    359  CG2 THR A  47     -20.881   6.504   4.532  1.00 82.18           C  
ANISOU  359  CG2 THR A  47     9644  10690  10892    -22   -101    836       C  
ATOM    360  OG1 THR A  47     -19.154   7.045   6.115  1.00 75.52           O  
ANISOU  360  OG1 THR A  47     8861   9791  10040      5    -58    762       O  
ATOM    361  N   GLU A  48     -22.759   9.511   5.986  1.00 95.24           N  
ANISOU  361  N   GLU A  48    11259  12290  12637     56     11    948       N  
ATOM    362  CA  GLU A  48     -24.090  10.045   5.719  1.00110.79           C  
ANISOU  362  CA  GLU A  48    13187  14271  14638     67     23   1017       C  
ATOM    363  C   GLU A  48     -23.952  11.314   4.922  1.00106.92           C  
ANISOU  363  C   GLU A  48    12684  13785  14156     77     39   1045       C  
ATOM    364  O   GLU A  48     -24.577  11.477   3.872  1.00107.31           O  
ANISOU  364  O   GLU A  48    12697  13866  14208     68     20   1091       O  
ATOM    365  CB  GLU A  48     -24.872  10.382   6.999  1.00125.85           C  
ANISOU  365  CB  GLU A  48    15093  16145  16578     96     65   1039       C  
ATOM    366  CG  GLU A  48     -26.316  10.835   6.706  1.00136.30           C  
ANISOU  366  CG  GLU A  48    16370  17482  17935    108     77   1115       C  
ATOM    367  CD  GLU A  48     -26.789  12.020   7.540  1.00136.58           C  
ANISOU  367  CD  GLU A  48    16405  17483  18007    145    135   1146       C  
ATOM    368  OE1 GLU A  48     -27.009  11.842   8.766  1.00132.85           O  
ANISOU  368  OE1 GLU A  48    15949  16981  17547    162    162   1134       O  
ATOM    369  OE2 GLU A  48     -26.968  13.113   6.952  1.00124.36           O1-
ANISOU  369  OE2 GLU A  48    14839  15937  16475    157    154   1183       O1-
ATOM    370  N   PHE A  49     -23.156  12.226   5.466  1.00 99.39           N  
ANISOU  370  N   PHE A  49    11759  12798  13207     97     75   1020       N  
ATOM    371  CA  PHE A  49     -22.930  13.495   4.834  1.00 91.55           C  
ANISOU  371  CA  PHE A  49    10758  11803  12224    109     97   1043       C  
ATOM    372  C   PHE A  49     -22.532  13.282   3.373  1.00 87.18           C  
ANISOU  372  C   PHE A  49    10191  11290  11644     83     55   1045       C  
ATOM    373  O   PHE A  49     -23.098  13.907   2.489  1.00103.84           O  
ANISOU  373  O   PHE A  49    12268  13421  13766     86     55   1096       O  
ATOM    374  CB  PHE A  49     -21.859  14.265   5.585  1.00 88.89           C  
ANISOU  374  CB  PHE A  49    10461  11427  11887    125    132   1000       C  
ATOM    375  CG  PHE A  49     -21.506  15.576   4.962  1.00 88.86           C  
ANISOU  375  CG  PHE A  49    10453  11417  11894    137    156   1018       C  
ATOM    376  CD1 PHE A  49     -21.916  16.744   5.544  1.00 95.09           C  
ANISOU  376  CD1 PHE A  49    11240  12174  12717    166    207   1047       C  
ATOM    377  CD2 PHE A  49     -20.738  15.642   3.812  1.00 90.58           C  
ANISOU  377  CD2 PHE A  49    10669  11659  12088    119    129   1007       C  
ATOM    378  CE1 PHE A  49     -21.586  17.972   4.988  1.00101.43           C  
ANISOU  378  CE1 PHE A  49    12039  12968  13533    177    232   1064       C  
ATOM    379  CE2 PHE A  49     -20.411  16.857   3.245  1.00 96.15           C  
ANISOU  379  CE2 PHE A  49    11370  12358  12805    130    152   1025       C  
ATOM    380  CZ  PHE A  49     -20.844  18.029   3.830  1.00 99.78           C  
ANISOU  380  CZ  PHE A  49    11827  12785  13302    159    204   1055       C  
ATOM    381  N   ALA A  50     -21.595  12.387   3.100  1.00 73.07           N  
ANISOU  381  N   ALA A  50     8427   9515   9822     59     21    993       N  
ATOM    382  CA  ALA A  50     -21.160  12.178   1.723  1.00 75.29           C  
ANISOU  382  CA  ALA A  50     8699   9832  10075     35    -16    991       C  
ATOM    383  C   ALA A  50     -22.293  11.863   0.763  1.00 82.50           C  
ANISOU  383  C   ALA A  50     9568  10786  10991     21    -45   1046       C  
ATOM    384  O   ALA A  50     -22.288  12.314  -0.379  1.00 83.54           O  
ANISOU  384  O   ALA A  50     9681  10946  11115     13    -58   1072       O  
ATOM    385  CB  ALA A  50     -20.162  11.061   1.662  1.00 75.72           C  
ANISOU  385  CB  ALA A  50     8784   9894  10093     11    -49    929       C  
ATOM    386  N   LYS A  51     -23.244  11.057   1.237  1.00100.73           N  
ANISOU  386  N   LYS A  51    11862  13100  13310     16    -56   1062       N  
ATOM    387  CA  LYS A  51     -24.360  10.533   0.411  1.00106.52           C  
ANISOU  387  CA  LYS A  51    12554  13875  14044     -3    -89   1110       C  
ATOM    388  C   LYS A  51     -25.335  11.637  -0.096  1.00117.29           C  
ANISOU  388  C   LYS A  51    13875  15252  15437     14    -70   1185       C  
ATOM    389  O   LYS A  51     -25.873  11.579  -1.217  1.00104.61           O  
ANISOU  389  O   LYS A  51    12236  13687  13823     -3    -99   1224       O  
ATOM    390  CB  LYS A  51     -25.137   9.463   1.198  1.00 97.08           C  
ANISOU  390  CB  LYS A  51    11354  12676  12857    -10   -100   1110       C  
ATOM    391  CG  LYS A  51     -24.372   8.189   1.504  1.00 95.05           C  
ANISOU  391  CG  LYS A  51    11130  12415  12571    -32   -127   1046       C  
ATOM    392  CD  LYS A  51     -25.265   7.164   2.195  1.00 97.66           C  
ANISOU  392  CD  LYS A  51    11449  12743  12912    -39   -137   1054       C  
ATOM    393  CE  LYS A  51     -24.531   6.369   3.273  1.00 98.68           C  
ANISOU  393  CE  LYS A  51    11619  12843  13032    -37   -131    994       C  
ATOM    394  NZ  LYS A  51     -25.382   5.988   4.441  1.00 94.54           N1+
ANISOU  394  NZ  LYS A  51    11088  12298  12534    -23   -112   1010       N1+
ATOM    395  N   THR A  52     -25.544  12.641   0.743  1.00121.41           N  
ANISOU  395  N   THR A  52    14399  15738  15993     48    -20   1204       N  
ATOM    396  CA  THR A  52     -26.290  13.832   0.361  1.00123.02           C  
ANISOU  396  CA  THR A  52    14568  15946  16228     69      8   1271       C  
ATOM    397  C   THR A  52     -25.638  14.492  -0.882  1.00118.58           C  
ANISOU  397  C   THR A  52    14001  15407  15647     62     -3   1276       C  
ATOM    398  O   THR A  52     -26.329  14.901  -1.825  1.00121.70           O  
ANISOU  398  O   THR A  52    14356  15834  16048     59    -13   1334       O  
ATOM    399  CB  THR A  52     -26.404  14.826   1.559  1.00123.70           C  
ANISOU  399  CB  THR A  52    14668  15982  16351    108     70   1279       C  
ATOM    400  CG2 THR A  52     -26.520  14.076   2.907  1.00119.39           C  
ANISOU  400  CG2 THR A  52    14145  15407  15810    113     80   1246       C  
ATOM    401  OG1 THR A  52     -25.275  15.708   1.607  1.00119.39           O  
ANISOU  401  OG1 THR A  52    14152  15410  15799    120     96   1245       O  
ATOM    402  N   CYS A  53     -24.303  14.547  -0.888  1.00111.03           N  
ANISOU  402  N   CYS A  53    13084  14436  14667     57     -3   1217       N  
ATOM    403  CA  CYS A  53     -23.541  15.147  -1.989  1.00107.04           C  
ANISOU  403  CA  CYS A  53    12579  13948  14143     51    -11   1216       C  
ATOM    404  C   CYS A  53     -23.600  14.343  -3.271  1.00 97.12           C  
ANISOU  404  C   CYS A  53    11305  12744  12851     17    -66   1220       C  
ATOM    405  O   CYS A  53     -23.364  14.889  -4.359  1.00 96.40           O  
ANISOU  405  O   CYS A  53    11201  12679  12749     13    -75   1241       O  
ATOM    406  CB  CYS A  53     -22.091  15.343  -1.576  1.00110.18           C  
ANISOU  406  CB  CYS A  53    13024  14314  14524     54      3   1150       C  
ATOM    407  SG  CYS A  53     -21.930  16.394  -0.122  1.00122.21           S  
ANISOU  407  SG  CYS A  53    14571  15776  16086     92     68   1141       S  
ATOM    408  N   VAL A  54     -23.904  13.054  -3.128  1.00 91.23           N  
ANISOU  408  N   VAL A  54    10562  12014  12089     -7   -101   1200       N  
ATOM    409  CA  VAL A  54     -24.204  12.186  -4.253  1.00 94.92           C  
ANISOU  409  CA  VAL A  54    11010  12530  12525    -41   -153   1209       C  
ATOM    410  C   VAL A  54     -25.528  12.580  -4.866  1.00 99.02           C  
ANISOU  410  C   VAL A  54    11477  13083  13065    -39   -159   1287       C  
ATOM    411  O   VAL A  54     -25.656  12.653  -6.091  1.00 96.84           O  
ANISOU  411  O   VAL A  54    11177  12848  12768    -57   -187   1313       O  
ATOM    412  CB  VAL A  54     -24.346  10.719  -3.821  1.00100.07           C  
ANISOU  412  CB  VAL A  54    11675  13186  13161    -65   -185   1172       C  
ATOM    413  CG1 VAL A  54     -24.611   9.834  -5.036  1.00105.05           C  
ANISOU  413  CG1 VAL A  54    12288  13867  13758   -103   -239   1178       C  
ATOM    414  CG2 VAL A  54     -23.114  10.254  -3.051  1.00104.39           C  
ANISOU  414  CG2 VAL A  54    12273  13699  13692    -64   -177   1098       C  
ATOM    415  N   ALA A  55     -26.511  12.811  -3.993  1.00108.36           N  
ANISOU  415  N   ALA A  55    12640  14246  14286    -19   -132   1324       N  
ATOM    416  CA  ALA A  55     -27.855  13.234  -4.389  1.00114.25           C  
ANISOU  416  CA  ALA A  55    13333  15018  15058    -13   -131   1404       C  
ATOM    417  C   ALA A  55     -27.868  14.610  -5.072  1.00120.14           C  
ANISOU  417  C   ALA A  55    14057  15771  15818      9   -106   1453       C  
ATOM    418  O   ALA A  55     -28.150  14.680  -6.275  1.00123.69           O  
ANISOU  418  O   ALA A  55    14478  16267  16252     -8   -135   1488       O  
ATOM    419  CB  ALA A  55     -28.782  13.218  -3.181  1.00120.11           C  
ANISOU  419  CB  ALA A  55    14065  15732  15840      9   -101   1429       C  
ATOM    420  N   ASP A  56     -27.578  15.683  -4.316  1.00117.87           N  
ANISOU  420  N   ASP A  56    13785  15440  15562     44    -51   1455       N  
ATOM    421  CA  ASP A  56     -27.399  17.036  -4.886  1.00119.76           C  
ANISOU  421  CA  ASP A  56    14010  15677  15817     66    -21   1492       C  
ATOM    422  C   ASP A  56     -25.942  17.471  -4.761  1.00107.83           C  
ANISOU  422  C   ASP A  56    12544  14135  14290     72     -3   1432       C  
ATOM    423  O   ASP A  56     -25.399  17.555  -3.663  1.00100.53           O  
ANISOU  423  O   ASP A  56    11656  13165  13375     87     26   1388       O  
ATOM    424  CB  ASP A  56     -28.318  18.073  -4.199  1.00134.79           C  
ANISOU  424  CB  ASP A  56    15889  17553  17773    104     32   1552       C  
ATOM    425  CG  ASP A  56     -28.609  19.320  -5.079  1.00138.29           C  
ANISOU  425  CG  ASP A  56    16297  18011  18234    122     53   1617       C  
ATOM    426  OD1 ASP A  56     -29.779  19.798  -5.106  1.00125.79           O  
ANISOU  426  OD1 ASP A  56    14671  16438  16685    139     70   1690       O  
ATOM    427  OD2 ASP A  56     -27.673  19.823  -5.735  1.00142.88           O1-
ANISOU  427  OD2 ASP A  56    16894  18596  18798    120     53   1597       O1-
ATOM    428  N   GLU A  57     -25.329  17.771  -5.900  1.00104.13           N  
ANISOU  428  N   GLU A  57    12074  13694  13797     61    -22   1432       N  
ATOM    429  CA  GLU A  57     -23.944  18.252  -5.955  1.00113.13           C  
ANISOU  429  CA  GLU A  57    13251  14810  14922     65     -6   1382       C  
ATOM    430  C   GLU A  57     -23.781  19.604  -5.266  1.00108.76           C  
ANISOU  430  C   GLU A  57    12705  14209  14408    102     55   1396       C  
ATOM    431  O   GLU A  57     -22.693  19.964  -4.825  1.00 97.51           O  
ANISOU  431  O   GLU A  57    11319  12750  12981    109     77   1347       O  
ATOM    432  CB  GLU A  57     -23.513  18.424  -7.417  1.00127.17           C  
ANISOU  432  CB  GLU A  57    15017  16631  16669     49    -35   1395       C  
ATOM    433  CG  GLU A  57     -23.563  17.158  -8.258  1.00138.08           C  
ANISOU  433  CG  GLU A  57    16394  18062  18008     10    -96   1378       C  
ATOM    434  CD  GLU A  57     -22.370  16.262  -8.022  1.00142.93           C  
ANISOU  434  CD  GLU A  57    17057  18664  18588    -10   -116   1296       C  
ATOM    435  OE1 GLU A  57     -21.267  16.640  -8.469  1.00141.00           O  
ANISOU  435  OE1 GLU A  57    16834  18414  18324    -10   -112   1266       O  
ATOM    436  OE2 GLU A  57     -22.538  15.185  -7.405  1.00147.39           O1-
ANISOU  436  OE2 GLU A  57    17634  19223  19143    -25   -135   1264       O1-
ATOM    437  N   SER A  58     -24.878  20.355  -5.212  1.00113.34           N  
ANISOU  437  N   SER A  58    13249  14789  15027    125     83   1466       N  
ATOM    438  CA  SER A  58     -24.867  21.761  -4.826  1.00111.44           C  
ANISOU  438  CA  SER A  58    13007  14509  14826    160    142   1494       C  
ATOM    439  C   SER A  58     -25.164  21.987  -3.350  1.00104.29           C  
ANISOU  439  C   SER A  58    12121  13552  13955    185    188   1482       C  
ATOM    440  O   SER A  58     -24.946  23.088  -2.844  1.00101.90           O  
ANISOU  440  O   SER A  58    11830  13207  13682    212    240   1487       O  
ATOM    441  CB  SER A  58     -25.899  22.535  -5.662  1.00111.49           C  
ANISOU  441  CB  SER A  58    12959  14544  14856    174    152   1582       C  
ATOM    442  OG  SER A  58     -25.830  22.190  -7.040  1.00104.99           O  
ANISOU  442  OG  SER A  58    12114  13778  13999    149    104   1599       O  
ATOM    443  N   ALA A  59     -25.661  20.966  -2.652  1.00 96.52           N  
ANISOU  443  N   ALA A  59    11140  12568  12966    175    169   1466       N  
ATOM    444  CA  ALA A  59     -26.093  21.160  -1.268  1.00 95.98           C  
ANISOU  444  CA  ALA A  59    11086  12454  12930    199    212   1462       C  
ATOM    445  C   ALA A  59     -24.912  21.520  -0.357  1.00 96.37           C  
ANISOU  445  C   ALA A  59    11188  12453  12976    208    244   1395       C  
ATOM    446  O   ALA A  59     -23.742  21.373  -0.742  1.00105.98           O  
ANISOU  446  O   ALA A  59    12433  13673  14163    192    224   1344       O  
ATOM    447  CB  ALA A  59     -26.852  19.953  -0.751  1.00 94.87           C  
ANISOU  447  CB  ALA A  59    10936  12326  12783    185    185   1460       C  
ATOM    448  N   GLU A  60     -25.228  21.977   0.850  1.00 87.91           N  
ANISOU  448  N   GLU A  60    10131  11336  11936    234    291   1394       N  
ATOM    449  CA  GLU A  60     -24.359  22.910   1.576  1.00 89.40           C  
ANISOU  449  CA  GLU A  60    10359  11473  12137    253    338   1357       C  
ATOM    450  C   GLU A  60     -22.875  22.775   1.224  1.00 83.57           C  
ANISOU  450  C   GLU A  60     9656  10735  11363    233    317   1292       C  
ATOM    451  O   GLU A  60     -22.350  23.538   0.412  1.00 80.30           O  
ANISOU  451  O   GLU A  60     9236  10326  10949    234    323   1302       O  
ATOM    452  CB  GLU A  60     -24.581  22.840   3.087  1.00 93.40           C  
ANISOU  452  CB  GLU A  60    10893  11936  12661    270    374   1333       C  
ATOM    453  CG  GLU A  60     -24.047  24.078   3.833  1.00 99.21           C  
ANISOU  453  CG  GLU A  60    11659  12616  13421    295    434   1315       C  
ATOM    454  CD  GLU A  60     -24.903  25.352   3.677  1.00 93.04           C  
ANISOU  454  CD  GLU A  60    10849  11817  12686    326    486   1385       C  
ATOM    455  OE1 GLU A  60     -24.359  26.486   3.724  1.00 93.94           O  
ANISOU  455  OE1 GLU A  60    10979  11898  12817    342    527   1380       O  
ATOM    456  OE2 GLU A  60     -26.126  25.238   3.536  1.00 79.55           O1-
ANISOU  456  OE2 GLU A  60     9100  10126  10998    337    488   1447       O1-
ATOM    457  N   ASN A  61     -22.203  21.783   1.786  1.00 79.65           N  
ANISOU  457  N   ASN A  61     9192  10235  10837    214    291   1229       N  
ATOM    458  CA  ASN A  61     -20.742  21.790   1.785  1.00 72.33           C  
ANISOU  458  CA  ASN A  61     8304   9296   9883    201    283   1163       C  
ATOM    459  C   ASN A  61     -20.058  20.759   0.930  1.00 70.89           C  
ANISOU  459  C   ASN A  61     8125   9153   9657    169    226   1131       C  
ATOM    460  O   ASN A  61     -18.873  20.516   1.070  1.00 74.82           O  
ANISOU  460  O   ASN A  61     8657   9642  10131    157    215   1072       O  
ATOM    461  CB  ASN A  61     -20.316  21.673   3.210  1.00 66.47           C  
ANISOU  461  CB  ASN A  61     7602   8510   9143    209    308   1112       C  
ATOM    462  CG  ASN A  61     -20.882  22.783   4.007  1.00 62.95           C  
ANISOU  462  CG  ASN A  61     7157   8021   8738    241    368   1140       C  
ATOM    463  ND2 ASN A  61     -21.732  22.455   4.961  1.00 60.37           N  
ANISOU  463  ND2 ASN A  61     6829   7681   8428    253    384   1152       N  
ATOM    464  OD1 ASN A  61     -20.614  23.943   3.708  1.00 57.00           O  
ANISOU  464  OD1 ASN A  61     6403   7250   8004    254    401   1156       O  
ATOM    465  N   CYS A  62     -20.802  20.219  -0.009  1.00 72.93           N  
ANISOU  465  N   CYS A  62     8347   9456   9906    156    190   1171       N  
ATOM    466  CA  CYS A  62     -20.322  19.170  -0.877  1.00 91.35           C  
ANISOU  466  CA  CYS A  62    10681  11830  12198    124    135   1145       C  
ATOM    467  C   CYS A  62     -19.085  19.518  -1.714  1.00 98.58           C  
ANISOU  467  C   CYS A  62    11613  12754  13090    114    125   1116       C  
ATOM    468  O   CYS A  62     -18.253  18.650  -2.061  1.00 94.40           O  
ANISOU  468  O   CYS A  62    11103  12242  12524     90     88   1069       O  
ATOM    469  CB  CYS A  62     -21.477  18.783  -1.767  1.00 98.89           C  
ANISOU  469  CB  CYS A  62    11591  12831  13153    114    106   1204       C  
ATOM    470  SG  CYS A  62     -22.773  18.129  -0.734  1.00113.25           S  
ANISOU  470  SG  CYS A  62    13394  14641  14994    122    111   1227       S  
ATOM    471  N   ASP A  63     -18.973  20.798  -2.024  1.00102.80           N  
ANISOU  471  N   ASP A  63    12138  13274  13647    133    160   1145       N  
ATOM    472  CA  ASP A  63     -17.859  21.299  -2.811  1.00118.85           C  
ANISOU  472  CA  ASP A  63    14184  15311  15664    127    157   1125       C  
ATOM    473  C   ASP A  63     -16.529  21.264  -2.040  1.00123.65           C  
ANISOU  473  C   ASP A  63    14839  15884  16260    124    167   1053       C  
ATOM    474  O   ASP A  63     -15.462  21.106  -2.657  1.00117.80           O  
ANISOU  474  O   ASP A  63    14112  15154  15491    108    147   1020       O  
ATOM    475  CB  ASP A  63     -18.161  22.710  -3.328  1.00129.14           C  
ANISOU  475  CB  ASP A  63    15462  16606  16998    149    194   1180       C  
ATOM    476  CG  ASP A  63     -18.512  23.686  -2.213  1.00140.21           C  
ANISOU  476  CG  ASP A  63    16872  17957  18443    179    252   1192       C  
ATOM    477  OD1 ASP A  63     -18.888  23.233  -1.105  1.00142.31           O  
ANISOU  477  OD1 ASP A  63    17152  18201  18717    184    261   1174       O  
ATOM    478  OD2 ASP A  63     -18.417  24.909  -2.456  1.00149.03           O1-
ANISOU  478  OD2 ASP A  63    17982  19056  19587    198    290   1220       O1-
ATOM    479  N   LYS A  64     -16.609  21.384  -0.704  1.00123.23           N  
ANISOU  479  N   LYS A  64    14807  15789  16225    137    198   1031       N  
ATOM    480  CA  LYS A  64     -15.426  21.496   0.189  1.00110.54           C  
ANISOU  480  CA  LYS A  64    13244  14145  14612    137    214    967       C  
ATOM    481  C   LYS A  64     -14.345  20.453  -0.062  1.00 94.01           C  
ANISOU  481  C   LYS A  64    11174  12070  12477    111    172    910       C  
ATOM    482  O   LYS A  64     -14.631  19.378  -0.578  1.00 95.74           O  
ANISOU  482  O   LYS A  64    11382  12325  12672     93    130    911       O  
ATOM    483  CB  LYS A  64     -15.831  21.473   1.682  1.00106.60           C  
ANISOU  483  CB  LYS A  64    12763  13607  14131    152    244    952       C  
ATOM    484  CG  LYS A  64     -16.424  22.785   2.155  1.00112.34           C  
ANISOU  484  CG  LYS A  64    13484  14299  14902    181    300    989       C  
ATOM    485  CD  LYS A  64     -16.468  22.995   3.660  1.00120.01           C  
ANISOU  485  CD  LYS A  64    14484  15224  15890    196    337    962       C  
ATOM    486  CE  LYS A  64     -17.221  24.307   3.934  1.00137.38           C  
ANISOU  486  CE  LYS A  64    16672  17393  18134    225    393   1010       C  
ATOM    487  NZ  LYS A  64     -17.470  24.680   5.356  1.00141.01           N1+
ANISOU  487  NZ  LYS A  64    17157  17806  18615    244    437    994       N1+
ATOM    488  N   SER A  65     -13.111  20.787   0.319  1.00 85.84           N  
ANISOU  488  N   SER A  65    10172  11010  11435    109    184    861       N  
ATOM    489  CA  SER A  65     -11.981  19.871   0.171  1.00 84.92           C  
ANISOU  489  CA  SER A  65    10079  10907  11281     87    149    805       C  
ATOM    490  C   SER A  65     -12.043  18.740   1.177  1.00 81.42           C  
ANISOU  490  C   SER A  65     9654  10457  10823     80    134    768       C  
ATOM    491  O   SER A  65     -12.521  18.894   2.299  1.00 72.78           O  
ANISOU  491  O   SER A  65     8569   9335   9749     94    160    767       O  
ATOM    492  CB  SER A  65     -10.632  20.579   0.330  1.00 84.02           C  
ANISOU  492  CB  SER A  65     9992  10767  11165     87    167    765       C  
ATOM    493  OG  SER A  65     -10.219  20.599   1.681  1.00 73.86           O  
ANISOU  493  OG  SER A  65     8736   9443   9883     93    188    724       O  
ATOM    494  N   LEU A  66     -11.497  17.615   0.758  1.00 78.55           N  
ANISOU  494  N   LEU A  66     9299  10120  10426     58     93    737       N  
ATOM    495  CA  LEU A  66     -11.575  16.385   1.510  1.00 84.51           C  
ANISOU  495  CA  LEU A  66    10069  10877  11165     49     72    706       C  
ATOM    496  C   LEU A  66     -10.862  16.610   2.844  1.00 85.96           C  
ANISOU  496  C   LEU A  66    10286  11021  11355     57     98    662       C  
ATOM    497  O   LEU A  66     -11.395  16.282   3.911  1.00 76.12           O  
ANISOU  497  O   LEU A  66     9047   9758  10117     65    109    657       O  
ATOM    498  CB  LEU A  66     -10.939  15.274   0.675  1.00 99.23           C  
ANISOU  498  CB  LEU A  66    11938  12775  12993     24     27    679       C  
ATOM    499  CG  LEU A  66     -11.434  15.288  -0.804  1.00116.13           C  
ANISOU  499  CG  LEU A  66    14046  14954  15123     14      4    721       C  
ATOM    500  CD1 LEU A  66     -10.625  14.411  -1.755  1.00118.52           C  
ANISOU  500  CD1 LEU A  66    14357  15287  15389     -9    -35    692       C  
ATOM    501  CD2 LEU A  66     -12.903  14.920  -0.863  1.00123.37           C  
ANISOU  501  CD2 LEU A  66    14934  15888  16053     15     -5    767       C  
ATOM    502  N   HIS A  67      -9.684  17.243   2.753  1.00 92.04           N  
ANISOU  502  N   HIS A  67    11074  11777  12119     56    108    633       N  
ATOM    503  CA  HIS A  67      -8.866  17.644   3.903  1.00 80.85           C  
ANISOU  503  CA  HIS A  67     9689  10323  10706     62    133    590       C  
ATOM    504  C   HIS A  67      -9.460  18.706   4.798  1.00 81.63           C  
ANISOU  504  C   HIS A  67     9790  10386  10838     84    180    609       C  
ATOM    505  O   HIS A  67      -9.199  18.702   6.003  1.00 80.87           O  
ANISOU  505  O   HIS A  67     9719  10262  10744     89    197    577       O  
ATOM    506  CB  HIS A  67      -7.511  18.145   3.428  1.00 76.88           C  
ANISOU  506  CB  HIS A  67     9200   9817  10192     54    133    561       C  
ATOM    507  CG  HIS A  67      -6.489  17.081   3.373  1.00 89.88           C  
ANISOU  507  CG  HIS A  67    10865  11479  11805     36     99    515       C  
ATOM    508  CD2 HIS A  67      -5.306  17.019   2.728  1.00103.95           C  
ANISOU  508  CD2 HIS A  67    12655  13271  13568     23     84    489       C  
ATOM    509  ND1 HIS A  67      -6.610  15.901   4.074  1.00102.09           N  
ANISOU  509  ND1 HIS A  67    12422  13030  13336     30     80    491       N  
ATOM    510  CE1 HIS A  67      -5.556  15.146   3.841  1.00107.03           C  
ANISOU  510  CE1 HIS A  67    13063  13669  13935     14     54    453       C  
ATOM    511  NE2 HIS A  67      -4.746  15.801   3.030  1.00111.31           N  
ANISOU  511  NE2 HIS A  67    13604  14216  14474     10     56    451       N  
ATOM    512  N   THR A  68     -10.202  19.643   4.206  1.00 85.10           N  
ANISOU  512  N   THR A  68    10206  10825  11304     97    201    659       N  
ATOM    513  CA  THR A  68     -10.976  20.612   4.970  1.00 82.81           C  
ANISOU  513  CA  THR A  68     9915  10501  11049    120    247    685       C  
ATOM    514  C   THR A  68     -12.078  19.828   5.662  1.00 88.70           C  
ANISOU  514  C   THR A  68    10653  11250  11798    125    243    700       C  
ATOM    515  O   THR A  68     -12.244  19.924   6.879  1.00 90.40           O  
ANISOU  515  O   THR A  68    10887  11436  12023    136    268    684       O  
ATOM    516  CB  THR A  68     -11.565  21.715   4.079  1.00 80.69           C  
ANISOU  516  CB  THR A  68     9617  10234  10807    133    270    741       C  
ATOM    517  CG2 THR A  68     -12.412  22.686   4.886  1.00 80.83           C  
ANISOU  517  CG2 THR A  68     9633  10216  10862    158    320    770       C  
ATOM    518  OG1 THR A  68     -10.495  22.427   3.447  1.00 80.84           O  
ANISOU  518  OG1 THR A  68     9644  10250  10823    127    274    726       O  
ATOM    519  N   LEU A  69     -12.810  19.016   4.900  1.00 87.22           N  
ANISOU  519  N   LEU A  69    10438  11100  11602    117    210    730       N  
ATOM    520  CA  LEU A  69     -13.775  18.123   5.516  1.00 82.43           C  
ANISOU  520  CA  LEU A  69     9823  10499  10997    119    201    741       C  
ATOM    521  C   LEU A  69     -13.150  17.244   6.614  1.00 81.63           C  
ANISOU  521  C   LEU A  69     9755  10385  10875    112    191    686       C  
ATOM    522  O   LEU A  69     -13.598  17.340   7.756  1.00 75.26           O  
ANISOU  522  O   LEU A  69     8960   9553  10083    126    218    683       O  
ATOM    523  CB  LEU A  69     -14.520  17.309   4.473  1.00 85.24           C  
ANISOU  523  CB  LEU A  69    10147  10898  11343    106    162    776       C  
ATOM    524  CG  LEU A  69     -15.548  18.150   3.705  1.00 95.25           C  
ANISOU  524  CG  LEU A  69    11377  12176  12637    119    178    843       C  
ATOM    525  CD1 LEU A  69     -15.975  17.466   2.399  1.00104.90           C  
ANISOU  525  CD1 LEU A  69    12569  13447  13843    100    134    872       C  
ATOM    526  CD2 LEU A  69     -16.766  18.475   4.563  1.00 90.88           C  
ANISOU  526  CD2 LEU A  69    10811  11602  12116    141    211    880       C  
ATOM    527  N   PHE A  70     -12.132  16.423   6.312  1.00 83.57           N  
ANISOU  527  N   PHE A  70    10016  10649  11089     92    157    643       N  
ATOM    528  CA  PHE A  70     -11.444  15.646   7.374  1.00 90.40           C  
ANISOU  528  CA  PHE A  70    10912  11501  11935     86    150    591       C  
ATOM    529  C   PHE A  70     -11.106  16.613   8.516  1.00101.95           C  
ANISOU  529  C   PHE A  70    12400  12923  13413    102    193    571       C  
ATOM    530  O   PHE A  70     -11.453  16.375   9.672  1.00103.46           O  
ANISOU  530  O   PHE A  70    12606  13096  13609    111    208    561       O  
ATOM    531  CB  PHE A  70     -10.119  15.042   6.916  1.00 89.42           C  
ANISOU  531  CB  PHE A  70    10805  11392  11779     66    119    546       C  
ATOM    532  CG  PHE A  70     -10.217  13.722   6.196  1.00 97.71           C  
ANISOU  532  CG  PHE A  70    11843  12477  12804     47     74    544       C  
ATOM    533  CD1 PHE A  70     -11.231  13.450   5.279  1.00100.40           C  
ANISOU  533  CD1 PHE A  70    12153  12845  13151     43     57    588       C  
ATOM    534  CD2 PHE A  70      -9.188  12.780   6.340  1.00100.25           C  
ANISOU  534  CD2 PHE A  70    12187  12807  13098     32     49    496       C  
ATOM    535  CE1 PHE A  70     -11.251  12.235   4.584  1.00 96.76           C  
ANISOU  535  CE1 PHE A  70    11684  12416  12666     23     16    582       C  
ATOM    536  CE2 PHE A  70      -9.205  11.581   5.634  1.00 89.92           C  
ANISOU  536  CE2 PHE A  70    10870  11528  11768     14     11    492       C  
ATOM    537  CZ  PHE A  70     -10.229  11.313   4.750  1.00 87.62           C  
ANISOU  537  CZ  PHE A  70    10550  11262  11481      9     -6    533       C  
ATOM    538  N   GLY A  71     -10.430  17.708   8.160  1.00102.85           N  
ANISOU  538  N   GLY A  71    12520  13023  13535    104    212    567       N  
ATOM    539  CA  GLY A  71      -9.835  18.635   9.123  1.00 97.03           C  
ANISOU  539  CA  GLY A  71    11811  12247  12808    113    249    540       C  
ATOM    540  C   GLY A  71     -10.827  19.234  10.097  1.00 91.97           C  
ANISOU  540  C   GLY A  71    11172  11576  12194    135    290    562       C  
ATOM    541  O   GLY A  71     -10.696  19.098  11.301  1.00 78.94           O  
ANISOU  541  O   GLY A  71     9548   9905  10541    140    305    533       O  
ATOM    542  N   ASP A  72     -11.840  19.888   9.565  1.00 97.07           N  
ANISOU  542  N   ASP A  72    11791  12222  12868    149    310    616       N  
ATOM    543  CA  ASP A  72     -12.881  20.462  10.388  1.00111.71           C  
ANISOU  543  CA  ASP A  72    13645  14050  14752    172    351    644       C  
ATOM    544  C   ASP A  72     -13.338  19.404  11.397  1.00126.43           C  
ANISOU  544  C   ASP A  72    15519  15915  16605    173    342    630       C  
ATOM    545  O   ASP A  72     -13.443  19.688  12.590  1.00135.52           O  
ANISOU  545  O   ASP A  72    16692  17035  17762    186    373    613       O  
ATOM    546  CB  ASP A  72     -14.074  20.890   9.524  1.00125.18           C  
ANISOU  546  CB  ASP A  72    15310  15767  16484    185    361    712       C  
ATOM    547  CG  ASP A  72     -13.743  22.024   8.545  1.00131.94           C  
ANISOU  547  CG  ASP A  72    16155  16621  17356    187    376    733       C  
ATOM    548  OD1 ASP A  72     -12.645  22.605   8.631  1.00133.58           O  
ANISOU  548  OD1 ASP A  72    16386  16810  17557    181    386    697       O  
ATOM    549  OD2 ASP A  72     -14.596  22.339   7.678  1.00135.51           O1-
ANISOU  549  OD2 ASP A  72    16572  17089  17827    195    378    789       O1-
ATOM    550  N   LYS A  73     -13.591  18.183  10.902  1.00122.92           N  
ANISOU  550  N   LYS A  73    15056  15506  16142    160    299    635       N  
ATOM    551  CA  LYS A  73     -14.091  17.078  11.731  1.00 99.26           C  
ANISOU  551  CA  LYS A  73    12064  12514  13136    160    286    627       C  
ATOM    552  C   LYS A  73     -13.052  16.727  12.779  1.00 89.77           C  
ANISOU  552  C   LYS A  73    10901  11297  11911    154    285    567       C  
ATOM    553  O   LYS A  73     -13.371  16.524  13.937  1.00 85.75           O  
ANISOU  553  O   LYS A  73    10408  10770  11403    165    303    556       O  
ATOM    554  CB  LYS A  73     -14.450  15.858  10.892  1.00 87.27           C  
ANISOU  554  CB  LYS A  73    10521  11036  11602    144    239    641       C  
ATOM    555  CG  LYS A  73     -15.414  14.909  11.592  1.00 88.67           C  
ANISOU  555  CG  LYS A  73    10691  11217  11782    149    234    655       C  
ATOM    556  CD  LYS A  73     -16.833  15.470  11.727  1.00 99.47           C  
ANISOU  556  CD  LYS A  73    12033  12577  13186    170    264    713       C  
ATOM    557  CE  LYS A  73     -17.809  14.801  10.747  1.00103.64           C  
ANISOU  557  CE  LYS A  73    12520  13140  13718    161    233    759       C  
ATOM    558  NZ  LYS A  73     -19.208  15.331  10.808  1.00105.58           N1+
ANISOU  558  NZ  LYS A  73    12736  13380  13999    181    261    820       N1+
ATOM    559  N   LEU A  74     -11.795  16.719  12.374  1.00 89.57           N  
ANISOU  559  N   LEU A  74    10891  11279  11864    138    266    529       N  
ATOM    560  CA  LEU A  74     -10.696  16.445  13.299  1.00 96.79           C  
ANISOU  560  CA  LEU A  74    11840  12181  12756    130    263    473       C  
ATOM    561  C   LEU A  74     -10.561  17.524  14.375  1.00 97.27           C  
ANISOU  561  C   LEU A  74    11927  12202  12830    144    309    458       C  
ATOM    562  O   LEU A  74     -10.150  17.252  15.497  1.00101.29           O  
ANISOU  562  O   LEU A  74    12464  12698  13325    144    315    422       O  
ATOM    563  CB  LEU A  74      -9.380  16.286  12.527  1.00 94.58           C  
ANISOU  563  CB  LEU A  74    11566  11917  12452    110    234    441       C  
ATOM    564  CG  LEU A  74      -9.277  15.084  11.568  1.00 89.66           C  
ANISOU  564  CG  LEU A  74    10925  11332  11809     93    187    443       C  
ATOM    565  CD1 LEU A  74      -8.165  15.336  10.558  1.00 97.07           C  
ANISOU  565  CD1 LEU A  74    11865  12284  12734     78    169    426       C  
ATOM    566  CD2 LEU A  74      -9.058  13.779  12.315  1.00 78.58           C  
ANISOU  566  CD2 LEU A  74     9536   9937  10383     86    164    413       C  
ATOM    567  N   CYS A  75     -10.923  18.747  14.040  1.00 98.63           N  
ANISOU  567  N   CYS A  75    12091  12355  13028    156    342    486       N  
ATOM    568  CA  CYS A  75     -10.877  19.814  15.019  1.00112.95           C  
ANISOU  568  CA  CYS A  75    13930  14129  14858    170    389    474       C  
ATOM    569  C   CYS A  75     -11.988  19.729  16.071  1.00119.83           C  
ANISOU  569  C   CYS A  75    14805  14982  15743    190    418    492       C  
ATOM    570  O   CYS A  75     -11.860  20.334  17.140  1.00132.66           O  
ANISOU  570  O   CYS A  75    16459  16575  17371    199    453    470       O  
ATOM    571  CB  CYS A  75     -10.899  21.180  14.326  1.00123.40           C  
ANISOU  571  CB  CYS A  75    15244  15434  16207    177    419    499       C  
ATOM    572  SG  CYS A  75      -9.257  21.708  13.784  1.00133.26           S  
ANISOU  572  SG  CYS A  75    16511  16683  17441    156    407    456       S  
ATOM    573  N   THR A  76     -13.047  18.958  15.803  1.00110.83           N  
ANISOU  573  N   THR A  76    13638  13863  14610    196    404    530       N  
ATOM    574  CA  THR A  76     -14.248  18.997  16.641  1.00103.62           C  
ANISOU  574  CA  THR A  76    12722  12933  13717    218    435    559       C  
ATOM    575  C   THR A  76     -14.117  18.352  18.026  1.00 99.03           C  
ANISOU  575  C   THR A  76    12169  12341  13116    221    439    524       C  
ATOM    576  O   THR A  76     -14.737  18.847  18.978  1.00 96.31           O  
ANISOU  576  O   THR A  76    11838  11968  12787    240    480    532       O  
ATOM    577  CB  THR A  76     -15.464  18.371  15.943  1.00101.45           C  
ANISOU  577  CB  THR A  76    12406  12684  13456    223    418    614       C  
ATOM    578  CG2 THR A  76     -15.765  19.079  14.622  1.00 96.00           C  
ANISOU  578  CG2 THR A  76    11684  12005  12787    223    418    657       C  
ATOM    579  OG1 THR A  76     -15.216  16.981  15.725  1.00106.22           O  
ANISOU  579  OG1 THR A  76    13005  13321  14034    205    369    597       O  
ATOM    580  N   VAL A  77     -13.373  17.250  18.149  1.00 90.47           N  
ANISOU  580  N   VAL A  77    11094  11279  12000    203    399    487       N  
ATOM    581  CA  VAL A  77     -13.111  16.696  19.476  1.00 91.67           C  
ANISOU  581  CA  VAL A  77    11275  11421  12132    205    403    451       C  
ATOM    582  C   VAL A  77     -11.722  16.108  19.592  1.00104.14           C  
ANISOU  582  C   VAL A  77    12877  13015  13677    183    371    398       C  
ATOM    583  O   VAL A  77     -11.538  15.078  20.236  1.00115.01           O  
ANISOU  583  O   VAL A  77    14263  14403  15032    179    351    376       O  
ATOM    584  CB  VAL A  77     -14.150  15.644  19.946  1.00101.88           C  
ANISOU  584  CB  VAL A  77    12555  12726  13428    214    396    475       C  
ATOM    585  CG1 VAL A  77     -14.392  15.800  21.443  1.00105.37           C  
ANISOU  585  CG1 VAL A  77    13025  13141  13867    231    431    460       C  
ATOM    586  CG2 VAL A  77     -15.483  15.756  19.208  1.00106.45           C  
ANISOU  586  CG2 VAL A  77    13096  13313  14039    226    403    538       C  
ATOM    587  N   ALA A  78     -10.737  16.766  18.980  1.00133.75           N  
ANISOU  587  N   ALA A  78    16633  16763  17422    170    365    378       N  
ATOM    588  CA  ALA A  78      -9.316  16.612  19.405  1.00144.54           C  
ANISOU  588  CA  ALA A  78    18028  18132  18760    153    349    322       C  
ATOM    589  C   ALA A  78      -9.197  17.242  20.802  1.00152.84           C  
ANISOU  589  C   ALA A  78    19114  19151  19808    163    386    296       C  
ATOM    590  O   ALA A  78      -8.159  17.078  21.491  1.00104.83           O  
ANISOU  590  O   ALA A  78    13060  13070  13701    151    377    250       O  
ATOM    591  CB  ALA A  78      -8.348  17.285  18.423  1.00136.02           C  
ANISOU  591  CB  ALA A  78    16946  17055  17680    139    340    311       C  
ATOM    592  N   THR A  79     -10.266  18.006  21.131  1.00165.53           N  
ANISOU  592  N   THR A  79    20718  20733  21442    184    429    328       N  
ATOM    593  CA  THR A  79     -10.687  18.458  22.469  1.00148.11           C  
ANISOU  593  CA  THR A  79    18539  18496  19239    200    470    318       C  
ATOM    594  C   THR A  79     -10.810  17.258  23.386  1.00143.09           C  
ANISOU  594  C   THR A  79    17912  17875  18580    201    453    304       C  
ATOM    595  O   THR A  79     -11.890  16.881  23.825  1.00128.87           O  
ANISOU  595  O   THR A  79    16102  16071  16790    218    466    333       O  
ATOM    596  CB  THR A  79     -12.072  19.169  22.421  1.00142.66           C  
ANISOU  596  CB  THR A  79    17834  17785  18586    225    512    370       C  
ATOM    597  CG2 THR A  79     -12.283  20.069  23.649  1.00145.26           C  
ANISOU  597  CG2 THR A  79    18196  18075  18921    240    564    355       C  
ATOM    598  OG1 THR A  79     -12.187  19.947  21.223  1.00131.85           O  
ANISOU  598  OG1 THR A  79    16441  16415  17241    224    517    399       O  
ATOM    599  N   LEU A  80      -9.666  16.643  23.605  1.00142.30           N  
ANISOU  599  N   LEU A  80    17827  17791  18448    182    421    261       N  
ATOM    600  CA  LEU A  80      -9.475  15.539  24.512  1.00143.37           C  
ANISOU  600  CA  LEU A  80    17976  17942  18557    181    403    239       C  
ATOM    601  C   LEU A  80      -7.967  15.533  24.713  1.00151.48           C  
ANISOU  601  C   LEU A  80    19026  18976  19555    160    382    188       C  
ATOM    602  O   LEU A  80      -7.417  14.624  25.324  1.00162.32           O  
ANISOU  602  O   LEU A  80    20409  20365  20900    153    359    161       O  
ATOM    603  CB  LEU A  80      -9.924  14.228  23.870  1.00134.98           C  
ANISOU  603  CB  LEU A  80    16883  16910  17493    178    365    263       C  
ATOM    604  CG  LEU A  80     -11.391  13.894  23.598  1.00135.74           C  
ANISOU  604  CG  LEU A  80    16950  17008  17615    195    374    315       C  
ATOM    605  CD1 LEU A  80     -11.483  12.715  22.636  1.00131.14           C  
ANISOU  605  CD1 LEU A  80    16339  16459  17029    183    329    330       C  
ATOM    606  CD2 LEU A  80     -12.153  13.606  24.886  1.00141.45           C  
ANISOU  606  CD2 LEU A  80    17688  17719  18339    214    399    320       C  
ATOM    607  N   ARG A  81      -7.304  16.552  24.158  1.00146.12           N  
ANISOU  607  N   ARG A  81    18351  18285  18882    150    389    176       N  
ATOM    608  CA  ARG A  81      -5.874  16.725  24.252  1.00138.16           C  
ANISOU  608  CA  ARG A  81    17362  17282  17851    129    372    131       C  
ATOM    609  C   ARG A  81      -5.392  16.463  25.679  1.00146.22           C  
ANISOU  609  C   ARG A  81    18416  18299  18844    126    377     92       C  
ATOM    610  O   ARG A  81      -4.231  16.126  25.881  1.00156.62           O  
ANISOU  610  O   ARG A  81    19744  19631  20135    109    352     56       O  
ATOM    611  CB  ARG A  81      -5.489  18.106  23.731  1.00129.54           C  
ANISOU  611  CB  ARG A  81    16275  16166  16777    123    395    127       C  
ATOM    612  CG  ARG A  81      -6.423  19.216  24.183  1.00137.02           C  
ANISOU  612  CG  ARG A  81    17233  17077  17750    142    447    147       C  
ATOM    613  CD  ARG A  81      -5.808  19.992  25.334  1.00147.90           C  
ANISOU  613  CD  ARG A  81    18651  18429  19115    136    474    105       C  
ATOM    614  NE  ARG A  81      -6.779  20.444  26.330  1.00145.72           N  
ANISOU  614  NE  ARG A  81    18393  18125  18849    157    519    115       N  
ATOM    615  CZ  ARG A  81      -6.475  21.250  27.345  1.00139.15           C  
ANISOU  615  CZ  ARG A  81    17598  17266  18009    155    551     83       C  
ATOM    616  NH1 ARG A  81      -5.237  21.701  27.501  1.00142.45           N1+
ANISOU  616  NH1 ARG A  81    18036  17680  18409    132    542     39       N1+
ATOM    617  NH2 ARG A  81      -7.408  21.618  28.209  1.00143.07           N  
ANISOU  617  NH2 ARG A  81    18110  17736  18515    175    593     94       N  
ATOM    618  N   GLU A  82      -6.303  16.580  26.651  1.00147.85           N  
ANISOU  618  N   GLU A  82    18635  18488  19055    145    409    103       N  
ATOM    619  CA  GLU A  82      -6.136  16.005  27.993  1.00156.50           C  
ANISOU  619  CA  GLU A  82    19754  19585  20121    147    409     76       C  
ATOM    620  C   GLU A  82      -5.525  14.599  27.903  1.00179.35           C  
ANISOU  620  C   GLU A  82    22638  22516  22991    136    362     65       C  
ATOM    621  O   GLU A  82      -4.822  14.171  28.825  1.00193.78           O  
ANISOU  621  O   GLU A  82    24486  24352  24788    129    352     32       O  
ATOM    622  CB  GLU A  82      -7.505  15.953  28.716  1.00162.93           C  
ANISOU  622  CB  GLU A  82    20570  20384  20950    173    443    106       C  
ATOM    623  CG  GLU A  82      -7.533  15.409  30.148  1.00161.21           C  
ANISOU  623  CG  GLU A  82    20379  20168  20706    180    450     85       C  
ATOM    624  CD  GLU A  82      -8.957  15.199  30.696  1.00158.96           C  
ANISOU  624  CD  GLU A  82    20089  19871  20438    206    480    121       C  
ATOM    625  OE1 GLU A  82      -9.863  14.755  29.943  1.00144.53           O  
ANISOU  625  OE1 GLU A  82    18229  18052  18635    217    474    164       O  
ATOM    626  OE2 GLU A  82      -9.177  15.462  31.903  1.00147.69           O1-
ANISOU  626  OE2 GLU A  82    18690  18427  18998    217    510    107       O1-
ATOM    627  N   THR A  83      -5.822  13.891  26.803  1.00191.41           N  
ANISOU  627  N   THR A  83    24133  24064  24531    135    336     93       N  
ATOM    628  CA  THR A  83      -5.255  12.569  26.501  1.00184.25           C  
ANISOU  628  CA  THR A  83    23213  23189  23604    125    292     85       C  
ATOM    629  C   THR A  83      -4.389  12.588  25.238  1.00171.18           C  
ANISOU  629  C   THR A  83    21542  21549  21950    107    263     79       C  
ATOM    630  O   THR A  83      -3.717  11.597  24.943  1.00202.93           O  
ANISOU  630  O   THR A  83    25555  25595  25953     96    227     67       O  
ATOM    631  CB  THR A  83      -6.352  11.481  26.317  1.00178.03           C  
ANISOU  631  CB  THR A  83    22402  22415  22828    138    282    120       C  
ATOM    632  CG2 THR A  83      -5.851  10.090  26.775  1.00170.51           C  
ANISOU  632  CG2 THR A  83    21451  21488  21849    132    250    104       C  
ATOM    633  OG1 THR A  83      -7.531  11.830  27.054  1.00180.06           O  
ANISOU  633  OG1 THR A  83    22664  22651  23100    159    318    143       O  
ATOM    634  N   TYR A  84      -4.419  13.682  24.478  1.00144.15           N  
ANISOU  634  N   TYR A  84    18113  18110  18547    104    278     89       N  
ATOM    635  CA  TYR A  84      -3.457  13.877  23.390  1.00150.56           C  
ANISOU  635  CA  TYR A  84    18915  18934  19357     87    255     79       C  
ATOM    636  C   TYR A  84      -2.483  14.968  23.794  1.00143.95           C  
ANISOU  636  C   TYR A  84    18102  18079  18513     75    270     45       C  
ATOM    637  O   TYR A  84      -1.533  14.699  24.545  1.00163.15           O  
ANISOU  637  O   TYR A  84    20553  20518  20918     64    258      9       O  
ATOM    638  CB  TYR A  84      -4.143  14.172  22.057  1.00155.61           C  
ANISOU  638  CB  TYR A  84    19525  19575  20024     90    255    118       C  
ATOM    639  CG  TYR A  84      -5.360  13.324  21.849  1.00169.29           C  
ANISOU  639  CG  TYR A  84    21236  21318  21767    103    249    155       C  
ATOM    640  CD1 TYR A  84      -5.261  12.002  21.416  1.00161.03           C  
ANISOU  640  CD1 TYR A  84    20175  20301  20709     96    212    158       C  
ATOM    641  CD2 TYR A  84      -6.620  13.839  22.113  1.00202.36           C  
ANISOU  641  CD2 TYR A  84    25419  25487  25980    122    282    188       C  
ATOM    642  CE1 TYR A  84      -6.388  11.215  21.248  1.00174.01           C  
ANISOU  642  CE1 TYR A  84    21799  21954  22364    106    207    191       C  
ATOM    643  CE2 TYR A  84      -7.747  13.066  21.947  1.00217.67           C  
ANISOU  643  CE2 TYR A  84    27336  27437  27930    133    276    223       C  
ATOM    644  CZ  TYR A  84      -7.634  11.762  21.520  1.00202.27           C  
ANISOU  644  CZ  TYR A  84    25371  25514  25967    124    238    224       C  
ATOM    645  OH  TYR A  84      -8.802  11.055  21.375  1.00203.10           O  
ANISOU  645  OH  TYR A  84    25455  25628  26086    134    235    259       O  
ATOM    646  N   GLY A  85      -2.700  16.197  23.339  1.00113.26           N  
ANISOU  646  N   GLY A  85    14215  14169  14650     77    297     56       N  
ATOM    647  CA  GLY A  85      -1.890  17.274  23.856  1.00104.47           C  
ANISOU  647  CA  GLY A  85    13127  13035  13532     67    317     24       C  
ATOM    648  C   GLY A  85      -1.779  18.502  23.007  1.00103.44           C  
ANISOU  648  C   GLY A  85    12991  12885  13426     63    336     34       C  
ATOM    649  O   GLY A  85      -2.425  19.516  23.277  1.00119.16           O  
ANISOU  649  O   GLY A  85    14992  14845  15438     75    376     45       O  
ATOM    650  N   GLU A  86      -0.921  18.433  22.000  1.00 98.01           N  
ANISOU  650  N   GLU A  86    12288  12213  12736     48    310     29       N  
ATOM    651  CA  GLU A  86      -0.582  19.622  21.238  1.00 99.58           C  
ANISOU  651  CA  GLU A  86    12485  12395  12957     42    326     33       C  
ATOM    652  C   GLU A  86      -0.759  19.442  19.747  1.00102.61           C  
ANISOU  652  C   GLU A  86    12836  12797  13355     43    308     66       C  
ATOM    653  O   GLU A  86      -0.102  20.110  18.951  1.00 86.59           O  
ANISOU  653  O   GLU A  86    10801  10765  11335     33    307     64       O  
ATOM    654  CB  GLU A  86       0.825  20.062  21.596  1.00107.78           C  
ANISOU  654  CB  GLU A  86    13543  13430  13978     20    319    -11       C  
ATOM    655  CG  GLU A  86       0.843  20.834  22.910  1.00121.17           C  
ANISOU  655  CG  GLU A  86    15274  15097  15669     20    352    -39       C  
ATOM    656  CD  GLU A  86       2.215  21.347  23.269  1.00131.28           C  
ANISOU  656  CD  GLU A  86    16574  16373  16934     -4    345    -83       C  
ATOM    657  OE1 GLU A  86       3.171  20.533  23.221  1.00123.39           O  
ANISOU  657  OE1 GLU A  86    15570  15403  15910    -19    308   -103       O  
ATOM    658  OE2 GLU A  86       2.321  22.553  23.606  1.00129.21           O1-
ANISOU  658  OE2 GLU A  86    16330  16078  16684     -9    378    -96       O1-
ATOM    659  N   MET A  87      -1.675  18.546  19.383  1.00117.64           N  
ANISOU  659  N   MET A  87    14718  14718  15261     55    295     97       N  
ATOM    660  CA  MET A  87      -2.225  18.504  18.027  1.00117.38           C  
ANISOU  660  CA  MET A  87    14655  14699  15246     59    286    137       C  
ATOM    661  C   MET A  87      -3.294  19.580  17.950  1.00110.19           C  
ANISOU  661  C   MET A  87    13739  13761  14369     77    327    172       C  
ATOM    662  O   MET A  87      -3.637  20.050  16.862  1.00114.44           O  
ANISOU  662  O   MET A  87    14255  14301  14927     80    331    204       O  
ATOM    663  CB  MET A  87      -2.870  17.153  17.682  1.00119.09           C  
ANISOU  663  CB  MET A  87    14850  14944  15454     64    256    158       C  
ATOM    664  CG  MET A  87      -2.505  15.985  18.577  1.00127.04           C  
ANISOU  664  CG  MET A  87    15870  15966  16433     59    234    131       C  
ATOM    665  SD  MET A  87      -2.650  14.485  17.601  1.00150.14           S  
ANISOU  665  SD  MET A  87    18771  18930  19347     54    189    147       S  
ATOM    666  CE  MET A  87      -3.293  13.283  18.765  1.00152.17           C  
ANISOU  666  CE  MET A  87    19035  19193  19591     63    183    144       C  
ATOM    667  N   ALA A  88      -3.833  19.944  19.113  1.00 97.12           N  
ANISOU  667  N   ALA A  88    12104  12080  12718     88    359    166       N  
ATOM    668  CA  ALA A  88      -4.814  21.008  19.223  1.00 95.87           C  
ANISOU  668  CA  ALA A  88    11944  11890  12590    106    404    196       C  
ATOM    669  C   ALA A  88      -4.282  22.320  18.668  1.00104.56           C  
ANISOU  669  C   ALA A  88    13048  12969  13710    101    427    194       C  
ATOM    670  O   ALA A  88      -5.038  23.057  18.043  1.00106.72           O  
ANISOU  670  O   ALA A  88    13306  13230  14014    114    452    232       O  
ATOM    671  CB  ALA A  88      -5.228  21.184  20.669  1.00 95.58           C  
ANISOU  671  CB  ALA A  88    11936  11830  12550    117    435    179       C  
ATOM    672  N   ASP A  89      -2.987  22.602  18.900  1.00117.22           N  
ANISOU  672  N   ASP A  89    14672  14570  15297     81    418    150       N  
ATOM    673  CA  ASP A  89      -2.293  23.754  18.295  1.00116.68           C  
ANISOU  673  CA  ASP A  89    14605  14483  15244     72    433    144       C  
ATOM    674  C   ASP A  89      -2.780  23.944  16.872  1.00109.14           C  
ANISOU  674  C   ASP A  89    13615  13540  14312     79    429    191       C  
ATOM    675  O   ASP A  89      -3.260  25.021  16.504  1.00103.52           O  
ANISOU  675  O   ASP A  89    12898  12804  13631     90    464    217       O  
ATOM    676  CB  ASP A  89      -0.761  23.534  18.203  1.00126.77           C  
ANISOU  676  CB  ASP A  89    15893  15776  16498     47    402    101       C  
ATOM    677  CG  ASP A  89      -0.044  23.593  19.540  1.00127.38           C  
ANISOU  677  CG  ASP A  89    16006  15840  16553     35    407     52       C  
ATOM    678  OD1 ASP A  89       1.011  22.936  19.642  1.00116.45           O  
ANISOU  678  OD1 ASP A  89    14625  14478  15142     17    373     21       O  
ATOM    679  OD2 ASP A  89      -0.494  24.287  20.469  1.00128.07           O1-
ANISOU  679  OD2 ASP A  89    16116  15897  16649     42    444     44       O1-
ATOM    680  N   CYS A  90      -2.656  22.864  16.096  1.00109.45           N  
ANISOU  680  N   CYS A  90    13633  13617  14335     74    387    200       N  
ATOM    681  CA  CYS A  90      -2.819  22.880  14.641  1.00108.42           C  
ANISOU  681  CA  CYS A  90    13471  13508  14217     74    372    236       C  
ATOM    682  C   CYS A  90      -4.191  23.363  14.176  1.00109.04           C  
ANISOU  682  C   CYS A  90    13526  13577  14326     95    398    291       C  
ATOM    683  O   CYS A  90      -4.314  23.883  13.054  1.00104.12           O  
ANISOU  683  O   CYS A  90    12881  12959  13720     98    400    322       O  
ATOM    684  CB  CYS A  90      -2.524  21.492  14.073  1.00109.12           C  
ANISOU  684  CB  CYS A  90    13544  13637  14279     64    322    233       C  
ATOM    685  SG  CYS A  90      -0.902  20.836  14.542  1.00120.52           S  
ANISOU  685  SG  CYS A  90    15010  15094  15687     41    290    174       S  
ATOM    686  N   CYS A  91      -5.212  23.204  15.026  1.00110.98           N  
ANISOU  686  N   CYS A  91    13777  13810  14579    111    418    304       N  
ATOM    687  CA  CYS A  91      -6.569  23.656  14.686  1.00107.22           C  
ANISOU  687  CA  CYS A  91    13279  13325  14133    133    445    358       C  
ATOM    688  C   CYS A  91      -6.671  25.137  14.420  1.00103.79           C  
ANISOU  688  C   CYS A  91    12845  12859  13732    142    489    376       C  
ATOM    689  O   CYS A  91      -7.621  25.564  13.803  1.00 99.60           O  
ANISOU  689  O   CYS A  91    12290  12326  13227    158    507    426       O  
ATOM    690  CB  CYS A  91      -7.574  23.250  15.756  1.00110.21           C  
ANISOU  690  CB  CYS A  91    13666  13694  14515    149    462    366       C  
ATOM    691  SG  CYS A  91      -8.126  21.562  15.478  1.00130.27           S  
ANISOU  691  SG  CYS A  91    16183  16279  17034    146    414    381       S  
ATOM    692  N   ALA A  92      -5.693  25.904  14.890  1.00122.29           N  
ANISOU  692  N   ALA A  92    15216  15175  16073    132    506    337       N  
ATOM    693  CA  ALA A  92      -5.563  27.341  14.590  1.00146.45           C  
ANISOU  693  CA  ALA A  92    18279  18202  19163    137    547    348       C  
ATOM    694  C   ALA A  92      -5.166  27.639  13.124  1.00163.41           C  
ANISOU  694  C   ALA A  92    20399  20368  21320    131    531    372       C  
ATOM    695  O   ALA A  92      -5.725  28.545  12.472  1.00158.53           O  
ANISOU  695  O   ALA A  92    19763  19736  20733    145    560    414       O  
ATOM    696  CB  ALA A  92      -4.543  27.969  15.541  1.00147.76           C  
ANISOU  696  CB  ALA A  92    18484  18337  19321    123    565    293       C  
ATOM    697  N   LYS A  93      -4.193  26.874  12.628  1.00175.15           N  
ANISOU  697  N   LYS A  93    21883  21887  22779    111    486    347       N  
ATOM    698  CA  LYS A  93      -3.680  27.012  11.259  1.00169.38           C  
ANISOU  698  CA  LYS A  93    21130  21178  22050    103    466    365       C  
ATOM    699  C   LYS A  93      -4.690  26.423  10.270  1.00167.03           C  
ANISOU  699  C   LYS A  93    20795  20913  21756    114    447    417       C  
ATOM    700  O   LYS A  93      -5.519  25.583  10.660  1.00167.91           O  
ANISOU  700  O   LYS A  93    20901  21038  21860    121    435    428       O  
ATOM    701  CB  LYS A  93      -2.330  26.284  11.133  1.00164.60           C  
ANISOU  701  CB  LYS A  93    20533  20595  21411     79    424    320       C  
ATOM    702  CG  LYS A  93      -1.222  26.885  11.990  1.00160.74           C  
ANISOU  702  CG  LYS A  93    20077  20078  20917     64    439    269       C  
ATOM    703  CD  LYS A  93      -0.479  25.854  12.829  1.00154.66           C  
ANISOU  703  CD  LYS A  93    19328  19325  20112     49    407    222       C  
ATOM    704  CE  LYS A  93      -0.215  26.404  14.228  1.00155.62           C  
ANISOU  704  CE  LYS A  93    19485  19412  20233     45    435    183       C  
ATOM    705  NZ  LYS A  93       0.524  25.466  15.121  1.00157.19           N1+
ANISOU  705  NZ  LYS A  93    19704  19625  20397     30    406    138       N1+
ATOM    706  N   GLN A  94      -4.631  26.860   9.003  1.00147.06           N  
ANISOU  706  N   GLN A  94    18241  18397  19238    114    443    449       N  
ATOM    707  CA  GLN A  94      -5.531  26.315   7.974  1.00131.99           C  
ANISOU  707  CA  GLN A  94    16296  16523  17330    122    422    498       C  
ATOM    708  C   GLN A  94      -4.860  25.980   6.620  1.00115.57           C  
ANISOU  708  C   GLN A  94    14198  14480  15234    108    386    505       C  
ATOM    709  O   GLN A  94      -3.773  26.471   6.311  1.00108.20           O  
ANISOU  709  O   GLN A  94    13274  13539  14298     97    387    482       O  
ATOM    710  CB  GLN A  94      -6.778  27.202   7.847  1.00140.40           C  
ANISOU  710  CB  GLN A  94    17343  17570  18433    146    462    553       C  
ATOM    711  CG  GLN A  94      -7.980  26.664   8.659  1.00148.64           C  
ANISOU  711  CG  GLN A  94    18384  18611  19481    160    470    571       C  
ATOM    712  CD  GLN A  94      -8.571  27.629   9.704  1.00143.59           C  
ANISOU  712  CD  GLN A  94    17762  17925  18871    179    526    576       C  
ATOM    713  NE2 GLN A  94      -8.449  28.929   9.475  1.00152.55           N  
ANISOU  713  NE2 GLN A  94    18898  19029  20035    187    566    591       N  
ATOM    714  OE1 GLN A  94      -9.156  27.194  10.692  1.00116.18           O  
ANISOU  714  OE1 GLN A  94    14302  14444  15397    186    534    569       O  
ATOM    715  N   GLU A  95      -5.553  25.147   5.833  1.00108.37           N  
ANISOU  715  N   GLU A  95    13259  13605  14311    109    356    537       N  
ATOM    716  CA  GLU A  95      -4.981  24.354   4.698  1.00105.98           C  
ANISOU  716  CA  GLU A  95    12942  13344  13981     93    311    534       C  
ATOM    717  C   GLU A  95      -4.135  25.125   3.645  1.00102.06           C  
ANISOU  717  C   GLU A  95    12437  12851  13488     87    314    540       C  
ATOM    718  O   GLU A  95      -4.541  26.175   3.167  1.00117.90           O  
ANISOU  718  O   GLU A  95    14429  14844  15523    100    343    578       O  
ATOM    719  CB  GLU A  95      -6.104  23.585   3.962  1.00102.56           C  
ANISOU  719  CB  GLU A  95    12478  12947  13542     96    286    578       C  
ATOM    720  CG  GLU A  95      -6.934  22.622   4.811  1.00 98.33           C  
ANISOU  720  CG  GLU A  95    11946  12416  13000     99    276    575       C  
ATOM    721  CD  GLU A  95      -6.172  21.385   5.268  1.00108.48           C  
ANISOU  721  CD  GLU A  95    13252  13715  14251     82    241    525       C  
ATOM    722  OE1 GLU A  95      -5.158  21.013   4.631  1.00112.17           O  
ANISOU  722  OE1 GLU A  95    13724  14201  14696     66    214    500       O  
ATOM    723  OE2 GLU A  95      -6.600  20.759   6.273  1.00119.90           O1-
ANISOU  723  OE2 GLU A  95    14710  15154  15693     85    240    511       O1-
ATOM    724  N   PRO A  96      -2.982  24.573   3.229  1.00 94.15           N  
ANISOU  724  N   PRO A  96    11445  11868  12460     69    283    506       N  
ATOM    725  CA  PRO A  96      -2.448  23.248   3.510  1.00 96.15           C  
ANISOU  725  CA  PRO A  96    11711  12143  12679     54    244    467       C  
ATOM    726  C   PRO A  96      -1.713  23.101   4.851  1.00 93.99           C  
ANISOU  726  C   PRO A  96    11471  11845  12398     47    251    415       C  
ATOM    727  O   PRO A  96      -1.285  22.002   5.178  1.00 86.47           O  
ANISOU  727  O   PRO A  96    10528  10908  11418     36    221    383       O  
ATOM    728  CB  PRO A  96      -1.480  23.018   2.349  1.00 99.06           C  
ANISOU  728  CB  PRO A  96    12072  12538  13028     40    218    460       C  
ATOM    729  CG  PRO A  96      -0.997  24.377   1.985  1.00 97.25           C  
ANISOU  729  CG  PRO A  96    11841  12287  12823     45    249    471       C  
ATOM    730  CD  PRO A  96      -2.083  25.348   2.356  1.00 94.72           C  
ANISOU  730  CD  PRO A  96    11512  11940  12537     64    289    508       C  
ATOM    731  N   GLU A  97      -1.595  24.185   5.616  1.00104.65           N  
ANISOU  731  N   GLU A  97    12836  13156  13771     54    289    406       N  
ATOM    732  CA  GLU A  97      -0.799  24.213   6.860  1.00116.20           C  
ANISOU  732  CA  GLU A  97    14330  14594  15226     46    297    355       C  
ATOM    733  C   GLU A  97      -1.162  23.169   7.910  1.00110.88           C  
ANISOU  733  C   GLU A  97    13670  13924  14534     45    283    333       C  
ATOM    734  O   GLU A  97      -0.309  22.443   8.404  1.00120.74           O  
ANISOU  734  O   GLU A  97    14936  15182  15759     32    260    293       O  
ATOM    735  CB  GLU A  97      -0.946  25.571   7.533  1.00129.17           C  
ANISOU  735  CB  GLU A  97    15986  16192  16900     55    345    356       C  
ATOM    736  CG  GLU A  97      -0.145  26.680   6.896  1.00140.80           C  
ANISOU  736  CG  GLU A  97    17458  17650  18389     51    363    357       C  
ATOM    737  CD  GLU A  97      -0.264  27.938   7.707  1.00159.89           C  
ANISOU  737  CD  GLU A  97    19894  20021  20837     58    412    352       C  
ATOM    738  OE1 GLU A  97       0.749  28.365   8.310  1.00168.94           O  
ANISOU  738  OE1 GLU A  97    21063  21146  21980     44    420    310       O  
ATOM    739  OE2 GLU A  97      -1.394  28.473   7.764  1.00178.96           O1-
ANISOU  739  OE2 GLU A  97    22299  22420  23277     77    442    390       O1-
ATOM    740  N   ARG A  98      -2.436  23.145   8.268  1.00108.77           N  
ANISOU  740  N   ARG A  98    13395  13651  14281     61    298    363       N  
ATOM    741  CA  ARG A  98      -2.954  22.297   9.331  1.00107.58           C  
ANISOU  741  CA  ARG A  98    13256  13500  14119     64    292    349       C  
ATOM    742  C   ARG A  98      -2.649  20.805   9.132  1.00120.26           C  
ANISOU  742  C   ARG A  98    14860  15142  15693     52    246    332       C  
ATOM    743  O   ARG A  98      -2.149  20.157  10.053  1.00135.36           O  
ANISOU  743  O   ARG A  98    16793  17053  17586     45    235    294       O  
ATOM    744  CB  ARG A  98      -4.469  22.542   9.474  1.00109.03           C  
ANISOU  744  CB  ARG A  98    13424  13675  14327     85    316    395       C  
ATOM    745  CG  ARG A  98      -5.210  21.549  10.353  1.00111.51           C  
ANISOU  745  CG  ARG A  98    13744  13995  14630     90    307    391       C  
ATOM    746  CD  ARG A  98      -6.691  21.869  10.416  1.00114.40           C  
ANISOU  746  CD  ARG A  98    14091  14352  15023    110    332    440       C  
ATOM    747  NE  ARG A  98      -7.396  21.575   9.173  1.00110.38           N  
ANISOU  747  NE  ARG A  98    13546  13874  14518    112    312    487       N  
ATOM    748  CZ  ARG A  98      -8.646  21.940   8.936  1.00115.80           C  
ANISOU  748  CZ  ARG A  98    14210  14559  15231    129    332    538       C  
ATOM    749  NH1 ARG A  98      -9.333  22.623   9.850  1.00119.91           N1+
ANISOU  749  NH1 ARG A  98    14739  15046  15775    147    373    550       N1+
ATOM    750  NH2 ARG A  98      -9.213  21.635   7.781  1.00118.86           N  
ANISOU  750  NH2 ARG A  98    14564  14977  15618    127    310    578       N  
ATOM    751  N   ASN A  99      -2.957  20.262   7.948  1.00133.66           N  
ANISOU  751  N   ASN A  99    16531  16870  17382     49    219    359       N  
ATOM    752  CA  ASN A  99      -2.749  18.822   7.644  1.00126.49           C  
ANISOU  752  CA  ASN A  99    15619  15995  16445     37    177    346       C  
ATOM    753  C   ASN A  99      -1.254  18.423   7.772  1.00127.17           C  
ANISOU  753  C   ASN A  99    15725  16087  16507     21    157    298       C  
ATOM    754  O   ASN A  99      -0.920  17.344   8.287  1.00105.36           O  
ANISOU  754  O   ASN A  99    12974  13337  13723     14    134    270       O  
ATOM    755  CB  ASN A  99      -3.342  18.498   6.246  1.00113.92           C  
ANISOU  755  CB  ASN A  99    13997  14435  14851     36    156    386       C  
ATOM    756  CG  ASN A  99      -2.929  17.131   5.715  1.00103.40           C  
ANISOU  756  CG  ASN A  99    12663  13136  13488     21    113    369       C  
ATOM    757  ND2 ASN A  99      -2.105  17.131   4.659  1.00 98.95           N  
ANISOU  757  ND2 ASN A  99    12094  12590  12911     10     96    364       N  
ATOM    758  OD1 ASN A  99      -3.358  16.091   6.226  1.00 96.36           O  
ANISOU  758  OD1 ASN A  99    11774  12254  12585     19     96    361       O  
ATOM    759  N   GLU A 100      -0.365  19.313   7.324  1.00128.01           N  
ANISOU  759  N   GLU A 100    15834  16184  16619     16    167    290       N  
ATOM    760  CA  GLU A 100       1.071  19.097   7.468  1.00126.17           C  
ANISOU  760  CA  GLU A 100    15618  15954  16368      1    153    247       C  
ATOM    761  C   GLU A 100       1.423  19.188   8.970  1.00126.32           C  
ANISOU  761  C   GLU A 100    15663  15948  16384      0    167    211       C  
ATOM    762  O   GLU A 100       2.325  18.494   9.442  1.00147.47           O  
ANISOU  762  O   GLU A 100    18356  18635  19040    -11    147    175       O  
ATOM    763  CB  GLU A 100       1.890  20.084   6.587  1.00127.91           C  
ANISOU  763  CB  GLU A 100    15832  16170  16597     -4    162    251       C  
ATOM    764  CG  GLU A 100       1.880  19.777   5.074  1.00124.02           C  
ANISOU  764  CG  GLU A 100    15316  15708  16097     -7    140    277       C  
ATOM    765  CD  GLU A 100       2.526  20.864   4.185  1.00117.04           C  
ANISOU  765  CD  GLU A 100    14424  14818  15227     -9    155    289       C  
ATOM    766  OE1 GLU A 100       2.147  22.056   4.242  1.00104.95           O  
ANISOU  766  OE1 GLU A 100    12890  13263  13724      1    188    309       O  
ATOM    767  OE2 GLU A 100       3.402  20.526   3.376  1.00113.10           O1-
ANISOU  767  OE2 GLU A 100    13922  14340  14712    -19    134    279       O1-
ATOM    768  N   CYS A 101       0.684  20.017   9.712  1.00112.97           N  
ANISOU  768  N   CYS A 101    13979  14229  14715     12    201    221       N  
ATOM    769  CA  CYS A 101       0.870  20.173  11.162  1.00103.98           C  
ANISOU  769  CA  CYS A 101    12867  13066  13573     12    217    189       C  
ATOM    770  C   CYS A 101       0.413  18.905  11.870  1.00102.75           C  
ANISOU  770  C   CYS A 101    12716  12925  13399     15    198    181       C  
ATOM    771  O   CYS A 101       1.085  18.401  12.774  1.00128.67           O  
ANISOU  771  O   CYS A 101    16019  16208  16663      7    188    145       O  
ATOM    772  CB  CYS A 101       0.086  21.380  11.685  1.00106.05           C  
ANISOU  772  CB  CYS A 101    13135  13293  13865     26    262    207       C  
ATOM    773  SG  CYS A 101       0.433  21.877  13.388  1.00115.64           S  
ANISOU  773  SG  CYS A 101    14387  14474  15078     24    289    165       S  
ATOM    774  N   PHE A 102      -0.729  18.393  11.443  1.00 93.63           N  
ANISOU  774  N   PHE A 102    11541  11783  12249     25    192    216       N  
ATOM    775  CA  PHE A 102      -1.220  17.121  11.924  1.00 95.94           C  
ANISOU  775  CA  PHE A 102    11835  12093  12526     26    171    213       C  
ATOM    776  C   PHE A 102      -0.261  15.959  11.677  1.00 79.93           C  
ANISOU  776  C   PHE A 102     9809  10091  10469     12    133    186       C  
ATOM    777  O   PHE A 102       0.114  15.248  12.608  1.00 65.01           O  
ANISOU  777  O   PHE A 102     7936   8203   8562      8    123    157       O  
ATOM    778  CB  PHE A 102      -2.547  16.793  11.246  1.00115.47           C  
ANISOU  778  CB  PHE A 102    14283  14580  15012     37    167    259       C  
ATOM    779  CG  PHE A 102      -3.716  17.498  11.840  1.00135.80           C  
ANISOU  779  CG  PHE A 102    16855  17130  17612     54    203    287       C  
ATOM    780  CD1 PHE A 102      -3.747  17.814  13.205  1.00145.72           C  
ANISOU  780  CD1 PHE A 102    18135  18360  18870     61    228    265       C  
ATOM    781  CD2 PHE A 102      -4.817  17.810  11.047  1.00154.66           C  
ANISOU  781  CD2 PHE A 102    19218  19525  20022     65    211    336       C  
ATOM    782  CE1 PHE A 102      -4.839  18.453  13.756  1.00161.60           C  
ANISOU  782  CE1 PHE A 102    20147  20348  20906     79    263    291       C  
ATOM    783  CE2 PHE A 102      -5.917  18.446  11.597  1.00176.11           C  
ANISOU  783  CE2 PHE A 102    21931  22219  22764     83    245    364       C  
ATOM    784  CZ  PHE A 102      -5.925  18.775  12.952  1.00177.60           C  
ANISOU  784  CZ  PHE A 102    22146  22379  22956     91    272    342       C  
ATOM    785  N   LEU A 103       0.124  15.778  10.417  1.00 69.67           N  
ANISOU  785  N   LEU A 103     8494   8813   9164      3    112    196       N  
ATOM    786  CA  LEU A 103       0.911  14.643  10.034  1.00 68.13           C  
ANISOU  786  CA  LEU A 103     8300   8644   8944     -9     78    175       C  
ATOM    787  C   LEU A 103       2.182  14.596  10.878  1.00 69.85           C  
ANISOU  787  C   LEU A 103     8539   8854   9146    -18     75    131       C  
ATOM    788  O   LEU A 103       2.741  13.537  11.152  1.00 69.90           O  
ANISOU  788  O   LEU A 103     8552   8875   9131    -24     52    109       O  
ATOM    789  CB  LEU A 103       1.259  14.726   8.558  1.00 78.12           C  
ANISOU  789  CB  LEU A 103     9547   9928  10206    -16     63    190       C  
ATOM    790  CG  LEU A 103       0.143  14.647   7.504  1.00 88.22           C  
ANISOU  790  CG  LEU A 103    10802  11223  11495    -11     58    233       C  
ATOM    791  CD1 LEU A 103       0.639  15.318   6.232  1.00 98.94           C  
ANISOU  791  CD1 LEU A 103    12148  12590  12856    -16     57    247       C  
ATOM    792  CD2 LEU A 103      -0.328  13.228   7.189  1.00 90.52           C  
ANISOU  792  CD2 LEU A 103    11085  11540  11768    -16     28    238       C  
ATOM    793  N   GLN A 104       2.631  15.757  11.322  1.00 72.44           N  
ANISOU  793  N   GLN A 104     8880   9159   9487    -18    100    120       N  
ATOM    794  CA  GLN A 104       3.808  15.841  12.177  1.00 73.13           C  
ANISOU  794  CA  GLN A 104     8987   9239   9561    -28     99     79       C  
ATOM    795  C   GLN A 104       3.596  15.111  13.497  1.00 64.58           C  
ANISOU  795  C   GLN A 104     7920   8153   8464    -25     96     60       C  
ATOM    796  O   GLN A 104       4.549  14.654  14.093  1.00 65.21           O  
ANISOU  796  O   GLN A 104     8012   8239   8525    -34     83     29       O  
ATOM    797  CB  GLN A 104       4.173  17.308  12.431  1.00 82.68           C  
ANISOU  797  CB  GLN A 104    10207  10420  10789    -30    129     72       C  
ATOM    798  CG  GLN A 104       5.646  17.538  12.720  1.00 93.34           C  
ANISOU  798  CG  GLN A 104    11570  11769  12127    -46    122     36       C  
ATOM    799  CD  GLN A 104       5.869  18.422  13.918  1.00104.97           C  
ANISOU  799  CD  GLN A 104    13066  13214  13605    -49    147     12       C  
ATOM    800  NE2 GLN A 104       4.872  19.237  14.234  1.00111.33           N  
ANISOU  800  NE2 GLN A 104    13874  13993  14431    -37    179     30       N  
ATOM    801  OE1 GLN A 104       6.911  18.353  14.574  1.00111.19           O  
ANISOU  801  OE1 GLN A 104    13868  14002  14378    -62    138    -22       O  
ATOM    802  N   HIS A 105       2.347  14.984  13.939  1.00 62.38           N  
ANISOU  802  N   HIS A 105     7640   7867   8196    -11    109     81       N  
ATOM    803  CA  HIS A 105       2.043  14.275  15.181  1.00 66.12           C  
ANISOU  803  CA  HIS A 105     8127   8338   8657     -6    109     67       C  
ATOM    804  C   HIS A 105       1.683  12.813  15.047  1.00 70.12           C  
ANISOU  804  C   HIS A 105     8625   8869   9149     -4     82     73       C  
ATOM    805  O   HIS A 105       1.221  12.223  16.024  1.00 74.64           O  
ANISOU  805  O   HIS A 105     9206   9439   9715      2     84     69       O  
ATOM    806  CB  HIS A 105       0.888  14.924  15.903  1.00 73.07           C  
ANISOU  806  CB  HIS A 105     9013   9195   9556      9    141     85       C  
ATOM    807  CG  HIS A 105       1.197  16.281  16.419  1.00 84.55           C  
ANISOU  807  CG  HIS A 105    10483  10620  11021      8    173     72       C  
ATOM    808  CD2 HIS A 105       1.737  16.688  17.590  1.00 88.96           C  
ANISOU  808  CD2 HIS A 105    11067  11161  11571      4    187     39       C  
ATOM    809  ND1 HIS A 105       0.936  17.423  15.690  1.00 99.97           N  
ANISOU  809  ND1 HIS A 105    12428  12557  12999     12    195     93       N  
ATOM    810  CE1 HIS A 105       1.311  18.479  16.389  1.00100.18           C  
ANISOU  810  CE1 HIS A 105    12474  12556  13032      9    222     74       C  
ATOM    811  NE2 HIS A 105       1.793  18.060  17.549  1.00 98.65           N  
ANISOU  811  NE2 HIS A 105    12302  12362  12818      4    217     40       N  
ATOM    812  N   LYS A 106       1.861  12.228  13.865  1.00 69.81           N  
ANISOU  812  N   LYS A 106     8569   8852   9105    -11     58     84       N  
ATOM    813  CA  LYS A 106       1.700  10.792  13.692  1.00 64.84           C  
ANISOU  813  CA  LYS A 106     7932   8245   8460    -13     31     85       C  
ATOM    814  C   LYS A 106       2.749  10.056  14.520  1.00 66.41           C  
ANISOU  814  C   LYS A 106     8146   8449   8636    -19     17     50       C  
ATOM    815  O   LYS A 106       3.956  10.228  14.315  1.00 63.78           O  
ANISOU  815  O   LYS A 106     7819   8122   8294    -29      8     28       O  
ATOM    816  CB  LYS A 106       1.821  10.391  12.212  1.00 68.33           C  
ANISOU  816  CB  LYS A 106     8355   8707   8899    -20      9    100       C  
ATOM    817  CG  LYS A 106       0.599  10.753  11.398  1.00 75.53           C  
ANISOU  817  CG  LYS A 106     9248   9620   9829    -14     16    140       C  
ATOM    818  CD  LYS A 106       0.435   9.965  10.105  1.00 83.75           C  
ANISOU  818  CD  LYS A 106    10272  10687  10862    -22    -10    155       C  
ATOM    819  CE  LYS A 106      -1.018  10.064   9.627  1.00 92.08           C  
ANISOU  819  CE  LYS A 106    11307  11745  11934    -15     -5    196       C  
ATOM    820  NZ  LYS A 106      -1.262   9.372   8.340  1.00104.53           N1+
ANISOU  820  NZ  LYS A 106    12867  13347  13502    -25    -30    212       N1+
ATOM    821  N   ASP A 107       2.273   9.239  15.457  1.00 75.87           N  
ANISOU  821  N   ASP A 107     9352   9649   9828    -12     15     46       N  
ATOM    822  CA  ASP A 107       3.137   8.417  16.321  1.00 86.51           C  
ANISOU  822  CA  ASP A 107    10712  11004  11153    -16      1     17       C  
ATOM    823  C   ASP A 107       3.541   7.062  15.669  1.00 77.37           C  
ANISOU  823  C   ASP A 107     9545   9870   9981    -22    -28     14       C  
ATOM    824  O   ASP A 107       2.754   6.107  15.557  1.00 59.17           O  
ANISOU  824  O   ASP A 107     7233   7573   7677    -17    -37     29       O  
ATOM    825  CB  ASP A 107       2.466   8.197  17.688  1.00104.89           C  
ANISOU  825  CB  ASP A 107    13052  13322  13480     -5     15     15       C  
ATOM    826  CG  ASP A 107       3.429   7.669  18.734  1.00125.13           C  
ANISOU  826  CG  ASP A 107    15631  15891  16020     -8      7    -15       C  
ATOM    827  OD1 ASP A 107       4.521   7.179  18.341  1.00144.86           O  
ANISOU  827  OD1 ASP A 107    18128  18406  18506    -18    -14    -32       O  
ATOM    828  OD2 ASP A 107       3.093   7.747  19.946  1.00132.15           O1-
ANISOU  828  OD2 ASP A 107    16535  16771  16907      0     21    -22       O1-
ATOM    829  N   ASP A 108       4.800   7.011  15.252  1.00 78.43           N  
ANISOU  829  N   ASP A 108     9681  10014  10104    -32    -41     -5       N  
ATOM    830  CA  ASP A 108       5.378   5.841  14.605  1.00 82.52           C  
ANISOU  830  CA  ASP A 108    10193  10552  10608    -38    -66    -11       C  
ATOM    831  C   ASP A 108       5.558   4.693  15.578  1.00 81.68           C  
ANISOU  831  C   ASP A 108    10095  10453  10488    -34    -75    -24       C  
ATOM    832  O   ASP A 108       5.863   3.557  15.181  1.00 78.03           O  
ANISOU  832  O   ASP A 108     9628  10004  10015    -37    -93    -27       O  
ATOM    833  CB  ASP A 108       6.728   6.208  13.993  1.00 91.33           C  
ANISOU  833  CB  ASP A 108    11310  11676  11717    -49    -73    -27       C  
ATOM    834  CG  ASP A 108       6.598   6.734  12.590  1.00101.98           C  
ANISOU  834  CG  ASP A 108    12646  13028  13076    -53    -74    -10       C  
ATOM    835  OD1 ASP A 108       6.327   5.886  11.695  1.00110.24           O  
ANISOU  835  OD1 ASP A 108    13681  14087  14116    -55    -90      1       O  
ATOM    836  OD2 ASP A 108       6.774   7.968  12.382  1.00 95.65           O1-
ANISOU  836  OD2 ASP A 108    11843  12215  12285    -55    -60     -8       O1-
ATOM    837  N   ASN A 109       5.370   4.995  16.857  1.00 76.65           N  
ANISOU  837  N   ASN A 109     9470   9805   9850    -28    -61    -32       N  
ATOM    838  CA  ASN A 109       5.491   3.996  17.876  1.00 75.91           C  
ANISOU  838  CA  ASN A 109     9384   9717   9742    -22    -67    -43       C  
ATOM    839  C   ASN A 109       4.576   4.322  19.052  1.00 75.67           C  
ANISOU  839  C   ASN A 109     9363   9672   9716    -11    -48    -37       C  
ATOM    840  O   ASN A 109       5.036   4.795  20.083  1.00 84.77           O  
ANISOU  840  O   ASN A 109    10530  10819  10860    -11    -38    -55       O  
ATOM    841  CB  ASN A 109       6.949   3.974  18.285  1.00 75.48           C  
ANISOU  841  CB  ASN A 109     9337   9671   9670    -30    -76    -69       C  
ATOM    842  CG  ASN A 109       7.214   3.061  19.437  1.00 77.33           C  
ANISOU  842  CG  ASN A 109     9580   9913   9890    -24    -81    -80       C  
ATOM    843  ND2 ASN A 109       6.332   2.073  19.636  1.00 84.97           N  
ANISOU  843  ND2 ASN A 109    10543  10882  10859    -15    -84    -66       N  
ATOM    844  OD1 ASN A 109       8.198   3.243  20.154  1.00 68.08           O  
ANISOU  844  OD1 ASN A 109     8416   8746   8704    -29    -84   -100       O  
ATOM    845  N   PRO A 110       3.267   4.099  18.901  1.00 72.17           N  
ANISOU  845  N   PRO A 110     8911   9223   9287     -3    -41    -12       N  
ATOM    846  CA  PRO A 110       2.382   4.528  19.982  1.00 75.21           C  
ANISOU  846  CA  PRO A 110     9305   9592   9678      9    -19     -5       C  
ATOM    847  C   PRO A 110       2.397   3.596  21.193  1.00 81.46           C  
ANISOU  847  C   PRO A 110    10106  10389  10455     17    -21    -14       C  
ATOM    848  O   PRO A 110       2.686   2.381  21.053  1.00 71.66           O  
ANISOU  848  O   PRO A 110     8859   9162   9205     15    -40    -16       O  
ATOM    849  CB  PRO A 110       0.993   4.578  19.328  1.00 72.57           C  
ANISOU  849  CB  PRO A 110     8955   9251   9365     15    -12     28       C  
ATOM    850  CG  PRO A 110       1.095   3.692  18.139  1.00 73.41           C  
ANISOU  850  CG  PRO A 110     9047   9375   9471      7    -36     35       C  
ATOM    851  CD  PRO A 110       2.530   3.664  17.705  1.00 75.49           C  
ANISOU  851  CD  PRO A 110     9314   9649   9718     -5    -51     11       C  
ATOM    852  N   ASN A 111       2.090   4.169  22.367  1.00 82.73           N  
ANISOU  852  N   ASN A 111    10282  10537  10615     25     -1    -19       N  
ATOM    853  CA  ASN A 111       1.878   3.367  23.559  1.00 87.94           C  
ANISOU  853  CA  ASN A 111    10951  11200  11262     35      1    -23       C  
ATOM    854  C   ASN A 111       0.546   2.631  23.567  1.00 87.05           C  
ANISOU  854  C   ASN A 111    10828  11085  11164     47      5      5       C  
ATOM    855  O   ASN A 111      -0.359   2.898  24.364  1.00 85.32           O  
ANISOU  855  O   ASN A 111    10614  10853  10951     59     26     17       O  
ATOM    856  CB  ASN A 111       2.101   4.180  24.823  1.00 96.31           C  
ANISOU  856  CB  ASN A 111    12033  12250  12312     38     21    -40       C  
ATOM    857  CG  ASN A 111       3.524   4.034  25.316  1.00110.72           C  
ANISOU  857  CG  ASN A 111    13868  14089  14112     28      6    -70       C  
ATOM    858  ND2 ASN A 111       3.729   3.208  26.343  1.00110.48           N  
ANISOU  858  ND2 ASN A 111    13845  14070  14064     34      2    -77       N  
ATOM    859  OD1 ASN A 111       4.439   4.609  24.740  1.00135.34           O  
ANISOU  859  OD1 ASN A 111    16986  17211  17228     15     -1    -84       O  
ATOM    860  N   LEU A 112       0.465   1.647  22.689  1.00 83.10           N  
ANISOU  860  N   LEU A 112    10311  10595  10667     42    -15     15       N  
ATOM    861  CA  LEU A 112      -0.716   0.834  22.628  1.00 82.91           C  
ANISOU  861  CA  LEU A 112    10276  10571  10656     50    -15     41       C  
ATOM    862  C   LEU A 112      -0.383  -0.606  22.998  1.00 89.05           C  
ANISOU  862  C   LEU A 112    11052  11360  11421     52    -31     34       C  
ATOM    863  O   LEU A 112       0.436  -1.281  22.325  1.00 88.22           O  
ANISOU  863  O   LEU A 112    10943  11269  11308     42    -51     24       O  
ATOM    864  CB  LEU A 112      -1.368   0.914  21.248  1.00 75.36           C  
ANISOU  864  CB  LEU A 112     9300   9615   9717     43    -22     63       C  
ATOM    865  CG  LEU A 112      -1.788   2.311  20.848  1.00 63.01           C  
ANISOU  865  CG  LEU A 112     7734   8038   8168     44     -5     74       C  
ATOM    866  CD1 LEU A 112      -1.918   2.399  19.354  1.00 65.12           C  
ANISOU  866  CD1 LEU A 112     7983   8313   8445     33    -19     88       C  
ATOM    867  CD2 LEU A 112      -3.079   2.683  21.499  1.00 58.01           C  
ANISOU  867  CD2 LEU A 112     7100   7391   7552     58     19     98       C  
ATOM    868  N   PRO A 113      -1.012  -1.069  24.087  1.00 82.81           N  
ANISOU  868  N   PRO A 113    10267  10567  10631     65    -19     42       N  
ATOM    869  CA  PRO A 113      -1.128  -2.464  24.395  1.00 80.33           C  
ANISOU  869  CA  PRO A 113     9949  10260  10313     69    -30     47       C  
ATOM    870  C   PRO A 113      -0.947  -3.341  23.168  1.00 76.60           C  
ANISOU  870  C   PRO A 113     9462   9798   9846     57    -53     50       C  
ATOM    871  O   PRO A 113      -1.602  -3.147  22.149  1.00 60.31           O  
ANISOU  871  O   PRO A 113     7386   7732   7797     50    -56     66       O  
ATOM    872  CB  PRO A 113      -2.555  -2.551  24.929  1.00 79.37           C  
ANISOU  872  CB  PRO A 113     9821  10127  10207     82    -13     73       C  
ATOM    873  CG  PRO A 113      -2.907  -1.145  25.363  1.00 79.46           C  
ANISOU  873  CG  PRO A 113     9843  10125  10224     88     11     75       C  
ATOM    874  CD  PRO A 113      -1.719  -0.275  25.097  1.00 77.16           C  
ANISOU  874  CD  PRO A 113     9562   9837   9920     78      7     49       C  
ATOM    875  N   ARG A 114      -0.004  -4.262  23.280  1.00 89.74           N  
ANISOU  875  N   ARG A 114    11129  11472  11495     55    -67     34       N  
ATOM    876  CA  ARG A 114       0.185  -5.292  22.280  1.00105.49           C  
ANISOU  876  CA  ARG A 114    13114  13475  13492     45    -86     35       C  
ATOM    877  C   ARG A 114      -1.182  -5.928  22.043  1.00101.95           C  
ANISOU  877  C   ARG A 114    12653  13020  13063     47    -84     61       C  
ATOM    878  O   ARG A 114      -1.901  -6.336  22.960  1.00 94.53           O  
ANISOU  878  O   ARG A 114    11713  12074  12128     59    -74     73       O  
ATOM    879  CB  ARG A 114       1.225  -6.341  22.733  1.00113.63           C  
ANISOU  879  CB  ARG A 114    14150  14516  14507     47    -95     19       C  
ATOM    880  CG  ARG A 114       2.417  -6.531  21.785  1.00119.27           C  
ANISOU  880  CG  ARG A 114    14863  15240  15212     35   -111      3       C  
ATOM    881  CD  ARG A 114       2.111  -7.456  20.609  1.00126.14           C  
ANISOU  881  CD  ARG A 114    15724  16112  16092     25   -124     10       C  
ATOM    882  NE  ARG A 114       3.304  -7.841  19.850  1.00123.64           N  
ANISOU  882  NE  ARG A 114    15409  15805  15765     17   -137     -7       N  
ATOM    883  CZ  ARG A 114       3.291  -8.608  18.755  1.00124.13           C  
ANISOU  883  CZ  ARG A 114    15465  15868  15830      7   -149     -6       C  
ATOM    884  NH1 ARG A 114       2.152  -9.082  18.260  1.00117.18           N1+
ANISOU  884  NH1 ARG A 114    14577  14981  14963      2   -151     10       N1+
ATOM    885  NH2 ARG A 114       4.429  -8.904  18.139  1.00126.31           N  
ANISOU  885  NH2 ARG A 114    15744  16152  16096      1   -157    -21       N  
ATOM    886  N   LEU A 115      -1.571  -5.953  20.793  1.00102.40           N  
ANISOU  886  N   LEU A 115    12699  13079  13131     35    -95     70       N  
ATOM    887  CA  LEU A 115      -2.861  -6.468  20.463  1.00106.76           C  
ANISOU  887  CA  LEU A 115    13238  13627  13701     33    -96     95       C  
ATOM    888  C   LEU A 115      -2.823  -8.000  20.684  1.00112.67           C  
ANISOU  888  C   LEU A 115    13984  14376  14448     33   -105     93       C  
ATOM    889  O   LEU A 115      -2.164  -8.728  19.918  1.00 97.43           O  
ANISOU  889  O   LEU A 115    12054  12453  12511     22   -121     80       O  
ATOM    890  CB  LEU A 115      -3.179  -6.023  19.034  1.00102.62           C  
ANISOU  890  CB  LEU A 115    12701  13106  13184     18   -107    104       C  
ATOM    891  CG  LEU A 115      -4.336  -6.613  18.247  1.00100.37           C  
ANISOU  891  CG  LEU A 115    12399  12822  12915      9   -117    127       C  
ATOM    892  CD1 LEU A 115      -5.668  -6.509  18.974  1.00 98.17           C  
ANISOU  892  CD1 LEU A 115    12111  12533  12655     20   -102    154       C  
ATOM    893  CD2 LEU A 115      -4.382  -5.880  16.907  1.00 94.82           C  
ANISOU  893  CD2 LEU A 115    11688  12126  12215     -5   -126    132       C  
ATOM    894  N   VAL A 116      -3.469  -8.467  21.769  1.00114.16           N  
ANISOU  894  N   VAL A 116    14174  14559  14643     47    -93    105       N  
ATOM    895  CA  VAL A 116      -3.630  -9.932  22.026  1.00113.80           C  
ANISOU  895  CA  VAL A 116    14125  14513  14601     48    -99    108       C  
ATOM    896  C   VAL A 116      -4.733 -10.573  21.180  1.00112.05           C  
ANISOU  896  C   VAL A 116    13887  14287  14398     37   -108    128       C  
ATOM    897  O   VAL A 116      -5.783  -9.952  20.969  1.00126.98           O  
ANISOU  897  O   VAL A 116    15768  16175  16305     36   -103    149       O  
ATOM    898  CB  VAL A 116      -3.922 -10.283  23.523  1.00107.87           C  
ANISOU  898  CB  VAL A 116    13380  13756  13850     68    -82    115       C  
ATOM    899  CG1 VAL A 116      -5.272  -9.742  24.022  1.00115.52           C  
ANISOU  899  CG1 VAL A 116    14342  14716  14836     77    -66    141       C  
ATOM    900  CG2 VAL A 116      -3.866 -11.788  23.735  1.00 97.93           C  
ANISOU  900  CG2 VAL A 116    12119  12497  12594     69    -88    117       C  
ATOM    901  N   ARG A 117      -4.511 -11.799  20.702  1.00103.87           N  
ANISOU  901  N   ARG A 117    12850  13252  13363     27   -120    122       N  
ATOM    902  CA  ARG A 117      -5.592 -12.532  20.034  1.00113.00           C  
ANISOU  902  CA  ARG A 117    13993  14405  14537     14   -129    139       C  
ATOM    903  C   ARG A 117      -6.102 -13.698  20.894  1.00114.84           C  
ANISOU  903  C   ARG A 117    14223  14629  14781     23   -122    150       C  
ATOM    904  O   ARG A 117      -5.302 -14.454  21.445  1.00121.14           O  
ANISOU  904  O   ARG A 117    15031  15426  15570     31   -120    136       O  
ATOM    905  CB  ARG A 117      -5.178 -12.996  18.653  1.00110.17           C  
ANISOU  905  CB  ARG A 117    13634  14052  14174     -7   -149    127       C  
ATOM    906  CG  ARG A 117      -3.919 -13.807  18.630  1.00106.39           C  
ANISOU  906  CG  ARG A 117    13167  13575  13680     -7   -153    102       C  
ATOM    907  CD  ARG A 117      -3.405 -13.787  17.223  1.00115.45           C  
ANISOU  907  CD  ARG A 117    14317  14730  14819    -26   -169     88       C  
ATOM    908  NE  ARG A 117      -3.109 -15.129  16.728  1.00133.52           N  
ANISOU  908  NE  ARG A 117    16610  17015  17107    -37   -177     76       N  
ATOM    909  CZ  ARG A 117      -2.602 -15.371  15.518  1.00150.19           C  
ANISOU  909  CZ  ARG A 117    18724  19131  19209    -54   -190     62       C  
ATOM    910  NH1 ARG A 117      -2.325 -14.354  14.696  1.00159.27           N1+
ANISOU  910  NH1 ARG A 117    19875  20292  20350    -61   -197     58       N1+
ATOM    911  NH2 ARG A 117      -2.349 -16.625  15.127  1.00139.93           N  
ANISOU  911  NH2 ARG A 117    17432  17826  17910    -62   -195     51       N  
ATOM    912  N   PRO A 118      -7.437 -13.828  21.032  1.00107.71           N  
ANISOU  912  N   PRO A 118    13306  13720  13899     23   -118    177       N  
ATOM    913  CA  PRO A 118      -8.014 -14.802  21.950  1.00106.24           C  
ANISOU  913  CA  PRO A 118    13117  13525  13726     33   -108    190       C  
ATOM    914  C   PRO A 118      -8.036 -16.196  21.339  1.00101.87           C  
ANISOU  914  C   PRO A 118    12560  12967  13179     18   -121    185       C  
ATOM    915  O   PRO A 118      -7.660 -16.371  20.178  1.00 91.59           O  
ANISOU  915  O   PRO A 118    11259  11670  11871     -2   -138    172       O  
ATOM    916  CB  PRO A 118      -9.457 -14.287  22.158  1.00111.00           C  
ANISOU  916  CB  PRO A 118    13703  14122  14349     37   -100    222       C  
ATOM    917  CG  PRO A 118      -9.618 -13.087  21.263  1.00105.76           C  
ANISOU  917  CG  PRO A 118    13035  13466  13684     27   -106    225       C  
ATOM    918  CD  PRO A 118      -8.490 -13.125  20.280  1.00105.95           C  
ANISOU  918  CD  PRO A 118    13068  13499  13690     12   -123    198       C  
ATOM    919  N   GLU A 119      -8.505 -17.171  22.107  1.00 99.49           N  
ANISOU  919  N   GLU A 119    12256  12656  12891     26   -113    197       N  
ATOM    920  CA  GLU A 119      -8.565 -18.537  21.611  1.00104.21           C  
ANISOU  920  CA  GLU A 119    12851  13246  13497     12   -122    193       C  
ATOM    921  C   GLU A 119      -9.370 -18.550  20.326  1.00101.15           C  
ANISOU  921  C   GLU A 119    12451  12861  13121    -15   -140    200       C  
ATOM    922  O   GLU A 119     -10.129 -17.625  20.014  1.00 90.30           O  
ANISOU  922  O   GLU A 119    11065  11492  11752    -19   -143    217       O  
ATOM    923  CB  GLU A 119      -9.197 -19.499  22.616  1.00115.60           C  
ANISOU  923  CB  GLU A 119    14288  14677  14957     24   -109    211       C  
ATOM    924  CG  GLU A 119      -9.249 -19.026  24.059  1.00121.67           C  
ANISOU  924  CG  GLU A 119    15060  15446  15723     52    -88    222       C  
ATOM    925  CD  GLU A 119     -10.045 -19.983  24.935  1.00132.85           C  
ANISOU  925  CD  GLU A 119    16469  16850  17160     62    -75    244       C  
ATOM    926  OE1 GLU A 119      -9.443 -20.940  25.482  1.00140.66           O  
ANISOU  926  OE1 GLU A 119    17464  17834  18145     71    -69    237       O  
ATOM    927  OE2 GLU A 119     -11.280 -19.775  25.070  1.00121.04           O1-
ANISOU  927  OE2 GLU A 119    14957  15349  15683     62    -70    271       O1-
ATOM    928  N   VAL A 120      -9.232 -19.627  19.583  1.00106.20           N  
ANISOU  928  N   VAL A 120    13093  13495  13763    -34   -152    189       N  
ATOM    929  CA  VAL A 120      -9.712 -19.604  18.223  1.00102.88           C  
ANISOU  929  CA  VAL A 120    12664  13080  13345    -62   -172    188       C  
ATOM    930  C   VAL A 120     -11.226 -19.677  18.119  1.00 99.65           C  
ANISOU  930  C   VAL A 120    12234  12669  12960    -72   -176    219       C  
ATOM    931  O   VAL A 120     -11.807 -18.944  17.310  1.00103.52           O  
ANISOU  931  O   VAL A 120    12712  13169  13450    -86   -189    229       O  
ATOM    932  CB  VAL A 120      -9.041 -20.688  17.405  1.00 99.77           C  
ANISOU  932  CB  VAL A 120    12282  12682  12945    -80   -183    164       C  
ATOM    933  CG1 VAL A 120      -9.456 -20.555  15.953  1.00 97.85           C  
ANISOU  933  CG1 VAL A 120    12033  12447  12698   -110   -205    161       C  
ATOM    934  CG2 VAL A 120      -7.527 -20.561  17.579  1.00101.70           C  
ANISOU  934  CG2 VAL A 120    12546  12930  13167    -66   -177    137       C  
ATOM    935  N   ASP A 121     -11.862 -20.537  18.925  1.00101.17           N  
ANISOU  935  N   ASP A 121    12420  12848  13172    -66   -166    234       N  
ATOM    936  CA  ASP A 121     -13.321 -20.574  18.946  1.00110.51           C  
ANISOU  936  CA  ASP A 121    13580  14029  14379    -74   -168    266       C  
ATOM    937  C   ASP A 121     -13.851 -19.174  19.136  1.00102.22           C  
ANISOU  937  C   ASP A 121    12519  12988  13330    -62   -162    287       C  
ATOM    938  O   ASP A 121     -14.801 -18.766  18.457  1.00 89.76           O  
ANISOU  938  O   ASP A 121    10923  11418  11764    -77   -174    308       O  
ATOM    939  CB  ASP A 121     -13.862 -21.475  20.055  1.00119.36           C  
ANISOU  939  CB  ASP A 121    14697  15135  15521    -60   -152    283       C  
ATOM    940  CG  ASP A 121     -13.904 -22.937  19.646  1.00142.43           C  
ANISOU  940  CG  ASP A 121    17620  18043  18453    -80   -160    273       C  
ATOM    941  OD1 ASP A 121     -13.187 -23.725  20.291  1.00162.08           O  
ANISOU  941  OD1 ASP A 121    20122  20522  20940    -67   -148    259       O  
ATOM    942  OD2 ASP A 121     -14.636 -23.300  18.684  1.00146.08           O1-
ANISOU  942  OD2 ASP A 121    18070  18507  18925   -109   -178    278       O1-
ATOM    943  N   VAL A 122     -13.203 -18.439  20.037  1.00 98.18           N  
ANISOU  943  N   VAL A 122    12020  12478  12807    -35   -145    282       N  
ATOM    944  CA  VAL A 122     -13.697 -17.123  20.457  1.00 96.97           C  
ANISOU  944  CA  VAL A 122    11858  12329  12656    -20   -133    302       C  
ATOM    945  C   VAL A 122     -13.742 -16.140  19.274  1.00 97.78           C  
ANISOU  945  C   VAL A 122    11955  12446  12751    -36   -148    302       C  
ATOM    946  O   VAL A 122     -14.742 -15.422  19.065  1.00 72.84           O  
ANISOU  946  O   VAL A 122     8778   9291   9606    -37   -147    330       O  
ATOM    947  CB  VAL A 122     -12.875 -16.549  21.639  1.00 85.98           C  
ANISOU  947  CB  VAL A 122    10483  10935  11248      9   -111    291       C  
ATOM    948  CG1 VAL A 122     -13.454 -15.229  22.103  1.00 75.99           C  
ANISOU  948  CG1 VAL A 122     9213   9673   9989     25    -96    312       C  
ATOM    949  CG2 VAL A 122     -12.845 -17.548  22.792  1.00 96.68           C  
ANISOU  949  CG2 VAL A 122    11843  12279  12610     25    -97    294       C  
ATOM    950  N   MET A 123     -12.661 -16.139  18.492  1.00102.90           N  
ANISOU  950  N   MET A 123    12618  13102  13379    -47   -161    272       N  
ATOM    951  CA  MET A 123     -12.552 -15.293  17.303  1.00 96.66           C  
ANISOU  951  CA  MET A 123    11824  12325  12579    -63   -176    269       C  
ATOM    952  C   MET A 123     -13.578 -15.753  16.276  1.00 97.87           C  
ANISOU  952  C   MET A 123    11957  12484  12744    -90   -196    286       C  
ATOM    953  O   MET A 123     -14.271 -14.940  15.658  1.00 90.45           O  
ANISOU  953  O   MET A 123    11001  11554  11810    -98   -203    307       O  
ATOM    954  CB  MET A 123     -11.147 -15.399  16.704  1.00 95.91           C  
ANISOU  954  CB  MET A 123    11748  12235  12458    -69   -185    233       C  
ATOM    955  CG  MET A 123     -10.020 -15.125  17.686  1.00 94.71           C  
ANISOU  955  CG  MET A 123    11615  12078  12291    -46   -168    213       C  
ATOM    956  SD  MET A 123      -8.426 -15.256  16.892  1.00 94.02           S  
ANISOU  956  SD  MET A 123    11548  11999  12178    -55   -180    175       S  
ATOM    957  CE  MET A 123      -8.261 -13.577  16.286  1.00100.29           C  
ANISOU  957  CE  MET A 123    12339  12805  12962    -55   -181    178       C  
ATOM    958  N   CYS A 124     -13.673 -17.067  16.101  1.00100.62           N  
ANISOU  958  N   CYS A 124    12307  12825  13098   -105   -205    278       N  
ATOM    959  CA  CYS A 124     -14.618 -17.631  15.144  1.00 95.24           C  
ANISOU  959  CA  CYS A 124    11609  12149  12428   -135   -226    291       C  
ATOM    960  C   CYS A 124     -16.086 -17.451  15.567  1.00 98.22           C  
ANISOU  960  C   CYS A 124    11960  12525  12833   -132   -222    332       C  
ATOM    961  O   CYS A 124     -16.982 -17.447  14.717  1.00 91.92           O  
ANISOU  961  O   CYS A 124    11143  11739  12045   -155   -240    351       O  
ATOM    962  CB  CYS A 124     -14.277 -19.099  14.857  1.00 99.23           C  
ANISOU  962  CB  CYS A 124    12126  12645  12933   -152   -236    268       C  
ATOM    963  SG  CYS A 124     -13.335 -19.364  13.333  1.00 92.32           S  
ANISOU  963  SG  CYS A 124    11267  11780  12030   -180   -258    233       S  
ATOM    964  N   THR A 125     -16.326 -17.301  16.872  1.00103.23           N  
ANISOU  964  N   THR A 125    12594  13149  13481   -104   -198    347       N  
ATOM    965  CA  THR A 125     -17.664 -16.966  17.387  1.00 98.95           C  
ANISOU  965  CA  THR A 125    12027  12605  12965    -96   -188    388       C  
ATOM    966  C   THR A 125     -17.970 -15.483  17.056  1.00100.41           C  
ANISOU  966  C   THR A 125    12201  12802  13147    -89   -185    407       C  
ATOM    967  O   THR A 125     -19.042 -15.133  16.530  1.00 86.83           O  
ANISOU  967  O   THR A 125    10456  11091  11444   -101   -193    439       O  
ATOM    968  CB  THR A 125     -17.769 -17.221  18.929  1.00 92.54           C  
ANISOU  968  CB  THR A 125    11220  11777  12165    -66   -160    398       C  
ATOM    969  CG2 THR A 125     -19.170 -16.958  19.459  1.00 86.28           C  
ANISOU  969  CG2 THR A 125    10401  10981  11400    -58   -148    441       C  
ATOM    970  OG1 THR A 125     -17.424 -18.576  19.240  1.00 91.12           O  
ANISOU  970  OG1 THR A 125    11050  11585  11986    -71   -161    381       O  
ATOM    971  N   ALA A 126     -17.002 -14.617  17.352  1.00101.51           N  
ANISOU  971  N   ALA A 126    12359  12942  13268    -71   -172    389       N  
ATOM    972  CA  ALA A 126     -17.197 -13.179  17.224  1.00 98.40           C  
ANISOU  972  CA  ALA A 126    11958  12555  12874    -60   -163    405       C  
ATOM    973  C   ALA A 126     -17.326 -12.785  15.780  1.00 91.39           C  
ANISOU  973  C   ALA A 126    11059  11686  11980    -85   -187    408       C  
ATOM    974  O   ALA A 126     -17.770 -11.684  15.452  1.00 91.31           O  
ANISOU  974  O   ALA A 126    11035  11684  11975    -81   -183    431       O  
ATOM    975  CB  ALA A 126     -16.043 -12.427  17.864  1.00100.06           C  
ANISOU  975  CB  ALA A 126    12192  12760  13064    -38   -146    380       C  
ATOM    976  N   PHE A 127     -16.915 -13.678  14.904  1.00 93.46           N  
ANISOU  976  N   PHE A 127    11327  11954  12230   -110   -211    386       N  
ATOM    977  CA  PHE A 127     -17.080 -13.412  13.503  1.00 99.72           C  
ANISOU  977  CA  PHE A 127    12110  12766  13015   -136   -235    389       C  
ATOM    978  C   PHE A 127     -18.558 -13.373  13.181  1.00102.44           C  
ANISOU  978  C   PHE A 127    12421  13118  13382   -149   -244    432       C  
ATOM    979  O   PHE A 127     -19.047 -12.346  12.720  1.00106.32           O  
ANISOU  979  O   PHE A 127    12896  13622  13878   -147   -245    457       O  
ATOM    980  CB  PHE A 127     -16.369 -14.456  12.659  1.00 99.35           C  
ANISOU  980  CB  PHE A 127    12078  12722  12950   -162   -257    356       C  
ATOM    981  CG  PHE A 127     -16.373 -14.146  11.201  1.00 89.35           C  
ANISOU  981  CG  PHE A 127    10804  11476  11669   -188   -282    354       C  
ATOM    982  CD1 PHE A 127     -15.558 -13.141  10.706  1.00 84.69           C  
ANISOU  982  CD1 PHE A 127    10223  10895  11059   -182   -281    342       C  
ATOM    983  CD2 PHE A 127     -17.196 -14.862  10.318  1.00 86.68           C  
ANISOU  983  CD2 PHE A 127    10451  11149  11336   -219   -307    365       C  
ATOM    984  CE1 PHE A 127     -15.562 -12.840   9.354  1.00 86.37           C  
ANISOU  984  CE1 PHE A 127    10430  11129  11258   -205   -303    342       C  
ATOM    985  CE2 PHE A 127     -17.188 -14.567   8.958  1.00 83.23           C  
ANISOU  985  CE2 PHE A 127    10009  10734  10882   -244   -330    364       C  
ATOM    986  CZ  PHE A 127     -16.370 -13.558   8.482  1.00 83.59           C  
ANISOU  986  CZ  PHE A 127    10064  10789  10909   -236   -328    353       C  
ATOM    987  N   HIS A 128     -19.263 -14.468  13.459  1.00110.33           N  
ANISOU  987  N   HIS A 128    13411  14110  14398   -159   -249    441       N  
ATOM    988  CA  HIS A 128     -20.657 -14.618  13.028  1.00125.21           C  
ANISOU  988  CA  HIS A 128    15264  16005  16306   -177   -263    480       C  
ATOM    989  C   HIS A 128     -21.610 -13.747  13.796  1.00119.48           C  
ANISOU  989  C   HIS A 128    14517  15277  15604   -153   -241    522       C  
ATOM    990  O   HIS A 128     -22.669 -13.412  13.271  1.00124.11           O  
ANISOU  990  O   HIS A 128    15073  15876  16206   -165   -251    559       O  
ATOM    991  CB  HIS A 128     -21.103 -16.071  13.120  1.00140.22           C  
ANISOU  991  CB  HIS A 128    17161  17897  18218   -197   -274    476       C  
ATOM    992  CG  HIS A 128     -20.379 -16.956  12.167  1.00167.96           C  
ANISOU  992  CG  HIS A 128    20692  21415  21710   -226   -298    439       C  
ATOM    993  CD2 HIS A 128     -20.569 -17.176  10.845  1.00188.31           C  
ANISOU  993  CD2 HIS A 128    23262  24010  24276   -261   -328    435       C  
ATOM    994  ND1 HIS A 128     -19.270 -17.693  12.527  1.00168.02           N  
ANISOU  994  ND1 HIS A 128    20729  21407  21703   -220   -291    399       N  
ATOM    995  CE1 HIS A 128     -18.829 -18.358  11.473  1.00187.71           C  
ANISOU  995  CE1 HIS A 128    23234  23908  24180   -250   -314    373       C  
ATOM    996  NE2 HIS A 128     -19.597 -18.059  10.441  1.00202.72           N  
ANISOU  996  NE2 HIS A 128    25115  25829  26081   -275   -336    392       N  
ATOM    997  N   ASP A 129     -21.234 -13.384  15.025  1.00109.11           N  
ANISOU  997  N   ASP A 129    13217  13945  14293   -120   -211    518       N  
ATOM    998  CA  ASP A 129     -22.013 -12.446  15.822  1.00108.90           C  
ANISOU  998  CA  ASP A 129    13176  13914  14288    -93   -184    555       C  
ATOM    999  C   ASP A 129     -22.176 -11.105  15.076  1.00104.88           C  
ANISOU  999  C   ASP A 129    12654  13419  13775    -92   -185    574       C  
ATOM   1000  O   ASP A 129     -23.285 -10.700  14.684  1.00 97.91           O  
ANISOU 1000  O   ASP A 129    11741  12548  12913    -98   -189    616       O  
ATOM   1001  CB  ASP A 129     -21.360 -12.234  17.195  1.00110.84           C  
ANISOU 1001  CB  ASP A 129    13445  14140  14529    -60   -153    539       C  
ATOM   1002  CG  ASP A 129     -22.169 -11.275  18.086  1.00118.56           C  
ANISOU 1002  CG  ASP A 129    14410  15109  15527    -31   -122    576       C  
ATOM   1003  OD1 ASP A 129     -22.885 -11.778  18.979  1.00131.75           O  
ANISOU 1003  OD1 ASP A 129    16073  16768  17218    -19   -107    596       O  
ATOM   1004  OD2 ASP A 129     -22.124 -10.032  17.883  1.00107.65           O1-
ANISOU 1004  OD2 ASP A 129    13027  13731  14143    -20   -111    585       O1-
ATOM   1005  N   ASN A 130     -21.053 -10.430  14.872  1.00102.71           N  
ANISOU 1005  N   ASN A 130    12403  13146  13478    -85   -181    545       N  
ATOM   1006  CA  ASN A 130     -21.012  -9.215  14.075  1.00 92.61           C  
ANISOU 1006  CA  ASN A 130    11115  11880  12192    -85   -183    557       C  
ATOM   1007  C   ASN A 130     -19.710  -9.150  13.270  1.00 84.69           C  
ANISOU 1007  C   ASN A 130    10134  10885  11158    -98   -199    515       C  
ATOM   1008  O   ASN A 130     -18.651  -8.811  13.801  1.00 75.08           O  
ANISOU 1008  O   ASN A 130     8944   9658   9926    -82   -184    486       O  
ATOM   1009  CB  ASN A 130     -21.165  -8.003  14.981  1.00 91.78           C  
ANISOU 1009  CB  ASN A 130    11011  11762  12099    -52   -148    575       C  
ATOM   1010  CG  ASN A 130     -21.557  -6.763  14.220  1.00 96.09           C  
ANISOU 1010  CG  ASN A 130    11538  12320  12650    -51   -146    603       C  
ATOM   1011  ND2 ASN A 130     -21.728  -5.661  14.935  1.00 98.95           N  
ANISOU 1011  ND2 ASN A 130    11903  12671  13024    -23   -113    620       N  
ATOM   1012  OD1 ASN A 130     -21.717  -6.795  13.000  1.00 98.55           O  
ANISOU 1012  OD1 ASN A 130    11835  12653  12955    -75   -173    610       O  
ATOM   1013  N   GLU A 131     -19.800  -9.508  11.991  1.00 85.69           N  
ANISOU 1013  N   GLU A 131    10252  11032  11275   -128   -230    514       N  
ATOM   1014  CA  GLU A 131     -18.618  -9.570  11.126  1.00 89.25           C  
ANISOU 1014  CA  GLU A 131    10723  11492  11696   -143   -246    476       C  
ATOM   1015  C   GLU A 131     -18.237  -8.205  10.523  1.00 87.64           C  
ANISOU 1015  C   GLU A 131    10518  11298  11483   -135   -241    482       C  
ATOM   1016  O   GLU A 131     -17.072  -7.977  10.197  1.00 89.31           O  
ANISOU 1016  O   GLU A 131    10751  11510  11671   -135   -243    449       O  
ATOM   1017  CB  GLU A 131     -18.791 -10.631  10.021  1.00 89.30           C  
ANISOU 1017  CB  GLU A 131    10725  11514  11693   -179   -280    467       C  
ATOM   1018  CG  GLU A 131     -19.448 -10.145   8.738  1.00 93.78           C  
ANISOU 1018  CG  GLU A 131    11268  12107  12258   -201   -303    493       C  
ATOM   1019  CD  GLU A 131     -19.326 -11.139   7.596  1.00 97.93           C  
ANISOU 1019  CD  GLU A 131    11797  12648  12765   -238   -336    473       C  
ATOM   1020  OE1 GLU A 131     -19.599 -12.351   7.837  1.00 93.53           O  
ANISOU 1020  OE1 GLU A 131    11242  12083  12214   -252   -345    464       O  
ATOM   1021  OE2 GLU A 131     -18.969 -10.694   6.468  1.00 88.28           O1-
ANISOU 1021  OE2 GLU A 131    10575  11446  11523   -253   -353    468       O1-
ATOM   1022  N   GLU A 132     -19.199  -7.302  10.377  1.00 89.45           N  
ANISOU 1022  N   GLU A 132    10722  11535  11731   -129   -234    524       N  
ATOM   1023  CA  GLU A 132     -18.864  -5.948   9.974  1.00 87.01           C  
ANISOU 1023  CA  GLU A 132    10412  11232  11417   -117   -223    532       C  
ATOM   1024  C   GLU A 132     -17.945  -5.390  11.056  1.00 84.34           C  
ANISOU 1024  C   GLU A 132    10100  10871  11075    -89   -193    507       C  
ATOM   1025  O   GLU A 132     -16.819  -4.981  10.771  1.00 91.99           O  
ANISOU 1025  O   GLU A 132    11089  11839  12023    -88   -193    477       O  
ATOM   1026  CB  GLU A 132     -20.109  -5.083   9.805  1.00 91.08           C  
ANISOU 1026  CB  GLU A 132    10893  11755  11957   -110   -215    586       C  
ATOM   1027  CG  GLU A 132     -21.238  -5.740   9.025  1.00102.61           C  
ANISOU 1027  CG  GLU A 132    12323  13236  13427   -137   -243    617       C  
ATOM   1028  CD  GLU A 132     -21.332  -5.272   7.581  1.00116.10           C  
ANISOU 1028  CD  GLU A 132    14016  14974  15123   -158   -267    632       C  
ATOM   1029  OE1 GLU A 132     -20.385  -5.570   6.808  1.00114.62           O  
ANISOU 1029  OE1 GLU A 132    13847  14796  14908   -175   -285    596       O  
ATOM   1030  OE2 GLU A 132     -22.372  -4.634   7.224  1.00117.13           O1-
ANISOU 1030  OE2 GLU A 132    14114  15119  15272   -157   -266    680       O1-
ATOM   1031  N   THR A 133     -18.399  -5.429  12.304  1.00 78.80           N  
ANISOU 1031  N   THR A 133     9399  10150  10391    -68   -169    518       N  
ATOM   1032  CA  THR A 133     -17.573  -4.986  13.423  1.00 81.08           C  
ANISOU 1032  CA  THR A 133     9714  10418  10673    -42   -142    493       C  
ATOM   1033  C   THR A 133     -16.220  -5.685  13.479  1.00 79.70           C  
ANISOU 1033  C   THR A 133     9569  10241  10473    -49   -152    444       C  
ATOM   1034  O   THR A 133     -15.220  -5.072  13.797  1.00 82.41           O  
ANISOU 1034  O   THR A 133     9933  10577  10803    -37   -139    419       O  
ATOM   1035  CB  THR A 133     -18.275  -5.186  14.774  1.00 78.38           C  
ANISOU 1035  CB  THR A 133     9371  10058  10352    -21   -117    510       C  
ATOM   1036  CG2 THR A 133     -17.304  -4.906  15.954  1.00 74.99           C  
ANISOU 1036  CG2 THR A 133     8973   9610   9911      2    -92    478       C  
ATOM   1037  OG1 THR A 133     -19.401  -4.307  14.850  1.00 70.47           O  
ANISOU 1037  OG1 THR A 133     8345   9056   9375     -9    -99    556       O  
ATOM   1038  N   PHE A 134     -16.192  -6.971  13.186  1.00 89.63           N  
ANISOU 1038  N   PHE A 134    10828  11504  11724    -68   -174    430       N  
ATOM   1039  CA  PHE A 134     -14.969  -7.749  13.374  1.00101.03           C  
ANISOU 1039  CA  PHE A 134    12298  12942  13146    -72   -180    387       C  
ATOM   1040  C   PHE A 134     -13.867  -7.248  12.445  1.00 97.07           C  
ANISOU 1040  C   PHE A 134    11810  12452  12622    -81   -191    361       C  
ATOM   1041  O   PHE A 134     -12.732  -7.041  12.863  1.00 97.96           O  
ANISOU 1041  O   PHE A 134    11945  12557  12719    -70   -182    331       O  
ATOM   1042  CB  PHE A 134     -15.262  -9.233  13.141  1.00108.39           C  
ANISOU 1042  CB  PHE A 134    13228  13877  14080    -92   -201    380       C  
ATOM   1043  CG  PHE A 134     -14.125 -10.151  13.495  1.00110.25           C  
ANISOU 1043  CG  PHE A 134    13489  14104  14297    -92   -203    340       C  
ATOM   1044  CD1 PHE A 134     -13.852 -10.461  14.820  1.00110.95           C  
ANISOU 1044  CD1 PHE A 134    13591  14177  14390    -71   -183    331       C  
ATOM   1045  CD2 PHE A 134     -13.355 -10.736  12.498  1.00112.83           C  
ANISOU 1045  CD2 PHE A 134    13826  14440  14604   -113   -225    313       C  
ATOM   1046  CE1 PHE A 134     -12.822 -11.324  15.141  1.00116.84           C  
ANISOU 1046  CE1 PHE A 134    14357  14916  15120    -71   -185    297       C  
ATOM   1047  CE2 PHE A 134     -12.324 -11.601  12.817  1.00110.45           C  
ANISOU 1047  CE2 PHE A 134    13547  14131  14289   -112   -225    278       C  
ATOM   1048  CZ  PHE A 134     -12.060 -11.895  14.141  1.00112.37           C  
ANISOU 1048  CZ  PHE A 134    13800  14358  14536    -91   -205    272       C  
ATOM   1049  N   LEU A 135     -14.229  -7.025  11.187  1.00 93.07           N  
ANISOU 1049  N   LEU A 135    11287  11963  12112   -100   -211    375       N  
ATOM   1050  CA  LEU A 135     -13.290  -6.547  10.186  1.00 81.21           C  
ANISOU 1050  CA  LEU A 135     9795  10473  10589   -110   -221    356       C  
ATOM   1051  C   LEU A 135     -12.984  -5.088  10.416  1.00 73.75           C  
ANISOU 1051  C   LEU A 135     8851   9523   9647    -91   -200    363       C  
ATOM   1052  O   LEU A 135     -11.833  -4.710  10.331  1.00 72.04           O  
ANISOU 1052  O   LEU A 135     8653   9304   9413    -87   -196    336       O  
ATOM   1053  CB  LEU A 135     -13.829  -6.758   8.784  1.00 86.67           C  
ANISOU 1053  CB  LEU A 135    10468  11187  11276   -137   -249    371       C  
ATOM   1054  CG  LEU A 135     -14.110  -8.229   8.463  1.00101.07           C  
ANISOU 1054  CG  LEU A 135    12291  13014  13095   -160   -271    360       C  
ATOM   1055  CD1 LEU A 135     -15.090  -8.340   7.300  1.00108.58           C  
ANISOU 1055  CD1 LEU A 135    13219  13989  14048   -186   -296    387       C  
ATOM   1056  CD2 LEU A 135     -12.824  -9.011   8.192  1.00106.13           C  
ANISOU 1056  CD2 LEU A 135    12960  13653  13712   -169   -280    315       C  
ATOM   1057  N   LYS A 136     -13.993  -4.283  10.746  1.00 73.68           N  
ANISOU 1057  N   LYS A 136     8824   9512   9661    -78   -184    400       N  
ATOM   1058  CA  LYS A 136     -13.783  -2.856  11.053  1.00 76.79           C  
ANISOU 1058  CA  LYS A 136     9220   9897  10060    -58   -159    409       C  
ATOM   1059  C   LYS A 136     -12.847  -2.635  12.235  1.00 77.05           C  
ANISOU 1059  C   LYS A 136     9279   9909  10086    -38   -137    379       C  
ATOM   1060  O   LYS A 136     -12.089  -1.680  12.258  1.00 84.12           O  
ANISOU 1060  O   LYS A 136    10187  10800  10975    -30   -124    366       O  
ATOM   1061  CB  LYS A 136     -15.095  -2.133  11.325  1.00 80.40           C  
ANISOU 1061  CB  LYS A 136     9653  10351  10545    -45   -142    455       C  
ATOM   1062  CG  LYS A 136     -15.812  -1.683  10.066  1.00 94.30           C  
ANISOU 1062  CG  LYS A 136    11386  12132  12311    -59   -157    489       C  
ATOM   1063  CD  LYS A 136     -16.503  -0.348  10.278  1.00106.29           C  
ANISOU 1063  CD  LYS A 136    12889  13645  13853    -40   -130    527       C  
ATOM   1064  CE  LYS A 136     -16.833   0.308   8.948  1.00115.32           C  
ANISOU 1064  CE  LYS A 136    14010  14810  14996    -52   -143    555       C  
ATOM   1065  NZ  LYS A 136     -17.793  -0.500   8.142  1.00115.55           N1+
ANISOU 1065  NZ  LYS A 136    14013  14862  15028    -74   -173    580       N1+
ATOM   1066  N   LYS A 137     -12.885  -3.527  13.205  1.00 74.60           N  
ANISOU 1066  N   LYS A 137     8979   9589   9777    -32   -133    367       N  
ATOM   1067  CA  LYS A 137     -11.924  -3.502  14.271  1.00 74.38           C  
ANISOU 1067  CA  LYS A 137     8976   9546   9738    -17   -117    337       C  
ATOM   1068  C   LYS A 137     -10.581  -4.002  13.779  1.00 69.45           C  
ANISOU 1068  C   LYS A 137     8370   8929   9089    -30   -134    298       C  
ATOM   1069  O   LYS A 137      -9.562  -3.525  14.223  1.00 73.50           O  
ANISOU 1069  O   LYS A 137     8901   9435   9589    -21   -124    273       O  
ATOM   1070  CB  LYS A 137     -12.378  -4.398  15.407  1.00 93.42           C  
ANISOU 1070  CB  LYS A 137    11391  11947  12158     -8   -109    338       C  
ATOM   1071  CG  LYS A 137     -11.645  -4.163  16.715  1.00107.59           C  
ANISOU 1071  CG  LYS A 137    13209  13726  13944     12    -87    316       C  
ATOM   1072  CD  LYS A 137     -12.263  -2.987  17.463  1.00125.49           C  
ANISOU 1072  CD  LYS A 137    15474  15980  16228     33    -56    337       C  
ATOM   1073  CE  LYS A 137     -11.910  -3.077  18.933  1.00139.15           C  
ANISOU 1073  CE  LYS A 137    17225  17696  17952     52    -35    321       C  
ATOM   1074  NZ  LYS A 137     -12.413  -1.890  19.675  1.00161.79           N1+
ANISOU 1074  NZ  LYS A 137    20094  20547  20831     72     -3    338       N1+
ATOM   1075  N   TYR A 138     -10.564  -4.986  12.895  1.00 63.43           N  
ANISOU 1075  N   TYR A 138     7603   8179   8319    -50   -160    292       N  
ATOM   1076  CA  TYR A 138      -9.311  -5.406  12.317  1.00 62.60           C  
ANISOU 1076  CA  TYR A 138     7514   8081   8190    -62   -174    258       C  
ATOM   1077  C   TYR A 138      -8.594  -4.174  11.745  1.00 62.56           C  
ANISOU 1077  C   TYR A 138     7513   8081   8177    -60   -169    252       C  
ATOM   1078  O   TYR A 138      -7.463  -3.874  12.153  1.00 80.84           O  
ANISOU 1078  O   TYR A 138     9847  10390  10480    -52   -161    225       O  
ATOM   1079  CB  TYR A 138      -9.532  -6.507  11.284  1.00 65.45           C  
ANISOU 1079  CB  TYR A 138     7868   8455   8545    -86   -201    255       C  
ATOM   1080  CG  TYR A 138      -8.342  -6.797  10.407  1.00 74.16           C  
ANISOU 1080  CG  TYR A 138     8986   9567   9625    -99   -216    225       C  
ATOM   1081  CD1 TYR A 138      -7.393  -7.769  10.748  1.00 75.73           C  
ANISOU 1081  CD1 TYR A 138     9203   9761   9811    -99   -218    193       C  
ATOM   1082  CD2 TYR A 138      -8.152  -6.089   9.232  1.00 76.93           C  
ANISOU 1082  CD2 TYR A 138     9330   9932   9966   -110   -225    229       C  
ATOM   1083  CE1 TYR A 138      -6.297  -8.019   9.920  1.00 74.91           C  
ANISOU 1083  CE1 TYR A 138     9112   9665   9687   -110   -230    167       C  
ATOM   1084  CE2 TYR A 138      -7.068  -6.336   8.398  1.00 71.85           C  
ANISOU 1084  CE2 TYR A 138     8701   9298   9302   -121   -237    202       C  
ATOM   1085  CZ  TYR A 138      -6.158  -7.290   8.736  1.00 69.83           C  
ANISOU 1085  CZ  TYR A 138     8463   9035   9034   -121   -239    172       C  
ATOM   1086  OH  TYR A 138      -5.112  -7.448   7.883  1.00 64.96           O  
ANISOU 1086  OH  TYR A 138     7858   8426   8397   -131   -249    148       O  
ATOM   1087  N   LEU A 139      -9.254  -3.423  10.878  1.00 53.96           N  
ANISOU 1087  N   LEU A 139     6406   7001   7096    -66   -173    278       N  
ATOM   1088  CA  LEU A 139      -8.681  -2.172  10.372  1.00 55.46           C  
ANISOU 1088  CA  LEU A 139     6598   7194   7282    -62   -165    277       C  
ATOM   1089  C   LEU A 139      -8.170  -1.295  11.470  1.00 54.01           C  
ANISOU 1089  C   LEU A 139     6428   6992   7102    -42   -138    267       C  
ATOM   1090  O   LEU A 139      -6.986  -0.984  11.538  1.00 53.94           O  
ANISOU 1090  O   LEU A 139     6435   6980   7079    -40   -135    239       O  
ATOM   1091  CB  LEU A 139      -9.689  -1.322   9.613  1.00 54.24           C  
ANISOU 1091  CB  LEU A 139     6418   7048   7141    -64   -164    316       C  
ATOM   1092  CG  LEU A 139     -10.304  -1.978   8.397  1.00 57.59           C  
ANISOU 1092  CG  LEU A 139     6826   7494   7562    -87   -191    332       C  
ATOM   1093  CD1 LEU A 139     -11.271  -0.979   7.765  1.00 56.94           C  
ANISOU 1093  CD1 LEU A 139     6718   7421   7494    -86   -187    374       C  
ATOM   1094  CD2 LEU A 139      -9.251  -2.546   7.429  1.00 56.20           C  
ANISOU 1094  CD2 LEU A 139     6663   7332   7360   -105   -213    301       C  
ATOM   1095  N   TYR A 140      -9.064  -0.869  12.332  1.00 54.78           N  
ANISOU 1095  N   TYR A 140     6519   7077   7219    -26   -118    290       N  
ATOM   1096  CA  TYR A 140      -8.667   0.158  13.293  1.00 63.16           C  
ANISOU 1096  CA  TYR A 140     7594   8121   8284     -8    -90    282       C  
ATOM   1097  C   TYR A 140      -7.430  -0.231  14.149  1.00 67.41           C  
ANISOU 1097  C   TYR A 140     8158   8652   8804     -4    -88    242       C  
ATOM   1098  O   TYR A 140      -6.558   0.597  14.370  1.00 69.52           O  
ANISOU 1098  O   TYR A 140     8438   8913   9064      1    -77    224       O  
ATOM   1099  CB  TYR A 140      -9.858   0.565  14.131  1.00 60.97           C  
ANISOU 1099  CB  TYR A 140     7306   7829   8028      9    -67    312       C  
ATOM   1100  CG  TYR A 140      -9.584   1.051  15.519  1.00 67.36           C  
ANISOU 1100  CG  TYR A 140     8135   8619   8839     28    -40    298       C  
ATOM   1101  CD1 TYR A 140      -9.436   2.406  15.789  1.00 78.45           C  
ANISOU 1101  CD1 TYR A 140     9547  10011  10251     39    -15    301       C  
ATOM   1102  CD2 TYR A 140      -9.561   0.174  16.589  1.00 71.59           C  
ANISOU 1102  CD2 TYR A 140     8681   9148   9369     35    -37    286       C  
ATOM   1103  CE1 TYR A 140      -9.243   2.868  17.092  1.00 76.75           C  
ANISOU 1103  CE1 TYR A 140     9350   9776  10035     56     12    288       C  
ATOM   1104  CE2 TYR A 140      -9.361   0.630  17.880  1.00 78.75           C  
ANISOU 1104  CE2 TYR A 140     9607  10039  10276     52    -12    275       C  
ATOM   1105  CZ  TYR A 140      -9.214   1.981  18.119  1.00 75.88           C  
ANISOU 1105  CZ  TYR A 140     9251   9663   9918     62     12    275       C  
ATOM   1106  OH  TYR A 140      -9.030   2.442  19.388  1.00 81.88           O  
ANISOU 1106  OH  TYR A 140    10030  10405  10674     77     37    262       O  
ATOM   1107  N   GLU A 141      -7.318  -1.480  14.579  1.00 67.29           N  
ANISOU 1107  N   GLU A 141     8149   8639   8781     -7    -99    229       N  
ATOM   1108  CA  GLU A 141      -6.214  -1.850  15.453  1.00 68.13           C  
ANISOU 1108  CA  GLU A 141     8276   8740   8871     -1    -96    195       C  
ATOM   1109  C   GLU A 141      -4.907  -1.880  14.701  1.00 69.43           C  
ANISOU 1109  C   GLU A 141     8450   8914   9017    -13   -111    168       C  
ATOM   1110  O   GLU A 141      -3.863  -1.479  15.233  1.00 74.73           O  
ANISOU 1110  O   GLU A 141     9137   9581   9677     -8   -103    144       O  
ATOM   1111  CB  GLU A 141      -6.413  -3.219  16.102  1.00 73.54           C  
ANISOU 1111  CB  GLU A 141     8964   9424   9554      0   -103    191       C  
ATOM   1112  CG  GLU A 141      -7.571  -3.336  17.084  1.00 75.52           C  
ANISOU 1112  CG  GLU A 141     9209   9665   9822     14    -87    214       C  
ATOM   1113  CD  GLU A 141      -7.530  -2.363  18.256  1.00 78.16           C  
ANISOU 1113  CD  GLU A 141     9555   9984  10158     33    -59    212       C  
ATOM   1114  OE1 GLU A 141      -6.518  -1.669  18.489  1.00 80.07           O  
ANISOU 1114  OE1 GLU A 141     9813  10224  10388     35    -52    189       O  
ATOM   1115  OE2 GLU A 141      -8.550  -2.302  18.974  1.00 87.55           O1-
ANISOU 1115  OE2 GLU A 141    10738  11164  11363     46    -42    235       O1-
ATOM   1116  N   ILE A 142      -4.958  -2.402  13.484  1.00 64.20           N  
ANISOU 1116  N   ILE A 142     7778   8265   8350    -29   -132    172       N  
ATOM   1117  CA  ILE A 142      -3.797  -2.422  12.615  1.00 66.82           C  
ANISOU 1117  CA  ILE A 142     8117   8608   8665    -40   -145    150       C  
ATOM   1118  C   ILE A 142      -3.386  -0.981  12.293  1.00 67.13           C  
ANISOU 1118  C   ILE A 142     8156   8644   8705    -37   -134    151       C  
ATOM   1119  O   ILE A 142      -2.205  -0.598  12.323  1.00 68.59           O  
ANISOU 1119  O   ILE A 142     8354   8830   8879    -37   -132    128       O  
ATOM   1120  CB  ILE A 142      -4.143  -3.141  11.290  1.00 70.67           C  
ANISOU 1120  CB  ILE A 142     8594   9111   9149    -58   -168    157       C  
ATOM   1121  CG1 ILE A 142      -4.453  -4.639  11.527  1.00 74.07           C  
ANISOU 1121  CG1 ILE A 142     9025   9541   9577    -64   -180    152       C  
ATOM   1122  CG2 ILE A 142      -3.046  -2.922  10.247  1.00 69.39           C  
ANISOU 1122  CG2 ILE A 142     8436   8958   8969    -69   -178    139       C  
ATOM   1123  CD1 ILE A 142      -3.357  -5.632  11.156  1.00 75.08           C  
ANISOU 1123  CD1 ILE A 142     9166   9674   9686    -73   -193    123       C  
ATOM   1124  N   ALA A 143      -4.401  -0.186  11.995  1.00 63.77           N  
ANISOU 1124  N   ALA A 143     7715   8217   8296    -34   -125    181       N  
ATOM   1125  CA  ALA A 143      -4.215   1.079  11.337  1.00 59.73           C  
ANISOU 1125  CA  ALA A 143     7199   7706   7789    -34   -117    190       C  
ATOM   1126  C   ALA A 143      -3.602   2.087  12.279  1.00 55.54           C  
ANISOU 1126  C   ALA A 143     6682   7158   7260    -21    -94    176       C  
ATOM   1127  O   ALA A 143      -2.682   2.812  11.917  1.00 53.17           O  
ANISOU 1127  O   ALA A 143     6389   6859   6954    -24    -91    162       O  
ATOM   1128  CB  ALA A 143      -5.553   1.567  10.805  1.00 62.45           C  
ANISOU 1128  CB  ALA A 143     7522   8053   8152    -34   -113    229       C  
ATOM   1129  N   ARG A 144      -4.106   2.113  13.500  1.00 58.90           N  
ANISOU 1129  N   ARG A 144     7114   7570   7694     -8    -77    179       N  
ATOM   1130  CA  ARG A 144      -3.630   3.050  14.488  1.00 68.50           C  
ANISOU 1130  CA  ARG A 144     8346   8770   8912      3    -54    165       C  
ATOM   1131  C   ARG A 144      -2.210   2.707  14.917  1.00 75.29           C  
ANISOU 1131  C   ARG A 144     9223   9632   9750     -1    -61    128       C  
ATOM   1132  O   ARG A 144      -1.505   3.553  15.480  1.00 85.75           O  
ANISOU 1132  O   ARG A 144    10561  10947  11072      3    -47    111       O  
ATOM   1133  CB  ARG A 144      -4.563   3.081  15.697  1.00 71.80           C  
ANISOU 1133  CB  ARG A 144     8766   9173   9341     18    -33    178       C  
ATOM   1134  CG  ARG A 144      -4.495   1.875  16.624  1.00 73.79           C  
ANISOU 1134  CG  ARG A 144     9027   9427   9584     22    -40    165       C  
ATOM   1135  CD  ARG A 144      -5.837   1.643  17.320  1.00 83.01           C  
ANISOU 1135  CD  ARG A 144    10187  10586  10768     34    -26    191       C  
ATOM   1136  NE  ARG A 144      -6.099   2.565  18.432  1.00 88.27           N  
ANISOU 1136  NE  ARG A 144    10864  11233  11441     50      4    193       N  
ATOM   1137  CZ  ARG A 144      -6.178   2.214  19.714  1.00 93.01           C  
ANISOU 1137  CZ  ARG A 144    11478  11825  12037     62     16    184       C  
ATOM   1138  NH1 ARG A 144      -6.034   0.943  20.089  1.00 96.80           N1+
ANISOU 1138  NH1 ARG A 144    11961  12314  12507     60      1    175       N1+
ATOM   1139  NH2 ARG A 144      -6.422   3.140  20.638  1.00 94.67           N  
ANISOU 1139  NH2 ARG A 144    11701  12018  12253     75     45    185       N  
ATOM   1140  N   ARG A 145      -1.787   1.475  14.647  1.00 74.10           N  
ANISOU 1140  N   ARG A 145     9074   9494   9587     -9    -83    115       N  
ATOM   1141  CA  ARG A 145      -0.444   1.043  14.988  1.00 72.80           C  
ANISOU 1141  CA  ARG A 145     8924   9335   9404    -12    -91     84       C  
ATOM   1142  C   ARG A 145       0.505   1.309  13.877  1.00 70.17           C  
ANISOU 1142  C   ARG A 145     8590   9012   9062    -24   -103     73       C  
ATOM   1143  O   ARG A 145       1.674   1.565  14.122  1.00 82.74           O  
ANISOU 1143  O   ARG A 145    10192  10604  10642    -26   -102     50       O  
ATOM   1144  CB  ARG A 145      -0.423  -0.435  15.364  1.00 77.41           C  
ANISOU 1144  CB  ARG A 145     9510   9925   9978    -13   -104     76       C  
ATOM   1145  CG  ARG A 145      -0.907  -0.612  16.790  1.00 86.40           C  
ANISOU 1145  CG  ARG A 145    10656  11052  11120      1    -90     77       C  
ATOM   1146  CD  ARG A 145      -0.731  -1.999  17.355  1.00 87.99           C  
ANISOU 1146  CD  ARG A 145    10861  11258  11312      3    -99     68       C  
ATOM   1147  NE  ARG A 145      -1.386  -2.080  18.653  1.00 92.18           N  
ANISOU 1147  NE  ARG A 145    11397  11779  11848     17    -84     75       N  
ATOM   1148  CZ  ARG A 145      -2.707  -2.220  18.835  1.00 91.15           C  
ANISOU 1148  CZ  ARG A 145    11256  11642  11733     23    -76    101       C  
ATOM   1149  NH1 ARG A 145      -3.534  -2.295  17.792  1.00 79.17           N1+
ANISOU 1149  NH1 ARG A 145     9723  10128  10229     15    -84    123       N1+
ATOM   1150  NH2 ARG A 145      -3.204  -2.289  20.076  1.00 86.44           N  
ANISOU 1150  NH2 ARG A 145    10666  11036  11140     38    -60    106       N  
ATOM   1151  N   HIS A 146       0.014   1.244  12.653  1.00 68.29           N  
ANISOU 1151  N   HIS A 146     8337   8782   8827    -32   -113     90       N  
ATOM   1152  CA  HIS A 146       0.842   1.510  11.500  1.00 71.29           C  
ANISOU 1152  CA  HIS A 146     8714   9173   9199    -43   -124     83       C  
ATOM   1153  C   HIS A 146       0.277   2.730  10.810  1.00 74.61           C  
ANISOU 1153  C   HIS A 146     9124   9591   9633    -43   -114    106       C  
ATOM   1154  O   HIS A 146      -0.401   2.611   9.790  1.00 83.14           O  
ANISOU 1154  O   HIS A 146    10190  10682  10717    -50   -123    127       O  
ATOM   1155  CB  HIS A 146       0.847   0.300  10.561  1.00 71.29           C  
ANISOU 1155  CB  HIS A 146     8710   9189   9189    -54   -146     82       C  
ATOM   1156  CG  HIS A 146       1.394  -0.935  11.192  1.00 71.62           C  
ANISOU 1156  CG  HIS A 146     8762   9231   9218    -54   -154     61       C  
ATOM   1157  CD2 HIS A 146       0.788  -2.072  11.604  1.00 77.53           C  
ANISOU 1157  CD2 HIS A 146     9510   9979   9968    -53   -160     64       C  
ATOM   1158  ND1 HIS A 146       2.731  -1.091  11.475  1.00 73.55           N  
ANISOU 1158  ND1 HIS A 146     9019   9478   9450    -53   -156     35       N  
ATOM   1159  CE1 HIS A 146       2.924  -2.261  12.054  1.00 76.76           C  
ANISOU 1159  CE1 HIS A 146     9431   9884   9850    -51   -161     24       C  
ATOM   1160  NE2 HIS A 146       1.760  -2.882  12.138  1.00 78.53           N  
ANISOU 1160  NE2 HIS A 146     9648  10106  10082    -51   -164     40       N  
ATOM   1161  N   PRO A 147       0.564   3.919  11.345  1.00 67.25           N  
ANISOU 1161  N   PRO A 147     8198   8645   8709    -36    -94    103       N  
ATOM   1162  CA  PRO A 147      -0.085   5.087  10.809  1.00 64.40           C  
ANISOU 1162  CA  PRO A 147     7825   8279   8365    -33    -80    128       C  
ATOM   1163  C   PRO A 147       0.409   5.504   9.441  1.00 58.19           C  
ANISOU 1163  C   PRO A 147     7031   7505   7575    -43    -89    133       C  
ATOM   1164  O   PRO A 147      -0.110   6.502   8.929  1.00 51.32           O  
ANISOU 1164  O   PRO A 147     6150   6632   6719    -40    -77    156       O  
ATOM   1165  CB  PRO A 147       0.260   6.169  11.838  1.00 65.68           C  
ANISOU 1165  CB  PRO A 147     8000   8420   8534    -24    -55    117       C  
ATOM   1166  CG  PRO A 147       1.573   5.779  12.388  1.00 62.25           C  
ANISOU 1166  CG  PRO A 147     7582   7988   8083    -28    -62     82       C  
ATOM   1167  CD  PRO A 147       1.656   4.278  12.258  1.00 67.72           C  
ANISOU 1167  CD  PRO A 147     8274   8696   8761    -33    -85     75       C  
ATOM   1168  N   TYR A 148       1.399   4.808   8.862  1.00 61.23           N  
ANISOU 1168  N   TYR A 148     7420   7904   7941    -53   -107    113       N  
ATOM   1169  CA  TYR A 148       1.835   5.194   7.495  1.00 74.54           C  
ANISOU 1169  CA  TYR A 148     9098   9602   9623    -61   -115    119       C  
ATOM   1170  C   TYR A 148       1.395   4.202   6.432  1.00 70.11           C  
ANISOU 1170  C   TYR A 148     8528   9061   9051    -72   -138    129       C  
ATOM   1171  O   TYR A 148       1.544   4.466   5.251  1.00 79.54           O  
ANISOU 1171  O   TYR A 148     9713  10268  10239    -79   -145    138       O  
ATOM   1172  CB  TYR A 148       3.343   5.577   7.373  1.00 77.70           C  
ANISOU 1172  CB  TYR A 148     9507  10001  10012    -65   -114     93       C  
ATOM   1173  CG  TYR A 148       3.637   7.008   7.849  1.00 74.94           C  
ANISOU 1173  CG  TYR A 148     9161   9634   9677    -59    -91     93       C  
ATOM   1174  CD1 TYR A 148       4.032   7.250   9.158  1.00 80.15           C  
ANISOU 1174  CD1 TYR A 148     9836  10279  10339    -54    -79     73       C  
ATOM   1175  CD2 TYR A 148       3.453   8.104   7.027  1.00 76.12           C  
ANISOU 1175  CD2 TYR A 148     9300   9783   9839    -59    -81    113       C  
ATOM   1176  CE1 TYR A 148       4.268   8.528   9.627  1.00 76.74           C  
ANISOU 1176  CE1 TYR A 148     9409   9830   9920    -50    -57     71       C  
ATOM   1177  CE2 TYR A 148       3.680   9.398   7.492  1.00 79.16           C  
ANISOU 1177  CE2 TYR A 148     9689  10148  10238    -54    -58    113       C  
ATOM   1178  CZ  TYR A 148       4.091   9.592   8.797  1.00 81.33           C  
ANISOU 1178  CZ  TYR A 148     9980  10407  10515    -50    -46     90       C  
ATOM   1179  OH  TYR A 148       4.332  10.853   9.291  1.00 92.83           O  
ANISOU 1179  OH  TYR A 148    11443  11843  11986    -47    -22     87       O  
ATOM   1180  N   PHE A 149       0.752   3.127   6.852  1.00 64.08           N  
ANISOU 1180  N   PHE A 149     7764   8299   8284    -72   -147    129       N  
ATOM   1181  CA  PHE A 149       0.325   2.089   5.941  1.00 64.06           C  
ANISOU 1181  CA  PHE A 149     7755   8314   8272    -84   -169    135       C  
ATOM   1182  C   PHE A 149      -0.271   2.548   4.607  1.00 75.28           C  
ANISOU 1182  C   PHE A 149     9160   9751   9693    -93   -176    162       C  
ATOM   1183  O   PHE A 149      -1.037   3.518   4.530  1.00 87.57           O  
ANISOU 1183  O   PHE A 149    10702  11304  11265    -87   -164    189       O  
ATOM   1184  CB  PHE A 149      -0.680   1.179   6.610  1.00 61.74           C  
ANISOU 1184  CB  PHE A 149     7458   8016   7983    -83   -173    143       C  
ATOM   1185  CG  PHE A 149      -0.458  -0.265   6.288  1.00 65.00           C  
ANISOU 1185  CG  PHE A 149     7877   8439   8380    -94   -192    127       C  
ATOM   1186  CD1 PHE A 149      -0.460  -0.710   4.962  1.00 77.27           C  
ANISOU 1186  CD1 PHE A 149     9427  10011   9921   -109   -210    130       C  
ATOM   1187  CD2 PHE A 149      -0.212  -1.180   7.288  1.00 58.84           C  
ANISOU 1187  CD2 PHE A 149     7108   7650   7597    -89   -192    109       C  
ATOM   1188  CE1 PHE A 149      -0.252  -2.045   4.653  1.00 76.24           C  
ANISOU 1188  CE1 PHE A 149     9304   9887   9776   -120   -226    113       C  
ATOM   1189  CE2 PHE A 149      -0.016  -2.511   6.991  1.00 58.44           C  
ANISOU 1189  CE2 PHE A 149     7064   7606   7535    -99   -207     95       C  
ATOM   1190  CZ  PHE A 149      -0.030  -2.946   5.680  1.00 66.50           C  
ANISOU 1190  CZ  PHE A 149     8082   8642   8544   -114   -224     96       C  
ATOM   1191  N   TYR A 150       0.109   1.824   3.556  1.00 77.09           N  
ANISOU 1191  N   TYR A 150     9390   9997   9903   -106   -195    154       N  
ATOM   1192  CA  TYR A 150      -0.442   2.008   2.222  1.00 80.48           C  
ANISOU 1192  CA  TYR A 150     9805  10446  10327   -117   -207    177       C  
ATOM   1193  C   TYR A 150      -1.893   1.582   2.252  1.00 71.82           C  
ANISOU 1193  C   TYR A 150     8694   9354   9239   -121   -215    203       C  
ATOM   1194  O   TYR A 150      -2.196   0.395   2.285  1.00 81.51           O  
ANISOU 1194  O   TYR A 150     9925  10587  10459   -130   -230    194       O  
ATOM   1195  CB  TYR A 150       0.354   1.131   1.255  1.00 82.07           C  
ANISOU 1195  CB  TYR A 150    10016  10662  10504   -130   -225    156       C  
ATOM   1196  CG  TYR A 150       0.196   1.378  -0.236  1.00 78.32           C  
ANISOU 1196  CG  TYR A 150     9531  10210  10016   -142   -237    172       C  
ATOM   1197  CD1 TYR A 150      -0.426   2.502  -0.745  1.00 75.45           C  
ANISOU 1197  CD1 TYR A 150     9151   9854   9664   -139   -230    204       C  
ATOM   1198  CD2 TYR A 150       0.772   0.492  -1.133  1.00 84.50           C  
ANISOU 1198  CD2 TYR A 150    10325  11007  10775   -155   -252    154       C  
ATOM   1199  CE1 TYR A 150      -0.516   2.697  -2.109  1.00 79.08           C  
ANISOU 1199  CE1 TYR A 150     9601  10336  10109   -150   -242    219       C  
ATOM   1200  CE2 TYR A 150       0.696   0.682  -2.493  1.00 86.44           C  
ANISOU 1200  CE2 TYR A 150    10564  11275  11006   -167   -264    166       C  
ATOM   1201  CZ  TYR A 150       0.056   1.777  -2.978  1.00 77.97           C  
ANISOU 1201  CZ  TYR A 150     9473  10211   9943   -164   -259    199       C  
ATOM   1202  OH  TYR A 150       0.019   1.913  -4.334  1.00 72.38           O  
ANISOU 1202  OH  TYR A 150     8758   9527   9217   -175   -271    212       O  
ATOM   1203  N   ALA A 151      -2.790   2.549   2.240  1.00 63.18           N  
ANISOU 1203  N   ALA A 151     7583   8259   8164   -114   -204    235       N  
ATOM   1204  CA  ALA A 151      -4.176   2.258   2.581  1.00 70.67           C  
ANISOU 1204  CA  ALA A 151     8516   9208   9127   -114   -207    262       C  
ATOM   1205  C   ALA A 151      -4.878   1.199   1.740  1.00 67.39           C  
ANISOU 1205  C   ALA A 151     8092   8814   8699   -133   -233    270       C  
ATOM   1206  O   ALA A 151      -5.446   0.274   2.287  1.00 70.92           O  
ANISOU 1206  O   ALA A 151     8540   9257   9150   -137   -240    268       O  
ATOM   1207  CB  ALA A 151      -4.991   3.525   2.609  1.00 79.31           C  
ANISOU 1207  CB  ALA A 151     9592  10299  10243   -103   -189    299       C  
ATOM   1208  N   PRO A 152      -4.852   1.327   0.416  1.00 68.26           N  
ANISOU 1208  N   PRO A 152     8194   8947   8795   -146   -248    280       N  
ATOM   1209  CA  PRO A 152      -5.448   0.282  -0.425  1.00 66.21           C  
ANISOU 1209  CA  PRO A 152     7930   8709   8520   -168   -275    284       C  
ATOM   1210  C   PRO A 152      -4.914  -1.111  -0.172  1.00 63.22           C  
ANISOU 1210  C   PRO A 152     7570   8324   8125   -178   -286    248       C  
ATOM   1211  O   PRO A 152      -5.601  -2.100  -0.431  1.00 61.61           O  
ANISOU 1211  O   PRO A 152     7363   8129   7917   -193   -305    250       O  
ATOM   1212  CB  PRO A 152      -5.074   0.719  -1.825  1.00 67.76           C  
ANISOU 1212  CB  PRO A 152     8121   8927   8697   -178   -285    291       C  
ATOM   1213  CG  PRO A 152      -5.076   2.194  -1.719  1.00 75.16           C  
ANISOU 1213  CG  PRO A 152     9047   9858   9652   -161   -264    314       C  
ATOM   1214  CD  PRO A 152      -4.507   2.519  -0.372  1.00 71.14           C  
ANISOU 1214  CD  PRO A 152     8551   9320   9159   -142   -240    296       C  
ATOM   1215  N   GLU A 153      -3.696  -1.211   0.325  1.00 62.52           N  
ANISOU 1215  N   GLU A 153     7503   8222   8031   -169   -276    216       N  
ATOM   1216  CA  GLU A 153      -3.231  -2.520   0.692  1.00 70.18           C  
ANISOU 1216  CA  GLU A 153     8490   9184   8990   -175   -284    185       C  
ATOM   1217  C   GLU A 153      -3.901  -3.042   1.965  1.00 68.92           C  
ANISOU 1217  C   GLU A 153     8329   9007   8849   -167   -277    188       C  
ATOM   1218  O   GLU A 153      -4.293  -4.208   2.023  1.00 70.21           O  
ANISOU 1218  O   GLU A 153     8496   9171   9009   -178   -289    180       O  
ATOM   1219  CB  GLU A 153      -1.708  -2.558   0.766  1.00 74.99           C  
ANISOU 1219  CB  GLU A 153     9119   9786   9586   -169   -276    152       C  
ATOM   1220  CG  GLU A 153      -1.080  -3.005  -0.545  1.00 83.66           C  
ANISOU 1220  CG  GLU A 153    10226  10901  10659   -184   -290    138       C  
ATOM   1221  CD  GLU A 153      -1.153  -4.515  -0.737  1.00 95.86           C  
ANISOU 1221  CD  GLU A 153    11783  12448  12191   -199   -305    118       C  
ATOM   1222  OE1 GLU A 153      -0.614  -5.246   0.123  1.00101.20           O  
ANISOU 1222  OE1 GLU A 153    12473  13108  12869   -192   -299     96       O  
ATOM   1223  OE2 GLU A 153      -1.762  -4.976  -1.726  1.00103.48           O1-
ANISOU 1223  OE2 GLU A 153    12744  13430  13144   -219   -323    126       O1-
ATOM   1224  N   LEU A 154      -4.049  -2.178   2.961  1.00 72.94           N  
ANISOU 1224  N   LEU A 154     8834   9501   9377   -148   -257    198       N  
ATOM   1225  CA  LEU A 154      -4.715  -2.562   4.200  1.00 79.12           C  
ANISOU 1225  CA  LEU A 154     9616  10269  10178   -138   -248    203       C  
ATOM   1226  C   LEU A 154      -5.966  -3.324   3.838  1.00 80.32           C  
ANISOU 1226  C   LEU A 154     9753  10431  10334   -153   -265    224       C  
ATOM   1227  O   LEU A 154      -6.237  -4.420   4.349  1.00 80.64           O  
ANISOU 1227  O   LEU A 154     9798  10464  10376   -157   -270    214       O  
ATOM   1228  CB  LEU A 154      -5.096  -1.338   5.038  1.00 80.95           C  
ANISOU 1228  CB  LEU A 154     9839  10487  10430   -119   -225    223       C  
ATOM   1229  CG  LEU A 154      -5.551  -1.600   6.475  1.00 86.15           C  
ANISOU 1229  CG  LEU A 154    10502  11127  11105   -105   -210    224       C  
ATOM   1230  CD1 LEU A 154      -4.796  -2.764   7.097  1.00 88.48           C  
ANISOU 1230  CD1 LEU A 154    10816  11415  11389   -105   -215    191       C  
ATOM   1231  CD2 LEU A 154      -5.338  -0.350   7.319  1.00 92.89           C  
ANISOU 1231  CD2 LEU A 154    11358  11964  11971    -85   -184    228       C  
ATOM   1232  N   LEU A 155      -6.712  -2.705   2.928  1.00 78.25           N  
ANISOU 1232  N   LEU A 155     9472  10186  10075   -161   -272    254       N  
ATOM   1233  CA  LEU A 155      -7.907  -3.275   2.348  1.00 72.67           C  
ANISOU 1233  CA  LEU A 155     8747   9494   9370   -178   -291    277       C  
ATOM   1234  C   LEU A 155      -7.683  -4.673   1.866  1.00 70.59           C  
ANISOU 1234  C   LEU A 155     8496   9238   9088   -199   -312    252       C  
ATOM   1235  O   LEU A 155      -8.424  -5.579   2.206  1.00 74.55           O  
ANISOU 1235  O   LEU A 155     8994   9736   9597   -207   -321    256       O  
ATOM   1236  CB  LEU A 155      -8.318  -2.457   1.138  1.00 72.07           C  
ANISOU 1236  CB  LEU A 155     8653   9441   9289   -187   -301    305       C  
ATOM   1237  CG  LEU A 155      -8.959  -1.123   1.389  1.00 69.34           C  
ANISOU 1237  CG  LEU A 155     8288   9093   8966   -170   -283    342       C  
ATOM   1238  CD1 LEU A 155      -9.600  -0.725   0.072  1.00 69.74           C  
ANISOU 1238  CD1 LEU A 155     8316   9172   9009   -185   -300    373       C  
ATOM   1239  CD2 LEU A 155      -9.939  -1.256   2.533  1.00 76.13           C  
ANISOU 1239  CD2 LEU A 155     9138   9938   9851   -159   -271    360       C  
ATOM   1240  N   PHE A 156      -6.668  -4.856   1.048  1.00 68.10           N  
ANISOU 1240  N   PHE A 156     8196   8930   8750   -208   -320    227       N  
ATOM   1241  CA  PHE A 156      -6.473  -6.145   0.461  1.00 71.47           C  
ANISOU 1241  CA  PHE A 156     8635   9362   9157   -229   -339    204       C  
ATOM   1242  C   PHE A 156      -6.263  -7.192   1.543  1.00 75.07           C  
ANISOU 1242  C   PHE A 156     9106   9798   9621   -223   -332    182       C  
ATOM   1243  O   PHE A 156      -6.807  -8.295   1.423  1.00 83.68           O  
ANISOU 1243  O   PHE A 156    10197  10889  10710   -239   -345    178       O  
ATOM   1244  CB  PHE A 156      -5.315  -6.112  -0.522  1.00 78.05           C  
ANISOU 1244  CB  PHE A 156     9485  10206   9964   -235   -343    180       C  
ATOM   1245  CG  PHE A 156      -4.951  -7.453  -1.038  1.00 79.04           C  
ANISOU 1245  CG  PHE A 156     9627  10333  10070   -254   -357    152       C  
ATOM   1246  CD1 PHE A 156      -5.907  -8.261  -1.637  1.00 74.14           C  
ANISOU 1246  CD1 PHE A 156     9000   9724   9445   -279   -378    159       C  
ATOM   1247  CD2 PHE A 156      -3.660  -7.916  -0.904  1.00 85.33           C  
ANISOU 1247  CD2 PHE A 156    10447  11118  10854   -248   -349    117       C  
ATOM   1248  CE1 PHE A 156      -5.569  -9.499  -2.101  1.00 78.53           C  
ANISOU 1248  CE1 PHE A 156     9575  10280   9984   -297   -389    131       C  
ATOM   1249  CE2 PHE A 156      -3.307  -9.160  -1.377  1.00 88.90           C  
ANISOU 1249  CE2 PHE A 156    10918  11570  11291   -264   -358     91       C  
ATOM   1250  CZ  PHE A 156      -4.263  -9.947  -1.981  1.00 88.21           C  
ANISOU 1250  CZ  PHE A 156    10825  11492  11198   -289   -378     97       C  
ATOM   1251  N   PHE A 157      -5.489  -6.850   2.585  1.00 77.25           N  
ANISOU 1251  N   PHE A 157     9392  10055   9905   -200   -311    169       N  
ATOM   1252  CA  PHE A 157      -5.275  -7.729   3.758  1.00 72.26           C  
ANISOU 1252  CA  PHE A 157     8772   9403   9281   -191   -302    151       C  
ATOM   1253  C   PHE A 157      -6.613  -8.024   4.422  1.00 63.73           C  
ANISOU 1253  C   PHE A 157     7676   8318   8222   -191   -303    176       C  
ATOM   1254  O   PHE A 157      -7.051  -9.173   4.543  1.00 58.33           O  
ANISOU 1254  O   PHE A 157     6994   7630   7541   -202   -312    171       O  
ATOM   1255  CB  PHE A 157      -4.347  -7.084   4.800  1.00 69.85           C  
ANISOU 1255  CB  PHE A 157     8477   9082   8980   -166   -281    139       C  
ATOM   1256  CG  PHE A 157      -2.911  -6.989   4.379  1.00 66.62           C  
ANISOU 1256  CG  PHE A 157     8085   8676   8553   -165   -278    111       C  
ATOM   1257  CD1 PHE A 157      -2.297  -5.760   4.140  1.00 62.49           C  
ANISOU 1257  CD1 PHE A 157     7560   8156   8026   -156   -270    114       C  
ATOM   1258  CD2 PHE A 157      -2.171  -8.109   4.264  1.00 71.30           C  
ANISOU 1258  CD2 PHE A 157     8694   9264   9132   -171   -283     84       C  
ATOM   1259  CE1 PHE A 157      -0.977  -5.672   3.775  1.00 57.20           C  
ANISOU 1259  CE1 PHE A 157     6905   7488   7342   -155   -267     90       C  
ATOM   1260  CE2 PHE A 157      -0.839  -8.034   3.895  1.00 74.50           C  
ANISOU 1260  CE2 PHE A 157     9114   9671   9521   -168   -280     61       C  
ATOM   1261  CZ  PHE A 157      -0.243  -6.811   3.643  1.00 61.81           C  
ANISOU 1261  CZ  PHE A 157     7504   8069   7912   -160   -272     64       C  
ATOM   1262  N   ALA A 158      -7.272  -6.968   4.834  1.00 60.95           N  
ANISOU 1262  N   ALA A 158     7307   7965   7886   -178   -292    205       N  
ATOM   1263  CA  ALA A 158      -8.625  -7.096   5.312  1.00 70.32           C  
ANISOU 1263  CA  ALA A 158     8475   9149   9094   -178   -292    235       C  
ATOM   1264  C   ALA A 158      -9.441  -8.112   4.472  1.00 72.24           C  
ANISOU 1264  C   ALA A 158     8708   9405   9333   -205   -316    241       C  
ATOM   1265  O   ALA A 158     -10.122  -8.971   5.020  1.00 66.41           O  
ANISOU 1265  O   ALA A 158     7966   8658   8607   -209   -319    246       O  
ATOM   1266  CB  ALA A 158      -9.299  -5.719   5.309  1.00 72.99           C  
ANISOU 1266  CB  ALA A 158     8794   9492   9447   -167   -281    269       C  
ATOM   1267  N   LYS A 159      -9.366  -8.019   3.144  1.00 79.36           N  
ANISOU 1267  N   LYS A 159     9608  10328  10217   -225   -335    242       N  
ATOM   1268  CA  LYS A 159     -10.103  -8.950   2.297  1.00 77.96           C  
ANISOU 1268  CA  LYS A 159     9424  10165  10034   -254   -360    246       C  
ATOM   1269  C   LYS A 159      -9.594 -10.316   2.646  1.00 88.43           C  
ANISOU 1269  C   LYS A 159    10771  11477  11353   -260   -362    213       C  
ATOM   1270  O   LYS A 159     -10.373 -11.173   3.041  1.00108.67           O  
ANISOU 1270  O   LYS A 159    13329  14033  13930   -269   -367    219       O  
ATOM   1271  CB  LYS A 159      -9.921  -8.714   0.791  1.00 73.05           C  
ANISOU 1271  CB  LYS A 159     8800   9569   9387   -275   -379    245       C  
ATOM   1272  CG  LYS A 159     -11.102  -9.238  -0.020  1.00 74.80           C  
ANISOU 1272  CG  LYS A 159     9004   9810   9607   -303   -405    266       C  
ATOM   1273  CD  LYS A 159     -10.957  -9.141  -1.536  1.00 73.46           C  
ANISOU 1273  CD  LYS A 159     8835   9668   9410   -327   -426    264       C  
ATOM   1274  CE  LYS A 159     -10.490 -10.449  -2.162  1.00 70.12           C  
ANISOU 1274  CE  LYS A 159     8434   9245   8963   -352   -442    227       C  
ATOM   1275  NZ  LYS A 159     -11.317 -10.790  -3.340  1.00 70.62           N1+
ANISOU 1275  NZ  LYS A 159     8485   9335   9011   -385   -471    240       N1+
ATOM   1276  N   ARG A 160      -8.283 -10.509   2.531  1.00 89.18           N  
ANISOU 1276  N   ARG A 160    10889  11565  11430   -255   -355    179       N  
ATOM   1277  CA  ARG A 160      -7.686 -11.800   2.848  1.00104.19           C  
ANISOU 1277  CA  ARG A 160    12811  13450  13325   -259   -354    147       C  
ATOM   1278  C   ARG A 160      -7.939 -12.319   4.284  1.00104.19           C  
ANISOU 1278  C   ARG A 160    12812  13428  13347   -242   -339    149       C  
ATOM   1279  O   ARG A 160      -8.007 -13.547   4.493  1.00114.29           O  
ANISOU 1279  O   ARG A 160    14100  14697  14629   -252   -342    134       O  
ATOM   1280  CB  ARG A 160      -6.192 -11.807   2.528  1.00114.36           C  
ANISOU 1280  CB  ARG A 160    14123  14736  14593   -253   -348    115       C  
ATOM   1281  CG  ARG A 160      -5.830 -12.703   1.346  1.00122.81           C  
ANISOU 1281  CG  ARG A 160    15208  15814  15640   -278   -364     92       C  
ATOM   1282  CD  ARG A 160      -4.360 -13.060   1.386  1.00122.04           C  
ANISOU 1282  CD  ARG A 160    15135  15706  15528   -268   -352     58       C  
ATOM   1283  NE  ARG A 160      -3.511 -11.867   1.257  1.00125.92           N  
ANISOU 1283  NE  ARG A 160    15627  16205  16012   -252   -342     58       N  
ATOM   1284  CZ  ARG A 160      -2.394 -11.637   1.945  1.00131.30           C  
ANISOU 1284  CZ  ARG A 160    16319  16874  16693   -231   -325     43       C  
ATOM   1285  NH1 ARG A 160      -1.969 -12.507   2.864  1.00139.87           N1+
ANISOU 1285  NH1 ARG A 160    17417  17942  17787   -221   -315     27       N1+
ATOM   1286  NH2 ARG A 160      -1.696 -10.520   1.723  1.00126.29           N  
ANISOU 1286  NH2 ARG A 160    15683  16247  16053   -220   -318     45       N  
ATOM   1287  N   TYR A 161      -8.083 -11.407   5.248  1.00 91.94           N  
ANISOU 1287  N   TYR A 161    11251  11869  11811   -218   -322    166       N  
ATOM   1288  CA  TYR A 161      -8.406 -11.769   6.644  1.00 87.01           C  
ANISOU 1288  CA  TYR A 161    10626  11226  11207   -201   -306    171       C  
ATOM   1289  C   TYR A 161      -9.819 -12.361   6.744  1.00 89.66           C  
ANISOU 1289  C   TYR A 161    10943  11562  11561   -214   -316    197       C  
ATOM   1290  O   TYR A 161     -10.009 -13.405   7.350  1.00 88.35           O  
ANISOU 1290  O   TYR A 161    10781  11382  11404   -215   -313    190       O  
ATOM   1291  CB  TYR A 161      -8.283 -10.519   7.503  1.00 89.62           C  
ANISOU 1291  CB  TYR A 161    10952  11552  11548   -175   -286    185       C  
ATOM   1292  CG  TYR A 161      -8.517 -10.640   8.992  1.00 83.57           C  
ANISOU 1292  CG  TYR A 161    10186  10768  10799   -153   -267    191       C  
ATOM   1293  CD1 TYR A 161      -7.547 -11.146   9.832  1.00 81.89           C  
ANISOU 1293  CD1 TYR A 161     9992  10541  10580   -139   -255    165       C  
ATOM   1294  CD2 TYR A 161      -9.683 -10.150   9.568  1.00 84.60           C  
ANISOU 1294  CD2 TYR A 161    10298  10895  10951   -144   -259    223       C  
ATOM   1295  CE1 TYR A 161      -7.752 -11.203  11.205  1.00 82.40           C  
ANISOU 1295  CE1 TYR A 161    10058  10593  10659   -119   -237    171       C  
ATOM   1296  CE2 TYR A 161      -9.900 -10.205  10.933  1.00 77.80           C  
ANISOU 1296  CE2 TYR A 161     9438  10018  10103   -123   -239    229       C  
ATOM   1297  CZ  TYR A 161      -8.940 -10.725  11.742  1.00 76.60           C  
ANISOU 1297  CZ  TYR A 161     9305   9854   9944   -111   -229    203       C  
ATOM   1298  OH  TYR A 161      -9.189 -10.767  13.086  1.00 74.89           O  
ANISOU 1298  OH  TYR A 161     9090   9624   9739    -91   -211    210       O  
ATOM   1299  N   LYS A 162     -10.796 -11.679   6.137  1.00 91.42           N  
ANISOU 1299  N   LYS A 162    11144  11802  11791   -223   -326    227       N  
ATOM   1300  CA  LYS A 162     -12.153 -12.200   5.944  1.00 84.54           C  
ANISOU 1300  CA  LYS A 162    10251  10935  10934   -241   -340    253       C  
ATOM   1301  C   LYS A 162     -12.160 -13.536   5.201  1.00 81.20           C  
ANISOU 1301  C   LYS A 162     9837  10514  10500   -271   -360    233       C  
ATOM   1302  O   LYS A 162     -12.888 -14.436   5.567  1.00 81.11           O  
ANISOU 1302  O   LYS A 162     9820  10495  10503   -280   -364    239       O  
ATOM   1303  CB  LYS A 162     -12.985 -11.184   5.161  1.00 86.66           C  
ANISOU 1303  CB  LYS A 162    10495  11226  11206   -249   -350    288       C  
ATOM   1304  CG  LYS A 162     -14.408 -11.598   4.780  1.00 89.14           C  
ANISOU 1304  CG  LYS A 162    10784  11552  11534   -270   -368    319       C  
ATOM   1305  CD  LYS A 162     -15.209 -10.358   4.404  1.00 89.28           C  
ANISOU 1305  CD  LYS A 162    10774  11586  11561   -266   -368    360       C  
ATOM   1306  CE  LYS A 162     -16.550 -10.624   3.772  1.00 87.59           C  
ANISOU 1306  CE  LYS A 162    10531  11392  11357   -291   -391    394       C  
ATOM   1307  NZ  LYS A 162     -17.017  -9.317   3.237  1.00 91.04           N1+
ANISOU 1307  NZ  LYS A 162    10945  11848  11797   -285   -390    430       N1+
ATOM   1308  N   ALA A 163     -11.368 -13.668   4.149  1.00 83.76           N  
ANISOU 1308  N   ALA A 163    10177  10849  10799   -286   -372    208       N  
ATOM   1309  CA  ALA A 163     -11.269 -14.947   3.448  1.00 90.72           C  
ANISOU 1309  CA  ALA A 163    11072  11731  11667   -313   -388    184       C  
ATOM   1310  C   ALA A 163     -10.838 -16.033   4.428  1.00 87.72           C  
ANISOU 1310  C   ALA A 163    10708  11324  11297   -303   -374    162       C  
ATOM   1311  O   ALA A 163     -11.351 -17.166   4.381  1.00 84.72           O  
ANISOU 1311  O   ALA A 163    10330  10937  10924   -322   -383    157       O  
ATOM   1312  CB  ALA A 163     -10.292 -14.862   2.278  1.00 92.03           C  
ANISOU 1312  CB  ALA A 163    11256  11909  11803   -326   -398    158       C  
ATOM   1313  N   ALA A 164      -9.910 -15.676   5.319  1.00 79.52           N  
ANISOU 1313  N   ALA A 164     9683  10273  10260   -274   -352    151       N  
ATOM   1314  CA  ALA A 164      -9.404 -16.628   6.297  1.00 80.83           C  
ANISOU 1314  CA  ALA A 164     9863  10416  10433   -262   -337    132       C  
ATOM   1315  C   ALA A 164     -10.498 -17.059   7.265  1.00 75.27           C  
ANISOU 1315  C   ALA A 164     9143   9699   9756   -257   -332    156       C  
ATOM   1316  O   ALA A 164     -10.655 -18.238   7.524  1.00 82.32           O  
ANISOU 1316  O   ALA A 164    10042  10579  10657   -265   -332    146       O  
ATOM   1317  CB  ALA A 164      -8.220 -16.058   7.046  1.00 82.84           C  
ANISOU 1317  CB  ALA A 164    10131  10662  10681   -232   -317    118       C  
ATOM   1318  N   PHE A 165     -11.281 -16.124   7.772  1.00 66.18           N  
ANISOU 1318  N   PHE A 165     7971   8553   8620   -244   -326    187       N  
ATOM   1319  CA  PHE A 165     -12.325 -16.478   8.706  1.00 61.62           C  
ANISOU 1319  CA  PHE A 165     7379   7966   8070   -237   -319    212       C  
ATOM   1320  C   PHE A 165     -13.506 -17.120   8.031  1.00 64.95           C  
ANISOU 1320  C   PHE A 165     7782   8394   8500   -267   -340    229       C  
ATOM   1321  O   PHE A 165     -14.101 -18.061   8.564  1.00 72.97           O  
ANISOU 1321  O   PHE A 165     8794   9397   9534   -272   -338    234       O  
ATOM   1322  CB  PHE A 165     -12.777 -15.259   9.476  1.00 62.59           C  
ANISOU 1322  CB  PHE A 165     7486   8090   8206   -213   -304    241       C  
ATOM   1323  CG  PHE A 165     -11.899 -14.948  10.623  1.00 72.98           C  
ANISOU 1323  CG  PHE A 165     8817   9392   9520   -182   -280    228       C  
ATOM   1324  CD1 PHE A 165     -12.206 -15.423  11.891  1.00 79.00           C  
ANISOU 1324  CD1 PHE A 165     9579  10138  10300   -164   -263    236       C  
ATOM   1325  CD2 PHE A 165     -10.740 -14.214  10.441  1.00 80.86           C  
ANISOU 1325  CD2 PHE A 165     9830  10395  10499   -171   -274    208       C  
ATOM   1326  CE1 PHE A 165     -11.384 -15.145  12.970  1.00 84.95           C  
ANISOU 1326  CE1 PHE A 165    10347  10881  11049   -137   -242    224       C  
ATOM   1327  CE2 PHE A 165      -9.907 -13.929  11.508  1.00 86.25           C  
ANISOU 1327  CE2 PHE A 165    10526  11066  11179   -145   -254    196       C  
ATOM   1328  CZ  PHE A 165     -10.230 -14.395  12.778  1.00 90.24           C  
ANISOU 1328  CZ  PHE A 165    11031  11556  11700   -128   -238    203       C  
ATOM   1329  N   THR A 166     -13.867 -16.612   6.864  1.00 69.39           N  
ANISOU 1329  N   THR A 166     8334   8978   9052   -288   -360    238       N  
ATOM   1330  CA  THR A 166     -15.043 -17.118   6.172  1.00 68.42           C  
ANISOU 1330  CA  THR A 166     8192   8867   8937   -319   -383    257       C  
ATOM   1331  C   THR A 166     -14.895 -18.614   5.999  1.00 71.37           C  
ANISOU 1331  C   THR A 166     8582   9228   9309   -341   -390    230       C  
ATOM   1332  O   THR A 166     -15.859 -19.325   6.184  1.00 72.18           O  
ANISOU 1332  O   THR A 166     8670   9325   9430   -356   -397    245       O  
ATOM   1333  CB  THR A 166     -15.267 -16.434   4.820  1.00 61.69           C  
ANISOU 1333  CB  THR A 166     7330   8044   8067   -341   -405    266       C  
ATOM   1334  CG2 THR A 166     -16.175 -17.248   3.976  1.00 64.68           C  
ANISOU 1334  CG2 THR A 166     7697   8433   8445   -379   -432    273       C  
ATOM   1335  OG1 THR A 166     -15.872 -15.166   5.041  1.00 56.16           O  
ANISOU 1335  OG1 THR A 166     6605   7354   7378   -324   -399    303       O  
ATOM   1336  N   GLU A 167     -13.688 -19.080   5.679  1.00 72.32           N  
ANISOU 1336  N   GLU A 167     8731   9341   9408   -342   -387    192       N  
ATOM   1337  CA  GLU A 167     -13.448 -20.493   5.525  1.00 75.78           C  
ANISOU 1337  CA  GLU A 167     9186   9762   9844   -360   -390    164       C  
ATOM   1338  C   GLU A 167     -13.138 -21.174   6.878  1.00 78.82           C  
ANISOU 1338  C   GLU A 167     9580  10119  10248   -335   -366    158       C  
ATOM   1339  O   GLU A 167     -13.779 -22.164   7.235  1.00 83.46           O  
ANISOU 1339  O   GLU A 167    10163  10694  10855   -346   -366    163       O  
ATOM   1340  CB  GLU A 167     -12.329 -20.744   4.518  1.00 83.81           C  
ANISOU 1340  CB  GLU A 167    10229  10783  10830   -372   -396    127       C  
ATOM   1341  CG  GLU A 167     -12.218 -22.219   4.111  1.00 99.58           C  
ANISOU 1341  CG  GLU A 167    12246  12766  12825   -398   -402     99       C  
ATOM   1342  CD  GLU A 167     -10.784 -22.684   3.811  1.00111.77           C  
ANISOU 1342  CD  GLU A 167    13822  14298  14347   -392   -390     59       C  
ATOM   1343  OE1 GLU A 167     -10.039 -21.915   3.163  1.00133.00           O  
ANISOU 1343  OE1 GLU A 167    16518  17002  17013   -388   -393     50       O  
ATOM   1344  OE2 GLU A 167     -10.390 -23.819   4.195  1.00 96.32           O1-
ANISOU 1344  OE2 GLU A 167    11882  12318  12397   -392   -378     39       O1-
ATOM   1345  N   CYS A 168     -12.183 -20.652   7.644  1.00 81.65           N  
ANISOU 1345  N   CYS A 168     9950  10472  10602   -303   -345    150       N  
ATOM   1346  CA  CYS A 168     -11.691 -21.365   8.840  1.00 75.98           C  
ANISOU 1346  CA  CYS A 168     9242   9729   9896   -280   -323    141       C  
ATOM   1347  C   CYS A 168     -12.716 -21.557   9.962  1.00 69.92           C  
ANISOU 1347  C   CYS A 168     8457   8952   9159   -268   -313    170       C  
ATOM   1348  O   CYS A 168     -12.513 -22.377  10.829  1.00 63.70           O  
ANISOU 1348  O   CYS A 168     7677   8144   8383   -256   -298    164       O  
ATOM   1349  CB  CYS A 168     -10.465 -20.678   9.432  1.00 79.99           C  
ANISOU 1349  CB  CYS A 168     9765  10236  10392   -249   -305    128       C  
ATOM   1350  SG  CYS A 168      -8.958 -20.630   8.422  1.00 96.89           S  
ANISOU 1350  SG  CYS A 168    11931  12382  12499   -254   -308     90       S  
ATOM   1351  N   CYS A 169     -13.809 -20.822   9.973  1.00 71.66           N  
ANISOU 1351  N   CYS A 169     8652   9184   9391   -270   -320    204       N  
ATOM   1352  CA  CYS A 169     -14.795 -21.080  11.007  1.00 80.90           C  
ANISOU 1352  CA  CYS A 169     9805  10343  10591   -260   -309    232       C  
ATOM   1353  C   CYS A 169     -15.674 -22.255  10.684  1.00 88.82           C  
ANISOU 1353  C   CYS A 169    10800  11339  11610   -288   -322    237       C  
ATOM   1354  O   CYS A 169     -16.379 -22.743  11.558  1.00103.57           O  
ANISOU 1354  O   CYS A 169    12655  13193  13502   -281   -312    256       O  
ATOM   1355  CB  CYS A 169     -15.618 -19.851  11.307  1.00 90.04           C  
ANISOU 1355  CB  CYS A 169    10939  11513  11759   -246   -306    269       C  
ATOM   1356  SG  CYS A 169     -14.547 -18.526  11.900  1.00107.93           S  
ANISOU 1356  SG  CYS A 169    13217  13782  14009   -211   -285    261       S  
ATOM   1357  N   GLN A 170     -15.598 -22.749   9.457  1.00 91.54           N  
ANISOU 1357  N   GLN A 170    11151  11690  11940   -322   -344    218       N  
ATOM   1358  CA  GLN A 170     -16.297 -23.971   9.098  1.00 96.05           C  
ANISOU 1358  CA  GLN A 170    11719  12253  12524   -353   -356    215       C  
ATOM   1359  C   GLN A 170     -15.310 -25.071   8.723  1.00 86.89           C  
ANISOU 1359  C   GLN A 170    10588  11076  11349   -364   -354    174       C  
ATOM   1360  O   GLN A 170     -15.689 -26.146   8.256  1.00 83.80           O  
ANISOU 1360  O   GLN A 170    10201  10674  10964   -393   -364    163       O  
ATOM   1361  CB  GLN A 170     -17.283 -23.703   7.958  1.00105.72           C  
ANISOU 1361  CB  GLN A 170    12923  13500  13745   -388   -386    232       C  
ATOM   1362  CG  GLN A 170     -18.730 -23.558   8.417  1.00111.02           C  
ANISOU 1362  CG  GLN A 170    13560  14175  14446   -391   -390    275       C  
ATOM   1363  CD  GLN A 170     -19.176 -22.115   8.611  1.00122.56           C  
ANISOU 1363  CD  GLN A 170    15000  15656  15911   -371   -387    310       C  
ATOM   1364  NE2 GLN A 170     -18.859 -21.248   7.644  1.00114.85           N  
ANISOU 1364  NE2 GLN A 170    14025  14703  14911   -379   -401    306       N  
ATOM   1365  OE1 GLN A 170     -19.816 -21.785   9.620  1.00148.93           O  
ANISOU 1365  OE1 GLN A 170    18323  18990  19275   -348   -371    341       O  
ATOM   1366  N   ALA A 171     -14.031 -24.803   8.930  1.00 83.35           N  
ANISOU 1366  N   ALA A 171    10162  10624  10883   -341   -339    151       N  
ATOM   1367  CA  ALA A 171     -13.004 -25.827   8.767  1.00 89.14           C  
ANISOU 1367  CA  ALA A 171    10924  11339  11607   -344   -330    114       C  
ATOM   1368  C   ALA A 171     -13.235 -26.926   9.767  1.00 96.07           C  
ANISOU 1368  C   ALA A 171    11802  12190  12510   -335   -313    118       C  
ATOM   1369  O   ALA A 171     -13.611 -26.660  10.906  1.00109.39           O  
ANISOU 1369  O   ALA A 171    13475  13872  14216   -310   -299    142       O  
ATOM   1370  CB  ALA A 171     -11.631 -25.251   8.982  1.00 88.83           C  
ANISOU 1370  CB  ALA A 171    10902  11301  11547   -316   -315     95       C  
ATOM   1371  N   ALA A 172     -13.001 -28.166   9.358  1.00 94.01           N  
ANISOU 1371  N   ALA A 172    11558  11911  12251   -355   -313     93       N  
ATOM   1372  CA  ALA A 172     -13.171 -29.289  10.260  1.00 85.03           C  
ANISOU 1372  CA  ALA A 172    10423  10747  11139   -347   -295     96       C  
ATOM   1373  C   ALA A 172     -12.439 -28.990  11.588  1.00 87.04           C  
ANISOU 1373  C   ALA A 172    10679  10993  11397   -302   -268    103       C  
ATOM   1374  O   ALA A 172     -13.041 -28.995  12.667  1.00 89.78           O  
ANISOU 1374  O   ALA A 172    11011  11334  11767   -284   -256    129       O  
ATOM   1375  CB  ALA A 172     -12.670 -30.555   9.600  1.00 80.49           C  
ANISOU 1375  CB  ALA A 172     9871  10151  10559   -370   -293     62       C  
ATOM   1376  N   ASP A 173     -11.154 -28.671  11.491  1.00 89.57           N  
ANISOU 1376  N   ASP A 173    11019  11317  11695   -285   -260     81       N  
ATOM   1377  CA  ASP A 173     -10.385 -28.138  12.614  1.00 89.74           C  
ANISOU 1377  CA  ASP A 173    11043  11340  11715   -245   -239     87       C  
ATOM   1378  C   ASP A 173     -10.111 -26.646  12.371  1.00 89.24           C  
ANISOU 1378  C   ASP A 173    10975  11302  11632   -235   -247     92       C  
ATOM   1379  O   ASP A 173      -9.251 -26.263  11.557  1.00 89.95           O  
ANISOU 1379  O   ASP A 173    11078  11401  11697   -240   -254     70       O  
ATOM   1380  CB  ASP A 173      -9.070 -28.901  12.742  1.00 99.56           C  
ANISOU 1380  CB  ASP A 173    12311  12568  12950   -233   -222     60       C  
ATOM   1381  CG  ASP A 173      -8.235 -28.458  13.932  1.00112.86           C  
ANISOU 1381  CG  ASP A 173    13996  14253  14630   -193   -202     66       C  
ATOM   1382  OD1 ASP A 173      -8.474 -27.367  14.492  1.00113.75           O  
ANISOU 1382  OD1 ASP A 173    14097  14382  14741   -176   -203     84       O  
ATOM   1383  OD2 ASP A 173      -7.322 -29.224  14.296  1.00129.60           O1-
ANISOU 1383  OD2 ASP A 173    16131  16360  16750   -179   -185     51       O1-
ATOM   1384  N   LYS A 174     -10.843 -25.811  13.094  1.00 87.66           N  
ANISOU 1384  N   LYS A 174    10755  11110  11442   -220   -245    121       N  
ATOM   1385  CA  LYS A 174     -10.738 -24.356  12.966  1.00 84.77           C  
ANISOU 1385  CA  LYS A 174    10382  10766  11062   -210   -250    130       C  
ATOM   1386  C   LYS A 174      -9.291 -23.859  13.095  1.00 79.94           C  
ANISOU 1386  C   LYS A 174     9788  10158  10428   -189   -241    108       C  
ATOM   1387  O   LYS A 174      -8.720 -23.356  12.117  1.00 89.05           O  
ANISOU 1387  O   LYS A 174    10950  11325  11560   -200   -252     92       O  
ATOM   1388  CB  LYS A 174     -11.666 -23.659  13.993  1.00 93.93           C  
ANISOU 1388  CB  LYS A 174    11520  11928  12240   -191   -242    165       C  
ATOM   1389  CG  LYS A 174     -13.134 -23.540  13.550  1.00 98.32           C  
ANISOU 1389  CG  LYS A 174    12053  12491  12813   -213   -257    192       C  
ATOM   1390  CD  LYS A 174     -14.164 -23.992  14.596  1.00102.86           C  
ANISOU 1390  CD  LYS A 174    12610  13053  13418   -203   -246    221       C  
ATOM   1391  CE  LYS A 174     -15.286 -24.796  13.944  1.00102.84           C  
ANISOU 1391  CE  LYS A 174    12593  13048  13434   -237   -263    232       C  
ATOM   1392  NZ  LYS A 174     -16.031 -25.700  14.862  1.00107.50           N1+
ANISOU 1392  NZ  LYS A 174    13174  13620  14053   -231   -250    251       N1+
ATOM   1393  N   ALA A 175      -8.694 -24.019  14.278  1.00 71.48           N  
ANISOU 1393  N   ALA A 175     8722   9077   9359   -160   -220    108       N  
ATOM   1394  CA  ALA A 175      -7.366 -23.450  14.561  1.00 67.62           C  
ANISOU 1394  CA  ALA A 175     8248   8596   8851   -139   -211     92       C  
ATOM   1395  C   ALA A 175      -6.303 -23.830  13.561  1.00 70.26           C  
ANISOU 1395  C   ALA A 175     8600   8930   9166   -151   -216     62       C  
ATOM   1396  O   ALA A 175      -5.419 -23.033  13.284  1.00 70.57           O  
ANISOU 1396  O   ALA A 175     8646   8981   9186   -144   -217     50       O  
ATOM   1397  CB  ALA A 175      -6.894 -23.831  15.954  1.00 67.21           C  
ANISOU 1397  CB  ALA A 175     8199   8532   8805   -110   -189     96       C  
ATOM   1398  N   ALA A 176      -6.374 -25.054  13.031  1.00 76.04           N  
ANISOU 1398  N   ALA A 176     9340   9647   9904   -170   -218     49       N  
ATOM   1399  CA  ALA A 176      -5.371 -25.551  12.056  1.00 76.97           C  
ANISOU 1399  CA  ALA A 176     9479   9763  10005   -182   -221     19       C  
ATOM   1400  C   ALA A 176      -5.366 -24.780  10.717  1.00 79.81           C  
ANISOU 1400  C   ALA A 176     9840  10141  10344   -204   -240     10       C  
ATOM   1401  O   ALA A 176      -4.309 -24.473  10.155  1.00 64.60           O  
ANISOU 1401  O   ALA A 176     7926   8221   8397   -201   -240     -9       O  
ATOM   1402  CB  ALA A 176      -5.602 -27.040  11.826  1.00 76.64           C  
ANISOU 1402  CB  ALA A 176     9445   9698   9975   -198   -217      9       C  
ATOM   1403  N   CYS A 177      -6.571 -24.503  10.222  1.00 87.55           N  
ANISOU 1403  N   CYS A 177    10805  11130  11331   -225   -257     26       N  
ATOM   1404  CA  CYS A 177      -6.776 -23.631   9.080  1.00 88.48           C  
ANISOU 1404  CA  CYS A 177    10919  11268  11432   -244   -276     25       C  
ATOM   1405  C   CYS A 177      -6.289 -22.221   9.404  1.00 90.99           C  
ANISOU 1405  C   CYS A 177    11231  11602  11740   -222   -273     34       C  
ATOM   1406  O   CYS A 177      -5.504 -21.611   8.667  1.00 93.99           O  
ANISOU 1406  O   CYS A 177    11620  11994  12099   -223   -277     20       O  
ATOM   1407  CB  CYS A 177      -8.276 -23.590   8.769  1.00 87.58           C  
ANISOU 1407  CB  CYS A 177    10784  11159  11331   -266   -293     48       C  
ATOM   1408  SG  CYS A 177      -8.842 -22.434   7.481  1.00 89.89           S  
ANISOU 1408  SG  CYS A 177    11064  11482  11608   -289   -318     59       S  
ATOM   1409  N   LEU A 178      -6.750 -21.727  10.544  1.00 86.64           N  
ANISOU 1409  N   LEU A 178    10666  11049  11204   -201   -263     56       N  
ATOM   1410  CA  LEU A 178      -6.692 -20.306  10.843  1.00 96.96           C  
ANISOU 1410  CA  LEU A 178    11964  12371  12506   -184   -261     70       C  
ATOM   1411  C   LEU A 178      -5.293 -19.737  11.056  1.00 95.52           C  
ANISOU 1411  C   LEU A 178    11796  12193  12307   -165   -250     52       C  
ATOM   1412  O   LEU A 178      -4.842 -18.860  10.325  1.00 95.89           O  
ANISOU 1412  O   LEU A 178    11844  12253  12338   -168   -257     47       O  
ATOM   1413  CB  LEU A 178      -7.542 -20.026  12.083  1.00101.55           C  
ANISOU 1413  CB  LEU A 178    12530  12947  13109   -166   -250     98       C  
ATOM   1414  CG  LEU A 178      -7.929 -18.567  12.322  1.00104.22           C  
ANISOU 1414  CG  LEU A 178    12855  13298  13447   -154   -248    118       C  
ATOM   1415  CD1 LEU A 178      -8.727 -18.037  11.125  1.00100.28           C  
ANISOU 1415  CD1 LEU A 178    12342  12814  12946   -178   -268    131       C  
ATOM   1416  CD2 LEU A 178      -8.689 -18.439  13.647  1.00107.03           C  
ANISOU 1416  CD2 LEU A 178    13198  13644  13822   -134   -233    143       C  
ATOM   1417  N   LEU A 179      -4.625 -20.262  12.070  1.00 92.25           N  
ANISOU 1417  N   LEU A 179    11389  11766  11895   -144   -234     45       N  
ATOM   1418  CA  LEU A 179      -3.395 -19.689  12.599  1.00 84.62           C  
ANISOU 1418  CA  LEU A 179    10432  10804  10916   -122   -223     34       C  
ATOM   1419  C   LEU A 179      -2.348 -19.385  11.525  1.00 76.03           C  
ANISOU 1419  C   LEU A 179     9356   9725   9807   -131   -229     12       C  
ATOM   1420  O   LEU A 179      -1.913 -18.237  11.394  1.00 75.67           O  
ANISOU 1420  O   LEU A 179     9309   9692   9751   -124   -230     13       O  
ATOM   1421  CB  LEU A 179      -2.837 -20.620  13.689  1.00 86.11           C  
ANISOU 1421  CB  LEU A 179    10629  10979  11112   -104   -206     29       C  
ATOM   1422  CG  LEU A 179      -3.852 -20.917  14.813  1.00 87.10           C  
ANISOU 1422  CG  LEU A 179    10742  11095  11258    -93   -198     52       C  
ATOM   1423  CD1 LEU A 179      -3.348 -22.046  15.699  1.00 89.62           C  
ANISOU 1423  CD1 LEU A 179    11069  11400  11583    -78   -183     48       C  
ATOM   1424  CD2 LEU A 179      -4.203 -19.672  15.626  1.00 83.55           C  
ANISOU 1424  CD2 LEU A 179    10282  10653  10809    -76   -192     70       C  
ATOM   1425  N   PRO A 180      -1.949 -20.394  10.746  1.00 67.06           N  
ANISOU 1425  N   PRO A 180     8233   8583   8665   -145   -232     -6       N  
ATOM   1426  CA  PRO A 180      -0.913 -20.174   9.738  1.00 71.16           C  
ANISOU 1426  CA  PRO A 180     8764   9109   9163   -152   -236    -27       C  
ATOM   1427  C   PRO A 180      -1.241 -19.008   8.816  1.00 68.28           C  
ANISOU 1427  C   PRO A 180     8392   8763   8788   -164   -250    -21       C  
ATOM   1428  O   PRO A 180      -0.388 -18.189   8.452  1.00 59.11           O  
ANISOU 1428  O   PRO A 180     7233   7612   7612   -158   -250    -28       O  
ATOM   1429  CB  PRO A 180      -0.908 -21.489   8.934  1.00 72.19           C  
ANISOU 1429  CB  PRO A 180     8908   9229   9293   -171   -239    -44       C  
ATOM   1430  CG  PRO A 180      -2.047 -22.303   9.449  1.00 73.88           C  
ANISOU 1430  CG  PRO A 180     9114   9430   9528   -178   -239    -30       C  
ATOM   1431  CD  PRO A 180      -2.374 -21.794  10.810  1.00 69.06           C  
ANISOU 1431  CD  PRO A 180     8490   8819   8931   -155   -230    -10       C  
ATOM   1432  N   LYS A 181      -2.505 -18.972   8.445  1.00 70.02           N  
ANISOU 1432  N   LYS A 181     8600   8987   9017   -181   -263     -5       N  
ATOM   1433  CA  LYS A 181      -3.002 -17.960   7.574  1.00 77.17           C  
ANISOU 1433  CA  LYS A 181     9496   9910   9916   -194   -277      6       C  
ATOM   1434  C   LYS A 181      -2.822 -16.592   8.210  1.00 73.42           C  
ANISOU 1434  C   LYS A 181     9011   9443   9442   -174   -270     20       C  
ATOM   1435  O   LYS A 181      -2.328 -15.674   7.574  1.00 86.69           O  
ANISOU 1435  O   LYS A 181    10692  11136  11109   -174   -273     17       O  
ATOM   1436  CB  LYS A 181      -4.466 -18.264   7.274  1.00 88.18           C  
ANISOU 1436  CB  LYS A 181    10876  11307  11323   -214   -291     25       C  
ATOM   1437  CG  LYS A 181      -4.669 -19.621   6.622  1.00 89.82           C  
ANISOU 1437  CG  LYS A 181    11094  11506  11529   -238   -298     10       C  
ATOM   1438  CD  LYS A 181      -5.991 -19.669   5.886  1.00100.54           C  
ANISOU 1438  CD  LYS A 181    12438  12873  12891   -265   -318     26       C  
ATOM   1439  CE  LYS A 181      -5.850 -20.356   4.537  1.00103.31           C  
ANISOU 1439  CE  LYS A 181    12801  13228  13223   -295   -333      5       C  
ATOM   1440  NZ  LYS A 181      -7.089 -20.184   3.731  1.00104.29           N1+
ANISOU 1440  NZ  LYS A 181    12910  13368  13347   -322   -355     23       N1+
ATOM   1441  N   LEU A 182      -3.201 -16.472   9.477  1.00 73.83           N  
ANISOU 1441  N   LEU A 182     9056   9487   9510   -156   -258     34       N  
ATOM   1442  CA  LEU A 182      -3.074 -15.227  10.219  1.00 74.16           C  
ANISOU 1442  CA  LEU A 182     9091   9533   9554   -136   -248     45       C  
ATOM   1443  C   LEU A 182      -1.617 -14.839  10.478  1.00 74.87           C  
ANISOU 1443  C   LEU A 182     9194   9625   9630   -121   -239     26       C  
ATOM   1444  O   LEU A 182      -1.267 -13.656  10.428  1.00 69.65           O  
ANISOU 1444  O   LEU A 182     8530   8971   8963   -114   -237     28       O  
ATOM   1445  CB  LEU A 182      -3.820 -15.348  11.547  1.00 85.23           C  
ANISOU 1445  CB  LEU A 182    10485  10925  10975   -121   -237     63       C  
ATOM   1446  CG  LEU A 182      -5.355 -15.482  11.488  1.00 90.81           C  
ANISOU 1446  CG  LEU A 182    11175  11631  11700   -131   -244     89       C  
ATOM   1447  CD1 LEU A 182      -5.889 -15.472  12.913  1.00 96.33           C  
ANISOU 1447  CD1 LEU A 182    11868  12319  12416   -111   -228    106       C  
ATOM   1448  CD2 LEU A 182      -6.066 -14.387  10.691  1.00 87.42           C  
ANISOU 1448  CD2 LEU A 182    10730  11214  11270   -142   -253    108       C  
ATOM   1449  N   ASP A 183      -0.765 -15.822  10.753  1.00 77.39           N  
ANISOU 1449  N   ASP A 183     9526   9935   9944   -116   -233      8       N  
ATOM   1450  CA  ASP A 183       0.663 -15.555  10.927  1.00 78.50           C  
ANISOU 1450  CA  ASP A 183     9677  10078  10071   -103   -225    -10       C  
ATOM   1451  C   ASP A 183       1.277 -15.122   9.615  1.00 73.21           C  
ANISOU 1451  C   ASP A 183     9012   9419   9385   -116   -234    -22       C  
ATOM   1452  O   ASP A 183       2.152 -14.276   9.606  1.00 84.30           O  
ANISOU 1452  O   ASP A 183    10418  10831  10781   -108   -230    -28       O  
ATOM   1453  CB  ASP A 183       1.413 -16.793  11.424  1.00 83.64           C  
ANISOU 1453  CB  ASP A 183    10338  10718  10722    -95   -217    -24       C  
ATOM   1454  CG  ASP A 183       1.027 -17.200  12.830  1.00 85.75           C  
ANISOU 1454  CG  ASP A 183    10602  10976  11003    -79   -206    -13       C  
ATOM   1455  OD1 ASP A 183       0.210 -16.490  13.489  1.00 73.48           O  
ANISOU 1455  OD1 ASP A 183     9037   9423   9457    -72   -204      5       O  
ATOM   1456  OD2 ASP A 183       1.579 -18.254  13.247  1.00 82.76           O1-
ANISOU 1456  OD2 ASP A 183    10231  10589  10626    -71   -198    -21       O1-
ATOM   1457  N   GLU A 184       0.838 -15.714   8.511  1.00 72.86           N  
ANISOU 1457  N   GLU A 184     8970   9377   9338   -137   -245    -26       N  
ATOM   1458  CA  GLU A 184       1.265 -15.252   7.208  1.00 77.44           C  
ANISOU 1458  CA  GLU A 184     9554   9969   9901   -150   -254    -34       C  
ATOM   1459  C   GLU A 184       0.793 -13.817   6.971  1.00 76.63           C  
ANISOU 1459  C   GLU A 184     9438   9880   9799   -150   -259    -17       C  
ATOM   1460  O   GLU A 184       1.487 -13.059   6.297  1.00 74.70           O  
ANISOU 1460  O   GLU A 184     9196   9645   9543   -151   -260    -22       O  
ATOM   1461  CB  GLU A 184       0.771 -16.171   6.095  1.00 91.52           C  
ANISOU 1461  CB  GLU A 184    11343  11752  11678   -174   -266    -41       C  
ATOM   1462  CG  GLU A 184       1.381 -15.838   4.734  1.00108.53           C  
ANISOU 1462  CG  GLU A 184    13505  13920  13812   -187   -274    -53       C  
ATOM   1463  CD  GLU A 184       1.893 -17.071   4.005  1.00122.78           C  
ANISOU 1463  CD  GLU A 184    15328  15717  15606   -199   -273    -76       C  
ATOM   1464  OE1 GLU A 184       1.057 -17.924   3.616  1.00133.75           O  
ANISOU 1464  OE1 GLU A 184    16719  17101  16997   -218   -282    -77       O  
ATOM   1465  OE2 GLU A 184       3.130 -17.188   3.820  1.00115.25           O1-
ANISOU 1465  OE2 GLU A 184    14387  14761  14641   -190   -264    -93       O1-
ATOM   1466  N   LEU A 185      -0.362 -13.442   7.531  1.00 73.28           N  
ANISOU 1466  N   LEU A 185     8999   9453   9389   -149   -260      6       N  
ATOM   1467  CA  LEU A 185      -0.837 -12.060   7.484  1.00 74.22           C  
ANISOU 1467  CA  LEU A 185     9105   9582   9513   -145   -260     25       C  
ATOM   1468  C   LEU A 185      -0.045 -11.159   8.422  1.00 76.06           C  
ANISOU 1468  C   LEU A 185     9341   9812   9747   -124   -246     22       C  
ATOM   1469  O   LEU A 185       0.506 -10.182   7.956  1.00 81.96           O  
ANISOU 1469  O   LEU A 185    10087  10566  10486   -123   -245     20       O  
ATOM   1470  CB  LEU A 185      -2.337 -11.954   7.784  1.00 77.07           C  
ANISOU 1470  CB  LEU A 185     9449   9941   9891   -149   -264     52       C  
ATOM   1471  CG  LEU A 185      -3.368 -12.253   6.690  1.00 78.63           C  
ANISOU 1471  CG  LEU A 185     9637  10149  10089   -173   -282     64       C  
ATOM   1472  CD1 LEU A 185      -4.768 -11.786   7.119  1.00 79.76           C  
ANISOU 1472  CD1 LEU A 185     9760  10293  10252   -172   -282     96       C  
ATOM   1473  CD2 LEU A 185      -3.018 -11.578   5.380  1.00 79.90           C  
ANISOU 1473  CD2 LEU A 185     9799  10328  10233   -185   -292     62       C  
ATOM   1474  N   ARG A 186       0.031 -11.474   9.719  1.00 83.81           N  
ANISOU 1474  N   ARG A 186    10325  10782  10737   -108   -234     21       N  
ATOM   1475  CA  ARG A 186       0.906 -10.714  10.658  1.00 90.51           C  
ANISOU 1475  CA  ARG A 186    11178  11629  11584    -90   -221     14       C  
ATOM   1476  C   ARG A 186       2.293 -10.480  10.040  1.00 77.29           C  
ANISOU 1476  C   ARG A 186     9513   9961   9893    -91   -222     -6       C  
ATOM   1477  O   ARG A 186       2.782  -9.364  10.073  1.00 73.63           O  
ANISOU 1477  O   ARG A 186     9048   9502   9426    -86   -217     -6       O  
ATOM   1478  CB  ARG A 186       1.016 -11.390  12.051  1.00 99.82           C  
ANISOU 1478  CB  ARG A 186    12361  12797  12769    -74   -210     12       C  
ATOM   1479  CG  ARG A 186       1.982 -10.719  13.050  1.00112.87           C  
ANISOU 1479  CG  ARG A 186    14019  14449  14415    -58   -199      2       C  
ATOM   1480  CD  ARG A 186       3.357 -11.418  13.121  1.00133.89           C  
ANISOU 1480  CD  ARG A 186    16692  17113  17065    -53   -198    -19       C  
ATOM   1481  NE  ARG A 186       4.458 -10.603  13.696  1.00155.13           N  
ANISOU 1481  NE  ARG A 186    19386  19808  19746    -43   -192    -29       N  
ATOM   1482  CZ  ARG A 186       5.777 -10.810  13.500  1.00152.96           C  
ANISOU 1482  CZ  ARG A 186    19118  19539  19460    -42   -192    -45       C  
ATOM   1483  NH1 ARG A 186       6.201 -11.804  12.733  1.00154.93           N1+
ANISOU 1483  NH1 ARG A 186    19372  19789  19706    -48   -197    -54       N1+
ATOM   1484  NH2 ARG A 186       6.694 -10.010  14.054  1.00134.90           N  
ANISOU 1484  NH2 ARG A 186    16832  17257  17166    -34   -188    -53       N  
ATOM   1485  N   ASP A 187       2.894 -11.520   9.455  1.00 74.14           N  
ANISOU 1485  N   ASP A 187     9123   9562   9485    -98   -227    -21       N  
ATOM   1486  CA  ASP A 187       4.171 -11.415   8.748  1.00 71.41           C  
ANISOU 1486  CA  ASP A 187     8786   9223   9125   -100   -227    -39       C  
ATOM   1487  C   ASP A 187       4.051 -10.446   7.567  1.00 77.35           C  
ANISOU 1487  C   ASP A 187     9533   9987   9870   -111   -235    -33       C  
ATOM   1488  O   ASP A 187       4.735  -9.415   7.565  1.00 85.17           O  
ANISOU 1488  O   ASP A 187    10522  10982  10857   -105   -230    -35       O  
ATOM   1489  CB  ASP A 187       4.651 -12.789   8.252  1.00 72.65           C  
ANISOU 1489  CB  ASP A 187     8953   9376   9274   -106   -229    -54       C  
ATOM   1490  CG  ASP A 187       5.661 -13.462   9.191  1.00 83.22           C  
ANISOU 1490  CG  ASP A 187    10299  10707  10612    -90   -218    -66       C  
ATOM   1491  OD1 ASP A 187       6.535 -14.222   8.704  1.00 82.50           O  
ANISOU 1491  OD1 ASP A 187    10218  10615  10513    -91   -216    -81       O  
ATOM   1492  OD2 ASP A 187       5.601 -13.249  10.417  1.00 93.20           O1-
ANISOU 1492  OD2 ASP A 187    11560  11968  11884    -76   -211    -60       O1-
ATOM   1493  N   GLU A 188       3.177 -10.754   6.595  1.00 70.82           N  
ANISOU 1493  N   GLU A 188     8702   9164   9042   -128   -246    -26       N  
ATOM   1494  CA  GLU A 188       3.069  -9.987   5.330  1.00 78.04           C  
ANISOU 1494  CA  GLU A 188     9612  10092   9946   -140   -255    -20       C  
ATOM   1495  C   GLU A 188       2.926  -8.488   5.530  1.00 73.58           C  
ANISOU 1495  C   GLU A 188     9037   9532   9389   -132   -249     -4       C  
ATOM   1496  O   GLU A 188       3.546  -7.681   4.809  1.00 74.35           O  
ANISOU 1496  O   GLU A 188     9133   9638   9477   -134   -249     -6       O  
ATOM   1497  CB  GLU A 188       1.882 -10.485   4.486  1.00 86.07           C  
ANISOU 1497  CB  GLU A 188    10624  11115  10963   -159   -269     -9       C  
ATOM   1498  CG  GLU A 188       1.892 -10.009   3.025  1.00 98.49           C  
ANISOU 1498  CG  GLU A 188    12196  12706  12522   -175   -280     -6       C  
ATOM   1499  CD  GLU A 188       1.709 -11.141   1.993  1.00120.28           C  
ANISOU 1499  CD  GLU A 188    14964  15469  15267   -195   -292    -18       C  
ATOM   1500  OE1 GLU A 188       1.451 -12.322   2.364  1.00120.12           O  
ANISOU 1500  OE1 GLU A 188    14952  15438  15252   -199   -293    -26       O  
ATOM   1501  OE2 GLU A 188       1.830 -10.851   0.780  1.00127.16           O1-
ANISOU 1501  OE2 GLU A 188    15837  16355  16123   -208   -301    -18       O1-
ATOM   1502  N   GLY A 189       2.089  -8.143   6.509  1.00 71.48           N  
ANISOU 1502  N   GLY A 189     8762   9259   9139   -124   -244     11       N  
ATOM   1503  CA  GLY A 189       1.709  -6.761   6.819  1.00 69.03           C  
ANISOU 1503  CA  GLY A 189     8442   8949   8839   -116   -236     28       C  
ATOM   1504  C   GLY A 189       2.868  -5.943   7.321  1.00 65.58           C  
ANISOU 1504  C   GLY A 189     8011   8509   8399   -104   -224     16       C  
ATOM   1505  O   GLY A 189       3.190  -4.895   6.763  1.00 62.26           O  
ANISOU 1505  O   GLY A 189     7586   8094   7976   -105   -222     20       O  
ATOM   1506  N   LYS A 190       3.492  -6.428   8.381  1.00 67.33           N  
ANISOU 1506  N   LYS A 190     8240   8722   8620    -93   -217      2       N  
ATOM   1507  CA  LYS A 190       4.736  -5.836   8.864  1.00 73.39           C  
ANISOU 1507  CA  LYS A 190     9015   9489   9383    -84   -209    -13       C  
ATOM   1508  C   LYS A 190       5.705  -5.442   7.693  1.00 69.13           C  
ANISOU 1508  C   LYS A 190     8476   8959   8830    -92   -213    -22       C  
ATOM   1509  O   LYS A 190       6.082  -4.256   7.595  1.00 64.57           O  
ANISOU 1509  O   LYS A 190     7895   8382   8254    -90   -207    -19       O  
ATOM   1510  CB  LYS A 190       5.430  -6.773   9.876  1.00 76.03           C  
ANISOU 1510  CB  LYS A 190     9358   9818   9713    -75   -205    -28       C  
ATOM   1511  CG  LYS A 190       4.586  -7.169  11.069  1.00 75.87           C  
ANISOU 1511  CG  LYS A 190     9336   9788   9702    -66   -200    -20       C  
ATOM   1512  CD  LYS A 190       5.336  -7.046  12.369  1.00 82.57           C  
ANISOU 1512  CD  LYS A 190    10190  10633  10549    -53   -190    -30       C  
ATOM   1513  CE  LYS A 190       5.087  -5.697  13.004  1.00 95.15           C  
ANISOU 1513  CE  LYS A 190    11782  12223  12148    -47   -180    -24       C  
ATOM   1514  NZ  LYS A 190       6.336  -5.162  13.621  1.00108.80           N1+
ANISOU 1514  NZ  LYS A 190    13517  13954  13868    -42   -175    -40       N1+
ATOM   1515  N   ALA A 191       6.087  -6.404   6.825  1.00 54.97           N  
ANISOU 1515  N   ALA A 191     6689   7171   7026   -100   -221    -32       N  
ATOM   1516  CA  ALA A 191       6.873  -6.082   5.639  1.00 49.47           C  
ANISOU 1516  CA  ALA A 191     5994   6484   6317   -107   -225    -38       C  
ATOM   1517  C   ALA A 191       6.156  -5.061   4.804  1.00 52.97           C  
ANISOU 1517  C   ALA A 191     6427   6935   6763   -114   -228    -20       C  
ATOM   1518  O   ALA A 191       6.720  -3.995   4.503  1.00 53.33           O  
ANISOU 1518  O   ALA A 191     6470   6985   6809   -112   -222    -18       O  
ATOM   1519  CB  ALA A 191       7.175  -7.293   4.801  1.00 46.49           C  
ANISOU 1519  CB  ALA A 191     5626   6112   5928   -116   -232    -50       C  
ATOM   1520  N   SER A 192       4.906  -5.353   4.444  1.00 59.50           N  
ANISOU 1520  N   SER A 192     7248   7766   7595   -123   -236     -4       N  
ATOM   1521  CA  SER A 192       4.146  -4.419   3.605  1.00 65.37           C  
ANISOU 1521  CA  SER A 192     7979   8518   8340   -130   -240     17       C  
ATOM   1522  C   SER A 192       4.150  -2.984   4.162  1.00 64.37           C  
ANISOU 1522  C   SER A 192     7844   8386   8227   -119   -226     29       C  
ATOM   1523  O   SER A 192       4.289  -2.004   3.411  1.00 64.55           O  
ANISOU 1523  O   SER A 192     7860   8415   8249   -121   -224     39       O  
ATOM   1524  CB  SER A 192       2.726  -4.881   3.415  1.00 67.52           C  
ANISOU 1524  CB  SER A 192     8242   8793   8618   -139   -249     35       C  
ATOM   1525  OG  SER A 192       2.071  -3.973   2.546  1.00 78.14           O  
ANISOU 1525  OG  SER A 192     9575  10151   9966   -145   -253     58       O  
ATOM   1526  N   SER A 193       4.034  -2.876   5.478  1.00 63.73           N  
ANISOU 1526  N   SER A 193     7765   8291   8157   -108   -216     27       N  
ATOM   1527  CA  SER A 193       3.962  -1.572   6.131  1.00 62.94           C  
ANISOU 1527  CA  SER A 193     7661   8184   8071    -98   -202     36       C  
ATOM   1528  C   SER A 193       5.287  -0.831   6.075  1.00 61.60           C  
ANISOU 1528  C   SER A 193     7496   8013   7896    -95   -194     21       C  
ATOM   1529  O   SER A 193       5.298   0.377   5.844  1.00 62.62           O  
ANISOU 1529  O   SER A 193     7619   8140   8033    -93   -186     31       O  
ATOM   1530  CB  SER A 193       3.495  -1.704   7.592  1.00 64.05           C  
ANISOU 1530  CB  SER A 193     7804   8310   8223    -87   -192     36       C  
ATOM   1531  OG  SER A 193       3.916  -0.615   8.369  1.00 68.74           O  
ANISOU 1531  OG  SER A 193     8400   8894   8823    -77   -177     33       O  
ATOM   1532  N   ALA A 194       6.404  -1.527   6.287  1.00 60.45           N  
ANISOU 1532  N   ALA A 194     7360   7868   7739    -94   -197     -1       N  
ATOM   1533  CA  ALA A 194       7.711  -0.832   6.315  1.00 58.94           C  
ANISOU 1533  CA  ALA A 194     7173   7677   7544    -91   -190    -15       C  
ATOM   1534  C   ALA A 194       8.105  -0.291   4.924  1.00 62.05           C  
ANISOU 1534  C   ALA A 194     7563   8082   7933    -99   -193    -10       C  
ATOM   1535  O   ALA A 194       8.482   0.889   4.818  1.00 59.31           O  
ANISOU 1535  O   ALA A 194     7211   7732   7591    -97   -184     -6       O  
ATOM   1536  CB  ALA A 194       8.808  -1.701   6.911  1.00 56.81           C  
ANISOU 1536  CB  ALA A 194     6913   7407   7266    -87   -192    -37       C  
ATOM   1537  N   LYS A 195       7.987  -1.143   3.881  1.00 64.32           N  
ANISOU 1537  N   LYS A 195     7850   8380   8207   -107   -205     -9       N  
ATOM   1538  CA  LYS A 195       8.099  -0.749   2.472  1.00 57.41           C  
ANISOU 1538  CA  LYS A 195     6971   7518   7324   -115   -209     -1       C  
ATOM   1539  C   LYS A 195       7.505   0.631   2.344  1.00 56.88           C  
ANISOU 1539  C   LYS A 195     6892   7449   7270   -113   -201     20       C  
ATOM   1540  O   LYS A 195       8.187   1.604   1.976  1.00 53.07           O  
ANISOU 1540  O   LYS A 195     6406   6967   6790   -111   -193     22       O  
ATOM   1541  CB  LYS A 195       7.370  -1.772   1.552  1.00 67.52           C  
ANISOU 1541  CB  LYS A 195     8253   8810   8593   -126   -223      3       C  
ATOM   1542  CG  LYS A 195       8.258  -2.580   0.557  1.00 72.17           C  
ANISOU 1542  CG  LYS A 195     8852   9408   9161   -133   -230    -13       C  
ATOM   1543  CD  LYS A 195       7.749  -4.011   0.209  1.00 75.17           C  
ANISOU 1543  CD  LYS A 195     9240   9791   9530   -142   -241    -20       C  
ATOM   1544  CE  LYS A 195       6.435  -4.077  -0.612  1.00 85.67           C  
ANISOU 1544  CE  LYS A 195    10562  11132  10856   -156   -254     -1       C  
ATOM   1545  NZ  LYS A 195       5.487  -5.262  -0.413  1.00 80.90           N1+
ANISOU 1545  NZ  LYS A 195     9962  10526  10252   -165   -264     -3       N1+
ATOM   1546  N   GLN A 196       6.230   0.727   2.700  1.00 60.64           N  
ANISOU 1546  N   GLN A 196     7361   7921   7758   -112   -201     38       N  
ATOM   1547  CA  GLN A 196       5.523   1.994   2.598  1.00 66.96           C  
ANISOU 1547  CA  GLN A 196     8149   8719   8573   -109   -192     62       C  
ATOM   1548  C   GLN A 196       6.112   3.132   3.390  1.00 67.11           C  
ANISOU 1548  C   GLN A 196     8170   8724   8606   -100   -174     58       C  
ATOM   1549  O   GLN A 196       6.109   4.269   2.917  1.00 66.11           O  
ANISOU 1549  O   GLN A 196     8035   8596   8487    -99   -165     72       O  
ATOM   1550  CB  GLN A 196       4.079   1.860   3.029  1.00 69.75           C  
ANISOU 1550  CB  GLN A 196     8495   9069   8939   -108   -193     82       C  
ATOM   1551  CG  GLN A 196       3.283   3.132   2.760  1.00 68.28           C  
ANISOU 1551  CG  GLN A 196     8294   8881   8768   -104   -182    112       C  
ATOM   1552  CD  GLN A 196       3.215   3.480   1.297  1.00 70.50           C  
ANISOU 1552  CD  GLN A 196     8566   9181   9042   -112   -190    128       C  
ATOM   1553  NE2 GLN A 196       3.642   2.553   0.432  1.00 73.25           N  
ANISOU 1553  NE2 GLN A 196     8919   9543   9368   -123   -206    116       N  
ATOM   1554  OE1 GLN A 196       2.748   4.559   0.937  1.00 74.36           O  
ANISOU 1554  OE1 GLN A 196     9041   9670   9542   -109   -180    153       O  
ATOM   1555  N   ARG A 197       6.577   2.838   4.600  1.00 72.85           N  
ANISOU 1555  N   ARG A 197     8907   9439   9334    -94   -169     39       N  
ATOM   1556  CA  ARG A 197       7.141   3.871   5.479  1.00 70.96           C  
ANISOU 1556  CA  ARG A 197     8671   9185   9105    -88   -153     31       C  
ATOM   1557  C   ARG A 197       8.345   4.494   4.830  1.00 64.41           C  
ANISOU 1557  C   ARG A 197     7841   8359   8271    -91   -151     22       C  
ATOM   1558  O   ARG A 197       8.523   5.701   4.874  1.00 75.94           O  
ANISOU 1558  O   ARG A 197     9299   9811   9745    -89   -137     28       O  
ATOM   1559  CB  ARG A 197       7.534   3.322   6.846  1.00 68.92           C  
ANISOU 1559  CB  ARG A 197     8424   8918   8845    -82   -151     11       C  
ATOM   1560  CG  ARG A 197       7.969   4.391   7.838  1.00 68.72           C  
ANISOU 1560  CG  ARG A 197     8403   8878   8830    -78   -135      2       C  
ATOM   1561  CD  ARG A 197       6.810   5.277   8.297  1.00 70.35           C  
ANISOU 1561  CD  ARG A 197     8606   9070   9053    -72   -120     21       C  
ATOM   1562  NE  ARG A 197       7.224   6.347   9.212  1.00 71.16           N  
ANISOU 1562  NE  ARG A 197     8715   9156   9165    -69   -103     11       N  
ATOM   1563  CZ  ARG A 197       7.530   7.594   8.842  1.00 88.20           C  
ANISOU 1563  CZ  ARG A 197    10871  11307  11334    -70    -90     16       C  
ATOM   1564  NH1 ARG A 197       7.478   7.999   7.555  1.00100.79           N1+
ANISOU 1564  NH1 ARG A 197    12454  12909  12932    -74    -91     33       N1+
ATOM   1565  NH2 ARG A 197       7.879   8.462   9.775  1.00 93.72           N  
ANISOU 1565  NH2 ARG A 197    11579  11990  12041    -69    -74      4       N  
ATOM   1566  N   LEU A 198       9.163   3.690   4.197  1.00 57.07           N  
ANISOU 1566  N   LEU A 198     6916   7442   7327    -96   -162     10       N  
ATOM   1567  CA  LEU A 198      10.223   4.265   3.445  1.00 61.06           C  
ANISOU 1567  CA  LEU A 198     7419   7952   7828    -99   -159      6       C  
ATOM   1568  C   LEU A 198       9.668   5.299   2.490  1.00 66.28           C  
ANISOU 1568  C   LEU A 198     8069   8616   8498   -100   -153     30       C  
ATOM   1569  O   LEU A 198       9.975   6.491   2.604  1.00 66.16           O  
ANISOU 1569  O   LEU A 198     8050   8592   8496    -98   -139     34       O  
ATOM   1570  CB  LEU A 198      10.913   3.197   2.654  1.00 66.29           C  
ANISOU 1570  CB  LEU A 198     8086   8629   8473   -103   -171     -5       C  
ATOM   1571  CG  LEU A 198      12.098   3.686   1.861  1.00 70.17           C  
ANISOU 1571  CG  LEU A 198     8576   9127   8960   -106   -168    -10       C  
ATOM   1572  CD1 LEU A 198      12.929   4.690   2.620  1.00 76.20           C  
ANISOU 1572  CD1 LEU A 198     9338   9878   9735   -103   -156    -18       C  
ATOM   1573  CD2 LEU A 198      12.948   2.478   1.550  1.00 77.35           C  
ANISOU 1573  CD2 LEU A 198     9493  10045   9852   -107   -177    -27       C  
ATOM   1574  N   LYS A 199       8.823   4.835   1.576  1.00 66.72           N  
ANISOU 1574  N   LYS A 199     8120   8685   8547   -105   -163     46       N  
ATOM   1575  CA  LYS A 199       8.301   5.672   0.505  1.00 71.93           C  
ANISOU 1575  CA  LYS A 199     8767   9353   9211   -106   -160     71       C  
ATOM   1576  C   LYS A 199       7.865   7.003   1.044  1.00 79.10           C  
ANISOU 1576  C   LYS A 199     9668  10245  10142   -100   -142     87       C  
ATOM   1577  O   LYS A 199       8.176   8.048   0.463  1.00 95.74           O  
ANISOU 1577  O   LYS A 199    11768  12351  12256    -99   -131     98       O  
ATOM   1578  CB  LYS A 199       7.107   5.009  -0.178  1.00 71.08           C  
ANISOU 1578  CB  LYS A 199     8653   9259   9096   -112   -174     90       C  
ATOM   1579  CG  LYS A 199       7.447   3.644  -0.751  1.00 77.38           C  
ANISOU 1579  CG  LYS A 199     9460  10071   9871   -120   -191     74       C  
ATOM   1580  CD  LYS A 199       6.239   2.881  -1.223  1.00 75.29           C  
ANISOU 1580  CD  LYS A 199     9191   9818   9599   -128   -206     87       C  
ATOM   1581  CE  LYS A 199       6.564   1.416  -1.480  1.00 67.64           C  
ANISOU 1581  CE  LYS A 199     8234   8856   8609   -136   -220     66       C  
ATOM   1582  NZ  LYS A 199       7.323   1.344  -2.748  1.00 67.96           N1+
ANISOU 1582  NZ  LYS A 199     8279   8912   8631   -142   -224     62       N1+
ATOM   1583  N   CYS A 200       7.156   6.965   2.166  1.00 77.50           N  
ANISOU 1583  N   CYS A 200     9468  10029   9950    -94   -136     87       N  
ATOM   1584  CA  CYS A 200       6.586   8.176   2.748  1.00 82.98           C  
ANISOU 1584  CA  CYS A 200    10157  10706  10667    -87   -116    102       C  
ATOM   1585  C   CYS A 200       7.649   9.145   3.215  1.00 77.59           C  
ANISOU 1585  C   CYS A 200     9480  10008   9993    -86   -101     87       C  
ATOM   1586  O   CYS A 200       7.609  10.334   2.903  1.00 72.98           O  
ANISOU 1586  O   CYS A 200     8890   9416   9424    -83    -85    101       O  
ATOM   1587  CB  CYS A 200       5.651   7.822   3.910  1.00 97.08           C  
ANISOU 1587  CB  CYS A 200    11947  12480  12461    -81   -113    103       C  
ATOM   1588  SG  CYS A 200       3.923   7.586   3.404  1.00108.59           S  
ANISOU 1588  SG  CYS A 200    13388  13947  13925    -80   -118    139       S  
ATOM   1589  N   ALA A 201       8.605   8.613   3.955  1.00 79.44           N  
ANISOU 1589  N   ALA A 201     9726  10239  10218    -88   -105     58       N  
ATOM   1590  CA  ALA A 201       9.652   9.409   4.541  1.00 77.04           C  
ANISOU 1590  CA  ALA A 201     9428   9922   9920    -89    -94     40       C  
ATOM   1591  C   ALA A 201      10.454  10.101   3.428  1.00 77.17           C  
ANISOU 1591  C   ALA A 201     9438   9945   9939    -93    -91     46       C  
ATOM   1592  O   ALA A 201      10.729  11.296   3.533  1.00 94.21           O  
ANISOU 1592  O   ALA A 201    11594  12089  12112    -93    -74     49       O  
ATOM   1593  CB  ALA A 201      10.539   8.533   5.421  1.00 74.87           C  
ANISOU 1593  CB  ALA A 201     9166   9650   9633    -91   -103     11       C  
ATOM   1594  N   SER A 202      10.794   9.386   2.355  1.00 69.27           N  
ANISOU 1594  N   SER A 202     8434   8964   8922    -97   -105     48       N  
ATOM   1595  CA  SER A 202      11.507  10.007   1.223  1.00 73.10           C  
ANISOU 1595  CA  SER A 202     8911   9456   9406    -99   -102     56       C  
ATOM   1596  C   SER A 202      10.768  11.164   0.630  1.00 71.61           C  
ANISOU 1596  C   SER A 202     8711   9263   9234    -96    -87     85       C  
ATOM   1597  O   SER A 202      11.350  12.209   0.359  1.00 69.63           O  
ANISOU 1597  O   SER A 202     8456   9005   8997    -96    -74     89       O  
ATOM   1598  CB  SER A 202      11.742   9.013   0.130  1.00 77.92           C  
ANISOU 1598  CB  SER A 202     9521  10089   9996   -103   -118     57       C  
ATOM   1599  OG  SER A 202      11.972   7.789   0.763  1.00102.52           O  
ANISOU 1599  OG  SER A 202    12647  13208  13098   -104   -131     36       O  
ATOM   1600  N   LEU A 203       9.474  10.983   0.435  1.00 75.59           N  
ANISOU 1600  N   LEU A 203     9208   9772   9740    -93    -90    107       N  
ATOM   1601  CA  LEU A 203       8.646  12.088  -0.019  1.00 82.62           C  
ANISOU 1601  CA  LEU A 203    10086  10657  10649    -88    -75    138       C  
ATOM   1602  C   LEU A 203       8.690  13.262   0.962  1.00 77.93           C  
ANISOU 1602  C   LEU A 203     9495  10035  10080    -83    -51    135       C  
ATOM   1603  O   LEU A 203       8.804  14.415   0.556  1.00 86.80           O  
ANISOU 1603  O   LEU A 203    10611  11150  11220    -81    -34    151       O  
ATOM   1604  CB  LEU A 203       7.210  11.628  -0.284  1.00 89.26           C  
ANISOU 1604  CB  LEU A 203    10918  11508  11488    -86    -83    163       C  
ATOM   1605  CG  LEU A 203       6.987  10.639  -1.462  1.00 98.45           C  
ANISOU 1605  CG  LEU A 203    12077  12701  12629    -93   -106    171       C  
ATOM   1606  CD1 LEU A 203       5.638   9.917  -1.332  1.00109.02           C  
ANISOU 1606  CD1 LEU A 203    13410  14047  13964    -93   -118    186       C  
ATOM   1607  CD2 LEU A 203       7.061  11.302  -2.834  1.00 98.30           C  
ANISOU 1607  CD2 LEU A 203    12045  12697  12607    -94   -104    195       C  
ATOM   1608  N   GLN A 204       8.648  12.972   2.250  1.00 75.78           N  
ANISOU 1608  N   GLN A 204     9236   9749   9810    -82    -49    115       N  
ATOM   1609  CA  GLN A 204       8.476  14.011   3.248  1.00 75.75           C  
ANISOU 1609  CA  GLN A 204     9237   9718   9827    -78    -25    113       C  
ATOM   1610  C   GLN A 204       9.771  14.616   3.795  1.00 75.00           C  
ANISOU 1610  C   GLN A 204     9151   9608   9735    -84    -17     86       C  
ATOM   1611  O   GLN A 204       9.760  15.749   4.259  1.00 72.60           O  
ANISOU 1611  O   GLN A 204     8850   9283   9452    -83      6     87       O  
ATOM   1612  CB  GLN A 204       7.618  13.468   4.382  1.00 83.23           C  
ANISOU 1612  CB  GLN A 204    10192  10657  10774    -73    -25    107       C  
ATOM   1613  CG  GLN A 204       6.193  13.178   3.940  1.00 87.47           C  
ANISOU 1613  CG  GLN A 204    10717  11203  11316    -66    -28    139       C  
ATOM   1614  CD  GLN A 204       5.443  12.266   4.880  1.00 92.93           C  
ANISOU 1614  CD  GLN A 204    11414  11892  12001    -63    -35    133       C  
ATOM   1615  NE2 GLN A 204       4.118  12.384   4.898  1.00 95.89           N  
ANISOU 1615  NE2 GLN A 204    11780  12266  12388    -55    -29    161       N  
ATOM   1616  OE1 GLN A 204       6.046  11.445   5.573  1.00115.58           O  
ANISOU 1616  OE1 GLN A 204    14296  14763  14855    -67    -47    105       O  
ATOM   1617  N   LYS A 205      10.880  13.885   3.756  1.00 79.92           N  
ANISOU 1617  N   LYS A 205     9781  10245  10342    -91    -33     62       N  
ATOM   1618  CA  LYS A 205      12.185  14.479   4.114  1.00 87.28           C  
ANISOU 1618  CA  LYS A 205    10717  11166  11277    -99    -27     40       C  
ATOM   1619  C   LYS A 205      12.947  14.919   2.863  1.00 85.58           C  
ANISOU 1619  C   LYS A 205    10492  10961  11064   -102    -26     51       C  
ATOM   1620  O   LYS A 205      13.523  16.011   2.832  1.00 89.20           O  
ANISOU 1620  O   LYS A 205    10948  11405  11538   -106    -10     50       O  
ATOM   1621  CB  LYS A 205      13.078  13.529   4.940  1.00 90.54           C  
ANISOU 1621  CB  LYS A 205    11142  11587  11673   -105    -43      9       C  
ATOM   1622  CG  LYS A 205      12.395  12.731   6.043  1.00 95.76           C  
ANISOU 1622  CG  LYS A 205    11812  12245  12326   -101    -49     -1       C  
ATOM   1623  CD  LYS A 205      11.613  13.598   7.015  1.00107.91           C  
ANISOU 1623  CD  LYS A 205    13359  13761  13882    -97    -28      2       C  
ATOM   1624  CE  LYS A 205      12.429  13.956   8.251  1.00115.30           C  
ANISOU 1624  CE  LYS A 205    14309  14684  14818   -104    -23    -28       C  
ATOM   1625  NZ  LYS A 205      11.716  14.971   9.088  1.00123.03           N1+
ANISOU 1625  NZ  LYS A 205    15296  15636  15813   -101      1    -26       N1+
ATOM   1626  N   PHE A 206      12.935  14.084   1.829  1.00 74.29           N  
ANISOU 1626  N   PHE A 206     9055   9554   9617   -101    -43     60       N  
ATOM   1627  CA  PHE A 206      13.801  14.304   0.689  1.00 69.78           C  
ANISOU 1627  CA  PHE A 206     8475   8995   9042   -104    -44     66       C  
ATOM   1628  C   PHE A 206      13.147  14.911  -0.528  1.00 82.20           C  
ANISOU 1628  C   PHE A 206    10035  10575  10622   -100    -37    100       C  
ATOM   1629  O   PHE A 206      13.832  15.531  -1.330  1.00 83.63           O  
ANISOU 1629  O   PHE A 206    10209  10760  10808   -101    -30    108       O  
ATOM   1630  CB  PHE A 206      14.452  13.012   0.324  1.00 64.96           C  
ANISOU 1630  CB  PHE A 206     7868   8406   8407   -107    -65     52       C  
ATOM   1631  CG  PHE A 206      15.225  12.429   1.448  1.00 68.07           C  
ANISOU 1631  CG  PHE A 206     8273   8795   8794   -111    -72     22       C  
ATOM   1632  CD1 PHE A 206      16.549  12.731   1.608  1.00 65.78           C  
ANISOU 1632  CD1 PHE A 206     7983   8503   8507   -117    -70      6       C  
ATOM   1633  CD2 PHE A 206      14.623  11.585   2.359  1.00 70.70           C  
ANISOU 1633  CD2 PHE A 206     8615   9128   9120   -109    -81     12       C  
ATOM   1634  CE1 PHE A 206      17.265  12.188   2.647  1.00 67.42           C  
ANISOU 1634  CE1 PHE A 206     8199   8710   8708   -121    -78    -19       C  
ATOM   1635  CE2 PHE A 206      15.331  11.039   3.410  1.00 65.82           C  
ANISOU 1635  CE2 PHE A 206     8005   8507   8494   -112    -88    -14       C  
ATOM   1636  CZ  PHE A 206      16.652  11.346   3.558  1.00 68.39           C  
ANISOU 1636  CZ  PHE A 206     8332   8833   8822   -118    -87    -29       C  
ATOM   1637  N   GLY A 207      11.838  14.713  -0.683  1.00 95.79           N  
ANISOU 1637  N   GLY A 207    11751  12301  12343    -94    -39    120       N  
ATOM   1638  CA  GLY A 207      11.081  15.314  -1.782  1.00 89.03           C  
ANISOU 1638  CA  GLY A 207    10880  11453  11493    -89    -32    156       C  
ATOM   1639  C   GLY A 207      10.779  14.345  -2.915  1.00 78.97           C  
ANISOU 1639  C   GLY A 207     9601  10208  10194    -91    -53    168       C  
ATOM   1640  O   GLY A 207      11.204  13.182  -2.900  1.00 65.15           O  
ANISOU 1640  O   GLY A 207     7860   8472   8423    -96    -71    147       O  
ATOM   1641  N   GLU A 208      10.056  14.860  -3.914  1.00 82.36           N  
ANISOU 1641  N   GLU A 208    10016  10649  10628    -87    -49    202       N  
ATOM   1642  CA  GLU A 208       9.519  14.048  -5.007  1.00 77.59           C  
ANISOU 1642  CA  GLU A 208     9406  10075  10001    -90    -68    217       C  
ATOM   1643  C   GLU A 208      10.479  13.845  -6.183  1.00 74.00           C  
ANISOU 1643  C   GLU A 208     8951   9640   9527    -94    -75    215       C  
ATOM   1644  O   GLU A 208      10.372  12.881  -6.916  1.00 68.31           O  
ANISOU 1644  O   GLU A 208     8233   8942   8781    -99    -94    214       O  
ATOM   1645  CB  GLU A 208       8.170  14.599  -5.483  1.00 81.20           C  
ANISOU 1645  CB  GLU A 208     9847  10538  10468    -85    -63    257       C  
ATOM   1646  CG  GLU A 208       8.248  15.728  -6.487  1.00 97.46           C  
ANISOU 1646  CG  GLU A 208    11891  12602  12538    -80    -48    288       C  
ATOM   1647  CD  GLU A 208       6.994  15.852  -7.349  1.00117.40           C  
ANISOU 1647  CD  GLU A 208    14398  15148  15061    -77    -54    329       C  
ATOM   1648  OE1 GLU A 208       5.886  15.498  -6.859  1.00119.31           O  
ANISOU 1648  OE1 GLU A 208    14637  15390  15306    -76    -59    338       O  
ATOM   1649  OE2 GLU A 208       7.122  16.336  -8.509  1.00132.77           O1-
ANISOU 1649  OE2 GLU A 208    16332  17111  17002    -76    -51    353       O1-
ATOM   1650  N   ARG A 209      11.417  14.760  -6.366  1.00 87.34           N  
ANISOU 1650  N   ARG A 209    10637  11319  11229    -92    -59    215       N  
ATOM   1651  CA  ARG A 209      12.480  14.590  -7.361  1.00 83.60           C  
ANISOU 1651  CA  ARG A 209    10163  10860  10739    -94    -63    210       C  
ATOM   1652  C   ARG A 209      13.322  13.399  -6.934  1.00 78.16           C  
ANISOU 1652  C   ARG A 209     9490  10175  10032   -100    -78    175       C  
ATOM   1653  O   ARG A 209      13.673  12.562  -7.755  1.00 78.47           O  
ANISOU 1653  O   ARG A 209     9533  10234  10046   -103    -91    170       O  
ATOM   1654  CB  ARG A 209      13.324  15.858  -7.436  1.00 89.01           C  
ANISOU 1654  CB  ARG A 209    10842  11530  11447    -91    -41    216       C  
ATOM   1655  CG  ARG A 209      14.078  16.068  -8.740  1.00 95.24           C  
ANISOU 1655  CG  ARG A 209    11625  12336  12225    -91    -39    228       C  
ATOM   1656  CD  ARG A 209      14.571  17.517  -8.818  1.00 98.42           C  
ANISOU 1656  CD  ARG A 209    12018  12722  12657    -87    -14    243       C  
ATOM   1657  NE  ARG A 209      15.640  17.724  -9.787  1.00103.40           N  
ANISOU 1657  NE  ARG A 209    12644  13363  13281    -86     -9    247       N  
ATOM   1658  CZ  ARG A 209      16.904  17.325  -9.620  1.00109.63           C  
ANISOU 1658  CZ  ARG A 209    13441  14150  14064    -91    -12    221       C  
ATOM   1659  NH1 ARG A 209      17.286  16.672  -8.523  1.00100.92           N1+
ANISOU 1659  NH1 ARG A 209    12349  13036  12959    -96    -21    188       N1+
ATOM   1660  NH2 ARG A 209      17.800  17.565 -10.576  1.00113.26           N  
ANISOU 1660  NH2 ARG A 209    13894  14620  14518    -89     -6    228       N  
ATOM   1661  N   ALA A 210      13.599  13.320  -5.635  1.00 76.71           N  
ANISOU 1661  N   ALA A 210     9315   9971   9859   -101    -75    151       N  
ATOM   1662  CA  ALA A 210      14.209  12.141  -5.032  1.00 83.06           C  
ANISOU 1662  CA  ALA A 210    10134  10778  10648   -105    -89    120       C  
ATOM   1663  C   ALA A 210      13.388  10.847  -5.211  1.00 81.36           C  
ANISOU 1663  C   ALA A 210     9924  10579  10411   -107   -108    118       C  
ATOM   1664  O   ALA A 210      13.922   9.805  -5.622  1.00 85.38           O  
ANISOU 1664  O   ALA A 210    10442  11101  10899   -111   -120    103       O  
ATOM   1665  CB  ALA A 210      14.448  12.388  -3.558  1.00 89.97           C  
ANISOU 1665  CB  ALA A 210    11015  11629  11539   -105    -82    100       C  
ATOM   1666  N   PHE A 211      12.101  10.897  -4.893  1.00 76.94           N  
ANISOU 1666  N   PHE A 211     9360  10016   9857   -106   -110    133       N  
ATOM   1667  CA  PHE A 211      11.227   9.757  -5.183  1.00 74.37           C  
ANISOU 1667  CA  PHE A 211     9038   9707   9513   -110   -129    134       C  
ATOM   1668  C   PHE A 211      11.179   9.478  -6.691  1.00 69.65           C  
ANISOU 1668  C   PHE A 211     8436   9135   8893   -114   -138    149       C  
ATOM   1669  O   PHE A 211      11.256   8.334  -7.097  1.00 73.70           O  
ANISOU 1669  O   PHE A 211     8958   9661   9382   -120   -153    136       O  
ATOM   1670  CB  PHE A 211       9.800   9.933  -4.605  1.00 74.05           C  
ANISOU 1670  CB  PHE A 211     8992   9660   9486   -108   -128    152       C  
ATOM   1671  CG  PHE A 211       8.928   8.702  -4.734  1.00 76.63           C  
ANISOU 1671  CG  PHE A 211     9321  10001   9795   -114   -148    151       C  
ATOM   1672  CD1 PHE A 211       9.095   7.622  -3.875  1.00 86.05           C  
ANISOU 1672  CD1 PHE A 211    10527  11187  10980   -116   -157    125       C  
ATOM   1673  CD2 PHE A 211       7.946   8.618  -5.712  1.00 80.69           C  
ANISOU 1673  CD2 PHE A 211     9825  10535  10300   -118   -158    177       C  
ATOM   1674  CE1 PHE A 211       8.322   6.473  -4.000  1.00 87.37           C  
ANISOU 1674  CE1 PHE A 211    10698  11366  11133   -122   -174    123       C  
ATOM   1675  CE2 PHE A 211       7.160   7.481  -5.835  1.00 82.11           C  
ANISOU 1675  CE2 PHE A 211    10008  10727  10464   -126   -177    175       C  
ATOM   1676  CZ  PHE A 211       7.354   6.407  -4.980  1.00 87.40           C  
ANISOU 1676  CZ  PHE A 211    10692  11388  11127   -128   -185    148       C  
ATOM   1677  N   LYS A 212      11.082  10.494  -7.538  1.00 65.83           N  
ANISOU 1677  N   LYS A 212     7940   8657   8416   -112   -128    175       N  
ATOM   1678  CA  LYS A 212      10.882  10.208  -8.955  1.00 67.07           C  
ANISOU 1678  CA  LYS A 212     8093   8842   8550   -116   -139    192       C  
ATOM   1679  C   LYS A 212      11.999   9.323  -9.518  1.00 63.85           C  
ANISOU 1679  C   LYS A 212     7698   8444   8117   -120   -146    168       C  
ATOM   1680  O   LYS A 212      11.723   8.378 -10.281  1.00 65.13           O  
ANISOU 1680  O   LYS A 212     7867   8627   8253   -127   -161    165       O  
ATOM   1681  CB  LYS A 212      10.621  11.481  -9.781  1.00 71.31           C  
ANISOU 1681  CB  LYS A 212     8612   9384   9097   -111   -126    227       C  
ATOM   1682  CG  LYS A 212       9.126  11.841  -9.845  1.00 75.45           C  
ANISOU 1682  CG  LYS A 212     9122   9915   9631   -110   -128    259       C  
ATOM   1683  CD  LYS A 212       8.795  12.995 -10.800  1.00 81.77           C  
ANISOU 1683  CD  LYS A 212     9904  10727  10440   -105   -117    298       C  
ATOM   1684  CE  LYS A 212       7.288  13.156 -11.017  1.00 83.82           C  
ANISOU 1684  CE  LYS A 212    10147  10997  10702   -105   -123    332       C  
ATOM   1685  NZ  LYS A 212       6.943  13.735 -12.346  1.00 81.99           N1+
ANISOU 1685  NZ  LYS A 212     9898  10791  10461   -104   -124    369       N1+
ATOM   1686  N   ALA A 213      13.235   9.581  -9.101  1.00 61.32           N  
ANISOU 1686  N   ALA A 213     7383   8111   7806   -116   -135    150       N  
ATOM   1687  CA  ALA A 213      14.345   8.748  -9.534  1.00 63.09           C  
ANISOU 1687  CA  ALA A 213     7619   8343   8010   -118   -139    128       C  
ATOM   1688  C   ALA A 213      14.101   7.368  -9.012  1.00 65.90           C  
ANISOU 1688  C   ALA A 213     7989   8699   8352   -123   -153    105       C  
ATOM   1689  O   ALA A 213      14.182   6.412  -9.760  1.00 62.56           O  
ANISOU 1689  O   ALA A 213     7576   8291   7903   -128   -163     97       O  
ATOM   1690  CB  ALA A 213      15.661   9.261  -9.005  1.00 62.44           C  
ANISOU 1690  CB  ALA A 213     7536   8244   7943   -113   -124    114       C  
ATOM   1691  N   TRP A 214      13.781   7.268  -7.725  1.00 72.20           N  
ANISOU 1691  N   TRP A 214     8788   9479   9165   -121   -154     94       N  
ATOM   1692  CA  TRP A 214      13.480   5.976  -7.119  1.00 83.37           C  
ANISOU 1692  CA  TRP A 214    10215  10892  10569   -125   -166     74       C  
ATOM   1693  C   TRP A 214      12.595   5.248  -8.088  1.00 80.14           C  
ANISOU 1693  C   TRP A 214     9808  10503  10138   -133   -181     84       C  
ATOM   1694  O   TRP A 214      12.983   4.213  -8.638  1.00 81.72           O  
ANISOU 1694  O   TRP A 214    10021  10713  10316   -138   -189     68       O  
ATOM   1695  CB  TRP A 214      12.765   6.138  -5.768  1.00 95.75           C  
ANISOU 1695  CB  TRP A 214    11782  12443  12158   -123   -165     73       C  
ATOM   1696  CG  TRP A 214      12.583   4.866  -4.999  1.00 99.84           C  
ANISOU 1696  CG  TRP A 214    12311  12956  12668   -125   -176     52       C  
ATOM   1697  CD1 TRP A 214      11.545   4.004  -5.090  1.00106.04           C  
ANISOU 1697  CD1 TRP A 214    13099  13748  13443   -131   -189     55       C  
ATOM   1698  CD2 TRP A 214      13.461   4.338  -4.011  1.00115.12           C  
ANISOU 1698  CD2 TRP A 214    14256  14880  14606   -121   -174     27       C  
ATOM   1699  CE2 TRP A 214      12.899   3.129  -3.561  1.00121.52           C  
ANISOU 1699  CE2 TRP A 214    15074  15689  15407   -124   -185     16       C  
ATOM   1700  CE3 TRP A 214      14.697   4.758  -3.477  1.00143.19           C  
ANISOU 1700  CE3 TRP A 214    17811  18425  18170   -117   -164     14       C  
ATOM   1701  NE1 TRP A 214      11.729   2.953  -4.238  1.00109.17           N  
ANISOU 1701  NE1 TRP A 214    13506  14136  13836   -130   -194     33       N  
ATOM   1702  CZ2 TRP A 214      13.517   2.322  -2.594  1.00154.66           C  
ANISOU 1702  CZ2 TRP A 214    19281  19878  19605   -120   -185     -6       C  
ATOM   1703  CZ3 TRP A 214      15.315   3.960  -2.499  1.00161.47           C  
ANISOU 1703  CZ3 TRP A 214    20134  20733  20484   -114   -166     -8       C  
ATOM   1704  CH2 TRP A 214      14.722   2.752  -2.076  1.00173.46           C  
ANISOU 1704  CH2 TRP A 214    21662  22252  21994   -115   -176    -17       C  
ATOM   1705  N   ALA A 215      11.447   5.866  -8.353  1.00 76.92           N  
ANISOU 1705  N   ALA A 215     9389  10102   9737   -135   -184    110       N  
ATOM   1706  CA  ALA A 215      10.408   5.316  -9.216  1.00 82.10           C  
ANISOU 1706  CA  ALA A 215    10043  10778  10373   -145   -200    124       C  
ATOM   1707  C   ALA A 215      10.975   4.908 -10.546  1.00 81.89           C  
ANISOU 1707  C   ALA A 215    10024  10772  10318   -150   -204    121       C  
ATOM   1708  O   ALA A 215      10.877   3.730 -10.944  1.00 83.33           O  
ANISOU 1708  O   ALA A 215    10219  10964  10477   -160   -217    105       O  
ATOM   1709  CB  ALA A 215       9.303   6.342  -9.426  1.00 80.64           C  
ANISOU 1709  CB  ALA A 215     9840  10599  10203   -144   -198    159       C  
ATOM   1710  N   VAL A 216      11.595   5.874 -11.218  1.00 74.43           N  
ANISOU 1710  N   VAL A 216     9071   9833   9376   -145   -192    135       N  
ATOM   1711  CA  VAL A 216      12.138   5.616 -12.543  1.00 76.73           C  
ANISOU 1711  CA  VAL A 216     9369  10145   9640   -149   -194    135       C  
ATOM   1712  C   VAL A 216      12.993   4.349 -12.561  1.00 76.61           C  
ANISOU 1712  C   VAL A 216     9375  10128   9606   -151   -198    102       C  
ATOM   1713  O   VAL A 216      12.727   3.422 -13.326  1.00 69.60           O  
ANISOU 1713  O   VAL A 216     8499   9256   8691   -161   -209     95       O  
ATOM   1714  CB  VAL A 216      12.965   6.804 -13.046  1.00 77.96           C  
ANISOU 1714  CB  VAL A 216     9515  10301   9806   -139   -177    150       C  
ATOM   1715  CG1 VAL A 216      13.667   6.472 -14.370  1.00 77.42           C  
ANISOU 1715  CG1 VAL A 216     9455  10253   9709   -142   -177    148       C  
ATOM   1716  CG2 VAL A 216      12.072   8.021 -13.203  1.00 83.39           C  
ANISOU 1716  CG2 VAL A 216    10182  10992  10511   -136   -172    186       C  
ATOM   1717  N   ALA A 217      14.008   4.332 -11.697  1.00 83.98           N  
ANISOU 1717  N   ALA A 217    10312  11042  10555   -143   -186     83       N  
ATOM   1718  CA  ALA A 217      14.980   3.241 -11.611  1.00 83.84           C  
ANISOU 1718  CA  ALA A 217    10311  11019  10523   -142   -185     55       C  
ATOM   1719  C   ALA A 217      14.241   1.939 -11.493  1.00 83.12           C  
ANISOU 1719  C   ALA A 217    10234  10930  10417   -152   -200     40       C  
ATOM   1720  O   ALA A 217      14.389   1.086 -12.359  1.00 88.92           O  
ANISOU 1720  O   ALA A 217    10982  11677  11125   -159   -205     30       O  
ATOM   1721  CB  ALA A 217      15.914   3.441 -10.415  1.00 81.77           C  
ANISOU 1721  CB  ALA A 217    10048  10735  10285   -133   -174     40       C  
ATOM   1722  N   ARG A 218      13.408   1.821 -10.455  1.00 85.09           N  
ANISOU 1722  N   ARG A 218    10480  11169  10683   -153   -207     40       N  
ATOM   1723  CA  ARG A 218      12.748   0.547 -10.096  1.00 83.20           C  
ANISOU 1723  CA  ARG A 218    10252  10927  10434   -162   -220     25       C  
ATOM   1724  C   ARG A 218      11.624   0.132 -11.067  1.00 73.23           C  
ANISOU 1724  C   ARG A 218     8990   9684   9149   -177   -236     36       C  
ATOM   1725  O   ARG A 218      11.397  -1.065 -11.258  1.00 62.80           O  
ANISOU 1725  O   ARG A 218     7685   8366   7812   -187   -245     19       O  
ATOM   1726  CB  ARG A 218      12.247   0.581  -8.635  1.00 87.00           C  
ANISOU 1726  CB  ARG A 218    10728  11390  10940   -157   -220     23       C  
ATOM   1727  CG  ARG A 218      11.636  -0.716  -8.103  1.00 84.37           C  
ANISOU 1727  CG  ARG A 218    10405  11050  10601   -164   -231      7       C  
ATOM   1728  CD  ARG A 218      12.700  -1.761  -7.811  1.00 88.07           C  
ANISOU 1728  CD  ARG A 218    10890  11510  11063   -160   -225    -20       C  
ATOM   1729  NE  ARG A 218      12.284  -2.702  -6.766  1.00 95.26           N  
ANISOU 1729  NE  ARG A 218    11807  12407  11982   -160   -230    -33       N  
ATOM   1730  CZ  ARG A 218      11.685  -3.871  -6.976  1.00 91.60           C  
ANISOU 1730  CZ  ARG A 218    11354  11944  11505   -171   -240    -43       C  
ATOM   1731  NH1 ARG A 218      11.416  -4.289  -8.226  1.00 84.61           N1+
ANISOU 1731  NH1 ARG A 218    10478  11075  10596   -183   -248    -44       N1+
ATOM   1732  NH2 ARG A 218      11.355  -4.622  -5.920  1.00 87.97           N  
ANISOU 1732  NH2 ARG A 218    10898  11470  11056   -169   -242    -53       N  
ATOM   1733  N   LEU A 219      10.941   1.084 -11.699  1.00 73.84           N  
ANISOU 1733  N   LEU A 219     9052   9776   9227   -179   -239     64       N  
ATOM   1734  CA  LEU A 219      10.008   0.696 -12.778  1.00 78.26           C  
ANISOU 1734  CA  LEU A 219     9613  10360   9761   -195   -256     75       C  
ATOM   1735  C   LEU A 219      10.755   0.172 -14.015  1.00 88.29           C  
ANISOU 1735  C   LEU A 219    10900  11646  11000   -201   -255     62       C  
ATOM   1736  O   LEU A 219      10.362  -0.831 -14.601  1.00 98.90           O  
ANISOU 1736  O   LEU A 219    12258  13001  12319   -215   -268     51       O  
ATOM   1737  CB  LEU A 219       9.043   1.811 -13.188  1.00 67.91           C  
ANISOU 1737  CB  LEU A 219     8281   9065   8459   -196   -260    111       C  
ATOM   1738  CG  LEU A 219       7.920   2.103 -12.196  1.00 68.33           C  
ANISOU 1738  CG  LEU A 219     8318   9106   8536   -195   -265    127       C  
ATOM   1739  CD1 LEU A 219       7.140   3.349 -12.592  1.00 68.23           C  
ANISOU 1739  CD1 LEU A 219     8282   9107   8535   -193   -264    166       C  
ATOM   1740  CD2 LEU A 219       6.965   0.944 -12.043  1.00 65.73           C  
ANISOU 1740  CD2 LEU A 219     7996   8782   8197   -210   -284    118       C  
ATOM   1741  N   SER A 220      11.833   0.837 -14.407  1.00 96.00           N  
ANISOU 1741  N   SER A 220    11876  12624  11978   -190   -240     65       N  
ATOM   1742  CA  SER A 220      12.551   0.450 -15.620  1.00 98.26           C  
ANISOU 1742  CA  SER A 220    12176  12924  12233   -193   -237     56       C  
ATOM   1743  C   SER A 220      13.078  -0.969 -15.471  1.00 92.06           C  
ANISOU 1743  C   SER A 220    11415  12129  11433   -197   -236     22       C  
ATOM   1744  O   SER A 220      13.106  -1.719 -16.435  1.00 95.73           O  
ANISOU 1744  O   SER A 220    11897  12607  11867   -208   -241     11       O  
ATOM   1745  CB  SER A 220      13.684   1.441 -15.922  1.00110.43           C  
ANISOU 1745  CB  SER A 220    13711  14465  13783   -178   -218     65       C  
ATOM   1746  OG  SER A 220      13.202   2.791 -15.939  1.00110.07           O  
ANISOU 1746  OG  SER A 220    13643  14425  13756   -173   -215     97       O  
ATOM   1747  N   GLN A 221      13.464  -1.330 -14.247  1.00 87.75           N  
ANISOU 1747  N   GLN A 221    10872  11560  10910   -189   -230      6       N  
ATOM   1748  CA  GLN A 221      13.918  -2.686 -13.926  1.00 83.96           C  
ANISOU 1748  CA  GLN A 221    10413  11066  10422   -190   -228    -24       C  
ATOM   1749  C   GLN A 221      12.737  -3.659 -14.099  1.00 89.21           C  
ANISOU 1749  C   GLN A 221    11088  11738  11072   -209   -246    -31       C  
ATOM   1750  O   GLN A 221      12.903  -4.793 -14.550  1.00 95.67           O  
ANISOU 1750  O   GLN A 221    11927  12555  11869   -217   -247    -53       O  
ATOM   1751  CB  GLN A 221      14.455  -2.776 -12.482  1.00 78.72           C  
ANISOU 1751  CB  GLN A 221     9745  10377   9786   -177   -219    -35       C  
ATOM   1752  CG  GLN A 221      15.899  -2.329 -12.209  1.00 73.31           C  
ANISOU 1752  CG  GLN A 221     9057   9683   9114   -161   -200    -40       C  
ATOM   1753  CD  GLN A 221      16.265  -2.379 -10.705  1.00 67.97           C  
ANISOU 1753  CD  GLN A 221     8375   8985   8465   -151   -195    -48       C  
ATOM   1754  NE2 GLN A 221      17.378  -3.014 -10.362  1.00 64.36           N  
ANISOU 1754  NE2 GLN A 221     7927   8518   8009   -142   -184    -65       N  
ATOM   1755  OE1 GLN A 221      15.551  -1.846  -9.876  1.00 70.68           O  
ANISOU 1755  OE1 GLN A 221     8706   9322   8827   -151   -201    -38       O  
ATOM   1756  N   ARG A 222      11.547  -3.195 -13.737  1.00 89.72           N  
ANISOU 1756  N   ARG A 222    11136  11807  11148   -215   -260    -12       N  
ATOM   1757  CA  ARG A 222      10.332  -4.003 -13.805  1.00 90.80           C  
ANISOU 1757  CA  ARG A 222    11277  11949  11275   -234   -279    -14       C  
ATOM   1758  C   ARG A 222       9.907  -4.267 -15.256  1.00 82.43           C  
ANISOU 1758  C   ARG A 222    10225  10915  10179   -252   -291    -11       C  
ATOM   1759  O   ARG A 222       9.736  -5.404 -15.664  1.00 81.20           O  
ANISOU 1759  O   ARG A 222    10089  10761  10002   -267   -298    -31       O  
ATOM   1760  CB  ARG A 222       9.208  -3.272 -13.055  1.00 97.23           C  
ANISOU 1760  CB  ARG A 222    12067  12762  12113   -233   -288     11       C  
ATOM   1761  CG  ARG A 222       8.223  -4.146 -12.325  1.00 99.48           C  
ANISOU 1761  CG  ARG A 222    12354  13038  12406   -243   -301      4       C  
ATOM   1762  CD  ARG A 222       8.921  -4.792 -11.164  1.00109.92           C  
ANISOU 1762  CD  ARG A 222    13686  14333  13745   -232   -289    -19       C  
ATOM   1763  NE  ARG A 222       7.994  -5.011 -10.069  1.00111.99           N  
ANISOU 1763  NE  ARG A 222    13940  14584  14029   -232   -296    -14       N  
ATOM   1764  CZ  ARG A 222       7.663  -4.100  -9.165  1.00109.47           C  
ANISOU 1764  CZ  ARG A 222    13602  14256  13735   -221   -291      4       C  
ATOM   1765  NH1 ARG A 222       6.835  -4.438  -8.205  1.00118.74           N1+
ANISOU 1765  NH1 ARG A 222    14771  15419  14927   -222   -296      7       N1+
ATOM   1766  NH2 ARG A 222       8.157  -2.871  -9.198  1.00105.57           N  
ANISOU 1766  NH2 ARG A 222    13096  13764  13251   -209   -280     19       N  
ATOM   1767  N   PHE A 223       9.766  -3.201 -16.035  1.00 77.57           N  
ANISOU 1767  N   PHE A 223     9595  10320   9556   -251   -293     15       N  
ATOM   1768  CA  PHE A 223       9.295  -3.288 -17.416  1.00 73.99           C  
ANISOU 1768  CA  PHE A 223     9147   9897   9068   -268   -306     23       C  
ATOM   1769  C   PHE A 223      10.387  -2.800 -18.347  1.00 78.30           C  
ANISOU 1769  C   PHE A 223     9699  10453   9597   -259   -291     24       C  
ATOM   1770  O   PHE A 223      10.281  -1.720 -18.952  1.00 73.28           O  
ANISOU 1770  O   PHE A 223     9047   9836   8960   -255   -290     52       O  
ATOM   1771  CB  PHE A 223       8.069  -2.415 -17.611  1.00 69.33           C  
ANISOU 1771  CB  PHE A 223     8531   9327   8484   -275   -322     59       C  
ATOM   1772  CG  PHE A 223       7.134  -2.435 -16.454  1.00 70.98           C  
ANISOU 1772  CG  PHE A 223     8726   9521   8722   -275   -329     67       C  
ATOM   1773  CD1 PHE A 223       6.494  -3.595 -16.086  1.00 76.09           C  
ANISOU 1773  CD1 PHE A 223     9383  10161   9365   -290   -342     49       C  
ATOM   1774  CD2 PHE A 223       6.892  -1.288 -15.724  1.00 68.50           C  
ANISOU 1774  CD2 PHE A 223     8387   9199   8439   -260   -322     93       C  
ATOM   1775  CE1 PHE A 223       5.622  -3.611 -15.003  1.00 78.49           C  
ANISOU 1775  CE1 PHE A 223     9673  10452   9696   -290   -348     58       C  
ATOM   1776  CE2 PHE A 223       6.027  -1.302 -14.642  1.00 65.79           C  
ANISOU 1776  CE2 PHE A 223     8032   8842   8123   -259   -327    101       C  
ATOM   1777  CZ  PHE A 223       5.397  -2.457 -14.275  1.00 66.18           C  
ANISOU 1777  CZ  PHE A 223     8091   8886   8168   -273   -340     84       C  
ATOM   1778  N   PRO A 224      11.447  -3.605 -18.488  1.00 80.18           N  
ANISOU 1778  N   PRO A 224     9961  10680   9824   -254   -277     -5       N  
ATOM   1779  CA  PRO A 224      12.576  -3.171 -19.286  1.00 81.20           C  
ANISOU 1779  CA  PRO A 224    10096  10815   9940   -243   -260     -5       C  
ATOM   1780  C   PRO A 224      12.260  -3.132 -20.769  1.00 86.02           C  
ANISOU 1780  C   PRO A 224    10714  11458  10511   -257   -269      4       C  
ATOM   1781  O   PRO A 224      13.043  -2.591 -21.548  1.00 97.91           O  
ANISOU 1781  O   PRO A 224    12222  12975  12006   -248   -256     11       O  
ATOM   1782  CB  PRO A 224      13.643  -4.212 -18.976  1.00 82.98           C  
ANISOU 1782  CB  PRO A 224    10345  11019  10164   -236   -244    -38       C  
ATOM   1783  CG  PRO A 224      12.886  -5.434 -18.584  1.00 83.33           C  
ANISOU 1783  CG  PRO A 224    10404  11055  10203   -252   -257    -59       C  
ATOM   1784  CD  PRO A 224      11.605  -4.978 -17.980  1.00 76.90           C  
ANISOU 1784  CD  PRO A 224     9568  10245   9407   -260   -276    -38       C  
ATOM   1785  N   LYS A 225      11.120  -3.688 -21.163  1.00 90.37           N  
ANISOU 1785  N   LYS A 225    11269  12025  11042   -280   -292      4       N  
ATOM   1786  CA  LYS A 225      10.718  -3.647 -22.571  1.00 97.09           C  
ANISOU 1786  CA  LYS A 225    12127  12910  11853   -297   -304     13       C  
ATOM   1787  C   LYS A 225      10.254  -2.260 -22.980  1.00 83.31           C  
ANISOU 1787  C   LYS A 225    10353  11189  10114   -292   -309     55       C  
ATOM   1788  O   LYS A 225      10.462  -1.855 -24.119  1.00 81.50           O  
ANISOU 1788  O   LYS A 225    10126  10985   9857   -293   -308     67       O  
ATOM   1789  CB  LYS A 225       9.638  -4.715 -22.893  1.00108.92           C  
ANISOU 1789  CB  LYS A 225    13639  14419  13326   -326   -328     -1       C  
ATOM   1790  CG  LYS A 225      10.231  -6.020 -23.437  1.00118.26           C  
ANISOU 1790  CG  LYS A 225    14859  15596  14479   -336   -321    -40       C  
ATOM   1791  CD  LYS A 225       9.384  -7.259 -23.192  1.00116.33           C  
ANISOU 1791  CD  LYS A 225    14630  15345  14227   -361   -338    -64       C  
ATOM   1792  CE  LYS A 225      10.162  -8.521 -23.553  1.00115.27           C  
ANISOU 1792  CE  LYS A 225    14534  15194  14069   -366   -324   -104       C  
ATOM   1793  NZ  LYS A 225       9.315  -9.746 -23.545  1.00116.60           N1+
ANISOU 1793  NZ  LYS A 225    14720  15358  14223   -393   -341   -128       N1+
ATOM   1794  N   ALA A 226       9.684  -1.526 -22.032  1.00 71.19           N  
ANISOU 1794  N   ALA A 226     8791   9643   8614   -283   -312     77       N  
ATOM   1795  CA  ALA A 226       8.914  -0.345 -22.350  1.00 71.88           C  
ANISOU 1795  CA  ALA A 226     8850   9752   8708   -282   -320    118       C  
ATOM   1796  C   ALA A 226       9.775   0.875 -22.596  1.00 72.32           C  
ANISOU 1796  C   ALA A 226     8893   9809   8777   -261   -299    139       C  
ATOM   1797  O   ALA A 226      10.911   0.955 -22.140  1.00 68.06           O  
ANISOU 1797  O   ALA A 226     8360   9246   8253   -244   -278    123       O  
ATOM   1798  CB  ALA A 226       7.879  -0.074 -21.264  1.00 71.01           C  
ANISOU 1798  CB  ALA A 226     8718   9630   8632   -283   -330    134       C  
ATOM   1799  N   GLU A 227       9.191   1.827 -23.324  1.00 77.52           N  
ANISOU 1799  N   GLU A 227     9531  10494   9429   -262   -305    176       N  
ATOM   1800  CA  GLU A 227       9.899   2.992 -23.829  1.00 79.59           C  
ANISOU 1800  CA  GLU A 227     9780  10763   9697   -244   -287    200       C  
ATOM   1801  C   GLU A 227       9.924   4.106 -22.827  1.00 77.51           C  
ANISOU 1801  C   GLU A 227     9493  10477   9481   -226   -273    221       C  
ATOM   1802  O   GLU A 227       9.109   4.131 -21.919  1.00 77.59           O  
ANISOU 1802  O   GLU A 227     9491  10475   9515   -228   -281    226       O  
ATOM   1803  CB  GLU A 227       9.222   3.500 -25.085  1.00 93.94           C  
ANISOU 1803  CB  GLU A 227    11587  12621  11487   -254   -299    233       C  
ATOM   1804  CG  GLU A 227       9.088   2.469 -26.195  1.00 95.81           C  
ANISOU 1804  CG  GLU A 227    11848  12885  11671   -275   -315    215       C  
ATOM   1805  CD  GLU A 227       9.628   3.004 -27.505  1.00107.74           C  
ANISOU 1805  CD  GLU A 227    13361  14424  13152   -271   -307    231       C  
ATOM   1806  OE1 GLU A 227       9.262   4.155 -27.875  1.00106.75           O  
ANISOU 1806  OE1 GLU A 227    13209  14317  13035   -263   -306    273       O  
ATOM   1807  OE2 GLU A 227      10.451   2.287 -28.135  1.00119.26           O1-
ANISOU 1807  OE2 GLU A 227    14848  15885  14580   -274   -300    203       O1-
ATOM   1808  N   PHE A 228      10.839   5.051 -23.007  1.00 83.28           N  
ANISOU 1808  N   PHE A 228    10216  11203  10225   -208   -251    233       N  
ATOM   1809  CA  PHE A 228      11.020   6.093 -22.006  1.00 95.49           C  
ANISOU 1809  CA  PHE A 228    11742  12724  11817   -191   -235    248       C  
ATOM   1810  C   PHE A 228       9.750   6.891 -21.791  1.00104.52           C  
ANISOU 1810  C   PHE A 228    12859  13875  12979   -192   -244    284       C  
ATOM   1811  O   PHE A 228       9.378   7.163 -20.648  1.00118.09           O  
ANISOU 1811  O   PHE A 228    14567  15569  14731   -187   -240    285       O  
ATOM   1812  CB  PHE A 228      12.128   7.054 -22.381  1.00102.35           C  
ANISOU 1812  CB  PHE A 228    12605  13588  12696   -174   -211    259       C  
ATOM   1813  CG  PHE A 228      12.390   8.115 -21.334  1.00114.15           C  
ANISOU 1813  CG  PHE A 228    14081  15054  14237   -159   -193    270       C  
ATOM   1814  CD1 PHE A 228      12.892   7.759 -20.080  1.00113.05           C  
ANISOU 1814  CD1 PHE A 228    13949  14882  14122   -154   -187    242       C  
ATOM   1815  CD2 PHE A 228      12.148   9.474 -21.600  1.00113.82           C  
ANISOU 1815  CD2 PHE A 228    14015  15016  14215   -149   -182    309       C  
ATOM   1816  CE1 PHE A 228      13.159   8.727 -19.122  1.00109.31           C  
ANISOU 1816  CE1 PHE A 228    13462  14383  13689   -142   -171    249       C  
ATOM   1817  CE2 PHE A 228      12.408  10.443 -20.638  1.00111.72           C  
ANISOU 1817  CE2 PHE A 228    13735  14722  13992   -136   -164    316       C  
ATOM   1818  CZ  PHE A 228      12.925  10.070 -19.403  1.00109.14           C  
ANISOU 1818  CZ  PHE A 228    13417  14364  13686   -133   -159    285       C  
ATOM   1819  N   ALA A 229       9.089   7.274 -22.880  1.00 96.59           N  
ANISOU 1819  N   ALA A 229    11842  12904  11952   -199   -254    316       N  
ATOM   1820  CA  ALA A 229       7.859   8.048 -22.771  1.00 91.42           C  
ANISOU 1820  CA  ALA A 229    11161  12260  11315   -199   -261    356       C  
ATOM   1821  C   ALA A 229       6.771   7.329 -21.916  1.00 91.89           C  
ANISOU 1821  C   ALA A 229    11220  12312  11383   -211   -280    347       C  
ATOM   1822  O   ALA A 229       6.031   7.960 -21.163  1.00 93.41           O  
ANISOU 1822  O   ALA A 229    11391  12492  11608   -205   -277    369       O  
ATOM   1823  CB  ALA A 229       7.354   8.383 -24.162  1.00 96.80           C  
ANISOU 1823  CB  ALA A 229    11832  12984  11965   -206   -272    389       C  
ATOM   1824  N   GLU A 230       6.710   6.006 -21.994  1.00 95.79           N  
ANISOU 1824  N   GLU A 230    11736  12810  11851   -228   -297    315       N  
ATOM   1825  CA  GLU A 230       5.708   5.231 -21.241  1.00 92.66           C  
ANISOU 1825  CA  GLU A 230    11339  12407  11460   -241   -315    305       C  
ATOM   1826  C   GLU A 230       5.996   5.292 -19.764  1.00 86.23           C  
ANISOU 1826  C   GLU A 230    10525  11552  10685   -228   -301    288       C  
ATOM   1827  O   GLU A 230       5.114   5.582 -18.966  1.00 88.93           O  
ANISOU 1827  O   GLU A 230    10851  11884  11053   -226   -303    305       O  
ATOM   1828  CB  GLU A 230       5.689   3.747 -21.699  1.00 95.06           C  
ANISOU 1828  CB  GLU A 230    11670  12722  11727   -263   -334    271       C  
ATOM   1829  CG  GLU A 230       4.665   2.828 -21.026  1.00 88.51           C  
ANISOU 1829  CG  GLU A 230    10842  11887  10901   -279   -354    260       C  
ATOM   1830  CD  GLU A 230       3.243   3.400 -20.988  1.00 92.08           C  
ANISOU 1830  CD  GLU A 230    11264  12357  11366   -285   -369    302       C  
ATOM   1831  OE1 GLU A 230       2.748   3.918 -22.016  1.00 94.45           O  
ANISOU 1831  OE1 GLU A 230    11550  12691  11647   -292   -379    334       O  
ATOM   1832  OE2 GLU A 230       2.604   3.322 -19.919  1.00 90.40           O1-
ANISOU 1832  OE2 GLU A 230    11041  12124  11181   -283   -370    304       O1-
ATOM   1833  N   VAL A 231       7.245   5.028 -19.415  1.00 82.07           N  
ANISOU 1833  N   VAL A 231    10017  11004  10162   -219   -285    257       N  
ATOM   1834  CA  VAL A 231       7.621   4.845 -18.030  1.00 83.65           C  
ANISOU 1834  CA  VAL A 231    10223  11169  10393   -209   -274    234       C  
ATOM   1835  C   VAL A 231       7.425   6.141 -17.266  1.00 76.88           C  
ANISOU 1835  C   VAL A 231     9343  10294   9575   -193   -258    260       C  
ATOM   1836  O   VAL A 231       6.872   6.123 -16.171  1.00 73.07           O  
ANISOU 1836  O   VAL A 231     8854   9792   9116   -191   -258    259       O  
ATOM   1837  CB  VAL A 231       9.072   4.323 -17.923  1.00 91.43           C  
ANISOU 1837  CB  VAL A 231    11230  12137  11371   -203   -261    199       C  
ATOM   1838  CG1 VAL A 231       9.488   4.078 -16.475  1.00 95.41           C  
ANISOU 1838  CG1 VAL A 231    11740  12608  11905   -194   -251    175       C  
ATOM   1839  CG2 VAL A 231       9.223   3.042 -18.725  1.00 96.44           C  
ANISOU 1839  CG2 VAL A 231    11888  12788  11966   -219   -274    174       C  
ATOM   1840  N   SER A 232       7.832   7.260 -17.864  1.00 75.98           N  
ANISOU 1840  N   SER A 232     9216  10187   9466   -183   -244    285       N  
ATOM   1841  CA  SER A 232       7.735   8.562 -17.201  1.00 81.25           C  
ANISOU 1841  CA  SER A 232     9864  10836  10173   -167   -225    309       C  
ATOM   1842  C   SER A 232       6.295   8.789 -16.794  1.00 82.82           C  
ANISOU 1842  C   SER A 232    10044  11038  10387   -170   -234    336       C  
ATOM   1843  O   SER A 232       6.005   9.236 -15.676  1.00 73.68           O  
ANISOU 1843  O   SER A 232     8878   9854   9261   -161   -223    338       O  
ATOM   1844  CB  SER A 232       8.196   9.694 -18.131  1.00 78.03           C  
ANISOU 1844  CB  SER A 232     9442  10440   9764   -157   -210    337       C  
ATOM   1845  OG  SER A 232       9.397   9.343 -18.785  1.00 69.89           O  
ANISOU 1845  OG  SER A 232     8428   9414   8712   -157   -205    316       O  
ATOM   1846  N   LYS A 233       5.403   8.454 -17.722  1.00 83.81           N  
ANISOU 1846  N   LYS A 233    10162  11196  10486   -183   -254    356       N  
ATOM   1847  CA  LYS A 233       3.975   8.523 -17.486  1.00 93.28           C  
ANISOU 1847  CA  LYS A 233    11343  12404  11695   -189   -267    383       C  
ATOM   1848  C   LYS A 233       3.589   7.750 -16.224  1.00 95.48           C  
ANISOU 1848  C   LYS A 233    11630  12658  11990   -192   -272    359       C  
ATOM   1849  O   LYS A 233       2.890   8.293 -15.364  1.00106.86           O  
ANISOU 1849  O   LYS A 233    13057  14084  13462   -184   -264    377       O  
ATOM   1850  CB  LYS A 233       3.224   7.981 -18.705  1.00 96.66           C  
ANISOU 1850  CB  LYS A 233    11768  12874  12087   -208   -293    399       C  
ATOM   1851  CG  LYS A 233       1.782   8.450 -18.819  1.00 95.90           C  
ANISOU 1851  CG  LYS A 233    11643  12796  12000   -211   -303    444       C  
ATOM   1852  CD  LYS A 233       0.810   7.378 -18.365  1.00102.46           C  
ANISOU 1852  CD  LYS A 233    12477  13629  12826   -228   -327    433       C  
ATOM   1853  CE  LYS A 233      -0.634   7.832 -18.498  1.00107.29           C  
ANISOU 1853  CE  LYS A 233    13058  14261  13448   -232   -338    480       C  
ATOM   1854  NZ  LYS A 233      -0.878   9.175 -17.914  1.00111.06           N1+
ANISOU 1854  NZ  LYS A 233    13512  14720  13966   -209   -312    515       N1+
ATOM   1855  N   LEU A 234       4.063   6.503 -16.116  1.00 89.37           N  
ANISOU 1855  N   LEU A 234    10881  11881  11195   -203   -283    319       N  
ATOM   1856  CA  LEU A 234       3.752   5.629 -14.982  1.00 83.38           C  
ANISOU 1856  CA  LEU A 234    10131  11101  10447   -207   -289    295       C  
ATOM   1857  C   LEU A 234       4.334   6.193 -13.693  1.00 85.59           C  
ANISOU 1857  C   LEU A 234    10412  11345  10762   -189   -266    283       C  
ATOM   1858  O   LEU A 234       3.651   6.255 -12.662  1.00 81.81           O  
ANISOU 1858  O   LEU A 234     9927  10849  10308   -185   -264    288       O  
ATOM   1859  CB  LEU A 234       4.298   4.222 -15.229  1.00 85.99           C  
ANISOU 1859  CB  LEU A 234    10489  11434  10748   -221   -302    255       C  
ATOM   1860  CG  LEU A 234       3.634   3.420 -16.368  1.00 95.53           C  
ANISOU 1860  CG  LEU A 234    11701  12676  11919   -243   -327    258       C  
ATOM   1861  CD1 LEU A 234       4.554   2.298 -16.811  1.00 99.84           C  
ANISOU 1861  CD1 LEU A 234    12276  13222  12436   -252   -331    218       C  
ATOM   1862  CD2 LEU A 234       2.268   2.832 -16.008  1.00 92.55           C  
ANISOU 1862  CD2 LEU A 234    11314  12305  11546   -258   -347    268       C  
ATOM   1863  N   VAL A 235       5.593   6.624 -13.777  1.00 89.80           N  
ANISOU 1863  N   VAL A 235    10954  11868  11297   -179   -249    269       N  
ATOM   1864  CA  VAL A 235       6.346   7.183 -12.643  1.00 87.60           C  
ANISOU 1864  CA  VAL A 235    10678  11557  11048   -164   -228    256       C  
ATOM   1865  C   VAL A 235       5.568   8.342 -12.027  1.00 84.75           C  
ANISOU 1865  C   VAL A 235    10298  11184  10721   -153   -215    286       C  
ATOM   1866  O   VAL A 235       5.350   8.389 -10.803  1.00 75.52           O  
ANISOU 1866  O   VAL A 235     9129   9991   9575   -147   -207    278       O  
ATOM   1867  CB  VAL A 235       7.789   7.619 -13.088  1.00 88.55           C  
ANISOU 1867  CB  VAL A 235    10806  11674  11164   -156   -213    243       C  
ATOM   1868  CG1 VAL A 235       8.483   8.490 -12.044  1.00 94.86           C  
ANISOU 1868  CG1 VAL A 235    11604  12443  11996   -142   -191    237       C  
ATOM   1869  CG2 VAL A 235       8.662   6.402 -13.379  1.00 83.17           C  
ANISOU 1869  CG2 VAL A 235    10149  10997  10456   -164   -221    208       C  
ATOM   1870  N   THR A 236       5.144   9.249 -12.911  1.00 90.27           N  
ANISOU 1870  N   THR A 236    10978  11900  11420   -150   -211    323       N  
ATOM   1871  CA  THR A 236       4.373  10.448 -12.565  1.00 89.47           C  
ANISOU 1871  CA  THR A 236    10854  11790  11349   -139   -196    359       C  
ATOM   1872  C   THR A 236       3.156  10.097 -11.753  1.00 83.26           C  
ANISOU 1872  C   THR A 236    10062  10998  10577   -141   -204    368       C  
ATOM   1873  O   THR A 236       2.947  10.638 -10.663  1.00 85.36           O  
ANISOU 1873  O   THR A 236    10324  11237  10873   -130   -187    369       O  
ATOM   1874  CB  THR A 236       3.878  11.168 -13.835  1.00 94.22           C  
ANISOU 1874  CB  THR A 236    11437  12421  11943   -139   -198    401       C  
ATOM   1875  CG2 THR A 236       3.264  12.479 -13.478  1.00 99.83           C  
ANISOU 1875  CG2 THR A 236    12125  13117  12687   -125   -177    438       C  
ATOM   1876  OG1 THR A 236       4.973  11.398 -14.733  1.00107.59           O  
ANISOU 1876  OG1 THR A 236    13136  14124  13619   -138   -193    395       O  
ATOM   1877  N   ASP A 237       2.378   9.170 -12.305  1.00 83.60           N  
ANISOU 1877  N   ASP A 237    10103  11065  10595   -156   -229    372       N  
ATOM   1878  CA  ASP A 237       1.113   8.745 -11.738  1.00 85.15           C  
ANISOU 1878  CA  ASP A 237    10289  11262  10801   -161   -240    385       C  
ATOM   1879  C   ASP A 237       1.354   7.949 -10.465  1.00 78.48           C  
ANISOU 1879  C   ASP A 237     9463  10391   9965   -161   -239    349       C  
ATOM   1880  O   ASP A 237       0.610   8.078  -9.475  1.00 69.19           O  
ANISOU 1880  O   ASP A 237     8279   9197   8812   -154   -232    357       O  
ATOM   1881  CB  ASP A 237       0.337   7.931 -12.770  1.00 89.13           C  
ANISOU 1881  CB  ASP A 237    10788  11802  11275   -181   -269    397       C  
ATOM   1882  CG  ASP A 237      -0.171   8.791 -13.935  1.00100.03           C  
ANISOU 1882  CG  ASP A 237    12146  13212  12650   -181   -271    441       C  
ATOM   1883  OD1 ASP A 237       0.480   9.812 -14.279  1.00107.33           O  
ANISOU 1883  OD1 ASP A 237    13065  14132  13582   -168   -252    454       O  
ATOM   1884  OD2 ASP A 237      -1.226   8.445 -14.517  1.00 99.37           O1-
ANISOU 1884  OD2 ASP A 237    12048  13155  12552   -194   -292    466       O1-
ATOM   1885  N   LEU A 238       2.424   7.159 -10.479  1.00 73.10           N  
ANISOU 1885  N   LEU A 238     8804   9705   9266   -165   -243    310       N  
ATOM   1886  CA  LEU A 238       2.806   6.429  -9.286  1.00 71.62           C  
ANISOU 1886  CA  LEU A 238     8634   9493   9086   -163   -240    275       C  
ATOM   1887  C   LEU A 238       3.225   7.379  -8.188  1.00 76.37           C  
ANISOU 1887  C   LEU A 238     9234  10065   9718   -146   -215    273       C  
ATOM   1888  O   LEU A 238       2.817   7.218  -7.036  1.00 84.64           O  
ANISOU 1888  O   LEU A 238    10283  11092  10783   -141   -210    267       O  
ATOM   1889  CB  LEU A 238       3.955   5.472  -9.546  1.00 62.63           C  
ANISOU 1889  CB  LEU A 238     7518   8356   7923   -170   -247    237       C  
ATOM   1890  CG  LEU A 238       4.361   4.697  -8.281  1.00 59.18           C  
ANISOU 1890  CG  LEU A 238     7097   7894   7494   -167   -244    204       C  
ATOM   1891  CD1 LEU A 238       3.162   4.256  -7.453  1.00 56.61           C  
ANISOU 1891  CD1 LEU A 238     6766   7562   7182   -169   -251    212       C  
ATOM   1892  CD2 LEU A 238       5.223   3.482  -8.635  1.00 63.51           C  
ANISOU 1892  CD2 LEU A 238     7667   8447   8016   -175   -254    170       C  
ATOM   1893  N   THR A 239       4.067   8.344  -8.535  1.00 71.91           N  
ANISOU 1893  N   THR A 239     8668   9496   9159   -138   -199    277       N  
ATOM   1894  CA  THR A 239       4.451   9.353  -7.577  1.00 76.70           C  
ANISOU 1894  CA  THR A 239     9273  10074   9795   -124   -175    276       C  
ATOM   1895  C   THR A 239       3.198   9.981  -6.949  1.00 79.51           C  
ANISOU 1895  C   THR A 239     9613  10420  10177   -117   -166    305       C  
ATOM   1896  O   THR A 239       3.088  10.102  -5.730  1.00 70.73           O  
ANISOU 1896  O   THR A 239     8506   9283   9084   -109   -154    294       O  
ATOM   1897  CB  THR A 239       5.300  10.439  -8.242  1.00 84.79           C  
ANISOU 1897  CB  THR A 239    10293  11099  10825   -118   -159    286       C  
ATOM   1898  CG2 THR A 239       5.368  11.666  -7.339  1.00 92.22           C  
ANISOU 1898  CG2 THR A 239    11228  12011  11799   -105   -132    293       C  
ATOM   1899  OG1 THR A 239       6.622   9.931  -8.490  1.00 78.47           O  
ANISOU 1899  OG1 THR A 239     9508  10300  10007   -121   -162    254       O  
ATOM   1900  N   LYS A 240       2.251  10.352  -7.804  1.00 88.59           N  
ANISOU 1900  N   LYS A 240    10744  11591  11326   -119   -171    343       N  
ATOM   1901  CA  LYS A 240       1.030  11.059  -7.386  1.00 91.75           C  
ANISOU 1901  CA  LYS A 240    11125  11984  11751   -110   -160    378       C  
ATOM   1902  C   LYS A 240       0.323  10.285  -6.292  1.00 80.41           C  
ANISOU 1902  C   LYS A 240     9694  10536  10323   -111   -166    367       C  
ATOM   1903  O   LYS A 240      -0.169  10.843  -5.301  1.00 78.07           O  
ANISOU 1903  O   LYS A 240     9394  10217  10053   -100   -147    376       O  
ATOM   1904  CB  LYS A 240       0.069  11.234  -8.589  1.00 92.48           C  
ANISOU 1904  CB  LYS A 240    11194  12108  11834   -116   -173    421       C  
ATOM   1905  CG  LYS A 240      -1.145  12.122  -8.334  1.00 89.99           C  
ANISOU 1905  CG  LYS A 240    10856  11789  11548   -105   -158    465       C  
ATOM   1906  CD  LYS A 240      -2.343  11.750  -9.205  1.00 93.51           C  
ANISOU 1906  CD  LYS A 240    11280  12268  11981   -115   -181    501       C  
ATOM   1907  CE  LYS A 240      -3.422  12.827  -9.087  1.00100.52           C  
ANISOU 1907  CE  LYS A 240    12141  13152  12900   -101   -162    551       C  
ATOM   1908  NZ  LYS A 240      -4.770  12.516  -9.645  1.00 97.43           N1+
ANISOU 1908  NZ  LYS A 240    11726  12791  12504   -109   -182    590       N1+
ATOM   1909  N   VAL A 241       0.271   8.983  -6.498  1.00 69.92           N  
ANISOU 1909  N   VAL A 241     8375   9222   8970   -125   -190    348       N  
ATOM   1910  CA  VAL A 241      -0.562   8.168  -5.687  1.00 69.41           C  
ANISOU 1910  CA  VAL A 241     8311   9151   8910   -128   -199    344       C  
ATOM   1911  C   VAL A 241       0.053   8.239  -4.310  1.00 73.71           C  
ANISOU 1911  C   VAL A 241     8872   9664   9470   -117   -182    315       C  
ATOM   1912  O   VAL A 241      -0.573   8.694  -3.338  1.00 75.06           O  
ANISOU 1912  O   VAL A 241     9038   9816   9665   -107   -166    326       O  
ATOM   1913  CB  VAL A 241      -0.579   6.749  -6.230  1.00 68.57           C  
ANISOU 1913  CB  VAL A 241     8215   9066   8774   -146   -227    325       C  
ATOM   1914  CG1 VAL A 241      -1.098   5.791  -5.176  1.00 68.32           C  
ANISOU 1914  CG1 VAL A 241     8190   9021   8748   -149   -234    309       C  
ATOM   1915  CG2 VAL A 241      -1.385   6.676  -7.528  1.00 64.80           C  
ANISOU 1915  CG2 VAL A 241     7720   8622   8281   -159   -247    355       C  
ATOM   1916  N   HIS A 242       1.319   7.849  -4.254  1.00 68.69           N  
ANISOU 1916  N   HIS A 242     8255   9023   8820   -120   -183    279       N  
ATOM   1917  CA  HIS A 242       2.016   7.783  -3.001  1.00 76.94           C  
ANISOU 1917  CA  HIS A 242     9316  10042   9875   -112   -171    249       C  
ATOM   1918  C   HIS A 242       2.117   9.128  -2.324  1.00 77.42           C  
ANISOU 1918  C   HIS A 242     9374  10080   9963    -98   -143    259       C  
ATOM   1919  O   HIS A 242       2.207   9.210  -1.092  1.00 82.83           O  
ANISOU 1919  O   HIS A 242    10068  10742  10661    -91   -131    244       O  
ATOM   1920  CB  HIS A 242       3.406   7.172  -3.185  1.00 81.13           C  
ANISOU 1920  CB  HIS A 242     9865  10574  10386   -118   -177    214       C  
ATOM   1921  CG  HIS A 242       3.389   5.683  -3.301  1.00 84.49           C  
ANISOU 1921  CG  HIS A 242    10301  11011  10790   -129   -198    193       C  
ATOM   1922  CD2 HIS A 242       3.955   4.851  -4.203  1.00 88.25           C  
ANISOU 1922  CD2 HIS A 242    10786  11505  11240   -140   -214    178       C  
ATOM   1923  ND1 HIS A 242       2.734   4.876  -2.395  1.00 90.49           N  
ANISOU 1923  ND1 HIS A 242    11065  11763  11554   -129   -204    186       N  
ATOM   1924  CE1 HIS A 242       2.870   3.611  -2.749  1.00 90.34           C  
ANISOU 1924  CE1 HIS A 242    11056  11755  11514   -140   -222    169       C  
ATOM   1925  NE2 HIS A 242       3.617   3.568  -3.839  1.00 91.93           N  
ANISOU 1925  NE2 HIS A 242    11261  11971  11697   -147   -228    163       N  
ATOM   1926  N   THR A 243       2.098  10.197  -3.104  1.00 75.84           N  
ANISOU 1926  N   THR A 243     9160   9884   9771    -95   -132    285       N  
ATOM   1927  CA  THR A 243       2.155  11.493  -2.464  1.00 75.99           C  
ANISOU 1927  CA  THR A 243     9176   9879   9817    -82   -104    294       C  
ATOM   1928  C   THR A 243       0.884  11.603  -1.635  1.00 73.22           C  
ANISOU 1928  C   THR A 243     8818   9517   9486    -74    -95    314       C  
ATOM   1929  O   THR A 243       0.925  12.016  -0.474  1.00 78.10           O  
ANISOU 1929  O   THR A 243     9444  10108  10121    -65    -76    303       O  
ATOM   1930  CB  THR A 243       2.323  12.694  -3.431  1.00 73.63           C  
ANISOU 1930  CB  THR A 243     8864   9585   9528    -77    -90    321       C  
ATOM   1931  CG2 THR A 243       2.432  13.983  -2.614  1.00 71.37           C  
ANISOU 1931  CG2 THR A 243     8577   9267   9271    -65    -58    326       C  
ATOM   1932  OG1 THR A 243       3.501  12.544  -4.259  1.00 62.81           O  
ANISOU 1932  OG1 THR A 243     7500   8228   8138    -84    -99    304       O  
ATOM   1933  N   GLU A 244      -0.221  11.152  -2.212  1.00 71.85           N  
ANISOU 1933  N   GLU A 244     8628   9363   9308    -78   -110    342       N  
ATOM   1934  CA  GLU A 244      -1.517  11.319  -1.577  1.00 82.57           C  
ANISOU 1934  CA  GLU A 244     9974  10712  10686    -70   -101    368       C  
ATOM   1935  C   GLU A 244      -1.702  10.432  -0.331  1.00 79.57           C  
ANISOU 1935  C   GLU A 244     9608  10318  10306    -70   -105    343       C  
ATOM   1936  O   GLU A 244      -2.223  10.892   0.700  1.00 71.93           O  
ANISOU 1936  O   GLU A 244     8642   9329   9360    -58    -84    350       O  
ATOM   1937  CB  GLU A 244      -2.622  11.105  -2.609  1.00 89.90           C  
ANISOU 1937  CB  GLU A 244    10879  11670  11609    -77   -118    407       C  
ATOM   1938  CG  GLU A 244      -2.683  12.231  -3.645  1.00 95.18           C  
ANISOU 1938  CG  GLU A 244    11530  12349  12285    -72   -108    442       C  
ATOM   1939  CD  GLU A 244      -3.431  11.861  -4.932  1.00103.78           C  
ANISOU 1939  CD  GLU A 244    12598  13475  13358    -84   -132    473       C  
ATOM   1940  OE1 GLU A 244      -3.560  10.654  -5.248  1.00108.52           O  
ANISOU 1940  OE1 GLU A 244    13203  14095  13934    -99   -160    459       O  
ATOM   1941  OE2 GLU A 244      -3.898  12.793  -5.637  1.00102.51           O1-
ANISOU 1941  OE2 GLU A 244    12417  13324  13208    -77   -122    513       O1-
ATOM   1942  N   CYS A 245      -1.239   9.187  -0.410  1.00 77.87           N  
ANISOU 1942  N   CYS A 245     9405  10115  10067    -82   -128    315       N  
ATOM   1943  CA  CYS A 245      -1.328   8.276   0.741  1.00 85.08           C  
ANISOU 1943  CA  CYS A 245    10332  11015  10979    -81   -131    291       C  
ATOM   1944  C   CYS A 245      -0.420   8.641   1.907  1.00 84.48           C  
ANISOU 1944  C   CYS A 245    10275  10913  10910    -72   -113    261       C  
ATOM   1945  O   CYS A 245      -0.645   8.199   3.034  1.00 82.27           O  
ANISOU 1945  O   CYS A 245    10004  10619  10635    -68   -109    248       O  
ATOM   1946  CB  CYS A 245      -1.044   6.828   0.328  1.00 91.52           C  
ANISOU 1946  CB  CYS A 245    11156  11849  11768    -96   -159    269       C  
ATOM   1947  SG  CYS A 245      -2.545   5.846   0.162  1.00 98.79           S  
ANISOU 1947  SG  CYS A 245    12062  12785  12688   -105   -179    293       S  
ATOM   1948  N   CYS A 246       0.625   9.410   1.627  1.00 85.51           N  
ANISOU 1948  N   CYS A 246    10411  11038  11040    -71   -103    249       N  
ATOM   1949  CA  CYS A 246       1.519   9.897   2.673  1.00 95.55           C  
ANISOU 1949  CA  CYS A 246    11700  12287  12319    -65    -85    222       C  
ATOM   1950  C   CYS A 246       0.994  11.189   3.238  1.00 98.95           C  
ANISOU 1950  C   CYS A 246    12126  12695  12776    -53    -56    241       C  
ATOM   1951  O   CYS A 246       1.185  11.513   4.419  1.00 92.56           O  
ANISOU 1951  O   CYS A 246    11329  11862  11976    -46    -39    224       O  
ATOM   1952  CB  CYS A 246       2.909  10.141   2.102  1.00100.29           C  
ANISOU 1952  CB  CYS A 246    12307  12891  12907    -71    -88    201       C  
ATOM   1953  SG  CYS A 246       3.775   8.628   1.657  1.00105.31           S  
ANISOU 1953  SG  CYS A 246    12953  13546  13512    -83   -116    172       S  
ATOM   1954  N   HIS A 247       0.318  11.919   2.367  1.00101.55           N  
ANISOU 1954  N   HIS A 247    12436  13031  13117    -50    -50    277       N  
ATOM   1955  CA  HIS A 247      -0.174  13.225   2.694  1.00 97.62           C  
ANISOU 1955  CA  HIS A 247    11932  12512  12646    -37    -20    300       C  
ATOM   1956  C   HIS A 247      -1.551  13.095   3.344  1.00 84.65           C  
ANISOU 1956  C   HIS A 247    10281  10862  11019    -28    -11    324       C  
ATOM   1957  O   HIS A 247      -2.216  14.072   3.626  1.00 77.83           O  
ANISOU 1957  O   HIS A 247     9411   9983  10180    -16     15    349       O  
ATOM   1958  CB  HIS A 247      -0.232  14.039   1.413  1.00104.04           C  
ANISOU 1958  CB  HIS A 247    12728  13338  13466    -37    -16    330       C  
ATOM   1959  CG  HIS A 247       0.360  15.390   1.546  1.00113.86           C  
ANISOU 1959  CG  HIS A 247    13975  14559  14728    -30     13    330       C  
ATOM   1960  CD2 HIS A 247       1.640  15.804   1.456  1.00116.90           C  
ANISOU 1960  CD2 HIS A 247    14371  14937  15110    -35     17    305       C  
ATOM   1961  ND1 HIS A 247      -0.401  16.509   1.818  1.00120.19           N  
ANISOU 1961  ND1 HIS A 247    14767  15340  15559    -17     43    359       N  
ATOM   1962  CE1 HIS A 247       0.388  17.561   1.898  1.00130.27           C  
ANISOU 1962  CE1 HIS A 247    16052  16597  16849    -15     65    350       C  
ATOM   1963  NE2 HIS A 247       1.630  17.162   1.670  1.00145.98           N  
ANISOU 1963  NE2 HIS A 247    18052  18594  18818    -26     49    318       N  
ATOM   1964  N   GLY A 248      -1.978  11.861   3.565  1.00 86.45           N  
ANISOU 1964  N   GLY A 248    10511  11104  11234    -34    -33    317       N  
ATOM   1965  CA  GLY A 248      -3.235  11.594   4.241  1.00 84.18           C  
ANISOU 1965  CA  GLY A 248    10216  10810  10959    -26    -27    338       C  
ATOM   1966  C   GLY A 248      -4.430  11.517   3.319  1.00 76.79           C  
ANISOU 1966  C   GLY A 248     9253   9895  10029    -27    -37    382       C  
ATOM   1967  O   GLY A 248      -5.508  11.104   3.735  1.00 76.07           O  
ANISOU 1967  O   GLY A 248     9152   9805   9947    -23    -38    401       O  
ATOM   1968  N   ASP A 249      -4.215  11.902   2.068  1.00 80.87           N  
ANISOU 1968  N   ASP A 249     9756  10430  10540    -33    -45    398       N  
ATOM   1969  CA  ASP A 249      -5.267  12.022   1.058  1.00 90.53           C  
ANISOU 1969  CA  ASP A 249    10953  11676  11768    -35    -54    444       C  
ATOM   1970  C   ASP A 249      -5.786  10.658   0.623  1.00 85.33           C  
ANISOU 1970  C   ASP A 249    10288  11045  11090    -50    -88    444       C  
ATOM   1971  O   ASP A 249      -5.665  10.283  -0.545  1.00 87.49           O  
ANISOU 1971  O   ASP A 249    10554  11346  11344    -64   -111    450       O  
ATOM   1972  CB  ASP A 249      -4.699  12.760  -0.167  1.00104.56           C  
ANISOU 1972  CB  ASP A 249    12721  13468  13540    -38    -55    456       C  
ATOM   1973  CG  ASP A 249      -4.334  14.198   0.131  1.00111.26           C  
ANISOU 1973  CG  ASP A 249    13572  14290  14412    -24    -20    463       C  
ATOM   1974  OD1 ASP A 249      -5.115  14.840   0.850  1.00115.67           O  
ANISOU 1974  OD1 ASP A 249    14125  14828  14997     -9      6    484       O  
ATOM   1975  OD2 ASP A 249      -3.294  14.690  -0.358  1.00103.03           O1-
ANISOU 1975  OD2 ASP A 249    12536  13246  13363    -26    -16    449       O1-
ATOM   1976  N   LEU A 250      -6.398   9.935   1.555  1.00 82.16           N  
ANISOU 1976  N   LEU A 250     9890  10635  10693    -48    -90    439       N  
ATOM   1977  CA  LEU A 250      -6.582   8.497   1.405  1.00 78.27           C  
ANISOU 1977  CA  LEU A 250     9400  10160  10180    -64   -120    424       C  
ATOM   1978  C   LEU A 250      -7.539   8.107   0.299  1.00 79.48           C  
ANISOU 1978  C   LEU A 250     9529  10344  10327    -77   -144    458       C  
ATOM   1979  O   LEU A 250      -7.282   7.161  -0.451  1.00 84.83           O  
ANISOU 1979  O   LEU A 250    10209  11043  10979    -95   -172    444       O  
ATOM   1980  CB  LEU A 250      -7.048   7.901   2.724  1.00 78.99           C  
ANISOU 1980  CB  LEU A 250     9500  10233  10281    -57   -114    414       C  
ATOM   1981  CG  LEU A 250      -6.043   7.848   3.871  1.00 86.03           C  
ANISOU 1981  CG  LEU A 250    10418  11099  11169    -50   -100    372       C  
ATOM   1982  CD1 LEU A 250      -6.657   7.132   5.058  1.00 89.31           C  
ANISOU 1982  CD1 LEU A 250    10839  11501  11592    -44    -96    367       C  
ATOM   1983  CD2 LEU A 250      -4.759   7.126   3.446  1.00 93.70           C  
ANISOU 1983  CD2 LEU A 250    11408  12081  12114    -63   -120    332       C  
ATOM   1984  N   LEU A 251      -8.641   8.829   0.187  1.00 74.23           N  
ANISOU 1984  N   LEU A 251     8839   9681   9684    -68   -132    504       N  
ATOM   1985  CA  LEU A 251      -9.630   8.467  -0.787  1.00 80.01           C  
ANISOU 1985  CA  LEU A 251     9545  10444  10410    -81   -155    540       C  
ATOM   1986  C   LEU A 251      -9.106   8.595  -2.223  1.00 92.83           C  
ANISOU 1986  C   LEU A 251    11163  12095  12011    -94   -174    543       C  
ATOM   1987  O   LEU A 251      -9.304   7.680  -3.034  1.00 97.79           O  
ANISOU 1987  O   LEU A 251    11787  12751  12616   -115   -205    541       O  
ATOM   1988  CB  LEU A 251     -10.890   9.281  -0.566  1.00 85.71           C  
ANISOU 1988  CB  LEU A 251    10241  11163  11164    -66   -136    591       C  
ATOM   1989  CG  LEU A 251     -11.648   8.765   0.657  1.00 92.13           C  
ANISOU 1989  CG  LEU A 251    11054  11956  11993    -58   -127    591       C  
ATOM   1990  CD1 LEU A 251     -12.408   9.866   1.385  1.00 87.13           C  
ANISOU 1990  CD1 LEU A 251    10409  11301  11395    -34    -91    626       C  
ATOM   1991  CD2 LEU A 251     -12.596   7.637   0.245  1.00105.75           C  
ANISOU 1991  CD2 LEU A 251    12762  13708  13710    -77   -159    607       C  
ATOM   1992  N   GLU A 252      -8.442   9.713  -2.537  1.00 94.97           N  
ANISOU 1992  N   GLU A 252    11436  12360  12288    -84   -154    547       N  
ATOM   1993  CA  GLU A 252      -7.918   9.945  -3.894  1.00 88.39           C  
ANISOU 1993  CA  GLU A 252    10598  11552  11434    -94   -168    553       C  
ATOM   1994  C   GLU A 252      -6.711   9.035  -4.150  1.00 86.06           C  
ANISOU 1994  C   GLU A 252    10328  11261  11107   -108   -187    503       C  
ATOM   1995  O   GLU A 252      -6.504   8.554  -5.280  1.00 82.82           O  
ANISOU 1995  O   GLU A 252     9917  10880  10671   -125   -211    501       O  
ATOM   1996  CB  GLU A 252      -7.589  11.418  -4.142  1.00 91.58           C  
ANISOU 1996  CB  GLU A 252    10994  11946  11856    -77   -140    574       C  
ATOM   1997  CG  GLU A 252      -6.740  12.103  -3.068  1.00111.86           C  
ANISOU 1997  CG  GLU A 252    13585  14476  14442    -61   -108    546       C  
ATOM   1998  CD  GLU A 252      -7.539  12.723  -1.907  1.00124.49           C  
ANISOU 1998  CD  GLU A 252    15179  16047  16076    -43    -78    565       C  
ATOM   1999  OE1 GLU A 252      -8.078  11.958  -1.070  1.00122.48           O  
ANISOU 1999  OE1 GLU A 252    14929  15785  15824    -43    -84    556       O  
ATOM   2000  OE2 GLU A 252      -7.584  13.978  -1.805  1.00125.81           O1-
ANISOU 2000  OE2 GLU A 252    15339  16196  16267    -26    -48    587       O1-
ATOM   2001  N   CYS A 253      -5.947   8.767  -3.090  1.00 83.89           N  
ANISOU 2001  N   CYS A 253    10078  10960  10836   -102   -175    464       N  
ATOM   2002  CA  CYS A 253      -4.872   7.787  -3.152  1.00 80.25           C  
ANISOU 2002  CA  CYS A 253     9641  10500  10348   -114   -192    418       C  
ATOM   2003  C   CYS A 253      -5.431   6.477  -3.671  1.00 75.52           C  
ANISOU 2003  C   CYS A 253     9041   9926   9729   -134   -223    415       C  
ATOM   2004  O   CYS A 253      -4.930   5.886  -4.634  1.00 73.95           O  
ANISOU 2004  O   CYS A 253     8847   9747   9502   -150   -244    400       O  
ATOM   2005  CB  CYS A 253      -4.216   7.568  -1.782  1.00 81.95           C  
ANISOU 2005  CB  CYS A 253     9880  10686  10572   -104   -177    381       C  
ATOM   2006  SG  CYS A 253      -3.088   6.158  -1.772  1.00 94.25           S  
ANISOU 2006  SG  CYS A 253    11464  12247  12100   -118   -198    330       S  
ATOM   2007  N   ALA A 254      -6.497   6.016  -3.055  1.00 75.84           N  
ANISOU 2007  N   ALA A 254     9071   9963   9782   -134   -227    429       N  
ATOM   2008  CA  ALA A 254      -6.980   4.713  -3.444  1.00 84.74           C  
ANISOU 2008  CA  ALA A 254    10197  11109  10890   -155   -256    423       C  
ATOM   2009  C   ALA A 254      -7.471   4.747  -4.897  1.00 84.77           C  
ANISOU 2009  C   ALA A 254    10183  11149  10877   -171   -278    450       C  
ATOM   2010  O   ALA A 254      -7.069   3.916  -5.717  1.00 82.81           O  
ANISOU 2010  O   ALA A 254     9946  10920  10600   -190   -301    430       O  
ATOM   2011  CB  ALA A 254      -8.060   4.242  -2.484  1.00 89.77           C  
ANISOU 2011  CB  ALA A 254    10826  11735  11547   -152   -255    435       C  
ATOM   2012  N   ASP A 255      -8.293   5.753  -5.197  1.00 83.81           N  
ANISOU 2012  N   ASP A 255    10035  11035  10772   -163   -269    496       N  
ATOM   2013  CA  ASP A 255      -8.911   5.924  -6.503  1.00 80.23           C  
ANISOU 2013  CA  ASP A 255     9560  10619  10306   -177   -289    531       C  
ATOM   2014  C   ASP A 255      -7.873   5.958  -7.584  1.00 83.65           C  
ANISOU 2014  C   ASP A 255    10005  11069  10710   -186   -298    512       C  
ATOM   2015  O   ASP A 255      -8.000   5.261  -8.578  1.00 94.55           O  
ANISOU 2015  O   ASP A 255    11384  12477  12061   -207   -325    510       O  
ATOM   2016  CB  ASP A 255      -9.692   7.230  -6.546  1.00 92.21           C  
ANISOU 2016  CB  ASP A 255    11048  12137  11851   -160   -269    583       C  
ATOM   2017  CG  ASP A 255     -10.602   7.324  -7.752  1.00102.88           C  
ANISOU 2017  CG  ASP A 255    12370  13527  13191   -174   -291    626       C  
ATOM   2018  OD1 ASP A 255     -10.722   6.310  -8.471  1.00107.52           O  
ANISOU 2018  OD1 ASP A 255    12962  14142  13751   -199   -323    615       O  
ATOM   2019  OD2 ASP A 255     -11.210   8.405  -7.964  1.00110.34           O1-
ANISOU 2019  OD2 ASP A 255    13289  14477  14156   -160   -276    673       O1-
ATOM   2020  N   ASP A 256      -6.830   6.756  -7.389  1.00 79.05           N  
ANISOU 2020  N   ASP A 256     9435  10468  10133   -170   -275    497       N  
ATOM   2021  CA  ASP A 256      -5.780   6.831  -8.378  1.00 76.25           C  
ANISOU 2021  CA  ASP A 256     9092  10126   9752   -176   -280    480       C  
ATOM   2022  C   ASP A 256      -4.997   5.534  -8.495  1.00 75.68           C  
ANISOU 2022  C   ASP A 256     9047  10056   9651   -192   -299    433       C  
ATOM   2023  O   ASP A 256      -4.619   5.131  -9.593  1.00 82.77           O  
ANISOU 2023  O   ASP A 256     9951  10979  10519   -207   -316    425       O  
ATOM   2024  CB  ASP A 256      -4.890   8.007  -8.074  1.00 78.48           C  
ANISOU 2024  CB  ASP A 256     9381  10388  10052   -156   -250    477       C  
ATOM   2025  CG  ASP A 256      -5.634   9.295  -8.183  1.00 89.23           C  
ANISOU 2025  CG  ASP A 256    10715  11749  11439   -141   -232    526       C  
ATOM   2026  OD1 ASP A 256      -6.692   9.279  -8.858  1.00106.86           O  
ANISOU 2026  OD1 ASP A 256    12924  14009  13669   -149   -247    565       O  
ATOM   2027  OD2 ASP A 256      -5.194  10.315  -7.610  1.00 94.72           O1-
ANISOU 2027  OD2 ASP A 256    11413  12419  12159   -122   -202    528       O1-
ATOM   2028  N   ARG A 257      -4.776   4.847  -7.390  1.00 69.86           N  
ANISOU 2028  N   ARG A 257     8326   9294   8922   -189   -294    402       N  
ATOM   2029  CA  ARG A 257      -4.075   3.587  -7.491  1.00 74.04           C  
ANISOU 2029  CA  ARG A 257     8880   9824   9426   -203   -310    360       C  
ATOM   2030  C   ARG A 257      -4.844   2.680  -8.467  1.00 72.28           C  
ANISOU 2030  C   ARG A 257     8652   9633   9180   -229   -341    368       C  
ATOM   2031  O   ARG A 257      -4.250   2.132  -9.406  1.00 65.46           O  
ANISOU 2031  O   ARG A 257     7802   8786   8286   -243   -355    349       O  
ATOM   2032  CB  ARG A 257      -3.899   2.951  -6.107  1.00 78.55           C  
ANISOU 2032  CB  ARG A 257     9467  10366  10012   -196   -301    332       C  
ATOM   2033  CG  ARG A 257      -3.090   1.644  -6.044  1.00 81.38           C  
ANISOU 2033  CG  ARG A 257     9851  10720  10349   -207   -312    287       C  
ATOM   2034  CD  ARG A 257      -3.538   0.791  -4.834  1.00 86.89           C  
ANISOU 2034  CD  ARG A 257    10555  11398  11061   -205   -312    274       C  
ATOM   2035  NE  ARG A 257      -2.795  -0.457  -4.608  1.00 92.55           N  
ANISOU 2035  NE  ARG A 257    11297  12107  11762   -213   -319    234       N  
ATOM   2036  CZ  ARG A 257      -3.293  -1.578  -4.049  1.00103.43           C  
ANISOU 2036  CZ  ARG A 257    12680  13477  13142   -221   -329    222       C  
ATOM   2037  NH1 ARG A 257      -4.558  -1.670  -3.647  1.00 97.58           N1+
ANISOU 2037  NH1 ARG A 257    11921  12737  12417   -224   -334    247       N1+
ATOM   2038  NH2 ARG A 257      -2.514  -2.652  -3.898  1.00115.22           N  
ANISOU 2038  NH2 ARG A 257    14195  14962  14621   -226   -332    186       N  
ATOM   2039  N   ALA A 258      -6.160   2.555  -8.271  1.00 76.28           N  
ANISOU 2039  N   ALA A 258     9138  10147   9700   -234   -350    398       N  
ATOM   2040  CA  ALA A 258      -6.994   1.637  -9.093  1.00 79.94           C  
ANISOU 2040  CA  ALA A 258     9594  10640  10142   -262   -381    406       C  
ATOM   2041  C   ALA A 258      -7.268   2.153 -10.509  1.00 77.15           C  
ANISOU 2041  C   ALA A 258     9223  10322   9767   -273   -396    435       C  
ATOM   2042  O   ALA A 258      -7.576   1.352 -11.399  1.00 72.18           O  
ANISOU 2042  O   ALA A 258     8595   9719   9109   -298   -423    431       O  
ATOM   2043  CB  ALA A 258      -8.301   1.279  -8.395  1.00 72.45           C  
ANISOU 2043  CB  ALA A 258     8626   9687   9214   -265   -388    429       C  
ATOM   2044  N   ASP A 259      -7.168   3.472 -10.707  1.00 72.44           N  
ANISOU 2044  N   ASP A 259     8612   9728   9184   -255   -378    465       N  
ATOM   2045  CA  ASP A 259      -7.056   4.026 -12.046  1.00 74.79           C  
ANISOU 2045  CA  ASP A 259     8900  10058   9460   -262   -387    487       C  
ATOM   2046  C   ASP A 259      -5.755   3.539 -12.653  1.00 74.11           C  
ANISOU 2046  C   ASP A 259     8842   9974   9342   -269   -390    445       C  
ATOM   2047  O   ASP A 259      -5.710   3.214 -13.826  1.00 84.70           O  
ANISOU 2047  O   ASP A 259    10185  11345  10650   -287   -410    445       O  
ATOM   2048  CB  ASP A 259      -7.043   5.555 -12.041  1.00 85.31           C  
ANISOU 2048  CB  ASP A 259    10213  11386  10817   -238   -361    523       C  
ATOM   2049  CG  ASP A 259      -8.463   6.184 -11.903  1.00 97.87           C  
ANISOU 2049  CG  ASP A 259    11767  12987  12433   -233   -361    578       C  
ATOM   2050  OD1 ASP A 259      -9.488   5.422 -11.821  1.00 80.24           O  
ANISOU 2050  OD1 ASP A 259     9522  10766  10198   -249   -382    589       O  
ATOM   2051  OD2 ASP A 259      -8.525   7.464 -11.863  1.00 94.15           O1-
ANISOU 2051  OD2 ASP A 259    11279  12510  11984   -212   -337    611       O1-
ATOM   2052  N   LEU A 260      -4.689   3.473 -11.862  1.00 74.95           N  
ANISOU 2052  N   LEU A 260     8971  10048   9457   -255   -370    409       N  
ATOM   2053  CA  LEU A 260      -3.381   3.154 -12.421  1.00 74.15           C  
ANISOU 2053  CA  LEU A 260     8896   9948   9330   -257   -369    373       C  
ATOM   2054  C   LEU A 260      -3.294   1.677 -12.712  1.00 74.43           C  
ANISOU 2054  C   LEU A 260     8953   9990   9338   -280   -391    339       C  
ATOM   2055  O   LEU A 260      -2.722   1.282 -13.719  1.00 71.32           O  
ANISOU 2055  O   LEU A 260     8573   9614   8912   -293   -401    323       O  
ATOM   2056  CB  LEU A 260      -2.235   3.618 -11.514  1.00 74.00           C  
ANISOU 2056  CB  LEU A 260     8892   9895   9331   -235   -341    349       C  
ATOM   2057  CG  LEU A 260      -0.766   3.273 -11.878  1.00 69.70           C  
ANISOU 2057  CG  LEU A 260     8373   9345   8764   -235   -336    311       C  
ATOM   2058  CD1 LEU A 260      -0.385   3.739 -13.255  1.00 73.55           C  
ANISOU 2058  CD1 LEU A 260     8858   9860   9228   -240   -340    324       C  
ATOM   2059  CD2 LEU A 260       0.228   3.881 -10.908  1.00 64.41           C  
ANISOU 2059  CD2 LEU A 260     7712   8643   8117   -213   -309    294       C  
ATOM   2060  N   ALA A 261      -3.847   0.844 -11.848  1.00 81.23           N  
ANISOU 2060  N   ALA A 261     9816  10836  10210   -286   -397    327       N  
ATOM   2061  CA  ALA A 261      -3.963  -0.567 -12.196  1.00 91.38           C  
ANISOU 2061  CA  ALA A 261    11120  12130  11472   -310   -419    299       C  
ATOM   2062  C   ALA A 261      -4.679  -0.717 -13.548  1.00 94.58           C  
ANISOU 2062  C   ALA A 261    11514  12575  11847   -335   -445    320       C  
ATOM   2063  O   ALA A 261      -4.217  -1.477 -14.408  1.00100.22           O  
ANISOU 2063  O   ALA A 261    12248  13303  12527   -353   -459    295       O  
ATOM   2064  CB  ALA A 261      -4.704  -1.332 -11.113  1.00 92.95           C  
ANISOU 2064  CB  ALA A 261    11317  12310  11691   -313   -423    294       C  
ATOM   2065  N   LYS A 262      -5.780   0.016 -13.743  1.00 90.09           N  
ANISOU 2065  N   LYS A 262    10914  12025  11290   -336   -452    366       N  
ATOM   2066  CA  LYS A 262      -6.555  -0.116 -14.977  1.00 91.90           C  
ANISOU 2066  CA  LYS A 262    11130  12297  11493   -361   -480    390       C  
ATOM   2067  C   LYS A 262      -5.847   0.330 -16.248  1.00 82.99           C  
ANISOU 2067  C   LYS A 262    10007  11193  10332   -364   -482    391       C  
ATOM   2068  O   LYS A 262      -5.834  -0.405 -17.222  1.00 91.95           O  
ANISOU 2068  O   LYS A 262    11155  12352  11430   -388   -503    377       O  
ATOM   2069  CB  LYS A 262      -7.944   0.519 -14.882  1.00100.72           C  
ANISOU 2069  CB  LYS A 262    12208  13429  12631   -361   -488    443       C  
ATOM   2070  CG  LYS A 262      -9.029  -0.536 -14.682  1.00118.37           C  
ANISOU 2070  CG  LYS A 262    14438  15672  14866   -385   -512    443       C  
ATOM   2071  CD  LYS A 262     -10.232  -0.361 -15.598  1.00136.48           C  
ANISOU 2071  CD  LYS A 262    16701  18008  17147   -406   -539    487       C  
ATOM   2072  CE  LYS A 262     -11.044  -1.650 -15.688  1.00140.28           C  
ANISOU 2072  CE  LYS A 262    17184  18499  17615   -439   -569    475       C  
ATOM   2073  NZ  LYS A 262     -11.879  -1.701 -16.918  1.00143.27           N1+
ANISOU 2073  NZ  LYS A 262    17544  18927  17965   -468   -601    504       N1+
ATOM   2074  N   TYR A 263      -5.251   1.514 -16.245  1.00 83.16           N  
ANISOU 2074  N   TYR A 263    10022  11209  10368   -339   -459    407       N  
ATOM   2075  CA  TYR A 263      -4.450   1.970 -17.404  1.00 81.04           C  
ANISOU 2075  CA  TYR A 263     9760  10962  10070   -339   -457    408       C  
ATOM   2076  C   TYR A 263      -3.410   0.915 -17.816  1.00 83.21           C  
ANISOU 2076  C   TYR A 263    10072  11232  10312   -351   -461    357       C  
ATOM   2077  O   TYR A 263      -3.176   0.688 -19.016  1.00 89.53           O  
ANISOU 2077  O   TYR A 263    10882  12062  11075   -367   -474    352       O  
ATOM   2078  CB  TYR A 263      -3.734   3.299 -17.106  1.00 76.96           C  
ANISOU 2078  CB  TYR A 263     9236  10428   9578   -309   -426    423       C  
ATOM   2079  CG  TYR A 263      -2.747   3.770 -18.185  1.00 78.20           C  
ANISOU 2079  CG  TYR A 263     9402  10602   9709   -305   -420    420       C  
ATOM   2080  CD1 TYR A 263      -3.067   4.825 -19.048  1.00 82.26           C  
ANISOU 2080  CD1 TYR A 263     9892  11143  10219   -300   -419    464       C  
ATOM   2081  CD2 TYR A 263      -1.500   3.188 -18.333  1.00 80.94           C  
ANISOU 2081  CD2 TYR A 263     9781  10937  10037   -305   -413    376       C  
ATOM   2082  CE1 TYR A 263      -2.178   5.280 -20.017  1.00 74.89           C  
ANISOU 2082  CE1 TYR A 263     8967  10225   9264   -296   -412    464       C  
ATOM   2083  CE2 TYR A 263      -0.612   3.631 -19.303  1.00 79.57           C  
ANISOU 2083  CE2 TYR A 263     9614  10777   9841   -301   -405    376       C  
ATOM   2084  CZ  TYR A 263      -0.961   4.675 -20.139  1.00 78.36           C  
ANISOU 2084  CZ  TYR A 263     9437  10651   9684   -296   -405    419       C  
ATOM   2085  OH  TYR A 263      -0.080   5.124 -21.085  1.00 81.71           O  
ANISOU 2085  OH  TYR A 263     9868  11090  10087   -291   -396    420       O  
ATOM   2086  N   ILE A 264      -2.806   0.272 -16.815  1.00 78.87           N  
ANISOU 2086  N   ILE A 264     9543  10648   9777   -344   -449    319       N  
ATOM   2087  CA  ILE A 264      -1.751  -0.688 -17.043  1.00 77.71           C  
ANISOU 2087  CA  ILE A 264     9430  10490   9605   -351   -447    272       C  
ATOM   2088  C   ILE A 264      -2.281  -1.934 -17.727  1.00 80.90           C  
ANISOU 2088  C   ILE A 264     9848  10914   9977   -383   -474    254       C  
ATOM   2089  O   ILE A 264      -1.747  -2.387 -18.763  1.00 76.18           O  
ANISOU 2089  O   ILE A 264     9269  10333   9341   -397   -481    235       O  
ATOM   2090  CB  ILE A 264      -1.091  -1.091 -15.722  1.00 79.06           C  
ANISOU 2090  CB  ILE A 264     9617  10620   9803   -334   -428    241       C  
ATOM   2091  CG1 ILE A 264      -0.261   0.060 -15.222  1.00 83.65           C  
ANISOU 2091  CG1 ILE A 264    10192  11183  10408   -306   -401    249       C  
ATOM   2092  CG2 ILE A 264      -0.177  -2.309 -15.886  1.00 81.20           C  
ANISOU 2092  CG2 ILE A 264     9922  10880  10050   -344   -428    193       C  
ATOM   2093  CD1 ILE A 264       0.062  -0.120 -13.763  1.00 89.23           C  
ANISOU 2093  CD1 ILE A 264    10905  11852  11145   -290   -384    230       C  
ATOM   2094  N   CYS A 265      -3.334  -2.491 -17.144  1.00 80.62           N  
ANISOU 2094  N   CYS A 265     9802  10875   9956   -395   -489    260       N  
ATOM   2095  CA  CYS A 265      -3.853  -3.754 -17.619  1.00 85.97           C  
ANISOU 2095  CA  CYS A 265    10493  11565  10607   -427   -514    240       C  
ATOM   2096  C   CYS A 265      -4.347  -3.654 -19.051  1.00 93.79           C  
ANISOU 2096  C   CYS A 265    11477  12600  11559   -451   -538    259       C  
ATOM   2097  O   CYS A 265      -4.255  -4.632 -19.797  1.00111.28           O  
ANISOU 2097  O   CYS A 265    13715  14827  13739   -477   -553    231       O  
ATOM   2098  CB  CYS A 265      -4.944  -4.259 -16.691  1.00 90.58           C  
ANISOU 2098  CB  CYS A 265    11063  12136  11216   -435   -524    249       C  
ATOM   2099  SG  CYS A 265      -4.297  -4.918 -15.135  1.00 96.95           S  
ANISOU 2099  SG  CYS A 265    11889  12892  12055   -416   -501    213       S  
ATOM   2100  N   GLU A 266      -4.840  -2.475 -19.436  1.00 88.53           N  
ANISOU 2100  N   GLU A 266    10781  11958  10900   -443   -539    305       N  
ATOM   2101  CA  GLU A 266      -5.174  -2.200 -20.819  1.00 84.48           C  
ANISOU 2101  CA  GLU A 266    10260  11490  10351   -461   -559    327       C  
ATOM   2102  C   GLU A 266      -3.913  -2.142 -21.677  1.00 88.46           C  
ANISOU 2102  C   GLU A 266    10789  11998  10822   -456   -547    303       C  
ATOM   2103  O   GLU A 266      -3.824  -2.827 -22.697  1.00 90.63           O  
ANISOU 2103  O   GLU A 266    11083  12297  11055   -481   -564    284       O  
ATOM   2104  CB  GLU A 266      -5.991  -0.919 -20.920  1.00 89.51           C  
ANISOU 2104  CB  GLU A 266    10856  12148  11007   -449   -560    386       C  
ATOM   2105  CG  GLU A 266      -7.454  -1.141 -20.545  1.00103.24           C  
ANISOU 2105  CG  GLU A 266    12566  13897  12761   -465   -581    415       C  
ATOM   2106  CD  GLU A 266      -8.081   0.020 -19.782  1.00112.59           C  
ANISOU 2106  CD  GLU A 266    13715  15073  13990   -439   -566    463       C  
ATOM   2107  OE1 GLU A 266      -8.069   1.163 -20.291  1.00118.58           O  
ANISOU 2107  OE1 GLU A 266    14454  15850  14751   -424   -558    500       O  
ATOM   2108  OE2 GLU A 266      -8.610  -0.216 -18.670  1.00122.81           O1-
ANISOU 2108  OE2 GLU A 266    15002  16342  15318   -433   -561    463       O1-
ATOM   2109  N   ASN A 267      -2.914  -1.383 -21.237  1.00 95.45           N  
ANISOU 2109  N   ASN A 267    11678  12861  11728   -425   -518    300       N  
ATOM   2110  CA  ASN A 267      -1.716  -1.113 -22.068  1.00100.96           C  
ANISOU 2110  CA  ASN A 267    12395  13565  12399   -417   -504    285       C  
ATOM   2111  C   ASN A 267      -0.556  -2.121 -21.880  1.00 93.57           C  
ANISOU 2111  C   ASN A 267    11499  12602  11452   -417   -491    230       C  
ATOM   2112  O   ASN A 267       0.645  -1.777 -21.867  1.00 91.52           O  
ANISOU 2112  O   ASN A 267    11253  12328  11195   -396   -468    216       O  
ATOM   2113  CB  ASN A 267      -1.249   0.323 -21.826  1.00100.86           C  
ANISOU 2113  CB  ASN A 267    12362  13544  12414   -385   -479    315       C  
ATOM   2114  CG  ASN A 267      -2.266   1.357 -22.291  1.00103.08           C  
ANISOU 2114  CG  ASN A 267    12606  13857  12701   -385   -489    371       C  
ATOM   2115  ND2 ASN A 267      -1.766   2.467 -22.797  1.00119.24           N  
ANISOU 2115  ND2 ASN A 267    14643  15914  14750   -367   -474    396       N  
ATOM   2116  OD1 ASN A 267      -3.482   1.157 -22.207  1.00 87.13           O  
ANISOU 2116  OD1 ASN A 267    10568  11853  10686   -401   -511    394       O  
ATOM   2117  N   GLN A 268      -0.939  -3.384 -21.812  1.00 83.47           N  
ANISOU 2117  N   GLN A 268    10237  11319  10158   -441   -508    202       N  
ATOM   2118  CA  GLN A 268      -0.053  -4.450 -21.385  1.00 81.46           C  
ANISOU 2118  CA  GLN A 268    10017  11034   9901   -440   -495    153       C  
ATOM   2119  C   GLN A 268       0.985  -4.895 -22.436  1.00 77.88           C  
ANISOU 2119  C   GLN A 268     9595  10589   9407   -446   -489    123       C  
ATOM   2120  O   GLN A 268       2.018  -5.476 -22.102  1.00 65.84           O  
ANISOU 2120  O   GLN A 268     8096   9036   7884   -435   -470     87       O  
ATOM   2121  CB  GLN A 268      -0.938  -5.601 -20.930  1.00 83.45           C  
ANISOU 2121  CB  GLN A 268    10274  11277  10155   -464   -514    136       C  
ATOM   2122  CG  GLN A 268      -0.313  -6.979 -20.876  1.00 85.60           C  
ANISOU 2122  CG  GLN A 268    10584  11528  10413   -475   -510     86       C  
ATOM   2123  CD  GLN A 268      -1.169  -7.943 -20.080  1.00 86.69           C  
ANISOU 2123  CD  GLN A 268    10722  11650  10568   -492   -523     75       C  
ATOM   2124  NE2 GLN A 268      -2.316  -7.469 -19.602  1.00 82.93           N  
ANISOU 2124  NE2 GLN A 268    10213  11182  10115   -494   -536    110       N  
ATOM   2125  OE1 GLN A 268      -0.791  -9.092 -19.872  1.00 95.56           O  
ANISOU 2125  OE1 GLN A 268    11873  12751  11685   -500   -518     36       O  
ATOM   2126  N   ASP A 269       0.731  -4.639 -23.707  1.00 84.02           N  
ANISOU 2126  N   ASP A 269    10371  11405  10148   -461   -504    138       N  
ATOM   2127  CA  ASP A 269       1.745  -4.970 -24.709  1.00 92.38           C  
ANISOU 2127  CA  ASP A 269    11460  12473  11168   -464   -494    112       C  
ATOM   2128  C   ASP A 269       2.685  -3.792 -24.884  1.00 95.13           C  
ANISOU 2128  C   ASP A 269    11799  12821  11526   -434   -470    131       C  
ATOM   2129  O   ASP A 269       3.796  -3.957 -25.369  1.00 92.22           O  
ANISOU 2129  O   ASP A 269    11454  12447  11138   -426   -453    108       O  
ATOM   2130  CB  ASP A 269       1.101  -5.407 -26.023  1.00 93.18           C  
ANISOU 2130  CB  ASP A 269    11569  12615  11219   -498   -521    113       C  
ATOM   2131  CG  ASP A 269       0.267  -6.675 -25.853  1.00 92.64           C  
ANISOU 2131  CG  ASP A 269    11514  12543  11142   -530   -544     89       C  
ATOM   2132  OD1 ASP A 269       0.868  -7.780 -25.935  1.00 82.09           O  
ANISOU 2132  OD1 ASP A 269    10215  11188   9790   -539   -536     44       O  
ATOM   2133  OD2 ASP A 269      -0.973  -6.557 -25.607  1.00 89.44           O1-
ANISOU 2133  OD2 ASP A 269    11082  12152  10748   -545   -567    116       O1-
ATOM   2134  N   SER A 270       2.244  -2.617 -24.441  1.00 96.98           N  
ANISOU 2134  N   SER A 270    11999  13058  11791   -418   -468    172       N  
ATOM   2135  CA  SER A 270       3.100  -1.431 -24.395  1.00101.76           C  
ANISOU 2135  CA  SER A 270    12593  13658  12415   -388   -443    191       C  
ATOM   2136  C   SER A 270       3.940  -1.351 -23.119  1.00 91.62           C  
ANISOU 2136  C   SER A 270    11313  12329  11170   -362   -417    172       C  
ATOM   2137  O   SER A 270       4.699  -0.383 -22.935  1.00 91.56           O  
ANISOU 2137  O   SER A 270    11295  12311  11181   -338   -396    185       O  
ATOM   2138  CB  SER A 270       2.251  -0.156 -24.510  1.00106.61           C  
ANISOU 2138  CB  SER A 270    13169  14294  13046   -381   -449    245       C  
ATOM   2139  OG  SER A 270       1.851   0.081 -25.841  1.00116.14           O  
ANISOU 2139  OG  SER A 270    14370  15545  14214   -396   -466    267       O  
ATOM   2140  N   ILE A 271       3.808  -2.343 -22.237  1.00 82.05           N  
ANISOU 2140  N   ILE A 271    10113  11091   9971   -369   -420    144       N  
ATOM   2141  CA  ILE A 271       4.509  -2.306 -20.961  1.00 80.43           C  
ANISOU 2141  CA  ILE A 271     9910  10846   9803   -346   -398    128       C  
ATOM   2142  C   ILE A 271       5.375  -3.536 -20.716  1.00 78.75           C  
ANISOU 2142  C   ILE A 271     9731  10610   9581   -348   -389     81       C  
ATOM   2143  O   ILE A 271       6.592  -3.471 -20.815  1.00 85.76           O  
ANISOU 2143  O   ILE A 271    10633  11486  10467   -333   -368     65       O  
ATOM   2144  CB  ILE A 271       3.550  -2.140 -19.758  1.00 75.83           C  
ANISOU 2144  CB  ILE A 271     9307  10248   9258   -343   -404    143       C  
ATOM   2145  CG1 ILE A 271       2.783  -0.826 -19.826  1.00 75.23           C  
ANISOU 2145  CG1 ILE A 271     9197  10189   9200   -336   -407    191       C  
ATOM   2146  CG2 ILE A 271       4.346  -2.154 -18.452  1.00 75.98           C  
ANISOU 2146  CG2 ILE A 271     9330  10227   9311   -321   -382    124       C  
ATOM   2147  CD1 ILE A 271       1.774  -0.675 -18.698  1.00 80.32           C  
ANISOU 2147  CD1 ILE A 271     9820  10819   9879   -333   -412    209       C  
ATOM   2148  N   SER A 272       4.742  -4.640 -20.348  1.00 80.63           N  
ANISOU 2148  N   SER A 272     9980  10839   9816   -367   -403     62       N  
ATOM   2149  CA  SER A 272       5.451  -5.811 -19.879  1.00 83.43           C  
ANISOU 2149  CA  SER A 272    10363  11167  10171   -366   -392     20       C  
ATOM   2150  C   SER A 272       4.659  -7.061 -20.229  1.00 87.95           C  
ANISOU 2150  C   SER A 272    10952  11745  10720   -397   -413      0       C  
ATOM   2151  O   SER A 272       3.423  -7.057 -20.279  1.00 76.02           O  
ANISOU 2151  O   SER A 272     9425  10250   9209   -415   -436     19       O  
ATOM   2152  CB  SER A 272       5.701  -5.726 -18.372  1.00 83.16           C  
ANISOU 2152  CB  SER A 272    10320  11098  10180   -346   -378     16       C  
ATOM   2153  OG  SER A 272       6.211  -6.942 -17.838  1.00 86.47           O  
ANISOU 2153  OG  SER A 272    10764  11491  10600   -347   -370    -20       O  
ATOM   2154  N   SER A 273       5.400  -8.130 -20.479  1.00 91.76           N  
ANISOU 2154  N   SER A 273    11467  12214  11184   -402   -403    -37       N  
ATOM   2155  CA  SER A 273       4.815  -9.386 -20.885  1.00 89.53           C  
ANISOU 2155  CA  SER A 273    11206  11934  10878   -431   -419    -62       C  
ATOM   2156  C   SER A 273       4.066 -10.090 -19.745  1.00 87.34           C  
ANISOU 2156  C   SER A 273    10923  11634  10629   -438   -426    -69       C  
ATOM   2157  O   SER A 273       3.008 -10.669 -19.959  1.00 80.32           O  
ANISOU 2157  O   SER A 273    10033  10755   9729   -465   -449    -69       O  
ATOM   2158  CB  SER A 273       5.916 -10.294 -21.401  1.00 97.31           C  
ANISOU 2158  CB  SER A 273    12229  12906  11839   -431   -401   -101       C  
ATOM   2159  OG  SER A 273       6.512 -11.017 -20.341  1.00111.83           O  
ANISOU 2159  OG  SER A 273    14079  14707  13704   -417   -382   -124       O  
ATOM   2160  N   LYS A 274       4.603 -10.005 -18.531  1.00 89.73           N  
ANISOU 2160  N   LYS A 274    11220  11905  10967   -413   -408    -72       N  
ATOM   2161  CA  LYS A 274       4.162 -10.855 -17.418  1.00 92.75           C  
ANISOU 2161  CA  LYS A 274    11604  12261  11375   -415   -409    -85       C  
ATOM   2162  C   LYS A 274       2.982 -10.253 -16.619  1.00102.36           C  
ANISOU 2162  C   LYS A 274    12788  13482  12621   -415   -424    -53       C  
ATOM   2163  O   LYS A 274       2.755 -10.622 -15.462  1.00112.23           O  
ANISOU 2163  O   LYS A 274    14034  14708  13901   -407   -419    -56       O  
ATOM   2164  CB  LYS A 274       5.316 -11.113 -16.444  1.00 97.09           C  
ANISOU 2164  CB  LYS A 274    12164  12777  11948   -388   -382   -104       C  
ATOM   2165  CG  LYS A 274       6.728 -11.058 -17.021  1.00103.56           C  
ANISOU 2165  CG  LYS A 274    13004  13594  12752   -374   -360   -121       C  
ATOM   2166  CD  LYS A 274       7.342 -12.436 -17.165  1.00 98.90           C  
ANISOU 2166  CD  LYS A 274    12446  12983  12147   -380   -347   -159       C  
ATOM   2167  CE  LYS A 274       8.761 -12.323 -17.697  1.00 94.20           C  
ANISOU 2167  CE  LYS A 274    11869  12385  11539   -363   -323   -172       C  
ATOM   2168  NZ  LYS A 274       9.426 -13.642 -17.695  1.00 98.40           N1+
ANISOU 2168  NZ  LYS A 274    12432  12893  12063   -364   -306   -208       N1+
ATOM   2169  N   LEU A 275       2.235  -9.328 -17.218  1.00101.43           N  
ANISOU 2169  N   LEU A 275    12648  13395  12496   -422   -440    -20       N  
ATOM   2170  CA  LEU A 275       1.072  -8.733 -16.552  1.00101.41           C  
ANISOU 2170  CA  LEU A 275    12614  13397  12520   -422   -452     14       C  
ATOM   2171  C   LEU A 275      -0.216  -9.556 -16.745  1.00100.38           C  
ANISOU 2171  C   LEU A 275    12480  13278  12381   -454   -479     16       C  
ATOM   2172  O   LEU A 275      -1.227  -9.306 -16.095  1.00 93.52           O  
ANISOU 2172  O   LEU A 275    11587  12409  11537   -455   -489     40       O  
ATOM   2173  CB  LEU A 275       0.861  -7.316 -17.085  1.00113.09           C  
ANISOU 2173  CB  LEU A 275    14068  14903  13999   -413   -455     53       C  
ATOM   2174  CG  LEU A 275       1.974  -6.258 -16.869  1.00113.27           C  
ANISOU 2174  CG  LEU A 275    14087  14917  14035   -382   -430     59       C  
ATOM   2175  CD1 LEU A 275       1.962  -5.238 -18.002  1.00119.76           C  
ANISOU 2175  CD1 LEU A 275    14896  15771  14836   -383   -435     87       C  
ATOM   2176  CD2 LEU A 275       1.873  -5.517 -15.536  1.00114.14           C  
ANISOU 2176  CD2 LEU A 275    14176  15005  14188   -358   -417     77       C  
ATOM   2177  N   LYS A 276      -0.164 -10.534 -17.646  1.00107.09           N  
ANISOU 2177  N   LYS A 276    13355  14136  13197   -479   -489    -11       N  
ATOM   2178  CA  LYS A 276      -1.301 -11.394 -17.977  1.00101.28           C  
ANISOU 2178  CA  LYS A 276    12620  13412  12448   -514   -516    -14       C  
ATOM   2179  C   LYS A 276      -2.004 -11.878 -16.739  1.00 98.96           C  
ANISOU 2179  C   LYS A 276    12315  13095  12191   -513   -517    -11       C  
ATOM   2180  O   LYS A 276      -3.222 -11.793 -16.632  1.00 96.26           O  
ANISOU 2180  O   LYS A 276    11949  12766  11858   -528   -538     14       O  
ATOM   2181  CB  LYS A 276      -0.831 -12.605 -18.810  1.00102.01           C  
ANISOU 2181  CB  LYS A 276    12751  13502  12505   -537   -517    -56       C  
ATOM   2182  CG  LYS A 276       0.231 -13.495 -18.136  1.00102.71           C  
ANISOU 2182  CG  LYS A 276    12869  13551  12606   -522   -490    -95       C  
ATOM   2183  CD  LYS A 276       0.880 -14.536 -19.064  1.00104.34           C  
ANISOU 2183  CD  LYS A 276    13114  13754  12775   -540   -485   -136       C  
ATOM   2184  CE  LYS A 276       2.157 -14.026 -19.753  1.00105.79           C  
ANISOU 2184  CE  LYS A 276    13314  13943  12938   -521   -465   -144       C  
ATOM   2185  NZ  LYS A 276       3.217 -15.065 -19.938  1.00103.25           N1+
ANISOU 2185  NZ  LYS A 276    13031  13597  12603   -519   -442   -186       N1+
ATOM   2186  N   GLU A 277      -1.227 -12.368 -15.785  1.00102.19           N  
ANISOU 2186  N   GLU A 277    12739  13468  12621   -493   -494    -35       N  
ATOM   2187  CA  GLU A 277      -1.811 -13.139 -14.701  1.00111.83           C  
ANISOU 2187  CA  GLU A 277    13956  14663  13870   -495   -495    -41       C  
ATOM   2188  C   GLU A 277      -2.433 -12.239 -13.637  1.00109.13           C  
ANISOU 2188  C   GLU A 277    13582  14318  13566   -475   -493     -5       C  
ATOM   2189  O   GLU A 277      -3.490 -12.549 -13.084  1.00110.58           O  
ANISOU 2189  O   GLU A 277    13749  14498  13768   -485   -505      9       O  
ATOM   2190  CB  GLU A 277      -0.786 -14.141 -14.142  1.00107.81           C  
ANISOU 2190  CB  GLU A 277    13477  14119  13367   -484   -472    -80       C  
ATOM   2191  CG  GLU A 277      -0.718 -15.417 -14.982  1.00112.49           C  
ANISOU 2191  CG  GLU A 277    14102  14711  13930   -513   -478   -115       C  
ATOM   2192  CD  GLU A 277       0.690 -15.891 -15.324  1.00129.53           C  
ANISOU 2192  CD  GLU A 277    16293  16852  16071   -502   -454   -149       C  
ATOM   2193  OE1 GLU A 277       1.673 -15.203 -14.949  1.00143.25           O  
ANISOU 2193  OE1 GLU A 277    18027  18582  17820   -471   -434   -145       O  
ATOM   2194  OE2 GLU A 277       0.808 -16.962 -15.980  1.00124.52           O1-
ANISOU 2194  OE2 GLU A 277    15686  16212  15412   -524   -455   -180       O1-
ATOM   2195  N   CYS A 278      -1.808 -11.099 -13.394  1.00101.34           N  
ANISOU 2195  N   CYS A 278    12583  13331  12589   -447   -477     11       N  
ATOM   2196  CA  CYS A 278      -2.328 -10.165 -12.414  1.00100.85           C  
ANISOU 2196  CA  CYS A 278    12492  13264  12562   -427   -472     44       C  
ATOM   2197  C   CYS A 278      -3.636  -9.587 -12.872  1.00 93.28           C  
ANISOU 2197  C   CYS A 278    11505  12334  11603   -443   -494     82       C  
ATOM   2198  O   CYS A 278      -4.581  -9.465 -12.096  1.00 77.51           O  
ANISOU 2198  O   CYS A 278     9486  10332   9633   -441   -499    105       O  
ATOM   2199  CB  CYS A 278      -1.330  -9.042 -12.216  1.00107.14           C  
ANISOU 2199  CB  CYS A 278    13285  14056  13366   -397   -451     51       C  
ATOM   2200  SG  CYS A 278       0.218  -9.649 -11.549  1.00112.99           S  
ANISOU 2200  SG  CYS A 278    14056  14765  14112   -376   -424     11       S  
ATOM   2201  N   CYS A 279      -3.681  -9.279 -14.162  1.00 94.03           N  
ANISOU 2201  N   CYS A 279    11600  12461  11667   -459   -508     90       N  
ATOM   2202  CA  CYS A 279      -4.727  -8.450 -14.721  1.00 91.16           C  
ANISOU 2202  CA  CYS A 279    11206  12130  11301   -468   -527    132       C  
ATOM   2203  C   CYS A 279      -6.023  -9.177 -14.924  1.00 92.74           C  
ANISOU 2203  C   CYS A 279    11395  12344  11497   -500   -555    141       C  
ATOM   2204  O   CYS A 279      -6.998  -8.582 -15.382  1.00 98.87           O  
ANISOU 2204  O   CYS A 279    12144  13149  12272   -511   -573    179       O  
ATOM   2205  CB  CYS A 279      -4.251  -7.847 -16.030  1.00 88.51           C  
ANISOU 2205  CB  CYS A 279    10874  11824  10932   -473   -532    138       C  
ATOM   2206  SG  CYS A 279      -3.103  -6.510 -15.690  1.00 95.42           S  
ANISOU 2206  SG  CYS A 279    11745  12687  11823   -433   -501    147       S  
ATOM   2207  N   GLU A 280      -6.038 -10.460 -14.585  1.00 96.55           N  
ANISOU 2207  N   GLU A 280    11899  12807  11979   -515   -557    109       N  
ATOM   2208  CA  GLU A 280      -7.230 -11.277 -14.736  1.00 98.29           C  
ANISOU 2208  CA  GLU A 280    12111  13037  12197   -547   -583    114       C  
ATOM   2209  C   GLU A 280      -7.992 -11.271 -13.436  1.00 87.39           C  
ANISOU 2209  C   GLU A 280    10710  11637  10860   -535   -578    133       C  
ATOM   2210  O   GLU A 280      -9.169 -11.587 -13.414  1.00 85.07           O  
ANISOU 2210  O   GLU A 280    10396  11353  10572   -556   -599    153       O  
ATOM   2211  CB  GLU A 280      -6.863 -12.716 -15.145  1.00 99.45           C  
ANISOU 2211  CB  GLU A 280    12294  13173  12320   -573   -588     67       C  
ATOM   2212  CG  GLU A 280      -6.182 -12.800 -16.503  1.00100.07           C  
ANISOU 2212  CG  GLU A 280    12396  13274  12354   -588   -594     46       C  
ATOM   2213  CD  GLU A 280      -6.230 -14.166 -17.145  1.00 99.53           C  
ANISOU 2213  CD  GLU A 280    12357  13203  12256   -623   -607      8       C  
ATOM   2214  OE1 GLU A 280      -6.790 -15.098 -16.537  1.00113.04           O  
ANISOU 2214  OE1 GLU A 280    14071  14894  13984   -637   -612     -3       O  
ATOM   2215  OE2 GLU A 280      -5.738 -14.307 -18.280  1.00 95.16           O1-
ANISOU 2215  OE2 GLU A 280    11826  12668  11664   -638   -611    -10       O1-
ATOM   2216  N   LYS A 281      -7.311 -10.887 -12.361  1.00 84.00           N  
ANISOU 2216  N   LYS A 281    10281  11177  10456   -501   -551    129       N  
ATOM   2217  CA  LYS A 281      -7.839 -11.031 -11.026  1.00 85.07           C  
ANISOU 2217  CA  LYS A 281    10404  11289  10630   -487   -542    140       C  
ATOM   2218  C   LYS A 281      -8.645  -9.814 -10.606  1.00 88.40           C  
ANISOU 2218  C   LYS A 281    10789  11721  11077   -471   -540    188       C  
ATOM   2219  O   LYS A 281      -8.634  -8.785 -11.279  1.00 87.88           O  
ANISOU 2219  O   LYS A 281    10710  11679  11002   -466   -542    212       O  
ATOM   2220  CB  LYS A 281      -6.712 -11.280 -10.045  1.00 91.41           C  
ANISOU 2220  CB  LYS A 281    11228  12055  11447   -460   -513    111       C  
ATOM   2221  CG  LYS A 281      -5.938 -12.540 -10.371  1.00106.00           C  
ANISOU 2221  CG  LYS A 281    13111  13889  13274   -473   -511     65       C  
ATOM   2222  CD  LYS A 281      -4.914 -12.882  -9.302  1.00116.29           C  
ANISOU 2222  CD  LYS A 281    14433  15157  14595   -447   -484     39       C  
ATOM   2223  CE  LYS A 281      -3.714 -13.576  -9.933  1.00124.89           C  
ANISOU 2223  CE  LYS A 281    15556  16239  15658   -450   -475     -1       C  
ATOM   2224  NZ  LYS A 281      -2.862 -14.296  -8.941  1.00129.01           N1+
ANISOU 2224  NZ  LYS A 281    16097  16727  16195   -432   -453    -27       N1+
ATOM   2225  N   PRO A 282      -9.390  -9.947  -9.499  1.00 98.44           N  
ANISOU 2225  N   PRO A 282    12045  12975  12382   -462   -535    204       N  
ATOM   2226  CA  PRO A 282     -10.267  -8.883  -9.020  1.00 93.62           C  
ANISOU 2226  CA  PRO A 282    11401  12372  11799   -447   -532    251       C  
ATOM   2227  C   PRO A 282      -9.507  -7.638  -8.665  1.00 86.21           C  
ANISOU 2227  C   PRO A 282    10459  11425  10870   -413   -507    260       C  
ATOM   2228  O   PRO A 282      -8.285  -7.608  -8.718  1.00 78.59           O  
ANISOU 2228  O   PRO A 282     9519  10449   9894   -401   -492    231       O  
ATOM   2229  CB  PRO A 282     -10.910  -9.487  -7.758  1.00105.08           C  
ANISOU 2229  CB  PRO A 282    12846  13798  13283   -441   -525    253       C  
ATOM   2230  CG  PRO A 282     -10.901 -10.954  -8.004  1.00112.47           C  
ANISOU 2230  CG  PRO A 282    13803  14727  14204   -469   -540    219       C  
ATOM   2231  CD  PRO A 282      -9.620 -11.212  -8.765  1.00111.86           C  
ANISOU 2231  CD  PRO A 282    13757  14650  14094   -471   -536    181       C  
ATOM   2232  N   LEU A 283     -10.243  -6.630  -8.247  1.00 91.20           N  
ANISOU 2232  N   LEU A 283    11063  12062  11528   -398   -500    302       N  
ATOM   2233  CA  LEU A 283      -9.729  -5.278  -8.283  1.00 97.40           C  
ANISOU 2233  CA  LEU A 283    11840  12848  12318   -373   -481    319       C  
ATOM   2234  C   LEU A 283      -8.669  -4.982  -7.217  1.00 95.48           C  
ANISOU 2234  C   LEU A 283    11614  12571  12091   -343   -451    295       C  
ATOM   2235  O   LEU A 283      -7.796  -4.142  -7.464  1.00 87.25           O  
ANISOU 2235  O   LEU A 283    10579  11530  11044   -327   -437    292       O  
ATOM   2236  CB  LEU A 283     -10.903  -4.297  -8.198  1.00102.72           C  
ANISOU 2236  CB  LEU A 283    12477  13537  13016   -366   -482    373       C  
ATOM   2237  CG  LEU A 283     -10.881  -2.980  -8.969  1.00 96.52           C  
ANISOU 2237  CG  LEU A 283    11673  12773  12225   -356   -478    406       C  
ATOM   2238  CD1 LEU A 283     -10.049  -3.002 -10.230  1.00100.89           C  
ANISOU 2238  CD1 LEU A 283    12243  13348  12741   -370   -489    387       C  
ATOM   2239  CD2 LEU A 283     -12.310  -2.638  -9.349  1.00101.94           C  
ANISOU 2239  CD2 LEU A 283    12324  13487  12923   -368   -495    456       C  
ATOM   2240  N   LEU A 284      -8.740  -5.657  -6.059  1.00 97.52           N  
ANISOU 2240  N   LEU A 284    11881  12803  12368   -335   -442    280       N  
ATOM   2241  CA  LEU A 284      -7.692  -5.553  -5.022  1.00 94.67           C  
ANISOU 2241  CA  LEU A 284    11539  12412  12019   -310   -417    254       C  
ATOM   2242  C   LEU A 284      -6.490  -6.449  -5.342  1.00103.40           C  
ANISOU 2242  C   LEU A 284    12676  13510  13100   -317   -417    209       C  
ATOM   2243  O   LEU A 284      -5.328  -6.021  -5.194  1.00105.91           O  
ANISOU 2243  O   LEU A 284    13008  13818  13414   -300   -401    190       O  
ATOM   2244  CB  LEU A 284      -8.232  -5.906  -3.630  1.00 81.61           C  
ANISOU 2244  CB  LEU A 284     9881  10733  10394   -297   -405    258       C  
ATOM   2245  CG  LEU A 284      -9.158  -4.900  -2.963  1.00 77.58           C  
ANISOU 2245  CG  LEU A 284     9344  10221   9913   -280   -393    299       C  
ATOM   2246  CD1 LEU A 284      -9.536  -5.365  -1.566  1.00 72.79           C  
ANISOU 2246  CD1 LEU A 284     8738   9587   9331   -267   -380    296       C  
ATOM   2247  CD2 LEU A 284      -8.512  -3.525  -2.908  1.00 77.46           C  
ANISOU 2247  CD2 LEU A 284     9327  10202   9903   -258   -372    308       C  
ATOM   2248  N   GLU A 285      -6.786  -7.680  -5.771  1.00107.45           N  
ANISOU 2248  N   GLU A 285    13200  14029  13599   -341   -436    192       N  
ATOM   2249  CA  GLU A 285      -5.762  -8.668  -6.131  1.00116.33           C  
ANISOU 2249  CA  GLU A 285    14354  15145  14701   -350   -436    149       C  
ATOM   2250  C   GLU A 285      -4.860  -8.096  -7.206  1.00104.84           C  
ANISOU 2250  C   GLU A 285    12908  13706  13219   -351   -436    141       C  
ATOM   2251  O   GLU A 285      -3.637  -8.148  -7.107  1.00101.62           O  
ANISOU 2251  O   GLU A 285    12521  13286  12804   -338   -421    115       O  
ATOM   2252  CB  GLU A 285      -6.404  -9.967  -6.659  1.00137.81           C  
ANISOU 2252  CB  GLU A 285    17081  17872  17407   -382   -458    137       C  
ATOM   2253  CG  GLU A 285      -6.884 -10.963  -5.606  1.00152.40           C  
ANISOU 2253  CG  GLU A 285    18931  19696  19276   -383   -456    129       C  
ATOM   2254  CD  GLU A 285      -8.248 -10.610  -5.028  1.00184.12           C  
ANISOU 2254  CD  GLU A 285    22919  23718  23321   -382   -461    167       C  
ATOM   2255  OE1 GLU A 285      -8.439  -9.450  -4.587  1.00213.18           O  
ANISOU 2255  OE1 GLU A 285    26582  27400  27019   -361   -450    195       O  
ATOM   2256  OE2 GLU A 285      -9.135 -11.497  -5.010  1.00197.59           O1-
ANISOU 2256  OE2 GLU A 285    24619  25424  25031   -403   -476    170       O1-
ATOM   2257  N   LYS A 286      -5.510  -7.582  -8.243  1.00 97.71           N  
ANISOU 2257  N   LYS A 286    11989  12833  12303   -366   -453    167       N  
ATOM   2258  CA  LYS A 286      -4.885  -6.868  -9.338  1.00 85.67           C  
ANISOU 2258  CA  LYS A 286    10467  11329  10755   -366   -454    169       C  
ATOM   2259  C   LYS A 286      -3.726  -6.014  -8.839  1.00 82.57           C  
ANISOU 2259  C   LYS A 286    10081  10919  10371   -337   -428    162       C  
ATOM   2260  O   LYS A 286      -2.580  -6.268  -9.174  1.00 81.70           O  
ANISOU 2260  O   LYS A 286     9993  10805  10244   -334   -420    133       O  
ATOM   2261  CB  LYS A 286      -5.933  -5.971  -9.988  1.00 79.33           C  
ANISOU 2261  CB  LYS A 286     9635  10556   9953   -374   -468    213       C  
ATOM   2262  CG  LYS A 286      -5.999  -6.013 -11.484  1.00 82.97           C  
ANISOU 2262  CG  LYS A 286    10096  11050  10377   -397   -488    217       C  
ATOM   2263  CD  LYS A 286      -7.006  -4.985 -11.951  1.00 88.58           C  
ANISOU 2263  CD  LYS A 286    10774  11789  11095   -399   -498    266       C  
ATOM   2264  CE  LYS A 286      -7.499  -5.261 -13.360  1.00103.72           C  
ANISOU 2264  CE  LYS A 286    12688  13745  12977   -430   -527    275       C  
ATOM   2265  NZ  LYS A 286      -8.027  -4.032 -14.029  1.00119.59           N1+
ANISOU 2265  NZ  LYS A 286    14668  15784  14986   -426   -531    321       N1+
ATOM   2266  N   SER A 287      -4.022  -5.022  -8.009  1.00 85.80           N  
ANISOU 2266  N   SER A 287    10472  11319  10809   -316   -414    187       N  
ATOM   2267  CA  SER A 287      -3.034  -3.995  -7.682  1.00 90.89           C  
ANISOU 2267  CA  SER A 287    11119  11953  11463   -291   -391    185       C  
ATOM   2268  C   SER A 287      -1.905  -4.540  -6.840  1.00 92.01           C  
ANISOU 2268  C   SER A 287    11283  12067  11607   -278   -375    149       C  
ATOM   2269  O   SER A 287      -0.746  -4.238  -7.093  1.00 88.37           O  
ANISOU 2269  O   SER A 287    10835  11603  11137   -269   -364    132       O  
ATOM   2270  CB  SER A 287      -3.670  -2.803  -6.981  1.00 98.60           C  
ANISOU 2270  CB  SER A 287    12071  12924  12469   -273   -378    220       C  
ATOM   2271  OG  SER A 287      -3.935  -1.758  -7.909  1.00117.05           O  
ANISOU 2271  OG  SER A 287    14390  15284  14800   -273   -381    251       O  
ATOM   2272  N   HIS A 288      -2.241  -5.352  -5.848  1.00 92.05           N  
ANISOU 2272  N   HIS A 288    11293  12054  11627   -277   -374    138       N  
ATOM   2273  CA  HIS A 288      -1.228  -6.038  -5.062  1.00 93.16           C  
ANISOU 2273  CA  HIS A 288    11455  12171  11769   -266   -361    105       C  
ATOM   2274  C   HIS A 288      -0.280  -6.844  -5.948  1.00 95.27           C  
ANISOU 2274  C   HIS A 288    11746  12444  12009   -278   -365     74       C  
ATOM   2275  O   HIS A 288       0.934  -6.878  -5.713  1.00 92.68           O  
ANISOU 2275  O   HIS A 288    11433  12104  11678   -265   -351     52       O  
ATOM   2276  CB  HIS A 288      -1.893  -6.989  -4.084  1.00 94.17           C  
ANISOU 2276  CB  HIS A 288    11584  12283  11914   -268   -363    100       C  
ATOM   2277  CG  HIS A 288      -0.921  -7.820  -3.319  1.00 95.54           C  
ANISOU 2277  CG  HIS A 288    11779  12434  12088   -259   -351     67       C  
ATOM   2278  CD2 HIS A 288      -0.481  -9.082  -3.516  1.00101.95           C  
ANISOU 2278  CD2 HIS A 288    12610  13239  12886   -269   -354     39       C  
ATOM   2279  ND1 HIS A 288      -0.253  -7.352  -2.212  1.00 93.27           N  
ANISOU 2279  ND1 HIS A 288    11494  12129  11817   -235   -332     62       N  
ATOM   2280  CE1 HIS A 288       0.550  -8.294  -1.751  1.00 96.87           C  
ANISOU 2280  CE1 HIS A 288    11967  12570  12269   -231   -325     34       C  
ATOM   2281  NE2 HIS A 288       0.439  -9.350  -2.531  1.00102.37           N  
ANISOU 2281  NE2 HIS A 288    12676  13272  12949   -251   -337     20       N  
ATOM   2282  N   CYS A 289      -0.857  -7.487  -6.966  1.00 97.94           N  
ANISOU 2282  N   CYS A 289    12086  12799  12326   -302   -385     74       N  
ATOM   2283  CA  CYS A 289      -0.124  -8.354  -7.878  1.00 95.61           C  
ANISOU 2283  CA  CYS A 289    11815  12509  12002   -316   -389     44       C  
ATOM   2284  C   CYS A 289       0.843  -7.564  -8.736  1.00 85.40           C  
ANISOU 2284  C   CYS A 289    10526  11229  10692   -309   -382     43       C  
ATOM   2285  O   CYS A 289       2.035  -7.896  -8.790  1.00 84.81           O  
ANISOU 2285  O   CYS A 289    10471  11144  10608   -301   -369     17       O  
ATOM   2286  CB  CYS A 289      -1.087  -9.122  -8.796  1.00101.29           C  
ANISOU 2286  CB  CYS A 289    12535  13247  12703   -347   -413     46       C  
ATOM   2287  SG  CYS A 289      -0.340 -10.471  -9.746  1.00109.67           S  
ANISOU 2287  SG  CYS A 289    13631  14308  13731   -367   -417      5       S  
ATOM   2288  N   ILE A 290       0.347  -6.523  -9.402  1.00 76.68           N  
ANISOU 2288  N   ILE A 290     9403  10147   9584   -312   -389     73       N  
ATOM   2289  CA  ILE A 290       1.216  -5.745 -10.280  1.00 79.29           C  
ANISOU 2289  CA  ILE A 290     9738  10491   9899   -305   -382     74       C  
ATOM   2290  C   ILE A 290       2.271  -4.992  -9.428  1.00 87.42           C  
ANISOU 2290  C   ILE A 290    10767  11500  10948   -278   -358     69       C  
ATOM   2291  O   ILE A 290       3.363  -4.632  -9.903  1.00 78.80           O  
ANISOU 2291  O   ILE A 290     9685  10411   9845   -270   -347     59       O  
ATOM   2292  CB  ILE A 290       0.444  -4.721 -11.140  1.00 67.96           C  
ANISOU 2292  CB  ILE A 290     8280   9085   8458   -312   -393    111       C  
ATOM   2293  CG1 ILE A 290      -0.819  -5.304 -11.756  1.00 56.62           C  
ANISOU 2293  CG1 ILE A 290     6835   7669   7008   -339   -419    123       C  
ATOM   2294  CG2 ILE A 290       1.338  -4.208 -12.250  1.00 71.74           C  
ANISOU 2294  CG2 ILE A 290     8767   9580   8913   -310   -388    108       C  
ATOM   2295  CD1 ILE A 290      -1.935  -4.294 -11.778  1.00 53.14           C  
ANISOU 2295  CD1 ILE A 290     6363   7244   6583   -337   -426    168       C  
ATOM   2296  N   ALA A 291       1.937  -4.765  -8.157  1.00 90.82           N  
ANISOU 2296  N   ALA A 291    11189  11912  11408   -265   -350     76       N  
ATOM   2297  CA  ALA A 291       2.865  -4.156  -7.228  1.00 83.28           C  
ANISOU 2297  CA  ALA A 291    10235  10937  10471   -242   -329     69       C  
ATOM   2298  C   ALA A 291       4.053  -5.061  -7.088  1.00 75.26           C  
ANISOU 2298  C   ALA A 291     9242   9908   9444   -238   -321     34       C  
ATOM   2299  O   ALA A 291       5.134  -4.582  -6.821  1.00 88.06           O  
ANISOU 2299  O   ALA A 291    10868  11521  11070   -223   -306     25       O  
ATOM   2300  CB  ALA A 291       2.198  -3.945  -5.869  1.00 87.24           C  
ANISOU 2300  CB  ALA A 291    10724  11420  11001   -231   -323     80       C  
ATOM   2301  N   GLU A 292       3.846  -6.366  -7.272  1.00 76.53           N  
ANISOU 2301  N   GLU A 292     9418  10067   9593   -253   -330     15       N  
ATOM   2302  CA  GLU A 292       4.857  -7.384  -7.004  1.00 81.56           C  
ANISOU 2302  CA  GLU A 292    10077  10689  10224   -249   -321    -17       C  
ATOM   2303  C   GLU A 292       5.300  -8.186  -8.246  1.00 82.88           C  
ANISOU 2303  C   GLU A 292    10264  10866  10360   -264   -326    -36       C  
ATOM   2304  O   GLU A 292       6.010  -9.193  -8.118  1.00 82.68           O  
ANISOU 2304  O   GLU A 292    10259  10828  10329   -263   -319    -62       O  
ATOM   2305  CB  GLU A 292       4.321  -8.349  -5.946  1.00 85.44           C  
ANISOU 2305  CB  GLU A 292    10571  11162  10730   -249   -323    -25       C  
ATOM   2306  CG  GLU A 292       4.375  -7.828  -4.518  1.00 96.17           C  
ANISOU 2306  CG  GLU A 292    11919  12504  12116   -229   -311    -18       C  
ATOM   2307  CD  GLU A 292       3.761  -8.795  -3.516  1.00114.16           C  
ANISOU 2307  CD  GLU A 292    14200  14766  14409   -230   -312    -23       C  
ATOM   2308  OE1 GLU A 292       3.393  -9.911  -3.935  1.00126.73           O  
ANISOU 2308  OE1 GLU A 292    15802  16358  15990   -246   -322    -35       O  
ATOM   2309  OE2 GLU A 292       3.651  -8.449  -2.318  1.00126.27           O1-
ANISOU 2309  OE2 GLU A 292    15726  16287  15964   -215   -304    -16       O1-
ATOM   2310  N   VAL A 293       4.894  -7.759  -9.438  1.00 81.52           N  
ANISOU 2310  N   VAL A 293    10088  10719  10169   -278   -338    -23       N  
ATOM   2311  CA  VAL A 293       5.276  -8.452 -10.688  1.00 86.00           C  
ANISOU 2311  CA  VAL A 293    10675  11298  10703   -294   -343    -41       C  
ATOM   2312  C   VAL A 293       6.791  -8.675 -10.811  1.00 83.47           C  
ANISOU 2312  C   VAL A 293    10373  10967  10375   -280   -323    -64       C  
ATOM   2313  O   VAL A 293       7.591  -7.790 -10.485  1.00 82.26           O  
ANISOU 2313  O   VAL A 293    10212  10810  10233   -261   -310    -58       O  
ATOM   2314  CB  VAL A 293       4.769  -7.684 -11.952  1.00100.34           C  
ANISOU 2314  CB  VAL A 293    12481  13145  12498   -307   -356    -19       C  
ATOM   2315  CG1 VAL A 293       5.465  -6.323 -12.135  1.00101.65           C  
ANISOU 2315  CG1 VAL A 293    12634  13318  12670   -288   -344     -2       C  
ATOM   2316  CG2 VAL A 293       4.928  -8.534 -13.211  1.00105.41           C  
ANISOU 2316  CG2 VAL A 293    13145  13801  13104   -328   -365    -39       C  
ATOM   2317  N   GLU A 294       7.187  -9.852 -11.286  1.00 79.81           N  
ANISOU 2317  N   GLU A 294     9934  10499   9893   -290   -321    -91       N  
ATOM   2318  CA  GLU A 294       8.611 -10.143 -11.431  1.00 82.05           C  
ANISOU 2318  CA  GLU A 294    10234  10771  10169   -276   -301   -112       C  
ATOM   2319  C   GLU A 294       9.175  -9.448 -12.638  1.00 83.55           C  
ANISOU 2319  C   GLU A 294    10428  10982  10337   -277   -298   -106       C  
ATOM   2320  O   GLU A 294       8.456  -9.146 -13.589  1.00 77.45           O  
ANISOU 2320  O   GLU A 294     9651  10232   9544   -293   -314    -94       O  
ATOM   2321  CB  GLU A 294       8.883 -11.640 -11.515  1.00 88.82           C  
ANISOU 2321  CB  GLU A 294    11119  11613  11016   -284   -296   -142       C  
ATOM   2322  CG  GLU A 294       8.209 -12.366 -12.669  1.00103.02           C  
ANISOU 2322  CG  GLU A 294    12933  13425  12784   -312   -310   -153       C  
ATOM   2323  CD  GLU A 294       7.618 -13.710 -12.234  1.00117.74           C  
ANISOU 2323  CD  GLU A 294    14811  15272  14653   -326   -315   -171       C  
ATOM   2324  OE1 GLU A 294       8.339 -14.476 -11.560  1.00114.27           O  
ANISOU 2324  OE1 GLU A 294    14384  14808  14226   -314   -297   -189       O  
ATOM   2325  OE2 GLU A 294       6.420 -13.972 -12.520  1.00127.27           O1-
ANISOU 2325  OE2 GLU A 294    16014  16489  15854   -350   -335   -165       O1-
ATOM   2326  N   ASN A 295      10.477  -9.203 -12.591  1.00 96.81           N  
ANISOU 2326  N   ASN A 295    12112  12654  12018   -258   -279   -114       N  
ATOM   2327  CA  ASN A 295      11.137  -8.412 -13.618  1.00103.50           C  
ANISOU 2327  CA  ASN A 295    12959  13519  12849   -254   -273   -106       C  
ATOM   2328  C   ASN A 295      11.042  -9.077 -14.978  1.00 96.55           C  
ANISOU 2328  C   ASN A 295    12100  12653  11931   -273   -278   -119       C  
ATOM   2329  O   ASN A 295      11.524 -10.200 -15.177  1.00 74.10           O  
ANISOU 2329  O   ASN A 295     9281   9798   9075   -276   -269   -145       O  
ATOM   2330  CB  ASN A 295      12.598  -8.143 -13.249  1.00111.34           C  
ANISOU 2330  CB  ASN A 295    13954  14498  13852   -231   -250   -113       C  
ATOM   2331  CG  ASN A 295      12.731  -7.154 -12.116  1.00108.53           C  
ANISOU 2331  CG  ASN A 295    13575  14134  13529   -215   -246    -96       C  
ATOM   2332  ND2 ASN A 295      13.939  -7.004 -11.598  1.00102.09           N  
ANISOU 2332  ND2 ASN A 295    12759  13305  12725   -197   -228   -103       N  
ATOM   2333  OD1 ASN A 295      11.749  -6.538 -11.705  1.00116.60           O  
ANISOU 2333  OD1 ASN A 295    14579  15159  14563   -219   -258    -78       O  
ATOM   2334  N   ASP A 296      10.422  -8.338 -15.897  1.00104.93           N  
ANISOU 2334  N   ASP A 296    13151  13741  12975   -284   -292    -99       N  
ATOM   2335  CA  ASP A 296      10.104  -8.805 -17.232  1.00105.25           C  
ANISOU 2335  CA  ASP A 296    13209  13803  12978   -305   -302   -107       C  
ATOM   2336  C   ASP A 296      11.367  -9.076 -18.026  1.00106.42           C  
ANISOU 2336  C   ASP A 296    13379  13950  13104   -297   -282   -125       C  
ATOM   2337  O   ASP A 296      12.458  -8.582 -17.721  1.00 98.80           O  
ANISOU 2337  O   ASP A 296    12411  12976  12154   -275   -262   -123       O  
ATOM   2338  CB  ASP A 296       9.241  -7.762 -17.966  1.00103.33           C  
ANISOU 2338  CB  ASP A 296    12946  13591  12724   -315   -319    -75       C  
ATOM   2339  CG  ASP A 296       8.611  -8.294 -19.238  1.00 98.58           C  
ANISOU 2339  CG  ASP A 296    12359  13015  12083   -342   -337    -81       C  
ATOM   2340  OD1 ASP A 296       8.623  -9.528 -19.448  1.00 97.57           O  
ANISOU 2340  OD1 ASP A 296    12257  12878  11937   -357   -337   -110       O  
ATOM   2341  OD2 ASP A 296       8.096  -7.469 -20.029  1.00 87.53           O1-
ANISOU 2341  OD2 ASP A 296    10945  11644  10668   -350   -349    -55       O1-
ATOM   2342  N   GLU A 297      11.193  -9.882 -19.055  1.00109.91           N  
ANISOU 2342  N   GLU A 297    13846  14404  13512   -317   -287   -142       N  
ATOM   2343  CA  GLU A 297      12.256 -10.172 -19.970  1.00105.31           C  
ANISOU 2343  CA  GLU A 297    13286  13823  12903   -312   -269   -159       C  
ATOM   2344  C   GLU A 297      12.767  -8.868 -20.532  1.00 94.60           C  
ANISOU 2344  C   GLU A 297    11913  12486  11544   -298   -263   -134       C  
ATOM   2345  O   GLU A 297      11.981  -8.046 -20.998  1.00101.40           O  
ANISOU 2345  O   GLU A 297    12757  13372  12398   -307   -280   -108       O  
ATOM   2346  CB  GLU A 297      11.720 -11.051 -21.097  1.00111.94           C  
ANISOU 2346  CB  GLU A 297    14152  14677  13702   -340   -280   -177       C  
ATOM   2347  CG  GLU A 297      11.184 -12.394 -20.619  1.00110.19           C  
ANISOU 2347  CG  GLU A 297    13949  14436  13484   -357   -285   -204       C  
ATOM   2348  CD  GLU A 297      12.237 -13.241 -19.910  1.00110.28           C  
ANISOU 2348  CD  GLU A 297    13977  14412  13512   -338   -258   -228       C  
ATOM   2349  OE1 GLU A 297      13.462 -12.978 -20.065  1.00101.94           O  
ANISOU 2349  OE1 GLU A 297    12925  13350  12456   -316   -235   -230       O  
ATOM   2350  OE2 GLU A 297      11.826 -14.193 -19.202  1.00106.39           O1-
ANISOU 2350  OE2 GLU A 297    13492  13898  13033   -346   -261   -244       O1-
ATOM   2351  N   MET A 298      14.076  -8.669 -20.440  1.00 92.73           N  
ANISOU 2351  N   MET A 298    11681  12237  11316   -276   -238   -138       N  
ATOM   2352  CA  MET A 298      14.740  -7.504 -21.020  1.00 96.85           C  
ANISOU 2352  CA  MET A 298    12190  12775  11835   -262   -228   -117       C  
ATOM   2353  C   MET A 298      14.939  -7.743 -22.505  1.00 96.00           C  
ANISOU 2353  C   MET A 298    12104  12689  11684   -272   -225   -123       C  
ATOM   2354  O   MET A 298      15.318  -8.848 -22.890  1.00114.21           O  
ANISOU 2354  O   MET A 298    14440  14986  13969   -278   -215   -152       O  
ATOM   2355  CB  MET A 298      16.104  -7.313 -20.347  1.00102.35           C  
ANISOU 2355  CB  MET A 298    12882  13448  12556   -235   -202   -121       C  
ATOM   2356  CG  MET A 298      16.991  -6.201 -20.909  1.00101.81           C  
ANISOU 2356  CG  MET A 298    12802  13393  12488   -219   -187   -101       C  
ATOM   2357  SD  MET A 298      18.733  -6.436 -20.493  1.00 97.49           S  
ANISOU 2357  SD  MET A 298    12262  12822  11958   -193   -155   -114       S  
ATOM   2358  CE  MET A 298      18.951  -8.170 -20.903  1.00103.04           C  
ANISOU 2358  CE  MET A 298    13003  13512  12634   -202   -146   -151       C  
ATOM   2359  N   PRO A 299      14.689  -6.720 -23.344  1.00 94.41           N  
ANISOU 2359  N   PRO A 299    11888  12516  11467   -274   -232    -97       N  
ATOM   2360  CA  PRO A 299      15.051  -6.776 -24.767  1.00101.54           C  
ANISOU 2360  CA  PRO A 299    12810  13442  12329   -280   -226   -100       C  
ATOM   2361  C   PRO A 299      16.496  -7.273 -24.964  1.00106.47           C  
ANISOU 2361  C   PRO A 299    13457  14049  12948   -263   -195   -121       C  
ATOM   2362  O   PRO A 299      17.387  -6.911 -24.197  1.00103.95           O  
ANISOU 2362  O   PRO A 299    13125  13710  12661   -240   -178   -117       O  
ATOM   2363  CB  PRO A 299      14.911  -5.318 -25.227  1.00 99.91           C  
ANISOU 2363  CB  PRO A 299    12576  13260  12124   -273   -231    -62       C  
ATOM   2364  CG  PRO A 299      13.959  -4.683 -24.271  1.00 99.35           C  
ANISOU 2364  CG  PRO A 299    12475  13186  12086   -274   -248    -40       C  
ATOM   2365  CD  PRO A 299      13.986  -5.472 -22.991  1.00 98.14           C  
ANISOU 2365  CD  PRO A 299    12327  13001  11961   -271   -246    -62       C  
ATOM   2366  N   ALA A 300      16.738  -8.076 -25.991  1.00105.55           N  
ANISOU 2366  N   ALA A 300    13372  13940  12793   -273   -188   -143       N  
ATOM   2367  CA  ALA A 300      17.954  -8.876 -26.014  1.00119.16           C  
ANISOU 2367  CA  ALA A 300    15121  15641  14515   -259   -159   -168       C  
ATOM   2368  C   ALA A 300      19.257  -8.074 -26.216  1.00133.39           C  
ANISOU 2368  C   ALA A 300    16913  17443  16328   -232   -132   -153       C  
ATOM   2369  O   ALA A 300      20.111  -8.011 -25.320  1.00128.77           O  
ANISOU 2369  O   ALA A 300    16317  16833  15776   -211   -116   -153       O  
ATOM   2370  CB  ALA A 300      17.825  -9.978 -27.060  1.00118.91           C  
ANISOU 2370  CB  ALA A 300    15127  15615  14437   -278   -156   -197       C  
ATOM   2371  N   ASP A 301      19.373  -7.438 -27.380  1.00141.90           N  
ANISOU 2371  N   ASP A 301    17992  18547  17376   -233   -130   -138       N  
ATOM   2372  CA  ASP A 301      20.665  -7.064 -27.958  1.00134.36           C  
ANISOU 2372  CA  ASP A 301    17041  17593  16417   -211   -102   -132       C  
ATOM   2373  C   ASP A 301      20.807  -5.554 -28.098  1.00115.25           C  
ANISOU 2373  C   ASP A 301    14588  15191  14012   -198   -103    -94       C  
ATOM   2374  O   ASP A 301      20.754  -4.999 -29.193  1.00113.86           O  
ANISOU 2374  O   ASP A 301    14412  15041  13807   -201   -103    -78       O  
ATOM   2375  CB  ASP A 301      20.735  -7.752 -29.328  1.00142.78           C  
ANISOU 2375  CB  ASP A 301    18142  18676  17431   -223    -94   -150       C  
ATOM   2376  CG  ASP A 301      22.111  -7.796 -29.903  1.00147.56           C  
ANISOU 2376  CG  ASP A 301    18762  19276  18029   -202    -59   -153       C  
ATOM   2377  OD1 ASP A 301      23.096  -7.582 -29.163  1.00176.80           O  
ANISOU 2377  OD1 ASP A 301    22451  22957  21767   -178    -39   -148       O  
ATOM   2378  OD2 ASP A 301      22.188  -8.076 -31.110  1.00153.97           O1-
ANISOU 2378  OD2 ASP A 301    19599  20106  18797   -209    -52   -161       O1-
ATOM   2379  N   LEU A 302      20.990  -4.886 -26.970  1.00103.23           N  
ANISOU 2379  N   LEU A 302    13037  13652  12534   -185   -103    -79       N  
ATOM   2380  CA  LEU A 302      20.812  -3.422 -26.882  1.00 99.75           C  
ANISOU 2380  CA  LEU A 302    12562  13224  12114   -177   -109    -43       C  
ATOM   2381  C   LEU A 302      22.143  -2.701 -27.030  1.00 88.62           C  
ANISOU 2381  C   LEU A 302    11142  11810  10720   -153    -82    -29       C  
ATOM   2382  O   LEU A 302      23.171  -3.254 -26.667  1.00 85.17           O  
ANISOU 2382  O   LEU A 302    10714  11351  10294   -140    -62    -46       O  
ATOM   2383  CB  LEU A 302      20.181  -3.063 -25.530  1.00102.23           C  
ANISOU 2383  CB  LEU A 302    12851  13522  12468   -178   -125    -36       C  
ATOM   2384  CG  LEU A 302      18.920  -3.855 -25.109  1.00102.74           C  
ANISOU 2384  CG  LEU A 302    12923  13585  12526   -200   -150    -50       C  
ATOM   2385  CD1 LEU A 302      19.007  -4.231 -23.623  1.00104.78           C  
ANISOU 2385  CD1 LEU A 302    13175  13814  12823   -193   -150    -63       C  
ATOM   2386  CD2 LEU A 302      17.631  -3.096 -25.445  1.00102.97           C  
ANISOU 2386  CD2 LEU A 302    12935  13641  12548   -215   -176    -24       C  
ATOM   2387  N   PRO A 303      22.142  -1.459 -27.544  1.00 85.63           N  
ANISOU 2387  N   PRO A 303    10741  11450  10343   -147    -82      2       N  
ATOM   2388  CA  PRO A 303      23.457  -0.833 -27.714  1.00 87.74           C  
ANISOU 2388  CA  PRO A 303    11000  11712  10626   -125    -55     15       C  
ATOM   2389  C   PRO A 303      24.079  -0.570 -26.364  1.00 85.56           C  
ANISOU 2389  C   PRO A 303    10704  11406  10398   -112    -48     14       C  
ATOM   2390  O   PRO A 303      23.416  -0.727 -25.331  1.00 85.53           O  
ANISOU 2390  O   PRO A 303    10693  11390  10416   -120    -64      7       O  
ATOM   2391  CB  PRO A 303      23.169   0.492 -28.457  1.00 84.52           C  
ANISOU 2391  CB  PRO A 303    10570  11328  10214   -123    -58     51       C  
ATOM   2392  CG  PRO A 303      21.749   0.786 -28.189  1.00 89.64           C  
ANISOU 2392  CG  PRO A 303    11206  11988  10863   -140    -87     62       C  
ATOM   2393  CD  PRO A 303      21.044  -0.523 -27.831  1.00 93.10           C  
ANISOU 2393  CD  PRO A 303    11667  12419  11287   -158   -103     31       C  
ATOM   2394  N   SER A 304      25.358  -0.225 -26.384  1.00 78.75           N  
ANISOU 2394  N   SER A 304     9836  10535   9552    -94    -23     20       N  
ATOM   2395  CA  SER A 304      26.026   0.269 -25.219  1.00 69.97           C  
ANISOU 2395  CA  SER A 304     8700   9400   8484    -81    -17     25       C  
ATOM   2396  C   SER A 304      25.575   1.721 -25.098  1.00 79.88           C  
ANISOU 2396  C   SER A 304     9926  10663   9760    -82    -25     56       C  
ATOM   2397  O   SER A 304      25.131   2.353 -26.090  1.00 74.58           O  
ANISOU 2397  O   SER A 304     9252  10016   9070    -85    -28     76       O  
ATOM   2398  CB  SER A 304      27.527   0.159 -25.407  1.00 67.51           C  
ANISOU 2398  CB  SER A 304     8391   9079   8180    -63     12     24       C  
ATOM   2399  OG  SER A 304      28.186   0.459 -24.210  1.00 72.85           O  
ANISOU 2399  OG  SER A 304     9048   9735   8898    -54     16     24       O  
ATOM   2400  N   LEU A 305      25.675   2.245 -23.878  1.00 91.27           N  
ANISOU 2400  N   LEU A 305    11347  12087  11243    -78    -29     59       N  
ATOM   2401  CA  LEU A 305      25.190   3.603 -23.564  1.00 96.92           C  
ANISOU 2401  CA  LEU A 305    12036  12805  11985    -79    -36     86       C  
ATOM   2402  C   LEU A 305      26.156   4.698 -24.017  1.00 99.14           C  
ANISOU 2402  C   LEU A 305    12299  13089  12282    -65    -15    110       C  
ATOM   2403  O   LEU A 305      25.750   5.745 -24.534  1.00 94.76           O  
ANISOU 2403  O   LEU A 305    11729  12547  11729    -65    -16    137       O  
ATOM   2404  CB  LEU A 305      25.008   3.767 -22.064  1.00 93.01           C  
ANISOU 2404  CB  LEU A 305    11526  12287  11526    -80    -44     79       C  
ATOM   2405  CG  LEU A 305      24.323   2.678 -21.264  1.00 91.74           C  
ANISOU 2405  CG  LEU A 305    11379  12115  11361    -90    -61     54       C  
ATOM   2406  CD1 LEU A 305      24.732   2.821 -19.809  1.00 95.47           C  
ANISOU 2406  CD1 LEU A 305    11839  12564  11872    -85    -60     46       C  
ATOM   2407  CD2 LEU A 305      22.818   2.765 -21.433  1.00 93.93           C  
ANISOU 2407  CD2 LEU A 305    11657  12407  11627   -104    -83     61       C  
ATOM   2408  N   ALA A 306      27.438   4.455 -23.777  1.00 98.34           N  
ANISOU 2408  N   ALA A 306    12198  12973  12192    -53      3    101       N  
ATOM   2409  CA  ALA A 306      28.476   5.439 -24.045  1.00105.73           C  
ANISOU 2409  CA  ALA A 306    13115  13908  13149    -41     23    122       C  
ATOM   2410  C   ALA A 306      28.187   6.204 -25.347  1.00102.41           C  
ANISOU 2410  C   ALA A 306    12691  13511  12707    -39     28    149       C  
ATOM   2411  O   ALA A 306      28.110   7.427 -25.356  1.00 92.98           O  
ANISOU 2411  O   ALA A 306    11475  12319  11536    -37     31    174       O  
ATOM   2412  CB  ALA A 306      29.840   4.753 -24.095  1.00110.48           C  
ANISOU 2412  CB  ALA A 306    13726  14501  13751    -28     44    110       C  
ATOM   2413  N   ALA A 307      27.999   5.471 -26.432  1.00 98.36           N  
ANISOU 2413  N   ALA A 307    12202  13018  12153    -41     30    143       N  
ATOM   2414  CA  ALA A 307      27.536   6.033 -27.690  1.00104.11           C  
ANISOU 2414  CA  ALA A 307    12930  13773  12854    -42     31    167       C  
ATOM   2415  C   ALA A 307      26.714   7.325 -27.526  1.00 97.64           C  
ANISOU 2415  C   ALA A 307    12084  12959  12056    -46     20    196       C  
ATOM   2416  O   ALA A 307      27.033   8.370 -28.103  1.00 80.39           O  
ANISOU 2416  O   ALA A 307     9883  10783   9880    -38     33    225       O  
ATOM   2417  CB  ALA A 307      26.707   4.971 -28.414  1.00115.71           C  
ANISOU 2417  CB  ALA A 307    14428  15262  14276    -55     17    150       C  
ATOM   2418  N   ASP A 308      25.656   7.235 -26.728  1.00 95.07           N  
ANISOU 2418  N   ASP A 308    11756  12628  11740    -58     -1    190       N  
ATOM   2419  CA  ASP A 308      24.660   8.289 -26.654  1.00 96.99           C  
ANISOU 2419  CA  ASP A 308    11978  12878  11997    -63    -12    217       C  
ATOM   2420  C   ASP A 308      24.919   9.197 -25.457  1.00101.01           C  
ANISOU 2420  C   ASP A 308    12463  13360  12557    -58     -7    223       C  
ATOM   2421  O   ASP A 308      24.469  10.333 -25.442  1.00101.50           O  
ANISOU 2421  O   ASP A 308    12504  13423  12639    -57     -6    250       O  
ATOM   2422  CB  ASP A 308      23.249   7.688 -26.561  1.00105.76           C  
ANISOU 2422  CB  ASP A 308    13098  14000  13087    -79    -39    209       C  
ATOM   2423  CG  ASP A 308      23.019   6.519 -27.547  1.00109.46           C  
ANISOU 2423  CG  ASP A 308    13595  14490  13504    -88    -46    192       C  
ATOM   2424  OD1 ASP A 308      23.760   5.504 -27.478  1.00119.39           O  
ANISOU 2424  OD1 ASP A 308    14874  15738  14751    -86    -38    164       O  
ATOM   2425  OD2 ASP A 308      22.078   6.595 -28.369  1.00 93.13           O1-
ANISOU 2425  OD2 ASP A 308    11529  12450  11408    -97    -60    207       O1-
ATOM   2426  N   PHE A 309      25.648   8.704 -24.459  1.00109.27           N  
ANISOU 2426  N   PHE A 309    13512  14382  13623    -56     -4    199       N  
ATOM   2427  CA  PHE A 309      25.919   9.477 -23.241  1.00111.30           C  
ANISOU 2427  CA  PHE A 309    13750  14614  13926    -54     -1    200       C  
ATOM   2428  C   PHE A 309      27.388   9.804 -22.997  1.00104.40           C  
ANISOU 2428  C   PHE A 309    12866  13724  13075    -44     19    199       C  
ATOM   2429  O   PHE A 309      27.701  10.457 -22.014  1.00 94.81           O  
ANISOU 2429  O   PHE A 309    11637  12490  11898    -44     22    199       O  
ATOM   2430  CB  PHE A 309      25.356   8.735 -22.027  1.00115.43           C  
ANISOU 2430  CB  PHE A 309    14280  15121  14457    -63    -18    174       C  
ATOM   2431  CG  PHE A 309      23.870   8.549 -22.081  1.00121.17           C  
ANISOU 2431  CG  PHE A 309    15012  15860  15168    -74    -39    178       C  
ATOM   2432  CD1 PHE A 309      23.024   9.639 -21.965  1.00130.35           C  
ANISOU 2432  CD1 PHE A 309    16155  17023  16348    -76    -43    203       C  
ATOM   2433  CD2 PHE A 309      23.316   7.293 -22.270  1.00127.80           C  
ANISOU 2433  CD2 PHE A 309    15873  16709  15976    -83    -53    157       C  
ATOM   2434  CE1 PHE A 309      21.644   9.482 -22.022  1.00132.33           C  
ANISOU 2434  CE1 PHE A 309    16407  17285  16586    -86    -61    210       C  
ATOM   2435  CE2 PHE A 309      21.940   7.121 -22.327  1.00133.93           C  
ANISOU 2435  CE2 PHE A 309    16651  17496  16739    -95    -73    162       C  
ATOM   2436  CZ  PHE A 309      21.102   8.218 -22.208  1.00134.57           C  
ANISOU 2436  CZ  PHE A 309    16712  17580  16839    -96    -78    190       C  
ATOM   2437  N   VAL A 310      28.277   9.365 -23.886  1.00103.85           N  
ANISOU 2437  N   VAL A 310    12807  13666  12985    -35     34    198       N  
ATOM   2438  CA  VAL A 310      29.722   9.603 -23.736  1.00108.03           C  
ANISOU 2438  CA  VAL A 310    13327  14183  13537    -25     54    199       C  
ATOM   2439  C   VAL A 310      30.353  10.138 -25.043  1.00110.45           C  
ANISOU 2439  C   VAL A 310    13629  14506  13831    -14     75    224       C  
ATOM   2440  O   VAL A 310      30.761  11.291 -25.119  1.00107.14           O  
ANISOU 2440  O   VAL A 310    13188  14081  13437     -9     87    247       O  
ATOM   2441  CB  VAL A 310      30.462   8.342 -23.191  1.00101.59           C  
ANISOU 2441  CB  VAL A 310    12527  13358  12716    -22     55    169       C  
ATOM   2442  CG1 VAL A 310      31.975   8.496 -23.281  1.00100.46           C  
ANISOU 2442  CG1 VAL A 310    12374  13207  12589    -10     78    174       C  
ATOM   2443  CG2 VAL A 310      30.048   8.050 -21.740  1.00 98.76           C  
ANISOU 2443  CG2 VAL A 310    12166  12980  12379    -31     39    149       C  
ATOM   2444  N   GLU A 311      30.422   9.319 -26.079  1.00115.42           N  
ANISOU 2444  N   GLU A 311    14280  15154  14420    -10     79    219       N  
ATOM   2445  CA  GLU A 311      31.031   9.764 -27.347  1.00113.99           C  
ANISOU 2445  CA  GLU A 311    14097  14990  14225      1    100    242       C  
ATOM   2446  C   GLU A 311      30.251  10.867 -28.087  1.00108.80           C  
ANISOU 2446  C   GLU A 311    13425  14349  13563      0     98    274       C  
ATOM   2447  O   GLU A 311      30.855  11.656 -28.802  1.00108.47           O  
ANISOU 2447  O   GLU A 311    13371  14314  13528     10    117    300       O  
ATOM   2448  CB  GLU A 311      31.209   8.585 -28.304  1.00110.12           C  
ANISOU 2448  CB  GLU A 311    13636  14516  13688      4    105    227       C  
ATOM   2449  CG  GLU A 311      32.289   7.602 -27.931  1.00104.68           C  
ANISOU 2449  CG  GLU A 311    12959  13813  13002     12    118    204       C  
ATOM   2450  CD  GLU A 311      32.221   6.400 -28.824  1.00108.69           C  
ANISOU 2450  CD  GLU A 311    13499  14335  13462     12    122    186       C  
ATOM   2451  OE1 GLU A 311      31.183   5.714 -28.760  1.00111.61           O  
ANISOU 2451  OE1 GLU A 311    13887  14711  13809     -1    102    169       O  
ATOM   2452  OE2 GLU A 311      33.174   6.161 -29.605  1.00115.16           O1-
ANISOU 2452  OE2 GLU A 311    14327  15160  14268     25    146    190       O1-
ATOM   2453  N   SER A 312      28.920  10.889 -27.961  1.00102.95           N  
ANISOU 2453  N   SER A 312    12688  13618  12813    -12     77    276       N  
ATOM   2454  CA  SER A 312      28.105  11.854 -28.701  1.00 98.54           C  
ANISOU 2454  CA  SER A 312    12116  13078  12248    -13     75    309       C  
ATOM   2455  C   SER A 312      28.655  13.216 -28.389  1.00108.61           C  
ANISOU 2455  C   SER A 312    13362  14336  13567     -5     91    334       C  
ATOM   2456  O   SER A 312      29.197  13.441 -27.297  1.00107.89           O  
ANISOU 2456  O   SER A 312    13261  14219  13514     -5     94    322       O  
ATOM   2457  CB  SER A 312      26.619  11.781 -28.323  1.00 93.19           C  
ANISOU 2457  CB  SER A 312    11438  12405  11563    -26     49    308       C  
ATOM   2458  OG  SER A 312      25.927  12.989 -28.624  1.00 71.05           O  
ANISOU 2458  OG  SER A 312     8613   9610   8773    -25     49    343       O  
ATOM   2459  N   LYS A 313      28.544  14.110 -29.365  1.00112.52           N  
ANISOU 2459  N   LYS A 313    13846  14849  14058      2    102    368       N  
ATOM   2460  CA  LYS A 313      29.137  15.439 -29.272  1.00110.03           C  
ANISOU 2460  CA  LYS A 313    13504  14520  13784     11    122    396       C  
ATOM   2461  C   LYS A 313      28.032  16.479 -29.156  1.00103.45           C  
ANISOU 2461  C   LYS A 313    12652  13687  12967      7    116    423       C  
ATOM   2462  O   LYS A 313      28.125  17.591 -29.652  1.00 94.55           O  
ANISOU 2462  O   LYS A 313    11505  12562  11857     15    132    456       O  
ATOM   2463  CB  LYS A 313      30.086  15.687 -30.465  1.00119.59           C  
ANISOU 2463  CB  LYS A 313    14713  15746  14980     24    146    416       C  
ATOM   2464  CG  LYS A 313      30.585  14.419 -31.195  1.00127.67           C  
ANISOU 2464  CG  LYS A 313    15764  16787  15959     28    148    396       C  
ATOM   2465  CD  LYS A 313      32.063  14.461 -31.599  1.00126.65           C  
ANISOU 2465  CD  LYS A 313    15632  16652  15837     42    176    400       C  
ATOM   2466  CE  LYS A 313      32.946  13.707 -30.600  1.00123.69           C  
ANISOU 2466  CE  LYS A 313    15262  16252  15481     41    177    368       C  
ATOM   2467  NZ  LYS A 313      34.340  14.224 -30.490  1.00116.52           N1+
ANISOU 2467  NZ  LYS A 313    14337  15330  14606     52    201    379       N1+
ATOM   2468  N   ASP A 314      26.959  16.077 -28.491  1.00113.49           N  
ANISOU 2468  N   ASP A 314    13930  14957  14235     -5     93    408       N  
ATOM   2469  CA  ASP A 314      25.871  16.970 -28.139  1.00120.23           C  
ANISOU 2469  CA  ASP A 314    14766  15806  15110     -9     87    430       C  
ATOM   2470  C   ASP A 314      25.564  16.776 -26.678  1.00112.28           C  
ANISOU 2470  C   ASP A 314    13760  14772  14131    -18     74    404       C  
ATOM   2471  O   ASP A 314      24.511  17.224 -26.206  1.00110.03           O  
ANISOU 2471  O   ASP A 314    13466  14481  13859    -23     65    415       O  
ATOM   2472  CB  ASP A 314      24.618  16.628 -28.946  1.00129.35           C  
ANISOU 2472  CB  ASP A 314    15928  16994  16225    -14     69    444       C  
ATOM   2473  CG  ASP A 314      24.793  16.864 -30.426  1.00145.69           C  
ANISOU 2473  CG  ASP A 314    17996  19095  18263     -5     79    473       C  
ATOM   2474  OD1 ASP A 314      24.444  17.968 -30.890  1.00171.17           O  
ANISOU 2474  OD1 ASP A 314    21203  22329  21504      1     89    512       O  
ATOM   2475  OD2 ASP A 314      25.279  15.958 -31.130  1.00152.37           O1-
ANISOU 2475  OD2 ASP A 314    18863  19958  19071     -5     79    457       O1-
ATOM   2476  N   VAL A 315      26.497  16.147 -25.956  1.00101.57           N  
ANISOU 2476  N   VAL A 315    12412  13396  12783    -19     76    373       N  
ATOM   2477  CA  VAL A 315      26.214  15.627 -24.618  1.00 99.26           C  
ANISOU 2477  CA  VAL A 315    12126  13083  12506    -29     61    343       C  
ATOM   2478  C   VAL A 315      25.909  16.771 -23.669  1.00105.96           C  
ANISOU 2478  C   VAL A 315    12955  13906  13399    -31     66    353       C  
ATOM   2479  O   VAL A 315      24.841  16.818 -23.043  1.00 98.52           O  
ANISOU 2479  O   VAL A 315    12012  12957  12462    -38     52    352       O  
ATOM   2480  CB  VAL A 315      27.379  14.796 -24.055  1.00 99.22           C  
ANISOU 2480  CB  VAL A 315    12132  13065  12503    -28     64    311       C  
ATOM   2481  CG1 VAL A 315      27.105  14.431 -22.611  1.00104.02           C  
ANISOU 2481  CG1 VAL A 315    12743  13650  13131    -37     50    284       C  
ATOM   2482  CG2 VAL A 315      27.585  13.525 -24.860  1.00100.58           C  
ANISOU 2482  CG2 VAL A 315    12328  13258  12631    -27     59    296       C  
ATOM   2483  N   CYS A 316      26.852  17.704 -23.593  1.00123.37           N  
ANISOU 2483  N   CYS A 316    15144  16095  15636    -26     86    365       N  
ATOM   2484  CA  CYS A 316      26.704  18.881 -22.750  1.00126.24           C  
ANISOU 2484  CA  CYS A 316    15491  16432  16044    -28     95    375       C  
ATOM   2485  C   CYS A 316      25.549  19.787 -23.135  1.00116.48           C  
ANISOU 2485  C   CYS A 316    14242  15201  14814    -26     98    408       C  
ATOM   2486  O   CYS A 316      24.862  20.327 -22.260  1.00119.86           O  
ANISOU 2486  O   CYS A 316    14664  15610  15268    -31     96    408       O  
ATOM   2487  CB  CYS A 316      28.008  19.663 -22.717  1.00125.82           C  
ANISOU 2487  CB  CYS A 316    15424  16362  16022    -24    117    381       C  
ATOM   2488  SG  CYS A 316      28.994  19.027 -21.375  1.00130.17           S  
ANISOU 2488  SG  CYS A 316    15981  16889  16589    -33    111    340       S  
ATOM   2489  N   LYS A 317      25.333  19.937 -24.439  1.00107.86           N  
ANISOU 2489  N   LYS A 317    13147  14136  13698    -18    103    437       N  
ATOM   2490  CA  LYS A 317      24.237  20.749 -24.933  1.00109.78           C  
ANISOU 2490  CA  LYS A 317    13377  14391  13945    -14    106    473       C  
ATOM   2491  C   LYS A 317      22.894  20.143 -24.547  1.00115.73           C  
ANISOU 2491  C   LYS A 317    14138  15152  14681    -22     82    465       C  
ATOM   2492  O   LYS A 317      21.974  20.862 -24.114  1.00133.39           O  
ANISOU 2492  O   LYS A 317    16364  17379  16941    -23     83    483       O  
ATOM   2493  CB  LYS A 317      24.311  20.931 -26.450  1.00105.56           C  
ANISOU 2493  CB  LYS A 317    12838  13888  13382     -5    114    505       C  
ATOM   2494  CG  LYS A 317      23.434  22.077 -26.957  1.00109.74           C  
ANISOU 2494  CG  LYS A 317    13347  14424  13926      2    124    550       C  
ATOM   2495  CD  LYS A 317      23.594  22.290 -28.453  1.00114.73           C  
ANISOU 2495  CD  LYS A 317    13974  15090  14531     12    133    583       C  
ATOM   2496  CE  LYS A 317      23.046  23.628 -28.942  1.00110.21           C  
ANISOU 2496  CE  LYS A 317    13376  14519  13981     22    151    632       C  
ATOM   2497  NZ  LYS A 317      21.577  23.565 -29.170  1.00102.92           N1+
ANISOU 2497  NZ  LYS A 317    12448  13617  13039     19    134    653       N1+
ATOM   2498  N   ASN A 318      22.780  18.827 -24.707  1.00105.28           N  
ANISOU 2498  N   ASN A 318    12835  13847  13319    -28     62    440       N  
ATOM   2499  CA  ASN A 318      21.543  18.160 -24.361  1.00102.39           C  
ANISOU 2499  CA  ASN A 318    12478  13490  12936    -37     39    432       C  
ATOM   2500  C   ASN A 318      21.370  17.996 -22.870  1.00107.49           C  
ANISOU 2500  C   ASN A 318    13127  14105  13609    -44     32    404       C  
ATOM   2501  O   ASN A 318      20.241  17.979 -22.382  1.00104.08           O  
ANISOU 2501  O   ASN A 318    12693  13672  13181    -49     20    408       O  
ATOM   2502  CB  ASN A 318      21.396  16.837 -25.093  1.00106.78           C  
ANISOU 2502  CB  ASN A 318    13055  14076  13442    -43     20    416       C  
ATOM   2503  CG  ASN A 318      20.599  16.994 -26.389  1.00124.67           C  
ANISOU 2503  CG  ASN A 318    15315  16377  15675    -42     15    449       C  
ATOM   2504  ND2 ASN A 318      20.430  15.895 -27.127  1.00138.68           N  
ANISOU 2504  ND2 ASN A 318    17109  18180  17404    -48     -1    436       N  
ATOM   2505  OD1 ASN A 318      20.117  18.090 -26.712  1.00104.57           O  
ANISOU 2505  OD1 ASN A 318    12750  13836  13148    -35     25    486       O  
ATOM   2506  N   TYR A 319      22.480  17.905 -22.143  1.00110.11           N  
ANISOU 2506  N   TYR A 319    13463  14414  13960    -45     40    379       N  
ATOM   2507  CA  TYR A 319      22.411  17.915 -20.695  1.00111.91           C  
ANISOU 2507  CA  TYR A 319    13692  14612  14216    -51     36    355       C  
ATOM   2508  C   TYR A 319      21.928  19.264 -20.174  1.00108.25           C  
ANISOU 2508  C   TYR A 319    13211  14127  13792    -49     51    377       C  
ATOM   2509  O   TYR A 319      21.051  19.321 -19.318  1.00114.59           O  
ANISOU 2509  O   TYR A 319    14014  14918  14608    -53     43    372       O  
ATOM   2510  CB  TYR A 319      23.755  17.596 -20.043  1.00119.90           C  
ANISOU 2510  CB  TYR A 319    14710  15607  15240    -52     42    326       C  
ATOM   2511  CG  TYR A 319      23.656  17.751 -18.543  1.00122.72           C  
ANISOU 2511  CG  TYR A 319    15067  15934  15626    -59     38    304       C  
ATOM   2512  CD1 TYR A 319      22.943  16.824 -17.789  1.00128.29           C  
ANISOU 2512  CD1 TYR A 319    15786  16639  16320    -66     19    282       C  
ATOM   2513  CD2 TYR A 319      24.206  18.853 -17.886  1.00113.73           C  
ANISOU 2513  CD2 TYR A 319    13916  14769  14528    -60     55    307       C  
ATOM   2514  CE1 TYR A 319      22.809  16.966 -16.424  1.00131.80           C  
ANISOU 2514  CE1 TYR A 319    16231  17058  16789    -72     16    263       C  
ATOM   2515  CE2 TYR A 319      24.066  19.008 -16.523  1.00116.35           C  
ANISOU 2515  CE2 TYR A 319    14249  15075  14883    -67     52    287       C  
ATOM   2516  CZ  TYR A 319      23.374  18.057 -15.796  1.00126.68           C  
ANISOU 2516  CZ  TYR A 319    15571  16385  16177    -72     33    265       C  
ATOM   2517  OH  TYR A 319      23.212  18.179 -14.436  1.00141.06           O  
ANISOU 2517  OH  TYR A 319    17396  18182  18019    -79     30    245       O  
ATOM   2518  N   ALA A 320      22.506  20.350 -20.663  1.00102.39           N  
ANISOU 2518  N   ALA A 320    12454  13379  13072    -42     73    401       N  
ATOM   2519  CA  ALA A 320      22.158  21.661 -20.131  1.00102.41           C  
ANISOU 2519  CA  ALA A 320    12440  13356  13116    -40     90    420       C  
ATOM   2520  C   ALA A 320      20.704  21.952 -20.454  1.00112.04           C  
ANISOU 2520  C   ALA A 320    13652  14588  14330    -37     85    449       C  
ATOM   2521  O   ALA A 320      19.969  22.466 -19.604  1.00109.88           O  
ANISOU 2521  O   ALA A 320    13374  14293  14082    -38     89    452       O  
ATOM   2522  CB  ALA A 320      23.065  22.730 -20.705  1.00104.99           C  
ANISOU 2522  CB  ALA A 320    12751  13675  13465    -33    116    442       C  
ATOM   2523  N   GLU A 321      20.289  21.572 -21.668  1.00120.37           N  
ANISOU 2523  N   GLU A 321    14706  15678  15350    -33     77    471       N  
ATOM   2524  CA  GLU A 321      18.924  21.826 -22.168  1.00125.57           C  
ANISOU 2524  CA  GLU A 321    15356  16356  16000    -30     71    504       C  
ATOM   2525  C   GLU A 321      17.819  21.215 -21.331  1.00112.77           C  
ANISOU 2525  C   GLU A 321    13741  14731  14375    -38     51    490       C  
ATOM   2526  O   GLU A 321      16.866  21.885 -20.958  1.00105.58           O  
ANISOU 2526  O   GLU A 321    12818  13810  13485    -35     57    511       O  
ATOM   2527  CB  GLU A 321      18.764  21.333 -23.603  1.00132.77           C  
ANISOU 2527  CB  GLU A 321    16269  17310  16869    -28     61    523       C  
ATOM   2528  CG  GLU A 321      18.993  22.423 -24.628  1.00139.52           C  
ANISOU 2528  CG  GLU A 321    17104  18174  17732    -16     83    566       C  
ATOM   2529  CD  GLU A 321      18.918  21.890 -26.027  1.00147.64           C  
ANISOU 2529  CD  GLU A 321    18136  19246  18713    -14     73    582       C  
ATOM   2530  OE1 GLU A 321      17.849  21.336 -26.390  1.00154.22           O  
ANISOU 2530  OE1 GLU A 321    18972  20106  19518    -19     52    591       O  
ATOM   2531  OE2 GLU A 321      19.938  22.023 -26.745  1.00161.78           O1-
ANISOU 2531  OE2 GLU A 321    19929  21044  20498     -8     86    586       O1-
ATOM   2532  N   ALA A 322      17.930  19.929 -21.066  1.00110.77           N  
ANISOU 2532  N   ALA A 322    13507  14487  14094    -46     30    455       N  
ATOM   2533  CA  ALA A 322      16.998  19.279 -20.163  1.00111.55           C  
ANISOU 2533  CA  ALA A 322    13613  14579  14190    -54     12    438       C  
ATOM   2534  C   ALA A 322      17.762  18.257 -19.322  1.00106.82           C  
ANISOU 2534  C   ALA A 322    13035  13968  13585    -62      1    391       C  
ATOM   2535  O   ALA A 322      17.794  17.071 -19.645  1.00101.18           O  
ANISOU 2535  O   ALA A 322    12336  13272  12837    -67    -17    372       O  
ATOM   2536  CB  ALA A 322      15.865  18.649 -20.948  1.00109.34           C  
ANISOU 2536  CB  ALA A 322    13334  14334  13876    -58     -9    455       C  
ATOM   2537  N   LYS A 323      18.403  18.756 -18.261  1.00103.23           N  
ANISOU 2537  N   LYS A 323    12579  13479  13163    -61     14    374       N  
ATOM   2538  CA  LYS A 323      19.184  17.925 -17.347  1.00104.43           C  
ANISOU 2538  CA  LYS A 323    12747  13617  13314    -68      7    333       C  
ATOM   2539  C   LYS A 323      18.334  16.850 -16.711  1.00116.66           C  
ANISOU 2539  C   LYS A 323    14309  15170  14847    -75    -16    313       C  
ATOM   2540  O   LYS A 323      18.743  15.685 -16.685  1.00127.24           O  
ANISOU 2540  O   LYS A 323    15664  16519  16162    -79    -29    286       O  
ATOM   2541  CB  LYS A 323      19.917  18.731 -16.256  1.00108.72           C  
ANISOU 2541  CB  LYS A 323    13286  14126  13897    -68     23    320       C  
ATOM   2542  CG  LYS A 323      19.514  20.186 -16.039  1.00121.01           C  
ANISOU 2542  CG  LYS A 323    14827  15663  15491    -64     44    346       C  
ATOM   2543  CD  LYS A 323      20.441  20.872 -15.033  1.00133.31           C  
ANISOU 2543  CD  LYS A 323    16383  17187  17082    -68     59    327       C  
ATOM   2544  CE  LYS A 323      20.452  22.400 -15.124  1.00132.77           C  
ANISOU 2544  CE  LYS A 323    16298  17097  17050    -63     86    354       C  
ATOM   2545  NZ  LYS A 323      21.014  23.066 -13.903  1.00125.46           N1+
ANISOU 2545  NZ  LYS A 323    15374  16136  16159    -70     99    333       N1+
ATOM   2546  N   ASP A 324      17.152  17.236 -16.226  1.00123.31           N  
ANISOU 2546  N   ASP A 324    15144  16006  15703    -75    -17    327       N  
ATOM   2547  CA  ASP A 324      16.236  16.306 -15.556  1.00119.19           C  
ANISOU 2547  CA  ASP A 324    14632  15486  15170    -81    -37    311       C  
ATOM   2548  C   ASP A 324      15.761  15.185 -16.480  1.00120.27           C  
ANISOU 2548  C   ASP A 324    14777  15655  15265    -87    -58    311       C  
ATOM   2549  O   ASP A 324      15.761  14.020 -16.084  1.00144.42           O  
ANISOU 2549  O   ASP A 324    17852  18716  18306    -93    -74    283       O  
ATOM   2550  CB  ASP A 324      15.041  17.055 -14.951  1.00124.56           C  
ANISOU 2550  CB  ASP A 324    15301  16152  15874    -79    -32    332       C  
ATOM   2551  CG  ASP A 324      15.415  17.859 -13.725  1.00131.87           C  
ANISOU 2551  CG  ASP A 324    16225  17042  16838    -77    -14    320       C  
ATOM   2552  OD1 ASP A 324      16.521  17.648 -13.188  1.00132.88           O  
ANISOU 2552  OD1 ASP A 324    16362  17156  16969    -80    -12    291       O  
ATOM   2553  OD2 ASP A 324      14.602  18.707 -13.312  1.00140.59           O1-
ANISOU 2553  OD2 ASP A 324    17319  18131  17966    -73     -2    340       O1-
ATOM   2554  N   VAL A 325      15.391  15.526 -17.711  1.00116.15           N  
ANISOU 2554  N   VAL A 325    14245  15158  14727    -84    -58    342       N  
ATOM   2555  CA  VAL A 325      14.976  14.519 -18.699  1.00111.01           C  
ANISOU 2555  CA  VAL A 325    13603  14540  14034    -91    -78    343       C  
ATOM   2556  C   VAL A 325      16.172  13.667 -19.188  1.00115.88           C  
ANISOU 2556  C   VAL A 325    14238  15165  14626    -93    -80    316       C  
ATOM   2557  O   VAL A 325      16.059  12.444 -19.314  1.00124.14           O  
ANISOU 2557  O   VAL A 325    15302  16223  15643   -101    -97    293       O  
ATOM   2558  CB  VAL A 325      14.242  15.158 -19.896  1.00102.97           C  
ANISOU 2558  CB  VAL A 325    12570  13550  13005    -89    -78    385       C  
ATOM   2559  CG1 VAL A 325      13.356  14.126 -20.579  1.00104.30           C  
ANISOU 2559  CG1 VAL A 325    12745  13750  13133   -100   -104    386       C  
ATOM   2560  CG2 VAL A 325      13.391  16.350 -19.453  1.00 99.10           C  
ANISOU 2560  CG2 VAL A 325    12058  13046  12549    -82    -66    418       C  
ATOM   2561  N   PHE A 326      17.305  14.320 -19.445  1.00110.93           N  
ANISOU 2561  N   PHE A 326    13607  14530  14011    -85    -60    319       N  
ATOM   2562  CA  PHE A 326      18.555  13.650 -19.812  1.00105.57           C  
ANISOU 2562  CA  PHE A 326    12942  13855  13315    -84    -57    296       C  
ATOM   2563  C   PHE A 326      18.995  12.652 -18.730  1.00 99.40           C  
ANISOU 2563  C   PHE A 326    12176  13055  12535    -88    -65    256       C  
ATOM   2564  O   PHE A 326      19.495  11.563 -19.029  1.00 96.22           O  
ANISOU 2564  O   PHE A 326    11791  12662  12107    -91    -71    234       O  
ATOM   2565  CB  PHE A 326      19.644  14.717 -20.044  1.00109.15           C  
ANISOU 2565  CB  PHE A 326    13384  14297  13792    -74    -33    309       C  
ATOM   2566  CG  PHE A 326      20.885  14.214 -20.738  1.00110.46           C  
ANISOU 2566  CG  PHE A 326    13560  14472  13938    -70    -26    297       C  
ATOM   2567  CD1 PHE A 326      20.887  13.981 -22.117  1.00111.66           C  
ANISOU 2567  CD1 PHE A 326    13715  14653  14056    -68    -26    312       C  
ATOM   2568  CD2 PHE A 326      22.063  14.024 -20.031  1.00106.48           C  
ANISOU 2568  CD2 PHE A 326    13059  13947  13450    -69    -17    272       C  
ATOM   2569  CE1 PHE A 326      22.024  13.528 -22.767  1.00101.37           C  
ANISOU 2569  CE1 PHE A 326    12422  13357  12735    -64    -17    301       C  
ATOM   2570  CE2 PHE A 326      23.203  13.579 -20.678  1.00106.92           C  
ANISOU 2570  CE2 PHE A 326    13123  14011  13490    -64     -9    264       C  
ATOM   2571  CZ  PHE A 326      23.180  13.321 -22.044  1.00102.45           C  
ANISOU 2571  CZ  PHE A 326    12563  13473  12891    -61     -8    278       C  
ATOM   2572  N   LEU A 327      18.812  13.017 -17.473  1.00 94.70           N  
ANISOU 2572  N   LEU A 327    11577  12435  11971    -89    -63    248       N  
ATOM   2573  CA  LEU A 327      19.270  12.146 -16.397  1.00 97.26           C  
ANISOU 2573  CA  LEU A 327    11914  12743  12299    -93    -69    213       C  
ATOM   2574  C   LEU A 327      18.296  11.018 -16.185  1.00 99.26           C  
ANISOU 2574  C   LEU A 327    12179  13004  12530   -100    -90    199       C  
ATOM   2575  O   LEU A 327      18.697   9.887 -15.902  1.00100.28           O  
ANISOU 2575  O   LEU A 327    12325  13132  12645   -104    -98    172       O  
ATOM   2576  CB  LEU A 327      19.464  12.912 -15.104  1.00 98.03           C  
ANISOU 2576  CB  LEU A 327    12003  12810  12434    -91    -60    207       C  
ATOM   2577  CG  LEU A 327      20.755  13.712 -15.126  1.00 96.84           C  
ANISOU 2577  CG  LEU A 327    11844  12648  12304    -86    -41    208       C  
ATOM   2578  CD1 LEU A 327      20.678  14.871 -14.131  1.00 98.25           C  
ANISOU 2578  CD1 LEU A 327    12011  12800  12521    -86    -29    213       C  
ATOM   2579  CD2 LEU A 327      21.923  12.788 -14.828  1.00 91.43           C  
ANISOU 2579  CD2 LEU A 327    11170  11959  11608    -87    -43    179       C  
ATOM   2580  N   GLY A 328      17.013  11.330 -16.333  1.00102.44           N  
ANISOU 2580  N   GLY A 328    12575  13416  12934   -104    -98    221       N  
ATOM   2581  CA  GLY A 328      15.962  10.324 -16.299  1.00 97.59           C  
ANISOU 2581  CA  GLY A 328    11969  12812  12297   -113   -119    214       C  
ATOM   2582  C   GLY A 328      16.158   9.297 -17.396  1.00 91.18           C  
ANISOU 2582  C   GLY A 328    11172  12025  11446   -119   -129    204       C  
ATOM   2583  O   GLY A 328      16.077   8.084 -17.147  1.00 86.00           O  
ANISOU 2583  O   GLY A 328    10533  11369  10772   -126   -142    179       O  
ATOM   2584  N   MET A 329      16.454   9.787 -18.598  1.00 93.42           N  
ANISOU 2584  N   MET A 329    11451  12328  11715   -115   -122    225       N  
ATOM   2585  CA  MET A 329      16.664   8.915 -19.747  1.00 95.92           C  
ANISOU 2585  CA  MET A 329    11783  12670  11991   -121   -129    218       C  
ATOM   2586  C   MET A 329      17.888   8.048 -19.536  1.00 92.04           C  
ANISOU 2586  C   MET A 329    11310  12168  11493   -118   -123    185       C  
ATOM   2587  O   MET A 329      17.871   6.876 -19.916  1.00 78.49           O  
ANISOU 2587  O   MET A 329     9613  10461   9747   -125   -132    165       O  
ATOM   2588  CB  MET A 329      16.813   9.708 -21.042  1.00103.13           C  
ANISOU 2588  CB  MET A 329    12687  13606  12892   -116   -120    248       C  
ATOM   2589  CG  MET A 329      15.992   9.116 -22.177  1.00110.44           C  
ANISOU 2589  CG  MET A 329    13620  14565  13776   -127   -138    257       C  
ATOM   2590  SD  MET A 329      15.302  10.324 -23.332  1.00117.14           S  
ANISOU 2590  SD  MET A 329    14447  15443  14619   -124   -136    307       S  
ATOM   2591  CE  MET A 329      15.152  11.774 -22.296  1.00104.08           C  
ANISOU 2591  CE  MET A 329    12767  13760  13020   -112   -119    330       C  
ATOM   2592  N   PHE A 330      18.937   8.629 -18.937  1.00101.08           N  
ANISOU 2592  N   PHE A 330    12448  13291  12665   -108   -106    180       N  
ATOM   2593  CA  PHE A 330      20.156   7.881 -18.565  1.00103.25           C  
ANISOU 2593  CA  PHE A 330    12736  13554  12939   -104    -98    152       C  
ATOM   2594  C   PHE A 330      19.807   6.770 -17.601  1.00 85.93           C  
ANISOU 2594  C   PHE A 330    10556  11348  10744   -110   -111    124       C  
ATOM   2595  O   PHE A 330      20.105   5.581 -17.837  1.00 75.27           O  
ANISOU 2595  O   PHE A 330     9226  10003   9372   -113   -115    102       O  
ATOM   2596  CB  PHE A 330      21.210   8.786 -17.899  1.00104.77           C  
ANISOU 2596  CB  PHE A 330    12916  13726  13167    -95    -80    154       C  
ATOM   2597  CG  PHE A 330      22.324   8.019 -17.213  1.00118.95           C  
ANISOU 2597  CG  PHE A 330    14721  15507  14967    -91    -76    126       C  
ATOM   2598  CD1 PHE A 330      23.421   7.567 -17.935  1.00136.98           C  
ANISOU 2598  CD1 PHE A 330    17013  17797  17235    -85    -64    119       C  
ATOM   2599  CD2 PHE A 330      22.276   7.733 -15.849  1.00121.69           C  
ANISOU 2599  CD2 PHE A 330    15069  15835  15334    -93    -82    107       C  
ATOM   2600  CE1 PHE A 330      24.449   6.854 -17.314  1.00135.93           C  
ANISOU 2600  CE1 PHE A 330    16887  17652  17108    -81    -59     97       C  
ATOM   2601  CE2 PHE A 330      23.296   7.019 -15.225  1.00118.42           C  
ANISOU 2601  CE2 PHE A 330    14661  15408  14923    -90    -78     84       C  
ATOM   2602  CZ  PHE A 330      24.379   6.580 -15.960  1.00125.75           C  
ANISOU 2602  CZ  PHE A 330    15597  16344  15838    -84    -66     80       C  
ATOM   2603  N   LEU A 331      19.172   7.189 -16.512  1.00 75.28           N  
ANISOU 2603  N   LEU A 331     9197   9984   9421   -112   -116    126       N  
ATOM   2604  CA  LEU A 331      18.833   6.279 -15.447  1.00 74.67           C  
ANISOU 2604  CA  LEU A 331     9129   9893   9348   -116   -127    103       C  
ATOM   2605  C   LEU A 331      17.998   5.128 -15.991  1.00 72.85           C  
ANISOU 2605  C   LEU A 331     8914   9678   9086   -127   -144     94       C  
ATOM   2606  O   LEU A 331      18.290   3.989 -15.685  1.00 59.38           O  
ANISOU 2606  O   LEU A 331     7224   7967   7369   -129   -148     69       O  
ATOM   2607  CB  LEU A 331      18.090   7.010 -14.326  1.00 75.61           C  
ANISOU 2607  CB  LEU A 331     9235   9996   9496   -117   -130    111       C  
ATOM   2608  CG  LEU A 331      17.757   6.126 -13.122  1.00 72.98           C  
ANISOU 2608  CG  LEU A 331     8911   9648   9169   -120   -140     88       C  
ATOM   2609  CD1 LEU A 331      19.032   5.492 -12.575  1.00 76.07           C  
ANISOU 2609  CD1 LEU A 331     9311  10028   9563   -115   -133     63       C  
ATOM   2610  CD2 LEU A 331      17.026   6.949 -12.076  1.00 75.71           C  
ANISOU 2610  CD2 LEU A 331     9243   9978   9543   -119   -140     98       C  
ATOM   2611  N   TYR A 332      16.969   5.453 -16.785  1.00 79.03           N  
ANISOU 2611  N   TYR A 332     9692  10481   9855   -134   -153    116       N  
ATOM   2612  CA  TYR A 332      16.089   4.475 -17.444  1.00 80.76           C  
ANISOU 2612  CA  TYR A 332     9924  10718  10042   -147   -171    111       C  
ATOM   2613  C   TYR A 332      16.923   3.515 -18.280  1.00 75.09           C  
ANISOU 2613  C   TYR A 332     9228  10010   9294   -148   -167     91       C  
ATOM   2614  O   TYR A 332      16.679   2.311 -18.261  1.00 77.33           O  
ANISOU 2614  O   TYR A 332     9529  10293   9559   -157   -177     69       O  
ATOM   2615  CB  TYR A 332      15.004   5.198 -18.296  1.00 93.23           C  
ANISOU 2615  CB  TYR A 332    11489  12321  11612   -153   -180    144       C  
ATOM   2616  CG  TYR A 332      14.476   4.448 -19.524  1.00102.50           C  
ANISOU 2616  CG  TYR A 332    12677  13524  12745   -166   -195    144       C  
ATOM   2617  CD1 TYR A 332      13.733   3.282 -19.394  1.00 99.69           C  
ANISOU 2617  CD1 TYR A 332    12334  13171  12371   -181   -213    126       C  
ATOM   2618  CD2 TYR A 332      14.705   4.930 -20.823  1.00115.48           C  
ANISOU 2618  CD2 TYR A 332    14319  15193  14367   -165   -190    163       C  
ATOM   2619  CE1 TYR A 332      13.259   2.601 -20.507  1.00105.24           C  
ANISOU 2619  CE1 TYR A 332    13050  13900  13035   -196   -226    124       C  
ATOM   2620  CE2 TYR A 332      14.230   4.252 -21.934  1.00118.30           C  
ANISOU 2620  CE2 TYR A 332    14688  15577  14683   -179   -204    162       C  
ATOM   2621  CZ  TYR A 332      13.512   3.088 -21.768  1.00112.66           C  
ANISOU 2621  CZ  TYR A 332    13989  14865  13951   -195   -222    141       C  
ATOM   2622  OH  TYR A 332      13.048   2.428 -22.877  1.00121.06           O  
ANISOU 2622  OH  TYR A 332    15067  15956  14974   -211   -236    139       O  
ATOM   2623  N   GLU A 333      17.922   4.036 -18.983  1.00 69.28           N  
ANISOU 2623  N   GLU A 333     8489   9279   8554   -139   -151     98       N  
ATOM   2624  CA  GLU A 333      18.772   3.176 -19.775  1.00 74.79           C  
ANISOU 2624  CA  GLU A 333     9209   9984   9224   -138   -143     80       C  
ATOM   2625  C   GLU A 333      19.576   2.224 -18.903  1.00 66.07           C  
ANISOU 2625  C   GLU A 333     8117   8858   8129   -133   -137     50       C  
ATOM   2626  O   GLU A 333      19.392   1.026 -18.955  1.00 65.13           O  
ANISOU 2626  O   GLU A 333     8019   8738   7991   -141   -144     28       O  
ATOM   2627  CB  GLU A 333      19.694   3.990 -20.694  1.00 86.79           C  
ANISOU 2627  CB  GLU A 333    10722  11514  10740   -127   -125     97       C  
ATOM   2628  CG  GLU A 333      18.992   4.791 -21.793  1.00 88.86           C  
ANISOU 2628  CG  GLU A 333    10974  11803  10986   -131   -130    128       C  
ATOM   2629  CD  GLU A 333      18.130   3.935 -22.727  1.00 98.31           C  
ANISOU 2629  CD  GLU A 333    12188  13025  12142   -147   -147    123       C  
ATOM   2630  OE1 GLU A 333      18.057   2.696 -22.548  1.00105.57           O  
ANISOU 2630  OE1 GLU A 333    13128  13938  13044   -155   -155     95       O  
ATOM   2631  OE2 GLU A 333      17.520   4.492 -23.669  1.00 93.45           O1-
ANISOU 2631  OE2 GLU A 333    11564  12434  11508   -151   -153    149       O1-
ATOM   2632  N   TYR A 334      20.447   2.758 -18.081  1.00 64.30           N  
ANISOU 2632  N   TYR A 334     7882   8615   7935   -122   -124     50       N  
ATOM   2633  CA  TYR A 334      21.276   1.922 -17.229  1.00 74.38           C  
ANISOU 2633  CA  TYR A 334     9168   9873   9222   -116   -118     25       C  
ATOM   2634  C   TYR A 334      20.389   0.990 -16.374  1.00 81.20           C  
ANISOU 2634  C   TYR A 334    10039  10726  10085   -125   -134      8       C  
ATOM   2635  O   TYR A 334      20.771  -0.134 -16.030  1.00 79.40           O  
ANISOU 2635  O   TYR A 334     9828  10489   9852   -124   -132    -15       O  
ATOM   2636  CB  TYR A 334      22.146   2.817 -16.329  1.00 85.14           C  
ANISOU 2636  CB  TYR A 334    10512  11219  10619   -105   -106     31       C  
ATOM   2637  CG  TYR A 334      23.495   2.241 -15.967  1.00 87.42           C  
ANISOU 2637  CG  TYR A 334    10806  11496  10914    -95    -92     14       C  
ATOM   2638  CD1 TYR A 334      23.594   1.083 -15.205  1.00 86.37           C  
ANISOU 2638  CD1 TYR A 334    10686  11352  10780    -95    -96     -9       C  
ATOM   2639  CD2 TYR A 334      24.678   2.877 -16.361  1.00 92.27           C  
ANISOU 2639  CD2 TYR A 334    11411  12111  11536    -85    -75     24       C  
ATOM   2640  CE1 TYR A 334      24.826   0.556 -14.861  1.00 89.65           C  
ANISOU 2640  CE1 TYR A 334    11104  11757  11202    -85    -83    -21       C  
ATOM   2641  CE2 TYR A 334      25.918   2.343 -16.032  1.00 93.42           C  
ANISOU 2641  CE2 TYR A 334    11560  12247  11689    -76    -62     11       C  
ATOM   2642  CZ  TYR A 334      25.980   1.182 -15.279  1.00 95.03           C  
ANISOU 2642  CZ  TYR A 334    11775  12440  11891    -76    -66    -10       C  
ATOM   2643  OH  TYR A 334      27.190   0.628 -14.937  1.00104.04           O  
ANISOU 2643  OH  TYR A 334    12918  13574  13040    -66    -53    -20       O  
ATOM   2644  N   ALA A 335      19.191   1.465 -16.032  1.00 87.99           N  
ANISOU 2644  N   ALA A 335    10889  11589  10953   -133   -148     21       N  
ATOM   2645  CA  ALA A 335      18.270   0.708 -15.167  1.00 88.28           C  
ANISOU 2645  CA  ALA A 335    10930  11616  10994   -141   -163      8       C  
ATOM   2646  C   ALA A 335      17.792  -0.532 -15.866  1.00 84.22           C  
ANISOU 2646  C   ALA A 335    10438  11113  10449   -152   -172     -7       C  
ATOM   2647  O   ALA A 335      17.927  -1.645 -15.350  1.00 75.11           O  
ANISOU 2647  O   ALA A 335     9298   9946   9292   -154   -173    -30       O  
ATOM   2648  CB  ALA A 335      17.073   1.563 -14.739  1.00 87.69           C  
ANISOU 2648  CB  ALA A 335    10839  11544  10936   -146   -174     29       C  
ATOM   2649  N   ARG A 336      17.252  -0.325 -17.060  1.00 89.26           N  
ANISOU 2649  N   ARG A 336    11079  11774  11062   -161   -179      6       N  
ATOM   2650  CA  ARG A 336      16.648  -1.397 -17.809  1.00 91.16           C  
ANISOU 2650  CA  ARG A 336    11340  12027  11271   -176   -191     -7       C  
ATOM   2651  C   ARG A 336      17.629  -2.517 -18.025  1.00 96.57           C  
ANISOU 2651  C   ARG A 336    12048  12703  11940   -173   -178    -34       C  
ATOM   2652  O   ARG A 336      17.219  -3.675 -18.008  1.00123.68           O  
ANISOU 2652  O   ARG A 336    15500  16132  15359   -184   -185    -55       O  
ATOM   2653  CB  ARG A 336      16.068  -0.905 -19.131  1.00 91.53           C  
ANISOU 2653  CB  ARG A 336    11384  12103  11291   -186   -199     13       C  
ATOM   2654  CG  ARG A 336      17.054  -0.679 -20.248  1.00 92.41           C  
ANISOU 2654  CG  ARG A 336    11504  12227  11382   -179   -183     15       C  
ATOM   2655  CD  ARG A 336      16.548   0.385 -21.214  1.00105.50           C  
ANISOU 2655  CD  ARG A 336    13146  13911  13028   -182   -188     47       C  
ATOM   2656  NE  ARG A 336      15.234   0.068 -21.758  1.00118.25           N  
ANISOU 2656  NE  ARG A 336    14763  15547  14618   -201   -211     54       N  
ATOM   2657  CZ  ARG A 336      15.000  -0.434 -22.973  1.00132.65           C  
ANISOU 2657  CZ  ARG A 336    16604  17395  16402   -215   -218     50       C  
ATOM   2658  NH1 ARG A 336      15.994  -0.695 -23.826  1.00131.10           N1+
ANISOU 2658  NH1 ARG A 336    16425  17205  16183   -209   -202     39       N1+
ATOM   2659  NH2 ARG A 336      13.748  -0.688 -23.338  1.00146.74           N  
ANISOU 2659  NH2 ARG A 336    18387  19199  18168   -234   -241     57       N  
ATOM   2660  N   ARG A 337      18.917  -2.199 -18.194  1.00 91.68           N  
ANISOU 2660  N   ARG A 337    11428  12079  11326   -158   -158    -35       N  
ATOM   2661  CA  ARG A 337      19.948  -3.242 -18.412  1.00 82.97           C  
ANISOU 2661  CA  ARG A 337    10347  10966  10210   -151   -141    -59       C  
ATOM   2662  C   ARG A 337      20.464  -3.891 -17.147  1.00 76.99           C  
ANISOU 2662  C   ARG A 337     9592  10185   9478   -143   -135    -75       C  
ATOM   2663  O   ARG A 337      21.072  -4.933 -17.240  1.00 73.71           O  
ANISOU 2663  O   ARG A 337     9195   9760   9053   -139   -124    -95       O  
ATOM   2664  CB  ARG A 337      21.135  -2.709 -19.219  1.00 79.53           C  
ANISOU 2664  CB  ARG A 337     9910  10537   9768   -138   -121    -50       C  
ATOM   2665  CG  ARG A 337      20.796  -2.384 -20.657  1.00 81.38           C  
ANISOU 2665  CG  ARG A 337    10151  10798   9970   -146   -124    -38       C  
ATOM   2666  CD  ARG A 337      21.465  -1.098 -21.119  1.00 86.45           C  
ANISOU 2666  CD  ARG A 337    10776  11450  10622   -134   -111    -13       C  
ATOM   2667  NE  ARG A 337      20.613  -0.387 -22.069  1.00 90.38           N  
ANISOU 2667  NE  ARG A 337    11267  11974  11101   -144   -123      9       N  
ATOM   2668  CZ  ARG A 337      21.032   0.205 -23.173  1.00 94.65           C  
ANISOU 2668  CZ  ARG A 337    11806  12532  11624   -139   -112     26       C  
ATOM   2669  NH1 ARG A 337      22.310   0.198 -23.506  1.00105.64           N1+
ANISOU 2669  NH1 ARG A 337    13203  13919  13016   -125    -90     22       N1+
ATOM   2670  NH2 ARG A 337      20.159   0.804 -23.960  1.00105.94           N  
ANISOU 2670  NH2 ARG A 337    13228  13987  13037   -148   -125     47       N  
ATOM   2671  N   HIS A 338      20.239  -3.300 -15.974  1.00 86.24           N  
ANISOU 2671  N   HIS A 338    10743  11344  10680   -139   -141    -67       N  
ATOM   2672  CA  HIS A 338      20.733  -3.916 -14.718  1.00 93.16           C  
ANISOU 2672  CA  HIS A 338    11619  12199  11578   -130   -136    -82       C  
ATOM   2673  C   HIS A 338      19.691  -4.247 -13.665  1.00 91.48           C  
ANISOU 2673  C   HIS A 338    11403  11977  11379   -138   -152    -86       C  
ATOM   2674  O   HIS A 338      19.640  -3.605 -12.622  1.00 82.22           O  
ANISOU 2674  O   HIS A 338    10213  10795  10232   -132   -155    -79       O  
ATOM   2675  CB  HIS A 338      21.805  -3.056 -14.060  1.00 93.31           C  
ANISOU 2675  CB  HIS A 338    11620  12211  11624   -115   -124    -73       C  
ATOM   2676  CG  HIS A 338      23.092  -3.043 -14.806  1.00 97.60           C  
ANISOU 2676  CG  HIS A 338    12167  12757  12159   -104   -104    -73       C  
ATOM   2677  CD2 HIS A 338      23.531  -2.245 -15.805  1.00104.02           C  
ANISOU 2677  CD2 HIS A 338    12975  13583  12963   -101    -96    -58       C  
ATOM   2678  ND1 HIS A 338      24.102  -3.944 -14.562  1.00 96.07           N  
ANISOU 2678  ND1 HIS A 338    11984  12552  11967    -94    -90    -88       N  
ATOM   2679  CE1 HIS A 338      25.121  -3.689 -15.361  1.00104.08           C  
ANISOU 2679  CE1 HIS A 338    12999  13573  12975    -85    -72    -82       C  
ATOM   2680  NE2 HIS A 338      24.799  -2.664 -16.128  1.00112.15           N  
ANISOU 2680  NE2 HIS A 338    14013  14610  13990    -89    -76    -65       N  
ATOM   2681  N   PRO A 339      18.909  -5.306 -13.893  1.00 95.49           N  
ANISOU 2681  N   PRO A 339    11929  12485  11870   -150   -162   -100       N  
ATOM   2682  CA  PRO A 339      18.064  -5.751 -12.802  1.00 98.30           C  
ANISOU 2682  CA  PRO A 339    12282  12829  12241   -155   -174   -105       C  
ATOM   2683  C   PRO A 339      18.861  -6.454 -11.699  1.00 89.38           C  
ANISOU 2683  C   PRO A 339    11154  11678  11128   -142   -163   -120       C  
ATOM   2684  O   PRO A 339      18.309  -6.727 -10.641  1.00 79.16           O  
ANISOU 2684  O   PRO A 339     9855  10373   9850   -143   -171   -122       O  
ATOM   2685  CB  PRO A 339      17.103  -6.723 -13.491  1.00102.93           C  
ANISOU 2685  CB  PRO A 339    12886  13421  12802   -173   -186   -116       C  
ATOM   2686  CG  PRO A 339      17.906  -7.311 -14.592  1.00102.04           C  
ANISOU 2686  CG  PRO A 339    12794  13313  12663   -172   -172   -129       C  
ATOM   2687  CD  PRO A 339      18.882  -6.248 -15.027  1.00 96.71           C  
ANISOU 2687  CD  PRO A 339    12107  12647  11992   -159   -159   -114       C  
ATOM   2688  N   ASP A 340      20.141  -6.723 -11.968  1.00 86.20           N  
ANISOU 2688  N   ASP A 340    10758  11271  10722   -131   -145   -127       N  
ATOM   2689  CA  ASP A 340      21.051  -7.392 -11.047  1.00 89.91           C  
ANISOU 2689  CA  ASP A 340    11229  11724  11207   -117   -133   -138       C  
ATOM   2690  C   ASP A 340      21.769  -6.418 -10.079  1.00 95.97           C  
ANISOU 2690  C   ASP A 340    11974  12489  12002   -105   -129   -126       C  
ATOM   2691  O   ASP A 340      22.471  -6.837  -9.147  1.00 95.57           O  
ANISOU 2691  O   ASP A 340    11920  12427  11966    -94   -122   -132       O  
ATOM   2692  CB  ASP A 340      22.063  -8.227 -11.849  1.00 95.57           C  
ANISOU 2692  CB  ASP A 340    11965  12440  11909   -110   -113   -150       C  
ATOM   2693  CG  ASP A 340      22.922  -7.386 -12.814  1.00102.63           C  
ANISOU 2693  CG  ASP A 340    12854  13347  12795   -104   -101   -139       C  
ATOM   2694  OD1 ASP A 340      22.399  -6.413 -13.394  1.00105.65           O  
ANISOU 2694  OD1 ASP A 340    13227  13743  13171   -111   -111   -125       O  
ATOM   2695  OD2 ASP A 340      24.126  -7.705 -12.997  1.00 97.00           O1-
ANISOU 2695  OD2 ASP A 340    12145  12629  12083    -91    -82   -143       O1-
ATOM   2696  N   TYR A 341      21.572  -5.122 -10.310  1.00 99.60           N  
ANISOU 2696  N   TYR A 341    12418  12958  12467   -107   -134   -109       N  
ATOM   2697  CA  TYR A 341      22.010  -4.073  -9.399  1.00 96.16           C  
ANISOU 2697  CA  TYR A 341    11961  12519  12056   -100   -133    -98       C  
ATOM   2698  C   TYR A 341      20.869  -3.662  -8.492  1.00 96.51           C  
ANISOU 2698  C   TYR A 341    11997  12559  12114   -107   -148    -93       C  
ATOM   2699  O   TYR A 341      19.696  -3.806  -8.853  1.00115.98           O  
ANISOU 2699  O   TYR A 341    14468  15030  14570   -118   -160    -91       O  
ATOM   2700  CB  TYR A 341      22.411  -2.842 -10.197  1.00 97.49           C  
ANISOU 2700  CB  TYR A 341    12119  12699  12225    -99   -128    -82       C  
ATOM   2701  CG  TYR A 341      23.736  -2.931 -10.902  1.00 97.62           C  
ANISOU 2701  CG  TYR A 341    12138  12719  12235    -89   -110    -83       C  
ATOM   2702  CD1 TYR A 341      24.344  -4.159 -11.173  1.00 93.72           C  
ANISOU 2702  CD1 TYR A 341    11661  12221  11729    -84   -100    -97       C  
ATOM   2703  CD2 TYR A 341      24.374  -1.764 -11.328  1.00100.93           C  
ANISOU 2703  CD2 TYR A 341    12542  13144  12662    -85   -103    -67       C  
ATOM   2704  CE1 TYR A 341      25.557  -4.214 -11.825  1.00102.00           C  
ANISOU 2704  CE1 TYR A 341    12711  13272  12773    -74    -82    -96       C  
ATOM   2705  CE2 TYR A 341      25.587  -1.806 -11.981  1.00105.02           C  
ANISOU 2705  CE2 TYR A 341    13062  13666  13176    -76    -86    -66       C  
ATOM   2706  CZ  TYR A 341      26.175  -3.024 -12.231  1.00109.21           C  
ANISOU 2706  CZ  TYR A 341    13608  14193  13694    -70    -75    -80       C  
ATOM   2707  OH  TYR A 341      27.379  -3.036 -12.896  1.00122.26           O  
ANISOU 2707  OH  TYR A 341    15262  15849  15343    -59    -57    -76       O  
ATOM   2708  N   SER A 342      21.204  -3.110  -7.335  1.00 91.43           N  
ANISOU 2708  N   SER A 342    11340  11907  11493   -101   -148    -91       N  
ATOM   2709  CA  SER A 342      20.183  -2.559  -6.449  1.00101.66           C  
ANISOU 2709  CA  SER A 342    12627  13198  12803   -106   -159    -84       C  
ATOM   2710  C   SER A 342      19.663  -1.214  -6.981  1.00 95.24           C  
ANISOU 2710  C   SER A 342    11802  12393  11994   -110   -161    -66       C  
ATOM   2711  O   SER A 342      20.256  -0.620  -7.876  1.00 81.68           O  
ANISOU 2711  O   SER A 342    10080  10683  10271   -109   -154    -58       O  
ATOM   2712  CB  SER A 342      20.721  -2.419  -5.024  1.00108.97           C  
ANISOU 2712  CB  SER A 342    13543  14112  13748    -98   -157    -89       C  
ATOM   2713  OG  SER A 342      21.410  -1.197  -4.860  1.00116.46           O  
ANISOU 2713  OG  SER A 342    14478  15062  14711    -96   -151    -81       O  
ATOM   2714  N   VAL A 343      18.542  -0.746  -6.443  1.00101.71           N  
ANISOU 2714  N   VAL A 343    12614  13209  12822   -115   -170    -57       N  
ATOM   2715  CA  VAL A 343      18.015   0.552  -6.863  1.00104.32           C  
ANISOU 2715  CA  VAL A 343    12932  13545  13160   -118   -170    -37       C  
ATOM   2716  C   VAL A 343      18.951   1.651  -6.354  1.00109.18           C  
ANISOU 2716  C   VAL A 343    13535  14152  13794   -112   -159    -33       C  
ATOM   2717  O   VAL A 343      19.300   2.564  -7.095  1.00116.13           O  
ANISOU 2717  O   VAL A 343    14408  15039  14677   -111   -152    -20       O  
ATOM   2718  CB  VAL A 343      16.562   0.814  -6.393  1.00102.65           C  
ANISOU 2718  CB  VAL A 343    12716  13331  12956   -124   -180    -27       C  
ATOM   2719  CG1 VAL A 343      16.102   2.199  -6.831  1.00105.17           C  
ANISOU 2719  CG1 VAL A 343    13021  13654  13285   -125   -177     -3       C  
ATOM   2720  CG2 VAL A 343      15.609  -0.231  -6.956  1.00102.14           C  
ANISOU 2720  CG2 VAL A 343    12663  13275  12873   -133   -192    -29       C  
ATOM   2721  N   VAL A 344      19.376   1.550  -5.100  1.00105.56           N  
ANISOU 2721  N   VAL A 344    13075  13683  13351   -108   -158    -44       N  
ATOM   2722  CA  VAL A 344      20.272   2.563  -4.522  1.00108.45           C  
ANISOU 2722  CA  VAL A 344    13430  14041  13735   -105   -149    -43       C  
ATOM   2723  C   VAL A 344      21.621   2.724  -5.280  1.00 97.61           C  
ANISOU 2723  C   VAL A 344    12054  12676  12359   -101   -139    -43       C  
ATOM   2724  O   VAL A 344      22.119   3.832  -5.501  1.00 83.25           O  
ANISOU 2724  O   VAL A 344    10224  10855  10551   -101   -131    -33       O  
ATOM   2725  CB  VAL A 344      20.475   2.321  -3.006  1.00115.34           C  
ANISOU 2725  CB  VAL A 344    14303  14903  14620   -102   -152    -56       C  
ATOM   2726  CG1 VAL A 344      19.205   2.704  -2.248  1.00121.55           C  
ANISOU 2726  CG1 VAL A 344    15088  15681  15416   -106   -157    -51       C  
ATOM   2727  CG2 VAL A 344      20.835   0.876  -2.707  1.00113.50           C  
ANISOU 2727  CG2 VAL A 344    14079  14670  14375    -98   -156    -71       C  
ATOM   2728  N   LEU A 345      22.187   1.604  -5.696  1.00 94.75           N  
ANISOU 2728  N   LEU A 345    11701  12318  11981    -97   -138    -53       N  
ATOM   2729  CA  LEU A 345      23.398   1.574  -6.508  1.00 85.26           C  
ANISOU 2729  CA  LEU A 345    10498  11123  10773    -92   -127    -52       C  
ATOM   2730  C   LEU A 345      23.223   2.269  -7.860  1.00 88.49           C  
ANISOU 2730  C   LEU A 345    10906  11543  11174    -94   -122    -36       C  
ATOM   2731  O   LEU A 345      23.982   3.201  -8.157  1.00 99.64           O  
ANISOU 2731  O   LEU A 345    12306  12956  12597    -92   -113    -26       O  
ATOM   2732  CB  LEU A 345      23.788   0.114  -6.706  1.00 84.69           C  
ANISOU 2732  CB  LEU A 345    10441  11053  10686    -87   -126    -65       C  
ATOM   2733  CG  LEU A 345      24.786  -0.293  -7.763  1.00 84.24           C  
ANISOU 2733  CG  LEU A 345    10388  11003  10615    -81   -114    -65       C  
ATOM   2734  CD1 LEU A 345      26.105   0.441  -7.570  1.00 93.15           C  
ANISOU 2734  CD1 LEU A 345    11503  12132  11760    -76   -103    -60       C  
ATOM   2735  CD2 LEU A 345      24.986  -1.792  -7.655  1.00 81.46           C  
ANISOU 2735  CD2 LEU A 345    10052  10649  10251    -77   -112    -81       C  
ATOM   2736  N   LEU A 346      22.245   1.809  -8.669  1.00 88.62           N  
ANISOU 2736  N   LEU A 346    10932  11568  11172    -99   -129    -33       N  
ATOM   2737  CA  LEU A 346      21.826   2.485  -9.932  1.00 80.75           C  
ANISOU 2737  CA  LEU A 346     9933  10585  10165   -102   -127    -15       C  
ATOM   2738  C   LEU A 346      21.635   3.967  -9.654  1.00 81.68           C  
ANISOU 2738  C   LEU A 346    10033  10697  10304   -103   -124      2       C  
ATOM   2739  O   LEU A 346      22.009   4.797 -10.470  1.00 83.54           O  
ANISOU 2739  O   LEU A 346    10260  10939  10540   -101   -115     17       O  
ATOM   2740  CB  LEU A 346      20.497   1.923 -10.519  1.00 76.06           C  
ANISOU 2740  CB  LEU A 346     9349  10000   9550   -111   -140    -13       C  
ATOM   2741  CG  LEU A 346      20.380   0.536 -11.205  1.00 83.39           C  
ANISOU 2741  CG  LEU A 346    10297  10936  10451   -115   -144    -27       C  
ATOM   2742  CD1 LEU A 346      18.953   0.024 -11.275  1.00 77.29           C  
ANISOU 2742  CD1 LEU A 346     9531  10168   9667   -126   -160    -27       C  
ATOM   2743  CD2 LEU A 346      20.969   0.499 -12.620  1.00 87.74           C  
ANISOU 2743  CD2 LEU A 346    10855  11502  10980   -113   -135    -23       C  
ATOM   2744  N   LEU A 347      21.053   4.269  -8.485  1.00 82.88           N  
ANISOU 2744  N   LEU A 347    10180  10836  10473   -105   -129      0       N  
ATOM   2745  CA  LEU A 347      20.795   5.634  -8.035  1.00 82.54           C  
ANISOU 2745  CA  LEU A 347    10123  10785  10454   -106   -124     13       C  
ATOM   2746  C   LEU A 347      22.068   6.397  -7.717  1.00 85.33           C  
ANISOU 2746  C   LEU A 347    10466  11130  10824   -103   -112     12       C  
ATOM   2747  O   LEU A 347      22.166   7.589  -8.019  1.00 76.63           O  
ANISOU 2747  O   LEU A 347     9353  10026   9737   -103   -103     27       O  
ATOM   2748  CB  LEU A 347      19.932   5.629  -6.778  1.00 88.05           C  
ANISOU 2748  CB  LEU A 347    10821  11470  11164   -108   -132      8       C  
ATOM   2749  CG  LEU A 347      18.420   5.488  -6.901  1.00100.83           C  
ANISOU 2749  CG  LEU A 347    12442  13093  12778   -113   -141     18       C  
ATOM   2750  CD1 LEU A 347      17.803   5.936  -5.573  1.00106.86           C  
ANISOU 2750  CD1 LEU A 347    13201  13840  13562   -113   -142     16       C  
ATOM   2751  CD2 LEU A 347      17.826   6.271  -8.078  1.00105.84           C  
ANISOU 2751  CD2 LEU A 347    13068  13739  13408   -114   -139     43       C  
ATOM   2752  N   ARG A 348      23.008   5.712  -7.062  1.00 90.99           N  
ANISOU 2752  N   ARG A 348    11186  11843  11541   -100   -113     -6       N  
ATOM   2753  CA  ARG A 348      24.326   6.262  -6.791  1.00 86.58           C  
ANISOU 2753  CA  ARG A 348    10618  11280  10998    -98   -103     -8       C  
ATOM   2754  C   ARG A 348      24.953   6.627  -8.121  1.00 78.44           C  
ANISOU 2754  C   ARG A 348     9583  10260   9961    -95    -92      6       C  
ATOM   2755  O   ARG A 348      25.361   7.762  -8.317  1.00 80.62           O  
ANISOU 2755  O   ARG A 348     9847  10533  10253    -96    -83     18       O  
ATOM   2756  CB  ARG A 348      25.202   5.263  -6.014  1.00100.42           C  
ANISOU 2756  CB  ARG A 348    12374  13031  12748    -95   -106    -26       C  
ATOM   2757  CG  ARG A 348      25.112   5.406  -4.490  1.00117.02           C  
ANISOU 2757  CG  ARG A 348    14475  15122  14866    -99   -112    -37       C  
ATOM   2758  CD  ARG A 348      25.575   4.156  -3.747  1.00126.47           C  
ANISOU 2758  CD  ARG A 348    15677  16319  16055    -95   -118    -53       C  
ATOM   2759  NE  ARG A 348      24.813   3.894  -2.515  1.00141.74           N  
ANISOU 2759  NE  ARG A 348    17617  18246  17993    -97   -128    -63       N  
ATOM   2760  CZ  ARG A 348      24.679   2.692  -1.940  1.00163.40           C  
ANISOU 2760  CZ  ARG A 348    20368  20989  20726    -93   -135    -74       C  
ATOM   2761  NH1 ARG A 348      25.255   1.614  -2.468  1.00185.78           N1+
ANISOU 2761  NH1 ARG A 348    23209  23831  23548    -87   -132    -78       N1+
ATOM   2762  NH2 ARG A 348      23.969   2.556  -0.824  1.00153.12           N  
ANISOU 2762  NH2 ARG A 348    19069  19679  19428    -95   -142    -81       N  
ATOM   2763  N   LEU A 349      24.960   5.678  -9.050  1.00 78.20           N  
ANISOU 2763  N   LEU A 349     9564  10243   9907    -91    -93      4       N  
ATOM   2764  CA  LEU A 349      25.620   5.876 -10.343  1.00 88.51           C  
ANISOU 2764  CA  LEU A 349    10867  11559  11202    -87    -82     16       C  
ATOM   2765  C   LEU A 349      25.013   7.040 -11.140  1.00 90.36           C  
ANISOU 2765  C   LEU A 349    11093  11799  11441    -89    -77     39       C  
ATOM   2766  O   LEU A 349      25.745   7.821 -11.735  1.00112.15           O  
ANISOU 2766  O   LEU A 349    13843  14561  14208    -86    -65     52       O  
ATOM   2767  CB  LEU A 349      25.640   4.590 -11.188  1.00 93.84           C  
ANISOU 2767  CB  LEU A 349    11560  12246  11848    -83    -83      8       C  
ATOM   2768  CG  LEU A 349      25.829   3.232 -10.475  1.00 95.12           C  
ANISOU 2768  CG  LEU A 349    11735  12404  12003    -81    -88    -13       C  
ATOM   2769  CD1 LEU A 349      26.050   2.094 -11.475  1.00 96.68           C  
ANISOU 2769  CD1 LEU A 349    11950  12611  12174    -77    -83    -20       C  
ATOM   2770  CD2 LEU A 349      26.944   3.265  -9.432  1.00 91.97           C  
ANISOU 2770  CD2 LEU A 349    11325  11994  11624    -77    -84    -21       C  
ATOM   2771  N   ALA A 350      23.694   7.178 -11.127  1.00 93.62           N  
ANISOU 2771  N   ALA A 350    11509  12214  11850    -94    -87     45       N  
ATOM   2772  CA  ALA A 350      23.019   8.314 -11.794  1.00 95.19           C  
ANISOU 2772  CA  ALA A 350    11697  12417  12055    -95    -82     70       C  
ATOM   2773  C   ALA A 350      23.282   9.672 -11.121  1.00 95.53           C  
ANISOU 2773  C   ALA A 350    11723  12443  12129    -96    -72     79       C  
ATOM   2774  O   ALA A 350      23.272  10.706 -11.786  1.00 95.05           O  
ANISOU 2774  O   ALA A 350    11652  12384  12077    -94    -62    100       O  
ATOM   2775  CB  ALA A 350      21.515   8.064 -11.891  1.00 94.77           C  
ANISOU 2775  CB  ALA A 350    11649  12370  11990   -100    -95     77       C  
ATOM   2776  N   LYS A 351      23.486   9.675  -9.807  1.00 98.81           N  
ANISOU 2776  N   LYS A 351    12139  12842  12562    -98    -75     63       N  
ATOM   2777  CA  LYS A 351      23.959  10.879  -9.109  1.00 94.59           C  
ANISOU 2777  CA  LYS A 351    11591  12290  12057   -101    -65     66       C  
ATOM   2778  C   LYS A 351      25.435  11.125  -9.480  1.00 91.88           C  
ANISOU 2778  C   LYS A 351    11241  11950  11721    -99    -54     66       C  
ATOM   2779  O   LYS A 351      25.832  12.251  -9.762  1.00 90.24           O  
ANISOU 2779  O   LYS A 351    11021  11736  11531    -99    -41     80       O  
ATOM   2780  CB  LYS A 351      23.735  10.760  -7.592  1.00 86.14           C  
ANISOU 2780  CB  LYS A 351    10525  11205  11000   -106    -72     48       C  
ATOM   2781  CG  LYS A 351      24.210  11.922  -6.745  1.00 83.51           C  
ANISOU 2781  CG  LYS A 351    10182  10853  10695   -111    -63     46       C  
ATOM   2782  CD  LYS A 351      23.593  13.263  -7.097  1.00 84.59           C  
ANISOU 2782  CD  LYS A 351    10309  10980  10850   -112    -50     67       C  
ATOM   2783  CE  LYS A 351      24.347  14.409  -6.407  1.00 90.21           C  
ANISOU 2783  CE  LYS A 351    11012  11673  11591   -118    -38     63       C  
ATOM   2784  NZ  LYS A 351      24.186  15.745  -7.067  1.00 89.28           N1+
ANISOU 2784  NZ  LYS A 351    10882  11547  11492   -118    -21     87       N1+
ATOM   2785  N   THR A 352      26.223  10.059  -9.528  1.00 95.69           N  
ANISOU 2785  N   THR A 352    11730  12440  12189    -95    -58     52       N  
ATOM   2786  CA  THR A 352      27.625  10.145  -9.939  1.00106.70           C  
ANISOU 2786  CA  THR A 352    13117  13837  13587    -92    -47     54       C  
ATOM   2787  C   THR A 352      27.807  10.648 -11.385  1.00101.49           C  
ANISOU 2787  C   THR A 352    12452  13190  12921    -86    -35     76       C  
ATOM   2788  O   THR A 352      28.713  11.427 -11.657  1.00107.93           O  
ANISOU 2788  O   THR A 352    13255  14002  13752    -85    -22     86       O  
ATOM   2789  CB  THR A 352      28.362   8.793  -9.731  1.00119.90           C  
ANISOU 2789  CB  THR A 352    14797  15516  15243    -87    -52     37       C  
ATOM   2790  CG2 THR A 352      29.889   8.966  -9.780  1.00128.29           C  
ANISOU 2790  CG2 THR A 352    15848  16579  16318    -84    -41     38       C  
ATOM   2791  OG1 THR A 352      28.002   8.232  -8.457  1.00124.98           O  
ANISOU 2791  OG1 THR A 352    15447  16151  15890    -91    -64     18       O  
ATOM   2792  N   TYR A 353      26.951  10.227 -12.304  1.00105.08           N  
ANISOU 2792  N   TYR A 353    12916  13658  13351    -83    -38     84       N  
ATOM   2793  CA  TYR A 353      27.010  10.723 -13.687  1.00110.89           C  
ANISOU 2793  CA  TYR A 353    13648  14407  14078    -79    -27    107       C  
ATOM   2794  C   TYR A 353      26.627  12.209 -13.773  1.00107.85           C  
ANISOU 2794  C   TYR A 353    13247  14014  13716    -81    -18    129       C  
ATOM   2795  O   TYR A 353      27.194  12.954 -14.578  1.00102.92           O  
ANISOU 2795  O   TYR A 353    12613  13394  13099    -76     -4    147       O  
ATOM   2796  CB  TYR A 353      26.092   9.895 -14.594  1.00111.50           C  
ANISOU 2796  CB  TYR A 353    13740  14503  14122    -78    -36    109       C  
ATOM   2797  CG  TYR A 353      26.082  10.323 -16.052  1.00107.36           C  
ANISOU 2797  CG  TYR A 353    13213  13996  13582    -73    -26    132       C  
ATOM   2798  CD1 TYR A 353      27.069   9.908 -16.925  1.00109.67           C  
ANISOU 2798  CD1 TYR A 353    13510  14299  13859    -66    -16    133       C  
ATOM   2799  CD2 TYR A 353      25.077  11.119 -16.558  1.00104.44           C  
ANISOU 2799  CD2 TYR A 353    12836  13633  13212    -75    -27    155       C  
ATOM   2800  CE1 TYR A 353      27.062  10.280 -18.263  1.00102.00           C  
ANISOU 2800  CE1 TYR A 353    12538  13346  12872    -61     -6    154       C  
ATOM   2801  CE2 TYR A 353      25.069  11.502 -17.891  1.00 99.68           C  
ANISOU 2801  CE2 TYR A 353    12231  13049  12595    -70    -19    178       C  
ATOM   2802  CZ  TYR A 353      26.067  11.082 -18.736  1.00 94.64           C  
ANISOU 2802  CZ  TYR A 353    11598  12421  11939    -63     -9    176       C  
ATOM   2803  OH  TYR A 353      26.061  11.459 -20.057  1.00 86.77           O  
ANISOU 2803  OH  TYR A 353    10600  11444  10925    -58      0    199       O  
ATOM   2804  N   GLU A 354      25.659  12.614 -12.946  1.00 97.51           N  
ANISOU 2804  N   GLU A 354    11936  12692  12419    -86    -25    127       N  
ATOM   2805  CA  GLU A 354      25.210  14.010 -12.865  1.00 91.23           C  
ANISOU 2805  CA  GLU A 354    11127  11885  11650    -88    -15    147       C  
ATOM   2806  C   GLU A 354      26.364  14.883 -12.411  1.00 93.02           C  
ANISOU 2806  C   GLU A 354    11342  12096  11906    -90     -1    145       C  
ATOM   2807  O   GLU A 354      26.689  15.880 -13.073  1.00 96.90           O  
ANISOU 2807  O   GLU A 354    11821  12586  12411    -88     14    167       O  
ATOM   2808  CB  GLU A 354      24.015  14.160 -11.888  1.00 94.57           C  
ANISOU 2808  CB  GLU A 354    11553  12295  12083    -93    -23    142       C  
ATOM   2809  CG  GLU A 354      23.322  15.548 -11.838  1.00 91.04           C  
ANISOU 2809  CG  GLU A 354    11094  11836  11661    -93    -11    165       C  
ATOM   2810  CD  GLU A 354      22.182  15.651 -10.789  1.00 92.17           C  
ANISOU 2810  CD  GLU A 354    11241  11964  11814    -97    -17    159       C  
ATOM   2811  OE1 GLU A 354      22.249  14.981  -9.740  1.00 92.52           O  
ANISOU 2811  OE1 GLU A 354    11295  12001  11858   -101    -28    134       O  
ATOM   2812  OE2 GLU A 354      21.203  16.409 -10.976  1.00 90.77           O1-
ANISOU 2812  OE2 GLU A 354    11057  11783  11647    -95    -11    181       O1-
ATOM   2813  N   THR A 355      26.994  14.504 -11.297  1.00 90.80           N  
ANISOU 2813  N   THR A 355    11063  11804  11633    -96     -7    122       N  
ATOM   2814  CA  THR A 355      28.036  15.342 -10.701  1.00 94.37           C  
ANISOU 2814  CA  THR A 355    11503  12240  12114   -102      3    118       C  
ATOM   2815  C   THR A 355      29.250  15.530 -11.632  1.00 95.53           C  
ANISOU 2815  C   THR A 355    11640  12395  12262    -97     15    130       C  
ATOM   2816  O   THR A 355      29.902  16.586 -11.597  1.00 97.86           O  
ANISOU 2816  O   THR A 355    11921  12678  12583   -101     28    139       O  
ATOM   2817  CB  THR A 355      28.500  14.824  -9.319  1.00 99.36           C  
ANISOU 2817  CB  THR A 355    12139  12862  12751   -109     -9     90       C  
ATOM   2818  CG2 THR A 355      27.397  15.009  -8.264  1.00 93.76           C  
ANISOU 2818  CG2 THR A 355    11437  12139  12049   -115    -16     81       C  
ATOM   2819  OG1 THR A 355      28.870  13.443  -9.412  1.00113.39           O  
ANISOU 2819  OG1 THR A 355    13926  14654  14504   -104    -19     77       O  
ATOM   2820  N   THR A 356      29.532  14.521 -12.463  1.00 86.71           N  
ANISOU 2820  N   THR A 356    10531  11298  11118    -88     13    130       N  
ATOM   2821  CA  THR A 356      30.594  14.599 -13.458  1.00 80.27           C  
ANISOU 2821  CA  THR A 356     9707  10492  10300    -81     26    143       C  
ATOM   2822  C   THR A 356      30.229  15.551 -14.560  1.00 79.04           C  
ANISOU 2822  C   THR A 356     9543  10341  10147    -76     40    172       C  
ATOM   2823  O   THR A 356      31.047  16.341 -14.987  1.00 74.83           O  
ANISOU 2823  O   THR A 356     8996   9804   9631    -75     55    187       O  
ATOM   2824  CB  THR A 356      30.835  13.252 -14.150  1.00 82.40           C  
ANISOU 2824  CB  THR A 356     9991  10781  10537    -72     22    137       C  
ATOM   2825  CG2 THR A 356      32.131  13.299 -14.939  1.00 82.30           C  
ANISOU 2825  CG2 THR A 356     9969  10775  10525    -65     37    147       C  
ATOM   2826  OG1 THR A 356      30.886  12.206 -13.178  1.00 84.69           O  
ANISOU 2826  OG1 THR A 356    10290  11068  10819    -75      8    111       O  
ATOM   2827  N   LEU A 357      28.996  15.444 -15.047  1.00 90.67           N  
ANISOU 2827  N   LEU A 357    11024  11823  11602    -74     34    181       N  
ATOM   2828  CA  LEU A 357      28.548  16.265 -16.162  1.00 90.51           C  
ANISOU 2828  CA  LEU A 357    10997  11812  11582    -68     46    211       C  
ATOM   2829  C   LEU A 357      28.482  17.704 -15.757  1.00 86.73           C  
ANISOU 2829  C   LEU A 357    10501  11312  11139    -73     59    226       C  
ATOM   2830  O   LEU A 357      28.834  18.594 -16.538  1.00 91.49           O  
ANISOU 2830  O   LEU A 357    11092  11916  11754    -68     76    250       O  
ATOM   2831  CB  LEU A 357      27.206  15.791 -16.716  1.00 94.46           C  
ANISOU 2831  CB  LEU A 357    11507  12329  12054    -66     34    219       C  
ATOM   2832  CG  LEU A 357      27.397  14.743 -17.823  1.00112.65           C  
ANISOU 2832  CG  LEU A 357    13824  14658  14319    -60     31    219       C  
ATOM   2833  CD1 LEU A 357      26.109  14.595 -18.609  1.00119.99           C  
ANISOU 2833  CD1 LEU A 357    14760  15607  15225    -60     22    234       C  
ATOM   2834  CD2 LEU A 357      28.555  15.076 -18.780  1.00117.43           C  
ANISOU 2834  CD2 LEU A 357    14421  15271  14925    -52     49    233       C  
ATOM   2835  N   GLU A 358      28.076  17.933 -14.520  1.00 83.20           N  
ANISOU 2835  N   GLU A 358    10055  10845  10710    -81     52    210       N  
ATOM   2836  CA  GLU A 358      28.085  19.270 -13.986  1.00 84.64           C  
ANISOU 2836  CA  GLU A 358    10226  11005  10930    -87     66    218       C  
ATOM   2837  C   GLU A 358      29.505  19.800 -13.971  1.00 83.21           C  
ANISOU 2837  C   GLU A 358    10033  10814  10770    -90     79    218       C  
ATOM   2838  O   GLU A 358      29.727  20.965 -14.295  1.00 89.35           O  
ANISOU 2838  O   GLU A 358    10796  11580  11572    -91     97    237       O  
ATOM   2839  CB  GLU A 358      27.446  19.316 -12.598  1.00 89.58           C  
ANISOU 2839  CB  GLU A 358    10859  11611  11568    -97     57    198       C  
ATOM   2840  CG  GLU A 358      25.922  19.400 -12.644  1.00103.26           C  
ANISOU 2840  CG  GLU A 358    12596  13344  13294    -93     52    209       C  
ATOM   2841  CD  GLU A 358      25.412  20.746 -13.168  1.00118.23           C  
ANISOU 2841  CD  GLU A 358    14478  15231  15212    -90     72    240       C  
ATOM   2842  OE1 GLU A 358      25.926  21.781 -12.719  1.00147.04           O  
ANISOU 2842  OE1 GLU A 358    18119  18857  18893    -95     88    241       O  
ATOM   2843  OE2 GLU A 358      24.504  20.793 -14.028  1.00110.49           O1-
ANISOU 2843  OE2 GLU A 358    13497  14266  14219    -82     73    265       O1-
ATOM   2844  N   LYS A 359      30.469  18.942 -13.644  1.00 81.18           N  
ANISOU 2844  N   LYS A 359     9779  10563  10504    -92     70    198       N  
ATOM   2845  CA  LYS A 359      31.886  19.336 -13.627  1.00 84.25           C  
ANISOU 2845  CA  LYS A 359    10154  10945  10912    -96     81    198       C  
ATOM   2846  C   LYS A 359      32.438  19.649 -15.010  1.00 90.90           C  
ANISOU 2846  C   LYS A 359    10986  11801  11751    -85     97    225       C  
ATOM   2847  O   LYS A 359      33.323  20.480 -15.129  1.00112.51           O  
ANISOU 2847  O   LYS A 359    13708  14528  14513    -88    112    236       O  
ATOM   2848  CB  LYS A 359      32.763  18.281 -12.918  1.00 80.86           C  
ANISOU 2848  CB  LYS A 359     9729  10521  10474    -99     67    173       C  
ATOM   2849  CG  LYS A 359      34.200  18.143 -13.422  1.00 77.19           C  
ANISOU 2849  CG  LYS A 359     9252  10064  10012    -96     77    179       C  
ATOM   2850  CD  LYS A 359      35.012  17.091 -12.660  1.00 80.08           C  
ANISOU 2850  CD  LYS A 359     9622  10435  10371    -98     64    156       C  
ATOM   2851  CE  LYS A 359      36.304  16.672 -13.380  1.00 84.08           C  
ANISOU 2851  CE  LYS A 359    10119  10954  10873    -90     74    166       C  
ATOM   2852  NZ  LYS A 359      36.179  15.695 -14.535  1.00 82.76           N1+
ANISOU 2852  NZ  LYS A 359     9963  10807  10672    -73     77    173       N1+
ATOM   2853  N   CYS A 360      31.925  19.019 -16.057  1.00 97.95           N  
ANISOU 2853  N   CYS A 360    11888  12716  12612    -73     96    237       N  
ATOM   2854  CA  CYS A 360      32.550  19.155 -17.375  1.00108.85           C  
ANISOU 2854  CA  CYS A 360    13262  14112  13984    -62    111    260       C  
ATOM   2855  C   CYS A 360      32.001  20.272 -18.269  1.00116.35           C  
ANISOU 2855  C   CYS A 360    14202  15063  14944    -56    127    293       C  
ATOM   2856  O   CYS A 360      32.768  21.004 -18.910  1.00105.08           O  
ANISOU 2856  O   CYS A 360    12759  13634  13532    -52    146    314       O  
ATOM   2857  CB  CYS A 360      32.496  17.817 -18.101  1.00112.15           C  
ANISOU 2857  CB  CYS A 360    13696  14555  14361    -53    103    254       C  
ATOM   2858  SG  CYS A 360      33.746  16.685 -17.458  1.00116.04           S  
ANISOU 2858  SG  CYS A 360    14193  15048  14849    -54     96    227       S  
ATOM   2859  N   CYS A 361      30.681  20.414 -18.294  1.00120.36           N  
ANISOU 2859  N   CYS A 361    14715  15573  15443    -56    121    300       N  
ATOM   2860  CA  CYS A 361      30.028  21.165 -19.365  1.00131.89           C  
ANISOU 2860  CA  CYS A 361    16168  17043  16902    -48    133    335       C  
ATOM   2861  C   CYS A 361      30.467  22.602 -19.539  1.00132.75           C  
ANISOU 2861  C   CYS A 361    16257  17134  17048    -47    157    359       C  
ATOM   2862  O   CYS A 361      30.208  23.181 -20.600  1.00128.36           O  
ANISOU 2862  O   CYS A 361    15693  16590  16489    -37    170    391       O  
ATOM   2863  CB  CYS A 361      28.509  21.115 -19.222  1.00139.61           C  
ANISOU 2863  CB  CYS A 361    17153  18025  17868    -48    122    339       C  
ATOM   2864  SG  CYS A 361      27.832  19.553 -19.795  1.00158.71           S  
ANISOU 2864  SG  CYS A 361    19592  20475  20233    -45     99    328       S  
ATOM   2865  N   ALA A 362      31.107  23.176 -18.517  1.00127.08           N  
ANISOU 2865  N   ALA A 362    15531  16389  16364    -58    162    344       N  
ATOM   2866  CA  ALA A 362      31.590  24.560 -18.592  1.00122.59           C  
ANISOU 2866  CA  ALA A 362    14944  15800  15836    -60    185    364       C  
ATOM   2867  C   ALA A 362      33.096  24.687 -18.371  1.00119.31           C  
ANISOU 2867  C   ALA A 362    14518  15375  15440    -67    192    355       C  
ATOM   2868  O   ALA A 362      33.698  25.713 -18.725  1.00111.78           O  
ANISOU 2868  O   ALA A 362    13548  14409  14515    -67    213    375       O  
ATOM   2869  CB  ALA A 362      30.833  25.434 -17.607  1.00113.45           C  
ANISOU 2869  CB  ALA A 362    13785  14613  14708    -70    188    360       C  
ATOM   2870  N   ALA A 363      33.697  23.649 -17.793  1.00115.20           N  
ANISOU 2870  N   ALA A 363    14006  14861  14905    -71    176    327       N  
ATOM   2871  CA  ALA A 363      35.128  23.636 -17.556  1.00118.36           C  
ANISOU 2871  CA  ALA A 363    14396  15255  15321    -77    181    319       C  
ATOM   2872  C   ALA A 363      35.854  23.262 -18.846  1.00123.43           C  
ANISOU 2872  C   ALA A 363    15033  15921  15945    -62    192    340       C  
ATOM   2873  O   ALA A 363      35.243  22.748 -19.798  1.00123.09           O  
ANISOU 2873  O   ALA A 363    15000  15900  15870    -49    191    352       O  
ATOM   2874  CB  ALA A 363      35.483  22.675 -16.426  1.00111.24           C  
ANISOU 2874  CB  ALA A 363    13503  14353  14411    -87    159    284       C  
ATOM   2875  N   ALA A 364      37.157  23.543 -18.850  1.00121.04           N  
ANISOU 2875  N   ALA A 364    14715  15612  15663    -65    202    343       N  
ATOM   2876  CA  ALA A 364      38.078  23.296 -19.962  1.00116.34           C  
ANISOU 2876  CA  ALA A 364    14112  15034  15058    -52    217    363       C  
ATOM   2877  C   ALA A 364      37.603  22.367 -21.121  1.00123.35           C  
ANISOU 2877  C   ALA A 364    15015  15951  15900    -33    216    372       C  
ATOM   2878  O   ALA A 364      37.114  22.881 -22.122  1.00120.00           O  
ANISOU 2878  O   ALA A 364    14589  15537  15469    -23    228    399       O  
ATOM   2879  CB  ALA A 364      39.424  22.845 -19.398  1.00114.27           C  
ANISOU 2879  CB  ALA A 364    13840  14769  14806    -58    214    348       C  
ATOM   2880  N   ASP A 365      37.749  21.036 -21.006  1.00132.52           N  
ANISOU 2880  N   ASP A 365    16193  17128  17031    -30    201    351       N  
ATOM   2881  CA  ASP A 365      37.460  20.096 -22.142  1.00130.52           C  
ANISOU 2881  CA  ASP A 365    15957  16903  16733    -14    202    358       C  
ATOM   2882  C   ASP A 365      36.469  18.953 -21.809  1.00113.53           C  
ANISOU 2882  C   ASP A 365    13829  14761  14547    -15    179    333       C  
ATOM   2883  O   ASP A 365      36.870  17.839 -21.406  1.00 99.99           O  
ANISOU 2883  O   ASP A 365    12126  13051  12817    -15    169    310       O  
ATOM   2884  CB  ASP A 365      38.757  19.504 -22.725  1.00136.31           C  
ANISOU 2884  CB  ASP A 365    16686  17646  17458     -3    215    362       C  
ATOM   2885  CG  ASP A 365      38.534  18.786 -24.059  1.00131.44           C  
ANISOU 2885  CG  ASP A 365    16086  17057  16799     13    222    373       C  
ATOM   2886  OD1 ASP A 365      37.403  18.835 -24.596  1.00129.41           O  
ANISOU 2886  OD1 ASP A 365    15840  16811  16518     16    217    380       O  
ATOM   2887  OD2 ASP A 365      39.495  18.168 -24.570  1.00129.56           O1-
ANISOU 2887  OD2 ASP A 365    15850  16829  16549     24    233    375       O1-
ATOM   2888  N   PRO A 366      35.175  19.216 -22.020  1.00 99.25           N  
ANISOU 2888  N   PRO A 366    12027  12956  12726    -16    172    340       N  
ATOM   2889  CA  PRO A 366      34.122  18.293 -21.659  1.00105.54           C  
ANISOU 2889  CA  PRO A 366    12844  13760  13495    -20    151    319       C  
ATOM   2890  C   PRO A 366      34.316  16.830 -22.137  1.00108.89           C  
ANISOU 2890  C   PRO A 366    13289  14204  13879    -13    144    304       C  
ATOM   2891  O   PRO A 366      34.374  15.934 -21.304  1.00 96.87           O  
ANISOU 2891  O   PRO A 366    11777  12677  12351    -18    130    276       O  
ATOM   2892  CB  PRO A 366      32.899  18.954 -22.267  1.00104.99           C  
ANISOU 2892  CB  PRO A 366    12774  13698  13418    -18    151    342       C  
ATOM   2893  CG  PRO A 366      33.194  20.403 -22.108  1.00104.17           C  
ANISOU 2893  CG  PRO A 366    12648  13576  13357    -21    168    363       C  
ATOM   2894  CD  PRO A 366      34.620  20.481 -22.520  1.00 98.54           C  
ANISOU 2894  CD  PRO A 366    11924  12863  12654    -15    185    370       C  
ATOM   2895  N   HIS A 367      34.450  16.587 -23.436  1.00116.43           N  
ANISOU 2895  N   HIS A 367    14251  15182  14807     -1    155    320       N  
ATOM   2896  CA  HIS A 367      34.683  15.222 -23.943  1.00108.56           C  
ANISOU 2896  CA  HIS A 367    13276  14202  13771      6    152    304       C  
ATOM   2897  C   HIS A 367      35.794  14.538 -23.223  1.00 93.48           C  
ANISOU 2897  C   HIS A 367    11365  12281  11873      6    154    284       C  
ATOM   2898  O   HIS A 367      35.758  13.346 -23.071  1.00 87.90           O  
ANISOU 2898  O   HIS A 367    10677  11579  11143      7    145    262       O  
ATOM   2899  CB  HIS A 367      35.047  15.216 -25.435  1.00128.59           C  
ANISOU 2899  CB  HIS A 367    15815  16760  16282     19    170    327       C  
ATOM   2900  CG  HIS A 367      33.891  15.504 -26.343  1.00151.81           C  
ANISOU 2900  CG  HIS A 367    18764  19721  19198     20    166    345       C  
ATOM   2901  CD2 HIS A 367      32.902  14.707 -26.813  1.00151.34           C  
ANISOU 2901  CD2 HIS A 367    18726  19680  19098     18    151    336       C  
ATOM   2902  ND1 HIS A 367      33.663  16.755 -26.879  1.00157.36           N  
ANISOU 2902  ND1 HIS A 367    19448  20426  19916     23    178    377       N  
ATOM   2903  CE1 HIS A 367      32.577  16.719 -27.630  1.00153.04           C  
ANISOU 2903  CE1 HIS A 367    18909  19899  19338     23    170    390       C  
ATOM   2904  NE2 HIS A 367      32.093  15.490 -27.599  1.00151.25           N  
ANISOU 2904  NE2 HIS A 367    18707  19684  19077     19    153    364       N  
ATOM   2905  N   GLU A 368      36.797  15.292 -22.803  1.00101.64           N  
ANISOU 2905  N   GLU A 368    12377  13300  12943      5    165    293       N  
ATOM   2906  CA  GLU A 368      37.994  14.698 -22.244  1.00119.50           C  
ANISOU 2906  CA  GLU A 368    14634  15554  15216      7    169    279       C  
ATOM   2907  C   GLU A 368      37.768  14.296 -20.801  1.00118.11           C  
ANISOU 2907  C   GLU A 368    14460  15364  15053     -5    148    252       C  
ATOM   2908  O   GLU A 368      38.081  13.162 -20.427  1.00115.36           O  
ANISOU 2908  O   GLU A 368    14123  15017  14690     -3    142    232       O  
ATOM   2909  CB  GLU A 368      39.199  15.648 -22.349  1.00128.65           C  
ANISOU 2909  CB  GLU A 368    15767  16705  16410      9    188    300       C  
ATOM   2910  CG  GLU A 368      40.556  14.933 -22.273  1.00128.73           C  
ANISOU 2910  CG  GLU A 368    15772  16716  16423     17    198    295       C  
ATOM   2911  CD  GLU A 368      41.719  15.846 -21.911  1.00132.78           C  
ANISOU 2911  CD  GLU A 368    16256  17216  16978     13    210    310       C  
ATOM   2912  OE1 GLU A 368      41.482  17.022 -21.561  1.00147.72           O  
ANISOU 2912  OE1 GLU A 368    18132  19095  18898      2    209    319       O  
ATOM   2913  OE2 GLU A 368      42.884  15.386 -21.964  1.00128.27           O1-
ANISOU 2913  OE2 GLU A 368    15676  16647  16412     20    221    313       O1-
ATOM   2914  N   CYS A 369      37.228  15.217 -19.998  1.00116.02           N  
ANISOU 2914  N   CYS A 369    14184  15084  14814    -18    139    252       N  
ATOM   2915  CA  CYS A 369      37.017  14.963 -18.566  1.00125.08           C  
ANISOU 2915  CA  CYS A 369    15332  16216  15975    -31    121    227       C  
ATOM   2916  C   CYS A 369      35.890  13.958 -18.300  1.00126.88           C  
ANISOU 2916  C   CYS A 369    15584  16451  16174    -32    102    207       C  
ATOM   2917  O   CYS A 369      36.031  13.093 -17.437  1.00142.23           O  
ANISOU 2917  O   CYS A 369    17536  18392  18115    -35     90    184       O  
ATOM   2918  CB  CYS A 369      36.744  16.257 -17.802  1.00125.94           C  
ANISOU 2918  CB  CYS A 369    15426  16306  16119    -44    119    231       C  
ATOM   2919  SG  CYS A 369      35.407  17.270 -18.476  1.00143.99           S  
ANISOU 2919  SG  CYS A 369    17713  18592  18404    -44    123    252       S  
ATOM   2920  N   TYR A 370      34.782  14.053 -19.032  1.00112.44           N  
ANISOU 2920  N   TYR A 370    13766  14632  14324    -30    100    216       N  
ATOM   2921  CA  TYR A 370      33.711  13.091 -18.842  1.00 97.90           C  
ANISOU 2921  CA  TYR A 370    11946  12798  12455    -32     82    198       C  
ATOM   2922  C   TYR A 370      33.923  11.744 -19.551  1.00 96.45           C  
ANISOU 2922  C   TYR A 370    11782  12629  12234    -23     83    188       C  
ATOM   2923  O   TYR A 370      33.234  10.790 -19.241  1.00126.20           O  
ANISOU 2923  O   TYR A 370    15567  16400  15982    -26     68    169       O  
ATOM   2924  CB  TYR A 370      32.346  13.701 -19.166  1.00 93.80           C  
ANISOU 2924  CB  TYR A 370    11429  12282  11930    -36     75    210       C  
ATOM   2925  CG  TYR A 370      31.979  13.940 -20.615  1.00 97.84           C  
ANISOU 2925  CG  TYR A 370    11943  12813  12418    -28     85    234       C  
ATOM   2926  CD1 TYR A 370      31.973  12.911 -21.550  1.00 99.47           C  
ANISOU 2926  CD1 TYR A 370    12169  13040  12586    -21     85    230       C  
ATOM   2927  CD2 TYR A 370      31.533  15.198 -21.029  1.00107.02           C  
ANISOU 2927  CD2 TYR A 370    13091  13975  13596    -28     93    261       C  
ATOM   2928  CE1 TYR A 370      31.594  13.143 -22.857  1.00104.62           C  
ANISOU 2928  CE1 TYR A 370    12823  13712  13214    -15     92    252       C  
ATOM   2929  CE2 TYR A 370      31.153  15.439 -22.342  1.00103.44           C  
ANISOU 2929  CE2 TYR A 370    12639  13542  13120    -21    101    286       C  
ATOM   2930  CZ  TYR A 370      31.174  14.406 -23.253  1.00104.58           C  
ANISOU 2930  CZ  TYR A 370    12802  13709  13225    -15    100    281       C  
ATOM   2931  OH  TYR A 370      30.802  14.628 -24.565  1.00 98.84           O  
ANISOU 2931  OH  TYR A 370    12078  13005  12472     -9    106    304       O  
ATOM   2932  N   ALA A 371      34.878  11.652 -20.462  1.00 82.07           N  
ANISOU 2932  N   ALA A 371     9958  10817  10406    -12    101    200       N  
ATOM   2933  CA  ALA A 371      35.075  10.452 -21.270  1.00 83.89           C  
ANISOU 2933  CA  ALA A 371    10210  11063  10601     -3    107    192       C  
ATOM   2934  C   ALA A 371      35.184   9.128 -20.509  1.00 86.61           C  
ANISOU 2934  C   ALA A 371    10570  11403  10937     -3     97    164       C  
ATOM   2935  O   ALA A 371      34.896   8.078 -21.080  1.00 93.21           O  
ANISOU 2935  O   ALA A 371    11428  12248  11739      1     96    153       O  
ATOM   2936  CB  ALA A 371      36.315  10.613 -22.137  1.00 93.83           C  
ANISOU 2936  CB  ALA A 371    11462  12329  11862     10    131    209       C  
ATOM   2937  N   LYS A 372      35.626   9.148 -19.257  1.00 88.25           N  
ANISOU 2937  N   LYS A 372    10766  11595  11171     -9     90    152       N  
ATOM   2938  CA  LYS A 372      35.826   7.896 -18.506  1.00 91.30           C  
ANISOU 2938  CA  LYS A 372    11164  11976  11550     -8     82    129       C  
ATOM   2939  C   LYS A 372      34.973   7.876 -17.259  1.00100.46           C  
ANISOU 2939  C   LYS A 372    12325  13125  12721    -20     60    113       C  
ATOM   2940  O   LYS A 372      35.401   7.398 -16.193  1.00111.38           O  
ANISOU 2940  O   LYS A 372    13704  14500  14117    -22     53     98       O  
ATOM   2941  CB  LYS A 372      37.298   7.696 -18.168  1.00 91.11           C  
ANISOU 2941  CB  LYS A 372    11126  11947  11544      0     95    131       C  
ATOM   2942  CG  LYS A 372      38.128   7.310 -19.384  1.00 96.12           C  
ANISOU 2942  CG  LYS A 372    11766  12592  12163     15    118    143       C  
ATOM   2943  CD  LYS A 372      39.329   8.227 -19.567  1.00 98.40           C  
ANISOU 2943  CD  LYS A 372    12030  12880  12480     20    135    165       C  
ATOM   2944  CE  LYS A 372      40.403   7.942 -18.528  1.00104.27           C  
ANISOU 2944  CE  LYS A 372    12756  13614  13248     20    135    159       C  
ATOM   2945  NZ  LYS A 372      40.961   9.196 -17.962  1.00104.74           N1+
ANISOU 2945  NZ  LYS A 372    12786  13665  13344     11    134    173       N1+
ATOM   2946  N   VAL A 373      33.753   8.390 -17.428  1.00 94.53           N  
ANISOU 2946  N   VAL A 373    11578  12376  11963    -28     50    117       N  
ATOM   2947  CA  VAL A 373      32.718   8.378 -16.401  1.00 92.77           C  
ANISOU 2947  CA  VAL A 373    11358  12144  11746    -39     30    103       C  
ATOM   2948  C   VAL A 373      32.385   6.966 -15.945  1.00 96.47           C  
ANISOU 2948  C   VAL A 373    11846  12613  12196    -39     19     80       C  
ATOM   2949  O   VAL A 373      32.236   6.700 -14.743  1.00 94.24           O  
ANISOU 2949  O   VAL A 373    11561  12319  11925    -44      7     65       O  
ATOM   2950  CB  VAL A 373      31.450   9.029 -16.953  1.00 97.26           C  
ANISOU 2950  CB  VAL A 373    11928  12719  12305    -44     24    116       C  
ATOM   2951  CG1 VAL A 373      30.190   8.379 -16.391  1.00105.76           C  
ANISOU 2951  CG1 VAL A 373    13020  13795  13370    -52      4    100       C  
ATOM   2952  CG2 VAL A 373      31.480  10.520 -16.644  1.00103.10           C  
ANISOU 2952  CG2 VAL A 373    12647  13449  13078    -49     28    133       C  
ATOM   2953  N   PHE A 374      32.283   6.066 -16.920  1.00 97.21           N  
ANISOU 2953  N   PHE A 374    11958  12718  12258    -32     24     77       N  
ATOM   2954  CA  PHE A 374      31.862   4.683 -16.680  1.00 95.20           C  
ANISOU 2954  CA  PHE A 374    11725  12464  11983    -33     16     55       C  
ATOM   2955  C   PHE A 374      32.904   3.930 -15.878  1.00 94.20           C  
ANISOU 2955  C   PHE A 374    11595  12327  11868    -26     21     43       C  
ATOM   2956  O   PHE A 374      32.625   2.885 -15.298  1.00 97.38           O  
ANISOU 2956  O   PHE A 374    12011  12725  12263    -27     13     25       O  
ATOM   2957  CB  PHE A 374      31.591   3.976 -18.017  1.00 93.39           C  
ANISOU 2957  CB  PHE A 374    11518  12249  11717    -29     23     54       C  
ATOM   2958  CG  PHE A 374      30.265   4.339 -18.629  1.00 88.88           C  
ANISOU 2958  CG  PHE A 374    10953  11689  11127    -38     11     61       C  
ATOM   2959  CD1 PHE A 374      29.824   5.676 -18.668  1.00 85.21           C  
ANISOU 2959  CD1 PHE A 374    10470  11226  10679    -42      8     82       C  
ATOM   2960  CD2 PHE A 374      29.451   3.357 -19.160  1.00 86.46           C  
ANISOU 2960  CD2 PHE A 374    10670  11391  10789    -43      3     48       C  
ATOM   2961  CE1 PHE A 374      28.597   6.011 -19.209  1.00 85.19           C  
ANISOU 2961  CE1 PHE A 374    10472  11236  10662    -50     -3     91       C  
ATOM   2962  CE2 PHE A 374      28.218   3.690 -19.699  1.00 89.75           C  
ANISOU 2962  CE2 PHE A 374    11091  11821  11190    -53    -10     57       C  
ATOM   2963  CZ  PHE A 374      27.789   5.019 -19.720  1.00 84.83           C  
ANISOU 2963  CZ  PHE A 374    10447  11200  10583    -55    -14     79       C  
ATOM   2964  N   ASP A 375      34.110   4.476 -15.852  1.00 92.48           N  
ANISOU 2964  N   ASP A 375    11360  12108  11671    -20     34     54       N  
ATOM   2965  CA  ASP A 375      35.194   3.868 -15.139  1.00 94.85           C  
ANISOU 2965  CA  ASP A 375    11653  12401  11983    -13     40     48       C  
ATOM   2966  C   ASP A 375      34.992   4.124 -13.665  1.00 81.91           C  
ANISOU 2966  C   ASP A 375    10003  10753  10368    -23     23     39       C  
ATOM   2967  O   ASP A 375      35.262   3.267 -12.826  1.00 82.39           O  
ANISOU 2967  O   ASP A 375    10066  10809  10431    -20     19     26       O  
ATOM   2968  CB  ASP A 375      36.508   4.470 -15.615  1.00118.65           C  
ANISOU 2968  CB  ASP A 375    14649  15419  15013     -5     59     66       C  
ATOM   2969  CG  ASP A 375      37.676   3.570 -15.375  1.00139.70           C  
ANISOU 2969  CG  ASP A 375    17314  18084  17683      7     71     63       C  
ATOM   2970  OD1 ASP A 375      37.475   2.401 -14.982  1.00158.20           O  
ANISOU 2970  OD1 ASP A 375    19672  20424  20014     10     68     47       O  
ATOM   2971  OD2 ASP A 375      38.814   4.031 -15.617  1.00143.78           O1-
ANISOU 2971  OD2 ASP A 375    17812  18602  18215     14     86     79       O1-
ATOM   2972  N   GLU A 376      34.484   5.303 -13.344  1.00 73.72           N  
ANISOU 2972  N   GLU A 376     8954   9711   9346    -33     15     46       N  
ATOM   2973  CA  GLU A 376      34.284   5.659 -11.951  1.00 78.46           C  
ANISOU 2973  CA  GLU A 376     9544  10301   9967    -43      0     37       C  
ATOM   2974  C   GLU A 376      33.230   4.807 -11.300  1.00 72.43           C  
ANISOU 2974  C   GLU A 376     8796   9534   9190    -47    -16     20       C  
ATOM   2975  O   GLU A 376      33.219   4.688 -10.105  1.00 82.72           O  
ANISOU 2975  O   GLU A 376    10094  10829  10505    -52    -26      9       O  
ATOM   2976  CB  GLU A 376      33.888   7.123 -11.794  1.00 89.18           C  
ANISOU 2976  CB  GLU A 376    10888  11653  11345    -53     -3     48       C  
ATOM   2977  CG  GLU A 376      34.915   8.133 -12.274  1.00101.87           C  
ANISOU 2977  CG  GLU A 376    12475  13260  12970    -52     12     66       C  
ATOM   2978  CD  GLU A 376      34.502   9.550 -11.916  1.00112.02           C  
ANISOU 2978  CD  GLU A 376    13747  14536  14279    -64      9     74       C  
ATOM   2979  OE1 GLU A 376      34.585   9.922 -10.722  1.00111.53           O  
ANISOU 2979  OE1 GLU A 376    13678  14464  14236    -74      0     65       O  
ATOM   2980  OE2 GLU A 376      34.078  10.288 -12.832  1.00120.00           O1-
ANISOU 2980  OE2 GLU A 376    14757  15550  15288    -62     17     90       O1-
ATOM   2981  N   PHE A 377      32.331   4.224 -12.069  1.00 74.88           N  
ANISOU 2981  N   PHE A 377     9126   9850   9476    -45    -17     16       N  
ATOM   2982  CA  PHE A 377      31.303   3.349 -11.498  1.00 81.38           C  
ANISOU 2982  CA  PHE A 377     9965  10670  10287    -49    -32      0       C  
ATOM   2983  C   PHE A 377      31.876   2.064 -10.853  1.00 81.93           C  
ANISOU 2983  C   PHE A 377    10041  10736  10353    -43    -31    -15       C  
ATOM   2984  O   PHE A 377      31.421   1.638  -9.777  1.00 83.84           O  
ANISOU 2984  O   PHE A 377    10285  10970  10599    -46    -44    -26       O  
ATOM   2985  CB  PHE A 377      30.270   2.937 -12.571  1.00 90.57           C  
ANISOU 2985  CB  PHE A 377    11148  11843  11423    -51    -34      0       C  
ATOM   2986  CG  PHE A 377      29.525   4.092 -13.246  1.00 99.62           C  
ANISOU 2986  CG  PHE A 377    12287  12994  12569    -57    -36     17       C  
ATOM   2987  CD1 PHE A 377      29.300   5.306 -12.610  1.00106.72           C  
ANISOU 2987  CD1 PHE A 377    13170  13886  13493    -63    -40     26       C  
ATOM   2988  CD2 PHE A 377      28.984   3.915 -14.528  1.00102.90           C  
ANISOU 2988  CD2 PHE A 377    12715  13423  12958    -57    -33     23       C  
ATOM   2989  CE1 PHE A 377      28.588   6.318 -13.243  1.00115.23           C  
ANISOU 2989  CE1 PHE A 377    14242  14968  14571    -67    -40     43       C  
ATOM   2990  CE2 PHE A 377      28.278   4.929 -15.165  1.00 97.99           C  
ANISOU 2990  CE2 PHE A 377    12087  12808  12335    -61    -35     41       C  
ATOM   2991  CZ  PHE A 377      28.090   6.130 -14.530  1.00107.06           C  
ANISOU 2991  CZ  PHE A 377    13218  13950  13512    -66    -37     52       C  
ATOM   2992  N   LYS A 378      32.856   1.443 -11.520  1.00 74.72           N  
ANISOU 2992  N   LYS A 378     9131   9827   9432    -31    -15    -12       N  
ATOM   2993  CA  LYS A 378      33.392   0.142 -11.100  1.00 68.68           C  
ANISOU 2993  CA  LYS A 378     8374   9058   8662    -22    -10    -24       C  
ATOM   2994  C   LYS A 378      33.498  -0.046  -9.585  1.00 66.89           C  
ANISOU 2994  C   LYS A 378     8137   8824   8453    -25    -22    -31       C  
ATOM   2995  O   LYS A 378      32.949  -1.001  -9.063  1.00 69.85           O  
ANISOU 2995  O   LYS A 378     8525   9194   8821    -25    -29    -44       O  
ATOM   2996  CB  LYS A 378      34.752  -0.114 -11.748  1.00 79.29           C  
ANISOU 2996  CB  LYS A 378     9714  10407  10008     -9     11    -14       C  
ATOM   2997  CG  LYS A 378      35.171  -1.585 -11.840  1.00 85.02           C  
ANISOU 2997  CG  LYS A 378    10455  11129  10721      3     23    -24       C  
ATOM   2998  CD  LYS A 378      36.672  -1.767 -12.086  1.00 87.49           C  
ANISOU 2998  CD  LYS A 378    10755  11443  11043     17     44    -12       C  
ATOM   2999  CE  LYS A 378      37.066  -1.475 -13.529  1.00 89.73           C  
ANISOU 2999  CE  LYS A 378    11045  11735  11314     24     63     -1       C  
ATOM   3000  NZ  LYS A 378      36.289  -2.319 -14.492  1.00 92.77           N1+
ANISOU 3000  NZ  LYS A 378    11461  12120  11667     25     69    -14       N1+
ATOM   3001  N   PRO A 379      34.173   0.870  -8.873  1.00 71.02           N  
ANISOU 3001  N   PRO A 379     8639   9347   9000    -29    -25    -24       N  
ATOM   3002  CA  PRO A 379      34.302   0.785  -7.405  1.00 71.99           C  
ANISOU 3002  CA  PRO A 379     8750   9464   9137    -33    -38    -31       C  
ATOM   3003  C   PRO A 379      32.975   0.723  -6.699  1.00 74.97           C  
ANISOU 3003  C   PRO A 379     9139   9836   9511    -42    -55    -42       C  
ATOM   3004  O   PRO A 379      32.790  -0.091  -5.801  1.00 78.63           O  
ANISOU 3004  O   PRO A 379     9606  10296   9973    -40    -62    -53       O  
ATOM   3005  CB  PRO A 379      35.000   2.101  -7.001  1.00 77.03           C  
ANISOU 3005  CB  PRO A 379     9366  10104   9800    -41    -40    -20       C  
ATOM   3006  CG  PRO A 379      35.354   2.835  -8.248  1.00 77.76           C  
ANISOU 3006  CG  PRO A 379     9454  10201   9892    -39    -26     -6       C  
ATOM   3007  CD  PRO A 379      34.808   2.084  -9.439  1.00 79.50           C  
ANISOU 3007  CD  PRO A 379     9696  10425  10087    -31    -17     -8       C  
ATOM   3008  N   LEU A 380      32.068   1.608  -7.105  1.00 84.82           N  
ANISOU 3008  N   LEU A 380    10389  11083  10757    -51    -60    -39       N  
ATOM   3009  CA  LEU A 380      30.750   1.732  -6.486  1.00 96.07           C  
ANISOU 3009  CA  LEU A 380    11821  12502  12181    -60    -75    -47       C  
ATOM   3010  C   LEU A 380      29.924   0.485  -6.731  1.00 92.29           C  
ANISOU 3010  C   LEU A 380    11363  12023  11682    -56    -78    -57       C  
ATOM   3011  O   LEU A 380      29.030   0.163  -5.960  1.00 94.58           O  
ANISOU 3011  O   LEU A 380    11659  12307  11970    -61    -90    -66       O  
ATOM   3012  CB  LEU A 380      29.988   2.952  -7.033  1.00110.39           C  
ANISOU 3012  CB  LEU A 380    13631  14314  13997    -68    -76    -37       C  
ATOM   3013  CG  LEU A 380      30.476   4.391  -6.748  1.00129.07           C  
ANISOU 3013  CG  LEU A 380    15979  16677  16386    -74    -73    -27       C  
ATOM   3014  CD1 LEU A 380      29.426   5.404  -7.210  1.00127.90           C  
ANISOU 3014  CD1 LEU A 380    15831  16526  16240    -81    -75    -17       C  
ATOM   3015  CD2 LEU A 380      30.841   4.621  -5.277  1.00135.28           C  
ANISOU 3015  CD2 LEU A 380    16754  17456  17189    -80    -82    -36       C  
ATOM   3016  N   VAL A 381      30.212  -0.209  -7.821  1.00 90.19           N  
ANISOU 3016  N   VAL A 381    11108  11761  11398    -49    -67    -56       N  
ATOM   3017  CA  VAL A 381      29.521  -1.440  -8.109  1.00 92.24           C  
ANISOU 3017  CA  VAL A 381    11388  12019  11638    -48    -68    -68       C  
ATOM   3018  C   VAL A 381      29.974  -2.553  -7.160  1.00 92.75           C  
ANISOU 3018  C   VAL A 381    11455  12078  11707    -40    -67    -78       C  
ATOM   3019  O   VAL A 381      29.143  -3.266  -6.582  1.00 92.50           O  
ANISOU 3019  O   VAL A 381    11434  12041  11671    -43    -77    -88       O  
ATOM   3020  CB  VAL A 381      29.724  -1.850  -9.579  1.00 98.36           C  
ANISOU 3020  CB  VAL A 381    12178  12802  12393    -43    -55    -66       C  
ATOM   3021  CG1 VAL A 381      29.196  -3.266  -9.824  1.00103.37           C  
ANISOU 3021  CG1 VAL A 381    12836  13433  13008    -42    -54    -81       C  
ATOM   3022  CG2 VAL A 381      29.026  -0.855 -10.501  1.00 99.56           C  
ANISOU 3022  CG2 VAL A 381    12329  12962  12537    -51    -58    -55       C  
ATOM   3023  N   GLU A 382      31.285  -2.686  -6.993  1.00 91.67           N  
ANISOU 3023  N   GLU A 382    11307  11942  11579    -31    -56    -73       N  
ATOM   3024  CA  GLU A 382      31.844  -3.859  -6.332  1.00 89.39           C  
ANISOU 3024  CA  GLU A 382    11021  11650  11293    -21    -51    -79       C  
ATOM   3025  C   GLU A 382      31.622  -3.800  -4.844  1.00 87.00           C  
ANISOU 3025  C   GLU A 382    10708  11343  11004    -24    -66    -83       C  
ATOM   3026  O   GLU A 382      31.344  -4.822  -4.227  1.00 93.71           O  
ANISOU 3026  O   GLU A 382    11566  12188  11851    -20    -68    -91       O  
ATOM   3027  CB  GLU A 382      33.327  -4.009  -6.651  1.00 96.86           C  
ANISOU 3027  CB  GLU A 382    11957  12600  12246     -8    -34    -70       C  
ATOM   3028  CG  GLU A 382      33.583  -4.510  -8.069  1.00100.43           C  
ANISOU 3028  CG  GLU A 382    12425  13054  12681     -1    -15    -69       C  
ATOM   3029  CD  GLU A 382      34.788  -3.866  -8.738  1.00104.52           C  
ANISOU 3029  CD  GLU A 382    12927  13578  13205      6      0    -53       C  
ATOM   3030  OE1 GLU A 382      35.245  -2.795  -8.281  1.00119.24           O  
ANISOU 3030  OE1 GLU A 382    14771  15448  15089      1     -6    -43       O  
ATOM   3031  OE2 GLU A 382      35.278  -4.420  -9.744  1.00102.87           O1-
ANISOU 3031  OE2 GLU A 382    12730  13370  12984     16     20    -51       O1-
ATOM   3032  N   GLU A 383      31.694  -2.601  -4.276  1.00 81.47           N  
ANISOU 3032  N   GLU A 383     9991  10645  10317    -33    -75    -78       N  
ATOM   3033  CA  GLU A 383      31.581  -2.443  -2.833  1.00 86.44           C  
ANISOU 3033  CA  GLU A 383    10611  11273  10959    -37    -88    -82       C  
ATOM   3034  C   GLU A 383      30.375  -3.174  -2.233  1.00 90.92           C  
ANISOU 3034  C   GLU A 383    11193  11833  11518    -39    -98    -93       C  
ATOM   3035  O   GLU A 383      30.538  -3.946  -1.276  1.00103.89           O  
ANISOU 3035  O   GLU A 383    12835  13475  13164    -34   -101    -97       O  
ATOM   3036  CB  GLU A 383      31.584  -0.966  -2.450  1.00 89.86           C  
ANISOU 3036  CB  GLU A 383    11029  11707  11405    -49    -96    -77       C  
ATOM   3037  CG  GLU A 383      31.517  -0.697  -0.950  1.00 90.89           C  
ANISOU 3037  CG  GLU A 383    11151  11836  11547    -55   -110    -82       C  
ATOM   3038  CD  GLU A 383      30.124  -0.374  -0.443  1.00 92.64           C  
ANISOU 3038  CD  GLU A 383    11383  12050  11766    -63   -121    -90       C  
ATOM   3039  OE1 GLU A 383      29.351   0.263  -1.195  1.00107.37           O  
ANISOU 3039  OE1 GLU A 383    13254  13912  13629    -69   -120    -87       O  
ATOM   3040  OE2 GLU A 383      29.811  -0.747   0.711  1.00 87.19           O1-
ANISOU 3040  OE2 GLU A 383    10693  11358  11077    -64   -130    -97       O1-
ATOM   3041  N   PRO A 384      29.168  -2.953  -2.777  1.00 94.66           N  
ANISOU 3041  N   PRO A 384    11680  12304  11984    -47   -104    -96       N  
ATOM   3042  CA  PRO A 384      28.047  -3.721  -2.231  1.00 95.43           C  
ANISOU 3042  CA  PRO A 384    11789  12394  12074    -48   -112   -105       C  
ATOM   3043  C   PRO A 384      28.250  -5.237  -2.305  1.00 90.75           C  
ANISOU 3043  C   PRO A 384    11209  11798  11473    -38   -105   -112       C  
ATOM   3044  O   PRO A 384      28.135  -5.883  -1.277  1.00 95.57           O  
ANISOU 3044  O   PRO A 384    11820  12405  12088    -35   -109   -116       O  
ATOM   3045  CB  PRO A 384      26.855  -3.268  -3.090  1.00 98.39           C  
ANISOU 3045  CB  PRO A 384    12175  12769  12441    -58   -117   -104       C  
ATOM   3046  CG  PRO A 384      27.209  -1.886  -3.521  1.00 96.04           C  
ANISOU 3046  CG  PRO A 384    11864  12475  12150    -62   -115    -93       C  
ATOM   3047  CD  PRO A 384      28.707  -1.923  -3.729  1.00 98.65           C  
ANISOU 3047  CD  PRO A 384    12185  12811  12486    -54   -103    -89       C  
ATOM   3048  N   GLN A 385      28.590  -5.777  -3.484  1.00 83.20           N  
ANISOU 3048  N   GLN A 385    10264  10843  10505    -34    -92   -112       N  
ATOM   3049  CA  GLN A 385      28.659  -7.229  -3.702  1.00 79.25           C  
ANISOU 3049  CA  GLN A 385     9779  10336   9995    -25    -81   -120       C  
ATOM   3050  C   GLN A 385      29.567  -7.931  -2.713  1.00 81.57           C  
ANISOU 3050  C   GLN A 385    10065  10629  10301    -13    -76   -118       C  
ATOM   3051  O   GLN A 385      29.346  -9.095  -2.350  1.00 86.56           O  
ANISOU 3051  O   GLN A 385    10706  11252  10930     -7    -72   -124       O  
ATOM   3052  CB  GLN A 385      29.116  -7.541  -5.117  1.00 83.24           C  
ANISOU 3052  CB  GLN A 385    10296  10843  10487    -21    -65   -120       C  
ATOM   3053  CG  GLN A 385      27.974  -7.784  -6.089  1.00 94.24           C  
ANISOU 3053  CG  GLN A 385    11710  12235  11861    -32    -69   -128       C  
ATOM   3054  CD  GLN A 385      28.331  -7.575  -7.562  1.00107.52           C  
ANISOU 3054  CD  GLN A 385    13400  13924  13527    -32    -57   -126       C  
ATOM   3055  NE2 GLN A 385      29.588  -7.205  -7.844  1.00109.12           N  
ANISOU 3055  NE2 GLN A 385    13592  14132  13737    -22    -43   -116       N  
ATOM   3056  OE1 GLN A 385      27.465  -7.730  -8.439  1.00112.53           O  
ANISOU 3056  OE1 GLN A 385    14051  14560  14143    -41    -61   -131       O  
ATOM   3057  N   ASN A 386      30.591  -7.215  -2.286  1.00 88.88           N  
ANISOU 3057  N   ASN A 386    10970  11562  11239    -10    -75   -108       N  
ATOM   3058  CA  ASN A 386      31.555  -7.749  -1.336  1.00106.86           C  
ANISOU 3058  CA  ASN A 386    13234  13841  13527      1    -71   -103       C  
ATOM   3059  C   ASN A 386      30.887  -7.941   0.001  1.00 99.29           C  
ANISOU 3059  C   ASN A 386    12273  12880  12573     -2    -86   -107       C  
ATOM   3060  O   ASN A 386      30.956  -9.001   0.611  1.00 95.47           O  
ANISOU 3060  O   ASN A 386    11792  12392  12091      7    -82   -108       O  
ATOM   3061  CB  ASN A 386      32.750  -6.795  -1.197  1.00118.98           C  
ANISOU 3061  CB  ASN A 386    14746  15387  15075      2    -70    -90       C  
ATOM   3062  CG  ASN A 386      33.338  -6.406  -2.545  1.00136.74           C  
ANISOU 3062  CG  ASN A 386    16996  17639  17319      4    -56    -84       C  
ATOM   3063  ND2 ASN A 386      33.487  -7.389  -3.439  1.00143.12           N  
ANISOU 3063  ND2 ASN A 386    17820  18442  18117     14    -39    -87       N  
ATOM   3064  OD1 ASN A 386      33.629  -5.235  -2.793  1.00146.91           O  
ANISOU 3064  OD1 ASN A 386    18272  18934  18614     -4    -59    -78       O  
ATOM   3065  N   LEU A 387      30.197  -6.901   0.423  1.00109.40           N  
ANISOU 3065  N   LEU A 387    13549  14163  13857    -15   -101   -109       N  
ATOM   3066  CA  LEU A 387      29.548  -6.896   1.720  1.00118.44           C  
ANISOU 3066  CA  LEU A 387    14690  15305  15005    -18   -115   -113       C  
ATOM   3067  C   LEU A 387      28.384  -7.876   1.765  1.00114.60           C  
ANISOU 3067  C   LEU A 387    14223  14808  14511    -17   -116   -121       C  
ATOM   3068  O   LEU A 387      28.079  -8.425   2.818  1.00106.49           O  
ANISOU 3068  O   LEU A 387    13195  13779  13487    -14   -121   -122       O  
ATOM   3069  CB  LEU A 387      29.087  -5.488   2.083  1.00133.75           C  
ANISOU 3069  CB  LEU A 387    16622  17247  16950    -32   -127   -113       C  
ATOM   3070  CG  LEU A 387      29.794  -4.982   3.343  1.00158.86           C  
ANISOU 3070  CG  LEU A 387    19785  20434  20140    -33   -135   -110       C  
ATOM   3071  CD1 LEU A 387      31.282  -4.699   3.103  1.00148.89           C  
ANISOU 3071  CD1 LEU A 387    18506  19182  18884    -30   -128   -101       C  
ATOM   3072  CD2 LEU A 387      29.103  -3.718   3.859  1.00180.36           C  
ANISOU 3072  CD2 LEU A 387    22505  23155  22867    -47   -147   -113       C  
ATOM   3073  N   ILE A 388      27.760  -8.125   0.616  1.00120.98           N  
ANISOU 3073  N   ILE A 388    15047  15611  15309    -21   -111   -126       N  
ATOM   3074  CA  ILE A 388      26.682  -9.104   0.519  1.00115.42           C  
ANISOU 3074  CA  ILE A 388    14360  14896  14597    -22   -112   -134       C  
ATOM   3075  C   ILE A 388      27.227 -10.496   0.820  1.00112.33           C  
ANISOU 3075  C   ILE A 388    13974  14499  14207     -9   -100   -135       C  
ATOM   3076  O   ILE A 388      26.787 -11.158   1.768  1.00111.99           O  
ANISOU 3076  O   ILE A 388    13932  14450  14168     -6   -104   -137       O  
ATOM   3077  CB  ILE A 388      26.004  -9.089  -0.878  1.00110.95           C  
ANISOU 3077  CB  ILE A 388    13810  14329  14018    -31   -110   -139       C  
ATOM   3078  CG1 ILE A 388      25.492  -7.691  -1.237  1.00110.99           C  
ANISOU 3078  CG1 ILE A 388    13808  14340  14023    -43   -120   -134       C  
ATOM   3079  CG2 ILE A 388      24.838 -10.063  -0.919  1.00110.37           C  
ANISOU 3079  CG2 ILE A 388    13753  14245  13937    -35   -113   -148       C  
ATOM   3080  CD1 ILE A 388      24.624  -7.051  -0.175  1.00114.73           C  
ANISOU 3080  CD1 ILE A 388    14275  14813  14506    -49   -135   -132       C  
ATOM   3081  N   LYS A 389      28.193 -10.935   0.025  1.00103.71           N  
ANISOU 3081  N   LYS A 389    12885  13408  13112      0    -83   -134       N  
ATOM   3082  CA  LYS A 389      28.778 -12.261   0.221  1.00104.29           C  
ANISOU 3082  CA  LYS A 389    12964  13474  13189     14    -68   -133       C  
ATOM   3083  C   LYS A 389      29.101 -12.523   1.672  1.00 91.74           C  
ANISOU 3083  C   LYS A 389    11359  11887  11611     22    -73   -126       C  
ATOM   3084  O   LYS A 389      28.748 -13.569   2.239  1.00 97.60           O  
ANISOU 3084  O   LYS A 389    12108  12621  12356     29    -69   -128       O  
ATOM   3085  CB  LYS A 389      30.066 -12.414  -0.585  1.00112.83           C  
ANISOU 3085  CB  LYS A 389    14043  14559  14270     25    -48   -127       C  
ATOM   3086  CG  LYS A 389      29.897 -13.221  -1.860  1.00117.08           C  
ANISOU 3086  CG  LYS A 389    14604  15086  14795     26    -32   -137       C  
ATOM   3087  CD  LYS A 389      30.929 -14.330  -1.996  1.00115.70           C  
ANISOU 3087  CD  LYS A 389    14433  14904  14624     44     -7   -133       C  
ATOM   3088  CE  LYS A 389      32.341 -13.807  -2.242  1.00120.64           C  
ANISOU 3088  CE  LYS A 389    15040  15540  15256     55      4   -118       C  
ATOM   3089  NZ  LYS A 389      33.328 -14.874  -2.586  1.00125.01           N1+
ANISOU 3089  NZ  LYS A 389    15598  16085  15813     74     32   -113       N1+
ATOM   3090  N   GLN A 390      29.771 -11.543   2.258  1.00 84.31           N  
ANISOU 3090  N   GLN A 390    10398  10960  10678     21    -81   -117       N  
ATOM   3091  CA  GLN A 390      30.319 -11.641   3.590  1.00 91.18           C  
ANISOU 3091  CA  GLN A 390    11251  11837  11557     28    -86   -108       C  
ATOM   3092  C   GLN A 390      29.241 -11.989   4.595  1.00 87.38           C  
ANISOU 3092  C   GLN A 390    10775  11351  11076     25    -98   -113       C  
ATOM   3093  O   GLN A 390      29.354 -12.967   5.353  1.00104.97           O  
ANISOU 3093  O   GLN A 390    13001  13575  13306     37    -93   -109       O  
ATOM   3094  CB  GLN A 390      30.956 -10.301   3.947  1.00100.34           C  
ANISOU 3094  CB  GLN A 390    12391  13012  12722     21    -98   -102       C  
ATOM   3095  CG  GLN A 390      32.222 -10.368   4.774  1.00111.86           C  
ANISOU 3095  CG  GLN A 390    13828  14484  14190     30    -97    -89       C  
ATOM   3096  CD  GLN A 390      33.074  -9.121   4.596  1.00127.04           C  
ANISOU 3096  CD  GLN A 390    15733  16419  16117     21   -102    -83       C  
ATOM   3097  NE2 GLN A 390      34.185  -9.054   5.330  1.00143.68           N  
ANISOU 3097  NE2 GLN A 390    17819  18541  18232     26   -104    -71       N  
ATOM   3098  OE1 GLN A 390      32.746  -8.230   3.803  1.00124.68           O  
ANISOU 3098  OE1 GLN A 390    15439  16118  15816     11   -104    -88       O  
ATOM   3099  N   ASN A 391      28.186 -11.194   4.576  1.00 80.21           N  
ANISOU 3099  N   ASN A 391     9872  10440  10163     11   -111   -121       N  
ATOM   3100  CA  ASN A 391      27.092 -11.358   5.506  1.00 81.51           C  
ANISOU 3100  CA  ASN A 391    10042  10600  10329      8   -122   -125       C  
ATOM   3101  C   ASN A 391      26.443 -12.709   5.325  1.00 80.04           C  
ANISOU 3101  C   ASN A 391     9872  10400  10141     14   -113   -129       C  
ATOM   3102  O   ASN A 391      26.143 -13.390   6.304  1.00 72.06           O  
ANISOU 3102  O   ASN A 391     8860   9386   9134     20   -115   -127       O  
ATOM   3103  CB  ASN A 391      26.019 -10.291   5.272  1.00 85.03           C  
ANISOU 3103  CB  ASN A 391    10492  11045  10772     -8   -135   -130       C  
ATOM   3104  CG  ASN A 391      26.499  -8.888   5.545  1.00 80.78           C  
ANISOU 3104  CG  ASN A 391     9938  10516  10236    -15   -143   -127       C  
ATOM   3105  ND2 ASN A 391      25.621  -7.922   5.294  1.00 81.87           N  
ANISOU 3105  ND2 ASN A 391    10081  10653  10374    -27   -151   -130       N  
ATOM   3106  OD1 ASN A 391      27.628  -8.670   5.985  1.00 80.70           O  
ANISOU 3106  OD1 ASN A 391     9915  10517  10231    -10   -142   -121       O  
ATOM   3107  N   CYS A 392      26.219 -13.080   4.063  1.00 90.17           N  
ANISOU 3107  N   CYS A 392    11169  11675  11417     10   -104   -136       N  
ATOM   3108  CA  CYS A 392      25.422 -14.263   3.731  1.00 96.53           C  
ANISOU 3108  CA  CYS A 392    11994  12465  12220     11    -98   -144       C  
ATOM   3109  C   CYS A 392      26.109 -15.546   4.163  1.00101.81           C  
ANISOU 3109  C   CYS A 392    12663  13127  12894     27    -81   -139       C  
ATOM   3110  O   CYS A 392      25.447 -16.452   4.692  1.00 97.89           O  
ANISOU 3110  O   CYS A 392    12173  12618  12401     30    -80   -141       O  
ATOM   3111  CB  CYS A 392      25.089 -14.300   2.242  1.00 98.96           C  
ANISOU 3111  CB  CYS A 392    12318  12767  12515      1    -92   -153       C  
ATOM   3112  SG  CYS A 392      23.446 -13.654   1.843  1.00101.56           S  
ANISOU 3112  SG  CYS A 392    12656  13096  12838    -19   -110   -159       S  
ATOM   3113  N   GLU A 393      27.429 -15.625   3.976  1.00 94.03           N  
ANISOU 3113  N   GLU A 393    11668  12147  11912     39    -69   -131       N  
ATOM   3114  CA  GLU A 393      28.130 -16.777   4.505  1.00 97.49           C  
ANISOU 3114  CA  GLU A 393    12104  12581  12359     57    -53   -123       C  
ATOM   3115  C   GLU A 393      27.979 -16.799   6.020  1.00 83.70           C  
ANISOU 3115  C   GLU A 393    10343  10841  10619     62    -64   -114       C  
ATOM   3116  O   GLU A 393      27.818 -17.854   6.647  1.00 74.35           O  
ANISOU 3116  O   GLU A 393     9160   9647   9441     72    -56   -110       O  
ATOM   3117  CB  GLU A 393      29.613 -16.857   4.090  1.00110.73           C  
ANISOU 3117  CB  GLU A 393    13770  14264  14039     70    -36   -113       C  
ATOM   3118  CG  GLU A 393      30.001 -18.334   3.808  1.00126.68           C  
ANISOU 3118  CG  GLU A 393    15801  16267  16063     86    -10   -111       C  
ATOM   3119  CD  GLU A 393      31.362 -18.783   4.329  1.00131.85           C  
ANISOU 3119  CD  GLU A 393    16438  16930  16730    106      5    -92       C  
ATOM   3120  OE1 GLU A 393      32.377 -18.190   3.916  1.00149.74           O  
ANISOU 3120  OE1 GLU A 393    18691  19207  18997    110      9    -84       O  
ATOM   3121  OE2 GLU A 393      31.421 -19.757   5.116  1.00115.24           O1-
ANISOU 3121  OE2 GLU A 393    14331  14820  14635    119     13    -84       O1-
ATOM   3122  N   LEU A 394      27.998 -15.620   6.614  1.00 79.48           N  
ANISOU 3122  N   LEU A 394     9794  10322  10084     54    -82   -111       N  
ATOM   3123  CA  LEU A 394      27.836 -15.544   8.041  1.00 83.85           C  
ANISOU 3123  CA  LEU A 394    10335  10883  10641     57    -93   -104       C  
ATOM   3124  C   LEU A 394      26.452 -16.080   8.416  1.00 86.95           C  
ANISOU 3124  C   LEU A 394    10741  11262  11033     53    -97   -111       C  
ATOM   3125  O   LEU A 394      26.274 -16.716   9.459  1.00 93.44           O  
ANISOU 3125  O   LEU A 394    11560  12084  11860     62    -97   -104       O  
ATOM   3126  CB  LEU A 394      28.029 -14.110   8.535  1.00 83.94           C  
ANISOU 3126  CB  LEU A 394    10332  10911  10650     46   -111   -103       C  
ATOM   3127  CG  LEU A 394      28.559 -14.062   9.967  1.00 87.48           C  
ANISOU 3127  CG  LEU A 394    10763  11375  11102     53   -119    -92       C  
ATOM   3128  CD1 LEU A 394      30.072 -14.303   9.955  1.00 92.14           C  
ANISOU 3128  CD1 LEU A 394    11336  11977  11696     64   -110    -78       C  
ATOM   3129  CD2 LEU A 394      28.209 -12.753  10.682  1.00 85.49           C  
ANISOU 3129  CD2 LEU A 394    10504  11134  10846     39   -138    -96       C  
ATOM   3130  N   PHE A 395      25.480 -15.848   7.547  1.00 82.61           N  
ANISOU 3130  N   PHE A 395    10207  10703  10479     40   -101   -123       N  
ATOM   3131  CA  PHE A 395      24.096 -16.167   7.861  1.00 89.82           C  
ANISOU 3131  CA  PHE A 395    11132  11605  11392     33   -108   -129       C  
ATOM   3132  C   PHE A 395      23.895 -17.690   7.928  1.00 92.38           C  
ANISOU 3132  C   PHE A 395    11466  11913  11721     43    -93   -128       C  
ATOM   3133  O   PHE A 395      23.186 -18.216   8.797  1.00 87.06           O  
ANISOU 3133  O   PHE A 395    10793  11233  11053     46    -95   -125       O  
ATOM   3134  CB  PHE A 395      23.143 -15.492   6.848  1.00 87.40           C  
ANISOU 3134  CB  PHE A 395    10836  11294  11079     15   -116   -139       C  
ATOM   3135  CG  PHE A 395      21.760 -16.072   6.847  1.00 92.12           C  
ANISOU 3135  CG  PHE A 395    11447  11879  11677      8   -120   -144       C  
ATOM   3136  CD1 PHE A 395      20.863 -15.760   7.854  1.00106.72           C  
ANISOU 3136  CD1 PHE A 395    13291  13728  13530      5   -131   -141       C  
ATOM   3137  CD2 PHE A 395      21.369 -16.955   5.852  1.00 93.50           C  
ANISOU 3137  CD2 PHE A 395    11639  12039  11848      3   -111   -153       C  
ATOM   3138  CE1 PHE A 395      19.597 -16.322   7.861  1.00117.67           C  
ANISOU 3138  CE1 PHE A 395    14688  15103  14919     -1   -134   -144       C  
ATOM   3139  CE2 PHE A 395      20.115 -17.520   5.851  1.00 98.60           C  
ANISOU 3139  CE2 PHE A 395    12295  12673  12495     -6   -115   -158       C  
ATOM   3140  CZ  PHE A 395      19.226 -17.207   6.857  1.00114.75           C  
ANISOU 3140  CZ  PHE A 395    14333  14720  14547     -7   -127   -152       C  
ATOM   3141  N   GLU A 396      24.553 -18.390   7.017  1.00 96.95           N  
ANISOU 3141  N   GLU A 396    12054  12484  12300     48    -76   -131       N  
ATOM   3142  CA  GLU A 396      24.384 -19.824   6.883  1.00 94.09           C  
ANISOU 3142  CA  GLU A 396    11705  12103  11944     56    -58   -133       C  
ATOM   3143  C   GLU A 396      25.186 -20.538   7.933  1.00 90.61           C  
ANISOU 3143  C   GLU A 396    11250  11664  11513     76    -48   -118       C  
ATOM   3144  O   GLU A 396      24.829 -21.630   8.337  1.00101.50           O  
ANISOU 3144  O   GLU A 396    12636  13029  12900     84    -37   -116       O  
ATOM   3145  CB  GLU A 396      24.847 -20.262   5.501  1.00 92.12           C  
ANISOU 3145  CB  GLU A 396    11470  11843  11689     55    -42   -143       C  
ATOM   3146  CG  GLU A 396      24.060 -19.601   4.389  1.00 93.22           C  
ANISOU 3146  CG  GLU A 396    11622  11982  11815     35    -52   -157       C  
ATOM   3147  CD  GLU A 396      22.651 -20.137   4.304  1.00 93.21           C  
ANISOU 3147  CD  GLU A 396    11636  11966  11813     22    -59   -167       C  
ATOM   3148  OE1 GLU A 396      22.393 -21.200   4.914  1.00104.47           O  
ANISOU 3148  OE1 GLU A 396    13066  13379  13249     29    -50   -165       O  
ATOM   3149  OE2 GLU A 396      21.810 -19.487   3.654  1.00 79.51           O1-
ANISOU 3149  OE2 GLU A 396     9906  10234  10068      4    -73   -175       O1-
ATOM   3150  N   GLN A 397      26.279 -19.913   8.352  1.00 85.48           N  
ANISOU 3150  N   GLN A 397    10582  11033  10864     84    -50   -106       N  
ATOM   3151  CA  GLN A 397      27.179 -20.471   9.337  1.00 96.93           C  
ANISOU 3151  CA  GLN A 397    12016  12491  12322    103    -42    -89       C  
ATOM   3152  C   GLN A 397      26.530 -20.506  10.689  1.00101.29           C  
ANISOU 3152  C   GLN A 397    12561  13049  12877    105    -54    -82       C  
ATOM   3153  O   GLN A 397      26.774 -21.410  11.505  1.00105.74           O  
ANISOU 3153  O   GLN A 397    13117  13611  13449    121    -44    -68       O  
ATOM   3154  CB  GLN A 397      28.410 -19.578   9.473  1.00106.32           C  
ANISOU 3154  CB  GLN A 397    13184  13703  13509    107    -47    -78       C  
ATOM   3155  CG  GLN A 397      29.632 -20.053   8.736  1.00114.52           C  
ANISOU 3155  CG  GLN A 397    14220  14740  14553    119    -26    -71       C  
ATOM   3156  CD  GLN A 397      30.873 -19.322   9.184  1.00109.78           C  
ANISOU 3156  CD  GLN A 397    13594  14164  13953    124    -33    -55       C  
ATOM   3157  NE2 GLN A 397      31.974 -20.050   9.342  1.00105.73           N  
ANISOU 3157  NE2 GLN A 397    13069  13655  13450    143    -15    -37       N  
ATOM   3158  OE1 GLN A 397      30.835 -18.112   9.405  1.00115.28           O  
ANISOU 3158  OE1 GLN A 397    14281  14875  14643    111    -52    -59       O  
ATOM   3159  N   LEU A 398      25.732 -19.479  10.938  1.00 97.86           N  
ANISOU 3159  N   LEU A 398    12126  12621  12436     90    -74    -89       N  
ATOM   3160  CA  LEU A 398      25.257 -19.221  12.279  1.00 98.94           C  
ANISOU 3160  CA  LEU A 398    12253  12768  12572     91    -87    -82       C  
ATOM   3161  C   LEU A 398      23.828 -19.708  12.474  1.00 93.37           C  
ANISOU 3161  C   LEU A 398    11562  12046  11870     86    -89    -89       C  
ATOM   3162  O   LEU A 398      23.507 -20.219  13.549  1.00106.72           O  
ANISOU 3162  O   LEU A 398    13248  13737  13564     95    -89    -79       O  
ATOM   3163  CB  LEU A 398      25.371 -17.715  12.603  1.00 96.73           C  
ANISOU 3163  CB  LEU A 398    11963  12506  12283     79   -107    -85       C  
ATOM   3164  CG  LEU A 398      26.737 -17.011  12.731  1.00 87.47           C  
ANISOU 3164  CG  LEU A 398    10772  11355  11108     82   -111    -77       C  
ATOM   3165  CD1 LEU A 398      26.521 -15.509  12.801  1.00 87.97           C  
ANISOU 3165  CD1 LEU A 398    10831  11428  11164     65   -129    -86       C  
ATOM   3166  CD2 LEU A 398      27.550 -17.453  13.940  1.00 86.28           C  
ANISOU 3166  CD2 LEU A 398    10603  11219  10959     96   -110    -60       C  
ATOM   3167  N   GLY A 399      22.993 -19.549  11.442  1.00 91.90           N  
ANISOU 3167  N   GLY A 399    11391  11846  11680     72    -91   -103       N  
ATOM   3168  CA  GLY A 399      21.556 -19.792  11.534  1.00 92.91           C  
ANISOU 3168  CA  GLY A 399    11530  11961  11811     62    -96   -109       C  
ATOM   3169  C   GLY A 399      20.902 -18.514  11.987  1.00100.41           C  
ANISOU 3169  C   GLY A 399    12475  12922  12755     51   -115   -110       C  
ATOM   3170  O   GLY A 399      21.390 -17.860  12.915  1.00119.02           O  
ANISOU 3170  O   GLY A 399    14818  15295  15108     56   -123   -103       O  
ATOM   3171  N   GLU A 400      19.793 -18.155  11.352  1.00106.83           N  
ANISOU 3171  N   GLU A 400    13298  13726  13566     36   -123   -119       N  
ATOM   3172  CA  GLU A 400      19.193 -16.820  11.545  1.00110.88           C  
ANISOU 3172  CA  GLU A 400    13806  14249  14074     25   -139   -121       C  
ATOM   3173  C   GLU A 400      19.221 -16.337  13.004  1.00103.75           C  
ANISOU 3173  C   GLU A 400    12893  13357  13172     32   -145   -112       C  
ATOM   3174  O   GLU A 400      19.619 -15.203  13.276  1.00 95.65           O  
ANISOU 3174  O   GLU A 400    11859  12345  12140     28   -153   -113       O  
ATOM   3175  CB  GLU A 400      17.761 -16.764  11.003  1.00114.78           C  
ANISOU 3175  CB  GLU A 400    14311  14732  14570     11   -145   -126       C  
ATOM   3176  CG  GLU A 400      17.373 -15.378  10.521  1.00125.24           C  
ANISOU 3176  CG  GLU A 400    15633  16064  15889     -3   -157   -129       C  
ATOM   3177  CD  GLU A 400      15.878 -15.133  10.526  1.00133.70           C  
ANISOU 3177  CD  GLU A 400    16708  17128  16964    -13   -165   -127       C  
ATOM   3178  OE1 GLU A 400      15.318 -14.862   9.443  1.00147.02           O  
ANISOU 3178  OE1 GLU A 400    18401  18813  18648    -26   -169   -131       O  
ATOM   3179  OE2 GLU A 400      15.265 -15.186  11.614  1.00131.53           O1-
ANISOU 3179  OE2 GLU A 400    16430  16852  16695     -8   -166   -120       O1-
ATOM   3180  N   TYR A 401      18.833 -17.201  13.938  1.00 99.60           N  
ANISOU 3180  N   TYR A 401    12366  12826  12651     42   -140   -105       N  
ATOM   3181  CA  TYR A 401      18.791 -16.800  15.342  1.00 96.90           C  
ANISOU 3181  CA  TYR A 401    12016  12496  12307     49   -146    -97       C  
ATOM   3182  C   TYR A 401      20.129 -16.299  15.829  1.00 93.86           C  
ANISOU 3182  C   TYR A 401    11618  12130  11914     55   -149    -93       C  
ATOM   3183  O   TYR A 401      20.217 -15.196  16.355  1.00 95.26           O  
ANISOU 3183  O   TYR A 401    11791  12320  12086     49   -159    -95       O  
ATOM   3184  CB  TYR A 401      18.339 -17.939  16.245  1.00102.16           C  
ANISOU 3184  CB  TYR A 401    12683  13155  12980     62   -139    -87       C  
ATOM   3185  CG  TYR A 401      18.294 -17.521  17.693  1.00101.63           C  
ANISOU 3185  CG  TYR A 401    12607  13101  12907     69   -144    -78       C  
ATOM   3186  CD1 TYR A 401      17.487 -16.466  18.092  1.00104.95           C  
ANISOU 3186  CD1 TYR A 401    13029  13524  13323     60   -154    -82       C  
ATOM   3187  CD2 TYR A 401      19.069 -18.162  18.656  1.00100.95           C  
ANISOU 3187  CD2 TYR A 401    12512  13025  12820     85   -139    -67       C  
ATOM   3188  CE1 TYR A 401      17.436 -16.062  19.409  1.00104.82           C  
ANISOU 3188  CE1 TYR A 401    13008  13520  13301     66   -158    -76       C  
ATOM   3189  CE2 TYR A 401      19.020 -17.773  19.981  1.00106.20           C  
ANISOU 3189  CE2 TYR A 401    13170  13704  13476     90   -145    -59       C  
ATOM   3190  CZ  TYR A 401      18.200 -16.714  20.350  1.00108.32           C  
ANISOU 3190  CZ  TYR A 401    13443  13974  13739     80   -154    -66       C  
ATOM   3191  OH  TYR A 401      18.135 -16.285  21.654  1.00107.48           O  
ANISOU 3191  OH  TYR A 401    13333  13882  13624     85   -159    -61       O  
ATOM   3192  N   LYS A 402      21.166 -17.113  15.654  1.00 96.53           N  
ANISOU 3192  N   LYS A 402    11951  12470  12255     66   -139    -88       N  
ATOM   3193  CA  LYS A 402      22.512 -16.739  16.089  1.00 90.76           C  
ANISOU 3193  CA  LYS A 402    11206  11759  11519     72   -141    -81       C  
ATOM   3194  C   LYS A 402      22.968 -15.489  15.357  1.00 82.33           C  
ANISOU 3194  C   LYS A 402    10136  10700  10446     58   -150    -91       C  
ATOM   3195  O   LYS A 402      23.507 -14.570  15.968  1.00 75.79           O  
ANISOU 3195  O   LYS A 402     9298   9888   9611     54   -159    -90       O  
ATOM   3196  CB  LYS A 402      23.503 -17.906  15.888  1.00 91.74           C  
ANISOU 3196  CB  LYS A 402    11325  11883  11649     87   -126    -71       C  
ATOM   3197  CG  LYS A 402      23.879 -18.617  17.180  1.00 93.22           C  
ANISOU 3197  CG  LYS A 402    11501  12080  11837    103   -123    -55       C  
ATOM   3198  CD  LYS A 402      23.904 -20.138  17.083  1.00 97.38           C  
ANISOU 3198  CD  LYS A 402    12031  12592  12376    119   -104    -45       C  
ATOM   3199  CE  LYS A 402      23.556 -20.751  18.451  1.00 99.41           C  
ANISOU 3199  CE  LYS A 402    12283  12855  12634    132   -103    -31       C  
ATOM   3200  NZ  LYS A 402      23.407 -22.237  18.449  1.00 98.00           N1+
ANISOU 3200  NZ  LYS A 402    12108  12658  12469    147    -83    -21       N1+
ATOM   3201  N   PHE A 403      22.713 -15.468  14.053  1.00 83.08           N  
ANISOU 3201  N   PHE A 403    10240  10782  10543     50   -145    -99       N  
ATOM   3202  CA  PHE A 403      23.095 -14.360  13.176  1.00 89.02           C  
ANISOU 3202  CA  PHE A 403    10991  11539  11291     38   -151   -107       C  
ATOM   3203  C   PHE A 403      22.607 -13.034  13.727  1.00 79.97           C  
ANISOU 3203  C   PHE A 403     9843  10400  10141     27   -164   -111       C  
ATOM   3204  O   PHE A 403      23.382 -12.081  13.807  1.00 66.24           O  
ANISOU 3204  O   PHE A 403     8095   8674   8400     21   -170   -112       O  
ATOM   3205  CB  PHE A 403      22.538 -14.611  11.754  1.00 96.59           C  
ANISOU 3205  CB  PHE A 403    11964  12483  12252     30   -145   -115       C  
ATOM   3206  CG  PHE A 403      22.809 -13.504  10.756  1.00 91.54           C  
ANISOU 3206  CG  PHE A 403    11325  11849  11609     18   -150   -122       C  
ATOM   3207  CD1 PHE A 403      24.067 -12.882  10.668  1.00 86.69           C  
ANISOU 3207  CD1 PHE A 403    10698  11248  10994     20   -150   -119       C  
ATOM   3208  CD2 PHE A 403      21.814 -13.125   9.867  1.00 86.39           C  
ANISOU 3208  CD2 PHE A 403    10683  11187  10955      6   -153   -129       C  
ATOM   3209  CE1 PHE A 403      24.303 -11.881   9.744  1.00 82.38           C  
ANISOU 3209  CE1 PHE A 403    10151  10705  10445      9   -153   -124       C  
ATOM   3210  CE2 PHE A 403      22.048 -12.134   8.931  1.00 88.15           C  
ANISOU 3210  CE2 PHE A 403    10905  11414  11174     -4   -156   -133       C  
ATOM   3211  CZ  PHE A 403      23.295 -11.509   8.876  1.00 87.55           C  
ANISOU 3211  CZ  PHE A 403    10817  11350  11098     -2   -155   -130       C  
ATOM   3212  N   GLN A 404      21.326 -13.019  14.115  1.00 80.09           N  
ANISOU 3212  N   GLN A 404     9867  10407  10158     23   -168   -113       N  
ATOM   3213  CA  GLN A 404      20.654 -11.868  14.735  1.00 74.55           C  
ANISOU 3213  CA  GLN A 404     9165   9708   9454     15   -177   -116       C  
ATOM   3214  C   GLN A 404      21.401 -11.396  15.946  1.00 66.56           C  
ANISOU 3214  C   GLN A 404     8143   8712   8435     18   -183   -114       C  
ATOM   3215  O   GLN A 404      21.887 -10.264  15.965  1.00 58.10           O  
ANISOU 3215  O   GLN A 404     7067   7649   7361      8   -189   -119       O  
ATOM   3216  CB  GLN A 404      19.246 -12.247  15.167  1.00 81.09           C  
ANISOU 3216  CB  GLN A 404    10001  10523  10285     16   -176   -114       C  
ATOM   3217  CG  GLN A 404      18.221 -12.072  14.059  1.00 94.12           C  
ANISOU 3217  CG  GLN A 404    11661  12161  11941      5   -177   -118       C  
ATOM   3218  CD  GLN A 404      16.939 -12.862  14.288  1.00 97.92           C  
ANISOU 3218  CD  GLN A 404    12149  12628  12427      7   -174   -114       C  
ATOM   3219  NE2 GLN A 404      15.880 -12.505  13.555  1.00100.24           N  
ANISOU 3219  NE2 GLN A 404    12448  12914  12724     -3   -177   -115       N  
ATOM   3220  OE1 GLN A 404      16.901 -13.783  15.113  1.00 93.66           O  
ANISOU 3220  OE1 GLN A 404    11609  12087  11890     18   -170   -108       O  
ATOM   3221  N   ASN A 405      21.505 -12.281  16.937  1.00 61.25           N  
ANISOU 3221  N   ASN A 405     7467   8044   7761     30   -180   -105       N  
ATOM   3222  CA  ASN A 405      22.334 -12.049  18.111  1.00 62.32           C  
ANISOU 3222  CA  ASN A 405     7593   8199   7889     34   -186   -101       C  
ATOM   3223  C   ASN A 405      23.640 -11.347  17.782  1.00 70.86           C  
ANISOU 3223  C   ASN A 405     8662   9295   8967     28   -191   -103       C  
ATOM   3224  O   ASN A 405      23.962 -10.292  18.331  1.00 82.77           O  
ANISOU 3224  O   ASN A 405    10167  10814  10469     18   -200   -108       O  
ATOM   3225  CB  ASN A 405      22.655 -13.362  18.785  1.00 59.29           C  
ANISOU 3225  CB  ASN A 405     7203   7819   7505     51   -180    -88       C  
ATOM   3226  CG  ASN A 405      21.428 -14.161  19.087  1.00 57.53           C  
ANISOU 3226  CG  ASN A 405     6990   7581   7288     58   -174    -85       C  
ATOM   3227  ND2 ASN A 405      21.572 -15.462  19.140  1.00 62.50           N  
ANISOU 3227  ND2 ASN A 405     7618   8206   7923     72   -164    -74       N  
ATOM   3228  OD1 ASN A 405      20.357 -13.617  19.246  1.00 57.23           O  
ANISOU 3228  OD1 ASN A 405     6960   7535   7249     51   -177    -90       O  
ATOM   3229  N   ALA A 406      24.390 -11.922  16.859  1.00 65.37           N  
ANISOU 3229  N   ALA A 406     7962   8598   8276     32   -184    -99       N  
ATOM   3230  CA  ALA A 406      25.591 -11.287  16.388  1.00 62.64           C  
ANISOU 3230  CA  ALA A 406     7606   8264   7931     27   -187   -100       C  
ATOM   3231  C   ALA A 406      25.361  -9.839  15.958  1.00 63.36           C  
ANISOU 3231  C   ALA A 406     7700   8353   8021      9   -194   -111       C  
ATOM   3232  O   ALA A 406      26.252  -9.017  16.059  1.00 69.67           O  
ANISOU 3232  O   ALA A 406     8489   9165   8818      1   -200   -113       O  
ATOM   3233  CB  ALA A 406      26.168 -12.074  15.231  1.00 67.59           C  
ANISOU 3233  CB  ALA A 406     8232   8885   8565     34   -175    -95       C  
ATOM   3234  N   LEU A 407      24.192  -9.511  15.440  1.00 63.17           N  
ANISOU 3234  N   LEU A 407     7690   8314   8000      3   -192   -118       N  
ATOM   3235  CA  LEU A 407      24.032  -8.182  14.885  1.00 68.01           C  
ANISOU 3235  CA  LEU A 407     8303   8922   8614    -11   -196   -127       C  
ATOM   3236  C   LEU A 407      23.642  -7.248  15.991  1.00 70.94           C  
ANISOU 3236  C   LEU A 407     8677   9298   8981    -19   -204   -132       C  
ATOM   3237  O   LEU A 407      23.862  -6.030  15.925  1.00 77.53           O  
ANISOU 3237  O   LEU A 407     9509  10134   9815    -32   -208   -139       O  
ATOM   3238  CB  LEU A 407      22.977  -8.177  13.796  1.00 72.66           C  
ANISOU 3238  CB  LEU A 407     8905   9495   9208    -15   -191   -130       C  
ATOM   3239  CG  LEU A 407      23.289  -8.816  12.438  1.00 75.42           C  
ANISOU 3239  CG  LEU A 407     9256   9839   9560    -12   -184   -128       C  
ATOM   3240  CD1 LEU A 407      22.586  -8.011  11.351  1.00 81.25           C  
ANISOU 3240  CD1 LEU A 407    10001  10568  10301    -23   -184   -133       C  
ATOM   3241  CD2 LEU A 407      24.765  -8.878  12.145  1.00 74.75           C  
ANISOU 3241  CD2 LEU A 407     9159   9766   9475     -9   -181   -125       C  
ATOM   3242  N   LEU A 408      23.039  -7.843  17.010  1.00 71.75           N  
ANISOU 3242  N   LEU A 408     8783   9400   9078    -11   -204   -129       N  
ATOM   3243  CA  LEU A 408      22.651  -7.116  18.196  1.00 73.22           C  
ANISOU 3243  CA  LEU A 408     8972   9590   9257    -16   -209   -134       C  
ATOM   3244  C   LEU A 408      23.909  -6.625  18.835  1.00 80.19           C  
ANISOU 3244  C   LEU A 408     9844  10493  10133    -22   -218   -136       C  
ATOM   3245  O   LEU A 408      23.945  -5.554  19.443  1.00 81.88           O  
ANISOU 3245  O   LEU A 408    10059  10710  10341    -34   -223   -145       O  
ATOM   3246  CB  LEU A 408      21.943  -8.042  19.181  1.00 77.41           C  
ANISOU 3246  CB  LEU A 408     9508  10120   9784     -4   -207   -128       C  
ATOM   3247  CG  LEU A 408      20.441  -8.255  19.053  1.00 77.13           C  
ANISOU 3247  CG  LEU A 408     9485  10067   9755     -1   -201   -127       C  
ATOM   3248  CD1 LEU A 408      19.848  -8.789  20.358  1.00 71.86           C  
ANISOU 3248  CD1 LEU A 408     8821   9401   9081      8   -200   -122       C  
ATOM   3249  CD2 LEU A 408      19.773  -6.951  18.657  1.00 84.78           C  
ANISOU 3249  CD2 LEU A 408    10460  11024  10727    -14   -201   -135       C  
ATOM   3250  N   VAL A 409      24.941  -7.449  18.695  1.00 74.55           N  
ANISOU 3250  N   VAL A 409     9117   9790   9417    -14   -218   -127       N  
ATOM   3251  CA  VAL A 409      26.275  -7.128  19.120  1.00 73.76           C  
ANISOU 3251  CA  VAL A 409     9003   9712   9313    -19   -226   -125       C  
ATOM   3252  C   VAL A 409      26.834  -6.017  18.229  1.00 67.57           C  
ANISOU 3252  C   VAL A 409     8214   8925   8534    -34   -228   -132       C  
ATOM   3253  O   VAL A 409      27.114  -4.933  18.716  1.00 59.12           O  
ANISOU 3253  O   VAL A 409     7142   7861   7460    -48   -235   -141       O  
ATOM   3254  CB  VAL A 409      27.123  -8.420  19.108  1.00 83.25           C  
ANISOU 3254  CB  VAL A 409    10192  10925  10516     -3   -223   -109       C  
ATOM   3255  CG1 VAL A 409      28.614  -8.150  19.309  1.00 85.72           C  
ANISOU 3255  CG1 VAL A 409    10485  11260  10825     -8   -231   -103       C  
ATOM   3256  CG2 VAL A 409      26.585  -9.372  20.173  1.00 82.47           C  
ANISOU 3256  CG2 VAL A 409    10096  10828  10410     10   -222   -102       C  
ATOM   3257  N   ARG A 410      26.951  -6.261  16.926  1.00 75.79           N  
ANISOU 3257  N   ARG A 410     9255   9956   9585    -30   -220   -129       N  
ATOM   3258  CA  ARG A 410      27.499  -5.254  16.001  1.00 83.82           C  
ANISOU 3258  CA  ARG A 410    10267  10972  10609    -43   -220   -134       C  
ATOM   3259  C   ARG A 410      26.923  -3.881  16.361  1.00 83.85           C  
ANISOU 3259  C   ARG A 410    10279  10969  10613    -59   -224   -146       C  
ATOM   3260  O   ARG A 410      27.664  -2.906  16.573  1.00 82.90           O  
ANISOU 3260  O   ARG A 410    10150  10856  10491    -72   -230   -152       O  
ATOM   3261  CB  ARG A 410      27.153  -5.598  14.529  1.00 92.37           C  
ANISOU 3261  CB  ARG A 410    11356  12041  11701    -38   -209   -132       C  
ATOM   3262  CG  ARG A 410      28.214  -5.243  13.475  1.00 87.32           C  
ANISOU 3262  CG  ARG A 410    10706  11405  11067    -41   -206   -128       C  
ATOM   3263  CD  ARG A 410      28.938  -6.478  12.950  1.00 96.53           C  
ANISOU 3263  CD  ARG A 410    11866  12576  12235    -26   -197   -117       C  
ATOM   3264  NE  ARG A 410      28.459  -6.957  11.634  1.00104.14           N  
ANISOU 3264  NE  ARG A 410    12841  13525  13203    -21   -186   -117       N  
ATOM   3265  CZ  ARG A 410      28.663  -8.195  11.134  1.00103.58           C  
ANISOU 3265  CZ  ARG A 410    12772  13451  13132     -7   -175   -111       C  
ATOM   3266  NH1 ARG A 410      29.299  -9.135  11.826  1.00112.73           N1+
ANISOU 3266  NH1 ARG A 410    13923  14619  14291      5   -173   -101       N1+
ATOM   3267  NH2 ARG A 410      28.206  -8.528   9.933  1.00 90.11           N  
ANISOU 3267  NH2 ARG A 410    11078  11732  11427     -6   -166   -113       N  
ATOM   3268  N   TYR A 411      25.600  -3.836  16.487  1.00 81.63           N  
ANISOU 3268  N   TYR A 411    10012  10672  10330    -57   -220   -151       N  
ATOM   3269  CA  TYR A 411      24.887  -2.572  16.524  1.00 81.92           C  
ANISOU 3269  CA  TYR A 411    10058  10697  10371    -69   -219   -160       C  
ATOM   3270  C   TYR A 411      24.817  -1.937  17.888  1.00 72.49           C  
ANISOU 3270  C   TYR A 411     8867   9508   9167    -77   -225   -169       C  
ATOM   3271  O   TYR A 411      25.151  -0.774  18.013  1.00 67.80           O  
ANISOU 3271  O   TYR A 411     8273   8914   8575    -92   -227   -179       O  
ATOM   3272  CB  TYR A 411      23.506  -2.714  15.869  1.00 87.83           C  
ANISOU 3272  CB  TYR A 411    10818  11427  11125    -64   -211   -158       C  
ATOM   3273  CG  TYR A 411      23.663  -2.708  14.368  1.00 98.02           C  
ANISOU 3273  CG  TYR A 411    12107  12712  12424    -65   -206   -154       C  
ATOM   3274  CD1 TYR A 411      24.116  -3.840  13.698  1.00 93.99           C  
ANISOU 3274  CD1 TYR A 411    11592  12205  11913    -55   -203   -147       C  
ATOM   3275  CD2 TYR A 411      23.444  -1.540  13.623  1.00 98.59           C  
ANISOU 3275  CD2 TYR A 411    12180  12775  12504    -75   -202   -157       C  
ATOM   3276  CE1 TYR A 411      24.307  -3.827  12.333  1.00 94.41           C  
ANISOU 3276  CE1 TYR A 411    11644  12255  11972    -55   -198   -144       C  
ATOM   3277  CE2 TYR A 411      23.640  -1.521  12.256  1.00 93.37           C  
ANISOU 3277  CE2 TYR A 411    11516  12111  11848    -76   -198   -152       C  
ATOM   3278  CZ  TYR A 411      24.072  -2.668  11.615  1.00 94.31           C  
ANISOU 3278  CZ  TYR A 411    11633  12236  11966    -66   -196   -146       C  
ATOM   3279  OH  TYR A 411      24.275  -2.680  10.246  1.00 99.63           O  
ANISOU 3279  OH  TYR A 411    12306  12907  12642    -66   -191   -142       O  
ATOM   3280  N   THR A 412      24.412  -2.680  18.903  1.00 74.07           N  
ANISOU 3280  N   THR A 412     9072   9714   9358    -68   -227   -167       N  
ATOM   3281  CA  THR A 412      24.423  -2.157  20.262  1.00 84.23           C  
ANISOU 3281  CA  THR A 412    10363  11009  10633    -75   -232   -176       C  
ATOM   3282  C   THR A 412      25.771  -1.504  20.588  1.00 89.47           C  
ANISOU 3282  C   THR A 412    11014  11689  11290    -90   -243   -182       C  
ATOM   3283  O   THR A 412      25.815  -0.378  21.094  1.00 78.63           O  
ANISOU 3283  O   THR A 412     9647  10315   9914   -105   -245   -195       O  
ATOM   3284  CB  THR A 412      24.134  -3.264  21.304  1.00 87.19           C  
ANISOU 3284  CB  THR A 412    10739  11393  10995    -61   -235   -169       C  
ATOM   3285  CG2 THR A 412      24.115  -2.686  22.716  1.00 84.53           C  
ANISOU 3285  CG2 THR A 412    10409  11066  10643    -69   -240   -179       C  
ATOM   3286  OG1 THR A 412      22.859  -3.869  21.033  1.00 87.54           O  
ANISOU 3286  OG1 THR A 412    10794  11421  11046    -49   -225   -163       O  
ATOM   3287  N   LYS A 413      26.867  -2.203  20.284  1.00 96.35           N  
ANISOU 3287  N   LYS A 413    11869  12577  12162    -85   -248   -171       N  
ATOM   3288  CA  LYS A 413      28.216  -1.682  20.554  1.00100.12           C  
ANISOU 3288  CA  LYS A 413    12332  13074  12636    -98   -259   -173       C  
ATOM   3289  C   LYS A 413      28.511  -0.512  19.698  1.00 92.07           C  
ANISOU 3289  C   LYS A 413    11310  12044  11628   -114   -256   -181       C  
ATOM   3290  O   LYS A 413      29.188   0.396  20.125  1.00 98.29           O  
ANISOU 3290  O   LYS A 413    12093  12839  12413   -131   -264   -190       O  
ATOM   3291  CB  LYS A 413      29.294  -2.715  20.263  1.00117.40           C  
ANISOU 3291  CB  LYS A 413    14502  15281  14826    -88   -262   -157       C  
ATOM   3292  CG  LYS A 413      29.625  -3.575  21.451  1.00134.24           C  
ANISOU 3292  CG  LYS A 413    16628  17435  16944    -79   -271   -148       C  
ATOM   3293  CD  LYS A 413      30.382  -4.816  21.033  1.00148.11           C  
ANISOU 3293  CD  LYS A 413    18368  19202  18705    -62   -268   -128       C  
ATOM   3294  CE  LYS A 413      31.224  -5.331  22.183  1.00164.21           C  
ANISOU 3294  CE  LYS A 413    20392  21270  20731    -59   -280   -118       C  
ATOM   3295  NZ  LYS A 413      32.372  -6.149  21.696  1.00183.33           N1+
ANISOU 3295  NZ  LYS A 413    22791  23706  23160    -48   -278    -98       N1+
ATOM   3296  N   LYS A 414      28.026  -0.566  18.468  1.00 84.36           N  
ANISOU 3296  N   LYS A 414    10338  11051  10665   -107   -246   -177       N  
ATOM   3297  CA  LYS A 414      28.250   0.492  17.532  1.00 76.97           C  
ANISOU 3297  CA  LYS A 414     9400  10104   9742   -119   -241   -181       C  
ATOM   3298  C   LYS A 414      27.470   1.763  17.892  1.00 74.17           C  
ANISOU 3298  C   LYS A 414     9060   9733   9389   -133   -237   -196       C  
ATOM   3299  O   LYS A 414      27.910   2.864  17.564  1.00 67.90           O  
ANISOU 3299  O   LYS A 414     8262   8933   8602   -148   -236   -202       O  
ATOM   3300  CB  LYS A 414      27.830   0.011  16.176  1.00 83.76           C  
ANISOU 3300  CB  LYS A 414    10262  10952  10612   -108   -231   -172       C  
ATOM   3301  CG  LYS A 414      28.807   0.414  15.117  1.00 93.86           C  
ANISOU 3301  CG  LYS A 414    11527  12233  11901   -113   -229   -167       C  
ATOM   3302  CD  LYS A 414      28.986  -0.705  14.142  1.00 96.05           C  
ANISOU 3302  CD  LYS A 414    11801  12512  12181    -97   -223   -155       C  
ATOM   3303  CE  LYS A 414      27.724  -0.846  13.332  1.00104.56           C  
ANISOU 3303  CE  LYS A 414    12894  13572  13263    -90   -213   -154       C  
ATOM   3304  NZ  LYS A 414      28.109  -0.842  11.908  1.00127.32           N1+
ANISOU 3304  NZ  LYS A 414    15772  16451  16153    -88   -206   -148       N1+
ATOM   3305  N   VAL A 415      26.326   1.607  18.565  1.00 72.14           N  
ANISOU 3305  N   VAL A 415     8818   9466   9125   -127   -233   -200       N  
ATOM   3306  CA  VAL A 415      25.438   2.734  18.902  1.00 74.47           C  
ANISOU 3306  CA  VAL A 415     9128   9743   9423   -137   -226   -212       C  
ATOM   3307  C   VAL A 415      24.601   2.483  20.167  1.00 80.53           C  
ANISOU 3307  C   VAL A 415     9910  10510  10178   -132   -225   -217       C  
ATOM   3308  O   VAL A 415      23.346   2.483  20.114  1.00 72.60           O  
ANISOU 3308  O   VAL A 415     8918   9489   9178   -124   -215   -215       O  
ATOM   3309  CB  VAL A 415      24.471   3.117  17.743  1.00 73.29           C  
ANISOU 3309  CB  VAL A 415     8985   9572   9290   -132   -212   -206       C  
ATOM   3310  CG1 VAL A 415      25.113   4.147  16.824  1.00 75.09           C  
ANISOU 3310  CG1 VAL A 415     9206   9795   9532   -145   -209   -208       C  
ATOM   3311  CG2 VAL A 415      23.981   1.899  16.960  1.00 73.18           C  
ANISOU 3311  CG2 VAL A 415     8969   9558   9278   -115   -210   -192       C  
ATOM   3312  N   PRO A 416      25.291   2.335  21.323  1.00 81.58           N  
ANISOU 3312  N   PRO A 416    10040  10662  10295   -138   -237   -224       N  
ATOM   3313  CA  PRO A 416      24.688   1.899  22.593  1.00 82.07           C  
ANISOU 3313  CA  PRO A 416    10114  10730  10341   -131   -238   -227       C  
ATOM   3314  C   PRO A 416      23.640   2.843  23.191  1.00 81.62           C  
ANISOU 3314  C   PRO A 416    10076  10652  10282   -137   -227   -240       C  
ATOM   3315  O   PRO A 416      22.824   2.409  24.031  1.00 80.85           O  
ANISOU 3315  O   PRO A 416     9990  10554  10174   -127   -223   -239       O  
ATOM   3316  CB  PRO A 416      25.876   1.799  23.546  1.00 80.54           C  
ANISOU 3316  CB  PRO A 416     9910  10563  10130   -142   -254   -231       C  
ATOM   3317  CG  PRO A 416      27.085   2.093  22.739  1.00 87.98           C  
ANISOU 3317  CG  PRO A 416    10834  11513  11081   -152   -261   -229       C  
ATOM   3318  CD  PRO A 416      26.652   2.836  21.528  1.00 81.10           C  
ANISOU 3318  CD  PRO A 416     9966  10617  10229   -155   -248   -230       C  
ATOM   3319  N   GLN A 417      23.651   4.104  22.754  1.00 77.19           N  
ANISOU 3319  N   GLN A 417     9520  10076   9732   -152   -219   -250       N  
ATOM   3320  CA  GLN A 417      22.750   5.114  23.301  1.00 78.00           C  
ANISOU 3320  CA  GLN A 417     9642  10158   9835   -158   -206   -263       C  
ATOM   3321  C   GLN A 417      21.259   4.820  22.993  1.00 79.96           C  
ANISOU 3321  C   GLN A 417     9901  10387  10094   -141   -191   -252       C  
ATOM   3322  O   GLN A 417      20.371   5.189  23.781  1.00 62.99           O  
ANISOU 3322  O   GLN A 417     7768   8226   7940   -139   -180   -258       O  
ATOM   3323  CB  GLN A 417      23.171   6.516  22.815  1.00 83.34           C  
ANISOU 3323  CB  GLN A 417    10320  10820  10525   -178   -200   -274       C  
ATOM   3324  CG  GLN A 417      24.610   6.933  23.160  1.00 87.79           C  
ANISOU 3324  CG  GLN A 417    10874  11403  11081   -199   -215   -286       C  
ATOM   3325  CD  GLN A 417      25.600   6.834  21.987  1.00 92.27           C  
ANISOU 3325  CD  GLN A 417    11419  11977  11661   -201   -222   -276       C  
ATOM   3326  NE2 GLN A 417      26.809   7.384  22.180  1.00 90.11           N  
ANISOU 3326  NE2 GLN A 417    11136  11716  11385   -221   -233   -285       N  
ATOM   3327  OE1 GLN A 417      25.295   6.255  20.939  1.00 90.41           O  
ANISOU 3327  OE1 GLN A 417    11176  11737  11437   -186   -218   -260       O  
ATOM   3328  N   VAL A 418      21.008   4.136  21.862  1.00 92.42           N  
ANISOU 3328  N   VAL A 418    11469  11963  11684   -129   -190   -235       N  
ATOM   3329  CA  VAL A 418      19.634   3.866  21.351  1.00 94.44           C  
ANISOU 3329  CA  VAL A 418    11731  12201  11952   -114   -178   -223       C  
ATOM   3330  C   VAL A 418      18.885   2.823  22.155  1.00 84.22           C  
ANISOU 3330  C   VAL A 418    10442  10912  10647    -99   -178   -216       C  
ATOM   3331  O   VAL A 418      19.473   1.885  22.667  1.00 80.08           O  
ANISOU 3331  O   VAL A 418     9911  10406  10109    -94   -189   -214       O  
ATOM   3332  CB  VAL A 418      19.638   3.393  19.873  1.00100.10           C  
ANISOU 3332  CB  VAL A 418    12435  12916  12682   -108   -179   -208       C  
ATOM   3333  CG1 VAL A 418      18.274   2.841  19.448  1.00 96.77           C  
ANISOU 3333  CG1 VAL A 418    12018  12483  12269    -94   -171   -194       C  
ATOM   3334  CG2 VAL A 418      20.061   4.533  18.942  1.00106.36           C  
ANISOU 3334  CG2 VAL A 418    13223  13699  13488   -121   -174   -211       C  
ATOM   3335  N   SER A 419      17.570   2.985  22.222  1.00 84.71           N  
ANISOU 3335  N   SER A 419    10514  10956  10716    -91   -165   -210       N  
ATOM   3336  CA  SER A 419      16.738   2.141  23.064  1.00 87.36           C  
ANISOU 3336  CA  SER A 419    10856  11292  11043    -77   -162   -203       C  
ATOM   3337  C   SER A 419      16.873   0.688  22.725  1.00 80.54           C  
ANISOU 3337  C   SER A 419     9982  10442  10179    -65   -172   -191       C  
ATOM   3338  O   SER A 419      17.097   0.299  21.576  1.00 82.01           O  
ANISOU 3338  O   SER A 419    10158  10629  10375    -64   -176   -183       O  
ATOM   3339  CB  SER A 419      15.257   2.483  22.943  1.00101.99           C  
ANISOU 3339  CB  SER A 419    12718  13124  12910    -69   -146   -194       C  
ATOM   3340  OG  SER A 419      14.574   1.471  22.203  1.00112.60           O  
ANISOU 3340  OG  SER A 419    14054  14466  14262    -57   -147   -177       O  
ATOM   3341  N   THR A 420      16.661  -0.093  23.766  1.00 75.80           N  
ANISOU 3341  N   THR A 420     9385   9850   9565    -55   -174   -188       N  
ATOM   3342  CA  THR A 420      16.796  -1.526  23.762  1.00 74.93           C  
ANISOU 3342  CA  THR A 420     9267   9752   9452    -42   -181   -177       C  
ATOM   3343  C   THR A 420      15.758  -2.231  22.848  1.00 76.41           C  
ANISOU 3343  C   THR A 420     9452   9927   9656    -32   -175   -161       C  
ATOM   3344  O   THR A 420      16.136  -2.994  21.972  1.00 71.53           O  
ANISOU 3344  O   THR A 420     8824   9312   9042    -30   -181   -155       O  
ATOM   3345  CB  THR A 420      16.734  -2.005  25.229  1.00 76.90           C  
ANISOU 3345  CB  THR A 420     9522  10013   9683    -35   -182   -177       C  
ATOM   3346  CG2 THR A 420      16.893  -3.481  25.344  1.00 78.22           C  
ANISOU 3346  CG2 THR A 420     9680  10191   9847    -21   -188   -164       C  
ATOM   3347  OG1 THR A 420      17.778  -1.357  25.976  1.00 81.96           O  
ANISOU 3347  OG1 THR A 420    10164  10669  10307    -47   -190   -192       O  
ATOM   3348  N   PRO A 421      14.452  -1.964  23.017  1.00 76.66           N  
ANISOU 3348  N   PRO A 421     9492   9942   9695    -27   -164   -156       N  
ATOM   3349  CA  PRO A 421      13.527  -2.656  22.131  1.00 72.43           C  
ANISOU 3349  CA  PRO A 421     8952   9396   9174    -20   -161   -141       C  
ATOM   3350  C   PRO A 421      13.738  -2.265  20.673  1.00 70.03           C  
ANISOU 3350  C   PRO A 421     8640   9087   8880    -29   -164   -140       C  
ATOM   3351  O   PRO A 421      13.437  -3.058  19.779  1.00 70.60           O  
ANISOU 3351  O   PRO A 421     8707   9157   8960    -25   -167   -130       O  
ATOM   3352  CB  PRO A 421      12.149  -2.165  22.603  1.00 75.00           C  
ANISOU 3352  CB  PRO A 421     9285   9705   9505    -15   -148   -134       C  
ATOM   3353  CG  PRO A 421      12.367  -1.478  23.891  1.00 73.27           C  
ANISOU 3353  CG  PRO A 421     9077   9488   9273    -16   -142   -146       C  
ATOM   3354  CD  PRO A 421      13.761  -0.962  23.840  1.00 78.62           C  
ANISOU 3354  CD  PRO A 421     9753  10179   9941    -29   -152   -161       C  
ATOM   3355  N   THR A 422      14.232  -1.052  20.443  1.00 64.06           N  
ANISOU 3355  N   THR A 422     7886   8328   8126    -40   -162   -149       N  
ATOM   3356  CA  THR A 422      14.516  -0.609  19.102  1.00 68.19           C  
ANISOU 3356  CA  THR A 422     8401   8848   8659    -48   -164   -148       C  
ATOM   3357  C   THR A 422      15.583  -1.485  18.492  1.00 69.92           C  
ANISOU 3357  C   THR A 422     8612   9082   8874    -48   -175   -148       C  
ATOM   3358  O   THR A 422      15.369  -2.054  17.431  1.00 73.00           O  
ANISOU 3358  O   THR A 422     8997   9471   9270    -46   -177   -140       O  
ATOM   3359  CB  THR A 422      14.919   0.872  19.076  1.00 74.96           C  
ANISOU 3359  CB  THR A 422     9263   9701   9520    -60   -158   -158       C  
ATOM   3360  CG2 THR A 422      15.610   1.273  17.773  1.00 75.54           C  
ANISOU 3360  CG2 THR A 422     9327   9775   9600    -68   -162   -157       C  
ATOM   3361  OG1 THR A 422      13.731   1.651  19.191  1.00 86.44           O  
ANISOU 3361  OG1 THR A 422    10723  11136  10984    -58   -145   -152       O  
ATOM   3362  N   LEU A 423      16.718  -1.622  19.162  1.00 73.06           N  
ANISOU 3362  N   LEU A 423     9006   9493   9259    -50   -182   -157       N  
ATOM   3363  CA  LEU A 423      17.820  -2.423  18.612  1.00 81.43           C  
ANISOU 3363  CA  LEU A 423    10057  10567  10316    -49   -190   -156       C  
ATOM   3364  C   LEU A 423      17.367  -3.851  18.324  1.00 68.50           C  
ANISOU 3364  C   LEU A 423     8418   8929   8680    -37   -191   -146       C  
ATOM   3365  O   LEU A 423      17.661  -4.408  17.285  1.00 58.78           O  
ANISOU 3365  O   LEU A 423     7182   7699   7453    -36   -192   -142       O  
ATOM   3366  CB  LEU A 423      19.028  -2.430  19.567  1.00 96.45           C  
ANISOU 3366  CB  LEU A 423    11955  12487  12205    -51   -198   -164       C  
ATOM   3367  CG  LEU A 423      19.718  -1.074  19.819  1.00112.55           C  
ANISOU 3367  CG  LEU A 423    13994  14528  14242    -66   -199   -177       C  
ATOM   3368  CD1 LEU A 423      20.366  -1.002  21.198  1.00119.09           C  
ANISOU 3368  CD1 LEU A 423    14824  15371  15054    -70   -206   -185       C  
ATOM   3369  CD2 LEU A 423      20.759  -0.791  18.746  1.00116.83           C  
ANISOU 3369  CD2 LEU A 423    14525  15075  14790    -74   -203   -177       C  
ATOM   3370  N   VAL A 424      16.619  -4.412  19.254  1.00 67.39           N  
ANISOU 3370  N   VAL A 424     8282   8786   8536    -28   -188   -142       N  
ATOM   3371  CA  VAL A 424      16.144  -5.780  19.162  1.00 68.23           C  
ANISOU 3371  CA  VAL A 424     8388   8891   8644    -16   -188   -132       C  
ATOM   3372  C   VAL A 424      15.378  -5.962  17.870  1.00 65.50           C  
ANISOU 3372  C   VAL A 424     8043   8533   8311    -19   -185   -126       C  
ATOM   3373  O   VAL A 424      15.749  -6.773  17.064  1.00 67.52           O  
ANISOU 3373  O   VAL A 424     8296   8791   8568    -18   -188   -124       O  
ATOM   3374  CB  VAL A 424      15.219  -6.139  20.367  1.00 79.01           C  
ANISOU 3374  CB  VAL A 424     9760  10253  10008     -7   -183   -127       C  
ATOM   3375  CG1 VAL A 424      14.570  -7.513  20.202  1.00 75.71           C  
ANISOU 3375  CG1 VAL A 424     9341   9829   9595      3   -181   -115       C  
ATOM   3376  CG2 VAL A 424      15.976  -6.063  21.691  1.00 81.44           C  
ANISOU 3376  CG2 VAL A 424    10068  10576  10300     -4   -186   -132       C  
ATOM   3377  N   GLU A 425      14.296  -5.216  17.686  1.00 65.43           N  
ANISOU 3377  N   GLU A 425     8039   8513   8310    -23   -181   -122       N  
ATOM   3378  CA  GLU A 425      13.467  -5.378  16.527  1.00 67.45           C  
ANISOU 3378  CA  GLU A 425     8294   8760   8576    -27   -180   -115       C  
ATOM   3379  C   GLU A 425      14.344  -5.157  15.353  1.00 65.68           C  
ANISOU 3379  C   GLU A 425     8065   8541   8350    -34   -184   -119       C  
ATOM   3380  O   GLU A 425      14.461  -6.020  14.510  1.00 65.88           O  
ANISOU 3380  O   GLU A 425     8089   8567   8376    -34   -187   -117       O  
ATOM   3381  CB  GLU A 425      12.341  -4.347  16.507  1.00 78.21           C  
ANISOU 3381  CB  GLU A 425     9658  10110   9946    -30   -174   -109       C  
ATOM   3382  CG  GLU A 425      11.414  -4.378  15.279  1.00 82.43           C  
ANISOU 3382  CG  GLU A 425    10190  10639  10491    -35   -175    -98       C  
ATOM   3383  CD  GLU A 425      10.343  -3.270  15.308  1.00 89.67           C  
ANISOU 3383  CD  GLU A 425    11107  11546  11418    -37   -167    -89       C  
ATOM   3384  OE1 GLU A 425      10.714  -2.089  15.547  1.00 89.34           O  
ANISOU 3384  OE1 GLU A 425    11067  11502  11377    -41   -161    -94       O  
ATOM   3385  OE2 GLU A 425       9.133  -3.571  15.101  1.00 84.78           O1-
ANISOU 3385  OE2 GLU A 425    10486  10919  10807    -36   -166    -75       O1-
ATOM   3386  N   VAL A 426      14.986  -4.001  15.312  1.00 75.36           N  
ANISOU 3386  N   VAL A 426     9289   9770   9576    -41   -184   -126       N  
ATOM   3387  CA  VAL A 426      15.687  -3.582  14.099  1.00 88.48           C  
ANISOU 3387  CA  VAL A 426    10945  11434  11238    -49   -186   -128       C  
ATOM   3388  C   VAL A 426      16.720  -4.614  13.684  1.00 93.91           C  
ANISOU 3388  C   VAL A 426    11630  12132  11920    -45   -190   -130       C  
ATOM   3389  O   VAL A 426      16.794  -5.017  12.520  1.00 97.12           O  
ANISOU 3389  O   VAL A 426    12036  12538  12328    -47   -190   -128       O  
ATOM   3390  CB  VAL A 426      16.356  -2.200  14.222  1.00 90.62           C  
ANISOU 3390  CB  VAL A 426    11215  11707  11511    -57   -184   -134       C  
ATOM   3391  CG1 VAL A 426      17.290  -1.950  13.024  1.00 88.11           C  
ANISOU 3391  CG1 VAL A 426    10890  11394  11193    -63   -185   -136       C  
ATOM   3392  CG2 VAL A 426      15.285  -1.111  14.328  1.00 88.70           C  
ANISOU 3392  CG2 VAL A 426    10975  11451  11276    -60   -176   -130       C  
ATOM   3393  N   SER A 427      17.503  -5.073  14.635  1.00 95.99           N  
ANISOU 3393  N   SER A 427    11892  12404  12177    -39   -192   -134       N  
ATOM   3394  CA  SER A 427      18.433  -6.126  14.320  1.00 97.76           C  
ANISOU 3394  CA  SER A 427    12112  12636  12398    -33   -193   -134       C  
ATOM   3395  C   SER A 427      17.726  -7.422  13.874  1.00 89.18           C  
ANISOU 3395  C   SER A 427    11030  11542  11313    -27   -191   -129       C  
ATOM   3396  O   SER A 427      18.147  -8.014  12.882  1.00 89.97           O  
ANISOU 3396  O   SER A 427    11129  11642  11412    -27   -189   -129       O  
ATOM   3397  CB  SER A 427      19.370  -6.348  15.493  1.00101.79           C  
ANISOU 3397  CB  SER A 427    12616  13158  12900    -28   -196   -136       C  
ATOM   3398  OG  SER A 427      20.107  -5.153  15.753  1.00 92.39           O  
ANISOU 3398  OG  SER A 427    11422  11975  11708    -37   -199   -143       O  
ATOM   3399  N   ARG A 428      16.663  -7.833  14.578  1.00 80.27           N  
ANISOU 3399  N   ARG A 428     9906  10406  10186    -22   -189   -124       N  
ATOM   3400  CA  ARG A 428      15.905  -9.053  14.244  1.00 79.17           C  
ANISOU 3400  CA  ARG A 428     9772  10259  10052    -18   -187   -119       C  
ATOM   3401  C   ARG A 428      15.515  -9.056  12.785  1.00 81.95           C  
ANISOU 3401  C   ARG A 428    10127  10606  10407    -27   -188   -119       C  
ATOM   3402  O   ARG A 428      15.726 -10.036  12.079  1.00 96.76           O  
ANISOU 3402  O   ARG A 428    12005  12479  12281    -26   -186   -120       O  
ATOM   3403  CB  ARG A 428      14.623  -9.171  15.073  1.00 79.78           C  
ANISOU 3403  CB  ARG A 428     9853  10328  10134    -15   -186   -112       C  
ATOM   3404  CG  ARG A 428      14.757  -9.948  16.364  1.00 81.89           C  
ANISOU 3404  CG  ARG A 428    10119  10598  10398     -2   -184   -109       C  
ATOM   3405  CD  ARG A 428      13.414 -10.077  17.081  1.00 90.83           C  
ANISOU 3405  CD  ARG A 428    11255  11721  11535      1   -181   -101       C  
ATOM   3406  NE  ARG A 428      12.816 -11.437  17.075  1.00 89.83           N  
ANISOU 3406  NE  ARG A 428    11129  11586  11414      7   -178    -94       N  
ATOM   3407  CZ  ARG A 428      11.671 -11.802  16.471  1.00 87.77           C  
ANISOU 3407  CZ  ARG A 428    10872  11314  11163      2   -177    -89       C  
ATOM   3408  NH1 ARG A 428      10.926 -10.935  15.768  1.00 90.67           N1+
ANISOU 3408  NH1 ARG A 428    11239  11677  11535     -8   -181    -87       N1+
ATOM   3409  NH2 ARG A 428      11.252 -13.060  16.577  1.00 81.72           N  
ANISOU 3409  NH2 ARG A 428    10107  10540  10403      7   -174    -84       N  
ATOM   3410  N   ASN A 429      14.933  -7.951  12.341  1.00 76.68           N  
ANISOU 3410  N   ASN A 429     9458   9935   9741    -36   -190   -117       N  
ATOM   3411  CA  ASN A 429      14.525  -7.805  10.964  1.00 77.40           C  
ANISOU 3411  CA  ASN A 429     9550  10024   9833    -45   -192   -115       C  
ATOM   3412  C   ASN A 429      15.729  -7.773  10.034  1.00 81.77           C  
ANISOU 3412  C   ASN A 429    10102  10585  10381    -47   -191   -122       C  
ATOM   3413  O   ASN A 429      15.704  -8.408   8.972  1.00 96.04           O  
ANISOU 3413  O   ASN A 429    11914  12391  12185    -51   -191   -123       O  
ATOM   3414  CB  ASN A 429      13.682  -6.550  10.802  1.00 81.30           C  
ANISOU 3414  CB  ASN A 429    10042  10515  10333    -52   -193   -109       C  
ATOM   3415  CG  ASN A 429      12.427  -6.566  11.676  1.00 79.39           C  
ANISOU 3415  CG  ASN A 429     9802  10266  10099    -49   -191   -101       C  
ATOM   3416  ND2 ASN A 429      11.581  -5.519  11.555  1.00 72.88           N  
ANISOU 3416  ND2 ASN A 429     8975   9437   9281    -53   -190    -93       N  
ATOM   3417  OD1 ASN A 429      12.226  -7.499  12.459  1.00 77.71           O  
ANISOU 3417  OD1 ASN A 429     9591  10050   9886    -41   -190   -101       O  
ATOM   3418  N   LEU A 430      16.784  -7.053  10.428  1.00 79.72           N  
ANISOU 3418  N   LEU A 430     9838  10333  10120    -46   -190   -125       N  
ATOM   3419  CA  LEU A 430      18.049  -7.069   9.667  1.00 81.61           C  
ANISOU 3419  CA  LEU A 430    10073  10579  10354    -46   -188   -130       C  
ATOM   3420  C   LEU A 430      18.542  -8.506   9.446  1.00 86.62           C  
ANISOU 3420  C   LEU A 430    10712  11214  10986    -38   -184   -132       C  
ATOM   3421  O   LEU A 430      19.162  -8.805   8.432  1.00 88.01           O  
ANISOU 3421  O   LEU A 430    10890  11393  11159    -39   -181   -134       O  
ATOM   3422  CB  LEU A 430      19.156  -6.235  10.341  1.00 79.44           C  
ANISOU 3422  CB  LEU A 430     9791  10314  10080    -45   -189   -133       C  
ATOM   3423  CG  LEU A 430      19.103  -4.701  10.266  1.00 86.10           C  
ANISOU 3423  CG  LEU A 430    10630  11157  10927    -55   -189   -133       C  
ATOM   3424  CD1 LEU A 430      20.015  -4.045  11.291  1.00 99.01           C  
ANISOU 3424  CD1 LEU A 430    12259  12799  12562    -55   -191   -138       C  
ATOM   3425  CD2 LEU A 430      19.459  -4.183   8.889  1.00 84.00           C  
ANISOU 3425  CD2 LEU A 430    10361  10892  10662    -61   -187   -131       C  
ATOM   3426  N   GLY A 431      18.269  -9.390  10.398  1.00 87.69           N  
ANISOU 3426  N   GLY A 431    10849  11346  11123    -30   -183   -130       N  
ATOM   3427  CA  GLY A 431      18.584 -10.800  10.224  1.00 85.87           C  
ANISOU 3427  CA  GLY A 431    10624  11113  10892    -22   -177   -131       C  
ATOM   3428  C   GLY A 431      17.717 -11.429   9.153  1.00 85.09           C  
ANISOU 3428  C   GLY A 431    10535  11004  10792    -29   -177   -133       C  
ATOM   3429  O   GLY A 431      18.201 -12.159   8.275  1.00 85.35           O  
ANISOU 3429  O   GLY A 431    10573  11034  10821    -28   -170   -137       O  
ATOM   3430  N   LYS A 432      16.435 -11.090   9.207  1.00 82.01           N  
ANISOU 3430  N   LYS A 432    10147  10609  10406    -36   -182   -129       N  
ATOM   3431  CA  LYS A 432      15.422 -11.647   8.309  1.00 85.92           C  
ANISOU 3431  CA  LYS A 432    10650  11095  10899    -45   -184   -130       C  
ATOM   3432  C   LYS A 432      15.749 -11.411   6.841  1.00 86.82           C  
ANISOU 3432  C   LYS A 432    10768  11213  11006    -54   -185   -134       C  
ATOM   3433  O   LYS A 432      15.139 -12.020   5.972  1.00 86.05           O  
ANISOU 3433  O   LYS A 432    10679  11111  10905    -63   -186   -137       O  
ATOM   3434  CB  LYS A 432      14.003 -11.114   8.662  1.00 91.18           C  
ANISOU 3434  CB  LYS A 432    11314  11757  11572    -51   -191   -122       C  
ATOM   3435  CG  LYS A 432      13.434 -11.639   9.999  1.00 81.68           C  
ANISOU 3435  CG  LYS A 432    10109  10548  10376    -43   -190   -117       C  
ATOM   3436  CD  LYS A 432      12.075 -11.065  10.381  1.00 74.28           C  
ANISOU 3436  CD  LYS A 432     9170   9607   9446    -47   -194   -107       C  
ATOM   3437  CE  LYS A 432      11.638 -11.513  11.780  1.00 79.54           C  
ANISOU 3437  CE  LYS A 432     9834  10268  10118    -37   -191   -101       C  
ATOM   3438  NZ  LYS A 432      10.155 -11.707  12.011  1.00 76.05           N1+
ANISOU 3438  NZ  LYS A 432     9391   9817   9686    -40   -193    -91       N1+
ATOM   3439  N   VAL A 433      16.722 -10.541   6.574  1.00 94.83           N  
ANISOU 3439  N   VAL A 433    11778  12237  12018    -53   -183   -135       N  
ATOM   3440  CA  VAL A 433      17.244 -10.355   5.215  1.00108.74           C  
ANISOU 3440  CA  VAL A 433    13542  14002  13770    -59   -181   -139       C  
ATOM   3441  C   VAL A 433      17.862 -11.666   4.674  1.00101.69           C  
ANISOU 3441  C   VAL A 433    12659  13105  12872    -54   -171   -146       C  
ATOM   3442  O   VAL A 433      17.550 -12.104   3.553  1.00103.21           O  
ANISOU 3442  O   VAL A 433    12863  13295  13057    -63   -171   -151       O  
ATOM   3443  CB  VAL A 433      18.259  -9.168   5.130  1.00109.74           C  
ANISOU 3443  CB  VAL A 433    13659  14139  13897    -58   -179   -137       C  
ATOM   3444  CG1 VAL A 433      19.597  -9.526   5.760  1.00114.29           C  
ANISOU 3444  CG1 VAL A 433    14230  14719  14475    -46   -172   -139       C  
ATOM   3445  CG2 VAL A 433      18.476  -8.724   3.683  1.00112.55           C  
ANISOU 3445  CG2 VAL A 433    14019  14501  14246    -65   -178   -137       C  
ATOM   3446  N   GLY A 434      18.694 -12.304   5.487  1.00 88.96           N  
ANISOU 3446  N   GLY A 434    11045  11491  11264    -42   -164   -147       N  
ATOM   3447  CA  GLY A 434      19.382 -13.499   5.070  1.00 88.10           C  
ANISOU 3447  CA  GLY A 434    10944  11376  11153    -35   -152   -152       C  
ATOM   3448  C   GLY A 434      18.407 -14.572   4.661  1.00 92.69           C  
ANISOU 3448  C   GLY A 434    11541  11946  11734    -41   -151   -158       C  
ATOM   3449  O   GLY A 434      18.628 -15.302   3.674  1.00 96.15           O  
ANISOU 3449  O   GLY A 434    11991  12378  12165    -44   -142   -166       O  
ATOM   3450  N   SER A 435      17.319 -14.673   5.421  1.00 90.00           N  
ANISOU 3450  N   SER A 435    11197  11599  11398    -44   -158   -154       N  
ATOM   3451  CA  SER A 435      16.316 -15.671   5.133  1.00 93.86           C  
ANISOU 3451  CA  SER A 435    11698  12076  11888    -52   -159   -158       C  
ATOM   3452  C   SER A 435      15.677 -15.285   3.846  1.00 92.35           C  
ANISOU 3452  C   SER A 435    11513  11887  11686    -69   -167   -162       C  
ATOM   3453  O   SER A 435      15.159 -16.136   3.128  1.00103.52           O  
ANISOU 3453  O   SER A 435    12942  13295  13097    -79   -165   -170       O  
ATOM   3454  CB  SER A 435      15.272 -15.760   6.238  1.00102.31           C  
ANISOU 3454  CB  SER A 435    12762  13141  12969    -51   -165   -151       C  
ATOM   3455  OG  SER A 435      15.706 -16.642   7.266  1.00120.28           O  
ANISOU 3455  OG  SER A 435    15038  15411  15254    -36   -156   -148       O  
ATOM   3456  N   LYS A 436      15.720 -13.996   3.532  1.00 89.37           N  
ANISOU 3456  N   LYS A 436    11127  11522  11305    -73   -174   -157       N  
ATOM   3457  CA  LYS A 436      15.155 -13.539   2.278  1.00101.10           C  
ANISOU 3457  CA  LYS A 436    12618  13014  12780    -89   -182   -158       C  
ATOM   3458  C   LYS A 436      16.130 -13.662   1.142  1.00 88.79           C  
ANISOU 3458  C   LYS A 436    11068  11460  11208    -89   -173   -166       C  
ATOM   3459  O   LYS A 436      15.822 -14.265   0.129  1.00108.97           O  
ANISOU 3459  O   LYS A 436    13637  14013  13753   -100   -173   -175       O  
ATOM   3460  CB  LYS A 436      14.614 -12.112   2.378  1.00107.02           C  
ANISOU 3460  CB  LYS A 436    13355  13774  13533    -94   -192   -146       C  
ATOM   3461  CG  LYS A 436      13.393 -11.971   3.281  1.00120.64           C  
ANISOU 3461  CG  LYS A 436    15073  15495  15269    -96   -200   -137       C  
ATOM   3462  CD  LYS A 436      12.357 -13.094   3.126  1.00122.31           C  
ANISOU 3462  CD  LYS A 436    15293  15697  15481   -105   -204   -140       C  
ATOM   3463  CE  LYS A 436      11.469 -13.184   4.358  1.00113.55           C  
ANISOU 3463  CE  LYS A 436    14176  14581  14386   -101   -208   -131       C  
ATOM   3464  NZ  LYS A 436      10.458 -14.259   4.215  1.00114.93           N1+
ANISOU 3464  NZ  LYS A 436    14359  14747  14564   -111   -212   -132       N1+
ATOM   3465  N   CYS A 437      17.316 -13.125   1.302  1.00 79.18           N  
ANISOU 3465  N   CYS A 437     9843  10248   9992    -78   -166   -165       N  
ATOM   3466  CA  CYS A 437      18.164 -12.949   0.146  1.00 87.33           C  
ANISOU 3466  CA  CYS A 437    10881  11287  11013    -79   -158   -169       C  
ATOM   3467  C   CYS A 437      19.220 -14.042  -0.100  1.00 94.57           C  
ANISOU 3467  C   CYS A 437    11809  12196  11927    -69   -141   -178       C  
ATOM   3468  O   CYS A 437      19.462 -14.398  -1.255  1.00109.22           O  
ANISOU 3468  O   CYS A 437    13677  14051  13769    -74   -134   -186       O  
ATOM   3469  CB  CYS A 437      18.806 -11.576   0.205  1.00 95.00           C  
ANISOU 3469  CB  CYS A 437    11838  12270  11987    -75   -160   -160       C  
ATOM   3470  SG  CYS A 437      17.604 -10.242   0.170  1.00107.82           S  
ANISOU 3470  SG  CYS A 437    13451  13902  13613    -88   -176   -149       S  
ATOM   3471  N   CYS A 438      19.854 -14.569   0.943  1.00 86.47           N  
ANISOU 3471  N   CYS A 438    10777  11164  10912    -54   -133   -176       N  
ATOM   3472  CA  CYS A 438      20.863 -15.596   0.734  1.00 89.44           C  
ANISOU 3472  CA  CYS A 438    11161  11532  11288    -42   -114   -181       C  
ATOM   3473  C   CYS A 438      20.291 -16.794  -0.033  1.00 92.08           C  
ANISOU 3473  C   CYS A 438    11518  11853  11615    -50   -107   -194       C  
ATOM   3474  O   CYS A 438      20.996 -17.472  -0.766  1.00 82.32           O  
ANISOU 3474  O   CYS A 438    10295  10612  10373    -46    -90   -202       O  
ATOM   3475  CB  CYS A 438      21.442 -16.050   2.064  1.00100.90           C  
ANISOU 3475  CB  CYS A 438    12603  12981  12754    -26   -108   -174       C  
ATOM   3476  SG  CYS A 438      22.197 -14.734   3.056  1.00113.64           S  
ANISOU 3476  SG  CYS A 438    14191  14611  14375    -18   -116   -162       S  
ATOM   3477  N   LYS A 439      18.998 -17.042   0.149  1.00111.20           N  
ANISOU 3477  N   LYS A 439    13944  14269  14037    -63   -119   -197       N  
ATOM   3478  CA  LYS A 439      18.255 -18.055  -0.608  1.00113.25           C  
ANISOU 3478  CA  LYS A 439    14224  14517  14289    -76   -117   -210       C  
ATOM   3479  C   LYS A 439      18.653 -18.044  -2.072  1.00109.44           C  
ANISOU 3479  C   LYS A 439    13756  14038  13787    -84   -110   -220       C  
ATOM   3480  O   LYS A 439      18.925 -19.089  -2.659  1.00116.32           O  
ANISOU 3480  O   LYS A 439    14647  14897  14652    -85    -95   -233       O  
ATOM   3481  CB  LYS A 439      16.734 -17.795  -0.476  1.00124.30           C  
ANISOU 3481  CB  LYS A 439    15622  15919  15690    -94   -137   -207       C  
ATOM   3482  CG  LYS A 439      15.844 -18.432  -1.542  1.00131.76           C  
ANISOU 3482  CG  LYS A 439    16585  16858  16621   -115   -142   -220       C  
ATOM   3483  CD  LYS A 439      15.620 -19.928  -1.305  1.00135.50           C  
ANISOU 3483  CD  LYS A 439    17074  17310  17101   -115   -130   -231       C  
ATOM   3484  CE  LYS A 439      15.159 -20.663  -2.566  1.00132.93           C  
ANISOU 3484  CE  LYS A 439    16772  16978  16758   -136   -129   -248       C  
ATOM   3485  NZ  LYS A 439      16.253 -20.898  -3.562  1.00127.83           N1+
ANISOU 3485  NZ  LYS A 439    16142  16331  16097   -131   -111   -260       N1+
ATOM   3486  N   HIS A 440      18.704 -16.849  -2.645  1.00105.81           N  
ANISOU 3486  N   HIS A 440    13289  13595  13318    -90   -120   -214       N  
ATOM   3487  CA  HIS A 440      18.839 -16.685  -4.082  1.00112.08           C  
ANISOU 3487  CA  HIS A 440    14096  14397  14092   -100   -117   -222       C  
ATOM   3488  C   HIS A 440      20.253 -16.773  -4.606  1.00123.81           C  
ANISOU 3488  C   HIS A 440    15587  15883  15572    -86    -97   -224       C  
ATOM   3489  O   HIS A 440      21.217 -16.739  -3.822  1.00130.86           O  
ANISOU 3489  O   HIS A 440    16468  16774  16480    -68    -86   -217       O  
ATOM   3490  CB  HIS A 440      18.244 -15.353  -4.483  1.00114.56           C  
ANISOU 3490  CB  HIS A 440    14399  14730  14400   -111   -136   -211       C  
ATOM   3491  CG  HIS A 440      16.781 -15.301  -4.266  1.00134.18           C  
ANISOU 3491  CG  HIS A 440    16881  17215  16886   -127   -155   -208       C  
ATOM   3492  CD2 HIS A 440      16.017 -14.502  -3.490  1.00145.67           C  
ANISOU 3492  CD2 HIS A 440    18318  18676  18353   -129   -170   -194       C  
ATOM   3493  ND1 HIS A 440      15.925 -16.200  -4.864  1.00154.97           N  
ANISOU 3493  ND1 HIS A 440    19532  19842  19509   -144   -159   -220       N  
ATOM   3494  CE1 HIS A 440      14.689 -15.942  -4.482  1.00168.08           C  
ANISOU 3494  CE1 HIS A 440    21183  21506  21175   -156   -177   -212       C  
ATOM   3495  NE2 HIS A 440      14.717 -14.919  -3.645  1.00169.61           N  
ANISOU 3495  NE2 HIS A 440    21356  21706  21383   -146   -183   -196       N  
ATOM   3496  N   PRO A 441      20.385 -16.899  -5.947  1.00122.32           N  
ANISOU 3496  N   PRO A 441    15416  15698  15363    -95    -91   -234       N  
ATOM   3497  CA  PRO A 441      21.700 -16.761  -6.588  1.00112.94           C  
ANISOU 3497  CA  PRO A 441    14231  14514  14169    -82    -71   -234       C  
ATOM   3498  C   PRO A 441      22.193 -15.304  -6.606  1.00104.01           C  
ANISOU 3498  C   PRO A 441    13078  13401  13040    -77    -79   -218       C  
ATOM   3499  O   PRO A 441      21.457 -14.408  -6.216  1.00 98.65           O  
ANISOU 3499  O   PRO A 441    12384  12731  12366    -85    -98   -208       O  
ATOM   3500  CB  PRO A 441      21.456 -17.302  -8.004  1.00111.20           C  
ANISOU 3500  CB  PRO A 441    14037  14292  13923    -96    -65   -250       C  
ATOM   3501  CG  PRO A 441      19.986 -17.209  -8.222  1.00109.03           C  
ANISOU 3501  CG  PRO A 441    13766  14022  13639   -119    -88   -253       C  
ATOM   3502  CD  PRO A 441      19.360 -17.406  -6.884  1.00111.88           C  
ANISOU 3502  CD  PRO A 441    14113  14374  14022   -117    -99   -247       C  
ATOM   3503  N   GLU A 442      23.418 -15.066  -7.070  1.00101.24           N  
ANISOU 3503  N   GLU A 442    12725  13054  12687    -64    -62   -214       N  
ATOM   3504  CA  GLU A 442      24.008 -13.711  -7.020  1.00 91.81           C  
ANISOU 3504  CA  GLU A 442    11510  11876  11499    -59    -67   -198       C  
ATOM   3505  C   GLU A 442      23.616 -12.731  -8.145  1.00 82.69           C  
ANISOU 3505  C   GLU A 442    10355  10736  10326    -72    -76   -194       C  
ATOM   3506  O   GLU A 442      24.079 -11.601  -8.194  1.00 75.98           O  
ANISOU 3506  O   GLU A 442     9489   9899   9482    -68    -78   -181       O  
ATOM   3507  CB  GLU A 442      25.518 -13.780  -6.850  1.00 91.38           C  
ANISOU 3507  CB  GLU A 442    11447  11820  11455    -39    -47   -192       C  
ATOM   3508  CG  GLU A 442      25.922 -13.733  -5.387  1.00 96.15           C  
ANISOU 3508  CG  GLU A 442    12031  12421  12082    -28    -49   -183       C  
ATOM   3509  CD  GLU A 442      27.386 -13.392  -5.190  1.00104.89           C  
ANISOU 3509  CD  GLU A 442    13121  13533  13199    -11    -36   -171       C  
ATOM   3510  OE1 GLU A 442      27.906 -13.689  -4.093  1.00102.05           O  
ANISOU 3510  OE1 GLU A 442    12749  13171  12856      1    -33   -164       O  
ATOM   3511  OE2 GLU A 442      28.016 -12.834  -6.130  1.00110.87           O1-
ANISOU 3511  OE2 GLU A 442    13878  14298  13948    -10    -27   -167       O1-
ATOM   3512  N   ALA A 443      22.714 -13.135  -9.012  1.00 92.32           N  
ANISOU 3512  N   ALA A 443    11594  11958  11527    -88    -82   -205       N  
ATOM   3513  CA  ALA A 443      21.998 -12.157  -9.798  1.00101.53           C  
ANISOU 3513  CA  ALA A 443    12757  13141  12680   -102    -97   -197       C  
ATOM   3514  C   ALA A 443      21.005 -11.510  -8.844  1.00107.43           C  
ANISOU 3514  C   ALA A 443    13486  13891  13443   -108   -118   -187       C  
ATOM   3515  O   ALA A 443      21.120 -10.322  -8.526  1.00120.74           O  
ANISOU 3515  O   ALA A 443    15152  15586  15139   -105   -125   -172       O  
ATOM   3516  CB  ALA A 443      21.281 -12.813 -10.967  1.00105.03           C  
ANISOU 3516  CB  ALA A 443    13224  13587  13096   -119   -100   -211       C  
ATOM   3517  N   LYS A 444      20.089 -12.332  -8.335  1.00112.03           N  
ANISOU 3517  N   LYS A 444    14076  14463  14028   -116   -127   -195       N  
ATOM   3518  CA  LYS A 444      18.940 -11.888  -7.533  1.00123.02           C  
ANISOU 3518  CA  LYS A 444    15455  15856  15432   -125   -146   -187       C  
ATOM   3519  C   LYS A 444      19.290 -11.258  -6.179  1.00109.99           C  
ANISOU 3519  C   LYS A 444    13783  14202  13805   -111   -148   -176       C  
ATOM   3520  O   LYS A 444      18.493 -10.504  -5.633  1.00103.95           O  
ANISOU 3520  O   LYS A 444    13005  13442  13051   -116   -161   -165       O  
ATOM   3521  CB  LYS A 444      17.988 -13.072  -7.265  1.00140.66           C  
ANISOU 3521  CB  LYS A 444    17703  18078  17664   -135   -152   -199       C  
ATOM   3522  CG  LYS A 444      17.407 -13.748  -8.506  1.00151.61           C  
ANISOU 3522  CG  LYS A 444    19111  19468  19025   -153   -155   -212       C  
ATOM   3523  CD  LYS A 444      16.203 -14.621  -8.167  1.00160.13           C  
ANISOU 3523  CD  LYS A 444    20198  20538  20107   -168   -167   -219       C  
ATOM   3524  CE  LYS A 444      15.002 -13.768  -7.754  1.00168.99           C  
ANISOU 3524  CE  LYS A 444    21301  21670  21237   -178   -189   -202       C  
ATOM   3525  NZ  LYS A 444      13.712 -14.515  -7.680  1.00170.06           N1+
ANISOU 3525  NZ  LYS A 444    21442  21800  21371   -196   -203   -207       N1+
ATOM   3526  N   ARG A 445      20.463 -11.569  -5.637  1.00102.34           N  
ANISOU 3526  N   ARG A 445    12811  13226  12846    -95   -133   -178       N  
ATOM   3527  CA  ARG A 445      20.790 -11.174  -4.269  1.00 91.53           C  
ANISOU 3527  CA  ARG A 445    11425  11854  11499    -84   -135   -171       C  
ATOM   3528  C   ARG A 445      20.914  -9.703  -4.047  1.00 85.36           C  
ANISOU 3528  C   ARG A 445    10625  11083  10726    -84   -142   -157       C  
ATOM   3529  O   ARG A 445      20.286  -9.157  -3.154  1.00 93.79           O  
ANISOU 3529  O   ARG A 445    11681  12150  11806    -86   -152   -151       O  
ATOM   3530  CB  ARG A 445      22.078 -11.809  -3.796  1.00 86.66           C  
ANISOU 3530  CB  ARG A 445    10807  11230  10890    -67   -118   -174       C  
ATOM   3531  CG  ARG A 445      21.879 -12.821  -2.699  1.00 86.60           C  
ANISOU 3531  CG  ARG A 445    10802  11209  10893    -61   -116   -178       C  
ATOM   3532  CD  ARG A 445      23.205 -13.000  -2.018  1.00 95.41           C  
ANISOU 3532  CD  ARG A 445    11908  12325  12021    -43   -103   -173       C  
ATOM   3533  NE  ARG A 445      23.473 -14.376  -1.645  1.00102.33           N  
ANISOU 3533  NE  ARG A 445    12793  13187  12901    -34    -90   -180       N  
ATOM   3534  CZ  ARG A 445      24.688 -14.859  -1.398  1.00104.77           C  
ANISOU 3534  CZ  ARG A 445    13099  13494  13216    -18    -73   -176       C  
ATOM   3535  NH1 ARG A 445      25.782 -14.096  -1.493  1.00104.43           N1+
ANISOU 3535  NH1 ARG A 445    13041  13462  13177    -10    -68   -167       N1+
ATOM   3536  NH2 ARG A 445      24.816 -16.126  -1.058  1.00103.13           N  
ANISOU 3536  NH2 ARG A 445    12900  13272  13013     -9    -60   -181       N  
ATOM   3537  N   MET A 446      21.737  -9.046  -4.835  1.00 82.01           N  
ANISOU 3537  N   MET A 446    10197  10668  10296    -81   -134   -152       N  
ATOM   3538  CA  MET A 446      22.061  -7.673  -4.514  1.00 88.80           C  
ANISOU 3538  CA  MET A 446    11038  11535  11167    -79   -138   -140       C  
ATOM   3539  C   MET A 446      20.802  -6.783  -4.419  1.00 93.86           C  
ANISOU 3539  C   MET A 446    11672  12180  11812    -91   -153   -131       C  
ATOM   3540  O   MET A 446      20.591  -6.121  -3.400  1.00 98.11           O  
ANISOU 3540  O   MET A 446    12198  12715  12365    -89   -159   -125       O  
ATOM   3541  CB  MET A 446      23.089  -7.105  -5.503  1.00 98.55           C  
ANISOU 3541  CB  MET A 446    12270  12778  12396    -75   -126   -135       C  
ATOM   3542  CG  MET A 446      24.051  -6.100  -4.870  1.00 94.55           C  
ANISOU 3542  CG  MET A 446    11743  12274  11906    -68   -123   -126       C  
ATOM   3543  SD  MET A 446      24.395  -4.679  -5.934  1.00 96.48           S  
ANISOU 3543  SD  MET A 446    11979  12531  12149    -72   -120   -112       S  
ATOM   3544  CE  MET A 446      25.592  -5.349  -7.103  1.00 94.57           C  
ANISOU 3544  CE  MET A 446    11746  12293  11892    -63   -101   -115       C  
ATOM   3545  N   PRO A 447      19.950  -6.764  -5.461  1.00 93.83           N  
ANISOU 3545  N   PRO A 447    11677  12183  11793   -102   -159   -129       N  
ATOM   3546  CA  PRO A 447      18.770  -5.895  -5.317  1.00 89.08           C  
ANISOU 3546  CA  PRO A 447    11065  11584  11195   -111   -172   -117       C  
ATOM   3547  C   PRO A 447      17.899  -6.317  -4.162  1.00 81.17           C  
ANISOU 3547  C   PRO A 447    10062  10573  10205   -112   -181   -119       C  
ATOM   3548  O   PRO A 447      17.293  -5.490  -3.530  1.00 76.60           O  
ANISOU 3548  O   PRO A 447     9472   9993   9639   -114   -187   -109       O  
ATOM   3549  CB  PRO A 447      18.014  -6.080  -6.642  1.00 97.25           C  
ANISOU 3549  CB  PRO A 447    12110  12630  12209   -124   -178   -115       C  
ATOM   3550  CG  PRO A 447      18.535  -7.359  -7.197  1.00103.04           C  
ANISOU 3550  CG  PRO A 447    12863  13360  12927   -123   -170   -132       C  
ATOM   3551  CD  PRO A 447      19.960  -7.477  -6.748  1.00 92.07           C  
ANISOU 3551  CD  PRO A 447    11471  11965  11547   -108   -155   -137       C  
ATOM   3552  N   CYS A 448      17.847  -7.612  -3.899  1.00 84.94           N  
ANISOU 3552  N   CYS A 448    10552  11043  10680   -111   -179   -132       N  
ATOM   3553  CA  CYS A 448      17.018  -8.154  -2.835  1.00 92.32           C  
ANISOU 3553  CA  CYS A 448    11486  11967  11624   -112   -186   -134       C  
ATOM   3554  C   CYS A 448      17.431  -7.542  -1.512  1.00 86.85           C  
ANISOU 3554  C   CYS A 448    10780  11269  10949   -102   -184   -129       C  
ATOM   3555  O   CYS A 448      16.646  -6.870  -0.852  1.00 89.69           O  
ANISOU 3555  O   CYS A 448    11131  11628  11320   -104   -191   -121       O  
ATOM   3556  CB  CYS A 448      17.164  -9.688  -2.802  1.00100.01           C  
ANISOU 3556  CB  CYS A 448    12477  12932  12593   -111   -181   -149       C  
ATOM   3557  SG  CYS A 448      16.410 -10.608  -1.430  1.00115.22           S  
ANISOU 3557  SG  CYS A 448    14403  14844  14532   -108   -185   -152       S  
ATOM   3558  N   ALA A 449      18.684  -7.764  -1.152  1.00 83.33           N  
ANISOU 3558  N   ALA A 449    10332  10821  10506    -91   -174   -135       N  
ATOM   3559  CA  ALA A 449      19.173  -7.461   0.174  1.00 80.61           C  
ANISOU 3559  CA  ALA A 449     9978  10474  10177    -81   -173   -134       C  
ATOM   3560  C   ALA A 449      19.354  -5.984   0.383  1.00 78.18           C  
ANISOU 3560  C   ALA A 449     9656  10171   9877    -83   -175   -125       C  
ATOM   3561  O   ALA A 449      18.892  -5.454   1.388  1.00 93.72           O  
ANISOU 3561  O   ALA A 449    11618  12136  11856    -82   -179   -121       O  
ATOM   3562  CB  ALA A 449      20.475  -8.200   0.418  1.00 81.45           C  
ANISOU 3562  CB  ALA A 449    10086  10579  10283    -70   -162   -140       C  
ATOM   3563  N   GLU A 450      20.004  -5.305  -0.551  1.00 70.31           N  
ANISOU 3563  N   GLU A 450     8656   9181   8876    -84   -170   -121       N  
ATOM   3564  CA  GLU A 450      20.276  -3.889  -0.358  1.00 79.49           C  
ANISOU 3564  CA  GLU A 450     9806  10348  10050    -85   -169   -113       C  
ATOM   3565  C   GLU A 450      18.966  -3.051  -0.328  1.00 86.15           C  
ANISOU 3565  C   GLU A 450    10646  11189  10898    -93   -177   -103       C  
ATOM   3566  O   GLU A 450      18.905  -1.987   0.317  1.00 75.08           O  
ANISOU 3566  O   GLU A 450     9235   9784   9509    -94   -176    -97       O  
ATOM   3567  CB  GLU A 450      21.295  -3.364  -1.399  1.00 84.00           C  
ANISOU 3567  CB  GLU A 450    10374  10927  10617    -84   -161   -109       C  
ATOM   3568  CG  GLU A 450      22.394  -2.497  -0.776  1.00 91.55           C  
ANISOU 3568  CG  GLU A 450    11316  11883  11585    -81   -157   -107       C  
ATOM   3569  CD  GLU A 450      23.199  -1.651  -1.769  1.00101.51           C  
ANISOU 3569  CD  GLU A 450    12571  13152  12847    -81   -149   -100       C  
ATOM   3570  OE1 GLU A 450      23.395  -2.084  -2.936  1.00110.53           O  
ANISOU 3570  OE1 GLU A 450    13721  14300  13977    -80   -143    -99       O  
ATOM   3571  OE2 GLU A 450      23.655  -0.542  -1.371  1.00 96.29           O1-
ANISOU 3571  OE2 GLU A 450    11897  12489  12198    -83   -147    -95       O1-
ATOM   3572  N   ASP A 451      17.915  -3.536  -1.000  1.00 94.78           N  
ANISOU 3572  N   ASP A 451    11746  12284  11981   -100   -183   -100       N  
ATOM   3573  CA  ASP A 451      16.640  -2.800  -1.065  1.00 89.98           C  
ANISOU 3573  CA  ASP A 451    11133  11676  11378   -107   -189    -87       C  
ATOM   3574  C   ASP A 451      15.742  -3.162   0.086  1.00 85.59           C  
ANISOU 3574  C   ASP A 451    10577  11111  10831   -106   -195    -88       C  
ATOM   3575  O   ASP A 451      14.881  -2.378   0.457  1.00101.68           O  
ANISOU 3575  O   ASP A 451    12609  13147  12880   -108   -197    -77       O  
ATOM   3576  CB  ASP A 451      15.905  -3.012  -2.392  1.00 97.44           C  
ANISOU 3576  CB  ASP A 451    12083  12631  12309   -116   -195    -80       C  
ATOM   3577  CG  ASP A 451      16.492  -2.162  -3.536  1.00117.49           C  
ANISOU 3577  CG  ASP A 451    14617  15180  14842   -117   -190    -72       C  
ATOM   3578  OD1 ASP A 451      16.777  -0.953  -3.318  1.00136.40           O  
ANISOU 3578  OD1 ASP A 451    17001  17575  17250   -115   -184    -63       O  
ATOM   3579  OD2 ASP A 451      16.657  -2.695  -4.663  1.00125.48           O1-
ANISOU 3579  OD2 ASP A 451    15638  16202  15836   -121   -190    -75       O1-
ATOM   3580  N   TYR A 452      15.934  -4.346   0.651  1.00 79.58           N  
ANISOU 3580  N   TYR A 452     9825  10345  10068   -102   -195    -99       N  
ATOM   3581  CA  TYR A 452      15.310  -4.703   1.904  1.00 77.36           C  
ANISOU 3581  CA  TYR A 452     9542  10054   9795    -98   -198   -101       C  
ATOM   3582  C   TYR A 452      16.008  -3.960   3.046  1.00 78.54           C  
ANISOU 3582  C   TYR A 452     9685  10200   9955    -91   -193   -103       C  
ATOM   3583  O   TYR A 452      15.378  -3.584   4.024  1.00 99.00           O  
ANISOU 3583  O   TYR A 452    12274  12786  12557    -89   -194    -99       O  
ATOM   3584  CB  TYR A 452      15.408  -6.196   2.120  1.00 85.64           C  
ANISOU 3584  CB  TYR A 452    10602  11099  10838    -95   -198   -111       C  
ATOM   3585  CG  TYR A 452      14.759  -6.668   3.408  1.00107.30           C  
ANISOU 3585  CG  TYR A 452    13345  13834  13591    -91   -200   -112       C  
ATOM   3586  CD1 TYR A 452      13.363  -6.735   3.532  1.00107.88           C  
ANISOU 3586  CD1 TYR A 452    13418  13904  13668    -96   -207   -103       C  
ATOM   3587  CD2 TYR A 452      15.539  -7.059   4.508  1.00113.45           C  
ANISOU 3587  CD2 TYR A 452    14124  14610  14374    -80   -196   -118       C  
ATOM   3588  CE1 TYR A 452      12.757  -7.178   4.703  1.00101.80           C  
ANISOU 3588  CE1 TYR A 452    12648  13125  12907    -91   -208   -102       C  
ATOM   3589  CE2 TYR A 452      14.948  -7.504   5.688  1.00123.23           C  
ANISOU 3589  CE2 TYR A 452    15361  15840  15619    -75   -197   -118       C  
ATOM   3590  CZ  TYR A 452      13.552  -7.559   5.789  1.00120.95           C  
ANISOU 3590  CZ  TYR A 452    15074  15547  15335    -80   -202   -110       C  
ATOM   3591  OH  TYR A 452      12.965  -8.011   6.969  1.00112.89           O  
ANISOU 3591  OH  TYR A 452    14053  14519  14322    -74   -202   -108       O  
ATOM   3592  N   LEU A 453      17.307  -3.742   2.923  1.00 69.21           N  
ANISOU 3592  N   LEU A 453     8501   9024   8773    -87   -188   -108       N  
ATOM   3593  CA  LEU A 453      18.061  -3.078   3.965  1.00 64.84           C  
ANISOU 3593  CA  LEU A 453     7940   8468   8227    -83   -184   -111       C  
ATOM   3594  C   LEU A 453      17.727  -1.643   4.082  1.00 70.11           C  
ANISOU 3594  C   LEU A 453     8601   9133   8906    -87   -183   -104       C  
ATOM   3595  O   LEU A 453      17.642  -1.140   5.176  1.00 71.81           O  
ANISOU 3595  O   LEU A 453     8814   9343   9129    -86   -182   -106       O  
ATOM   3596  CB  LEU A 453      19.539  -3.183   3.693  1.00 69.40           C  
ANISOU 3596  CB  LEU A 453     8515   9052   8802    -79   -179   -117       C  
ATOM   3597  CG  LEU A 453      20.021  -4.550   4.145  1.00 77.81           C  
ANISOU 3597  CG  LEU A 453     9585  10117   9863    -71   -179   -124       C  
ATOM   3598  CD1 LEU A 453      21.244  -5.010   3.360  1.00 86.41           C  
ANISOU 3598  CD1 LEU A 453    10674  11212  10945    -67   -172   -127       C  
ATOM   3599  CD2 LEU A 453      20.302  -4.529   5.642  1.00 73.43           C  
ANISOU 3599  CD2 LEU A 453     9026   9561   9314    -66   -180   -128       C  
ATOM   3600  N   SER A 454      17.571  -0.973   2.944  1.00 85.33           N  
ANISOU 3600  N   SER A 454    10526  11065  10832    -93   -181    -95       N  
ATOM   3601  CA  SER A 454      17.159   0.442   2.905  1.00 90.69           C  
ANISOU 3601  CA  SER A 454    11197  11740  11522    -97   -177    -85       C  
ATOM   3602  C   SER A 454      15.925   0.628   3.747  1.00 87.30           C  
ANISOU 3602  C   SER A 454    10769  11302  11101    -96   -178    -80       C  
ATOM   3603  O   SER A 454      15.783   1.618   4.472  1.00 88.16           O  
ANISOU 3603  O   SER A 454    10874  11401  11220    -96   -173    -78       O  
ATOM   3604  CB  SER A 454      16.813   0.874   1.468  1.00 94.18           C  
ANISOU 3604  CB  SER A 454    11637  12189  11960   -101   -176    -72       C  
ATOM   3605  OG  SER A 454      17.803   1.694   0.893  1.00 99.17           O  
ANISOU 3605  OG  SER A 454    12262  12824  12594   -102   -169    -70       O  
ATOM   3606  N   VAL A 455      15.026  -0.339   3.604  1.00 81.46           N  
ANISOU 3606  N   VAL A 455    10034  10562  10354    -96   -185    -77       N  
ATOM   3607  CA  VAL A 455      13.759  -0.339   4.292  1.00 86.69           C  
ANISOU 3607  CA  VAL A 455    10697  11218  11025    -96   -186    -70       C  
ATOM   3608  C   VAL A 455      14.000  -0.386   5.793  1.00 80.09           C  
ANISOU 3608  C   VAL A 455     9863  10373  10194    -90   -183    -80       C  
ATOM   3609  O   VAL A 455      13.444   0.437   6.548  1.00 74.96           O  
ANISOU 3609  O   VAL A 455     9212   9715   9555    -88   -178    -75       O  
ATOM   3610  CB  VAL A 455      12.905  -1.540   3.816  1.00 90.78           C  
ANISOU 3610  CB  VAL A 455    11220  11739  11534    -98   -195    -67       C  
ATOM   3611  CG1 VAL A 455      11.697  -1.763   4.718  1.00 96.18           C  
ANISOU 3611  CG1 VAL A 455    11904  12415  12227    -96   -196    -61       C  
ATOM   3612  CG2 VAL A 455      12.471  -1.330   2.370  1.00 90.00           C  
ANISOU 3612  CG2 VAL A 455    11117  11649  11428   -106   -199    -56       C  
ATOM   3613  N   VAL A 456      14.867  -1.319   6.199  1.00 76.46           N  
ANISOU 3613  N   VAL A 456     9408   9917   9726    -86   -186    -92       N  
ATOM   3614  CA  VAL A 456      15.104  -1.605   7.611  1.00 71.36           C  
ANISOU 3614  CA  VAL A 456     8765   9268   9083    -80   -185   -101       C  
ATOM   3615  C   VAL A 456      15.894  -0.531   8.330  1.00 64.61           C  
ANISOU 3615  C   VAL A 456     7906   8410   8232    -81   -180   -107       C  
ATOM   3616  O   VAL A 456      15.573  -0.168   9.457  1.00 69.55           O  
ANISOU 3616  O   VAL A 456     8533   9030   8862    -79   -177   -110       O  
ATOM   3617  CB  VAL A 456      15.794  -2.956   7.823  1.00 69.90           C  
ANISOU 3617  CB  VAL A 456     8583   9087   8888    -74   -189   -110       C  
ATOM   3618  CG1 VAL A 456      15.959  -3.216   9.299  1.00 74.00           C  
ANISOU 3618  CG1 VAL A 456     9104   9604   9408    -68   -188   -116       C  
ATOM   3619  CG2 VAL A 456      14.954  -4.079   7.236  1.00 74.04           C  
ANISOU 3619  CG2 VAL A 456     9113   9610   9408    -75   -193   -106       C  
ATOM   3620  N   LEU A 457      16.910   0.007   7.692  1.00 60.31           N  
ANISOU 3620  N   LEU A 457     7356   7871   7687    -84   -178   -110       N  
ATOM   3621  CA  LEU A 457      17.619   1.095   8.310  1.00 59.03           C  
ANISOU 3621  CA  LEU A 457     7191   7707   7531    -88   -174   -115       C  
ATOM   3622  C   LEU A 457      16.746   2.317   8.434  1.00 53.47           C  
ANISOU 3622  C   LEU A 457     6487   6991   6838    -92   -166   -108       C  
ATOM   3623  O   LEU A 457      16.841   3.041   9.412  1.00 62.54           O  
ANISOU 3623  O   LEU A 457     7637   8133   7992    -94   -162   -115       O  
ATOM   3624  CB  LEU A 457      18.933   1.359   7.592  1.00 60.88           C  
ANISOU 3624  CB  LEU A 457     7418   7949   7764    -91   -173   -118       C  
ATOM   3625  CG  LEU A 457      19.941   0.298   8.076  1.00 63.95           C  
ANISOU 3625  CG  LEU A 457     7807   8348   8144    -86   -179   -127       C  
ATOM   3626  CD1 LEU A 457      21.086   0.016   7.101  1.00 71.69           C  
ANISOU 3626  CD1 LEU A 457     8782   9338   9121    -86   -178   -127       C  
ATOM   3627  CD2 LEU A 457      20.493   0.721   9.427  1.00 65.78           C  
ANISOU 3627  CD2 LEU A 457     8038   8580   8377    -88   -180   -136       C  
ATOM   3628  N   ASN A 458      15.873   2.540   7.475  1.00 54.74           N  
ANISOU 3628  N   ASN A 458     6646   7150   7003    -93   -164    -94       N  
ATOM   3629  CA  ASN A 458      14.898   3.605   7.622  1.00 61.98           C  
ANISOU 3629  CA  ASN A 458     7562   8056   7933    -94   -156    -84       C  
ATOM   3630  C   ASN A 458      13.990   3.338   8.831  1.00 60.31           C  
ANISOU 3630  C   ASN A 458     7356   7835   7723    -89   -154    -85       C  
ATOM   3631  O   ASN A 458      13.563   4.281   9.514  1.00 61.93           O  
ANISOU 3631  O   ASN A 458     7564   8029   7938    -88   -144    -84       O  
ATOM   3632  CB  ASN A 458      14.090   3.813   6.337  1.00 62.83           C  
ANISOU 3632  CB  ASN A 458     7663   8165   8042    -95   -155    -66       C  
ATOM   3633  CG  ASN A 458      12.898   4.754   6.531  1.00 65.49           C  
ANISOU 3633  CG  ASN A 458     7998   8490   8394    -94   -145    -50       C  
ATOM   3634  ND2 ASN A 458      11.711   4.164   6.581  1.00 80.76           N  
ANISOU 3634  ND2 ASN A 458     9932  10424  10327    -91   -149    -40       N  
ATOM   3635  OD1 ASN A 458      13.028   5.988   6.610  1.00 58.26           O  
ANISOU 3635  OD1 ASN A 458     7080   7565   7490    -96   -133    -47       O  
ATOM   3636  N   GLN A 459      13.713   2.073   9.131  1.00 60.38           N  
ANISOU 3636  N   GLN A 459     7368   7849   7723    -84   -162    -87       N  
ATOM   3637  CA  GLN A 459      12.925   1.819  10.325  1.00 68.48           C  
ANISOU 3637  CA  GLN A 459     8401   8868   8751    -78   -160    -88       C  
ATOM   3638  C   GLN A 459      13.620   2.408  11.538  1.00 72.35           C  
ANISOU 3638  C   GLN A 459     8896   9354   9241    -79   -154   -102       C  
ATOM   3639  O   GLN A 459      13.011   3.162  12.282  1.00 74.62           O  
ANISOU 3639  O   GLN A 459     9187   9630   9536    -77   -145   -101       O  
ATOM   3640  CB  GLN A 459      12.569   0.341  10.560  1.00 72.54           C  
ANISOU 3640  CB  GLN A 459     8918   9387   9258    -73   -168    -89       C  
ATOM   3641  CG  GLN A 459      11.062   0.084  10.456  1.00 82.76           C  
ANISOU 3641  CG  GLN A 459    10211  10675  10558    -70   -167    -73       C  
ATOM   3642  CD  GLN A 459      10.496  -0.779  11.578  1.00 85.39           C  
ANISOU 3642  CD  GLN A 459    10550  11005  10891    -63   -168    -74       C  
ATOM   3643  NE2 GLN A 459       9.452  -0.280  12.259  1.00 86.54           N  
ANISOU 3643  NE2 GLN A 459    10695  11140  11045    -59   -159    -64       N  
ATOM   3644  OE1 GLN A 459      10.978  -1.886  11.821  1.00 88.98           O  
ANISOU 3644  OE1 GLN A 459    11007  11465  11336    -60   -174    -82       O  
ATOM   3645  N   LEU A 460      14.904   2.102  11.718  1.00 77.50           N  
ANISOU 3645  N   LEU A 460     9547  10016   9885    -81   -160   -115       N  
ATOM   3646  CA  LEU A 460      15.656   2.608  12.871  1.00 69.67           C  
ANISOU 3646  CA  LEU A 460     8559   9023   8889    -84   -158   -129       C  
ATOM   3647  C   LEU A 460      15.657   4.106  12.818  1.00 68.50           C  
ANISOU 3647  C   LEU A 460     8411   8863   8752    -91   -148   -130       C  
ATOM   3648  O   LEU A 460      15.491   4.754  13.828  1.00 75.08           O  
ANISOU 3648  O   LEU A 460     9252   9688   9587    -93   -140   -138       O  
ATOM   3649  CB  LEU A 460      17.090   2.054  12.878  1.00 76.97           C  
ANISOU 3649  CB  LEU A 460     9479   9963   9805    -86   -168   -140       C  
ATOM   3650  CG  LEU A 460      18.234   2.480  13.844  1.00 74.35           C  
ANISOU 3650  CG  LEU A 460     9146   9636   9466    -92   -170   -154       C  
ATOM   3651  CD1 LEU A 460      17.862   2.545  15.317  1.00 74.95           C  
ANISOU 3651  CD1 LEU A 460     9231   9709   9536    -90   -169   -162       C  
ATOM   3652  CD2 LEU A 460      19.378   1.490  13.670  1.00 67.97           C  
ANISOU 3652  CD2 LEU A 460     8332   8845   8650    -89   -180   -157       C  
ATOM   3653  N   CYS A 461      15.795   4.660  11.627  1.00 74.14           N  
ANISOU 3653  N   CYS A 461     9119   9578   9475    -95   -145   -122       N  
ATOM   3654  CA  CYS A 461      15.760   6.101  11.479  1.00 79.25           C  
ANISOU 3654  CA  CYS A 461     9765  10212  10134   -102   -133   -121       C  
ATOM   3655  C   CYS A 461      14.504   6.739  12.056  1.00 74.94           C  
ANISOU 3655  C   CYS A 461     9225   9649   9598    -98   -119   -113       C  
ATOM   3656  O   CYS A 461      14.594   7.638  12.900  1.00 78.24           O  
ANISOU 3656  O   CYS A 461     9651  10055  10021   -102   -109   -123       O  
ATOM   3657  CB  CYS A 461      15.963   6.501  10.015  1.00 81.68           C  
ANISOU 3657  CB  CYS A 461    10064  10523  10449   -105   -131   -109       C  
ATOM   3658  SG  CYS A 461      17.711   6.427   9.623  1.00 91.20           S  
ANISOU 3658  SG  CYS A 461    11262  11741  11648   -112   -139   -120       S  
ATOM   3659  N   VAL A 462      13.341   6.272  11.638  1.00 69.12           N  
ANISOU 3659  N   VAL A 462     8487   8911   8864    -90   -119    -97       N  
ATOM   3660  CA  VAL A 462      12.144   6.936  12.080  1.00 68.22           C  
ANISOU 3660  CA  VAL A 462     8377   8781   8762    -86   -105    -86       C  
ATOM   3661  C   VAL A 462      11.713   6.536  13.496  1.00 73.18           C  
ANISOU 3661  C   VAL A 462     9015   9404   9384    -80   -102    -95       C  
ATOM   3662  O   VAL A 462      11.264   7.400  14.239  1.00 77.77           O  
ANISOU 3662  O   VAL A 462     9604   9970   9973    -79    -87    -97       O  
ATOM   3663  CB  VAL A 462      11.014   6.814  11.060  1.00 70.06           C  
ANISOU 3663  CB  VAL A 462     8601   9015   9003    -81   -104    -62       C  
ATOM   3664  CG1 VAL A 462      11.423   7.528   9.781  1.00 71.41           C  
ANISOU 3664  CG1 VAL A 462     8762   9188   9180    -87   -102    -52       C  
ATOM   3665  CG2 VAL A 462      10.624   5.366  10.799  1.00 69.24           C  
ANISOU 3665  CG2 VAL A 462     8495   8924   8889    -77   -119    -57       C  
ATOM   3666  N   LEU A 463      11.877   5.258  13.870  1.00 78.61           N  
ANISOU 3666  N   LEU A 463     9704  10104  10058    -76   -115   -100       N  
ATOM   3667  CA  LEU A 463      11.762   4.798  15.284  1.00 76.49           C  
ANISOU 3667  CA  LEU A 463     9447   9836   9781    -71   -115   -111       C  
ATOM   3668  C   LEU A 463      12.569   5.650  16.256  1.00 79.39           C  
ANISOU 3668  C   LEU A 463     9822  10198  10144    -78   -109   -130       C  
ATOM   3669  O   LEU A 463      12.263   5.720  17.451  1.00 81.56           O  
ANISOU 3669  O   LEU A 463    10108  10468  10414    -74   -102   -138       O  
ATOM   3670  CB  LEU A 463      12.255   3.350  15.471  1.00 79.12           C  
ANISOU 3670  CB  LEU A 463     9778  10185  10100    -67   -131   -116       C  
ATOM   3671  CG  LEU A 463      11.302   2.130  15.409  1.00 88.09           C  
ANISOU 3671  CG  LEU A 463    10912  11323  11235    -58   -136   -104       C  
ATOM   3672  CD1 LEU A 463      11.850   0.996  16.284  1.00 87.29           C  
ANISOU 3672  CD1 LEU A 463    10814  11232  11119    -53   -145   -114       C  
ATOM   3673  CD2 LEU A 463       9.849   2.427  15.800  1.00 87.21           C  
ANISOU 3673  CD2 LEU A 463    10804  11199  11135    -51   -124    -89       C  
ATOM   3674  N   HIS A 464      13.619   6.267  15.738  1.00 78.80           N  
ANISOU 3674  N   HIS A 464     9743  10126  10070    -88   -111   -139       N  
ATOM   3675  CA  HIS A 464      14.572   6.963  16.548  1.00 78.07           C  
ANISOU 3675  CA  HIS A 464     9657  10032   9972    -98   -110   -158       C  
ATOM   3676  C   HIS A 464      14.252   8.432  16.570  1.00 79.28           C  
ANISOU 3676  C   HIS A 464     9817  10166  10140   -104    -91   -159       C  
ATOM   3677  O   HIS A 464      14.265   9.055  17.629  1.00 82.50           O  
ANISOU 3677  O   HIS A 464    10238  10564  10545   -108    -81   -173       O  
ATOM   3678  CB  HIS A 464      15.945   6.729  15.968  1.00 69.82           C  
ANISOU 3678  CB  HIS A 464     8603   9003   8921   -106   -123   -166       C  
ATOM   3679  CG  HIS A 464      16.959   7.705  16.421  1.00 75.34           C  
ANISOU 3679  CG  HIS A 464     9305   9701   9621   -121   -121   -183       C  
ATOM   3680  CD2 HIS A 464      17.344   8.894  15.899  1.00 82.88           C  
ANISOU 3680  CD2 HIS A 464    10258  10644  10588   -131   -112   -185       C  
ATOM   3681  ND1 HIS A 464      17.744   7.486  17.527  1.00 76.38           N  
ANISOU 3681  ND1 HIS A 464     9442   9843   9737   -126   -130   -200       N  
ATOM   3682  CE1 HIS A 464      18.571   8.504  17.672  1.00 87.75           C  
ANISOU 3682  CE1 HIS A 464    10882  11279  11180   -142   -127   -213       C  
ATOM   3683  NE2 HIS A 464      18.348   9.373  16.702  1.00 93.92           N  
ANISOU 3683  NE2 HIS A 464    11660  12046  11979   -144   -116   -205       N  
ATOM   3684  N   GLU A 465      13.954   8.988  15.403  1.00 81.22           N  
ANISOU 3684  N   GLU A 465    10055  10405  10402   -104    -84   -145       N  
ATOM   3685  CA  GLU A 465      13.776  10.421  15.303  1.00 82.76           C  
ANISOU 3685  CA  GLU A 465    10252  10579  10613   -110    -65   -144       C  
ATOM   3686  C   GLU A 465      12.717  10.863  16.281  1.00 75.24           C  
ANISOU 3686  C   GLU A 465     9314   9609   9665   -103    -47   -143       C  
ATOM   3687  O   GLU A 465      12.608  12.049  16.560  1.00 74.93           O  
ANISOU 3687  O   GLU A 465     9282   9550   9637   -108    -28   -148       O  
ATOM   3688  CB  GLU A 465      13.396  10.863  13.892  1.00 89.31           C  
ANISOU 3688  CB  GLU A 465    11070  11405  11459   -107    -59   -122       C  
ATOM   3689  CG  GLU A 465      13.757  12.323  13.629  1.00102.93           C  
ANISOU 3689  CG  GLU A 465    12795  13113  13200   -116    -42   -124       C  
ATOM   3690  CD  GLU A 465      12.788  13.045  12.692  1.00119.93           C  
ANISOU 3690  CD  GLU A 465    14940  15253  15373   -109    -26    -98       C  
ATOM   3691  OE1 GLU A 465      11.692  12.489  12.409  1.00133.42           O  
ANISOU 3691  OE1 GLU A 465    16645  16965  17083    -98    -27    -79       O  
ATOM   3692  OE2 GLU A 465      13.115  14.180  12.236  1.00111.73           O1-
ANISOU 3692  OE2 GLU A 465    13900  14202  14350   -116    -12    -96       O1-
ATOM   3693  N   LYS A 466      11.951   9.905  16.810  1.00 71.66           N  
ANISOU 3693  N   LYS A 466     8863   9161   9203    -92    -51   -137       N  
ATOM   3694  CA  LYS A 466      10.969  10.181  17.849  1.00 76.31           C  
ANISOU 3694  CA  LYS A 466     9466   9735   9795    -84    -34   -137       C  
ATOM   3695  C   LYS A 466      11.635  10.774  19.056  1.00 77.10           C  
ANISOU 3695  C   LYS A 466     9582   9828   9884    -94    -28   -163       C  
ATOM   3696  O   LYS A 466      11.448  11.945  19.326  1.00 87.48           O  
ANISOU 3696  O   LYS A 466    10907  11123  11210    -98     -8   -168       O  
ATOM   3697  CB  LYS A 466      10.198   8.934  18.251  1.00 76.50           C  
ANISOU 3697  CB  LYS A 466     9489   9768   9810    -72    -42   -127       C  
ATOM   3698  CG  LYS A 466       9.093   9.216  19.251  1.00 72.25           C  
ANISOU 3698  CG  LYS A 466     8963   9214   9275    -61    -23   -123       C  
ATOM   3699  CD  LYS A 466       8.004   8.162  19.172  1.00 75.23           C  
ANISOU 3699  CD  LYS A 466     9333   9597   9654    -48    -27   -102       C  
ATOM   3700  CE  LYS A 466       6.947   8.371  20.251  1.00 70.72           C  
ANISOU 3700  CE  LYS A 466     8774   9010   9086    -36     -7    -97       C  
ATOM   3701  NZ  LYS A 466       6.117   7.156  20.478  1.00 65.19           N1+
ANISOU 3701  NZ  LYS A 466     8069   8319   8383    -24    -14    -82       N1+
ATOM   3702  N   THR A 467      12.432  10.005  19.782  1.00 80.03           N  
ANISOU 3702  N   THR A 467     9956  10216  10234    -98    -45   -180       N  
ATOM   3703  CA  THR A 467      13.180  10.615  20.882  1.00 86.70           C  
ANISOU 3703  CA  THR A 467    10816  11059  11066   -110    -42   -206       C  
ATOM   3704  C   THR A 467      14.681  10.379  20.793  1.00 81.46           C  
ANISOU 3704  C   THR A 467    10145  10415  10390   -125    -63   -222       C  
ATOM   3705  O   THR A 467      15.200   9.456  21.398  1.00 78.04           O  
ANISOU 3705  O   THR A 467     9711  10002   9938   -124    -80   -229       O  
ATOM   3706  CB  THR A 467      12.588  10.239  22.253  1.00100.64           C  
ANISOU 3706  CB  THR A 467    12597  12823  12817   -102    -36   -213       C  
ATOM   3707  CG2 THR A 467      11.572  11.306  22.685  1.00108.42           C  
ANISOU 3707  CG2 THR A 467    13598  13780  13815    -98     -6   -211       C  
ATOM   3708  OG1 THR A 467      11.924   8.968  22.177  1.00100.08           O  
ANISOU 3708  OG1 THR A 467    12518  12764  12742    -87    -45   -196       O  
ATOM   3709  N   PRO A 468      15.381  11.250  20.044  1.00 84.06           N  
ANISOU 3709  N   PRO A 468    10469  10739  10732   -137    -61   -225       N  
ATOM   3710  CA  PRO A 468      16.775  11.039  19.662  1.00 83.28           C  
ANISOU 3710  CA  PRO A 468    10358  10659  10627   -150    -80   -234       C  
ATOM   3711  C   PRO A 468      17.693  10.904  20.868  1.00 82.34           C  
ANISOU 3711  C   PRO A 468    10247  10553  10486   -162    -92   -257       C  
ATOM   3712  O   PRO A 468      17.507  11.585  21.873  1.00 81.01           O  
ANISOU 3712  O   PRO A 468    10096  10373  10312   -169    -81   -273       O  
ATOM   3713  CB  PRO A 468      17.117  12.286  18.839  1.00 84.59           C  
ANISOU 3713  CB  PRO A 468    10520  10808  10812   -161    -68   -234       C  
ATOM   3714  CG  PRO A 468      16.130  13.312  19.259  1.00 84.42           C  
ANISOU 3714  CG  PRO A 468    10515  10759  10804   -159    -42   -235       C  
ATOM   3715  CD  PRO A 468      14.885  12.569  19.617  1.00 83.19           C  
ANISOU 3715  CD  PRO A 468    10363  10602  10643   -140    -37   -221       C  
ATOM   3716  N   VAL A 469      18.641   9.983  20.760  1.00 87.24           N  
ANISOU 3716  N   VAL A 469    10855  11199  11094   -163   -114   -257       N  
ATOM   3717  CA  VAL A 469      19.626   9.718  21.803  1.00 97.85           C  
ANISOU 3717  CA  VAL A 469    12201  12562  12417   -174   -129   -275       C  
ATOM   3718  C   VAL A 469      21.050   9.686  21.242  1.00 97.24           C  
ANISOU 3718  C   VAL A 469    12106  12501  12339   -187   -145   -278       C  
ATOM   3719  O   VAL A 469      22.002  10.072  21.931  1.00115.89           O  
ANISOU 3719  O   VAL A 469    14469  14872  14690   -204   -154   -295       O  
ATOM   3720  CB  VAL A 469      19.356   8.386  22.550  1.00104.46           C  
ANISOU 3720  CB  VAL A 469    13038  13417  13234   -160   -140   -270       C  
ATOM   3721  CG1 VAL A 469      20.105   8.384  23.881  1.00111.58           C  
ANISOU 3721  CG1 VAL A 469    13948  14335  14113   -172   -151   -289       C  
ATOM   3722  CG2 VAL A 469      17.871   8.178  22.802  1.00101.32           C  
ANISOU 3722  CG2 VAL A 469    12652  13004  12841   -143   -124   -260       C  
ATOM   3723  N   SER A 470      21.199   9.223  20.006  1.00 87.04           N  
ANISOU 3723  N   SER A 470    10799  11214  11059   -179   -149   -261       N  
ATOM   3724  CA  SER A 470      22.496   9.190  19.363  1.00 86.89           C  
ANISOU 3724  CA  SER A 470    10763  11210  11042   -189   -162   -261       C  
ATOM   3725  C   SER A 470      22.549  10.085  18.125  1.00 89.70           C  
ANISOU 3725  C   SER A 470    11112  11550  11420   -193   -151   -253       C  
ATOM   3726  O   SER A 470      21.751   9.994  17.207  1.00 85.32           O  
ANISOU 3726  O   SER A 470    10555  10985  10877   -181   -141   -238       O  
ATOM   3727  CB  SER A 470      22.903   7.755  19.049  1.00 86.14           C  
ANISOU 3727  CB  SER A 470    10655  11138  10938   -176   -177   -248       C  
ATOM   3728  OG  SER A 470      23.425   7.636  17.745  1.00 82.17           O  
ANISOU 3728  OG  SER A 470    10136  10637  10446   -174   -179   -236       O  
ATOM   3729  N   ASP A 471      23.556  10.941  18.142  1.00 99.39           N  
ANISOU 3729  N   ASP A 471    12335  12777  12652   -212   -153   -265       N  
ATOM   3730  CA  ASP A 471      23.852  11.923  17.118  1.00 99.22           C  
ANISOU 3730  CA  ASP A 471    12305  12741  12651   -220   -142   -260       C  
ATOM   3731  C   ASP A 471      24.282  11.228  15.828  1.00 97.73           C  
ANISOU 3731  C   ASP A 471    12099  12565  12468   -210   -149   -241       C  
ATOM   3732  O   ASP A 471      24.062  11.727  14.727  1.00100.18           O  
ANISOU 3732  O   ASP A 471    12404  12865  12796   -207   -138   -229       O  
ATOM   3733  CB  ASP A 471      25.019  12.779  17.629  1.00107.93           C  
ANISOU 3733  CB  ASP A 471    13406  13847  13755   -245   -148   -278       C  
ATOM   3734  CG  ASP A 471      25.322  12.535  19.129  1.00113.40           C  
ANISOU 3734  CG  ASP A 471    14110  14553  14426   -255   -160   -298       C  
ATOM   3735  OD1 ASP A 471      24.640  13.164  19.967  1.00136.48           O  
ANISOU 3735  OD1 ASP A 471    17052  17459  17345   -260   -148   -311       O  
ATOM   3736  OD2 ASP A 471      26.192  11.690  19.469  1.00 90.52           O1-
ANISOU 3736  OD2 ASP A 471    11200  11681  11512   -256   -179   -297       O1-
ATOM   3737  N   ARG A 472      24.899  10.067  15.990  1.00 97.26           N  
ANISOU 3737  N   ARG A 472    12030  12530  12394   -204   -166   -239       N  
ATOM   3738  CA  ARG A 472      25.564   9.374  14.906  1.00101.68           C  
ANISOU 3738  CA  ARG A 472    12573  13103  12956   -197   -173   -224       C  
ATOM   3739  C   ARG A 472      24.515   8.711  14.033  1.00102.24           C  
ANISOU 3739  C   ARG A 472    12647  13170  13031   -178   -166   -208       C  
ATOM   3740  O   ARG A 472      24.646   8.657  12.805  1.00 97.23           O  
ANISOU 3740  O   ARG A 472    12003  12535  12404   -173   -163   -195       O  
ATOM   3741  CB  ARG A 472      26.488   8.306  15.467  1.00100.41           C  
ANISOU 3741  CB  ARG A 472    12403  12968  12780   -195   -190   -225       C  
ATOM   3742  CG  ARG A 472      27.287   8.754  16.670  1.00103.94           C  
ANISOU 3742  CG  ARG A 472    12851  13425  13218   -213   -200   -242       C  
ATOM   3743  CD  ARG A 472      28.094   7.586  17.183  1.00108.50           C  
ANISOU 3743  CD  ARG A 472    13417  14029  13779   -208   -217   -239       C  
ATOM   3744  NE  ARG A 472      29.265   7.390  16.334  1.00104.17           N  
ANISOU 3744  NE  ARG A 472    12848  13493  13238   -209   -222   -228       N  
ATOM   3745  CZ  ARG A 472      29.867   6.228  16.114  1.00 95.89           C  
ANISOU 3745  CZ  ARG A 472    11787  12464  12184   -197   -231   -216       C  
ATOM   3746  NH1 ARG A 472      29.413   5.105  16.667  1.00 93.24           N1+
ANISOU 3746  NH1 ARG A 472    11456  12137  11834   -182   -235   -212       N1+
ATOM   3747  NH2 ARG A 472      30.926   6.196  15.316  1.00 91.14           N  
ANISOU 3747  NH2 ARG A 472    11167  11872  11590   -199   -232   -206       N  
ATOM   3748  N   VAL A 473      23.481   8.196  14.694  1.00 96.51           N  
ANISOU 3748  N   VAL A 473    11933  12440  12296   -168   -165   -209       N  
ATOM   3749  CA  VAL A 473      22.256   7.754  14.043  1.00 86.58           C  
ANISOU 3749  CA  VAL A 473    10680  11174  11042   -154   -158   -195       C  
ATOM   3750  C   VAL A 473      21.628   8.956  13.374  1.00 86.46           C  
ANISOU 3750  C   VAL A 473    10667  11138  11045   -157   -142   -189       C  
ATOM   3751  O   VAL A 473      21.435   8.982  12.155  1.00 83.85           O  
ANISOU 3751  O   VAL A 473    10330  10807  10723   -152   -138   -174       O  
ATOM   3752  CB  VAL A 473      21.248   7.244  15.073  1.00 83.31           C  
ANISOU 3752  CB  VAL A 473    10279  10756  10619   -145   -157   -198       C  
ATOM   3753  CG1 VAL A 473      19.930   6.950  14.394  1.00 85.46           C  
ANISOU 3753  CG1 VAL A 473    10554  11018  10897   -133   -149   -182       C  
ATOM   3754  CG2 VAL A 473      21.780   6.017  15.797  1.00 86.55           C  
ANISOU 3754  CG2 VAL A 473    10687  11187  11012   -140   -172   -201       C  
ATOM   3755  N   THR A 474      21.342   9.964  14.197  1.00 89.77           N  
ANISOU 3755  N   THR A 474    11097  11542  11469   -166   -132   -200       N  
ATOM   3756  CA  THR A 474      20.733  11.194  13.725  1.00 96.21           C  
ANISOU 3756  CA  THR A 474    11916  12336  12303   -169   -114   -194       C  
ATOM   3757  C   THR A 474      21.457  11.716  12.450  1.00103.13           C  
ANISOU 3757  C   THR A 474    12779  13214  13193   -174   -111   -185       C  
ATOM   3758  O   THR A 474      20.806  12.082  11.474  1.00111.67           O  
ANISOU 3758  O   THR A 474    13857  14286  14287   -168   -101   -168       O  
ATOM   3759  CB  THR A 474      20.665  12.289  14.834  1.00 89.45           C  
ANISOU 3759  CB  THR A 474    11074  11463  11451   -182   -102   -212       C  
ATOM   3760  CG2 THR A 474      19.738  13.373  14.412  1.00 85.83           C  
ANISOU 3760  CG2 THR A 474    10621  10979  11012   -180    -80   -203       C  
ATOM   3761  OG1 THR A 474      20.171  11.752  16.072  1.00 81.12           O  
ANISOU 3761  OG1 THR A 474    10032  10410  10381   -178   -106   -222       O  
ATOM   3762  N   LYS A 475      22.786  11.726  12.439  1.00101.12           N  
ANISOU 3762  N   LYS A 475    12515  12971  12936   -185   -121   -193       N  
ATOM   3763  CA  LYS A 475      23.533  12.169  11.251  1.00 99.64           C  
ANISOU 3763  CA  LYS A 475    12314  12786  12761   -189   -118   -183       C  
ATOM   3764  C   LYS A 475      23.256  11.313  10.005  1.00 93.86           C  
ANISOU 3764  C   LYS A 475    11574  12064  12025   -174   -121   -164       C  
ATOM   3765  O   LYS A 475      23.056  11.865   8.912  1.00 91.88           O  
ANISOU 3765  O   LYS A 475    11317  11807  11786   -172   -112   -150       O  
ATOM   3766  CB  LYS A 475      25.054  12.202  11.538  1.00107.26           C  
ANISOU 3766  CB  LYS A 475    13269  13764  13722   -203   -130   -195       C  
ATOM   3767  CG  LYS A 475      25.986  12.221  10.297  1.00105.98           C  
ANISOU 3767  CG  LYS A 475    13089  13610  13567   -203   -131   -182       C  
ATOM   3768  CD  LYS A 475      27.479  12.139  10.667  1.00108.29           C  
ANISOU 3768  CD  LYS A 475    13370  13919  13857   -216   -143   -191       C  
ATOM   3769  CE  LYS A 475      28.281  11.067   9.902  1.00102.85           C  
ANISOU 3769  CE  LYS A 475    12666  13251  13160   -206   -153   -179       C  
ATOM   3770  NZ  LYS A 475      28.373  11.267   8.427  1.00101.96           N1+
ANISOU 3770  NZ  LYS A 475    12545  13136  13059   -199   -143   -162       N1+
ATOM   3771  N   CYS A 476      23.278   9.982  10.168  1.00 89.78           N  
ANISOU 3771  N   CYS A 476    11056  11564  11492   -165   -135   -164       N  
ATOM   3772  CA  CYS A 476      23.235   9.039   9.028  1.00 90.36           C  
ANISOU 3772  CA  CYS A 476    11124  11650  11560   -153   -139   -150       C  
ATOM   3773  C   CYS A 476      21.882   9.036   8.343  1.00100.99           C  
ANISOU 3773  C   CYS A 476    12475  12987  12909   -144   -131   -135       C  
ATOM   3774  O   CYS A 476      21.783   8.839   7.126  1.00109.95           O  
ANISOU 3774  O   CYS A 476    13603  14127  14044   -138   -130   -121       O  
ATOM   3775  CB  CYS A 476      23.557   7.607   9.462  1.00 94.40           C  
ANISOU 3775  CB  CYS A 476    11635  12178  12054   -145   -153   -154       C  
ATOM   3776  SG  CYS A 476      25.315   7.142   9.451  1.00102.55           S  
ANISOU 3776  SG  CYS A 476    12654  13229  13082   -150   -163   -158       S  
ATOM   3777  N   CYS A 477      20.836   9.246   9.137  1.00104.94           N  
ANISOU 3777  N   CYS A 477    12985  13475  13411   -142   -126   -137       N  
ATOM   3778  CA  CYS A 477      19.480   9.343   8.628  1.00 95.73           C  
ANISOU 3778  CA  CYS A 477    11822  12300  12250   -134   -119   -122       C  
ATOM   3779  C   CYS A 477      19.358  10.604   7.826  1.00 85.37           C  
ANISOU 3779  C   CYS A 477    10505  10977  10956   -138   -104   -110       C  
ATOM   3780  O   CYS A 477      18.650  10.656   6.820  1.00 93.61           O  
ANISOU 3780  O   CYS A 477    11544  12021  12003   -132   -100    -92       O  
ATOM   3781  CB  CYS A 477      18.486   9.373   9.789  1.00102.27           C  
ANISOU 3781  CB  CYS A 477    12662  13118  13079   -131   -115   -127       C  
ATOM   3782  SG  CYS A 477      18.532   7.891  10.826  1.00111.94           S  
ANISOU 3782  SG  CYS A 477    13894  14356  14284   -125   -130   -139       S  
ATOM   3783  N   THR A 478      20.089  11.616   8.261  1.00 75.62           N  
ANISOU 3783  N   THR A 478     9270   9732   9731   -149    -97   -121       N  
ATOM   3784  CA  THR A 478      19.910  12.949   7.735  1.00 77.63           C  
ANISOU 3784  CA  THR A 478     9521   9971  10005   -153    -80   -111       C  
ATOM   3785  C   THR A 478      20.506  13.186   6.353  1.00 83.50           C  
ANISOU 3785  C   THR A 478    10252  10722  10754   -153    -78    -97       C  
ATOM   3786  O   THR A 478      19.840  13.767   5.500  1.00 74.70           O  
ANISOU 3786  O   THR A 478     9132   9600   9650   -148    -67    -78       O  
ATOM   3787  CB  THR A 478      20.442  13.992   8.726  1.00 68.20           C  
ANISOU 3787  CB  THR A 478     8332   8759   8820   -166    -71   -129       C  
ATOM   3788  CG2 THR A 478      20.331  15.412   8.150  1.00 61.50           C  
ANISOU 3788  CG2 THR A 478     7480   7891   7995   -171    -51   -119       C  
ATOM   3789  OG1 THR A 478      19.664  13.905   9.919  1.00 74.14           O  
ANISOU 3789  OG1 THR A 478     9099   9502   9568   -165    -68   -139       O  
ATOM   3790  N   GLU A 479      21.740  12.740   6.133  1.00 99.61           N  
ANISOU 3790  N   GLU A 479    12284  12776  12787   -157    -89   -104       N  
ATOM   3791  CA  GLU A 479      22.562  13.294   5.038  1.00112.48           C  
ANISOU 3791  CA  GLU A 479    13902  14409  14426   -161    -83    -94       C  
ATOM   3792  C   GLU A 479      22.130  12.851   3.648  1.00118.77           C  
ANISOU 3792  C   GLU A 479    14693  15217  15217   -150    -83    -73       C  
ATOM   3793  O   GLU A 479      21.848  13.688   2.786  1.00138.48           O  
ANISOU 3793  O   GLU A 479    17184  17708  17726   -149    -71    -56       O  
ATOM   3794  CB  GLU A 479      24.047  12.999   5.253  1.00116.41           C  
ANISOU 3794  CB  GLU A 479    14393  14919  14919   -169    -93   -107       C  
ATOM   3795  CG  GLU A 479      24.722  14.008   6.155  1.00122.15           C  
ANISOU 3795  CG  GLU A 479    15120  15633  15659   -184    -88   -122       C  
ATOM   3796  CD  GLU A 479      26.008  13.489   6.761  1.00132.27           C  
ANISOU 3796  CD  GLU A 479    16396  16929  16931   -193   -103   -137       C  
ATOM   3797  OE1 GLU A 479      26.420  14.057   7.792  1.00140.31           O  
ANISOU 3797  OE1 GLU A 479    17418  17940  17954   -207   -104   -153       O  
ATOM   3798  OE2 GLU A 479      26.598  12.523   6.215  1.00133.46           O1-
ANISOU 3798  OE2 GLU A 479    16539  17099  17071   -185   -112   -131       O1-
ATOM   3799  N   SER A 480      22.088  11.544   3.433  1.00111.99           N  
ANISOU 3799  N   SER A 480    13837  14376  14340   -142    -97    -74       N  
ATOM   3800  CA  SER A 480      21.681  10.994   2.167  1.00104.75           C  
ANISOU 3800  CA  SER A 480    12917  13471  13414   -134    -99    -58       C  
ATOM   3801  C   SER A 480      20.716   9.867   2.431  1.00100.15           C  
ANISOU 3801  C   SER A 480    12343  12894  12816   -127   -109    -59       C  
ATOM   3802  O   SER A 480      20.734   9.256   3.506  1.00 97.96           O  
ANISOU 3802  O   SER A 480    12072  12615  12532   -127   -117    -74       O  
ATOM   3803  CB  SER A 480      22.905  10.464   1.429  1.00112.76           C  
ANISOU 3803  CB  SER A 480    13924  14500  14419   -133   -103    -58       C  
ATOM   3804  OG  SER A 480      22.527   9.670   0.316  1.00128.63           O  
ANISOU 3804  OG  SER A 480    15936  16524  16415   -126   -107    -47       O  
ATOM   3805  N   LEU A 481      19.883   9.589   1.439  1.00 96.98           N  
ANISOU 3805  N   LEU A 481    11941  12499  12408   -122   -110    -43       N  
ATOM   3806  CA  LEU A 481      18.990   8.449   1.509  1.00101.12           C  
ANISOU 3806  CA  LEU A 481    12473  13030  12918   -117   -120    -43       C  
ATOM   3807  C   LEU A 481      19.664   7.201   0.957  1.00 96.47           C  
ANISOU 3807  C   LEU A 481    11886  12458  12311   -114   -130    -49       C  
ATOM   3808  O   LEU A 481      19.735   6.165   1.618  1.00101.16           O  
ANISOU 3808  O   LEU A 481    12487  13055  12896   -112   -139    -62       O  
ATOM   3809  CB  LEU A 481      17.718   8.738   0.739  1.00105.34           C  
ANISOU 3809  CB  LEU A 481    13005  13565  13454   -114   -118    -22       C  
ATOM   3810  CG  LEU A 481      16.633   7.690   0.945  1.00109.34           C  
ANISOU 3810  CG  LEU A 481    13518  14076  13950   -111   -128    -21       C  
ATOM   3811  CD1 LEU A 481      16.616   7.124   2.352  1.00 98.38           C  
ANISOU 3811  CD1 LEU A 481    12138  12681  12561   -110   -133    -38       C  
ATOM   3812  CD2 LEU A 481      15.282   8.308   0.609  1.00114.99           C  
ANISOU 3812  CD2 LEU A 481    14229  14788  14675   -109   -123      1       C  
ATOM   3813  N   VAL A 482      20.150   7.329  -0.265  1.00 94.77           N  
ANISOU 3813  N   VAL A 482    11665  12251  12091   -113   -127    -40       N  
ATOM   3814  CA  VAL A 482      21.002   6.331  -0.922  1.00 98.63           C  
ANISOU 3814  CA  VAL A 482    12157  12754  12565   -111   -132    -45       C  
ATOM   3815  C   VAL A 482      22.133   5.805  -0.025  1.00 85.87           C  
ANISOU 3815  C   VAL A 482    10541  11138  10948   -110   -135    -63       C  
ATOM   3816  O   VAL A 482      22.352   4.609   0.087  1.00 76.01           O  
ANISOU 3816  O   VAL A 482     9298   9896   9687   -106   -142    -71       O  
ATOM   3817  CB  VAL A 482      21.675   6.931  -2.200  1.00108.80           C  
ANISOU 3817  CB  VAL A 482    13437  14049  13853   -111   -124    -33       C  
ATOM   3818  CG1 VAL A 482      21.790   5.884  -3.287  1.00103.44           C  
ANISOU 3818  CG1 VAL A 482    12764  13385  13153   -107   -128    -32       C  
ATOM   3819  CG2 VAL A 482      20.911   8.139  -2.752  1.00112.23           C  
ANISOU 3819  CG2 VAL A 482    13864  14479  14298   -112   -116    -14       C  
ATOM   3820  N   ASN A 483      22.833   6.712   0.631  1.00 84.63           N  
ANISOU 3820  N   ASN A 483    10376  10973  10805   -115   -130    -67       N  
ATOM   3821  CA  ASN A 483      24.058   6.369   1.326  1.00 95.39           C  
ANISOU 3821  CA  ASN A 483    11736  12339  12168   -116   -133    -80       C  
ATOM   3822  C   ASN A 483      23.890   6.036   2.801  1.00100.88           C  
ANISOU 3822  C   ASN A 483    12436  13030  12864   -118   -141    -94       C  
ATOM   3823  O   ASN A 483      24.861   6.099   3.560  1.00121.77           O  
ANISOU 3823  O   ASN A 483    15077  15678  15513   -121   -143   -103       O  
ATOM   3824  CB  ASN A 483      25.052   7.512   1.170  1.00103.47           C  
ANISOU 3824  CB  ASN A 483    12748  13360  13207   -123   -125    -77       C  
ATOM   3825  CG  ASN A 483      25.222   7.923  -0.271  1.00120.00           C  
ANISOU 3825  CG  ASN A 483    14835  15458  15300   -121   -117    -61       C  
ATOM   3826  ND2 ASN A 483      25.360   6.935  -1.166  1.00134.54           N  
ANISOU 3826  ND2 ASN A 483    16681  17312  17126   -113   -118    -58       N  
ATOM   3827  OD1 ASN A 483      25.208   9.111  -0.585  1.00119.60           O  
ANISOU 3827  OD1 ASN A 483    14778  15400  15264   -125   -107    -52       O  
ATOM   3828  N   ARG A 484      22.679   5.661   3.208  1.00 95.74           N  
ANISOU 3828  N   ARG A 484    11794  12374  12209   -115   -144    -94       N  
ATOM   3829  CA  ARG A 484      22.453   5.248   4.591  1.00 87.80           C  
ANISOU 3829  CA  ARG A 484    10794  11365  11201   -115   -150   -106       C  
ATOM   3830  C   ARG A 484      23.207   3.964   4.943  1.00 80.07           C  
ANISOU 3830  C   ARG A 484     9815  10397  10210   -109   -158   -114       C  
ATOM   3831  O   ARG A 484      23.995   3.925   5.903  1.00 74.23           O  
ANISOU 3831  O   ARG A 484     9073   9660   9471   -111   -162   -123       O  
ATOM   3832  CB  ARG A 484      20.968   5.102   4.870  1.00 84.09           C  
ANISOU 3832  CB  ARG A 484    10333  10887  10731   -112   -151   -102       C  
ATOM   3833  CG  ARG A 484      20.302   6.439   5.134  1.00 87.98           C  
ANISOU 3833  CG  ARG A 484    10825  11366  11238   -117   -142    -97       C  
ATOM   3834  CD  ARG A 484      18.853   6.217   5.492  1.00 97.38           C  
ANISOU 3834  CD  ARG A 484    12022  12549  12428   -113   -142    -91       C  
ATOM   3835  NE  ARG A 484      18.106   7.436   5.803  1.00 99.84           N  
ANISOU 3835  NE  ARG A 484    12334  12845  12755   -115   -131    -84       N  
ATOM   3836  CZ  ARG A 484      16.797   7.466   6.067  1.00101.12           C  
ANISOU 3836  CZ  ARG A 484    12500  12999  12920   -111   -128    -76       C  
ATOM   3837  NH1 ARG A 484      16.074   6.345   6.056  1.00110.18           N1+
ANISOU 3837  NH1 ARG A 484    13652  14154  14058   -106   -137    -73       N1+
ATOM   3838  NH2 ARG A 484      16.200   8.615   6.336  1.00 93.73           N  
ANISOU 3838  NH2 ARG A 484    11565  12049  12000   -112   -114    -69       N  
ATOM   3839  N   ARG A 485      23.005   2.928   4.148  1.00 72.28           N  
ANISOU 3839  N   ARG A 485     8834   9417   9213   -102   -160   -110       N  
ATOM   3840  CA  ARG A 485      23.707   1.687   4.408  1.00 81.42           C  
ANISOU 3840  CA  ARG A 485     9992  10583  10361    -95   -164   -116       C  
ATOM   3841  C   ARG A 485      25.245   1.901   4.524  1.00 87.64           C  
ANISOU 3841  C   ARG A 485    10768  11379  11153    -97   -163   -118       C  
ATOM   3842  O   ARG A 485      25.832   1.541   5.543  1.00 84.15           O  
ANISOU 3842  O   ARG A 485    10322  10941  10709    -96   -168   -125       O  
ATOM   3843  CB  ARG A 485      23.335   0.620   3.381  1.00 84.98           C  
ANISOU 3843  CB  ARG A 485    10450  11037  10800    -89   -163   -112       C  
ATOM   3844  CG  ARG A 485      23.662  -0.807   3.822  1.00 88.65           C  
ANISOU 3844  CG  ARG A 485    10919  11506  11256    -81   -166   -118       C  
ATOM   3845  CD  ARG A 485      24.002  -1.693   2.629  1.00 92.55           C  
ANISOU 3845  CD  ARG A 485    11419  12005  11741    -75   -161   -117       C  
ATOM   3846  NE  ARG A 485      24.699  -0.956   1.575  1.00 99.07           N  
ANISOU 3846  NE  ARG A 485    12238  12836  12568    -78   -154   -110       N  
ATOM   3847  CZ  ARG A 485      26.002  -0.687   1.556  1.00 98.62           C  
ANISOU 3847  CZ  ARG A 485    12171  12785  12516    -76   -150   -109       C  
ATOM   3848  NH1 ARG A 485      26.796  -1.104   2.535  1.00 94.12           N1+
ANISOU 3848  NH1 ARG A 485    11594  12217  11949    -72   -152   -113       N1+
ATOM   3849  NH2 ARG A 485      26.511   0.017   0.547  1.00100.45           N  
ANISOU 3849  NH2 ARG A 485    12397  13019  12749    -78   -142   -101       N  
ATOM   3850  N   PRO A 486      25.889   2.525   3.516  1.00 98.67           N  
ANISOU 3850  N   PRO A 486    12158  12779  12554    -99   -156   -111       N  
ATOM   3851  CA  PRO A 486      27.301   2.969   3.656  1.00103.90           C  
ANISOU 3851  CA  PRO A 486    12807  13447  13223   -103   -154   -111       C  
ATOM   3852  C   PRO A 486      27.642   3.673   4.986  1.00 96.68           C  
ANISOU 3852  C   PRO A 486    11887  12531  12317   -112   -160   -120       C  
ATOM   3853  O   PRO A 486      28.528   3.218   5.725  1.00 88.90           O  
ANISOU 3853  O   PRO A 486    10894  11554  11330   -112   -166   -124       O  
ATOM   3854  CB  PRO A 486      27.469   3.957   2.484  1.00104.24           C  
ANISOU 3854  CB  PRO A 486    12845  13488  13274   -106   -145   -101       C  
ATOM   3855  CG  PRO A 486      26.536   3.454   1.440  1.00104.85           C  
ANISOU 3855  CG  PRO A 486    12932  13565  13341   -100   -142    -95       C  
ATOM   3856  CD  PRO A 486      25.394   2.741   2.141  1.00104.45           C  
ANISOU 3856  CD  PRO A 486    12893  13510  13283    -98   -150   -101       C  
ATOM   3857  N   CYS A 487      26.927   4.769   5.253  1.00 88.06           N  
ANISOU 3857  N   CYS A 487    10798  11427  11234   -121   -158   -122       N  
ATOM   3858  CA  CYS A 487      27.066   5.581   6.459  1.00 88.20           C  
ANISOU 3858  CA  CYS A 487    10813  11439  11258   -132   -161   -132       C  
ATOM   3859  C   CYS A 487      27.017   4.766   7.741  1.00 87.25           C  
ANISOU 3859  C   CYS A 487    10699  11325  11129   -129   -171   -141       C  
ATOM   3860  O   CYS A 487      27.857   4.941   8.640  1.00 75.68           O  
ANISOU 3860  O   CYS A 487     9226   9866   9663   -137   -178   -149       O  
ATOM   3861  CB  CYS A 487      25.920   6.580   6.496  1.00 97.67           C  
ANISOU 3861  CB  CYS A 487    12021  12622  12466   -137   -155   -131       C  
ATOM   3862  SG  CYS A 487      26.110   7.881   7.730  1.00111.63           S  
ANISOU 3862  SG  CYS A 487    13790  14380  14246   -153   -153   -144       S  
ATOM   3863  N   PHE A 488      26.009   3.897   7.826  1.00 86.42           N  
ANISOU 3863  N   PHE A 488    10604  11217  11014   -119   -173   -140       N  
ATOM   3864  CA  PHE A 488      25.816   3.065   9.002  1.00 90.33           C  
ANISOU 3864  CA  PHE A 488    11105  11718  11501   -115   -181   -147       C  
ATOM   3865  C   PHE A 488      26.907   2.015   9.053  1.00 94.83           C  
ANISOU 3865  C   PHE A 488    11665  12302  12063   -108   -185   -145       C  
ATOM   3866  O   PHE A 488      27.431   1.746  10.126  1.00100.52           O  
ANISOU 3866  O   PHE A 488    12381  13031  12779   -109   -193   -150       O  
ATOM   3867  CB  PHE A 488      24.425   2.393   9.010  1.00 89.88           C  
ANISOU 3867  CB  PHE A 488    11060  11653  11438   -106   -180   -145       C  
ATOM   3868  CG  PHE A 488      23.333   3.263   9.566  1.00 92.46           C  
ANISOU 3868  CG  PHE A 488    11394  11965  11770   -112   -176   -148       C  
ATOM   3869  CD1 PHE A 488      23.242   3.493  10.926  1.00 97.24           C  
ANISOU 3869  CD1 PHE A 488    12004  12569  12373   -115   -180   -158       C  
ATOM   3870  CD2 PHE A 488      22.396   3.864   8.729  1.00106.25           C  
ANISOU 3870  CD2 PHE A 488    13145  13702  13524   -112   -169   -140       C  
ATOM   3871  CE1 PHE A 488      22.250   4.323  11.445  1.00 96.47           C  
ANISOU 3871  CE1 PHE A 488    11915  12457  12280   -119   -174   -161       C  
ATOM   3872  CE2 PHE A 488      21.394   4.689   9.237  1.00103.60           C  
ANISOU 3872  CE2 PHE A 488    12816  13352  13195   -115   -163   -140       C  
ATOM   3873  CZ  PHE A 488      21.323   4.917  10.597  1.00100.57           C  
ANISOU 3873  CZ  PHE A 488    12438  12965  12810   -119   -165   -151       C  
ATOM   3874  N   SER A 489      27.238   1.438   7.889  1.00 96.90           N  
ANISOU 3874  N   SER A 489    11925  12568  12325   -100   -180   -137       N  
ATOM   3875  CA  SER A 489      28.282   0.408   7.760  1.00 96.23           C  
ANISOU 3875  CA  SER A 489    11832  12496  12235    -91   -181   -133       C  
ATOM   3876  C   SER A 489      29.592   0.895   8.319  1.00 91.58           C  
ANISOU 3876  C   SER A 489    11227  11918  11651    -99   -185   -133       C  
ATOM   3877  O   SER A 489      30.393   0.110   8.825  1.00 85.33           O  
ANISOU 3877  O   SER A 489    10427  11139  10855    -93   -189   -130       O  
ATOM   3878  CB  SER A 489      28.511   0.045   6.291  1.00101.22           C  
ANISOU 3878  CB  SER A 489    12465  13128  12867    -85   -171   -125       C  
ATOM   3879  OG  SER A 489      27.338  -0.477   5.701  1.00105.58           O  
ANISOU 3879  OG  SER A 489    13031  13672  13413    -80   -169   -124       O  
ATOM   3880  N   ALA A 490      29.781   2.209   8.207  1.00 96.88           N  
ANISOU 3880  N   ALA A 490    11894  12585  12332   -112   -184   -135       N  
ATOM   3881  CA  ALA A 490      31.018   2.896   8.562  1.00 94.26           C  
ANISOU 3881  CA  ALA A 490    11545  12261  12006   -123   -188   -135       C  
ATOM   3882  C   ALA A 490      31.274   2.963  10.056  1.00 84.08           C  
ANISOU 3882  C   ALA A 490    10254  10981  10713   -131   -200   -144       C  
ATOM   3883  O   ALA A 490      32.414   2.872  10.480  1.00 87.99           O  
ANISOU 3883  O   ALA A 490    10733  11490  11208   -136   -207   -142       O  
ATOM   3884  CB  ALA A 490      31.011   4.311   7.979  1.00 95.18           C  
ANISOU 3884  CB  ALA A 490    11660  12368  12136   -136   -182   -136       C  
ATOM   3885  N   LEU A 491      30.229   3.127  10.850  1.00 77.03           N  
ANISOU 3885  N   LEU A 491     9374  10079   9814   -134   -203   -154       N  
ATOM   3886  CA  LEU A 491      30.410   3.391  12.271  1.00 82.93           C  
ANISOU 3886  CA  LEU A 491    10121  10833  10555   -144   -214   -165       C  
ATOM   3887  C   LEU A 491      31.221   2.316  12.951  1.00 91.38           C  
ANISOU 3887  C   LEU A 491    11181  11924  11616   -137   -223   -159       C  
ATOM   3888  O   LEU A 491      31.206   1.149  12.543  1.00 95.08           O  
ANISOU 3888  O   LEU A 491    11650  12397  12081   -120   -220   -150       O  
ATOM   3889  CB  LEU A 491      29.090   3.482  12.995  1.00 77.96           C  
ANISOU 3889  CB  LEU A 491     9510  10191   9920   -143   -213   -174       C  
ATOM   3890  CG  LEU A 491      28.061   4.426  12.401  1.00 82.14           C  
ANISOU 3890  CG  LEU A 491    10051  10700  10459   -147   -202   -176       C  
ATOM   3891  CD1 LEU A 491      26.749   3.982  13.013  1.00 85.28           C  
ANISOU 3891  CD1 LEU A 491    10464  11089  10849   -139   -201   -179       C  
ATOM   3892  CD2 LEU A 491      28.352   5.906  12.668  1.00 79.74           C  
ANISOU 3892  CD2 LEU A 491     9746  10387  10165   -166   -200   -186       C  
ATOM   3893  N   GLU A 492      31.908   2.731  14.007  1.00 93.47           N  
ANISOU 3893  N   GLU A 492    11438  12201  11876   -150   -235   -166       N  
ATOM   3894  CA  GLU A 492      32.759   1.856  14.777  1.00108.66           C  
ANISOU 3894  CA  GLU A 492    13349  14147  13790   -145   -245   -159       C  
ATOM   3895  C   GLU A 492      32.379   1.981  16.239  1.00103.51           C  
ANISOU 3895  C   GLU A 492    12704  13500  13124   -153   -256   -171       C  
ATOM   3896  O   GLU A 492      31.640   2.887  16.592  1.00101.78           O  
ANISOU 3896  O   GLU A 492    12500  13267  12905   -164   -254   -185       O  
ATOM   3897  CB  GLU A 492      34.226   2.241  14.563  1.00135.15           C  
ANISOU 3897  CB  GLU A 492    16681  17517  17152   -156   -251   -152       C  
ATOM   3898  CG  GLU A 492      35.171   1.054  14.434  1.00161.58           C  
ANISOU 3898  CG  GLU A 492    20011  20884  20499   -141   -252   -134       C  
ATOM   3899  CD  GLU A 492      34.750   0.083  13.334  1.00195.54           C  
ANISOU 3899  CD  GLU A 492    24318  25174  24802   -119   -237   -124       C  
ATOM   3900  OE1 GLU A 492      34.433   0.522  12.203  1.00216.74           O  
ANISOU 3900  OE1 GLU A 492    27010  27844  27497   -118   -226   -124       O  
ATOM   3901  OE2 GLU A 492      34.741  -1.138  13.603  1.00221.74           O1-
ANISOU 3901  OE2 GLU A 492    27637  28500  28115   -102   -236   -115       O1-
ATOM   3902  N   VAL A 493      32.863   1.052  17.068  1.00 98.78           N  
ANISOU 3902  N   VAL A 493    12096  12921  12513   -146   -265   -164       N  
ATOM   3903  CA  VAL A 493      32.430   0.925  18.478  1.00 92.30           C  
ANISOU 3903  CA  VAL A 493    11284  12109  11676   -149   -274   -172       C  
ATOM   3904  C   VAL A 493      32.521   2.258  19.228  1.00 85.50           C  
ANISOU 3904  C   VAL A 493    10428  11246  10811   -174   -282   -190       C  
ATOM   3905  O   VAL A 493      33.491   2.992  19.064  1.00 84.10           O  
ANISOU 3905  O   VAL A 493    10238  11077  10641   -191   -288   -192       O  
ATOM   3906  CB  VAL A 493      33.216  -0.169  19.228  1.00 93.51           C  
ANISOU 3906  CB  VAL A 493    11423  12289  11819   -139   -285   -158       C  
ATOM   3907  CG1 VAL A 493      34.718   0.074  19.143  1.00108.84           C  
ANISOU 3907  CG1 VAL A 493    13339  14252  13764   -150   -294   -150       C  
ATOM   3908  CG2 VAL A 493      32.784  -0.257  20.688  1.00 94.84           C  
ANISOU 3908  CG2 VAL A 493    11599  12467  11967   -143   -294   -167       C  
ATOM   3909  N   ASP A 494      31.504   2.565  20.036  1.00 77.36           N  
ANISOU 3909  N   ASP A 494     9417  10206   9770   -177   -281   -204       N  
ATOM   3910  CA  ASP A 494      31.371   3.886  20.597  1.00 75.55           C  
ANISOU 3910  CA  ASP A 494     9198   9968   9539   -200   -282   -224       C  
ATOM   3911  C   ASP A 494      32.211   4.021  21.847  1.00 86.40           C  
ANISOU 3911  C   ASP A 494    10565  11367  10896   -216   -300   -231       C  
ATOM   3912  O   ASP A 494      31.896   3.459  22.905  1.00 81.19           O  
ANISOU 3912  O   ASP A 494     9912  10720  10218   -211   -306   -232       O  
ATOM   3913  CB  ASP A 494      29.929   4.243  20.895  1.00 75.44           C  
ANISOU 3913  CB  ASP A 494     9209   9931   9523   -196   -271   -235       C  
ATOM   3914  CG  ASP A 494      29.758   5.715  21.191  1.00 85.31           C  
ANISOU 3914  CG  ASP A 494    10472  11166  10778   -219   -266   -255       C  
ATOM   3915  OD1 ASP A 494      30.657   6.508  20.809  1.00 83.18           O  
ANISOU 3915  OD1 ASP A 494    10190  10897  10517   -236   -270   -258       O  
ATOM   3916  OD2 ASP A 494      28.733   6.087  21.807  1.00 89.88           O1-
ANISOU 3916  OD2 ASP A 494    11071  11730  11351   -219   -258   -266       O1-
ATOM   3917  N   GLU A 495      33.279   4.806  21.687  1.00 96.60           N  
ANISOU 3917  N   GLU A 495    11842  12666  12194   -237   -308   -234       N  
ATOM   3918  CA  GLU A 495      34.287   5.047  22.700  1.00 95.56           C  
ANISOU 3918  CA  GLU A 495    11699  12561  12047   -257   -327   -240       C  
ATOM   3919  C   GLU A 495      33.809   6.054  23.728  1.00104.37           C  
ANISOU 3919  C   GLU A 495    12835  13669  13151   -278   -329   -265       C  
ATOM   3920  O   GLU A 495      34.056   5.860  24.921  1.00118.95           O  
ANISOU 3920  O   GLU A 495    14682  15537  14974   -287   -344   -271       O  
ATOM   3921  CB  GLU A 495      35.585   5.530  22.037  1.00 96.47           C  
ANISOU 3921  CB  GLU A 495    11791  12686  12178   -272   -334   -233       C  
ATOM   3922  CG  GLU A 495      36.391   4.418  21.384  1.00 99.75           C  
ANISOU 3922  CG  GLU A 495    12181  13119  12599   -253   -336   -206       C  
ATOM   3923  CD  GLU A 495      36.523   3.201  22.293  1.00106.25           C  
ANISOU 3923  CD  GLU A 495    12997  13968  13404   -238   -346   -194       C  
ATOM   3924  OE1 GLU A 495      36.621   3.372  23.531  1.00105.99           O  
ANISOU 3924  OE1 GLU A 495    12968  13953  13351   -252   -361   -204       O  
ATOM   3925  OE2 GLU A 495      36.501   2.062  21.782  1.00104.76           O1-
ANISOU 3925  OE2 GLU A 495    12802  13783  13219   -213   -339   -174       O1-
ATOM   3926  N   THR A 496      33.143   7.122  23.264  1.00103.83           N  
ANISOU 3926  N   THR A 496    12784  13570  13096   -287   -314   -280       N  
ATOM   3927  CA  THR A 496      32.392   8.060  24.120  1.00105.75           C  
ANISOU 3927  CA  THR A 496    13053  13798  13330   -302   -309   -305       C  
ATOM   3928  C   THR A 496      31.683   7.338  25.271  1.00110.45           C  
ANISOU 3928  C   THR A 496    13662  14402  13900   -291   -312   -308       C  
ATOM   3929  O   THR A 496      31.784   7.713  26.445  1.00 96.02           O  
ANISOU 3929  O   THR A 496    11845  12586  12052   -308   -321   -324       O  
ATOM   3930  CB  THR A 496      31.285   8.761  23.286  1.00104.99           C  
ANISOU 3930  CB  THR A 496    12974  13663  13253   -296   -285   -309       C  
ATOM   3931  CG2 THR A 496      30.450   9.790  24.118  1.00 99.72           C  
ANISOU 3931  CG2 THR A 496    12335  12975  12580   -310   -274   -334       C  
ATOM   3932  OG1 THR A 496      31.863   9.366  22.119  1.00100.89           O  
ANISOU 3932  OG1 THR A 496    12442  13134  12759   -303   -280   -304       O  
ATOM   3933  N   TYR A 497      30.974   6.278  24.903  1.00117.42           N  
ANISOU 3933  N   TYR A 497    14546  15283  14785   -263   -305   -291       N  
ATOM   3934  CA  TYR A 497      29.954   5.704  25.751  1.00114.63           C  
ANISOU 3934  CA  TYR A 497    14211  14929  14416   -248   -300   -293       C  
ATOM   3935  C   TYR A 497      30.502   5.225  27.088  1.00111.26           C  
ANISOU 3935  C   TYR A 497    13779  14532  13960   -254   -318   -295       C  
ATOM   3936  O   TYR A 497      31.358   4.343  27.161  1.00101.74           O  
ANISOU 3936  O   TYR A 497    12552  13354  12749   -248   -333   -278       O  
ATOM   3937  CB  TYR A 497      29.223   4.580  25.016  1.00104.96           C  
ANISOU 3937  CB  TYR A 497    12983  13695  13200   -218   -290   -272       C  
ATOM   3938  CG  TYR A 497      27.980   4.107  25.726  1.00 99.40           C  
ANISOU 3938  CG  TYR A 497    12298  12983  12485   -202   -282   -273       C  
ATOM   3939  CD1 TYR A 497      26.826   4.893  25.784  1.00 94.68           C  
ANISOU 3939  CD1 TYR A 497    11723  12357  11892   -204   -265   -286       C  
ATOM   3940  CD2 TYR A 497      27.957   2.860  26.341  1.00104.16           C  
ANISOU 3940  CD2 TYR A 497    12896  13606  13074   -185   -289   -260       C  
ATOM   3941  CE1 TYR A 497      25.692   4.443  26.440  1.00 94.25           C  
ANISOU 3941  CE1 TYR A 497    11685  12296  11829   -189   -256   -285       C  
ATOM   3942  CE2 TYR A 497      26.826   2.391  26.988  1.00 99.09           C  
ANISOU 3942  CE2 TYR A 497    12271  12957  12423   -170   -280   -259       C  
ATOM   3943  CZ  TYR A 497      25.696   3.180  27.044  1.00 95.92           C  
ANISOU 3943  CZ  TYR A 497    11891  12528  12026   -172   -264   -272       C  
ATOM   3944  OH  TYR A 497      24.587   2.688  27.700  1.00 82.57           O  
ANISOU 3944  OH  TYR A 497    10216  10831  10327   -156   -255   -269       O  
ATOM   3945  N   VAL A 498      30.013   5.883  28.133  1.00110.23           N  
ANISOU 3945  N   VAL A 498    13672  14398  13813   -267   -317   -316       N  
ATOM   3946  CA  VAL A 498      30.103   5.410  29.497  1.00 99.95           C  
ANISOU 3946  CA  VAL A 498    12374  13122  12481   -268   -330   -319       C  
ATOM   3947  C   VAL A 498      29.134   4.244  29.646  1.00106.72           C  
ANISOU 3947  C   VAL A 498    13237  13977  13334   -237   -321   -302       C  
ATOM   3948  O   VAL A 498      27.987   4.358  29.211  1.00112.44           O  
ANISOU 3948  O   VAL A 498    13977  14673  14072   -224   -301   -303       O  
ATOM   3949  CB  VAL A 498      29.705   6.520  30.482  1.00 94.39           C  
ANISOU 3949  CB  VAL A 498    11696  12407  11760   -290   -326   -348       C  
ATOM   3950  CG1 VAL A 498      28.305   7.057  30.194  1.00 91.35           C  
ANISOU 3950  CG1 VAL A 498    11337  11983  11388   -280   -299   -357       C  
ATOM   3951  CG2 VAL A 498      29.806   6.027  31.912  1.00 96.69           C  
ANISOU 3951  CG2 VAL A 498    11993  12728  12017   -292   -339   -351       C  
ATOM   3952  N   PRO A 499      29.595   3.113  30.215  1.00112.80           N  
ANISOU 3952  N   PRO A 499    13992  14777  14088   -225   -334   -285       N  
ATOM   3953  CA  PRO A 499      28.763   1.899  30.392  1.00112.26           C  
ANISOU 3953  CA  PRO A 499    13927  14709  14018   -196   -326   -268       C  
ATOM   3954  C   PRO A 499      27.732   1.960  31.540  1.00113.85           C  
ANISOU 3954  C   PRO A 499    14153  14906  14198   -191   -318   -278       C  
ATOM   3955  O   PRO A 499      28.095   2.286  32.665  1.00110.65           O  
ANISOU 3955  O   PRO A 499    13754  14521  13767   -206   -330   -290       O  
ATOM   3956  CB  PRO A 499      29.796   0.786  30.621  1.00113.16           C  
ANISOU 3956  CB  PRO A 499    14015  14859  14123   -187   -343   -245       C  
ATOM   3957  CG  PRO A 499      31.079   1.463  30.960  1.00112.63           C  
ANISOU 3957  CG  PRO A 499    13934  14816  14046   -214   -362   -254       C  
ATOM   3958  CD  PRO A 499      31.037   2.830  30.353  1.00113.45           C  
ANISOU 3958  CD  PRO A 499    14048  14894  14164   -236   -356   -275       C  
ATOM   3959  N   LYS A 500      26.474   1.600  31.253  1.00133.90           N  
ANISOU 3959  N   LYS A 500    16706  17421  16749   -171   -300   -273       N  
ATOM   3960  CA  LYS A 500      25.308   1.978  32.112  1.00143.51           C  
ANISOU 3960  CA  LYS A 500    17951  18623  17954   -168   -286   -286       C  
ATOM   3961  C   LYS A 500      24.886   1.059  33.277  1.00125.91           C  
ANISOU 3961  C   LYS A 500    15727  16412  15702   -151   -288   -276       C  
ATOM   3962  O   LYS A 500      23.868   0.363  33.207  1.00116.13           O  
ANISOU 3962  O   LYS A 500    14494  15160  14470   -129   -274   -263       O  
ATOM   3963  CB  LYS A 500      24.052   2.332  31.261  1.00153.57           C  
ANISOU 3963  CB  LYS A 500    19238  19858  19253   -157   -263   -286       C  
ATOM   3964  CG  LYS A 500      23.487   1.231  30.362  1.00151.63           C  
ANISOU 3964  CG  LYS A 500    18983  19604  19028   -132   -256   -263       C  
ATOM   3965  CD  LYS A 500      21.973   1.061  30.528  1.00147.27           C  
ANISOU 3965  CD  LYS A 500    18448  19029  18481   -114   -237   -259       C  
ATOM   3966  CE  LYS A 500      21.188   2.309  30.147  1.00147.72           C  
ANISOU 3966  CE  LYS A 500    18522  19054  18551   -124   -220   -273       C  
ATOM   3967  NZ  LYS A 500      19.718   2.062  30.166  1.00138.92           N1+
ANISOU 3967  NZ  LYS A 500    17420  17917  17445   -105   -201   -264       N1+
ATOM   3968  N   GLU A 501      25.642   1.125  34.367  1.00121.64           N  
ANISOU 3968  N   GLU A 501    15184  15902  15132   -165   -304   -283       N  
ATOM   3969  CA  GLU A 501      25.182   0.616  35.668  1.00128.83           C  
ANISOU 3969  CA  GLU A 501    16107  16829  16015   -155   -304   -280       C  
ATOM   3970  C   GLU A 501      24.793  -0.869  35.643  1.00122.34           C  
ANISOU 3970  C   GLU A 501    15272  16013  15197   -124   -300   -251       C  
ATOM   3971  O   GLU A 501      25.336  -1.686  34.868  1.00126.74           O  
ANISOU 3971  O   GLU A 501    15806  16577  15771   -113   -306   -231       O  
ATOM   3972  CB  GLU A 501      23.989   1.465  36.201  1.00137.90           C  
ANISOU 3972  CB  GLU A 501    17287  17950  17157   -157   -284   -300       C  
ATOM   3973  CG  GLU A 501      24.275   2.938  36.490  1.00135.32           C  
ANISOU 3973  CG  GLU A 501    16979  17616  16822   -188   -284   -332       C  
ATOM   3974  CD  GLU A 501      25.071   3.174  37.770  1.00130.49           C  
ANISOU 3974  CD  GLU A 501    16371  17038  16171   -208   -303   -345       C  
ATOM   3975  OE1 GLU A 501      25.073   4.335  38.230  1.00115.18           O  
ANISOU 3975  OE1 GLU A 501    14453  15089  14220   -232   -299   -374       O  
ATOM   3976  OE2 GLU A 501      25.698   2.220  38.308  1.00124.12           O1-
ANISOU 3976  OE2 GLU A 501    15547  16266  15346   -201   -320   -328       O1-
ATOM   3977  N   PHE A 502      23.854  -1.233  36.507  1.00109.33           N  
ANISOU 3977  N   PHE A 502    13641  14364  13537   -109   -290   -248       N  
ATOM   3978  CA  PHE A 502      23.450  -2.616  36.609  1.00114.05           C  
ANISOU 3978  CA  PHE A 502    14229  14968  14138    -81   -285   -221       C  
ATOM   3979  C   PHE A 502      22.009  -2.780  37.055  1.00117.27           C  
ANISOU 3979  C   PHE A 502    14657  15355  14546    -64   -265   -220       C  
ATOM   3980  O   PHE A 502      21.671  -2.586  38.225  1.00138.95           O  
ANISOU 3980  O   PHE A 502    17419  18110  17266    -64   -262   -227       O  
ATOM   3981  CB  PHE A 502      24.389  -3.383  37.538  1.00117.96           C  
ANISOU 3981  CB  PHE A 502    14708  15506  14607    -79   -304   -207       C  
ATOM   3982  CG  PHE A 502      24.531  -4.830  37.169  1.00128.70           C  
ANISOU 3982  CG  PHE A 502    16046  16874  15981    -53   -303   -176       C  
ATOM   3983  CD1 PHE A 502      23.661  -5.791  37.708  1.00128.46           C  
ANISOU 3983  CD1 PHE A 502    16020  16840  15948    -28   -291   -159       C  
ATOM   3984  CD2 PHE A 502      25.496  -5.234  36.251  1.00131.77           C  
ANISOU 3984  CD2 PHE A 502    16411  17270  16388    -53   -313   -164       C  
ATOM   3985  CE1 PHE A 502      23.772  -7.121  37.359  1.00133.70           C  
ANISOU 3985  CE1 PHE A 502    16665  17509  16626     -5   -289   -131       C  
ATOM   3986  CE2 PHE A 502      25.622  -6.575  35.911  1.00140.10           C  
ANISOU 3986  CE2 PHE A 502    17447  18330  17456    -30   -309   -136       C  
ATOM   3987  CZ  PHE A 502      24.745  -7.515  36.454  1.00146.01           C  
ANISOU 3987  CZ  PHE A 502    18200  19074  18201     -6   -297   -120       C  
ATOM   3988  N   ASN A 503      21.166  -3.134  36.094  1.00117.41           N  
ANISOU 3988  N   ASN A 503    14674  15343  14593    -49   -250   -210       N  
ATOM   3989  CA  ASN A 503      19.797  -3.512  36.370  1.00126.41           C  
ANISOU 3989  CA  ASN A 503    15828  16464  15739    -29   -230   -202       C  
ATOM   3990  C   ASN A 503      19.832  -4.792  37.200  1.00131.05           C  
ANISOU 3990  C   ASN A 503    16406  17074  16312     -9   -234   -180       C  
ATOM   3991  O   ASN A 503      20.547  -5.744  36.852  1.00142.81           O  
ANISOU 3991  O   ASN A 503    17874  18579  17807     -1   -244   -162       O  
ATOM   3992  CB  ASN A 503      19.030  -3.795  35.078  1.00130.35           C  
ANISOU 3992  CB  ASN A 503    16323  16932  16273    -18   -218   -192       C  
ATOM   3993  CG  ASN A 503      19.393  -2.855  33.921  1.00131.81           C  
ANISOU 3993  CG  ASN A 503    16505  17101  16476    -36   -220   -205       C  
ATOM   3994  ND2 ASN A 503      18.733  -3.052  32.787  1.00127.26           N  
ANISOU 3994  ND2 ASN A 503    15925  16500  15928    -28   -210   -197       N  
ATOM   3995  OD1 ASN A 503      20.255  -1.977  34.039  1.00140.77           O  
ANISOU 3995  OD1 ASN A 503    17641  18246  17601    -57   -230   -223       O  
ATOM   3996  N   ALA A 504      19.091  -4.823  38.302  1.00117.09           N  
ANISOU 3996  N   ALA A 504    14654  15308  14525      0   -224   -180       N  
ATOM   3997  CA  ALA A 504      18.940  -6.065  39.042  1.00107.27           C  
ANISOU 3997  CA  ALA A 504    13403  14082  13271     22   -223   -156       C  
ATOM   3998  C   ALA A 504      17.870  -6.871  38.331  1.00109.82           C  
ANISOU 3998  C   ALA A 504    13723  14378  13626     43   -207   -138       C  
ATOM   3999  O   ALA A 504      18.124  -7.966  37.829  1.00106.39           O  
ANISOU 3999  O   ALA A 504    13270  13947  13206     56   -209   -118       O  
ATOM   4000  CB  ALA A 504      18.548  -5.795  40.482  1.00101.89           C  
ANISOU 4000  CB  ALA A 504    12741  13415  12558     23   -218   -162       C  
ATOM   4001  N   GLU A 505      16.686  -6.274  38.243  1.00118.27           N  
ANISOU 4001  N   GLU A 505    14812  15420  14706     45   -189   -146       N  
ATOM   4002  CA  GLU A 505      15.495  -6.961  37.765  1.00117.37           C  
ANISOU 4002  CA  GLU A 505    14697  15280  14617     64   -172   -129       C  
ATOM   4003  C   GLU A 505      15.454  -7.130  36.254  1.00116.09           C  
ANISOU 4003  C   GLU A 505    14523  15098  14488     62   -173   -125       C  
ATOM   4004  O   GLU A 505      14.571  -7.820  35.745  1.00121.71           O  
ANISOU 4004  O   GLU A 505    15231  15790  15222     75   -162   -110       O  
ATOM   4005  CB  GLU A 505      14.220  -6.226  38.227  1.00116.98           C  
ANISOU 4005  CB  GLU A 505    14671  15209  14568     67   -152   -136       C  
ATOM   4006  CG  GLU A 505      13.773  -6.531  39.659  1.00117.19           C  
ANISOU 4006  CG  GLU A 505    14708  15249  14569     80   -143   -130       C  
ATOM   4007  CD  GLU A 505      12.307  -6.193  39.922  1.00117.52           C  
ANISOU 4007  CD  GLU A 505    14768  15263  14620     91   -119   -127       C  
ATOM   4008  OE1 GLU A 505      11.638  -5.656  39.018  1.00120.46           O  
ANISOU 4008  OE1 GLU A 505    15144  15608  15019     87   -109   -131       O  
ATOM   4009  OE2 GLU A 505      11.815  -6.467  41.036  1.00113.10           O1-
ANISOU 4009  OE2 GLU A 505    14218  14711  14042    104   -109   -120       O1-
ATOM   4010  N   THR A 506      16.384  -6.514  35.531  1.00104.71           N  
ANISOU 4010  N   THR A 506    13075  13660  13049     44   -185   -139       N  
ATOM   4011  CA  THR A 506      16.390  -6.641  34.084  1.00104.38           C  
ANISOU 4011  CA  THR A 506    13023  13601  13036     41   -186   -136       C  
ATOM   4012  C   THR A 506      17.055  -7.933  33.674  1.00107.84           C  
ANISOU 4012  C   THR A 506    13441  14051  13482     52   -194   -118       C  
ATOM   4013  O   THR A 506      16.934  -8.379  32.533  1.00118.11           O  
ANISOU 4013  O   THR A 506    14733  15337  14806     55   -192   -111       O  
ATOM   4014  CB  THR A 506      17.136  -5.479  33.438  1.00104.64           C  
ANISOU 4014  CB  THR A 506    13056  13632  13070     19   -194   -156       C  
ATOM   4015  CG2 THR A 506      16.859  -5.412  31.938  1.00105.25           C  
ANISOU 4015  CG2 THR A 506    13127  13687  13177     16   -190   -154       C  
ATOM   4016  OG1 THR A 506      16.724  -4.266  34.076  1.00106.27           O  
ANISOU 4016  OG1 THR A 506    13283  13831  13264      8   -187   -174       O  
ATOM   4017  N   PHE A 507      17.761  -8.528  34.619  1.00106.84           N  
ANISOU 4017  N   PHE A 507    13307  13952  13335     58   -202   -109       N  
ATOM   4018  CA  PHE A 507      18.530  -9.712  34.349  1.00 99.95           C  
ANISOU 4018  CA  PHE A 507    12415  13094  12468     69   -208    -91       C  
ATOM   4019  C   PHE A 507      18.032 -10.861  35.208  1.00 98.86           C  
ANISOU 4019  C   PHE A 507    12275  12963  12326     91   -200    -70       C  
ATOM   4020  O   PHE A 507      18.686 -11.891  35.309  1.00 91.02           O  
ANISOU 4020  O   PHE A 507    11266  11984  11333    103   -204    -52       O  
ATOM   4021  CB  PHE A 507      20.001  -9.414  34.621  1.00 98.76           C  
ANISOU 4021  CB  PHE A 507    12252  12973  12299     57   -226    -96       C  
ATOM   4022  CG  PHE A 507      20.630  -8.461  33.635  1.00 87.96           C  
ANISOU 4022  CG  PHE A 507    10883  11600  10941     36   -234   -113       C  
ATOM   4023  CD1 PHE A 507      20.357  -7.110  33.671  1.00 86.77           C  
ANISOU 4023  CD1 PHE A 507    10747  11438  10784     18   -233   -136       C  
ATOM   4024  CD2 PHE A 507      21.533  -8.920  32.696  1.00 86.65           C  
ANISOU 4024  CD2 PHE A 507    10698  11437  10788     36   -240   -105       C  
ATOM   4025  CE1 PHE A 507      20.965  -6.232  32.762  1.00 87.39           C  
ANISOU 4025  CE1 PHE A 507    10822  11511  10872      0   -240   -150       C  
ATOM   4026  CE2 PHE A 507      22.144  -8.050  31.788  1.00 84.89           C  
ANISOU 4026  CE2 PHE A 507    10472  11209  10573     18   -247   -120       C  
ATOM   4027  CZ  PHE A 507      21.857  -6.706  31.814  1.00 76.96           C  
ANISOU 4027  CZ  PHE A 507     9482  10195   9564      0   -247   -141       C  
ATOM   4028  N   THR A 508      16.874 -10.671  35.840  1.00107.43           N  
ANISOU 4028  N   THR A 508    13376  14036  13408     98   -188    -70       N  
ATOM   4029  CA  THR A 508      16.103 -11.782  36.398  1.00119.93           C  
ANISOU 4029  CA  THR A 508    14958  15615  14996    120   -176    -49       C  
ATOM   4030  C   THR A 508      14.780 -11.836  35.649  1.00118.71           C  
ANISOU 4030  C   THR A 508    14811  15427  14868    125   -161    -47       C  
ATOM   4031  O   THR A 508      14.273 -10.805  35.212  1.00123.23           O  
ANISOU 4031  O   THR A 508    15394  15982  15445    112   -158    -63       O  
ATOM   4032  CB  THR A 508      15.835 -11.620  37.903  1.00127.54           C  
ANISOU 4032  CB  THR A 508    15933  16597  15931    127   -172    -46       C  
ATOM   4033  CG2 THR A 508      17.136 -11.589  38.706  1.00136.73           C  
ANISOU 4033  CG2 THR A 508    17088  17799  17065    121   -189    -47       C  
ATOM   4034  OG1 THR A 508      15.126 -10.406  38.133  1.00126.62           O  
ANISOU 4034  OG1 THR A 508    15836  16466  15807    116   -166    -66       O  
ATOM   4035  N   PHE A 509      14.242 -13.038  35.478  1.00124.08           N  
ANISOU 4035  N   PHE A 509    15483  16095  15565    141   -152    -27       N  
ATOM   4036  CA  PHE A 509      13.009 -13.245  34.714  1.00134.74           C  
ANISOU 4036  CA  PHE A 509    16837  17414  16942    145   -139    -22       C  
ATOM   4037  C   PHE A 509      12.020 -14.022  35.572  1.00129.72           C  
ANISOU 4037  C   PHE A 509    16204  16774  16310    164   -125     -3       C  
ATOM   4038  O   PHE A 509      12.431 -14.871  36.355  1.00166.73           O  
ANISOU 4038  O   PHE A 509    20884  21479  20986    177   -125     12       O  
ATOM   4039  CB  PHE A 509      13.281 -14.055  33.427  1.00152.40           C  
ANISOU 4039  CB  PHE A 509    19062  19639  19204    144   -142    -17       C  
ATOM   4040  CG  PHE A 509      14.524 -13.633  32.660  1.00160.80           C  
ANISOU 4040  CG  PHE A 509    20118  20713  20264    130   -155    -30       C  
ATOM   4041  CD1 PHE A 509      15.677 -14.402  32.718  1.00143.95           C  
ANISOU 4041  CD1 PHE A 509    17970  18598  18125    136   -162    -21       C  
ATOM   4042  CD2 PHE A 509      14.526 -12.492  31.844  1.00167.85           C  
ANISOU 4042  CD2 PHE A 509    21017  21597  21161    112   -160    -48       C  
ATOM   4043  CE1 PHE A 509      16.806 -14.044  31.997  1.00142.54           C  
ANISOU 4043  CE1 PHE A 509    17784  18429  17946    124   -173    -30       C  
ATOM   4044  CE2 PHE A 509      15.664 -12.125  31.146  1.00168.73           C  
ANISOU 4044  CE2 PHE A 509    21122  21718  21271    100   -172    -59       C  
ATOM   4045  CZ  PHE A 509      16.805 -12.909  31.217  1.00155.96           C  
ANISOU 4045  CZ  PHE A 509    19490  20119  19649    106   -178    -50       C  
ATOM   4046  N   HIS A 510      10.724 -13.762  35.436  1.00108.24           N  
ANISOU 4046  N   HIS A 510    13492  14030  13603    165   -113     -2       N  
ATOM   4047  CA  HIS A 510       9.739 -14.553  36.180  1.00107.93           C  
ANISOU 4047  CA  HIS A 510    13454  13984  13570    184    -98     19       C  
ATOM   4048  C   HIS A 510       9.294 -15.770  35.359  1.00104.86           C  
ANISOU 4048  C   HIS A 510    13054  13577  13210    191    -93     35       C  
ATOM   4049  O   HIS A 510       9.741 -15.942  34.226  1.00101.76           O  
ANISOU 4049  O   HIS A 510    12654  13178  12832    181   -101     28       O  
ATOM   4050  CB  HIS A 510       8.564 -13.673  36.645  1.00117.03           C  
ANISOU 4050  CB  HIS A 510    14622  15124  14722    184    -85     15       C  
ATOM   4051  CG  HIS A 510       8.780 -13.054  38.000  1.00122.09           C  
ANISOU 4051  CG  HIS A 510    15274  15783  15329    188    -83     10       C  
ATOM   4052  CD2 HIS A 510       9.705 -12.161  38.435  1.00120.94           C  
ANISOU 4052  CD2 HIS A 510    15136  15658  15156    176    -93     -9       C  
ATOM   4053  ND1 HIS A 510       8.010 -13.367  39.102  1.00124.48           N  
ANISOU 4053  ND1 HIS A 510    15584  16088  15625    204    -68     24       N  
ATOM   4054  CE1 HIS A 510       8.443 -12.687  40.150  1.00118.89           C  
ANISOU 4054  CE1 HIS A 510    14888  15400  14884    203    -69     14       C  
ATOM   4055  NE2 HIS A 510       9.473 -11.950  39.773  1.00114.38           N  
ANISOU 4055  NE2 HIS A 510    14318  14840  14301    184    -85     -7       N  
ATOM   4056  N   ALA A 511       8.437 -16.616  35.940  1.00100.48           N  
ANISOU 4056  N   ALA A 511    12498  13015  12666    207    -80     55       N  
ATOM   4057  CA  ALA A 511       7.977 -17.859  35.294  1.00104.15           C  
ANISOU 4057  CA  ALA A 511    12952  13462  13158    213    -74     70       C  
ATOM   4058  C   ALA A 511       6.768 -17.679  34.356  1.00102.53           C  
ANISOU 4058  C   ALA A 511    12748  13228  12979    205    -69     70       C  
ATOM   4059  O   ALA A 511       6.140 -18.658  33.889  1.00 90.26           O  
ANISOU 4059  O   ALA A 511    11188  11656  11449    208    -63     83       O  
ATOM   4060  CB  ALA A 511       7.664 -18.900  36.347  1.00111.70           C  
ANISOU 4060  CB  ALA A 511    13904  14423  14115    235    -62     94       C  
ATOM   4061  N   ASP A 512       6.449 -16.421  34.076  1.00110.91           N  
ANISOU 4061  N   ASP A 512    13818  14285  14036    192    -72     55       N  
ATOM   4062  CA  ASP A 512       5.534 -16.077  32.991  1.00120.04           C  
ANISOU 4062  CA  ASP A 512    14975  15419  15215    180    -71     53       C  
ATOM   4063  C   ASP A 512       6.180 -16.370  31.634  1.00116.68           C  
ANISOU 4063  C   ASP A 512    14543  14989  14801    167    -84     43       C  
ATOM   4064  O   ASP A 512       5.510 -16.356  30.603  1.00123.25           O  
ANISOU 4064  O   ASP A 512    15373  15805  15653    156    -85     42       O  
ATOM   4065  CB  ASP A 512       5.119 -14.596  33.073  1.00118.97           C  
ANISOU 4065  CB  ASP A 512    14849  15281  15071    172    -69     41       C  
ATOM   4066  CG  ASP A 512       6.280 -13.638  32.832  1.00120.80           C  
ANISOU 4066  CG  ASP A 512    15087  15528  15285    159    -82     18       C  
ATOM   4067  OD1 ASP A 512       7.425 -13.935  33.290  1.00131.83           O  
ANISOU 4067  OD1 ASP A 512    16481  16944  16663    162    -89     14       O  
ATOM   4068  OD2 ASP A 512       6.027 -12.585  32.193  1.00119.73           O1-
ANISOU 4068  OD2 ASP A 512    14956  15383  15154    146    -83      7       O1-
ATOM   4069  N   ILE A 513       7.483 -16.639  31.658  1.00113.23           N  
ANISOU 4069  N   ILE A 513    14103  14569  14351    167    -92     36       N  
ATOM   4070  CA  ILE A 513       8.284 -16.858  30.456  1.00114.45           C  
ANISOU 4070  CA  ILE A 513    14252  14722  14512    156   -102     25       C  
ATOM   4071  C   ILE A 513       7.973 -18.183  29.749  1.00114.14           C  
ANISOU 4071  C   ILE A 513    14206  14667  14495    158    -98     36       C  
ATOM   4072  O   ILE A 513       8.177 -18.313  28.543  1.00117.47           O  
ANISOU 4072  O   ILE A 513    14626  15079  14927    146   -104     27       O  
ATOM   4073  CB  ILE A 513       9.791 -16.836  30.822  1.00112.32           C  
ANISOU 4073  CB  ILE A 513    13979  14476  14222    158   -110     19       C  
ATOM   4074  CG1 ILE A 513      10.665 -16.468  29.611  1.00107.09           C  
ANISOU 4074  CG1 ILE A 513    13314  13814  13561    143   -122      3       C  
ATOM   4075  CG2 ILE A 513      10.211 -18.161  31.445  1.00106.59           C  
ANISOU 4075  CG2 ILE A 513    13246  13758  13497    175   -105     36       C  
ATOM   4076  CD1 ILE A 513      12.039 -15.967  30.003  1.00102.47           C  
ANISOU 4076  CD1 ILE A 513    12726  13253  12954    140   -131     -6       C  
ATOM   4077  N   CYS A 514       7.494 -19.156  30.520  1.00112.39           N  
ANISOU 4077  N   CYS A 514    13982  14442  14281    173    -87     54       N  
ATOM   4078  CA  CYS A 514       7.289 -20.518  30.043  1.00112.04           C  
ANISOU 4078  CA  CYS A 514    13931  14381  14257    177    -81     65       C  
ATOM   4079  C   CYS A 514       5.990 -20.633  29.244  1.00106.94           C  
ANISOU 4079  C   CYS A 514    13286  13712  13634    167    -79     67       C  
ATOM   4080  O   CYS A 514       5.820 -21.521  28.396  1.00104.41           O  
ANISOU 4080  O   CYS A 514    12963  13376  13332    161    -78     68       O  
ATOM   4081  CB  CYS A 514       7.253 -21.456  31.243  1.00121.45           C  
ANISOU 4081  CB  CYS A 514    15119  15579  15448    198    -69     85       C  
ATOM   4082  SG  CYS A 514       8.649 -21.244  32.379  1.00137.39           S  
ANISOU 4082  SG  CYS A 514    17135  17631  17437    211    -73     86       S  
ATOM   4083  N   THR A 515       5.089 -19.698  29.515  1.00102.44           N  
ANISOU 4083  N   THR A 515    12720  13140  13063    164    -78     68       N  
ATOM   4084  CA  THR A 515       3.803 -19.589  28.831  1.00105.52           C  
ANISOU 4084  CA  THR A 515    13109  13511  13473    153    -77     73       C  
ATOM   4085  C   THR A 515       4.001 -18.983  27.440  1.00 98.79           C  
ANISOU 4085  C   THR A 515    12257  12655  12623    133    -90     56       C  
ATOM   4086  O   THR A 515       3.118 -19.024  26.579  1.00 94.87           O  
ANISOU 4086  O   THR A 515    11759  12144  12143    120    -92     58       O  
ATOM   4087  CB  THR A 515       2.856 -18.661  29.620  1.00101.55           C  
ANISOU 4087  CB  THR A 515    12609  13009  12968    158    -70     80       C  
ATOM   4088  CG2 THR A 515       3.067 -18.801  31.138  1.00 96.95           C  
ANISOU 4088  CG2 THR A 515    12028  12438  12369    178    -60     90       C  
ATOM   4089  OG1 THR A 515       3.098 -17.301  29.242  1.00113.67           O  
ANISOU 4089  OG1 THR A 515    14150  14550  14491    147    -77     65       O  
ATOM   4090  N   LEU A 516       5.174 -18.399  27.252  1.00 99.91           N  
ANISOU 4090  N   LEU A 516    12402  12811  12748    129    -97     40       N  
ATOM   4091  CA  LEU A 516       5.477 -17.635  26.061  1.00105.45           C  
ANISOU 4091  CA  LEU A 516    13106  13513  13448    112   -108     25       C  
ATOM   4092  C   LEU A 516       6.066 -18.488  24.947  1.00 99.59           C  
ANISOU 4092  C   LEU A 516    12363  12765  12713    103   -113     17       C  
ATOM   4093  O   LEU A 516       6.705 -19.502  25.219  1.00109.71           O  
ANISOU 4093  O   LEU A 516    13642  14047  13994    113   -109     21       O  
ATOM   4094  CB  LEU A 516       6.436 -16.493  26.415  1.00111.36           C  
ANISOU 4094  CB  LEU A 516    13859  14279  14175    111   -114     11       C  
ATOM   4095  CG  LEU A 516       5.786 -15.159  26.807  1.00113.89           C  
ANISOU 4095  CG  LEU A 516    14184  14599  14490    108   -111     10       C  
ATOM   4096  CD1 LEU A 516       6.861 -14.080  26.678  1.00118.59           C  
ANISOU 4096  CD1 LEU A 516    14782  15208  15067    101   -119     -8       C  
ATOM   4097  CD2 LEU A 516       4.560 -14.801  25.962  1.00110.74           C  
ANISOU 4097  CD2 LEU A 516    13783  14185  14109     98   -111     16       C  
ATOM   4098  N   SER A 517       5.856 -18.059  23.700  1.00 82.48           N  
ANISOU 4098  N   SER A 517    10197  10592  10551     86   -122      8       N  
ATOM   4099  CA  SER A 517       6.263 -18.844  22.543  1.00 82.67           C  
ANISOU 4099  CA  SER A 517    10220  10608  10581     76   -126      0       C  
ATOM   4100  C   SER A 517       7.780 -18.900  22.351  1.00 91.20           C  
ANISOU 4100  C   SER A 517    11302  11700  11648     79   -128    -12       C  
ATOM   4101  O   SER A 517       8.545 -18.357  23.147  1.00103.84           O  
ANISOU 4101  O   SER A 517    12903  13317  13235     88   -128    -13       O  
ATOM   4102  CB  SER A 517       5.566 -18.336  21.263  1.00 84.33           C  
ANISOU 4102  CB  SER A 517    10431  10811  10798     57   -134     -6       C  
ATOM   4103  OG  SER A 517       5.930 -17.009  20.953  1.00 81.66           O  
ANISOU 4103  OG  SER A 517    10094  10483  10448     50   -141    -15       O  
ATOM   4104  N   GLU A 518       8.183 -19.598  21.296  1.00 97.72           N  
ANISOU 4104  N   GLU A 518    12131  12519  12480     72   -129    -20       N  
ATOM   4105  CA  GLU A 518       9.560 -19.678  20.848  1.00111.02           C  
ANISOU 4105  CA  GLU A 518    13816  14213  14154     73   -130    -30       C  
ATOM   4106  C   GLU A 518      10.118 -18.266  20.590  1.00106.85           C  
ANISOU 4106  C   GLU A 518    13288  13699  13612     65   -140    -40       C  
ATOM   4107  O   GLU A 518      10.958 -17.764  21.371  1.00108.57           O  
ANISOU 4107  O   GLU A 518    13503  13933  13818     74   -141    -41       O  
ATOM   4108  CB  GLU A 518       9.615 -20.563  19.578  1.00121.61           C  
ANISOU 4108  CB  GLU A 518    15163  15540  15505     62   -128    -38       C  
ATOM   4109  CG  GLU A 518      11.004 -20.864  19.026  1.00136.89           C  
ANISOU 4109  CG  GLU A 518    17099  17480  17433     65   -126    -47       C  
ATOM   4110  CD  GLU A 518      11.895 -21.573  20.031  1.00141.40           C  
ANISOU 4110  CD  GLU A 518    17665  18059  18003     85   -116    -37       C  
ATOM   4111  OE1 GLU A 518      11.503 -22.667  20.506  1.00142.93           O  
ANISOU 4111  OE1 GLU A 518    17859  18241  18209     94   -105    -27       O  
ATOM   4112  OE2 GLU A 518      12.987 -21.032  20.338  1.00138.80           O1-
ANISOU 4112  OE2 GLU A 518    17330  17746  17661     91   -119    -39       O1-
ATOM   4113  N   LYS A 519       9.624 -17.633  19.518  1.00 96.80           N  
ANISOU 4113  N   LYS A 519    12018  12421  12342     49   -147    -48       N  
ATOM   4114  CA  LYS A 519      10.014 -16.284  19.145  1.00 95.60           C  
ANISOU 4114  CA  LYS A 519    11865  12279  12179     41   -155    -56       C  
ATOM   4115  C   LYS A 519      10.099 -15.474  20.406  1.00101.19           C  
ANISOU 4115  C   LYS A 519    12571  12998  12878     50   -154    -53       C  
ATOM   4116  O   LYS A 519      11.132 -14.881  20.712  1.00124.53           O  
ANISOU 4116  O   LYS A 519    15525  15968  15822     52   -156    -59       O  
ATOM   4117  CB  LYS A 519       8.954 -15.596  18.266  1.00106.66           C  
ANISOU 4117  CB  LYS A 519    13267  13674  13586     26   -161    -57       C  
ATOM   4118  CG  LYS A 519       8.832 -16.054  16.833  1.00115.86           C  
ANISOU 4118  CG  LYS A 519    14435  14831  14755     12   -165    -63       C  
ATOM   4119  CD  LYS A 519       7.868 -15.151  16.064  1.00113.95           C  
ANISOU 4119  CD  LYS A 519    14192  14588  14517     -3   -172    -61       C  
ATOM   4120  CE  LYS A 519       7.634 -15.683  14.655  1.00125.13           C  
ANISOU 4120  CE  LYS A 519    15611  15998  15934    -18   -178    -66       C  
ATOM   4121  NZ  LYS A 519       7.617 -14.601  13.630  1.00143.05           N1+
ANISOU 4121  NZ  LYS A 519    17880  18275  18198    -31   -186    -70       N1+
ATOM   4122  N   GLU A 520       8.995 -15.455  21.146  1.00 98.66           N  
ANISOU 4122  N   GLU A 520    12251  12672  12565     54   -149    -42       N  
ATOM   4123  CA  GLU A 520       8.854 -14.498  22.220  1.00108.43           C  
ANISOU 4123  CA  GLU A 520    13488  13917  13793     60   -147    -40       C  
ATOM   4124  C   GLU A 520       9.667 -14.870  23.469  1.00112.19           C  
ANISOU 4124  C   GLU A 520    13964  14406  14257     75   -144    -38       C  
ATOM   4125  O   GLU A 520       9.932 -14.011  24.309  1.00122.09           O  
ANISOU 4125  O   GLU A 520    15220  15671  15499     77   -144    -41       O  
ATOM   4126  CB  GLU A 520       7.370 -14.187  22.476  1.00127.20           C  
ANISOU 4126  CB  GLU A 520    15866  16283  16181     60   -143    -29       C  
ATOM   4127  CG  GLU A 520       6.831 -13.091  21.539  1.00140.55           C  
ANISOU 4127  CG  GLU A 520    17558  17969  17876     45   -148    -32       C  
ATOM   4128  CD  GLU A 520       5.439 -13.352  20.952  1.00148.68           C  
ANISOU 4128  CD  GLU A 520    18583  18985  18923     39   -147    -20       C  
ATOM   4129  OE1 GLU A 520       4.790 -14.364  21.297  1.00147.08           O  
ANISOU 4129  OE1 GLU A 520    18379  18775  18730     44   -143     -9       O  
ATOM   4130  OE2 GLU A 520       4.984 -12.523  20.129  1.00142.22           O1-
ANISOU 4130  OE2 GLU A 520    17763  18165  18108     27   -151    -20       O1-
ATOM   4131  N   ARG A 521      10.110 -16.124  23.571  1.00111.89           N  
ANISOU 4131  N   ARG A 521    13923  14368  14223     84   -140    -32       N  
ATOM   4132  CA  ARG A 521      11.147 -16.463  24.547  1.00110.81           C  
ANISOU 4132  CA  ARG A 521    13783  14248  14073     97   -139    -29       C  
ATOM   4133  C   ARG A 521      12.490 -15.914  24.052  1.00108.67           C  
ANISOU 4133  C   ARG A 521    13509  13990  13791     90   -147    -42       C  
ATOM   4134  O   ARG A 521      13.192 -15.216  24.793  1.00102.96           O  
ANISOU 4134  O   ARG A 521    12784  13284  13052     91   -151    -45       O  
ATOM   4135  CB  ARG A 521      11.231 -17.965  24.763  1.00116.54           C  
ANISOU 4135  CB  ARG A 521    14505  14967  14808    109   -130    -17       C  
ATOM   4136  CG  ARG A 521      11.886 -18.374  26.079  1.00117.68           C  
ANISOU 4136  CG  ARG A 521    14645  15128  14941    126   -126     -7       C  
ATOM   4137  CD  ARG A 521      11.858 -19.884  26.301  1.00117.02           C  
ANISOU 4137  CD  ARG A 521    14557  15037  14870    140   -115      8       C  
ATOM   4138  NE  ARG A 521      10.494 -20.390  26.195  1.00108.10           N  
ANISOU 4138  NE  ARG A 521    13431  13886  13757    139   -108     15       N  
ATOM   4139  CZ  ARG A 521       9.977 -20.987  25.127  1.00103.89           C  
ANISOU 4139  CZ  ARG A 521    12900  13333  13242    130   -106     12       C  
ATOM   4140  NH1 ARG A 521      10.704 -21.213  24.026  1.00100.00           N1+
ANISOU 4140  NH1 ARG A 521    12408  12836  12750    122   -109      1       N1+
ATOM   4141  NH2 ARG A 521       8.709 -21.361  25.172  1.00111.40           N  
ANISOU 4141  NH2 ARG A 521    13853  14268  14208    128   -101     21       N  
ATOM   4142  N   GLN A 522      12.830 -16.216  22.795  1.00102.34           N  
ANISOU 4142  N   GLN A 522    12706  13180  12996     82   -149    -48       N  
ATOM   4143  CA  GLN A 522      14.058 -15.699  22.171  1.00 99.18           C  
ANISOU 4143  CA  GLN A 522    12304  12792  12589     75   -155    -59       C  
ATOM   4144  C   GLN A 522      14.118 -14.171  22.206  1.00 94.35           C  
ANISOU 4144  C   GLN A 522    11694  12188  11968     64   -163    -69       C  
ATOM   4145  O   GLN A 522      15.180 -13.579  22.349  1.00105.72           O  
ANISOU 4145  O   GLN A 522    13130  13643  13397     62   -168    -75       O  
ATOM   4146  CB  GLN A 522      14.158 -16.151  20.715  1.00106.03           C  
ANISOU 4146  CB  GLN A 522    13173  13647  13465     67   -154    -64       C  
ATOM   4147  CG  GLN A 522      14.274 -17.652  20.499  1.00115.21           C  
ANISOU 4147  CG  GLN A 522    14336  14800  14638     76   -145    -57       C  
ATOM   4148  CD  GLN A 522      14.440 -18.010  19.026  1.00120.45           C  
ANISOU 4148  CD  GLN A 522    15004  15452  15308     66   -144    -66       C  
ATOM   4149  NE2 GLN A 522      15.376 -18.907  18.729  1.00126.98           N  
ANISOU 4149  NE2 GLN A 522    15829  16279  16137     74   -136    -65       N  
ATOM   4150  OE1 GLN A 522      13.729 -17.489  18.167  1.00127.65           O  
ANISOU 4150  OE1 GLN A 522    15921  16357  16223     52   -149    -73       O  
ATOM   4151  N   ILE A 523      12.968 -13.538  22.064  1.00 87.26           N  
ANISOU 4151  N   ILE A 523    10801  11278  11074     57   -162    -69       N  
ATOM   4152  CA  ILE A 523      12.882 -12.091  22.062  1.00 88.62           C  
ANISOU 4152  CA  ILE A 523    10977  11454  11242     47   -166    -78       C  
ATOM   4153  C   ILE A 523      13.307 -11.487  23.396  1.00 84.51           C  
ANISOU 4153  C   ILE A 523    10457  10948  10706     52   -167    -80       C  
ATOM   4154  O   ILE A 523      13.946 -10.446  23.419  1.00 98.68           O  
ANISOU 4154  O   ILE A 523    12251  12750  12491     44   -171    -90       O  
ATOM   4155  CB  ILE A 523      11.462 -11.632  21.664  1.00 99.85           C  
ANISOU 4155  CB  ILE A 523    12402  12860  12675     41   -163    -74       C  
ATOM   4156  CG1 ILE A 523      11.364 -11.485  20.141  1.00103.44           C  
ANISOU 4156  CG1 ILE A 523    12857  13308  13138     29   -167    -78       C  
ATOM   4157  CG2 ILE A 523      11.093 -10.300  22.303  1.00105.12           C  
ANISOU 4157  CG2 ILE A 523    13075  13529  13337     38   -161    -77       C  
ATOM   4158  CD1 ILE A 523       9.980 -11.769  19.586  1.00109.74           C  
ANISOU 4158  CD1 ILE A 523    13656  14092  13950     25   -165    -69       C  
ATOM   4159  N   LYS A 524      12.974 -12.122  24.506  1.00 82.35           N  
ANISOU 4159  N   LYS A 524    10184  10677  10429     65   -162    -70       N  
ATOM   4160  CA  LYS A 524      13.421 -11.595  25.789  1.00 88.65           C  
ANISOU 4160  CA  LYS A 524    10984  11491  11209     69   -163    -73       C  
ATOM   4161  C   LYS A 524      14.913 -11.842  25.901  1.00 85.79           C  
ANISOU 4161  C   LYS A 524    10613  11148  10836     69   -171    -76       C  
ATOM   4162  O   LYS A 524      15.638 -11.006  26.433  1.00 77.62           O  
ANISOU 4162  O   LYS A 524     9578  10127   9785     63   -177    -85       O  
ATOM   4163  CB  LYS A 524      12.677 -12.232  26.966  1.00101.93           C  
ANISOU 4163  CB  LYS A 524    12669  13173  12889     83   -155    -60       C  
ATOM   4164  CG  LYS A 524      11.161 -12.317  26.808  1.00114.62           C  
ANISOU 4164  CG  LYS A 524    14280  14759  14510     85   -146    -52       C  
ATOM   4165  CD  LYS A 524      10.440 -10.996  27.033  1.00125.92           C  
ANISOU 4165  CD  LYS A 524    15721  16184  15940     78   -142    -58       C  
ATOM   4166  CE  LYS A 524       9.073 -11.025  26.358  1.00134.62           C  
ANISOU 4166  CE  LYS A 524    16823  17265  17062     77   -135    -50       C  
ATOM   4167  NZ  LYS A 524       8.058 -10.179  27.038  1.00143.35           N1+
ANISOU 4167  NZ  LYS A 524    17936  18363  18168     79   -125    -46       N1+
ATOM   4168  N   LYS A 525      15.367 -12.983  25.373  1.00 87.17           N  
ANISOU 4168  N   LYS A 525    10781  11323  11019     76   -170    -68       N  
ATOM   4169  CA  LYS A 525      16.801 -13.328  25.347  1.00 90.63           C  
ANISOU 4169  CA  LYS A 525    11208  11778  11449     78   -175    -68       C  
ATOM   4170  C   LYS A 525      17.602 -12.287  24.577  1.00 78.87           C  
ANISOU 4170  C   LYS A 525     9717  10294   9956     63   -183    -81       C  
ATOM   4171  O   LYS A 525      18.736 -11.945  24.923  1.00 78.27           O  
ANISOU 4171  O   LYS A 525     9633  10237   9869     60   -191    -84       O  
ATOM   4172  CB  LYS A 525      17.047 -14.704  24.690  1.00 97.12           C  
ANISOU 4172  CB  LYS A 525    12024  12592  12284     88   -169    -58       C  
ATOM   4173  CG  LYS A 525      16.672 -15.955  25.488  1.00 96.46           C  
ANISOU 4173  CG  LYS A 525    11939  12508  12204    105   -160    -41       C  
ATOM   4174  CD  LYS A 525      17.065 -17.217  24.700  1.00 89.67           C  
ANISOU 4174  CD  LYS A 525    11075  11638  11358    113   -152    -34       C  
ATOM   4175  CE  LYS A 525      16.017 -18.322  24.792  1.00 88.04           C  
ANISOU 4175  CE  LYS A 525    10873  11413  11167    122   -140    -23       C  
ATOM   4176  NZ  LYS A 525      16.501 -19.604  24.208  1.00 85.64           N1+
ANISOU 4176  NZ  LYS A 525    10565  11100  10875    131   -130    -16       N1+
ATOM   4177  N   GLN A 526      17.009 -11.801  23.509  1.00 72.97           N  
ANISOU 4177  N   GLN A 526     8976   9530   9221     53   -182    -88       N  
ATOM   4178  CA  GLN A 526      17.687 -10.857  22.669  1.00 77.25           C  
ANISOU 4178  CA  GLN A 526     9515  10075   9762     39   -188   -100       C  
ATOM   4179  C   GLN A 526      17.672  -9.506  23.326  1.00 72.28           C  
ANISOU 4179  C   GLN A 526     8890   9451   9122     29   -192   -110       C  
ATOM   4180  O   GLN A 526      18.569  -8.700  23.136  1.00 74.70           O  
ANISOU 4180  O   GLN A 526     9193   9767   9423     19   -199   -119       O  
ATOM   4181  CB  GLN A 526      17.044 -10.846  21.286  1.00 82.80           C  
ANISOU 4181  CB  GLN A 526    10221  10759  10478     33   -185   -102       C  
ATOM   4182  CG  GLN A 526      17.505 -12.030  20.448  1.00 88.44           C  
ANISOU 4182  CG  GLN A 526    10933  11471  11201     39   -181    -97       C  
ATOM   4183  CD  GLN A 526      16.747 -12.188  19.145  1.00 91.14           C  
ANISOU 4183  CD  GLN A 526    11279  11795  11553     32   -179    -99       C  
ATOM   4184  NE2 GLN A 526      17.477 -12.527  18.082  1.00 84.75           N  
ANISOU 4184  NE2 GLN A 526    10468  10985  10747     30   -178   -102       N  
ATOM   4185  OE1 GLN A 526      15.516 -12.026  19.094  1.00 91.09           O  
ANISOU 4185  OE1 GLN A 526    11280  11777  11554     29   -177    -97       O  
ATOM   4186  N   THR A 527      16.652  -9.268  24.124  1.00 72.75           N  
ANISOU 4186  N   THR A 527     8958   9504   9179     33   -187   -108       N  
ATOM   4187  CA  THR A 527      16.610  -8.066  24.919  1.00 79.04           C  
ANISOU 4187  CA  THR A 527     9762  10306   9965     24   -189   -119       C  
ATOM   4188  C   THR A 527      17.771  -8.082  25.905  1.00 79.11           C  
ANISOU 4188  C   THR A 527     9766  10339   9955     25   -197   -121       C  
ATOM   4189  O   THR A 527      18.557  -7.139  25.972  1.00 74.01           O  
ANISOU 4189  O   THR A 527     9118   9701   9300     12   -204   -133       O  
ATOM   4190  CB  THR A 527      15.304  -7.997  25.701  1.00 80.93           C  
ANISOU 4190  CB  THR A 527    10012  10533  10204     31   -179   -114       C  
ATOM   4191  CG2 THR A 527      15.235  -6.728  26.472  1.00 83.70           C  
ANISOU 4191  CG2 THR A 527    10372  10887  10544     23   -178   -126       C  
ATOM   4192  OG1 THR A 527      14.200  -8.062  24.795  1.00 85.04           O  
ANISOU 4192  OG1 THR A 527    10534  11033  10742     31   -173   -109       O  
ATOM   4193  N   ALA A 528      17.880  -9.170  26.660  1.00 75.26           N  
ANISOU 4193  N   ALA A 528     9273   9861   9461     39   -196   -109       N  
ATOM   4194  CA  ALA A 528      18.958  -9.307  27.632  1.00 78.46           C  
ANISOU 4194  CA  ALA A 528     9670  10292   9847     40   -205   -107       C  
ATOM   4195  C   ALA A 528      20.308  -9.075  26.975  1.00 76.08           C  
ANISOU 4195  C   ALA A 528     9357  10004   9546     31   -215   -111       C  
ATOM   4196  O   ALA A 528      21.163  -8.391  27.524  1.00 74.37           O  
ANISOU 4196  O   ALA A 528     9137   9806   9315     20   -225   -119       O  
ATOM   4197  CB  ALA A 528      18.918 -10.682  28.304  1.00 80.57           C  
ANISOU 4197  CB  ALA A 528     9932  10568  10113     59   -201    -89       C  
ATOM   4198  N   LEU A 529      20.483  -9.633  25.785  1.00 77.71           N  
ANISOU 4198  N   LEU A 529     9557  10200   9769     34   -212   -106       N  
ATOM   4199  CA  LEU A 529      21.728  -9.476  25.053  1.00 82.65           C  
ANISOU 4199  CA  LEU A 529    10170  10836  10396     27   -218   -108       C  
ATOM   4200  C   LEU A 529      22.041  -8.026  24.726  1.00 80.52           C  
ANISOU 4200  C   LEU A 529     9903  10565  10124      7   -224   -125       C  
ATOM   4201  O   LEU A 529      23.191  -7.616  24.748  1.00 83.37           O  
ANISOU 4201  O   LEU A 529    10254  10943  10480     -2   -233   -127       O  
ATOM   4202  CB  LEU A 529      21.699 -10.278  23.758  1.00 82.86           C  
ANISOU 4202  CB  LEU A 529    10194  10849  10441     33   -211   -102       C  
ATOM   4203  CG  LEU A 529      23.024 -10.269  22.988  1.00 80.55           C  
ANISOU 4203  CG  LEU A 529     9888  10566  10151     29   -215   -101       C  
ATOM   4204  CD1 LEU A 529      24.215 -10.510  23.915  1.00 81.34           C  
ANISOU 4204  CD1 LEU A 529     9974  10694  10239     33   -223    -92       C  
ATOM   4205  CD2 LEU A 529      22.971 -11.320  21.891  1.00 80.57           C  
ANISOU 4205  CD2 LEU A 529     9890  10555  10168     39   -205    -93       C  
ATOM   4206  N   VAL A 530      21.015  -7.258  24.410  1.00 76.56           N  
ANISOU 4206  N   VAL A 530     9415  10044   9629      0   -219   -134       N  
ATOM   4207  CA  VAL A 530      21.196  -5.855  24.133  1.00 86.87           C  
ANISOU 4207  CA  VAL A 530    10725  11347  10936    -17   -222   -148       C  
ATOM   4208  C   VAL A 530      21.671  -5.142  25.412  1.00 86.09           C  
ANISOU 4208  C   VAL A 530    10628  11264  10817    -26   -229   -158       C  
ATOM   4209  O   VAL A 530      22.606  -4.339  25.376  1.00 76.47           O  
ANISOU 4209  O   VAL A 530     9404  10056   9594    -41   -237   -167       O  
ATOM   4210  CB  VAL A 530      19.882  -5.210  23.615  1.00100.68           C  
ANISOU 4210  CB  VAL A 530    12487  13071  12696    -20   -212   -153       C  
ATOM   4211  CG1 VAL A 530      20.057  -3.706  23.428  1.00111.77           C  
ANISOU 4211  CG1 VAL A 530    13896  14470  14100    -38   -212   -168       C  
ATOM   4212  CG2 VAL A 530      19.444  -5.822  22.303  1.00101.42           C  
ANISOU 4212  CG2 VAL A 530    12578  13151  12806    -15   -206   -145       C  
ATOM   4213  N   GLU A 531      21.008  -5.445  26.529  1.00 92.07           N  
ANISOU 4213  N   GLU A 531    11395  12025  11564    -18   -226   -155       N  
ATOM   4214  CA  GLU A 531      21.319  -4.844  27.827  1.00 95.70           C  
ANISOU 4214  CA  GLU A 531    11859  12500  12001    -26   -232   -165       C  
ATOM   4215  C   GLU A 531      22.701  -5.265  28.344  1.00101.19           C  
ANISOU 4215  C   GLU A 531    12538  13226  12682    -28   -247   -160       C  
ATOM   4216  O   GLU A 531      23.361  -4.507  29.053  1.00100.08           O  
ANISOU 4216  O   GLU A 531    12398  13101  12525    -43   -257   -171       O  
ATOM   4217  CB  GLU A 531      20.245  -5.213  28.860  1.00101.37           C  
ANISOU 4217  CB  GLU A 531    12591  13215  12711    -14   -224   -161       C  
ATOM   4218  CG  GLU A 531      18.972  -4.376  28.764  1.00113.98           C  
ANISOU 4218  CG  GLU A 531    14205  14786  14316    -17   -211   -169       C  
ATOM   4219  CD  GLU A 531      19.150  -2.934  29.260  1.00136.03           C  
ANISOU 4219  CD  GLU A 531    17009  17577  17097    -35   -211   -190       C  
ATOM   4220  OE1 GLU A 531      19.766  -2.734  30.342  1.00154.63           O  
ANISOU 4220  OE1 GLU A 531    19368  19954  19430    -42   -219   -197       O  
ATOM   4221  OE2 GLU A 531      18.663  -1.994  28.573  1.00139.40           O1-
ANISOU 4221  OE2 GLU A 531    17444  17983  17538    -44   -203   -198       O1-
ATOM   4222  N   LEU A 532      23.123  -6.474  27.979  1.00103.97           N  
ANISOU 4222  N   LEU A 532    12877  13586  13041    -14   -248   -142       N  
ATOM   4223  CA  LEU A 532      24.425  -7.023  28.355  1.00 93.88           C  
ANISOU 4223  CA  LEU A 532    11580  12336  11753    -12   -259   -132       C  
ATOM   4224  C   LEU A 532      25.561  -6.209  27.815  1.00 84.75           C  
ANISOU 4224  C   LEU A 532    10413  11190  10599    -30   -270   -140       C  
ATOM   4225  O   LEU A 532      26.548  -5.976  28.484  1.00 95.41           O  
ANISOU 4225  O   LEU A 532    11753  12565  11934    -39   -283   -140       O  
ATOM   4226  CB  LEU A 532      24.584  -8.431  27.801  1.00108.74           C  
ANISOU 4226  CB  LEU A 532    13450  14217  13648      8   -253   -111       C  
ATOM   4227  CG  LEU A 532      24.028  -9.570  28.641  1.00138.54           C  
ANISOU 4227  CG  LEU A 532    17225  17995  17417     28   -247    -95       C  
ATOM   4228  CD1 LEU A 532      24.082 -10.873  27.862  1.00155.20           C  
ANISOU 4228  CD1 LEU A 532    19327  20097  19546     45   -237    -78       C  
ATOM   4229  CD2 LEU A 532      24.831  -9.708  29.926  1.00151.41           C  
ANISOU 4229  CD2 LEU A 532    18846  19658  19024     28   -259    -88       C  
ATOM   4230  N   VAL A 533      25.423  -5.788  26.578  1.00 83.68           N  
ANISOU 4230  N   VAL A 533    10279  11034  10481    -35   -264   -145       N  
ATOM   4231  CA  VAL A 533      26.463  -5.046  25.920  1.00 82.58           C  
ANISOU 4231  CA  VAL A 533    10128  10900  10347    -51   -271   -151       C  
ATOM   4232  C   VAL A 533      26.388  -3.565  26.250  1.00 85.89           C  
ANISOU 4232  C   VAL A 533    10559  11316  10760    -73   -275   -173       C  
ATOM   4233  O   VAL A 533      27.407  -2.891  26.333  1.00 82.28           O  
ANISOU 4233  O   VAL A 533    10093  10873  10299    -90   -286   -179       O  
ATOM   4234  CB  VAL A 533      26.348  -5.260  24.430  1.00 80.67           C  
ANISOU 4234  CB  VAL A 533     9885  10640  10127    -46   -262   -147       C  
ATOM   4235  CG1 VAL A 533      27.423  -4.477  23.707  1.00 82.93           C  
ANISOU 4235  CG1 VAL A 533    10159  10932  10420    -61   -268   -152       C  
ATOM   4236  CG2 VAL A 533      26.461  -6.749  24.151  1.00 77.69           C  
ANISOU 4236  CG2 VAL A 533     9498  10265   9755    -25   -256   -128       C  
ATOM   4237  N   LYS A 534      25.175  -3.062  26.431  1.00 98.74           N  
ANISOU 4237  N   LYS A 534    12206  12922  12388    -74   -265   -183       N  
ATOM   4238  CA  LYS A 534      24.974  -1.753  27.038  1.00114.80           C  
ANISOU 4238  CA  LYS A 534    14254  14952  14413    -93   -266   -203       C  
ATOM   4239  C   LYS A 534      25.714  -1.663  28.377  1.00123.25           C  
ANISOU 4239  C   LYS A 534    15322  16050  15458   -102   -280   -208       C  
ATOM   4240  O   LYS A 534      26.049  -0.550  28.809  1.00129.26           O  
ANISOU 4240  O   LYS A 534    16089  16814  16210   -123   -285   -226       O  
ATOM   4241  CB  LYS A 534      23.471  -1.454  27.251  1.00124.70           C  
ANISOU 4241  CB  LYS A 534    15530  16181  15670    -86   -251   -209       C  
ATOM   4242  CG  LYS A 534      22.770  -0.732  26.103  1.00120.58           C  
ANISOU 4242  CG  LYS A 534    15015  15631  15170    -90   -239   -213       C  
ATOM   4243  CD  LYS A 534      21.591   0.088  26.608  1.00114.12           C  
ANISOU 4243  CD  LYS A 534    14218  14793  14351    -92   -225   -224       C  
ATOM   4244  CE  LYS A 534      20.847   0.761  25.474  1.00114.93           C  
ANISOU 4244  CE  LYS A 534    14325  14868  14475    -94   -213   -224       C  
ATOM   4245  NZ  LYS A 534      19.715  -0.066  24.983  1.00115.57           N1+
ANISOU 4245  NZ  LYS A 534    14408  14936  14568    -75   -203   -209       N1+
ATOM   4246  N   HIS A 535      25.954  -2.818  29.019  1.00129.00           N  
ANISOU 4246  N   HIS A 535    16041  16799  16175    -87   -286   -192       N  
ATOM   4247  CA  HIS A 535      26.685  -2.896  30.305  1.00135.21           C  
ANISOU 4247  CA  HIS A 535    16821  17617  16935    -94   -301   -192       C  
ATOM   4248  C   HIS A 535      28.187  -3.117  30.142  1.00114.18           C  
ANISOU 4248  C   HIS A 535    14133  14982  14270   -101   -317   -182       C  
ATOM   4249  O   HIS A 535      28.946  -2.177  30.318  1.00113.92           O  
ANISOU 4249  O   HIS A 535    14096  14959  14229   -124   -329   -195       O  
ATOM   4250  CB  HIS A 535      26.094  -3.973  31.234  1.00148.61           C  
ANISOU 4250  CB  HIS A 535    18522  19325  18619    -73   -297   -178       C  
ATOM   4251  CG  HIS A 535      24.778  -3.596  31.849  1.00177.04           C  
ANISOU 4251  CG  HIS A 535    22148  22906  22213    -70   -285   -189       C  
ATOM   4252  CD2 HIS A 535      24.024  -4.217  32.790  1.00191.14           C  
ANISOU 4252  CD2 HIS A 535    23943  24696  23986    -55   -279   -181       C  
ATOM   4253  ND1 HIS A 535      24.063  -2.479  31.468  1.00193.83           N  
ANISOU 4253  ND1 HIS A 535    24292  25006  24348    -81   -274   -208       N  
ATOM   4254  CE1 HIS A 535      22.937  -2.419  32.162  1.00202.66           C  
ANISOU 4254  CE1 HIS A 535    25430  26113  25460    -74   -263   -211       C  
ATOM   4255  NE2 HIS A 535      22.887  -3.462  32.969  1.00207.72           N  
ANISOU 4255  NE2 HIS A 535    26066  26772  26087    -57   -265   -196       N  
ATOM   4256  N   LYS A 536      28.626  -4.332  29.830  1.00 97.07           N  
ANISOU 4256  N   LYS A 536    11947  12826  12110    -82   -317   -158       N  
ATOM   4257  CA  LYS A 536      30.048  -4.559  29.603  1.00 99.23           C  
ANISOU 4257  CA  LYS A 536    12195  13125  12385    -87   -330   -146       C  
ATOM   4258  C   LYS A 536      30.438  -4.544  28.096  1.00 94.57           C  
ANISOU 4258  C   LYS A 536    11595  12517  11821    -85   -323   -141       C  
ATOM   4259  O   LYS A 536      30.584  -5.591  27.489  1.00102.56           O  
ANISOU 4259  O   LYS A 536    12596  13527  12845    -66   -315   -123       O  
ATOM   4260  CB  LYS A 536      30.497  -5.858  30.307  1.00111.51           C  
ANISOU 4260  CB  LYS A 536    13734  14706  13929    -68   -335   -120       C  
ATOM   4261  CG  LYS A 536      32.028  -5.978  30.498  1.00132.90           C  
ANISOU 4261  CG  LYS A 536    16415  17450  16633    -76   -352   -106       C  
ATOM   4262  CD  LYS A 536      32.489  -6.616  31.823  1.00136.46           C  
ANISOU 4262  CD  LYS A 536    16853  17938  17058    -71   -365    -90       C  
ATOM   4263  CE  LYS A 536      32.882  -8.098  31.728  1.00128.95           C  
ANISOU 4263  CE  LYS A 536    15882  16999  16116    -43   -359    -57       C  
ATOM   4264  NZ  LYS A 536      33.004  -8.734  33.081  1.00124.03           N1+
ANISOU 4264  NZ  LYS A 536    15252  16407  15467    -34   -368    -41       N1+
ATOM   4265  N   PRO A 537      30.629  -3.350  27.489  1.00 78.73           N  
ANISOU 4265  N   PRO A 537     9593  10500   9823   -106   -324   -159       N  
ATOM   4266  CA  PRO A 537      31.160  -3.366  26.130  1.00 78.81           C  
ANISOU 4266  CA  PRO A 537     9590  10499   9855   -104   -319   -152       C  
ATOM   4267  C   PRO A 537      32.613  -3.761  26.085  1.00 95.59           C  
ANISOU 4267  C   PRO A 537    11687  12652  11981   -105   -330   -135       C  
ATOM   4268  O   PRO A 537      33.114  -4.117  25.024  1.00 92.56           O  
ANISOU 4268  O   PRO A 537    11292  12263  11615    -97   -323   -123       O  
ATOM   4269  CB  PRO A 537      31.053  -1.916  25.692  1.00 73.45           C  
ANISOU 4269  CB  PRO A 537     8921   9803   9183   -127   -318   -174       C  
ATOM   4270  CG  PRO A 537      31.045  -1.144  26.947  1.00 73.43           C  
ANISOU 4270  CG  PRO A 537     8928   9813   9159   -146   -329   -190       C  
ATOM   4271  CD  PRO A 537      30.370  -1.984  27.959  1.00 70.03           C  
ANISOU 4271  CD  PRO A 537     8507   9391   8712   -130   -328   -184       C  
ATOM   4272  N   LYS A 538      33.272  -3.686  27.242  1.00121.75           N  
ANISOU 4272  N   LYS A 538    14990  15995  15273   -115   -347   -133       N  
ATOM   4273  CA  LYS A 538      34.724  -3.773  27.350  1.00153.46           C  
ANISOU 4273  CA  LYS A 538    18978  20042  19288   -123   -362   -118       C  
ATOM   4274  C   LYS A 538      35.283  -5.178  27.064  1.00165.85           C  
ANISOU 4274  C   LYS A 538    20526  21623  20864    -97   -356    -87       C  
ATOM   4275  O   LYS A 538      35.700  -5.459  25.933  1.00154.24           O  
ANISOU 4275  O   LYS A 538    19046  20143  19415    -89   -346    -77       O  
ATOM   4276  CB  LYS A 538      35.172  -3.272  28.736  1.00158.14           C  
ANISOU 4276  CB  LYS A 538    19568  20665  19853   -143   -383   -126       C  
ATOM   4277  N   ALA A 539      35.301  -6.039  28.084  1.00179.08           N  
ANISOU 4277  N   ALA A 539    22196  23321  22524    -85   -362    -72       N  
ATOM   4278  CA  ALA A 539      35.836  -7.407  27.957  1.00186.90           C  
ANISOU 4278  CA  ALA A 539    23167  24325  23523    -59   -355    -41       C  
ATOM   4279  C   ALA A 539      34.795  -8.335  27.294  1.00194.16           C  
ANISOU 4279  C   ALA A 539    24102  25213  24457    -33   -332    -37       C  
ATOM   4280  O   ALA A 539      34.020  -9.008  27.991  1.00218.39           O  
ANISOU 4280  O   ALA A 539    27181  28281  27517    -19   -327    -33       O  
ATOM   4281  CB  ALA A 539      36.259  -7.943  29.326  1.00172.50           C  
ANISOU 4281  CB  ALA A 539    21329  22538  21676    -55   -369    -24       C  
ATOM   4282  N   THR A 540      34.789  -8.365  25.954  1.00168.00           N  
ANISOU 4282  N   THR A 540    20791  21876  21166    -28   -318    -39       N  
ATOM   4283  CA  THR A 540      33.653  -8.891  25.175  1.00122.26           C  
ANISOU 4283  CA  THR A 540    15018  16049  15386    -13   -298    -44       C  
ATOM   4284  C   THR A 540      34.026  -9.419  23.771  1.00106.02           C  
ANISOU 4284  C   THR A 540    12955  13976  13351     -1   -282    -34       C  
ATOM   4285  O   THR A 540      34.670  -8.729  22.975  1.00 93.58           O  
ANISOU 4285  O   THR A 540    11372  12399  11785    -12   -284    -39       O  
ATOM   4286  CB  THR A 540      32.609  -7.784  25.051  1.00103.47           C  
ANISOU 4286  CB  THR A 540    12662  13647  13004    -30   -299    -72       C  
ATOM   4287  CG2 THR A 540      31.971  -7.525  26.388  1.00 97.63           C  
ANISOU 4287  CG2 THR A 540    11935  12917  12243    -35   -307    -80       C  
ATOM   4288  OG1 THR A 540      33.256  -6.576  24.626  1.00 93.10           O  
ANISOU 4288  OG1 THR A 540    11344  12336  11693    -52   -307    -84       O  
ATOM   4289  N   LYS A 541      33.612 -10.647  23.478  1.00 93.02           N  
ANISOU 4289  N   LYS A 541    11313  12317  11714     22   -266    -21       N  
ATOM   4290  CA  LYS A 541      34.055 -11.325  22.274  1.00 89.90           C  
ANISOU 4290  CA  LYS A 541    10911  11909  11337     36   -250    -10       C  
ATOM   4291  C   LYS A 541      33.095 -12.438  21.950  1.00 91.41           C  
ANISOU 4291  C   LYS A 541    11119  12077  11537     56   -231     -8       C  
ATOM   4292  O   LYS A 541      32.287 -12.281  21.031  1.00 77.05           O  
ANISOU 4292  O   LYS A 541     9319  10232   9726     53   -222    -22       O  
ATOM   4293  CB  LYS A 541      35.466 -11.892  22.456  1.00 89.07           C  
ANISOU 4293  CB  LYS A 541    10778  11830  11236     46   -251     16       C  
ATOM   4294  N   GLU A 542      33.244 -13.558  22.672  1.00113.50           N  
ANISOU 4294  N   GLU A 542    13907  14884  14332     75   -226     13       N  
ATOM   4295  CA  GLU A 542      32.290 -14.706  22.695  1.00123.65           C  
ANISOU 4295  CA  GLU A 542    15208  16150  15625     93   -210     17       C  
ATOM   4296  C   GLU A 542      32.094 -15.221  24.137  1.00120.08           C  
ANISOU 4296  C   GLU A 542    14750  15717  15160    102   -216     30       C  
ATOM   4297  O   GLU A 542      31.248 -16.067  24.400  1.00122.87           O  
ANISOU 4297  O   GLU A 542    15113  16055  15515    116   -205     34       O  
ATOM   4298  CB  GLU A 542      32.760 -15.868  21.801  1.00120.11           C  
ANISOU 4298  CB  GLU A 542    14754  15689  15194    113   -189     33       C  
ATOM   4299  N   GLN A 543      32.935 -14.745  25.052  1.00106.74           N  
ANISOU 4299  N   GLN A 543    13042  14059  13455     95   -234     39       N  
ATOM   4300  CA  GLN A 543      32.664 -14.750  26.481  1.00100.98           C  
ANISOU 4300  CA  GLN A 543    12311  13351  12706     95   -246     43       C  
ATOM   4301  C   GLN A 543      31.230 -14.367  26.826  1.00102.63           C  
ANISOU 4301  C   GLN A 543    12546  13540  12907     89   -246     23       C  
ATOM   4302  O   GLN A 543      30.736 -14.642  27.921  1.00 92.15           O  
ANISOU 4302  O   GLN A 543    11222  12223  11567     94   -249     28       O  
ATOM   4303  CB  GLN A 543      33.580 -13.727  27.115  1.00107.09           C  
ANISOU 4303  CB  GLN A 543    13069  14156  13463     75   -269     41       C  
ATOM   4304  CG  GLN A 543      33.735 -12.453  26.289  1.00102.41           C  
ANISOU 4304  CG  GLN A 543    12483  13554  12874     51   -276     18       C  
ATOM   4305  CD  GLN A 543      35.119 -11.851  26.444  1.00115.45           C  
ANISOU 4305  CD  GLN A 543    14110  15236  14521     37   -292     26       C  
ATOM   4306  NE2 GLN A 543      35.875 -11.753  25.349  1.00110.52           N  
ANISOU 4306  NE2 GLN A 543    13475  14606  13914     37   -286     30       N  
ATOM   4307  OE1 GLN A 543      35.509 -11.482  27.549  1.00135.15           O  
ANISOU 4307  OE1 GLN A 543    16596  17760  16997     27   -310     28       O  
ATOM   4308  N   LEU A 544      30.591 -13.670  25.892  1.00108.93           N  
ANISOU 4308  N   LEU A 544    13361  14314  13714     76   -243      1       N  
ATOM   4309  CA  LEU A 544      29.170 -13.365  25.966  1.00100.44           C  
ANISOU 4309  CA  LEU A 544    12310  13216  12637     72   -239    -17       C  
ATOM   4310  C   LEU A 544      28.331 -14.561  25.620  1.00 99.83           C  
ANISOU 4310  C   LEU A 544    12242  13115  12574     92   -221     -9       C  
ATOM   4311  O   LEU A 544      27.435 -14.929  26.368  1.00 79.64           O  
ANISOU 4311  O   LEU A 544     9695  10554  10012     99   -218     -7       O  
ATOM   4312  CB  LEU A 544      28.827 -12.247  24.994  1.00 97.52           C  
ANISOU 4312  CB  LEU A 544    11953  12827  12274     54   -241    -40       C  
ATOM   4313  CG  LEU A 544      29.122 -10.863  25.550  1.00 96.76           C  
ANISOU 4313  CG  LEU A 544    11856  12746  12162     31   -258    -55       C  
ATOM   4314  CD1 LEU A 544      29.426  -9.854  24.446  1.00 95.29           C  
ANISOU 4314  CD1 LEU A 544    11671  12549  11986     15   -259    -70       C  
ATOM   4315  CD2 LEU A 544      27.939 -10.449  26.408  1.00 95.98           C  
ANISOU 4315  CD2 LEU A 544    11776  12640  12052     27   -259    -67       C  
ATOM   4316  N   LYS A 545      28.636 -15.150  24.466  1.00118.16           N  
ANISOU 4316  N   LYS A 545    14561  15421  14913     99   -208     -4       N  
ATOM   4317  CA  LYS A 545      28.028 -16.407  23.997  1.00135.12           C  
ANISOU 4317  CA  LYS A 545    16718  17547  17077    117   -189      4       C  
ATOM   4318  C   LYS A 545      28.049 -17.452  25.107  1.00132.30           C  
ANISOU 4318  C   LYS A 545    16352  17201  16715    136   -184     26       C  
ATOM   4319  O   LYS A 545      27.249 -18.387  25.112  1.00144.44           O  
ANISOU 4319  O   LYS A 545    17899  18720  18263    149   -170     31       O  
ATOM   4320  CB  LYS A 545      28.786 -16.936  22.757  1.00136.87           C  
ANISOU 4320  CB  LYS A 545    16933  17757  17313    123   -176      9       C  
ATOM   4321  CG  LYS A 545      28.141 -18.101  22.014  1.00121.22           C  
ANISOU 4321  CG  LYS A 545    14964  15747  15348    136   -155     12       C  
ATOM   4322  CD  LYS A 545      29.012 -18.557  20.852  1.00119.17           C  
ANISOU 4322  CD  LYS A 545    14698  15479  15100    142   -141     16       C  
ATOM   4323  CE  LYS A 545      29.007 -20.074  20.699  1.00117.41           C  
ANISOU 4323  CE  LYS A 545    14477  15241  14892    164   -119     32       C  
ATOM   4324  NZ  LYS A 545      30.195 -20.560  19.943  1.00113.32           N1+
ANISOU 4324  NZ  LYS A 545    13947  14724  14384    174   -105     43       N1+
ATOM   4325  N   ALA A 546      28.981 -17.279  26.039  1.00120.17           N  
ANISOU 4325  N   ALA A 546    14797  15696  15165    137   -196     39       N  
ATOM   4326  CA  ALA A 546      29.081 -18.115  27.218  1.00121.70           C  
ANISOU 4326  CA  ALA A 546    14980  15907  15352    154   -194     61       C  
ATOM   4327  C   ALA A 546      27.971 -17.768  28.185  1.00111.77           C  
ANISOU 4327  C   ALA A 546    13738  14650  14081    149   -200     52       C  
ATOM   4328  O   ALA A 546      27.147 -18.622  28.544  1.00108.09           O  
ANISOU 4328  O   ALA A 546    13279  14171  13620    164   -188     61       O  
ATOM   4329  CB  ALA A 546      30.439 -17.918  27.875  1.00130.75           C  
ANISOU 4329  CB  ALA A 546    16101  17091  16485    153   -207     78       C  
ATOM   4330  N   VAL A 547      27.942 -16.492  28.566  1.00104.38           N  
ANISOU 4330  N   VAL A 547    12807  13727  13128    129   -218     35       N  
ATOM   4331  CA  VAL A 547      26.926 -15.962  29.471  1.00 99.63           C  
ANISOU 4331  CA  VAL A 547    12220  13124  12510    123   -223     23       C  
ATOM   4332  C   VAL A 547      25.547 -16.010  28.806  1.00107.92           C  
ANISOU 4332  C   VAL A 547    13291  14138  13574    123   -211      9       C  
ATOM   4333  O   VAL A 547      24.526 -16.072  29.496  1.00104.86           O  
ANISOU 4333  O   VAL A 547    12917  13745  13182    127   -208      8       O  
ATOM   4334  CB  VAL A 547      27.275 -14.519  29.913  1.00 82.78           C  
ANISOU 4334  CB  VAL A 547    10088  11009  10356     99   -243      5       C  
ATOM   4335  CG1 VAL A 547      26.196 -13.950  30.826  1.00 73.62           C  
ANISOU 4335  CG1 VAL A 547     8946   9846   9180     94   -246     -8       C  
ATOM   4336  CG2 VAL A 547      28.629 -14.502  30.604  1.00 79.79           C  
ANISOU 4336  CG2 VAL A 547     9686  10668   9962     97   -257     19       C  
ATOM   4337  N   MET A 548      25.517 -15.993  27.471  1.00116.49           N  
ANISOU 4337  N   MET A 548    14381  15202  14678    118   -204      1       N  
ATOM   4338  CA  MET A 548      24.249 -16.009  26.750  1.00118.29           C  
ANISOU 4338  CA  MET A 548    14628  15398  14919    116   -194    -12       C  
ATOM   4339  C   MET A 548      23.635 -17.387  26.722  1.00108.37           C  
ANISOU 4339  C   MET A 548    13374  14125  13677    135   -178      3       C  
ATOM   4340  O   MET A 548      22.444 -17.536  26.959  1.00 93.44           O  
ANISOU 4340  O   MET A 548    11495  12218  11789    137   -172      0       O  
ATOM   4341  CB  MET A 548      24.399 -15.491  25.317  1.00122.73           C  
ANISOU 4341  CB  MET A 548    15194  15944  15493    104   -193    -26       C  
ATOM   4342  CG  MET A 548      23.145 -14.808  24.802  1.00127.00           C  
ANISOU 4342  CG  MET A 548    15753  16461  16038     92   -192    -43       C  
ATOM   4343  SD  MET A 548      22.470 -13.627  26.008  1.00128.00           S  
ANISOU 4343  SD  MET A 548    15889  16598  16147     81   -203    -54       S  
ATOM   4344  CE  MET A 548      20.854 -14.324  26.370  1.00128.11           C  
ANISOU 4344  CE  MET A 548    15917  16591  16169     93   -191    -49       C  
ATOM   4345  N   ASP A 549      24.449 -18.386  26.412  1.00112.32           N  
ANISOU 4345  N   ASP A 549    13862  14627  14186    149   -169     19       N  
ATOM   4346  CA  ASP A 549      24.000 -19.769  26.458  1.00121.90           C  
ANISOU 4346  CA  ASP A 549    15077  15825  15415    168   -151     35       C  
ATOM   4347  C   ASP A 549      23.592 -20.113  27.890  1.00124.68           C  
ANISOU 4347  C   ASP A 549    15425  16191  15755    179   -152     49       C  
ATOM   4348  O   ASP A 549      22.628 -20.851  28.109  1.00121.62           O  
ANISOU 4348  O   ASP A 549    15046  15786  15377    189   -140     55       O  
ATOM   4349  CB  ASP A 549      25.087 -20.718  25.947  1.00120.96           C  
ANISOU 4349  CB  ASP A 549    14945  15708  15308    181   -139     51       C  
ATOM   4350  CG  ASP A 549      25.296 -20.615  24.439  1.00116.92           C  
ANISOU 4350  CG  ASP A 549    14439  15177  14809    173   -133     37       C  
ATOM   4351  OD1 ASP A 549      24.861 -19.596  23.849  1.00114.54           O  
ANISOU 4351  OD1 ASP A 549    14149  14869  14504    154   -143     16       O  
ATOM   4352  OD2 ASP A 549      25.901 -21.548  23.850  1.00103.89           O1-
ANISOU 4352  OD2 ASP A 549    12784  13518  13172    185   -118     48       O1-
ATOM   4353  N   ASP A 550      24.303 -19.542  28.860  1.00113.25           N  
ANISOU 4353  N   ASP A 550    13967  14775  14288    177   -166     54       N  
ATOM   4354  CA  ASP A 550      23.897 -19.641  30.249  1.00115.75           C  
ANISOU 4354  CA  ASP A 550    14283  15108  14588    185   -169     65       C  
ATOM   4355  C   ASP A 550      22.458 -19.184  30.496  1.00116.92           C  
ANISOU 4355  C   ASP A 550    14451  15238  14735    178   -168     51       C  
ATOM   4356  O   ASP A 550      21.735 -19.821  31.252  1.00 93.91           O  
ANISOU 4356  O   ASP A 550    11541  12321  11821    192   -160     63       O  
ATOM   4357  CB  ASP A 550      24.811 -18.815  31.137  1.00124.89           C  
ANISOU 4357  CB  ASP A 550    15430  16303  15720    176   -188     65       C  
ATOM   4358  CG  ASP A 550      24.311 -18.762  32.572  1.00135.29           C  
ANISOU 4358  CG  ASP A 550    16750  17637  17017    181   -193     73       C  
ATOM   4359  OD1 ASP A 550      24.640 -19.692  33.350  1.00156.05           O  
ANISOU 4359  OD1 ASP A 550    19366  20282  19642    200   -188     98       O  
ATOM   4360  OD2 ASP A 550      23.568 -17.807  32.911  1.00118.27           O1-
ANISOU 4360  OD2 ASP A 550    14610  15478  14849    168   -199     54       O1-
ATOM   4361  N   PHE A 551      22.051 -18.064  29.896  1.00141.16           N  
ANISOU 4361  N   PHE A 551    17533  18298  17803    159   -176     27       N  
ATOM   4362  CA  PHE A 551      20.675 -17.572  30.081  1.00144.13           C  
ANISOU 4362  CA  PHE A 551    17927  18656  18179    153   -173     15       C  
ATOM   4363  C   PHE A 551      19.719 -18.502  29.369  1.00124.40           C  
ANISOU 4363  C   PHE A 551    15436  16127  15705    161   -158     20       C  
ATOM   4364  O   PHE A 551      18.730 -18.930  29.950  1.00106.36           O  
ANISOU 4364  O   PHE A 551    13157  13833  13423    170   -149     27       O  
ATOM   4365  CB  PHE A 551      20.474 -16.121  29.590  1.00152.40           C  
ANISOU 4365  CB  PHE A 551    18986  19699  19222    131   -183     -9       C  
ATOM   4366  CG  PHE A 551      21.082 -15.069  30.496  1.00158.96           C  
ANISOU 4366  CG  PHE A 551    19815  20556  20027    120   -198    -17       C  
ATOM   4367  CD1 PHE A 551      20.738 -14.997  31.843  1.00168.09           C  
ANISOU 4367  CD1 PHE A 551    20975  21727  21164    126   -199    -12       C  
ATOM   4368  CD2 PHE A 551      21.993 -14.142  29.999  1.00159.17           C  
ANISOU 4368  CD2 PHE A 551    19836  20593  20048    104   -209    -31       C  
ATOM   4369  CE1 PHE A 551      21.295 -14.032  32.677  1.00168.03           C  
ANISOU 4369  CE1 PHE A 551    20967  21744  21131    114   -213    -22       C  
ATOM   4370  CE2 PHE A 551      22.550 -13.175  30.829  1.00162.41           C  
ANISOU 4370  CE2 PHE A 551    20246  21027  20436     91   -223    -40       C  
ATOM   4371  CZ  PHE A 551      22.204 -13.121  32.169  1.00162.71           C  
ANISOU 4371  CZ  PHE A 551    20289  21079  20454     95   -225    -36       C  
ATOM   4372  N   ALA A 552      20.032 -18.822  28.117  1.00118.76           N  
ANISOU 4372  N   ALA A 552    14719  15396  15006    158   -153     15       N  
ATOM   4373  CA  ALA A 552      19.224 -19.739  27.339  1.00125.82           C  
ANISOU 4373  CA  ALA A 552    15622  16263  15923    163   -139     17       C  
ATOM   4374  C   ALA A 552      19.007 -21.040  28.099  1.00131.25           C  
ANISOU 4374  C   ALA A 552    16303  16947  16617    184   -126     39       C  
ATOM   4375  O   ALA A 552      17.885 -21.524  28.176  1.00144.20           O  
ANISOU 4375  O   ALA A 552    17953  18569  18269    187   -117     42       O  
ATOM   4376  CB  ALA A 552      19.882 -20.013  26.001  1.00128.66           C  
ANISOU 4376  CB  ALA A 552    15978  16611  16294    158   -136     11       C  
ATOM   4377  N   ALA A 553      20.074 -21.582  28.678  1.00124.71           N  
ANISOU 4377  N   ALA A 553    15461  16140  15783    197   -125     56       N  
ATOM   4378  CA  ALA A 553      20.013 -22.882  29.337  1.00119.30           C  
ANISOU 4378  CA  ALA A 553    14769  15454  15107    219   -110     80       C  
ATOM   4379  C   ALA A 553      19.175 -22.809  30.592  1.00103.08           C  
ANISOU 4379  C   ALA A 553    12717  13406  13041    225   -111     88       C  
ATOM   4380  O   ALA A 553      18.164 -23.490  30.717  1.00 89.43           O  
ANISOU 4380  O   ALA A 553    10995  11657  11326    233    -99     95       O  
ATOM   4381  CB  ALA A 553      21.416 -23.364  29.672  1.00130.42           C  
ANISOU 4381  CB  ALA A 553    16158  16885  16509    231   -109     98       C  
ATOM   4382  N   PHE A 554      19.598 -21.949  31.506  1.00103.60           N  
ANISOU 4382  N   PHE A 554    12779  13501  13082    222   -125     87       N  
ATOM   4383  CA  PHE A 554      18.950 -21.816  32.803  1.00117.40           C  
ANISOU 4383  CA  PHE A 554    14530  15261  14814    229   -125     95       C  
ATOM   4384  C   PHE A 554      17.451 -21.547  32.649  1.00123.81           C  
ANISOU 4384  C   PHE A 554    15359  16047  15636    223   -120     85       C  
ATOM   4385  O   PHE A 554      16.664 -21.995  33.478  1.00119.39           O  
ANISOU 4385  O   PHE A 554    14802  15484  15076    235   -111     98       O  
ATOM   4386  CB  PHE A 554      19.651 -20.729  33.638  1.00125.51           C  
ANISOU 4386  CB  PHE A 554    15555  16322  15811    219   -143     89       C  
ATOM   4387  CG  PHE A 554      18.726 -19.687  34.186  1.00136.16           C  
ANISOU 4387  CG  PHE A 554    16920  17670  17145    209   -149     73       C  
ATOM   4388  CD1 PHE A 554      18.153 -19.828  35.441  1.00147.47           C  
ANISOU 4388  CD1 PHE A 554    18356  19113  18563    220   -145     85       C  
ATOM   4389  CD2 PHE A 554      18.437 -18.553  33.449  1.00145.00           C  
ANISOU 4389  CD2 PHE A 554    18051  18778  18266    188   -156     48       C  
ATOM   4390  CE1 PHE A 554      17.294 -18.857  35.939  1.00166.86           C  
ANISOU 4390  CE1 PHE A 554    20828  21566  21006    211   -147     70       C  
ATOM   4391  CE2 PHE A 554      17.589 -17.579  33.945  1.00165.63           C  
ANISOU 4391  CE2 PHE A 554    20678  21387  20866    180   -158     35       C  
ATOM   4392  CZ  PHE A 554      17.009 -17.732  35.189  1.00174.56           C  
ANISOU 4392  CZ  PHE A 554    21814  22527  21984    191   -153     45       C  
ATOM   4393  N   VAL A 555      17.072 -20.825  31.590  1.00131.80           N  
ANISOU 4393  N   VAL A 555    16381  17041  16656    205   -124     63       N  
ATOM   4394  CA  VAL A 555      15.663 -20.598  31.234  1.00127.20           C  
ANISOU 4394  CA  VAL A 555    15812  16433  16086    198   -119     55       C  
ATOM   4395  C   VAL A 555      14.948 -21.897  30.962  1.00134.26           C  
ANISOU 4395  C   VAL A 555    16705  17302  17004    210   -103     69       C  
ATOM   4396  O   VAL A 555      13.825 -22.104  31.427  1.00135.85           O  
ANISOU 4396  O   VAL A 555    16913  17492  17213    215    -95     76       O  
ATOM   4397  CB  VAL A 555      15.524 -19.755  29.948  1.00125.45           C  
ANISOU 4397  CB  VAL A 555    15598  16196  15872    178   -126     33       C  
ATOM   4398  CG1 VAL A 555      14.201 -20.022  29.243  1.00110.75           C  
ANISOU 4398  CG1 VAL A 555    13745  14305  14031    173   -118     30       C  
ATOM   4399  CG2 VAL A 555      15.655 -18.281  30.263  1.00143.82           C  
ANISOU 4399  CG2 VAL A 555    17930  18537  18179    164   -139     17       C  
ATOM   4400  N   GLU A 556      15.598 -22.752  30.175  1.00141.62           N  
ANISOU 4400  N   GLU A 556    17632  18226  17951    213    -97     73       N  
ATOM   4401  CA  GLU A 556      15.025 -24.036  29.784  1.00139.78           C  
ANISOU 4401  CA  GLU A 556    17400  17968  17743    222    -81     83       C  
ATOM   4402  C   GLU A 556      14.950 -24.951  31.002  1.00120.82           C  
ANISOU 4402  C   GLU A 556    14991  15574  15342    244    -69    109       C  
ATOM   4403  O   GLU A 556      13.954 -25.637  31.214  1.00107.26           O  
ANISOU 4403  O   GLU A 556    13277  13838  13640    251    -57    119       O  
ATOM   4404  CB  GLU A 556      15.846 -24.698  28.665  1.00147.83           C  
ANISOU 4404  CB  GLU A 556    18416  18976  18775    221    -75     80       C  
ATOM   4405  CG  GLU A 556      16.089 -23.849  27.416  1.00157.53           C  
ANISOU 4405  CG  GLU A 556    19652  20201  20003    200    -86     57       C  
ATOM   4406  CD  GLU A 556      14.846 -23.155  26.874  1.00153.54           C  
ANISOU 4406  CD  GLU A 556    19158  19678  19502    183    -91     41       C  
ATOM   4407  OE1 GLU A 556      13.828 -23.828  26.639  1.00163.17           O  
ANISOU 4407  OE1 GLU A 556    20384  20876  20739    183    -82     45       O  
ATOM   4408  N   LYS A 557      15.998 -24.940  31.815  1.00110.03           N  
ANISOU 4408  N   LYS A 557    13612  14236  13957    255    -73    121       N  
ATOM   4409  CA  LYS A 557      16.012 -25.754  33.016  1.00110.89           C  
ANISOU 4409  CA  LYS A 557    13713  14357  14063    277    -63    147       C  
ATOM   4410  C   LYS A 557      14.927 -25.297  33.977  1.00106.13           C  
ANISOU 4410  C   LYS A 557    13118  13757  13450    279    -64    150       C  
ATOM   4411  O   LYS A 557      14.169 -26.097  34.474  1.00112.61           O  
ANISOU 4411  O   LYS A 557    13938  14566  14283    292    -50    166       O  
ATOM   4412  CB  LYS A 557      17.391 -25.721  33.681  1.00112.17           C  
ANISOU 4412  CB  LYS A 557    13860  14554  14206    287    -70    160       C  
ATOM   4413  CG  LYS A 557      17.590 -26.780  34.763  1.00114.00           C  
ANISOU 4413  CG  LYS A 557    14079  14798  14438    312    -57    192       C  
ATOM   4414  CD  LYS A 557      17.576 -26.199  36.172  1.00124.49           C  
ANISOU 4414  CD  LYS A 557    15405  16159  15736    317    -67    200       C  
ATOM   4415  CE  LYS A 557      18.957 -25.726  36.623  1.00134.22           C  
ANISOU 4415  CE  LYS A 557    16624  17431  16943    316    -83    205       C  
ATOM   4416  NZ  LYS A 557      19.375 -24.412  36.037  1.00144.42           N1+
ANISOU 4416  NZ  LYS A 557    17922  18730  18221    291   -102    176       N1+
ATOM   4417  N   CYS A 558      14.837 -24.004  34.217  1.00110.22           N  
ANISOU 4417  N   CYS A 558    13643  14289  13947    265    -78    133       N  
ATOM   4418  CA  CYS A 558      13.890 -23.481  35.202  1.00121.57           C  
ANISOU 4418  CA  CYS A 558    15089  15731  15372    268    -78    135       C  
ATOM   4419  C   CYS A 558      12.422 -23.638  34.824  1.00117.63           C  
ANISOU 4419  C   CYS A 558    14599  15201  14894    264    -67    133       C  
ATOM   4420  O   CYS A 558      11.565 -23.750  35.711  1.00119.06           O  
ANISOU 4420  O   CYS A 558    14784  15381  15074    275    -59    145       O  
ATOM   4421  CB  CYS A 558      14.191 -22.009  35.519  1.00143.34           C  
ANISOU 4421  CB  CYS A 558    17853  18509  18102    253    -94    115       C  
ATOM   4422  SG  CYS A 558      15.521 -21.805  36.728  1.00154.67           S  
ANISOU 4422  SG  CYS A 558    19277  19989  19502    260   -106    125       S  
ATOM   4423  N   CYS A 559      12.123 -23.650  33.527  1.00118.43           N  
ANISOU 4423  N   CYS A 559    14704  15278  15016    250    -68    119       N  
ATOM   4424  CA  CYS A 559      10.746 -23.869  33.081  1.00125.29           C  
ANISOU 4424  CA  CYS A 559    15579  16117  15906    246    -60    119       C  
ATOM   4425  C   CYS A 559      10.281 -25.296  33.348  1.00127.32           C  
ANISOU 4425  C   CYS A 559    15832  16359  16186    262    -43    141       C  
ATOM   4426  O   CYS A 559       9.107 -25.503  33.627  1.00116.18           O  
ANISOU 4426  O   CYS A 559    14423  14932  14787    264    -34    149       O  
ATOM   4427  CB  CYS A 559      10.566 -23.522  31.606  1.00130.58           C  
ANISOU 4427  CB  CYS A 559    16256  16769  16591    225    -67     99       C  
ATOM   4428  SG  CYS A 559      10.279 -21.765  31.282  1.00149.71           S  
ANISOU 4428  SG  CYS A 559    18688  19196  18998    205    -81     76       S  
ATOM   4429  N   LYS A 560      11.200 -26.262  33.254  1.00146.69           N  
ANISOU 4429  N   LYS A 560    18276  18814  18644    272    -36    151       N  
ATOM   4430  CA  LYS A 560      10.966 -27.650  33.698  1.00154.15           C  
ANISOU 4430  CA  LYS A 560    19213  19747  19608    291    -18    176       C  
ATOM   4431  C   LYS A 560      11.678 -27.916  35.033  1.00175.43           C  
ANISOU 4431  C   LYS A 560    21899  22471  22284    313    -14    198       C  
ATOM   4432  O   LYS A 560      12.623 -28.703  35.091  1.00194.97           O  
ANISOU 4432  O   LYS A 560    24364  24954  24763    325     -8    211       O  
ATOM   4433  CB  LYS A 560      11.444 -28.658  32.639  1.00136.58           C  
ANISOU 4433  CB  LYS A 560    16986  17501  17406    289     -9    174       C  
ATOM   4434  N   ALA A 561      11.240 -27.237  36.095  1.00192.60           N  
ANISOU 4434  N   ALA A 561    24076  24664  24439    317    -18    202       N  
ATOM   4435  CA  ALA A 561      11.783 -27.447  37.448  1.00192.55           C  
ANISOU 4435  CA  ALA A 561    24061  24687  24410    337    -16    224       C  
ATOM   4436  C   ALA A 561      10.699 -27.743  38.488  1.00194.18           C  
ANISOU 4436  C   ALA A 561    24270  24891  24618    351     -3    242       C  
ATOM   4437  O   ALA A 561      11.016 -28.157  39.606  1.00190.45           O  
ANISOU 4437  O   ALA A 561    23790  24440  24132    371      3    265       O  
ATOM   4438  CB  ALA A 561      12.599 -26.243  37.876  1.00184.52           C  
ANISOU 4438  CB  ALA A 561    23046  23704  23359    328    -35    210       C  
ATOM   4439  N   ASP A 562       9.430 -27.568  38.096  1.00187.71           N  
ANISOU 4439  N   ASP A 562    23460  24045  23817    343      2    235       N  
ATOM   4440  CA  ASP A 562       8.255 -27.756  38.968  1.00169.84           C  
ANISOU 4440  CA  ASP A 562    21199  21774  21557    354     15    252       C  
ATOM   4441  C   ASP A 562       8.494 -27.132  40.337  1.00163.81           C  
ANISOU 4441  C   ASP A 562    20438  21045  20759    366     12    260       C  
ATOM   4442  O   ASP A 562       8.431 -27.797  41.372  1.00143.86           O  
ANISOU 4442  O   ASP A 562    17904  18528  18226    387     24    285       O  
ATOM   4443  CB  ASP A 562       7.880 -29.239  39.090  1.00170.59           C  
ANISOU 4443  CB  ASP A 562    21285  21850  21682    371     36    278       C  
ATOM   4444  CG  ASP A 562       7.376 -29.834  37.771  1.00170.39           C  
ANISOU 4444  CG  ASP A 562    21261  21788  21692    357     40    269       C  
ATOM   4445  OD1 ASP A 562       8.212 -30.404  37.036  1.00164.19           O  
ANISOU 4445  OD1 ASP A 562    20471  20996  20916    354     40    265       O  
ATOM   4446  OD2 ASP A 562       6.162 -29.729  37.462  1.00159.92           O1-
ANISOU 4446  OD2 ASP A 562    19940  20439  20384    348     44    266       O1-
ATOM   4447  N   ASP A 563       8.757 -25.832  40.321  1.00169.64           N  
ANISOU 4447  N   ASP A 563    21186  21798  21472    351     -4    237       N  
ATOM   4448  CA  ASP A 563       9.308 -25.136  41.471  1.00171.19           C  
ANISOU 4448  CA  ASP A 563    21385  22030  21630    356    -11    237       C  
ATOM   4449  C   ASP A 563       8.304 -24.147  42.036  1.00182.01           C  
ANISOU 4449  C   ASP A 563    22770  23399  22986    353     -8    228       C  
ATOM   4450  O   ASP A 563       7.165 -24.085  41.568  1.00187.34           O  
ANISOU 4450  O   ASP A 563    23450  24045  23684    348      0    226       O  
ATOM   4451  CB  ASP A 563      10.595 -24.421  41.048  1.00163.10           C  
ANISOU 4451  CB  ASP A 563    20360  21027  20585    341    -31    217       C  
ATOM   4452  CG  ASP A 563      10.407 -23.519  39.819  1.00157.22           C  
ANISOU 4452  CG  ASP A 563    19624  20263  19851    317    -41    187       C  
ATOM   4453  OD1 ASP A 563       9.414 -23.654  39.065  1.00127.69           O  
ANISOU 4453  OD1 ASP A 563    15887  16491  16137    311    -34    184       O  
ATOM   4454  OD2 ASP A 563      11.281 -22.659  39.612  1.00163.66           O1-
ANISOU 4454  OD2 ASP A 563    20440  21095  20646    303    -58    169       O1-
ATOM   4455  N   LYS A 564       8.722 -23.397  43.060  1.00181.21           N  
ANISOU 4455  N   LYS A 564    22676  23328  22848    355    -15    224       N  
ATOM   4456  CA  LYS A 564       8.021 -22.174  43.477  1.00166.03           C  
ANISOU 4456  CA  LYS A 564    20771  21405  20907    346    -14    208       C  
ATOM   4457  C   LYS A 564       8.570 -21.014  42.652  1.00165.72           C  
ANISOU 4457  C   LYS A 564    20740  21367  20861    322    -32    176       C  
ATOM   4458  O   LYS A 564       8.957 -19.987  43.214  1.00158.60           O  
ANISOU 4458  O   LYS A 564    19848  20484  19927    313    -40    160       O  
ATOM   4459  CB  LYS A 564       8.205 -21.886  44.980  1.00148.61           C  
ANISOU 4459  CB  LYS A 564    18571  19230  18662    359    -12    216       C  
ATOM   4460  CG  LYS A 564       7.554 -22.902  45.907  1.00140.78           C  
ANISOU 4460  CG  LYS A 564    17575  18239  17676    384      7    248       C  
ATOM   4461  CD  LYS A 564       6.042 -22.952  45.742  1.00130.73           C  
ANISOU 4461  CD  LYS A 564    16307  16933  16430    389     26    255       C  
ATOM   4462  CE  LYS A 564       5.499 -24.347  46.004  1.00121.81           C  
ANISOU 4462  CE  LYS A 564    15165  15791  15327    411     44    288       C  
ATOM   4463  NZ  LYS A 564       4.052 -24.466  45.681  1.00121.06           N1+
ANISOU 4463  NZ  LYS A 564    15072  15661  15262    412     60    295       N1+
ATOM   4464  N   GLU A 565       8.589 -21.193  41.322  1.00170.29           N  
ANISOU 4464  N   GLU A 565    21313  21923  21468    309    -36    167       N  
ATOM   4465  CA  GLU A 565       9.265 -20.288  40.366  1.00168.22           C  
ANISOU 4465  CA  GLU A 565    21054  21661  21202    287    -53    140       C  
ATOM   4466  C   GLU A 565      10.669 -19.930  40.856  1.00163.92           C  
ANISOU 4466  C   GLU A 565    20505  21151  20626    283    -69    133       C  
ATOM   4467  O   GLU A 565      11.223 -18.865  40.551  1.00169.32           O  
ANISOU 4467  O   GLU A 565    21195  21843  21294    265    -82    110       O  
ATOM   4468  CB  GLU A 565       8.443 -19.016  40.150  1.00175.29           C  
ANISOU 4468  CB  GLU A 565    21964  22542  22095    273    -52    120       C  
ATOM   4469  CG  GLU A 565       6.967 -19.257  39.875  1.00168.28           C  
ANISOU 4469  CG  GLU A 565    21079  21623  21235    278    -36    131       C  
ATOM   4470  CD  GLU A 565       6.222 -17.978  39.552  1.00162.17           C  
ANISOU 4470  CD  GLU A 565    20319  20836  20462    264    -35    113       C  
ATOM   4471  OE1 GLU A 565       6.787 -16.882  39.779  1.00148.74           O  
ANISOU 4471  OE1 GLU A 565    18628  19149  18737    253    -44     93       O  
ATOM   4472  OE2 GLU A 565       5.071 -18.073  39.072  1.00150.61           O1-
ANISOU 4472  OE2 GLU A 565    18855  19347  19024    264    -25    120       O1-
ATOM   4473  N   THR A 566      11.244 -20.873  41.592  1.00148.38           N  
ANISOU 4473  N   THR A 566    18526  19203  18649    300    -66    155       N  
ATOM   4474  CA  THR A 566      12.326 -20.619  42.519  1.00140.57           C  
ANISOU 4474  CA  THR A 566    17533  18253  17624    301    -78    157       C  
ATOM   4475  C   THR A 566      13.602 -20.180  41.829  1.00147.62           C  
ANISOU 4475  C   THR A 566    18418  19159  18510    285    -98    141       C  
ATOM   4476  O   THR A 566      14.094 -19.068  42.042  1.00139.22           O  
ANISOU 4476  O   THR A 566    17363  18113  17421    268   -111    120       O  
ATOM   4477  CB  THR A 566      12.613 -21.893  43.333  1.00134.17           C  
ANISOU 4477  CB  THR A 566    16708  17459  16812    326    -70    190       C  
ATOM   4478  CG2 THR A 566      13.534 -21.586  44.502  1.00135.78           C  
ANISOU 4478  CG2 THR A 566    16909  17707  16974    328    -82    194       C  
ATOM   4479  OG1 THR A 566      11.379 -22.439  43.818  1.00120.33           O  
ANISOU 4479  OG1 THR A 566    14960  15689  15072    342    -50    207       O  
ATOM   4480  N   CYS A 567      14.115 -21.059  40.978  1.00166.86           N  
ANISOU 4480  N   CYS A 567    20840  21587  20971    288    -97    150       N  
ATOM   4481  CA  CYS A 567      15.425 -20.875  40.373  1.00176.27           C  
ANISOU 4481  CA  CYS A 567    22022  22795  22159    277   -113    142       C  
ATOM   4482  C   CYS A 567      15.474 -19.708  39.391  1.00181.49           C  
ANISOU 4482  C   CYS A 567    22692  23443  22823    252   -124    111       C  
ATOM   4483  O   CYS A 567      16.554 -19.300  38.972  1.00203.80           O  
ANISOU 4483  O   CYS A 567    25510  26282  25641    240   -138    101       O  
ATOM   4484  CB  CYS A 567      15.882 -22.165  39.686  1.00173.51           C  
ANISOU 4484  CB  CYS A 567    21655  22435  21837    289   -105    161       C  
ATOM   4485  SG  CYS A 567      14.786 -22.738  38.376  1.00161.41           S  
ANISOU 4485  SG  CYS A 567    20128  20853  20347    288    -90    157       S  
ATOM   4486  N   PHE A 568      14.309 -19.187  39.021  1.00176.69           N  
ANISOU 4486  N   PHE A 568    22099  22807  22227    246   -116     98       N  
ATOM   4487  CA  PHE A 568      14.228 -17.949  38.257  1.00169.53           C  
ANISOU 4487  CA  PHE A 568    21203  21890  21320    223   -125     70       C  
ATOM   4488  C   PHE A 568      14.646 -16.776  39.144  1.00180.02           C  
ANISOU 4488  C   PHE A 568    22542  23244  22615    212   -136     55       C  
ATOM   4489  O   PHE A 568      15.498 -15.953  38.771  1.00177.71           O  
ANISOU 4489  O   PHE A 568    22249  22962  22311    194   -150     37       O  
ATOM   4490  CB  PHE A 568      12.800 -17.732  37.742  1.00150.20           C  
ANISOU 4490  CB  PHE A 568    18766  19407  18894    221   -112     65       C  
ATOM   4491  CG  PHE A 568      12.508 -18.422  36.435  1.00129.66           C  
ANISOU 4491  CG  PHE A 568    16159  16779  16326    220   -108     68       C  
ATOM   4492  CD1 PHE A 568      13.265 -18.142  35.302  1.00120.66           C  
ANISOU 4492  CD1 PHE A 568    15015  15637  15195    205   -118     54       C  
ATOM   4493  CD2 PHE A 568      11.463 -19.334  36.333  1.00126.79           C  
ANISOU 4493  CD2 PHE A 568    15795  16393  15986    231    -93     84       C  
ATOM   4494  CE1 PHE A 568      12.991 -18.770  34.102  1.00123.28           C  
ANISOU 4494  CE1 PHE A 568    15344  15945  15554    203   -114     55       C  
ATOM   4495  CE2 PHE A 568      11.183 -19.962  35.133  1.00128.79           C  
ANISOU 4495  CE2 PHE A 568    16044  16622  16269    227    -89     84       C  
ATOM   4496  CZ  PHE A 568      11.947 -19.679  34.017  1.00131.23           C  
ANISOU 4496  CZ  PHE A 568    16350  16929  16582    213   -100     69       C  
ATOM   4497  N   ALA A 569      14.046 -16.723  40.329  1.00178.16           N  
ANISOU 4497  N   ALA A 569    22316  23017  22361    222   -128     62       N  
ATOM   4498  CA  ALA A 569      14.320 -15.666  41.286  1.00186.89           C  
ANISOU 4498  CA  ALA A 569    23433  24145  23431    212   -136     47       C  
ATOM   4499  C   ALA A 569      15.627 -15.932  42.034  1.00180.25           C  
ANISOU 4499  C   ALA A 569    22580  23344  22562    213   -151     55       C  
ATOM   4500  O   ALA A 569      16.552 -15.108  42.022  1.00159.80           O  
ANISOU 4500  O   ALA A 569    19990  20774  19954    195   -167     38       O  
ATOM   4501  CB  ALA A 569      13.160 -15.553  42.266  1.00191.92           C  
ANISOU 4501  CB  ALA A 569    24086  24776  24058    224   -119     52       C  
ATOM   4502  N   GLU A 570      15.694 -17.101  42.665  1.00180.15           N  
ANISOU 4502  N   GLU A 570    22555  23345  22548    235   -144     83       N  
ATOM   4503  CA  GLU A 570      16.787 -17.439  43.573  1.00183.36           C  
ANISOU 4503  CA  GLU A 570    22949  23793  22927    240   -157     98       C  
ATOM   4504  C   GLU A 570      18.128 -17.523  42.866  1.00180.44           C  
ANISOU 4504  C   GLU A 570    22561  23438  22561    230   -173     97       C  
ATOM   4505  O   GLU A 570      19.093 -16.863  43.267  1.00173.21           O  
ANISOU 4505  O   GLU A 570    21642  22552  21618    215   -192     87       O  
ATOM   4506  CB  GLU A 570      16.496 -18.753  44.314  1.00178.25           C  
ANISOU 4506  CB  GLU A 570    22291  23153  22282    268   -143    132       C  
ATOM   4507  CG  GLU A 570      15.480 -18.608  45.441  1.00185.84           C  
ANISOU 4507  CG  GLU A 570    23269  24116  23226    279   -131    136       C  
ATOM   4508  CD  GLU A 570      16.015 -17.850  46.649  1.00184.11           C  
ANISOU 4508  CD  GLU A 570    23058  23936  22959    270   -143    128       C  
ATOM   4509  OE1 GLU A 570      15.675 -16.659  46.817  1.00172.98           O  
ANISOU 4509  OE1 GLU A 570    21671  22522  21533    253   -146    100       O  
ATOM   4510  OE2 GLU A 570      16.784 -18.440  47.429  1.00194.73           O1-
ANISOU 4510  OE2 GLU A 570    24390  25317  24283    280   -151    149       O1-
ATOM   4511  N   GLU A 571      18.178 -18.306  41.798  1.00177.95           N  
ANISOU 4511  N   GLU A 571    22233  23100  22280    237   -167    106       N  
ATOM   4512  CA  GLU A 571      19.416 -18.481  41.054  1.00191.84           C  
ANISOU 4512  CA  GLU A 571    23973  24869  24046    230   -179    108       C  
ATOM   4513  C   GLU A 571      19.575 -17.366  40.019  1.00195.64           C  
ANISOU 4513  C   GLU A 571    24463  25335  24534    205   -188     77       C  
ATOM   4514  O   GLU A 571      20.557 -17.339  39.284  1.00209.37           O  
ANISOU 4514  O   GLU A 571    26189  27080  26281    197   -198     75       O  
ATOM   4515  CB  GLU A 571      19.501 -19.861  40.383  1.00198.51           C  
ANISOU 4515  CB  GLU A 571    24803  25699  24924    249   -165    132       C  
ATOM   4516  CG  GLU A 571      18.788 -20.999  41.102  1.00203.93           C  
ANISOU 4516  CG  GLU A 571    25486  26380  25616    275   -147    160       C  
ATOM   4517  CD  GLU A 571      19.255 -21.247  42.518  1.00211.86           C  
ANISOU 4517  CD  GLU A 571    26482  27424  26589    287   -152    180       C  
ATOM   4518  OE1 GLU A 571      20.468 -21.417  42.706  1.00225.06           O  
ANISOU 4518  OE1 GLU A 571    28137  29127  28249    287   -165    192       O  
ATOM   4519  OE2 GLU A 571      18.400 -21.317  43.430  1.00205.53           O1-
ANISOU 4519  OE2 GLU A 571    25691  26624  25776    297   -143    187       O1-
ATOM   4520  N   GLY A 572      18.595 -16.464  39.960  1.00183.34           N  
ANISOU 4520  N   GLY A 572    22927  23758  22977    194   -183     56       N  
ATOM   4521  CA  GLY A 572      18.737 -15.209  39.245  1.00184.71           C  
ANISOU 4521  CA  GLY A 572    23110  23921  23150    170   -192     27       C  
ATOM   4522  C   GLY A 572      19.812 -14.379  39.919  1.00192.24           C  
ANISOU 4522  C   GLY A 572    24062  24909  24071    153   -212     15       C  
ATOM   4523  O   GLY A 572      20.633 -13.757  39.245  1.00196.86           O  
ANISOU 4523  O   GLY A 572    24641  25498  24657    136   -225      1       O  
ATOM   4524  N   LYS A 573      19.818 -14.393  41.253  1.00183.17           N  
ANISOU 4524  N   LYS A 573    22917  23787  22892    159   -215     22       N  
ATOM   4525  CA  LYS A 573      20.863 -13.728  42.041  1.00171.62           C  
ANISOU 4525  CA  LYS A 573    21452  22363  21394    143   -235     14       C  
ATOM   4526  C   LYS A 573      22.263 -14.326  41.793  1.00177.48           C  
ANISOU 4526  C   LYS A 573    22165  23132  22137    144   -250     31       C  
ATOM   4527  O   LYS A 573      23.258 -13.591  41.791  1.00179.31           O  
ANISOU 4527  O   LYS A 573    22392  23386  22354    123   -268     19       O  
ATOM   4528  CB  LYS A 573      20.525 -13.769  43.535  1.00159.92           C  
ANISOU 4528  CB  LYS A 573    19980  20905  19878    151   -233     20       C  
ATOM   4529  CG  LYS A 573      21.549 -13.094  44.447  1.00148.68           C  
ANISOU 4529  CG  LYS A 573    18554  19523  18414    132   -255     11       C  
ATOM   4530  CD  LYS A 573      21.642 -11.585  44.256  1.00136.42           C  
ANISOU 4530  CD  LYS A 573    17020  17964  16850    102   -264    -26       C  
ATOM   4531  CE  LYS A 573      22.872 -11.034  44.960  1.00126.57           C  
ANISOU 4531  CE  LYS A 573    15765  16759  15567     81   -289    -34       C  
ATOM   4532  NZ  LYS A 573      22.807  -9.564  45.158  1.00120.02           N1+
ANISOU 4532  NZ  LYS A 573    14959  15924  14717     52   -295    -71       N1+
ATOM   4533  N   LYS A 574      22.328 -15.647  41.584  1.00171.87           N  
ANISOU 4533  N   LYS A 574    21438  22419  21446    167   -240     61       N  
ATOM   4534  CA  LYS A 574      23.581 -16.351  41.270  1.00164.58           C  
ANISOU 4534  CA  LYS A 574    20487  21517  20529    172   -249     82       C  
ATOM   4535  C   LYS A 574      24.209 -15.831  39.978  1.00165.61           C  
ANISOU 4535  C   LYS A 574    20611  21633  20679    156   -256     66       C  
ATOM   4536  O   LYS A 574      25.405 -15.540  39.930  1.00166.92           O  
ANISOU 4536  O   LYS A 574    20761  21825  20835    144   -272     67       O  
ATOM   4537  CB  LYS A 574      23.341 -17.859  41.101  1.00162.72           C  
ANISOU 4537  CB  LYS A 574    20237  21270  20318    202   -231    114       C  
ATOM   4538  CG  LYS A 574      22.602 -18.559  42.242  1.00165.07           C  
ANISOU 4538  CG  LYS A 574    20540  21576  20604    223   -219    134       C  
ATOM   4539  CD  LYS A 574      23.548 -19.088  43.321  1.00168.27           C  
ANISOU 4539  CD  LYS A 574    20925  22028  20983    233   -230    161       C  
ATOM   4540  CE  LYS A 574      22.992 -20.344  44.023  1.00156.04           C  
ANISOU 4540  CE  LYS A 574    19370  20478  19439    264   -212    194       C  
ATOM   4541  NZ  LYS A 574      23.861 -20.998  45.054  1.00143.55           N1+
ANISOU 4541  NZ  LYS A 574    17766  18942  17835    277   -219    227       N1+
ATOM   4542  N   LEU A 575      23.387 -15.727  38.933  1.00172.74           N  
ANISOU 4542  N   LEU A 575    21527  22496  21611    155   -242     52       N  
ATOM   4543  CA  LEU A 575      23.850 -15.351  37.595  1.00181.14           C  
ANISOU 4543  CA  LEU A 575    22586  23542  22695    142   -245     39       C  
ATOM   4544  C   LEU A 575      24.094 -13.839  37.445  1.00191.75           C  
ANISOU 4544  C   LEU A 575    23941  24889  24026    113   -259      8       C  
ATOM   4545  O   LEU A 575      24.955 -13.439  36.668  1.00196.73           O  
ANISOU 4545  O   LEU A 575    24562  25522  24665    100   -269      2       O  
ATOM   4546  CB  LEU A 575      22.874 -15.852  36.516  1.00175.14           C  
ANISOU 4546  CB  LEU A 575    21835  22740  21969    151   -226     38       C  
ATOM   4547  CG  LEU A 575      22.394 -17.318  36.598  1.00171.80           C  
ANISOU 4547  CG  LEU A 575    21406  22307  21564    178   -209     64       C  
ATOM   4548  CD1 LEU A 575      21.528 -17.664  35.391  1.00171.02           C  
ANISOU 4548  CD1 LEU A 575    21316  22167  21497    181   -193     58       C  
ATOM   4549  CD2 LEU A 575      23.531 -18.326  36.760  1.00157.73           C  
ANISOU 4549  CD2 LEU A 575    19599  20547  19783    193   -210     92       C  
ATOM   4550  N   VAL A 576      23.353 -13.001  38.173  1.00185.69           N  
ANISOU 4550  N   VAL A 576    23195  24120  23240    104   -260     -9       N  
ATOM   4551  CA  VAL A 576      23.619 -11.547  38.176  1.00175.45           C  
ANISOU 4551  CA  VAL A 576    21909  22826  21928     76   -272    -39       C  
ATOM   4552  C   VAL A 576      24.964 -11.218  38.854  1.00170.49           C  
ANISOU 4552  C   VAL A 576    21267  22240  21273     62   -294    -37       C  
ATOM   4553  O   VAL A 576      25.646 -10.281  38.456  1.00144.61           O  
ANISOU 4553  O   VAL A 576    17987  18966  17992     39   -307    -55       O  
ATOM   4554  CB  VAL A 576      22.461 -10.713  38.795  1.00175.34           C  
ANISOU 4554  CB  VAL A 576    21923  22797  21901     70   -263    -59       C  
ATOM   4555  CG1 VAL A 576      21.179 -10.883  37.981  1.00179.03           C  
ANISOU 4555  CG1 VAL A 576    22403  23223  22398     80   -243    -60       C  
ATOM   4556  CG2 VAL A 576      22.241 -11.035  40.266  1.00169.19           C  
ANISOU 4556  CG2 VAL A 576    21150  22043  21092     80   -263    -48       C  
ATOM   4557  N   ALA A 577      25.344 -12.008  39.859  1.00169.77           N  
ANISOU 4557  N   ALA A 577    21162  22179  21161     75   -299    -14       N  
ATOM   4558  CA  ALA A 577      26.652 -11.874  40.512  1.00158.49           C  
ANISOU 4558  CA  ALA A 577    19715  20795  19708     63   -322     -7       C  
ATOM   4559  C   ALA A 577      27.768 -12.546  39.693  1.00160.11           C  
ANISOU 4559  C   ALA A 577    19892  21010  19934     69   -327     14       C  
ATOM   4560  O   ALA A 577      28.859 -11.998  39.554  1.00145.43           O  
ANISOU 4560  O   ALA A 577    18018  19172  18068     50   -345      9       O  
ATOM   4561  CB  ALA A 577      26.600 -12.449  41.923  1.00147.25           C  
ANISOU 4561  CB  ALA A 577    18289  19403  18254     76   -325     11       C  
ATOM   4562  N   ALA A 578      27.489 -13.727  39.145  1.00168.79           N  
ANISOU 4562  N   ALA A 578    20981  22092  21059     95   -310     37       N  
ATOM   4563  CA  ALA A 578      28.477 -14.476  38.353  1.00165.47           C  
ANISOU 4563  CA  ALA A 578    20535  21676  20661    104   -310     58       C  
ATOM   4564  C   ALA A 578      28.719 -13.882  36.965  1.00161.54           C  
ANISOU 4564  C   ALA A 578    20038  21153  20187     90   -309     40       C  
ATOM   4565  O   ALA A 578      29.771 -14.137  36.366  1.00144.23           O  
ANISOU 4565  O   ALA A 578    17823  18971  18006     90   -313     53       O  
ATOM   4566  CB  ALA A 578      28.060 -15.936  38.225  1.00161.48           C  
ANISOU 4566  CB  ALA A 578    20021  21157  20175    136   -289     87       C  
ATOM   4567  N   SER A 579      27.753 -13.106  36.457  1.00155.63           N  
ANISOU 4567  N   SER A 579    19313  20372  19446     79   -301     13       N  
ATOM   4568  CA  SER A 579      27.880 -12.456  35.140  1.00147.56           C  
ANISOU 4568  CA  SER A 579    18294  19325  18446     66   -300     -5       C  
ATOM   4569  C   SER A 579      28.739 -11.198  35.216  1.00142.86           C  
ANISOU 4569  C   SER A 579    17696  18748  17835     37   -319    -24       C  
ATOM   4570  O   SER A 579      29.576 -10.979  34.339  1.00142.30           O  
ANISOU 4570  O   SER A 579    17612  18678  17779     28   -324    -24       O  
ATOM   4571  CB  SER A 579      26.512 -12.143  34.502  1.00138.67           C  
ANISOU 4571  CB  SER A 579    17193  18158  17336     66   -284    -23       C  
ATOM   4572  OG  SER A 579      25.679 -11.377  35.355  1.00131.55           O  
ANISOU 4572  OG  SER A 579    16313  17255  16415     57   -285    -41       O  
ATOM   4573  N   GLN A 580      28.560 -10.389  36.260  1.00136.42           N  
ANISOU 4573  N   GLN A 580    16893  17948  16991     21   -330    -40       N  
ATOM   4574  CA  GLN A 580      29.405  -9.205  36.452  1.00142.55           C  
ANISOU 4574  CA  GLN A 580    17667  18744  17752     -8   -350    -58       C  
ATOM   4575  C   GLN A 580      30.901  -9.572  36.579  1.00140.94           C  
ANISOU 4575  C   GLN A 580    17431  18578  17542    -11   -367    -37       C  
ATOM   4576  O   GLN A 580      31.775  -8.747  36.299  1.00131.64           O  
ANISOU 4576  O   GLN A 580    16244  17410  16361    -34   -382    -48       O  
ATOM   4577  CB  GLN A 580      28.927  -8.352  37.643  1.00138.14           C  
ANISOU 4577  CB  GLN A 580    17130  18196  17161    -24   -357    -79       C  
ATOM   4578  CG  GLN A 580      29.044  -6.849  37.430  1.00136.58           C  
ANISOU 4578  CG  GLN A 580    16946  17989  16958    -55   -365   -112       C  
ATOM   4579  CD  GLN A 580      30.147  -6.180  38.234  1.00132.29           C  
ANISOU 4579  CD  GLN A 580    16394  17484  16387    -81   -390   -120       C  
ATOM   4580  NE2 GLN A 580      31.411  -6.373  37.833  1.00131.04           N  
ANISOU 4580  NE2 GLN A 580    16206  17348  16234    -88   -404   -105       N  
ATOM   4581  OE1 GLN A 580      29.855  -5.464  39.191  1.00127.59           O  
ANISOU 4581  OE1 GLN A 580    15818  16897  15764    -97   -395   -139       O  
ATOM   4582  N   ALA A 581      31.183 -10.808  36.993  1.00144.72           N  
ANISOU 4582  N   ALA A 581    17892  19076  18020     12   -365     -5       N  
ATOM   4583  CA  ALA A 581      32.510 -11.396  36.821  1.00138.25           C  
ANISOU 4583  CA  ALA A 581    17040  18284  17205     17   -374     22       C  
ATOM   4584  C   ALA A 581      32.715 -11.703  35.333  1.00146.35           C  
ANISOU 4584  C   ALA A 581    18058  19282  18267     25   -360     26       C  
ATOM   4585  O   ALA A 581      33.484 -11.013  34.663  1.00148.25           O  
ANISOU 4585  O   ALA A 581    18289  19524  18515      8   -369     17       O  
ATOM   4586  CB  ALA A 581      32.669 -12.657  37.667  1.00128.16           C  
ANISOU 4586  CB  ALA A 581    15746  17032  15918     43   -372     56       C  
ATOM   4587  N   ALA A 582      31.989 -12.709  34.826  1.00155.09           N  
ANISOU 4587  N   ALA A 582    19171  20362  19396     51   -338     38       N  
ATOM   4588  CA  ALA A 582      32.108 -13.196  33.434  1.00145.65           C  
ANISOU 4588  CA  ALA A 582    17970  19139  18233     62   -322     43       C  
ATOM   4589  C   ALA A 582      31.579 -12.200  32.401  1.00138.62           C  
ANISOU 4589  C   ALA A 582    17098  18215  17355     45   -318     13       C  
ATOM   4590  O   ALA A 582      32.339 -11.456  31.781  1.00144.69           O  
ANISOU 4590  O   ALA A 582    17859  18988  18130     28   -327      4       O  
ATOM   4591  CB  ALA A 582      31.383 -14.532  33.283  1.00139.01           C  
ANISOU 4591  CB  ALA A 582    17132  18277  17408     92   -300     62       C  
TER   
END



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