CNRS Nantes University UFIP UFIP
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***  comp  ***

elNémo ID: 19090320400333965

Job options:

ID        	=	 19090320400333965
JOBID     	=	 comp
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER comp

HELIX    1   1 HIS A  349  ASN A  361  1                                  13
HELIX    2   2 THR A  374  ASN A  383  1                                  10
HELIX    3   3 GLY A  393  LYS A  401  1                                   9
HELIX    4   4 CYS A  418  ASP A  420  1                                   3
HELIX    5   5 TRP A  441  ASN A  443  1                                   3
HELIX    6   6 THR A  457  LEU A  466  1                                  10
HELIX    7   7 TYR A  468  LYS A  470  1                                   3
HELIX    8   8 PHE A  476  GLU A  478  1                                   3
HELIX    9   9 SER A  493  CYS A  495  1                                   3
HELIX   10  10 GLY A  502  ASN A  504  1                                   3
HELIX   11  11 GLY A  516  GLU A  526  1                                  11
HELIX   12  12 THR A  537  ASN A  541  1                                   5
HELIX   13  13 GLU A  556  ASP A  558  1                                   3
HELIX   14  14 VAL A  571  ASN A  576  1                                   6
HELIX   15  15 LYS A  591  PHE A  608  1                                  18
HELIX   16  16 TYR A  647  TYR A  650  1                                   4
HELIX   17  17 GLU A  653  CYS A  665  1                                  13
HELIX   18  18 SER A  669  THR A  675  1                                   7
SHEET    1   1 1 VAL A 342  ALA A 346  0
SHEET    2   2 1 ILE A 366  SER A 370  0
SHEET    3   3 1 ALA A 388  LEU A 391  0
SHEET    4   4 1 VAL A 405  ASN A 411  0
SHEET    5   5 1 TYR A 426  LYS A 433  0
SHEET    6   6 1 LYS A 448  HIS A 451  0
SHEET    7   7 1 GLU A 482  CYS A 484  0
SHEET    8   8 1 VAL A 530  LYS A 534  0
SHEET    9   9 1 TYR A 559  LEU A 562  0
SHEET   10  10 1 ARG A 568  PRO A 570  0
SHEET   11  11 1 ALA A 580  ALA A 582  0
SHEET   12  12 1 ALA A 586  THR A 589  0
SHEET   13  13 1 CYS A 637  LYS A 640  0
ATOM      1  N   CYS A 339      13.745 -19.651  -3.258  1.00 39.36           N
ANISOU    1  N   CYS A 339     4731   5497   4728   -272    -27     47       N
ATOM      2  CA  CYS A 339      12.959 -19.577  -4.491  1.00 43.16           C
ANISOU    2  CA  CYS A 339     5245   5881   5275   -260    -14     47       C
ATOM      3  C   CYS A 339      13.815 -19.742  -5.751  1.00 43.60           C
ANISOU    3  C   CYS A 339     5299   5905   5361   -242    -24     57       C
ATOM      4  O   CYS A 339      13.568 -20.624  -6.576  1.00 36.18           O
ANISOU    4  O   CYS A 339     4375   4917   4454   -209    -29     94       O
ATOM      5  CB  CYS A 339      12.179 -18.261  -4.560  1.00 47.35           C
ANISOU    5  CB  CYS A 339     5790   6372   5829   -295     13    -12       C
ATOM      6  SG  CYS A 339      11.172 -18.074  -6.056  1.00 93.87           S
ANISOU    6  SG  CYS A 339    11718  12153  11796   -277     24     -8       S
ATOM      7  N   LYS A 340      14.812 -18.882  -5.911  1.00 39.55           N
ANISOU    7  N   LYS A 340     4766   5420   4841   -268    -23     18       N
ATOM      8  CA  LYS A 340      15.731 -19.023  -7.028  1.00 37.52           C
ANISOU    8  CA  LYS A 340     4504   5145   4607   -256    -29     25       C
ATOM      9  C   LYS A 340      16.715 -20.145  -6.712  1.00 35.25           C
ANISOU    9  C   LYS A 340     4185   4915   4294   -223    -55     66       C
ATOM     10  O   LYS A 340      17.274 -20.199  -5.619  1.00 31.02           O
ANISOU   10  O   LYS A 340     3617   4459   3711   -230    -70     66       O
ATOM     11  CB  LYS A 340      16.481 -17.733  -7.289  1.00  0.00           C
ATOM     12  CG  LYS A 340      15.528 -16.672  -7.829  1.00  0.00           C
ATOM     13  CD  LYS A 340      16.299 -15.382  -8.090  1.00  0.00           C
ATOM     14  CE  LYS A 340      15.340 -14.311  -8.600  1.00  0.00           C
ATOM     15  NZ  LYS A 340      16.083 -13.067  -8.848  1.00  0.00           N
ATOM     16  N   PRO A 341      16.916 -21.064  -7.660  1.00 31.44           N
ANISOU   16  N   PRO A 341     3710   4395   3842   -186    -60    101       N
ATOM     17  CA  PRO A 341      16.236 -21.129  -8.954  1.00 26.70           C
ANISOU   17  CA  PRO A 341     3146   3710   3289   -176    -46    103       C
ATOM     18  C   PRO A 341      15.005 -22.034  -8.927  1.00 23.81           C
ANISOU   18  C   PRO A 341     2808   3297   2942   -149    -46    139       C
ATOM     19  O   PRO A 341      14.873 -22.895  -8.054  1.00 21.73           O
ANISOU   19  O   PRO A 341     2536   3061   2661   -129    -56    175       O
ATOM     20  CB  PRO A 341      17.294 -21.781  -9.836  1.00 31.09           C
ANISOU   20  CB  PRO A 341     3685   4267   3860   -150    -53    118       C
ATOM     21  CG  PRO A 341      17.952 -22.742  -8.908  1.00 36.42           C
ANISOU   21  CG  PRO A 341     4326   5002   4509   -120    -74    154       C
ATOM     22  CD  PRO A 341      18.017 -22.038  -7.577  1.00 33.33           C
ANISOU   22  CD  PRO A 341     3915   4678   4070   -151    -81    135       C
ATOM     23  N   VAL A 342      14.115 -21.845  -9.891  1.00 15.98           N
ANISOU   23  N   VAL A 342     1848   2237   1987   -150    -35    130       N
ATOM     24  CA  VAL A 342      13.016 -22.769 -10.098  1.00 13.81           C
ANISOU   24  CA  VAL A 342     1596   1914   1738   -126    -34    158       C
ATOM     25  C   VAL A 342      13.563 -23.919 -10.942  1.00 13.49           C
ANISOU   25  C   VAL A 342     1554   1854   1719    -92    -40    184       C
ATOM     26  O   VAL A 342      14.088 -23.700 -12.031  1.00 15.08           O
ANISOU   26  O   VAL A 342     1758   2038   1934    -92    -38    168       O
ATOM     27  CB  VAL A 342      11.855 -22.064 -10.828  1.00 18.41           C
ANISOU   27  CB  VAL A 342     2208   2439   2350   -140    -24    134       C
ATOM     28  CG1 VAL A 342      10.817 -23.073 -11.324  1.00 16.89           C
ANISOU   28  CG1 VAL A 342     2033   2196   2188   -117    -24    155       C
ATOM     29  CG2 VAL A 342      11.223 -21.020  -9.905  1.00 21.52           C
ANISOU   29  CG2 VAL A 342     2600   2846   2730   -169    -13    106       C
ATOM     30  N   LYS A 343      13.464 -25.141 -10.426  1.00 13.90           N
ANISOU   30  N   LYS A 343     1600   1906   1775    -63    -45    225       N
ATOM     31  CA  LYS A 343      13.924 -26.313 -11.157  1.00 16.38           C
ANISOU   31  CA  LYS A 343     1912   2193   2117    -28    -46    248       C
ATOM     32  C   LYS A 343      12.844 -26.878 -12.068  1.00 13.66           C
ANISOU   32  C   LYS A 343     1597   1779   1815    -21    -36    244       C
ATOM     33  O   LYS A 343      11.834 -27.403 -11.601  1.00 16.86           O
ANISOU   33  O   LYS A 343     2015   2160   2233    -19    -31    262       O
ATOM     34  CB  LYS A 343      14.385 -27.392 -10.183  1.00 17.20           C
ANISOU   34  CB  LYS A 343     1998   2326   2213      4    -54    297       C
ATOM     35  CG  LYS A 343      15.588 -26.972  -9.350  1.00 20.38           C
ANISOU   35  CG  LYS A 343     2363   2807   2571      3    -70    302       C
ATOM     36  CD  LYS A 343      16.052 -28.093  -8.425  1.00 34.36           C
ANISOU   36  CD  LYS A 343     4115   4609   4332     41    -82    361       C
ATOM     37  CE  LYS A 343      15.087 -28.297  -7.268  1.00 51.38           C
ANISOU   37  CE  LYS A 343     6286   6773   6463     33    -79    392       C
ATOM     38  NZ  LYS A 343      15.149 -27.175  -6.280  1.00 58.73           N
ANISOU   38  NZ  LYS A 343     7203   7776   7336     -4    -86    368       N
ATOM     39  N   TRP A 344      13.062 -26.759 -13.371  1.00 14.54           N
ANISOU   39  N   TRP A 344     1718   1864   1944    -21    -33    219       N
ATOM     40  CA  TRP A 344      12.088 -27.228 -14.348  1.00 14.39           C
ANISOU   40  CA  TRP A 344     1723   1788   1958    -18    -28    207       C
ATOM     41  C   TRP A 344      12.364 -28.679 -14.715  1.00 15.75           C
ANISOU   41  C   TRP A 344     1891   1930   2163     14    -22    225       C
ATOM     42  O   TRP A 344      13.524 -29.076 -14.794  1.00 21.24           O
ANISOU   42  O   TRP A 344     2568   2645   2858     34    -21    233       O
ATOM     43  CB  TRP A 344      12.156 -26.351 -15.593  1.00 14.62           C
ANISOU   43  CB  TRP A 344     1765   1807   1982    -35    -28    173       C
ATOM     44  CG  TRP A 344      10.866 -26.346 -16.325  1.00 14.48           C
ANISOU   44  CG  TRP A 344     1771   1746   1984    -42    -30    158       C
ATOM     45  CD1 TRP A 344      10.487 -27.191 -17.323  1.00 17.69           C
ANISOU   45  CD1 TRP A 344     2188   2119   2416    -31    -28    147       C
ATOM     46  CD2 TRP A 344       9.761 -25.465 -16.096  1.00 12.73           C
ANISOU   46  CD2 TRP A 344     1561   1516   1761    -61    -34    148       C
ATOM     47  NE1 TRP A 344       9.214 -26.892 -17.735  1.00 18.01           N
ANISOU   47  NE1 TRP A 344     2244   2135   2466    -43    -35    132       N
ATOM     48  CE2 TRP A 344       8.747 -25.831 -17.003  1.00 13.15           C
ANISOU   48  CE2 TRP A 344     1627   1531   1836    -58    -39    134       C
ATOM     49  CE3 TRP A 344       9.529 -24.409 -15.205  1.00 15.00           C
ANISOU   49  CE3 TRP A 344     1845   1823   2032    -79    -34    145       C
ATOM     50  CZ2 TRP A 344       7.514 -25.175 -17.058  1.00 15.13           C
ANISOU   50  CZ2 TRP A 344     1887   1766   2095    -70    -46    123       C
ATOM     51  CZ3 TRP A 344       8.311 -23.748 -15.259  1.00 18.74           C
ANISOU   51  CZ3 TRP A 344     2329   2274   2517    -90    -36    132       C
ATOM     52  CH2 TRP A 344       7.313 -24.136 -16.182  1.00 17.28           C
ANISOU   52  CH2 TRP A 344     2156   2054   2357    -83    -44    123       C
ATOM     53  N   CYS A 345      11.317 -29.479 -14.938  1.00 13.68           N
ANISOU   53  N   CYS A 345     1645   1620   1934     17    -15    227       N
ATOM     54  CA  CYS A 345      11.539 -30.889 -15.274  1.00 15.32           C
ANISOU   54  CA  CYS A 345     1851   1789   2181     45     -3    239       C
ATOM     55  C   CYS A 345      11.341 -31.151 -16.771  1.00 20.40           C
ANISOU   55  C   CYS A 345     2507   2399   2847     42      2    197       C
ATOM     56  O   CYS A 345      10.311 -30.801 -17.326  1.00 20.41           O
ANISOU   56  O   CYS A 345     2524   2381   2850     21     -2    172       O
ATOM     57  CB  CYS A 345      10.648 -31.815 -14.428  1.00 17.93           C
ANISOU   57  CB  CYS A 345     2188   2087   2539     51      7    272       C
ATOM     58  SG  CYS A 345      11.216 -33.571 -14.438  1.00 23.74           S
ANISOU   58  SG  CYS A 345     2918   2776   3328     93     26    304       S
ATOM     59  N   ALA A 346      12.340 -31.773 -17.408  1.00 14.26           N
ANISOU   59  N   ALA A 346     1719   1616   2084     64     11    189       N
ATOM     60  CA  ALA A 346      12.313 -32.068 -18.839  1.00 14.79           C
ANISOU   60  CA  ALA A 346     1795   1659   2164     61     19    145       C
ATOM     61  C   ALA A 346      12.090 -33.565 -19.044  1.00 16.33           C
ANISOU   61  C   ALA A 346     1991   1799   2415     82     39    143       C
ATOM     62  O   ALA A 346      12.715 -34.369 -18.379  1.00 17.64           O
ANISOU   62  O   ALA A 346     2142   1952   2607    112     48    176       O
ATOM     63  CB  ALA A 346      13.658 -31.668 -19.472  1.00 17.50           C
ANISOU   63  CB  ALA A 346     2124   2038   2486     68     23    129       C
ATOM     64  N   LEU A 347      11.227 -33.937 -19.979  1.00 18.42           N
ANISOU   64  N   LEU A 347     2271   2029   2699     66     44    103       N
ATOM     65  CA  LEU A 347      10.933 -35.357 -20.167  1.00 19.52           C
ANISOU   65  CA  LEU A 347     2412   2109   2897     79     66     93       C
ATOM     66  C   LEU A 347      11.418 -35.924 -21.499  1.00 22.48           C
ANISOU   66  C   LEU A 347     2786   2468   3288     83     83     40       C
ATOM     67  O   LEU A 347      11.027 -37.024 -21.896  1.00 22.85           O
ANISOU   67  O   LEU A 347     2836   2462   3384     86    103     14       O
ATOM     68  CB  LEU A 347       9.442 -35.625 -19.960  1.00 24.15           C
ANISOU   68  CB  LEU A 347     3010   2661   3505     55     66     87       C
ATOM     69  CG  LEU A 347       8.509 -34.545 -20.487  1.00 29.12           C
ANISOU   69  CG  LEU A 347     3650   3320   4096     22     43     59       C
ATOM     70  CD1 LEU A 347       8.539 -34.516 -22.001  1.00 28.64           C
ANISOU   70  CD1 LEU A 347     3595   3265   4022     11     40      1       C
ATOM     71  CD2 LEU A 347       7.096 -34.780 -19.976  1.00 26.92           C
ANISOU   71  CD2 LEU A 347     3374   3014   3842      2     43     61       C
ATOM     72  N   SER A 348      12.280 -35.185 -22.180  1.00 17.76           N
ANISOU   72  N   SER A 348     2183   1916   2649     82     77     21       N
ATOM     73  CA  SER A 348      12.907 -35.689 -23.408  1.00 18.55           C
ANISOU   73  CA  SER A 348     2281   2011   2758     87     97    -30       C
ATOM     74  C   SER A 348      14.252 -35.017 -23.595  1.00 21.88           C
ANISOU   74  C   SER A 348     2686   2483   3145     97     99    -27       C
ATOM     75  O   SER A 348      14.527 -33.993 -22.970  1.00 17.81           O
ANISOU   75  O   SER A 348     2166   2008   2592     91     81      6       O
ATOM     76  CB  SER A 348      12.027 -35.437 -24.633  1.00 21.26           C
ANISOU   76  CB  SER A 348     2643   2360   3076     53     90    -85       C
ATOM     77  OG  SER A 348      12.097 -34.075 -25.057  1.00 19.39           O
ANISOU   77  OG  SER A 348     2416   2178   2774     32     69    -84       O
ATOM     78  N   HIS A 349      15.091 -35.594 -24.447  1.00 18.50           N
ANISOU   78  N   HIS A 349     2246   2051   2732    110    124    -65       N
ATOM     79  CA  HIS A 349      16.387 -34.995 -24.713  1.00 16.63           C
ANISOU   79  CA  HIS A 349     1989   1863   2465    117    131    -68       C
ATOM     80  C   HIS A 349      16.224 -33.596 -25.293  1.00 16.05           C
ANISOU   80  C   HIS A 349     1935   1842   2323     79    115    -77       C
ATOM     81  O   HIS A 349      16.918 -32.660 -24.882  1.00 16.52           O
ANISOU   81  O   HIS A 349     1983   1944   2351     74    107    -53       O
ATOM     82  CB  HIS A 349      17.228 -35.858 -25.656  1.00 20.74           C
ANISOU   82  CB  HIS A 349     2495   2372   3014    134    165   -117       C
ATOM     83  CG  HIS A 349      18.593 -35.297 -25.903  1.00 25.89           C
ANISOU   83  CG  HIS A 349     3121   3077   3641    141    177   -122       C
ATOM     84  ND1 HIS A 349      19.476 -35.022 -24.881  1.00 26.50           N
ANISOU   84  ND1 HIS A 349     3166   3180   3723    165    168    -77       N
ATOM     85  CD2 HIS A 349      19.212 -34.924 -27.049  1.00 26.83           C
ANISOU   85  CD2 HIS A 349     3238   3232   3725    122    197   -168       C
ATOM     86  CE1 HIS A 349      20.589 -34.517 -25.389  1.00 33.09           C
ANISOU   86  CE1 HIS A 349     3978   4062   4533    160    183    -98       C
ATOM     87  NE2 HIS A 349      20.455 -34.449 -26.702  1.00 28.81           N
ANISOU   87  NE2 HIS A 349     3455   3526   3967    134    203   -152       N
ATOM     88  N   HIS A 350      15.311 -33.444 -26.246  1.00 15.82           N
ANISOU   88  N   HIS A 350     1932   1808   2269     51    109   -111       N
ATOM     89  CA  HIS A 350      15.098 -32.128 -26.851  1.00 18.13           C
ANISOU   89  CA  HIS A 350     2246   2145   2498     19     94   -112       C
ATOM     90  C   HIS A 350      14.542 -31.116 -25.838  1.00 17.17           C
ANISOU   90  C   HIS A 350     2132   2032   2361      9     66    -64       C
ATOM     91  O   HIS A 350      14.908 -29.931 -25.875  1.00 14.52           O
ANISOU   91  O   HIS A 350     1801   1731   1984     -8     60    -49       O
ATOM     92  CB  HIS A 350      14.167 -32.221 -28.053  1.00 18.49           C
ANISOU   92  CB  HIS A 350     2318   2190   2519     -5     88   -154       C
ATOM     93  CG  HIS A 350      14.775 -32.907 -29.235  1.00 27.17           C
ANISOU   93  CG  HIS A 350     3413   3297   3614     -6    118   -210       C
ATOM     94  ND1 HIS A 350      16.136 -32.985 -29.433  1.00 41.91           N
ANISOU   94  ND1 HIS A 350     5260   5185   5481      6    147   -220       N
ATOM     95  CD2 HIS A 350      14.205 -33.552 -30.280  1.00 29.06           C
ANISOU   95  CD2 HIS A 350     3664   3530   3847    -19    124   -264       C
ATOM     96  CE1 HIS A 350      16.380 -33.644 -30.551  1.00 41.94           C
ANISOU   96  CE1 HIS A 350     5263   5192   5479      1    173   -278       C
ATOM     97  NE2 HIS A 350      15.224 -34.000 -31.083  1.00 38.79           N
ANISOU   97  NE2 HIS A 350     4885   4778   5075    -15    159   -307       N
ATOM     98  N   GLU A 351      13.662 -31.569 -24.942  1.00 14.91           N
ANISOU   98  N   GLU A 351     1845   1711   2107     18     53    -43       N
ATOM     99  CA  GLU A 351      13.198 -30.694 -23.851  1.00 12.37           C
ANISOU   99  CA  GLU A 351     1526   1399   1775     11     32     -2       C
ATOM    100  C   GLU A 351      14.346 -30.284 -22.946  1.00 13.90           C
ANISOU  100  C   GLU A 351     1696   1621   1962     22     36     28       C
ATOM    101  O   GLU A 351      14.435 -29.121 -22.531  1.00 16.80           O
ANISOU  101  O   GLU A 351     2067   2018   2299      5     25     45       O
ATOM    102  CB  GLU A 351      12.081 -31.342 -23.011  1.00 13.86           C
ANISOU  102  CB  GLU A 351     1717   1549   2001     17     23     15       C
ATOM    103  CG  GLU A 351      10.713 -31.244 -23.671  1.00 19.03           C
ANISOU  103  CG  GLU A 351     2391   2189   2652     -4      9    -10       C
ATOM    104  CD  GLU A 351       9.563 -31.284 -22.675  1.00 22.87           C
ANISOU  104  CD  GLU A 351     2877   2653   3160     -8     -3     13       C
ATOM    105  OE1 GLU A 351       8.419 -30.954 -23.081  1.00 20.63           O
ANISOU  105  OE1 GLU A 351     2602   2366   2870    -25    -20     -3       O
ATOM    106  OE2 GLU A 351       9.802 -31.639 -21.493  1.00 20.24           O
ANISOU  106  OE2 GLU A 351     2531   2309   2849      6      5     47       O
ATOM    107  N   ARG A 352      15.227 -31.228 -22.628  1.00 13.53           N
ANISOU  107  N   ARG A 352     1625   1568   1947     51     51     33       N
ATOM    108  CA  ARG A 352      16.350 -30.896 -21.754  1.00 16.85           C
ANISOU  108  CA  ARG A 352     2017   2025   2362     64     51     60       C
ATOM    109  C   ARG A 352      17.284 -29.876 -22.413  1.00 14.63           C
ANISOU  109  C   ARG A 352     1729   1790   2041     43     59     41       C
ATOM    110  O   ARG A 352      17.757 -28.951 -21.752  1.00 17.57           O
ANISOU  110  O   ARG A 352     2089   2198   2389     31     51     58       O
ATOM    111  CB  ARG A 352      17.122 -32.150 -21.327  1.00 17.50           C
ANISOU  111  CB  ARG A 352     2069   2091   2488    107     64     73       C
ATOM    112  CG  ARG A 352      18.384 -31.867 -20.496  1.00 21.50           C
ANISOU  112  CG  ARG A 352     2537   2645   2986    124     59     99       C
ATOM    113  CD  ARG A 352      18.041 -31.146 -19.185  1.00 25.72           C
ANISOU  113  CD  ARG A 352     3070   3206   3495    113     35    138       C
ATOM    114  NE  ARG A 352      19.221 -30.823 -18.379  1.00 22.28           N
ANISOU  114  NE  ARG A 352     2594   2826   3044    126     26    157       N
ATOM    115  CZ  ARG A 352      19.681 -31.586 -17.390  1.00 29.14           C
ANISOU  115  CZ  ARG A 352     3436   3705   3933    164     17    197       C
ATOM    116  NH1 ARG A 352      19.072 -32.730 -17.093  1.00 26.93           N
ANISOU  116  NH1 ARG A 352     3167   3373   3691    193     21    225       N
ATOM    117  NH2 ARG A 352      20.755 -31.213 -16.698  1.00 31.18           N
ANISOU  117  NH2 ARG A 352     3652   4024   4170    173      5    211       N
ATOM    118  N   LEU A 353      17.534 -30.034 -23.711  1.00 14.37           N
ANISOU  118  N   LEU A 353     1704   1755   1999     36     77      3       N
ATOM    119  CA  LEU A 353      18.371 -29.065 -24.435  1.00 14.20           C
ANISOU  119  CA  LEU A 353     1682   1776   1939     11     90    -14       C
ATOM    120  C   LEU A 353      17.763 -27.664 -24.369  1.00 16.30           C
ANISOU  120  C   LEU A 353     1975   2053   2165    -24     74      1       C
ATOM    121  O   LEU A 353      18.481 -26.676 -24.187  1.00 15.29           O
ANISOU  121  O   LEU A 353     1837   1957   2014    -44     80      7       O
ATOM    122  CB  LEU A 353      18.534 -29.462 -25.899  1.00 14.26           C
ANISOU  122  CB  LEU A 353     1702   1782   1936      4    113    -57       C
ATOM    123  CG  LEU A 353      19.372 -30.711 -26.202  1.00 20.83           C
ANISOU  123  CG  LEU A 353     2503   2604   2806     36    140    -85       C
ATOM    124  CD1 LEU A 353      19.438 -30.937 -27.699  1.00 20.68           C
ANISOU  124  CD1 LEU A 353     2501   2591   2765     20    165   -135       C
ATOM    125  CD2 LEU A 353      20.763 -30.561 -25.622  1.00 22.98           C
ANISOU  125  CD2 LEU A 353     2731   2913   3088     51    151    -75       C
ATOM    126  N   LYS A 354      16.446 -27.576 -24.545  1.00 13.62           N
ANISOU  126  N   LYS A 354     1667   1687   1823    -32     57      5       N
ATOM    127  CA  LYS A 354      15.770 -26.278 -24.488  1.00 14.04           C
ANISOU  127  CA  LYS A 354     1745   1743   1847    -58     41     20       C
ATOM    128  C   LYS A 354      15.835 -25.708 -23.075  1.00 15.02           C
ANISOU  128  C   LYS A 354     1853   1875   1979    -60     31     47       C
ATOM    129  O   LYS A 354      16.078 -24.508 -22.876  1.00 14.34           O
ANISOU  129  O   LYS A 354     1772   1806   1872    -84     32     54       O
ATOM    130  CB  LYS A 354      14.316 -26.383 -24.950  1.00 13.15           C
ANISOU  130  CB  LYS A 354     1661   1602   1734    -60     22     17       C
ATOM    131  CG  LYS A 354      13.564 -25.046 -24.858  1.00 12.51           C
ANISOU  131  CG  LYS A 354     1603   1520   1631    -80      5     36       C
ATOM    132  CD  LYS A 354      12.158 -25.168 -25.453  1.00 13.43           C
ANISOU  132  CD  LYS A 354     1741   1616   1746    -79    -17     31       C
ATOM    133  CE  LYS A 354      11.355 -23.873 -25.249  1.00 14.25           C
ANISOU  133  CE  LYS A 354     1863   1713   1839    -91    -35     53       C
ATOM    134  NZ  LYS A 354      10.009 -23.959 -25.907  1.00 14.98           N
ANISOU  134  NZ  LYS A 354     1971   1793   1929    -87    -60     48       N
ATOM    135  N   CYS A 355      15.633 -26.573 -22.089  1.00 15.42           N
ANISOU  135  N   CYS A 355     1885   1913   2059    -36     23     61       N
ATOM    136  CA  CYS A 355      15.710 -26.152 -20.703  1.00 13.78           C
ANISOU  136  CA  CYS A 355     1661   1722   1852    -37     13     85       C
ATOM    137  C   CYS A 355      17.123 -25.670 -20.335  1.00 16.56           C
ANISOU  137  C   CYS A 355     1983   2120   2190    -44     22     83       C
ATOM    138  O   CYS A 355      17.278 -24.702 -19.589  1.00 13.99           O
ANISOU  138  O   CYS A 355     1651   1818   1848    -64     18     89       O
ATOM    139  CB  CYS A 355      15.248 -27.273 -19.773  1.00 21.15           C
ANISOU  139  CB  CYS A 355     2584   2637   2816    -10      5    106       C
ATOM    140  SG  CYS A 355      14.944 -26.659 -18.100  1.00 29.81           S
ANISOU  140  SG  CYS A 355     3669   3755   3901    -18     -9    134       S
ATOM    141  N   ASP A 356      18.147 -26.345 -20.851  1.00 13.56           N
ANISOU  141  N   ASP A 356     1579   1753   1818    -27     37     71       N
ATOM    142  CA  ASP A 356      19.525 -25.897 -20.652  1.00 14.26           C
ANISOU  142  CA  ASP A 356     1633   1890   1896    -35     48     63       C
ATOM    143  C   ASP A 356      19.722 -24.490 -21.205  1.00 12.12           C
ANISOU  143  C   ASP A 356     1378   1632   1593    -79     60     48       C
ATOM    144  O   ASP A 356      20.347 -23.639 -20.560  1.00 14.27           O
ANISOU  144  O   ASP A 356     1630   1939   1854   -101     61     46       O
ATOM    145  CB  ASP A 356      20.518 -26.831 -21.348  1.00 15.06           C
ANISOU  145  CB  ASP A 356     1707   1999   2014    -10     67     46       C
ATOM    146  CG  ASP A 356      20.634 -28.189 -20.672  1.00 22.62           C
ANISOU  146  CG  ASP A 356     2641   2944   3011     38     59     66       C
ATOM    147  OD1 ASP A 356      21.072 -29.145 -21.352  1.00 28.65           O
ANISOU  147  OD1 ASP A 356     3392   3692   3800     64     76     50       O
ATOM    148  OD2 ASP A 356      20.301 -28.303 -19.478  1.00 24.43           O
ANISOU  148  OD2 ASP A 356     2862   3177   3243     50     38     98       O
ATOM    149  N   GLU A 357      19.205 -24.259 -22.409  1.00 12.00           N
ANISOU  149  N   GLU A 357     1399   1593   1566    -92     70     37       N
ATOM    150  CA  GLU A 357      19.321 -22.950 -23.049  1.00 13.61           C
ANISOU  150  CA  GLU A 357     1627   1802   1743   -132     84     31       C
ATOM    151  C   GLU A 357      18.596 -21.900 -22.196  1.00 17.99           C
ANISOU  151  C   GLU A 357     2197   2345   2295   -151     69     46       C
ATOM    152  O   GLU A 357      19.119 -20.817 -21.924  1.00 14.04           O
ANISOU  152  O   GLU A 357     1691   1860   1785   -183     81     42       O
ATOM    153  CB  GLU A 357      18.764 -22.998 -24.479  1.00 14.37           C
ANISOU  153  CB  GLU A 357     1762   1877   1821   -137     91     24       C
ATOM    154  CG  GLU A 357      19.073 -21.723 -25.272  1.00 16.96           C
ANISOU  154  CG  GLU A 357     2115   2211   2117   -176    112     26       C
ATOM    155  CD  GLU A 357      18.556 -21.749 -26.705  1.00 23.33           C
ANISOU  155  CD  GLU A 357     2961   3008   2895   -180    117     24       C
ATOM    156  OE1 GLU A 357      18.026 -22.791 -27.142  1.00 23.80           O
ANISOU  156  OE1 GLU A 357     3025   3059   2959   -156    106     12       O
ATOM    157  OE2 GLU A 357      18.684 -20.709 -27.390  1.00 26.02           O
ANISOU  157  OE2 GLU A 357     3329   3351   3208   -209    132     35       O
ATOM    158  N   TRP A 358      17.389 -22.236 -21.761  1.00 13.80           N
ANISOU  158  N   TRP A 358     1682   1785   1777   -134     47     60       N
ATOM    159  CA  TRP A 358      16.623 -21.336 -20.899  1.00 15.31           C
ANISOU  159  CA  TRP A 358     1884   1962   1969   -149     35     70       C
ATOM    160  C   TRP A 358      17.422 -21.021 -19.642  1.00 13.63           C
ANISOU  160  C   TRP A 358     1635   1787   1755   -160     36     66       C
ATOM    161  O   TRP A 358      17.543 -19.863 -19.225  1.00 14.43           O
ANISOU  161  O   TRP A 358     1738   1894   1851   -190     44     57       O
ATOM    162  CB  TRP A 358      15.309 -22.011 -20.520  1.00 14.77           C
ANISOU  162  CB  TRP A 358     1828   1865   1918   -126     14     82       C
ATOM    163  CG  TRP A 358      14.337 -21.153 -19.783  1.00 12.07           C
ANISOU  163  CG  TRP A 358     1498   1506   1581   -138      4     88       C
ATOM    164  CD1 TRP A 358      14.421 -19.799 -19.534  1.00 13.39           C
ANISOU  164  CD1 TRP A 358     1673   1672   1743   -166     13     83       C
ATOM    165  CD2 TRP A 358      13.123 -21.599 -19.186  1.00 12.72           C
ANISOU  165  CD2 TRP A 358     1585   1567   1681   -123    -12     96       C
ATOM    166  NE1 TRP A 358      13.310 -19.386 -18.822  1.00 14.15           N
ANISOU  166  NE1 TRP A 358     1778   1747   1852   -166      3     85       N
ATOM    167  CE2 TRP A 358      12.503 -20.472 -18.597  1.00 14.00           C
ANISOU  167  CE2 TRP A 358     1755   1718   1845   -141    -12     94       C
ATOM    168  CE3 TRP A 358      12.496 -22.848 -19.094  1.00 15.67           C
ANISOU  168  CE3 TRP A 358     1955   1926   2072    -98    -22    103       C
ATOM    169  CZ2 TRP A 358      11.281 -20.564 -17.924  1.00 16.67           C
ANISOU  169  CZ2 TRP A 358     2096   2038   2200   -133    -23     98       C
ATOM    170  CZ3 TRP A 358      11.288 -22.939 -18.431  1.00 17.85           C
ANISOU  170  CZ3 TRP A 358     2236   2183   2364    -94    -32    109       C
ATOM    171  CH2 TRP A 358      10.688 -21.798 -17.860  1.00 14.03           C
ANISOU  171  CH2 TRP A 358     1757   1694   1879   -111    -32    106       C
ATOM    172  N   SER A 359      17.969 -22.061 -19.036  1.00 11.84           N
ANISOU  172  N   SER A 359     1375   1587   1537   -134     29     71       N
ATOM    173  CA  SER A 359      18.694 -21.894 -17.787  1.00 12.24           C
ANISOU  173  CA  SER A 359     1388   1684   1581   -139     23     70       C
ATOM    174  C   SER A 359      19.830 -20.870 -17.880  1.00 15.68           C
ANISOU  174  C   SER A 359     1801   2154   2001   -175     41     45       C
ATOM    175  O   SER A 359      19.931 -19.975 -17.036  1.00 14.33           O
ANISOU  175  O   SER A 359     1621   2005   1821   -204     41     33       O
ATOM    176  CB  SER A 359      19.235 -23.239 -17.292  1.00 15.54           C
ANISOU  176  CB  SER A 359     1770   2124   2008    -99     12     86       C
ATOM    177  OG  SER A 359      19.908 -23.072 -16.049  1.00 16.00           O
ANISOU  177  OG  SER A 359     1790   2237   2052   -101      1     89       O
ATOM    178  N   VAL A 360      20.702 -20.997 -18.878  1.00 14.11           N
ANISOU  178  N   VAL A 360     1595   1965   1803   -178     60     33       N
ATOM    179  CA  VAL A 360      21.835 -20.068 -18.946  1.00 13.54           C
ANISOU  179  CA  VAL A 360     1498   1928   1720   -217     82      8       C
ATOM    180  C   VAL A 360      21.382 -18.664 -19.315  1.00 14.13           C
ANISOU  180  C   VAL A 360     1610   1970   1789   -261    100      1       C
ATOM    181  O   VAL A 360      21.922 -17.686 -18.807  1.00 13.50           O
ANISOU  181  O   VAL A 360     1514   1911   1706   -300    112    -20       O
ATOM    182  CB  VAL A 360      22.988 -20.559 -19.875  1.00 15.57           C
ANISOU  182  CB  VAL A 360     1729   2209   1979   -212    103     -5       C
ATOM    183  CG1 VAL A 360      23.556 -21.872 -19.343  1.00 17.58           C
ANISOU  183  CG1 VAL A 360     1938   2496   2247   -165     86      2       C
ATOM    184  CG2 VAL A 360      22.517 -20.689 -21.325  1.00 16.20           C
ANISOU  184  CG2 VAL A 360     1854   2247   2055   -210    121     -2       C
ATOM    185  N   ASN A 361      20.373 -18.563 -20.173  1.00 12.21           N
ANISOU  185  N   ASN A 361     1417   1675   1547   -255    100     17       N
ATOM    186  CA  ASN A 361      19.836 -17.253 -20.526  1.00 14.61           C
ANISOU  186  CA  ASN A 361     1761   1941   1851   -288    115     19       C
ATOM    187  C   ASN A 361      19.184 -16.552 -19.334  1.00 14.89           C
ANISOU  187  C   ASN A 361     1796   1966   1896   -300    104     14       C
ATOM    188  O   ASN A 361      19.194 -15.318 -19.245  1.00 13.84           O
ANISOU  188  O   ASN A 361     1676   1813   1770   -337    123      2       O
ATOM    189  CB  ASN A 361      18.846 -17.382 -21.685  1.00 16.09           C
ANISOU  189  CB  ASN A 361     1996   2084   2034   -272    110     42       C
ATOM    190  CG  ASN A 361      19.537 -17.385 -23.036  1.00 15.12           C
ANISOU  190  CG  ASN A 361     1886   1967   1892   -284    135     42       C
ATOM    191  OD1 ASN A 361      19.822 -16.327 -23.585  1.00 15.82           O
ANISOU  191  OD1 ASN A 361     1996   2042   1973   -318    161     45       O
ATOM    192  ND2 ASN A 361      19.812 -18.572 -23.574  1.00 13.27           N
ANISOU  192  ND2 ASN A 361     1639   1751   1652   -257    132     37       N
ATOM    193  N   SER A 362      18.640 -17.347 -18.414  1.00 14.92           N
ANISOU  193  N   SER A 362     1784   1982   1903   -271     77     20       N
ATOM    194  CA  SER A 362      17.955 -16.831 -17.222  1.00 13.68           C
ANISOU  194  CA  SER A 362     1626   1822   1751   -280     68     13       C
ATOM    195  C   SER A 362      18.945 -16.402 -16.142  1.00 16.58           C
ANISOU  195  C   SER A 362     1949   2243   2106   -309     73    -16       C
ATOM    196  O   SER A 362      18.552 -15.865 -15.105  1.00 17.76           O
ANISOU  196  O   SER A 362     2093   2401   2256   -325     70    -32       O
ATOM    197  CB  SER A 362      17.022 -17.894 -16.635  1.00 11.16           C
ANISOU  197  CB  SER A 362     1306   1499   1435   -242     41     33       C
ATOM    198  OG  SER A 362      17.744 -18.875 -15.894  1.00 14.93           O
ANISOU  198  OG  SER A 362     1744   2028   1901   -223     28     37       O
ATOM    199  N   VAL A 363      20.227 -16.647 -16.400  1.00 14.89           N
ANISOU  199  N   VAL A 363     1702   2072   1884   -316     81    -27       N
ATOM    200  CA  VAL A 363      21.290 -16.431 -15.421  1.00 13.14           C
ANISOU  200  CA  VAL A 363     1428   1917   1649   -339     80    -55       C
ATOM    201  C   VAL A 363      20.897 -17.045 -14.077  1.00 21.28           C
ANISOU  201  C   VAL A 363     2437   2985   2664   -316     50    -47       C
ATOM    202  O   VAL A 363      20.913 -16.391 -13.052  1.00 24.41           O
ANISOU  202  O   VAL A 363     2816   3410   3047   -344     49    -73       O
ATOM    203  CB  VAL A 363      21.697 -14.947 -15.311  1.00 21.68           C
ANISOU  203  CB  VAL A 363     2508   2993   2735   -398    109    -94       C
ATOM    204  CG1 VAL A 363      22.942 -14.800 -14.439  1.00 28.13           C
ANISOU  204  CG1 VAL A 363     3264   3889   3536   -425    107   -130       C
ATOM    205  CG2 VAL A 363      21.974 -14.398 -16.682  1.00 19.07           C
ANISOU  205  CG2 VAL A 363     2208   2620   2418   -418    141    -90       C
ATOM    206  N   GLY A 364      20.510 -18.315 -14.122  1.00 33.22           N
ANISOU  206  N   GLY A 364     3951   4492   4177   -267     29    -11       N
ATOM    207  CA  GLY A 364      20.299 -19.096 -12.920  1.00 42.75           C
ANISOU  207  CA  GLY A 364     5136   5739   5367   -240      3      7       C
ATOM    208  C   GLY A 364      18.966 -18.962 -12.203  1.00 36.06           C
ANISOU  208  C   GLY A 364     4318   4865   4518   -240     -4     16       C
ATOM    209  O   GLY A 364      18.799 -19.563 -11.149  1.00 34.37           O
ANISOU  209  O   GLY A 364     4087   4688   4284   -222    -22     33       O
ATOM    210  N   LYS A 365      18.031 -18.176 -12.737  1.00 17.41           N
ANISOU  210  N   LYS A 365     1998   2443   2175   -257     12      6       N
ATOM    211  CA  LYS A 365      16.686 -18.128 -12.161  1.00 15.33           C
ANISOU  211  CA  LYS A 365     1758   2150   1916   -252      8     13       C
ATOM    212  C   LYS A 365      15.959 -19.433 -12.443  1.00 16.50           C
ANISOU  212  C   LYS A 365     1921   2273   2076   -207     -7     53       C
ATOM    213  O   LYS A 365      15.014 -19.800 -11.741  1.00 14.99           O
ANISOU  213  O   LYS A 365     1737   2074   1884   -196    -13     66       O
ATOM    214  CB  LYS A 365      15.893 -16.978 -12.757  1.00 16.74           C
ANISOU  214  CB  LYS A 365     1973   2269   2120   -275     27     -5       C
ATOM    215  CG  LYS A 365      16.397 -15.598 -12.332  1.00 24.38           C
ANISOU  215  CG  LYS A 365     2931   3249   3085   -323     47    -49       C
ATOM    216  CD  LYS A 365      15.526 -14.504 -12.921  1.00 38.28           C
ANISOU  216  CD  LYS A 365     4730   4937   4877   -338     67    -59       C
ATOM    217  CE  LYS A 365      16.142 -13.123 -12.703  1.00 47.35           C
ANISOU  217  CE  LYS A 365     5873   6084   6034   -388     95   -103       C
ATOM    218  NZ  LYS A 365      16.353 -12.837 -11.262  1.00 41.36           N
ANISOU  218  NZ  LYS A 365     5082   5380   5254   -414     95   -142       N
ATOM    219  N   ILE A 366      16.382 -20.113 -13.501  1.00 14.07           N
ANISOU  219  N   ILE A 366     1617   1948   1781   -185     -7     68       N
ATOM    220  CA  ILE A 366      15.799 -21.399 -13.884  1.00 11.50           C
ANISOU  220  CA  ILE A 366     1304   1593   1472   -146    -17     99       C
ATOM    221  C   ILE A 366      16.923 -22.417 -13.922  1.00 16.13           C
ANISOU  221  C   ILE A 366     1859   2214   2056   -119    -23    114       C
ATOM    222  O   ILE A 366      18.020 -22.099 -14.380  1.00 15.13           O
ANISOU  222  O   ILE A 366     1713   2112   1924   -129    -16     98       O
ATOM    223  CB  ILE A 366      15.189 -21.327 -15.286  1.00 12.56           C
ANISOU  223  CB  ILE A 366     1473   1672   1628   -143    -10     96       C
ATOM    224  CG1 ILE A 366      13.998 -20.362 -15.313  1.00 15.46           C
ANISOU  224  CG1 ILE A 366     1869   2002   2005   -161     -7     86       C
ATOM    225  CG2 ILE A 366      14.773 -22.724 -15.766  1.00 18.50           C
ANISOU  225  CG2 ILE A 366     2232   2398   2399   -107    -17    117       C
ATOM    226  CD1 ILE A 366      12.812 -20.834 -14.537  1.00 18.64           C
ANISOU  226  CD1 ILE A 366     2276   2390   2416   -149    -16     98       C
ATOM    227  N   GLU A 367      16.661 -23.629 -13.440  1.00 16.15           N
ANISOU  227  N   GLU A 367     1856   2214   2067    -85    -34    146       N
ATOM    228  CA  GLU A 367      17.615 -24.728 -13.561  1.00 14.72           C
ANISOU  228  CA  GLU A 367     1647   2051   1894    -49    -39    166       C
ATOM    229  C   GLU A 367      16.858 -25.926 -14.117  1.00 18.92           C
ANISOU  229  C   GLU A 367     2202   2527   2460    -18    -36    187       C
ATOM    230  O   GLU A 367      15.633 -25.923 -14.143  1.00 18.41           O
ANISOU  230  O   GLU A 367     2168   2423   2406    -25    -35    190       O
ATOM    231  CB  GLU A 367      18.204 -25.089 -12.207  1.00 23.24           C
ANISOU  231  CB  GLU A 367     2690   3190   2950    -35    -56    192       C
ATOM    232  CG  GLU A 367      19.243 -24.106 -11.718  1.00 35.42           C
ANISOU  232  CG  GLU A 367     4198   4801   4460    -63    -61    165       C
ATOM    233  CD  GLU A 367      19.910 -24.570 -10.438  1.00 57.89           C
ANISOU  233  CD  GLU A 367     7002   7717   7276    -44    -83    192       C
ATOM    234  OE1 GLU A 367      20.877 -23.912  -9.995  1.00 65.93           O
ANISOU  234  OE1 GLU A 367     7982   8802   8267    -65    -91    168       O
ATOM    235  OE2 GLU A 367      19.462 -25.593  -9.873  1.00 59.54           O
ANISOU  235  OE2 GLU A 367     7217   7917   7489     -9    -93    238       O
ATOM    236  N   CYS A 368      17.583 -26.940 -14.575  1.00 18.36           N
ANISOU  236  N   CYS A 368     2115   2451   2412     16    -33    198       N
ATOM    237  CA  CYS A 368      16.943 -28.049 -15.272  1.00 21.02           C
ANISOU  237  CA  CYS A 368     2473   2728   2786     41    -25    206       C
ATOM    238  C   CYS A 368      17.186 -29.376 -14.593  1.00 21.82           C
ANISOU  238  C   CYS A 368     2557   2823   2911     84    -29    248       C
ATOM    239  O   CYS A 368      18.272 -29.637 -14.071  1.00 21.34           O
ANISOU  239  O   CYS A 368     2460   2805   2844    107    -37    266       O
ATOM    240  CB  CYS A 368      17.437 -28.118 -16.718  1.00 31.03           C
ANISOU  240  CB  CYS A 368     3745   3978   4068     41    -10    174       C
ATOM    241  SG  CYS A 368      16.946 -26.673 -17.641  1.00 54.22           S
ANISOU  241  SG  CYS A 368     6712   6909   6979     -6     -4    138       S
ATOM    242  N   VAL A 369      16.153 -30.207 -14.604  1.00 16.88           N
ANISOU  242  N   VAL A 369     1956   2143   2315     95    -22    264       N
ATOM    243  CA  VAL A 369      16.246 -31.588 -14.176  1.00 18.49           C
ANISOU  243  CA  VAL A 369     2153   2319   2554    136    -18    304       C
ATOM    244  C   VAL A 369      15.550 -32.442 -15.238  1.00 15.57           C
ANISOU  244  C   VAL A 369     1807   1876   2232    141      1    283       C
ATOM    245  O   VAL A 369      14.590 -32.000 -15.852  1.00 19.17           O
ANISOU  245  O   VAL A 369     2289   2308   2685    111      4    252       O
ATOM    246  CB  VAL A 369      15.533 -31.798 -12.824  1.00 29.10           C
ANISOU  246  CB  VAL A 369     3503   3669   3884    136    -25    351       C
ATOM    247  CG1 VAL A 369      15.655 -33.238 -12.381  1.00 42.38           C
ANISOU  247  CG1 VAL A 369     5181   5317   5605    181    -18    402       C
ATOM    248  CG2 VAL A 369      16.119 -30.867 -11.764  1.00 32.87           C
ANISOU  248  CG2 VAL A 369     3957   4226   4305    123    -45    362       C
ATOM    249  N   SER A 370      16.034 -33.659 -15.447  1.00 18.46           N
ANISOU  249  N   SER A 370     2163   2209   2644    180     14    297       N
ATOM    250  CA  SER A 370      15.422 -34.566 -16.417  1.00 19.95           C
ANISOU  250  CA  SER A 370     2372   2327   2882    184     36    271       C
ATOM    251  C   SER A 370      14.796 -35.744 -15.702  1.00 15.87           C
ANISOU  251  C   SER A 370     1865   1756   2408    205     47    314       C
ATOM    252  O   SER A 370      15.296 -36.184 -14.666  1.00 20.31           O
ANISOU  252  O   SER A 370     2411   2331   2973    237     41    371       O
ATOM    253  CB  SER A 370      16.470 -35.119 -17.390  1.00 22.97           C
ANISOU  253  CB  SER A 370     2735   2699   3293    210     51    241       C
ATOM    254  OG  SER A 370      16.856 -34.156 -18.356  1.00 26.20           O
ANISOU  254  OG  SER A 370     3143   3143   3667    183     50    193       O
ATOM    255  N   ALA A 371      13.724 -36.272 -16.276  1.00 17.36           N
ANISOU  255  N   ALA A 371     2079   1884   2632    188     63    289       N
ATOM    256  CA  ALA A 371      13.175 -37.539 -15.814  1.00 20.83           C
ANISOU  256  CA  ALA A 371     2529   2258   3127    206     84    322       C
ATOM    257  C   ALA A 371      12.702 -38.333 -17.017  1.00 18.01           C
ANISOU  257  C   ALA A 371     2185   1835   2823    198    109    268       C
ATOM    258  O   ALA A 371      12.454 -37.774 -18.082  1.00 18.08           O
ANISOU  258  O   ALA A 371     2199   1856   2813    171    105    208       O
ATOM    259  CB  ALA A 371      12.039 -37.321 -14.814  1.00 20.94           C
ANISOU  259  CB  ALA A 371     2560   2273   3125    181     81    356       C
ATOM    260  N   GLU A 372      12.570 -39.643 -16.851  1.00 19.62           N
ANISOU  260  N   GLU A 372     2393   1969   3093    222    136    288       N
ATOM    261  CA  GLU A 372      12.314 -40.498 -18.001  1.00 19.90           C
ANISOU  261  CA  GLU A 372     2436   1940   3185    217    163    229       C
ATOM    262  C   GLU A 372      10.955 -40.273 -18.634  1.00 25.84           C
ANISOU  262  C   GLU A 372     3208   2677   3934    166    164    176       C
ATOM    263  O   GLU A 372      10.831 -40.252 -19.861  1.00 24.87           O
ANISOU  263  O   GLU A 372     3087   2550   3813    147    168    107       O
ATOM    264  CB  GLU A 372      12.490 -41.970 -17.639  1.00 23.45           C
ANISOU  264  CB  GLU A 372     2886   2308   3715    253    197    263       C
ATOM    265  CG  GLU A 372      13.926 -42.382 -17.503  1.00 35.39           C
ANISOU  265  CG  GLU A 372     4373   3826   5248    311    200    292       C
ATOM    266  CD  GLU A 372      14.085 -43.883 -17.519  1.00 39.45           C
ANISOU  266  CD  GLU A 372     4889   4244   5857    348    239    307       C
ATOM    267  OE1 GLU A 372      15.119 -44.354 -18.045  1.00 38.97           O
ANISOU  267  OE1 GLU A 372     4806   4169   5831    388    252    288       O
ATOM    268  OE2 GLU A 372      13.172 -44.583 -17.011  1.00 30.82           O
ANISOU  268  OE2 GLU A 372     3817   3087   4804    337    259    336       O
ATOM    269  N   THR A 373       9.939 -40.097 -17.794  1.00 17.85           N
ANISOU  269  N   THR A 373     2207   1661   2914    143    159    208       N
ATOM    270  CA  THR A 373       8.575 -39.969 -18.260  1.00 16.93           C
ANISOU  270  CA  THR A 373     2103   1528   2802     97    160    162       C
ATOM    271  C   THR A 373       7.864 -38.844 -17.523  1.00 18.80           C
ANISOU  271  C   THR A 373     2341   1817   2984     72    135    185       C
ATOM    272  O   THR A 373       8.370 -38.332 -16.520  1.00 17.43           O
ANISOU  272  O   THR A 373     2164   1684   2775     88    123    239       O
ATOM    273  CB  THR A 373       7.788 -41.261 -17.993  1.00 22.96           C
ANISOU  273  CB  THR A 373     2876   2209   3640     90    196    168       C
ATOM    274  OG1 THR A 373       7.654 -41.453 -16.578  1.00 22.53           O
ANISOU  274  OG1 THR A 373     2825   2146   3588    101    203    248       O
ATOM    275  CG2 THR A 373       8.511 -42.464 -18.597  1.00 23.00           C
ANISOU  275  CG2 THR A 373     2879   2150   3712    119    228    149       C
ATOM    276  N   THR A 374       6.682 -38.480 -18.008  1.00 15.91           N
ANISOU  276  N   THR A 374     1980   1453   2614     34    128    141       N
ATOM    277  CA  THR A 374       5.869 -37.470 -17.332  1.00 16.60           C
ANISOU  277  CA  THR A 374     2067   1581   2660     10    109    156       C
ATOM    278  C   THR A 374       5.630 -37.821 -15.861  1.00 16.01           C
ANISOU  278  C   THR A 374     1994   1494   2594     15    125    222       C
ATOM    279  O   THR A 374       5.799 -36.979 -14.978  1.00 16.71           O
ANISOU  279  O   THR A 374     2080   1632   2636     17    111    258       O
ATOM    280  CB  THR A 374       4.502 -37.306 -18.010  1.00 21.51           C
ANISOU  280  CB  THR A 374     2687   2193   3293    -27    103    102       C
ATOM    281  OG1 THR A 374       4.685 -36.895 -19.370  1.00 25.25           O
ANISOU  281  OG1 THR A 374     3160   2688   3745    -32     84     45       O
ATOM    282  CG2 THR A 374       3.666 -36.264 -17.274  1.00 22.14           C
ANISOU  282  CG2 THR A 374     2762   2311   3337    -47     87    117       C
ATOM    283  N   GLU A 375       5.220 -39.059 -15.599  1.00 17.80           N
ANISOU  283  N   GLU A 375     2227   1654   2881     14    158    238       N
ATOM    284  CA  GLU A 375       4.962 -39.478 -14.218  1.00 20.51           C
ANISOU  284  CA  GLU A 375     2577   1985   3232     17    178    307       C
ATOM    285  C   GLU A 375       6.205 -39.367 -13.344  1.00 18.68           C
ANISOU  285  C   GLU A 375     2343   1789   2967     58    169    374       C
ATOM    286  O   GLU A 375       6.100 -39.032 -12.166  1.00 17.77           O
ANISOU  286  O   GLU A 375     2229   1708   2815     56    167    426       O
ATOM    287  CB  GLU A 375       4.413 -40.912 -14.153  1.00 26.18           C
ANISOU  287  CB  GLU A 375     3304   2615   4028     10    221    316       C
ATOM    288  CG  GLU A 375       2.967 -41.051 -14.576  1.00 32.10           C
ANISOU  288  CG  GLU A 375     4050   3336   4810    -38    234    262       C
ATOM    289  CD  GLU A 375       2.460 -42.498 -14.489  1.00 50.31           C
ANISOU  289  CD  GLU A 375     6365   5550   7199    -50    283    268       C
ATOM    290  OE1 GLU A 375       3.081 -43.328 -13.778  1.00 41.75           O
ANISOU  290  OE1 GLU A 375     5295   4425   6144    -21    308    335       O
ATOM    291  OE2 GLU A 375       1.438 -42.805 -15.140  1.00 57.25           O
ANISOU  291  OE2 GLU A 375     7237   6398   8117    -90    295    206       O
ATOM    292  N   ASP A 376       7.380 -39.656 -13.904  1.00 16.71           N
ANISOU  292  N   ASP A 376     2088   1535   2727     93    163    371       N
ATOM    293  CA  ASP A 376       8.614 -39.521 -13.135  1.00 15.36           C
ANISOU  293  CA  ASP A 376     1907   1407   2524    134    149    430       C
ATOM    294  C   ASP A 376       8.888 -38.065 -12.790  1.00 17.13           C
ANISOU  294  C   ASP A 376     2120   1719   2668    122    115    425       C
ATOM    295  O   ASP A 376       9.391 -37.762 -11.703  1.00 18.06           O
ANISOU  295  O   ASP A 376     2232   1886   2745    136    103    478       O
ATOM    296  CB  ASP A 376       9.816 -40.072 -13.903  1.00 15.91           C
ANISOU  296  CB  ASP A 376     1965   1456   2623    174    151    417       C
ATOM    297  CG  ASP A 376       9.733 -41.568 -14.111  1.00 30.85           C
ANISOU  297  CG  ASP A 376     3866   3255   4600    194    189    429       C
ATOM    298  OD1 ASP A 376       9.196 -42.263 -13.222  1.00 27.03           O
ANISOU  298  OD1 ASP A 376     3396   2731   4143    194    210    484       O
ATOM    299  OD2 ASP A 376      10.200 -42.046 -15.166  1.00 37.02           O
ANISOU  299  OD2 ASP A 376     4642   4002   5422    207    200    380       O
ATOM    300  N   CYS A 377       8.580 -37.168 -13.724  1.00 16.02           N
ANISOU  300  N   CYS A 377     1979   1601   2508     95    100    361       N
ATOM    301  CA  CYS A 377       8.717 -35.732 -13.463  1.00 14.71           C
ANISOU  301  CA  CYS A 377     1806   1507   2276     79     73    350       C
ATOM    302  C   CYS A 377       7.764 -35.270 -12.369  1.00 17.54           C
ANISOU  302  C   CYS A 377     2168   1886   2608     53     75    373       C
ATOM    303  O   CYS A 377       8.145 -34.502 -11.485  1.00 16.15           O
ANISOU  303  O   CYS A 377     1986   1770   2382     53     61    397       O
ATOM    304  CB  CYS A 377       8.470 -34.905 -14.726  1.00 15.65           C
ANISOU  304  CB  CYS A 377     1926   1636   2383     57     59    283       C
ATOM    305  SG  CYS A 377       9.960 -34.614 -15.701  1.00 23.21           S
ANISOU  305  SG  CYS A 377     2873   2622   3326     80     47    259       S
ATOM    306  N   ILE A 378       6.520 -35.728 -12.429  1.00 15.29           N
ANISOU  306  N   ILE A 378     1894   1557   2359     30     94    361       N
ATOM    307  CA  ILE A 378       5.547 -35.339 -11.417  1.00 13.46           C
ANISOU  307  CA  ILE A 378     1663   1343   2107      3    102    378       C
ATOM    308  C   ILE A 378       6.041 -35.790 -10.044  1.00 18.34           C
ANISOU  308  C   ILE A 378     2283   1982   2703     21    112    452       C
ATOM    309  O   ILE A 378       5.990 -35.030  -9.071  1.00 17.28           O
ANISOU  309  O   ILE A 378     2144   1904   2516     10    105    470       O
ATOM    310  CB  ILE A 378       4.153 -35.903 -11.726  1.00 16.27           C
ANISOU  310  CB  ILE A 378     2024   1645   2512    -26    124    351       C
ATOM    311  CG1 ILE A 378       3.586 -35.225 -12.981  1.00 17.18           C
ANISOU  311  CG1 ILE A 378     2134   1761   2633    -45    105    279       C
ATOM    312  CG2 ILE A 378       3.215 -35.669 -10.544  1.00 20.22           C
ANISOU  312  CG2 ILE A 378     2524   2163   2995    -51    141    376       C
ATOM    313  CD1 ILE A 378       2.313 -35.885 -13.529  1.00 15.84           C
ANISOU  313  CD1 ILE A 378     1962   1541   2517    -71    123    242       C
ATOM    314  N   ALA A 379       6.551 -37.013  -9.977  1.00 17.07           N
ANISOU  314  N   ALA A 379     2128   1777   2581     51    128    494       N
ATOM    315  CA  ALA A 379       7.103 -37.541  -8.731  1.00 17.47           C
ANISOU  315  CA  ALA A 379     2181   1846   2610     76    134    575       C
ATOM    316  C   ALA A 379       8.265 -36.682  -8.226  1.00 22.81           C
ANISOU  316  C   ALA A 379     2840   2607   3219     95    101    592       C
ATOM    317  O   ALA A 379       8.395 -36.454  -7.023  1.00 19.82           O
ANISOU  317  O   ALA A 379     2459   2282   2790     95     96    639       O
ATOM    318  CB  ALA A 379       7.546 -38.987  -8.906  1.00 19.11           C
ANISOU  318  CB  ALA A 379     2397   1983   2882    111    156    617       C
ATOM    319  N   LYS A 380       9.111 -36.207  -9.136  1.00 17.74           N
ANISOU  319  N   LYS A 380     2185   1981   2575    109     79    550       N
ATOM    320  CA  LYS A 380      10.201 -35.327  -8.723  1.00 16.06           C
ANISOU  320  CA  LYS A 380     1951   1849   2302    120     49    556       C
ATOM    321  C   LYS A 380       9.686 -33.996  -8.166  1.00 17.71           C
ANISOU  321  C   LYS A 380     2158   2119   2453     81     39    528       C
ATOM    322  O   LYS A 380      10.253 -33.460  -7.225  1.00 19.32           O
ANISOU  322  O   LYS A 380     2348   2393   2600     82     23    551       O
ATOM    323  CB  LYS A 380      11.217 -35.103  -9.842  1.00 16.75           C
ANISOU  323  CB  LYS A 380     2023   1940   2403    139     34    516       C
ATOM    324  CG  LYS A 380      12.094 -36.327 -10.092  1.00 18.53           C
ANISOU  324  CG  LYS A 380     2240   2126   2674    188     41    551       C
ATOM    325  CD  LYS A 380      13.256 -36.024 -11.038  1.00 19.45           C
ANISOU  325  CD  LYS A 380     2335   2262   2794    207     28    512       C
ATOM    326  CE  LYS A 380      14.100 -37.283 -11.231  1.00 25.60           C
ANISOU  326  CE  LYS A 380     3101   2999   3626    260     38    546       C
ATOM    327  NZ  LYS A 380      15.342 -37.018 -11.999  1.00 36.25           N
ANISOU  327  NZ  LYS A 380     4421   4377   4975    281     27    513       N
ATOM    328  N   ILE A 381       8.605 -33.465  -8.726  1.00 15.41           N
ANISOU  328  N   ILE A 381     1877   1802   2176     46     47    477       N
ATOM    329  CA  ILE A 381       8.065 -32.225  -8.176  1.00 15.76           C
ANISOU  329  CA  ILE A 381     1918   1895   2174     12     42    450       C
ATOM    330  C   ILE A 381       7.504 -32.489  -6.765  1.00 21.43           C
ANISOU  330  C   ILE A 381     2641   2638   2864      1     58    496       C
ATOM    331  O   ILE A 381       7.726 -31.702  -5.835  1.00 18.53           O
ANISOU  331  O   ILE A 381     2264   2338   2437    -13     50    500       O
ATOM    332  CB  ILE A 381       7.019 -31.593  -9.107  1.00 15.34           C
ANISOU  332  CB  ILE A 381     1873   1809   2148    -16     45    389       C
ATOM    333  CG1 ILE A 381       7.685 -31.177 -10.423  1.00 14.71           C
ANISOU  333  CG1 ILE A 381     1790   1720   2078     -7     27    349       C
ATOM    334  CG2 ILE A 381       6.393 -30.373  -8.457  1.00 17.93           C
ANISOU  334  CG2 ILE A 381     2196   2178   2437    -47     44    364       C
ATOM    335  CD1 ILE A 381       6.691 -30.759 -11.497  1.00 15.72           C
ANISOU  335  CD1 ILE A 381     1926   1812   2234    -27     27    297       C
ATOM    336  N   MET A 382       6.805 -33.611  -6.605  1.00 17.12           N
ANISOU  336  N   MET A 382     2109   2038   2358      3     84    530       N
ATOM    337  CA  MET A 382       6.262 -33.981  -5.294  1.00 18.18           C
ANISOU  337  CA  MET A 382     2251   2192   2466     -8    106    581       C
ATOM    338  C   MET A 382       7.351 -34.078  -4.234  1.00 25.68           C
ANISOU  338  C   MET A 382     3193   3210   3356     17     89    642       C
ATOM    339  O   MET A 382       7.161 -33.622  -3.107  1.00 24.55           O
ANISOU  339  O   MET A 382     3048   3128   3153     -2     92    660       O
ATOM    340  CB  MET A 382       5.520 -35.315  -5.363  1.00 18.71           C
ANISOU  340  CB  MET A 382     2336   2182   2593     -6    139    616       C
ATOM    341  CG  MET A 382       4.257 -35.290  -6.187  1.00 16.72           C
ANISOU  341  CG  MET A 382     2087   1873   2394    -38    158    558       C
ATOM    342  SD  MET A 382       3.740 -36.979  -6.546  1.00 26.70           S
ANISOU  342  SD  MET A 382     3368   3036   3742    -32    195    589       S
ATOM    343  CE  MET A 382       3.318 -37.541  -4.897  1.00 27.12           C
ANISOU  343  CE  MET A 382     3435   3107   3764    -43    229    673       C
ATOM    344  N   ASN A 383       8.483 -34.684  -4.583  1.00 19.26           N
ANISOU  344  N   ASN A 383     2372   2388   2558     60     72    673       N
ATOM    345  CA  ASN A 383       9.524 -34.933  -3.584  1.00 25.04           C
ANISOU  345  CA  ASN A 383     3092   3184   3238     91     53    739       C
ATOM    346  C   ASN A 383      10.625 -33.874  -3.524  1.00 26.21           C
ANISOU  346  C   ASN A 383     3211   3416   3331     94     16    708       C
ATOM    347  O   ASN A 383      11.602 -34.028  -2.793  1.00 29.97           O
ANISOU  347  O   ASN A 383     3669   3954   3763    121     -6    755       O
ATOM    348  CB  ASN A 383      10.108 -36.346  -3.714  1.00 31.26           C
ANISOU  348  CB  ASN A 383     3885   3918   4075    142     59    807       C
ATOM    349  CG  ASN A 383      10.949 -36.527  -4.957  1.00 36.11           C
ANISOU  349  CG  ASN A 383     4485   4495   4740    172     45    772       C
ATOM    350  OD1 ASN A 383      11.479 -35.565  -5.516  1.00 31.11           O
ANISOU  350  OD1 ASN A 383     3833   3901   4086    162     23    714       O
ATOM    351  ND2 ASN A 383      11.089 -37.777  -5.395  1.00 41.90           N
ANISOU  351  ND2 ASN A 383     5228   5150   5542    207     63    806       N
ATOM    352  N   GLY A 384      10.461 -32.797  -4.289  1.00 22.97           N
ANISOU  352  N   GLY A 384     2795   3008   2924     65     10    629       N
ATOM    353  CA  GLY A 384      11.364 -31.660  -4.206  1.00 20.18           C
ANISOU  353  CA  GLY A 384     2416   2730   2521     56    -17    591       C
ATOM    354  C   GLY A 384      12.577 -31.690  -5.110  1.00 24.87           C
ANISOU  354  C   GLY A 384     2990   3323   3138     85    -38    576       C
ATOM    355  O   GLY A 384      13.380 -30.753  -5.096  1.00 24.15           O
ANISOU  355  O   GLY A 384     2875   3292   3010     74    -58    542       O
ATOM    356  N   GLU A 385      12.724 -32.752  -5.899  1.00 21.81           N
ANISOU  356  N   GLU A 385     2609   2866   2811    119    -29    597       N
ATOM    357  CA  GLU A 385      13.848 -32.834  -6.829  1.00 23.07           C
ANISOU  357  CA  GLU A 385     2747   3021   2996    146    -43    577       C
ATOM    358  C   GLU A 385      13.669 -31.890  -8.027  1.00 24.40           C
ANISOU  358  C   GLU A 385     2922   3171   3180    116    -40    500       C
ATOM    359  O   GLU A 385      14.634 -31.564  -8.715  1.00 23.80           O
ANISOU  359  O   GLU A 385     2826   3111   3107    124    -51    472       O
ATOM    360  CB  GLU A 385      14.079 -34.278  -7.292  1.00 27.73           C
ANISOU  360  CB  GLU A 385     3343   3542   3650    193    -31    618       C
ATOM    361  CG  GLU A 385      14.618 -35.193  -6.188  1.00 40.04           C
ANISOU  361  CG  GLU A 385     4892   5126   5196    236    -39    704       C
ATOM    362  CD  GLU A 385      14.662 -36.660  -6.595  1.00 52.94           C
ANISOU  362  CD  GLU A 385     6536   6674   6904    281    -19    748       C
ATOM    363  OE1 GLU A 385      14.733 -37.526  -5.694  1.00 56.55           O
ANISOU  363  OE1 GLU A 385     6998   7128   7362    313    -16    827       O
ATOM    364  OE2 GLU A 385      14.628 -36.948  -7.811  1.00 52.83           O
ANISOU  364  OE2 GLU A 385     6528   6596   6950    284     -3    702       O
ATOM    365  N   ALA A 386      12.428 -31.486  -8.283  1.00 18.59           N
ANISOU  365  N   ALA A 386     2211   2399   2455     81    -25    468       N
ATOM    366  CA  ALA A 386      12.128 -30.463  -9.288  1.00 14.34           C
ANISOU  366  CA  ALA A 386     1679   1847   1922     51    -25    403       C
ATOM    367  C   ALA A 386      11.045 -29.572  -8.711  1.00 14.85           C
ANISOU  367  C   ALA A 386     1756   1924   1962     13    -19    382       C
ATOM    368  O   ALA A 386      10.460 -29.900  -7.677  1.00 17.30           O
ANISOU  368  O   ALA A 386     2070   2246   2257      8    -10    414       O
ATOM    369  CB  ALA A 386      11.663 -31.093 -10.602  1.00 18.35           C
ANISOU  369  CB  ALA A 386     2204   2280   2487     59    -12    380       C
ATOM    370  N   ASP A 387      10.759 -28.452  -9.376  1.00 15.85           N
ANISOU  370  N   ASP A 387     1888   2048   2087    -14    -20    329       N
ATOM    371  CA  ASP A 387       9.744 -27.513  -8.882  1.00 15.26           C
ANISOU  371  CA  ASP A 387     1821   1982   1997    -48    -13    303       C
ATOM    372  C   ASP A 387       8.513 -27.367  -9.784  1.00 14.43           C
ANISOU  372  C   ASP A 387     1734   1817   1933    -60     -4    273       C
ATOM    373  O   ASP A 387       7.424 -27.134  -9.296  1.00 17.03           O
ANISOU  373  O   ASP A 387     2067   2138   2264    -77      7    265       O
ATOM    374  CB  ASP A 387      10.353 -26.123  -8.640  1.00 13.81           C
ANISOU  374  CB  ASP A 387     1624   1849   1775    -71    -21    268       C
ATOM    375  CG  ASP A 387      11.443 -26.140  -7.570  1.00 23.68           C
ANISOU  375  CG  ASP A 387     2849   3171   2976    -67    -33    291       C
ATOM    376  OD1 ASP A 387      11.259 -26.857  -6.563  1.00 24.01           O
ANISOU  376  OD1 ASP A 387     2888   3236   2997    -57    -30    333       O
ATOM    377  OD2 ASP A 387      12.489 -25.458  -7.740  1.00 21.73           O
ANISOU  377  OD2 ASP A 387     2584   2962   2709    -73    -44    269       O
ATOM    378  N   ALA A 388       8.679 -27.498 -11.096  1.00 13.35           N
ANISOU  378  N   ALA A 388     1604   1644   1824    -50    -10    254       N
ATOM    379  CA  ALA A 388       7.569 -27.148 -11.984  1.00 12.47           C
ANISOU  379  CA  ALA A 388     1506   1491   1741    -62     -9    221       C
ATOM    380  C   ALA A 388       7.696 -27.788 -13.346  1.00 13.60           C
ANISOU  380  C   ALA A 388     1658   1596   1914    -48    -13    210       C
ATOM    381  O   ALA A 388       8.794 -28.101 -13.778  1.00 12.55           O
ANISOU  381  O   ALA A 388     1521   1472   1777    -32    -17    215       O
ATOM    382  CB  ALA A 388       7.474 -25.613 -12.140  1.00 14.80           C
ANISOU  382  CB  ALA A 388     1802   1803   2017    -83    -15    187       C
ATOM    383  N   MET A 389       6.552 -27.963 -14.010  1.00 11.17           N
ANISOU  383  N   MET A 389     1359   1250   1636    -55    -13    189       N
ATOM    384  CA  MET A 389       6.493 -28.364 -15.418  1.00 11.80           C
ANISOU  384  CA  MET A 389     1447   1301   1737    -48    -19    166       C
ATOM    385  C   MET A 389       5.115 -28.013 -15.944  1.00 12.72           C
ANISOU  385  C   MET A 389     1566   1395   1871    -62    -27    138       C
ATOM    386  O   MET A 389       4.213 -27.759 -15.164  1.00 13.94           O
ANISOU  386  O   MET A 389     1715   1550   2033    -74    -21    140       O
ATOM    387  CB  MET A 389       6.693 -29.869 -15.552  1.00 10.86           C
ANISOU  387  CB  MET A 389     1327   1150   1650    -32     -7    179       C
ATOM    388  CG  MET A 389       5.539 -30.672 -14.982  1.00 12.67           C
ANISOU  388  CG  MET A 389     1555   1347   1912    -40      8    188       C
ATOM    389  SD  MET A 389       5.988 -32.426 -14.803  1.00 18.19           S
ANISOU  389  SD  MET A 389     2255   2003   2652    -18     31    218       S
ATOM    390  CE  MET A 389       6.291 -32.885 -16.517  1.00 16.45           C
ANISOU  390  CE  MET A 389     2040   1756   2456    -12     26    171       C
ATOM    391  N   SER A 390       4.945 -28.002 -17.267  1.00 10.45           N
ANISOU  391  N   SER A 390     1287   1095   1590    -61    -39    112       N
ATOM    392  CA  SER A 390       3.618 -27.780 -17.841  1.00 11.73           C
ANISOU  392  CA  SER A 390     1447   1242   1769    -70    -52     86       C
ATOM    393  C   SER A 390       2.984 -29.121 -18.195  1.00 14.91           C
ANISOU  393  C   SER A 390     1844   1613   2209    -73    -44     72       C
ATOM    394  O   SER A 390       3.666 -30.018 -18.702  1.00 17.30           O
ANISOU  394  O   SER A 390     2151   1902   2519    -64    -36     68       O
ATOM    395  CB  SER A 390       3.714 -26.898 -19.089  1.00 19.59           C
ANISOU  395  CB  SER A 390     2453   2249   2742    -69    -74     68       C
ATOM    396  OG  SER A 390       2.412 -26.490 -19.499  1.00 26.33           O
ANISOU  396  OG  SER A 390     3299   3095   3608    -74    -92     49       O
ATOM    397  N   LEU A 391       1.686 -29.259 -17.931  1.00 11.62           N
ANISOU  397  N   LEU A 391     1414   1182   1818    -85    -44     59       N
ATOM    398  CA  LEU A 391       0.999 -30.531 -18.121  1.00 12.40           C
ANISOU  398  CA  LEU A 391     1505   1248   1960    -95    -31     42       C
ATOM    399  C   LEU A 391      -0.317 -30.365 -18.868  1.00 17.53           C
ANISOU  399  C   LEU A 391     2138   1896   2626   -108    -50      2       C
ATOM    400  O   LEU A 391      -0.976 -29.334 -18.738  1.00 16.27           O
ANISOU  400  O   LEU A 391     1970   1756   2457   -109    -66     -1       O
ATOM    401  CB  LEU A 391       0.662 -31.166 -16.766  1.00 13.57           C
ANISOU  401  CB  LEU A 391     1647   1379   2132   -103     -1     70       C
ATOM    402  CG  LEU A 391       1.848 -31.606 -15.907  1.00 14.90           C
ANISOU  402  CG  LEU A 391     1826   1549   2288    -87     18    116       C
ATOM    403  CD1 LEU A 391       1.357 -32.121 -14.568  1.00 14.86           C
ANISOU  403  CD1 LEU A 391     1816   1533   2298    -97     45    149       C
ATOM    404  CD2 LEU A 391       2.658 -32.694 -16.634  1.00 13.84           C
ANISOU  404  CD2 LEU A 391     1700   1386   2174    -73     25    112       C
ATOM    405  N   ASP A 392      -0.712 -31.395 -19.620  1.00 17.96           N
ANISOU  405  N   ASP A 392     2187   1928   2709   -118    -47    -30       N
ATOM    406  CA  ASP A 392      -2.053 -31.412 -20.217  1.00 18.75           C
ANISOU  406  CA  ASP A 392     2264   2031   2830   -134    -65    -72       C
ATOM    407  C   ASP A 392      -3.114 -31.766 -19.162  1.00 17.19           C
ANISOU  407  C   ASP A 392     2044   1813   2673   -153    -42    -69       C
ATOM    408  O   ASP A 392      -2.780 -32.109 -18.026  1.00 17.36           O
ANISOU  408  O   ASP A 392     2073   1818   2703   -154    -11    -33       O
ATOM    409  CB  ASP A 392      -2.128 -32.320 -21.461  1.00 22.71           C
ANISOU  409  CB  ASP A 392     2764   2522   3343   -143    -72   -118       C
ATOM    410  CG  ASP A 392      -1.970 -33.808 -21.140  1.00 33.26           C
ANISOU  410  CG  ASP A 392     4101   3809   4727   -156    -33   -125       C
ATOM    411  OD1 ASP A 392      -1.580 -34.565 -22.058  1.00 40.14           O
ANISOU  411  OD1 ASP A 392     4979   4667   5605   -159    -30   -158       O
ATOM    412  OD2 ASP A 392      -2.236 -34.230 -19.997  1.00 28.75           O
ANISOU  412  OD2 ASP A 392     3526   3210   4187   -164     -3    -97       O
ATOM    413  N   GLY A 393      -4.388 -31.648 -19.528  1.00 18.59           N
ANISOU  413  N   GLY A 393     2193   1999   2872   -167    -58   -106       N
ATOM    414  CA  GLY A 393      -5.478 -31.863 -18.588  1.00 18.17           C
ANISOU  414  CA  GLY A 393     2112   1933   2857   -188    -35   -109       C
ATOM    415  C   GLY A 393      -5.437 -33.190 -17.854  1.00 20.71           C
ANISOU  415  C   GLY A 393     2439   2211   3218   -208     12    -96       C
ATOM    416  O   GLY A 393      -5.675 -33.248 -16.647  1.00 18.72           O
ANISOU  416  O   GLY A 393     2185   1951   2978   -217     43    -66       O
ATOM    417  N   GLY A 394      -5.140 -34.263 -18.581  1.00 19.16           N
ANISOU  417  N   GLY A 394     2251   1985   3045   -216     20   -119       N
ATOM    418  CA  GLY A 394      -5.084 -35.581 -17.975  1.00 24.26           C
ANISOU  418  CA  GLY A 394     2904   2578   3737   -234     67   -106       C
ATOM    419  C   GLY A 394      -4.039 -35.657 -16.880  1.00 22.63           C
ANISOU  419  C   GLY A 394     2726   2360   3513   -214     92    -37       C
ATOM    420  O   GLY A 394      -4.248 -36.285 -15.842  1.00 21.04           O
ANISOU  420  O   GLY A 394     2528   2131   3337   -226    131     -4       O
ATOM    421  N   PHE A 395      -2.899 -35.016 -17.112  1.00 19.00           N
ANISOU  421  N   PHE A 395     2286   1927   3007   -184     70    -16       N
ATOM    422  CA  PHE A 395      -1.842 -35.024 -16.108  1.00 19.57           C
ANISOU  422  CA  PHE A 395     2380   2000   3056   -163     87     46       C
ATOM    423  C   PHE A 395      -2.043 -33.996 -14.999  1.00 17.34           C
ANISOU  423  C   PHE A 395     2093   1757   2739   -162     86     77       C
ATOM    424  O   PHE A 395      -1.569 -34.198 -13.880  1.00 18.92           O
ANISOU  424  O   PHE A 395     2304   1959   2927   -157    109    127       O
ATOM    425  CB  PHE A 395      -0.463 -34.887 -16.758  1.00 17.87           C
ANISOU  425  CB  PHE A 395     2183   1796   2811   -133     70     53       C
ATOM    426  CG  PHE A 395       0.034 -36.162 -17.378  1.00 24.09           C
ANISOU  426  CG  PHE A 395     2979   2536   3637   -128     89     40       C
ATOM    427  CD1 PHE A 395       0.274 -37.276 -16.589  1.00 22.83           C
ANISOU  427  CD1 PHE A 395     2829   2330   3517   -125    127     79       C
ATOM    428  CD2 PHE A 395       0.275 -36.241 -18.741  1.00 21.21           C
ANISOU  428  CD2 PHE A 395     2615   2174   3270   -127     71    -10       C
ATOM    429  CE1 PHE A 395       0.745 -38.460 -17.159  1.00 23.96           C
ANISOU  429  CE1 PHE A 395     2980   2420   3706   -117    148     66       C
ATOM    430  CE2 PHE A 395       0.739 -37.415 -19.312  1.00 26.52           C
ANISOU  430  CE2 PHE A 395     3294   2801   3981   -123     93    -30       C
ATOM    431  CZ  PHE A 395       0.971 -38.522 -18.522  1.00 25.33           C
ANISOU  431  CZ  PHE A 395     3151   2595   3878   -117    132      6       C
ATOM    432  N   VAL A 396      -2.734 -32.889 -15.292  1.00 15.73           N
ANISOU  432  N   VAL A 396     1873   1586   2518   -167     60     47       N
ATOM    433  CA  VAL A 396      -3.115 -31.977 -14.217  1.00 15.91           C
ANISOU  433  CA  VAL A 396     1886   1639   2519   -172     67     65       C
ATOM    434  C   VAL A 396      -3.990 -32.725 -13.218  1.00 16.97           C
ANISOU  434  C   VAL A 396     2009   1752   2685   -198    107     77       C
ATOM    435  O   VAL A 396      -3.894 -32.532 -12.003  1.00 16.85           O
ANISOU  435  O   VAL A 396     1998   1754   2649   -202    130    113       O
ATOM    436  CB  VAL A 396      -3.864 -30.727 -14.747  1.00 17.11           C
ANISOU  436  CB  VAL A 396     2019   1819   2662   -170     36     28       C
ATOM    437  CG1 VAL A 396      -4.459 -29.920 -13.584  1.00 18.07           C
ANISOU  437  CG1 VAL A 396     2126   1963   2775   -179     52     35       C
ATOM    438  CG2 VAL A 396      -2.918 -29.863 -15.564  1.00 16.76           C
ANISOU  438  CG2 VAL A 396     1993   1797   2580   -146      2     27       C
ATOM    439  N   TYR A 397      -4.841 -33.596 -13.743  1.00 16.57           N
ANISOU  439  N   TYR A 397     1944   1668   2685   -219    118     46       N
ATOM    440  CA  TYR A 397      -5.662 -34.469 -12.902  1.00 17.66           C
ANISOU  440  CA  TYR A 397     2072   1777   2862   -249    163     57       C
ATOM    441  C   TYR A 397      -4.792 -35.373 -12.013  1.00 20.40           C
ANISOU  441  C   TYR A 397     2449   2098   3205   -242    198    121       C
ATOM    442  O   TYR A 397      -4.918 -35.361 -10.788  1.00 19.33           O
ANISOU  442  O   TYR A 397     2317   1974   3052   -252    227    162       O
ATOM    443  CB  TYR A 397      -6.583 -35.288 -13.797  1.00 21.36           C
ANISOU  443  CB  TYR A 397     2518   2211   3388   -275    167      4       C
ATOM    444  CG  TYR A 397      -7.363 -36.380 -13.111  1.00 27.89           C
ANISOU  444  CG  TYR A 397     3337   2995   4266   -311    219     12       C
ATOM    445  CD1 TYR A 397      -8.420 -36.083 -12.258  1.00 28.64           C
ANISOU  445  CD1 TYR A 397     3406   3106   4370   -337    244      8       C
ATOM    446  CD2 TYR A 397      -7.061 -37.714 -13.347  1.00 26.53           C
ANISOU  446  CD2 TYR A 397     3181   2762   4137   -320    247     20       C
ATOM    447  CE1 TYR A 397      -9.148 -37.097 -11.646  1.00 31.71           C
ANISOU  447  CE1 TYR A 397     3788   3455   4807   -376    297     16       C
ATOM    448  CE2 TYR A 397      -7.774 -38.727 -12.740  1.00 32.78           C
ANISOU  448  CE2 TYR A 397     3968   3508   4981   -357    299     29       C
ATOM    449  CZ  TYR A 397      -8.814 -38.417 -11.896  1.00 33.48           C
ANISOU  449  CZ  TYR A 397     4032   3616   5074   -386    324     29       C
ATOM    450  OH  TYR A 397      -9.519 -39.440 -11.302  1.00 32.74           O
ANISOU  450  OH  TYR A 397     3933   3474   5032   -426    382     40       O
ATOM    451  N   ILE A 398      -3.889 -36.129 -12.626  1.00 21.09           N
ANISOU  451  N   ILE A 398     2556   2152   3304   -224    194    131       N
ATOM    452  CA  ILE A 398      -2.998 -36.989 -11.847  1.00 21.52           C
ANISOU  452  CA  ILE A 398     2637   2181   3359   -209    222    197       C
ATOM    453  C   ILE A 398      -2.165 -36.177 -10.845  1.00 20.97           C
ANISOU  453  C   ILE A 398     2579   2166   3223   -187    212    248       C
ATOM    454  O   ILE A 398      -2.102 -36.511  -9.661  1.00 20.58           O
ANISOU  454  O   ILE A 398     2539   2120   3160   -190    240    303       O
ATOM    455  CB  ILE A 398      -2.099 -37.854 -12.755  1.00 22.77           C
ANISOU  455  CB  ILE A 398     2811   2296   3545   -186    218    193       C
ATOM    456  CG1 ILE A 398      -2.949 -38.852 -13.559  1.00 22.64           C
ANISOU  456  CG1 ILE A 398     2783   2220   3598   -215    238    142       C
ATOM    457  CG2 ILE A 398      -1.064 -38.619 -11.922  1.00 18.80           C
ANISOU  457  CG2 ILE A 398     2332   1771   3040   -159    241    268       C
ATOM    458  CD1 ILE A 398      -2.153 -39.693 -14.536  1.00 28.88           C
ANISOU  458  CD1 ILE A 398     3587   2968   4421   -197    238    123       C
ATOM    459  N   ALA A 399      -1.537 -35.099 -11.314  1.00 17.90           N
ANISOU  459  N   ALA A 399     2188   1821   2791   -167    173    229       N
ATOM    460  CA  ALA A 399      -0.726 -34.257 -10.444  1.00 19.22           C
ANISOU  460  CA  ALA A 399     2362   2042   2897   -151    162    265       C
ATOM    461  C   ALA A 399      -1.535 -33.723  -9.266  1.00 17.44           C
ANISOU  461  C   ALA A 399     2127   1849   2649   -175    182    275       C
ATOM    462  O   ALA A 399      -1.030 -33.627  -8.151  1.00 18.86           O
ANISOU  462  O   ALA A 399     2316   2063   2787   -170    193    322       O
ATOM    463  CB  ALA A 399      -0.113 -33.085 -11.239  1.00 15.21           C
ANISOU  463  CB  ALA A 399     1852   1571   2356   -134    121    232       C
ATOM    464  N   GLY A 400      -2.793 -33.367  -9.524  1.00 21.85           N
ANISOU  464  N   GLY A 400     2665   2403   3234   -200    187    228       N
ATOM    465  CA  GLY A 400      -3.665 -32.861  -8.478  1.00 15.61           C
ANISOU  465  CA  GLY A 400     1860   1642   2429   -224    211    227       C
ATOM    466  C   GLY A 400      -4.057 -33.923  -7.461  1.00 23.53           C
ANISOU  466  C   GLY A 400     2871   2625   3445   -245    259    273       C
ATOM    467  O   GLY A 400      -4.131 -33.644  -6.269  1.00 22.04           O
ANISOU  467  O   GLY A 400     2684   2474   3216   -257    281    302       O
ATOM    468  N   LYS A 401      -4.325 -35.137  -7.928  1.00 24.40           N
ANISOU  468  N   LYS A 401     2985   2675   3611   -254    278    278       N
ATOM    469  CA  LYS A 401      -4.566 -36.243  -7.010  1.00 26.08           C
ANISOU  469  CA  LYS A 401     3212   2858   3840   -271    327    333       C
ATOM    470  C   LYS A 401      -3.319 -36.459  -6.151  1.00 33.25           C
ANISOU  470  C   LYS A 401     4148   3789   4696   -242    327    409       C
ATOM    471  O   LYS A 401      -3.405 -36.939  -5.022  1.00 30.18           O
ANISOU  471  O   LYS A 401     3773   3407   4288   -253    362    467       O
ATOM    472  CB  LYS A 401      -4.935 -37.515  -7.769  1.00 27.19           C
ANISOU  472  CB  LYS A 401     3354   2920   4056   -283    348    321       C
ATOM    473  CG  LYS A 401      -6.323 -37.496  -8.385  1.00 37.79           C
ANISOU  473  CG  LYS A 401     4664   4245   5451   -321    356    250       C
ATOM    474  CD  LYS A 401      -7.387 -37.250  -7.323  1.00 40.26           C
ANISOU  474  CD  LYS A 401     4958   4581   5757   -357    395    254       C
ATOM    475  CE  LYS A 401      -8.538 -38.244  -7.439  1.00 54.89           C
ANISOU  475  CE  LYS A 401     6793   6379   7682   -402    440    231       C
ATOM    476  NZ  LYS A 401      -9.221 -38.186  -8.764  1.00 57.25           N
ANISOU  476  NZ  LYS A 401     7059   6662   8032   -413    413    148       N
ATOM    477  N   CYS A 402      -2.162 -36.075  -6.681  1.00 26.32           N
ANISOU  477  N   CYS A 402     3279   2930   3794   -206    286    410       N
ATOM    478  CA  CYS A 402      -0.907 -36.215  -5.943  1.00 24.81           C
ANISOU  478  CA  CYS A 402     3105   2768   3552   -175    278    478       C
ATOM    479  C   CYS A 402      -0.568 -34.985  -5.104  1.00 23.09           C
ANISOU  479  C   CYS A 402     2881   2635   3257   -175    260    479       C
ATOM    480  O   CYS A 402       0.506 -34.914  -4.508  1.00 24.71           O
ANISOU  480  O   CYS A 402     3096   2882   3412   -151    246    525       O
ATOM    481  CB  CYS A 402       0.250 -36.531  -6.898  1.00 23.68           C
ANISOU  481  CB  CYS A 402     2969   2601   3425   -136    248    478       C
ATOM    482  SG  CYS A 402       0.137 -38.147  -7.677  1.00 30.71           S
ANISOU  482  SG  CYS A 402     3873   3392   4404   -130    275    487       S
ATOM    483  N   GLY A 403      -1.475 -34.009  -5.069  1.00 22.79           N
ANISOU  483  N   GLY A 403     2825   2624   3212   -202    262    424       N
ATOM    484  CA  GLY A 403      -1.301 -32.851  -4.212  1.00 20.45           C
ANISOU  484  CA  GLY A 403     2521   2402   2848   -209    254    416       C
ATOM    485  C   GLY A 403      -0.669 -31.616  -4.839  1.00 21.41           C
ANISOU  485  C   GLY A 403     2633   2554   2947   -194    213    370       C
ATOM    486  O   GLY A 403      -0.505 -30.593  -4.168  1.00 24.91           O
ANISOU  486  O   GLY A 403     3069   3055   3340   -203    209    354       O
ATOM    487  N   LEU A 404      -0.303 -31.692  -6.114  1.00 18.41           N
ANISOU  487  N   LEU A 404     2254   2137   2602   -175    186    346       N
ATOM    488  CA  LEU A 404       0.263 -30.528  -6.787  1.00 16.26           C
ANISOU  488  CA  LEU A 404     1976   1890   2312   -163    150    305       C
ATOM    489  C   LEU A 404      -0.878 -29.644  -7.292  1.00 14.53           C
ANISOU  489  C   LEU A 404     1740   1662   2120   -181    148    244       C
ATOM    490  O   LEU A 404      -1.997 -30.127  -7.482  1.00 18.12           O
ANISOU  490  O   LEU A 404     2185   2084   2617   -197    166    228       O
ATOM    491  CB  LEU A 404       1.158 -30.969  -7.949  1.00 17.69           C
ANISOU  491  CB  LEU A 404     2167   2041   2515   -135    125    306       C
ATOM    492  CG  LEU A 404       2.302 -31.921  -7.573  1.00 16.70           C
ANISOU  492  CG  LEU A 404     2053   1916   2375   -110    126    366       C
ATOM    493  CD1 LEU A 404       3.141 -32.254  -8.815  1.00 15.49           C
ANISOU  493  CD1 LEU A 404     1904   1734   2248    -84    104    354       C
ATOM    494  CD2 LEU A 404       3.175 -31.313  -6.491  1.00 19.21           C
ANISOU  494  CD2 LEU A 404     2368   2303   2626   -105    118    394       C
ATOM    495  N   VAL A 405      -0.594 -28.362  -7.515  1.00 17.31           N
ANISOU  495  N   VAL A 405     2086   2041   2449   -177    127    211       N
ATOM    496  CA  VAL A 405      -1.624 -27.417  -7.938  1.00 16.22           C
ANISOU  496  CA  VAL A 405     1931   1896   2337   -187    123    159       C
ATOM    497  C   VAL A 405      -1.243 -26.729  -9.242  1.00 13.08           C
ANISOU  497  C   VAL A 405     1537   1483   1950   -168     87    132       C
ATOM    498  O   VAL A 405      -0.074 -26.451  -9.468  1.00 14.21           O
ANISOU  498  O   VAL A 405     1693   1641   2064   -155     70    144       O
ATOM    499  CB  VAL A 405      -1.847 -26.328  -6.868  1.00 17.73           C
ANISOU  499  CB  VAL A 405     2112   2131   2495   -203    139    140       C
ATOM    500  CG1 VAL A 405      -2.473 -26.947  -5.631  1.00 18.07           C
ANISOU  500  CG1 VAL A 405     2150   2192   2526   -226    179    161       C
ATOM    501  CG2 VAL A 405      -0.535 -25.654  -6.517  1.00 17.29           C
ANISOU  501  CG2 VAL A 405     2067   2114   2386   -196    125    149       C
ATOM    502  N   PRO A 406      -2.241 -26.455 -10.100  1.00 14.76           N
ANISOU  502  N   PRO A 406     1736   1670   2203   -168     76     97       N
ATOM    503  CA  PRO A 406      -1.972 -25.655 -11.295  1.00 12.22           C
ANISOU  503  CA  PRO A 406     1418   1339   1884   -150     42     75       C
ATOM    504  C   PRO A 406      -1.892 -24.180 -10.890  1.00 14.50           C
ANISOU  504  C   PRO A 406     1705   1650   2157   -151     41     56       C
ATOM    505  O   PRO A 406      -2.733 -23.714 -10.105  1.00 16.67           O
ANISOU  505  O   PRO A 406     1961   1932   2440   -163     61     38       O
ATOM    506  CB  PRO A 406      -3.188 -25.935 -12.181  1.00 13.86           C
ANISOU  506  CB  PRO A 406     1607   1519   2138   -150     31     47       C
ATOM    507  CG  PRO A 406      -4.313 -26.218 -11.200  1.00 16.62           C
ANISOU  507  CG  PRO A 406     1934   1871   2511   -171     62     38       C
ATOM    508  CD  PRO A 406      -3.661 -26.847  -9.982  1.00 14.74           C
ANISOU  508  CD  PRO A 406     1710   1649   2241   -183     93     76       C
ATOM    509  N   VAL A 407      -0.881 -23.463 -11.375  1.00 12.21           N
ANISOU  509  N   VAL A 407     1431   1367   1844   -140     23     59       N
ATOM    510  CA  VAL A 407      -0.676 -22.075 -10.955  1.00 14.50           C
ANISOU  510  CA  VAL A 407     1720   1670   2119   -144     27     40       C
ATOM    511  C   VAL A 407      -0.627 -21.082 -12.116  1.00 14.73           C
ANISOU  511  C   VAL A 407     1757   1676   2163   -129      3     27       C
ATOM    512  O   VAL A 407      -0.796 -19.879 -11.916  1.00 13.89           O
ANISOU  512  O   VAL A 407     1649   1566   2064   -130      8      7       O
ATOM    513  CB  VAL A 407       0.595 -21.921 -10.081  1.00 16.49           C
ANISOU  513  CB  VAL A 407     1982   1960   2325   -155     38     54       C
ATOM    514  CG1 VAL A 407       0.492 -22.828  -8.847  1.00 16.51           C
ANISOU  514  CG1 VAL A 407     1977   1989   2306   -169     62     75       C
ATOM    515  CG2 VAL A 407       1.863 -22.237 -10.882  1.00 15.23           C
ANISOU  515  CG2 VAL A 407     1839   1801   2145   -143     18     76       C
ATOM    516  N   LEU A 408      -0.391 -21.579 -13.324  1.00 13.43           N
ANISOU  516  N   LEU A 408     1603   1496   2001   -115    -21     39       N
ATOM    517  CA  LEU A 408      -0.414 -20.735 -14.520  1.00 11.51           C
ANISOU  517  CA  LEU A 408     1371   1235   1766    -99    -46     34       C
ATOM    518  C   LEU A 408      -1.079 -21.513 -15.641  1.00 13.98           C
ANISOU  518  C   LEU A 408     1680   1535   2097    -87    -70     33       C
ATOM    519  O   LEU A 408      -0.836 -22.708 -15.782  1.00 16.37           O
ANISOU  519  O   LEU A 408     1985   1841   2396    -91    -69     40       O
ATOM    520  CB  LEU A 408       1.020 -20.365 -14.941  1.00 12.73           C
ANISOU  520  CB  LEU A 408     1550   1399   1888   -100    -50     48       C
ATOM    521  CG  LEU A 408       1.822 -19.489 -13.973  1.00 14.66           C
ANISOU  521  CG  LEU A 408     1797   1660   2112   -116    -29     43       C
ATOM    522  CD1 LEU A 408       3.313 -19.739 -14.164  1.00 17.24           C
ANISOU  522  CD1 LEU A 408     2138   2009   2405   -122    -30     59       C
ATOM    523  CD2 LEU A 408       1.470 -17.994 -14.144  1.00 14.96           C
ANISOU  523  CD2 LEU A 408     1838   1674   2169   -114    -27     27       C
ATOM    524  N   ALA A 409      -1.930 -20.851 -16.427  1.00 14.11           N
ANISOU  524  N   ALA A 409     1688   1537   2134    -72    -93     23       N
ATOM    525  CA  ALA A 409      -2.457 -21.470 -17.645  1.00 12.59           C
ANISOU  525  CA  ALA A 409     1492   1343   1949    -61   -122     18       C
ATOM    526  C   ALA A 409      -1.655 -20.994 -18.846  1.00 12.39           C
ANISOU  526  C   ALA A 409     1495   1319   1894    -49   -145     34       C
ATOM    527  O   ALA A 409      -1.266 -19.827 -18.908  1.00 14.78           O
ANISOU  527  O   ALA A 409     1812   1614   2188    -42   -144     46       O
ATOM    528  CB  ALA A 409      -3.938 -21.108 -17.838  1.00 16.96           C
ANISOU  528  CB  ALA A 409     2015   1889   2540    -48   -139     -1       C
ATOM    529  N   GLU A 410      -1.414 -21.889 -19.801  1.00 12.45           N
ANISOU  529  N   GLU A 410     1509   1334   1885    -49   -160     33       N
ATOM    530  CA  GLU A 410      -0.878 -21.476 -21.095  1.00 11.31           C
ANISOU  530  CA  GLU A 410     1390   1198   1710    -39   -183     45       C
ATOM    531  C   GLU A 410      -2.062 -20.839 -21.811  1.00 12.86           C
ANISOU  531  C   GLU A 410     1572   1395   1920    -19   -217     42       C
ATOM    532  O   GLU A 410      -3.095 -21.485 -21.981  1.00 20.28           O
ANISOU  532  O   GLU A 410     2485   2341   2882    -18   -232     20       O
ATOM    533  CB  GLU A 410      -0.389 -22.683 -21.909  1.00 12.38           C
ANISOU  533  CB  GLU A 410     1532   1346   1825    -46   -188     35       C
ATOM    534  CG  GLU A 410       0.833 -23.390 -21.347  1.00 16.27           C
ANISOU  534  CG  GLU A 410     2037   1840   2307    -58   -158     40       C
ATOM    535  CD  GLU A 410       1.331 -24.527 -22.252  1.00 24.52           C
ANISOU  535  CD  GLU A 410     3088   2891   3338    -61   -160     26       C
ATOM    536  OE1 GLU A 410       2.315 -25.191 -21.868  1.00 22.46           O
ANISOU  536  OE1 GLU A 410     2833   2628   3074    -65   -137     31       O
ATOM    537  OE2 GLU A 410       0.727 -24.772 -23.327  1.00 21.15           O
ANISOU  537  OE2 GLU A 410     2659   2473   2904    -59   -184      8       O
ATOM    538  N   ASN A 411      -1.929 -19.572 -22.196  1.00 12.57           N
ANISOU  538  N   ASN A 411     1553   1350   1875     -4   -227     65       N
ATOM    539  CA  ASN A 411      -2.955 -18.907 -22.993  1.00 12.79           C
ANISOU  539  CA  ASN A 411     1570   1379   1912     23   -264     72       C
ATOM    540  C   ASN A 411      -2.542 -18.966 -24.457  1.00 19.05           C
ANISOU  540  C   ASN A 411     2387   2194   2657     29   -292     89       C
ATOM    541  O   ASN A 411      -1.373 -18.772 -24.775  1.00 16.88           O
ANISOU  541  O   ASN A 411     2146   1921   2348     19   -277    107       O
ATOM    542  CB  ASN A 411      -3.119 -17.436 -22.584  1.00 13.83           C
ANISOU  542  CB  ASN A 411     1706   1480   2067     40   -257     93       C
ATOM    543  CG  ASN A 411      -4.089 -17.243 -21.425  1.00 14.65           C
ANISOU  543  CG  ASN A 411     1773   1568   2224     43   -242     69       C
ATOM    544  OD1 ASN A 411      -4.637 -18.206 -20.886  1.00 17.02           O
ANISOU  544  OD1 ASN A 411     2045   1881   2540     30   -235     41       O
ATOM    545  ND2 ASN A 411      -4.298 -15.986 -21.031  1.00 17.61           N
ANISOU  545  ND2 ASN A 411     2150   1914   2628     59   -232     79       N
ATOM    546  N   TYR A 412      -3.500 -19.217 -25.341  1.00 15.59           N
ANISOU  546  N   TYR A 412     1930   1779   2214     44   -333     81       N
ATOM    547  CA  TYR A 412      -3.215 -19.363 -26.771  1.00 16.47           C
ANISOU  547  CA  TYR A 412     2062   1923   2271     49   -363     93       C
ATOM    548  C   TYR A 412      -3.744 -18.207 -27.625  1.00 18.56           C
ANISOU  548  C   TYR A 412     2335   2194   2521     82   -401    132       C
ATOM    549  O   TYR A 412      -3.469 -18.156 -28.824  1.00 21.04           O
ANISOU  549  O   TYR A 412     2673   2540   2782     87   -425    151       O
ATOM    550  CB  TYR A 412      -3.793 -20.686 -27.276  1.00 16.32           C
ANISOU  550  CB  TYR A 412     2017   1938   2247     36   -382     50       C
ATOM    551  CG  TYR A 412      -3.347 -21.858 -26.432  1.00 17.05           C
ANISOU  551  CG  TYR A 412     2102   2016   2361      7   -344     17       C
ATOM    552  CD1 TYR A 412      -4.264 -22.789 -25.955  1.00 19.57           C
ANISOU  552  CD1 TYR A 412     2382   2333   2719     -5   -343    -22       C
ATOM    553  CD2 TYR A 412      -2.012 -22.026 -26.103  1.00 17.74           C
ANISOU  553  CD2 TYR A 412     2219   2090   2431     -8   -307     27       C
ATOM    554  CE1 TYR A 412      -3.861 -23.865 -25.167  1.00 20.86           C
ANISOU  554  CE1 TYR A 412     2542   2478   2906    -29   -305    -43       C
ATOM    555  CE2 TYR A 412      -1.593 -23.106 -25.327  1.00 17.21           C
ANISOU  555  CE2 TYR A 412     2145   2009   2385    -28   -274      5       C
ATOM    556  CZ  TYR A 412      -2.524 -24.010 -24.853  1.00 24.20           C
ANISOU  556  CZ  TYR A 412     2997   2889   3310    -38   -273    -26       C
ATOM    557  OH  TYR A 412      -2.111 -25.073 -24.081  1.00 22.60           O
ANISOU  557  OH  TYR A 412     2790   2666   3129    -56   -238    -40       O
ATOM    558  N   ASN A 413      -4.485 -17.300 -27.043  1.00 15.95           N
ANISOU  558  N   ASN A 413     1987   1836   2239    106   -405    146       N
ATOM    559  CA  ASN A 413      -4.995 -16.151 -27.781  1.00 20.31           C
ANISOU  559  CA  ASN A 413     2547   2385   2787    145   -440    191       C
ATOM    560  C   ASN A 413      -4.309 -14.816 -27.406  1.00 23.14           C
ANISOU  560  C   ASN A 413     2941   2692   3159    153   -409    233       C
ATOM    561  O   ASN A 413      -3.932 -14.621 -26.289  1.00 25.76           O
ANISOU  561  O   ASN A 413     3273   2989   3526    136   -365    217       O
ATOM    562  CB  ASN A 413      -6.498 -16.023 -27.552  1.00 20.00           C
ATOM    563  CG  ASN A 413      -7.289 -17.255 -27.986  1.00 20.00           C
ATOM    564  OD1 ASN A 413      -6.858 -17.992 -28.798  1.00 20.00           O
ATOM    565  ND2 ASN A 413      -8.441 -17.443 -27.420  1.00 20.00           N
ATOM    566  N   LYS A 414      -4.193 -13.906 -28.355  1.00 23.10           N
ANISOU  566  N   LYS A 414     2966   2684   3125    178   -430    287       N
ATOM    567  CA  LYS A 414      -3.589 -12.599 -28.080  1.00 27.13           C
ANISOU  567  CA  LYS A 414     3513   3140   3657    184   -399    328       C
ATOM    568  C   LYS A 414      -4.565 -11.663 -27.367  1.00 32.39           C
ANISOU  568  C   LYS A 414     4152   3759   4397    219   -400    333       C
ATOM    569  O   LYS A 414      -5.769 -11.709 -27.612  1.00 32.62           O
ANISOU  569  O   LYS A 414     4142   3804   4448    254   -442    331       O
ATOM    570  CB  LYS A 414      -3.117 -11.937 -29.377  1.00 42.95           C
ANISOU  570  CB  LYS A 414     5562   5151   5605    197   -417    390       C
ATOM    571  CG  LYS A 414      -1.991 -12.668 -30.091  1.00 50.24           C
ANISOU  571  CG  LYS A 414     6518   6116   6456    161   -405    387       C
ATOM    572  CD  LYS A 414      -1.532 -11.876 -31.312  1.00 62.40           C
ANISOU  572  CD  LYS A 414     8106   7661   7941    172   -415    454       C
ATOM    573  CE  LYS A 414      -0.444 -12.605 -32.090  1.00 68.61           C
ANISOU  573  CE  LYS A 414     8922   8496   8652    135   -401    446       C
ATOM    574  NZ  LYS A 414      -0.938 -13.874 -32.697  1.00 72.24           N
ANISOU  574  NZ  LYS A 414     9354   9023   9069    132   -439    405       N
ATOM    575  N   SER A 415      -4.042 -10.813 -26.490  1.00 32.04           N
ANISOU  575  N   SER A 415     4123   3657   4393    209   -353    334       N
ATOM    576  CA  SER A 415      -4.867  -9.825 -25.793  1.00 38.40           C
ANISOU  576  CA  SER A 415     4906   4411   5274    241   -345    334       C
ATOM    577  C   SER A 415      -3.991  -8.915 -24.937  1.00 37.25           C
ANISOU  577  C   SER A 415     4788   4206   5160    217   -287    330       C
ATOM    578  O   SER A 415      -2.842  -9.243 -24.647  1.00 35.50           O
ANISOU  578  O   SER A 415     4590   3993   4906    173   -253    315       O
ATOM    579  CB  SER A 415      -5.914 -10.509 -24.913  1.00 37.22           C
ANISOU  579  CB  SER A 415     4697   4279   5167    244   -351    278       C
ATOM    580  OG  SER A 415      -5.372 -10.829 -23.646  1.00 35.44           O
ANISOU  580  OG  SER A 415     4467   4042   4957    203   -300    231       O
ATOM    581  N   ASP A 416      -4.538  -7.780 -24.516  1.00 35.31           N
ANISOU  581  N   ASP A 416     4535   3900   4981    247   -273    339       N
ATOM    582  CA  ASP A 416      -3.746  -6.800 -23.778  1.00 44.44           C
ANISOU  582  CA  ASP A 416     5718   4995   6171    223   -217    332       C
ATOM    583  C   ASP A 416      -3.570  -7.128 -22.298  1.00 39.16           C
ANISOU  583  C   ASP A 416     5023   4329   5528    186   -174    261       C
ATOM    584  O   ASP A 416      -2.714  -6.550 -21.627  1.00 46.38           O
ANISOU  584  O   ASP A 416     5957   5211   6455    153   -126    243       O
ATOM    585  CB  ASP A 416      -4.339  -5.399 -23.938  1.00 54.86           C
ANISOU  585  CB  ASP A 416     7045   6241   7558    269   -214    369       C
ATOM    586  CG  ASP A 416      -4.357  -4.942 -25.379  1.00 66.09           C
ANISOU  586  CG  ASP A 416     8502   7658   8950    305   -251    451       C
ATOM    587  OD1 ASP A 416      -3.263  -4.716 -25.942  1.00 68.73           O
ANISOU  587  OD1 ASP A 416     8887   7987   9240    277   -233    486       O
ATOM    588  OD2 ASP A 416      -5.463  -4.810 -25.946  1.00 69.31           O
ANISOU  588  OD2 ASP A 416     8887   8073   9376    361   -299    481       O
ATOM    589  N   ASN A 417      -4.378  -8.052 -21.790  1.00 28.51           N
ANISOU  589  N   ASN A 417     3628   3021   4185    189   -190    222       N
ATOM    590  CA  ASN A 417      -4.326  -8.409 -20.378  1.00 24.53           C
ANISOU  590  CA  ASN A 417     3098   2525   3699    155   -151    160       C
ATOM    591  C   ASN A 417      -4.004  -9.892 -20.202  1.00 23.95           C
ANISOU  591  C   ASN A 417     3013   2516   3572    123   -159    137       C
ATOM    592  O   ASN A 417      -4.400 -10.512 -19.215  1.00 23.73           O
ANISOU  592  O   ASN A 417     2951   2509   3555    107   -143     94       O
ATOM    593  CB  ASN A 417      -5.658  -8.074 -19.694  1.00 24.31           C
ANISOU  593  CB  ASN A 417     3021   2477   3739    186   -148    128       C
ATOM    594  CG  ASN A 417      -6.043  -6.600 -19.839  1.00 28.50           C
ANISOU  594  CG  ASN A 417     3560   2935   4335    224   -138    149       C
ATOM    595  OD1 ASN A 417      -6.873  -6.240 -20.680  1.00 32.67           O
ANISOU  595  OD1 ASN A 417     4078   3448   4887    276   -177    188       O
ATOM    596  ND2 ASN A 417      -5.440  -5.747 -19.024  1.00 27.10           N
ANISOU  596  ND2 ASN A 417     3398   2711   4187    200    -86    123       N
ATOM    597  N   CYS A 418      -3.264 -10.444 -21.159  1.00 22.86           N
ANISOU  597  N   CYS A 418     2904   2407   3376    113   -180    167       N
ATOM    598  CA  CYS A 418      -3.037 -11.889 -21.226  1.00 20.67           C
ANISOU  598  CA  CYS A 418     2615   2184   3053     91   -192    151       C
ATOM    599  C   CYS A 418      -2.584 -12.502 -19.899  1.00 22.36           C
ANISOU  599  C   CYS A 418     2815   2414   3265     54   -155    109       C
ATOM    600  O   CYS A 418      -3.176 -13.468 -19.426  1.00 20.05           O
ANISOU  600  O   CYS A 418     2493   2150   2977     48   -159     83       O
ATOM    601  CB  CYS A 418      -2.044 -12.233 -22.354  1.00 26.87           C
ANISOU  601  CB  CYS A 418     3439   2993   3778     80   -206    184       C
ATOM    602  SG  CYS A 418      -1.746 -14.032 -22.615  1.00 31.41           S
ANISOU  602  SG  CYS A 418     4003   3627   4304     58   -221    163       S
ATOM    603  N   GLU A 419      -1.541 -11.952 -19.285  1.00 17.44           N
ANISOU  603  N   GLU A 419     2214   1778   2636     26   -118    102       N
ATOM    604  CA  GLU A 419      -0.932 -12.654 -18.150  1.00 17.38           C
ANISOU  604  CA  GLU A 419     2195   1800   2610    -10    -89     70       C
ATOM    605  C   GLU A 419      -1.767 -12.609 -16.863  1.00 19.28           C
ANISOU  605  C   GLU A 419     2400   2038   2886    -13    -67     30       C
ATOM    606  O   GLU A 419      -1.458 -13.304 -15.886  1.00 19.42           O
ANISOU  606  O   GLU A 419     2407   2088   2885    -40    -47      7       O
ATOM    607  CB  GLU A 419       0.491 -12.146 -17.905  1.00 26.98           C
ANISOU  607  CB  GLU A 419     3437   3013   3801    -41    -60     71       C
ATOM    608  CG  GLU A 419       0.571 -10.683 -17.550  1.00 32.77           C
ANISOU  608  CG  GLU A 419     4181   3698   4571    -44    -33     62       C
ATOM    609  CD  GLU A 419       2.004 -10.235 -17.330  1.00 39.66           C
ANISOU  609  CD  GLU A 419     5076   4573   5420    -81     -3     57       C
ATOM    610  OE1 GLU A 419       2.204  -9.181 -16.694  1.00 38.22           O
ANISOU  610  OE1 GLU A 419     4896   4358   5267    -97     29     33       O
ATOM    611  OE2 GLU A 419       2.923 -10.950 -17.793  1.00 28.72           O
ANISOU  611  OE2 GLU A 419     3703   3222   3989    -95    -11     72       O
ATOM    612  N   ASP A 420      -2.825 -11.803 -16.864  1.00 18.31           N
ANISOU  612  N   ASP A 420     2261   1882   2815     14    -70     23       N
ATOM    613  CA  ASP A 420      -3.700 -11.695 -15.704  1.00 20.04           C
ANISOU  613  CA  ASP A 420     2444   2099   3071     12    -46    -18       C
ATOM    614  C   ASP A 420      -5.059 -12.313 -15.982  1.00 24.83           C
ANISOU  614  C   ASP A 420     3013   2717   3703     38    -73    -22       C
ATOM    615  O   ASP A 420      -5.953 -12.255 -15.139  1.00 25.16           O
ANISOU  615  O   ASP A 420     3020   2759   3781     40    -54    -57       O
ATOM    616  CB  ASP A 420      -3.893 -10.228 -15.306  1.00 21.85           C
ANISOU  616  CB  ASP A 420     2674   2277   3350     22    -18    -36       C
ATOM    617  CG  ASP A 420      -2.673  -9.646 -14.627  1.00 42.02           C
ANISOU  617  CG  ASP A 420     5253   4827   5886    -17     20    -53       C
ATOM    618  OD1 ASP A 420      -2.283  -8.512 -14.983  1.00 48.28           O
ANISOU  618  OD1 ASP A 420     6069   5571   6703    -12     31    -44       O
ATOM    619  OD2 ASP A 420      -2.108 -10.329 -13.741  1.00 43.42           O
ANISOU  619  OD2 ASP A 420     5424   5048   6024    -52     38    -76       O
ATOM    620  N   THR A 421      -5.202 -12.913 -17.161  1.00 19.43           N
ANISOU  620  N   THR A 421     2336   2048   3000     56   -115      8       N
ATOM    621  CA  THR A 421      -6.510 -13.365 -17.626  1.00 15.54           C
ANISOU  621  CA  THR A 421     1805   1566   2534     83   -147      4       C
ATOM    622  C   THR A 421      -6.438 -14.794 -18.202  1.00 16.21           C
ANISOU  622  C   THR A 421     1888   1692   2580     69   -172      9       C
ATOM    623  O   THR A 421      -6.369 -14.973 -19.406  1.00 17.75           O
ANISOU  623  O   THR A 421     2097   1897   2752     85   -210     35       O
ATOM    624  CB  THR A 421      -7.062 -12.365 -18.674  1.00 24.77           C
ANISOU  624  CB  THR A 421     2976   2705   3731    130   -182     34       C
ATOM    625  OG1 THR A 421      -6.791 -11.021 -18.238  1.00 25.01           O
ANISOU  625  OG1 THR A 421     3022   2686   3795    139   -152     35       O
ATOM    626  CG2 THR A 421      -8.552 -12.515 -18.838  1.00 26.38           C
ANISOU  626  CG2 THR A 421     3127   2917   3978    162   -209     19       C
ATOM    627  N   PRO A 422      -6.463 -15.815 -17.333  1.00 15.77           N
ANISOU  627  N   PRO A 422     1816   1659   2517     39   -149    -16       N
ATOM    628  CA  PRO A 422      -6.353 -17.199 -17.823  1.00 15.52           C
ANISOU  628  CA  PRO A 422     1785   1657   2457     24   -165    -14       C
ATOM    629  C   PRO A 422      -7.569 -17.680 -18.613  1.00 17.72           C
ANISOU  629  C   PRO A 422     2027   1949   2757     43   -203    -25       C
ATOM    630  O   PRO A 422      -8.710 -17.504 -18.175  1.00 17.82           O
ANISOU  630  O   PRO A 422     1997   1959   2814     52   -200    -49       O
ATOM    631  CB  PRO A 422      -6.185 -18.019 -16.539  1.00 16.36           C
ANISOU  631  CB  PRO A 422     1881   1776   2558    -10   -125    -34       C
ATOM    632  CG  PRO A 422      -6.741 -17.156 -15.457  1.00 22.13           C
ANISOU  632  CG  PRO A 422     2591   2495   3324     -9    -94    -57       C
ATOM    633  CD  PRO A 422      -6.453 -15.746 -15.863  1.00 17.96           C
ANISOU  633  CD  PRO A 422     2081   1937   2806     15   -102    -45       C
ATOM    634  N   GLU A 423      -7.309 -18.275 -19.777  1.00 14.39           N
ANISOU  634  N   GLU A 423     1619   1545   2303     46   -237    -12       N
ATOM    635  CA  GLU A 423      -8.345 -18.849 -20.626  1.00 17.58           C
ANISOU  635  CA  GLU A 423     1989   1971   2718     57   -276    -27       C
ATOM    636  C   GLU A 423      -8.895 -20.145 -20.026  1.00 17.65           C
ANISOU  636  C   GLU A 423     1966   1993   2746     26   -256    -62       C
ATOM    637  O   GLU A 423      -8.196 -20.847 -19.300  1.00 19.47           O
ANISOU  637  O   GLU A 423     2215   2219   2964     -3   -220    -64       O
ATOM    638  CB  GLU A 423      -7.759 -19.135 -22.008  1.00 16.81           C
ANISOU  638  CB  GLU A 423     1920   1894   2571     62   -312     -7       C
ATOM    639  CG  GLU A 423      -7.376 -17.868 -22.793  1.00 17.40           C
ANISOU  639  CG  GLU A 423     2025   1958   2626     94   -336     35       C
ATOM    640  CD  GLU A 423      -6.438 -18.145 -23.973  1.00 23.14           C
ANISOU  640  CD  GLU A 423     2793   2706   3292     89   -355     58       C
ATOM    641  OE1 GLU A 423      -5.851 -17.168 -24.490  1.00 20.86           O
ANISOU  641  OE1 GLU A 423     2539   2405   2981    106   -361     96       O
ATOM    642  OE2 GLU A 423      -6.278 -19.323 -24.385  1.00 19.08           O
ANISOU  642  OE2 GLU A 423     2277   2218   2754     68   -361     35       O
ATOM    643  N   ALA A 424     -10.142 -20.460 -20.360  1.00 16.15           N
ANISOU  643  N   ALA A 424     1728   1819   2588     33   -281    -89       N
ATOM    644  CA  ALA A 424     -10.824 -21.627 -19.800  1.00 19.42           C
ANISOU  644  CA  ALA A 424     2107   2241   3030      1   -259   -126       C
ATOM    645  C   ALA A 424     -10.777 -22.842 -20.732  1.00 20.76           C
ANISOU  645  C   ALA A 424     2277   2430   3180    -18   -280   -143       C
ATOM    646  O   ALA A 424     -11.208 -23.937 -20.363  1.00 23.13           O
ANISOU  646  O   ALA A 424     2554   2730   3503    -49   -258   -172       O
ATOM    647  CB  ALA A 424     -12.264 -21.272 -19.478  1.00 22.12           C
ANISOU  647  CB  ALA A 424     2389   2591   3427     14   -264   -155       C
ATOM    648  N   GLY A 425     -10.255 -22.650 -21.936  1.00 18.11           N
ANISOU  648  N   GLY A 425     1968   2110   2803     -1   -319   -126       N
ATOM    649  CA  GLY A 425     -10.154 -23.749 -22.883  1.00 15.38           C
ANISOU  649  CA  GLY A 425     1623   1785   2434    -20   -338   -149       C
ATOM    650  C   GLY A 425     -11.277 -23.715 -23.891  1.00 19.72           C
ANISOU  650  C   GLY A 425     2128   2373   2989     -6   -392   -175       C
ATOM    651  O   GLY A 425     -11.657 -22.652 -24.381  1.00 21.48           O
ANISOU  651  O   GLY A 425     2343   2612   3207     32   -430   -153       O
ATOM    652  N   TYR A 426     -11.819 -24.884 -24.206  1.00 15.20           N
ANISOU  652  N   TYR A 426     2030   2149   1597     57    352    172       N
ATOM    653  CA  TYR A 426     -12.920 -24.962 -25.158  1.00 14.28           C
ANISOU  653  CA  TYR A 426     1894   2020   1512     98    318    125       C
ATOM    654  C   TYR A 426     -13.860 -26.094 -24.760  1.00 12.27           C
ANISOU  654  C   TYR A 426     1638   1705   1318     97    316     57       C
ATOM    655  O   TYR A 426     -13.597 -26.835 -23.812  1.00 15.05           O
ANISOU  655  O   TYR A 426     2006   2031   1679     66    339     50       O
ATOM    656  CB  TYR A 426     -12.388 -25.179 -26.579  1.00 13.26           C
ANISOU  656  CB  TYR A 426     1751   1974   1315    169    280    138       C
ATOM    657  CG  TYR A 426     -11.616 -26.478 -26.723  1.00 18.02           C
ANISOU  657  CG  TYR A 426     2360   2617   1869    214    271    120       C
ATOM    658  CD1 TYR A 426     -10.228 -26.496 -26.688  1.00 21.59           C
ANISOU  658  CD1 TYR A 426     2809   3134   2259    216    278    169       C
ATOM    659  CD2 TYR A 426     -12.284 -27.688 -26.872  1.00 19.05           C
ANISOU  659  CD2 TYR A 426     2499   2707   2034    247    240     49       C
ATOM    660  CE1 TYR A 426      -9.519 -27.695 -26.808  1.00 23.53           C
ANISOU  660  CE1 TYR A 426     3059   3404   2477    258    256    141       C
ATOM    661  CE2 TYR A 426     -11.587 -28.889 -26.991  1.00 23.16           C
ANISOU  661  CE2 TYR A 426     3033   3255   2510    295    217     26       C
ATOM    662  CZ  TYR A 426     -10.208 -28.884 -26.964  1.00 21.21           C
ANISOU  662  CZ  TYR A 426     2787   3089   2183    313    235     72       C
ATOM    663  OH  TYR A 426      -9.513 -30.073 -27.077  1.00 25.31           O
ANISOU  663  OH  TYR A 426     3321   3638   2656    369    208     43       O
ATOM    664  N   PHE A 427     -14.980 -26.204 -25.464  1.00 12.14           N
ANISOU  664  N   PHE A 427     1603   1664   1346    125    284     12       N
ATOM    665  CA  PHE A 427     -15.959 -27.225 -25.130  1.00 12.79           C
ANISOU  665  CA  PHE A 427     1677   1687   1494    115    272    -43       C
ATOM    666  C   PHE A 427     -16.001 -28.279 -26.220  1.00 15.80           C
ANISOU  666  C   PHE A 427     2061   2083   1861    182    209    -81       C
ATOM    667  O   PHE A 427     -16.234 -27.969 -27.380  1.00 12.87           O
ANISOU  667  O   PHE A 427     1680   1739   1472    236    170    -91       O
ATOM    668  CB  PHE A 427     -17.326 -26.578 -24.904  1.00 12.27           C
ANISOU  668  CB  PHE A 427     1583   1573   1505     89    281    -67       C
ATOM    669  CG  PHE A 427     -17.312 -25.587 -23.776  1.00 12.12           C
ANISOU  669  CG  PHE A 427     1568   1539   1496     37    336    -39       C
ATOM    670  CD1 PHE A 427     -16.993 -24.262 -24.008  1.00 16.39           C
ANISOU  670  CD1 PHE A 427     2117   2099   2010     40    336     -6       C
ATOM    671  CD2 PHE A 427     -17.555 -25.998 -22.476  1.00 14.94           C
ANISOU  671  CD2 PHE A 427     1928   1863   1887    -14    380    -44       C
ATOM    672  CE1 PHE A 427     -16.928 -23.349 -22.952  1.00 15.33           C
ANISOU  672  CE1 PHE A 427     1997   1944   1883      0    373     15       C
ATOM    673  CE2 PHE A 427     -17.503 -25.094 -21.422  1.00 16.47           C
ANISOU  673  CE2 PHE A 427     2131   2045   2080    -51    426    -24       C
ATOM    674  CZ  PHE A 427     -17.194 -23.768 -21.662  1.00 16.57           C
ANISOU  674  CZ  PHE A 427     2157   2070   2068    -40    419      2       C
ATOM    675  N   ALA A 428     -15.714 -29.519 -25.844  1.00 12.12           N
ANISOU  675  N   ALA A 428     1612   1597   1395    182    192   -101       N
ATOM    676  CA  ALA A 428     -15.799 -30.628 -26.792  1.00 12.66           C
ANISOU  676  CA  ALA A 428     1692   1665   1453    251    117   -146       C
ATOM    677  C   ALA A 428     -17.265 -30.907 -27.078  1.00 14.48           C
ANISOU  677  C   ALA A 428     1901   1830   1772    244     75   -190       C
ATOM    678  O   ALA A 428     -18.066 -30.941 -26.152  1.00 15.45           O
ANISOU  678  O   ALA A 428     2004   1898   1968    174    103   -189       O
ATOM    679  CB  ALA A 428     -15.151 -31.862 -26.189  1.00 12.41           C
ANISOU  679  CB  ALA A 428     1691   1616   1408    247    100   -157       C
ATOM    680  N   VAL A 429     -17.601 -31.119 -28.352  1.00 13.23           N
ANISOU  680  N   VAL A 429     1742   1681   1604    318      7   -225       N
ATOM    681  CA  VAL A 429     -18.982 -31.357 -28.760  1.00 11.41           C
ANISOU  681  CA  VAL A 429     1490   1388   1458    317    -44   -265       C
ATOM    682  C   VAL A 429     -19.076 -32.541 -29.727  1.00 14.44           C
ANISOU  682  C   VAL A 429     1899   1751   1835    393   -148   -316       C
ATOM    683  O   VAL A 429     -18.092 -32.909 -30.368  1.00 16.36           O
ANISOU  683  O   VAL A 429     2175   2048   1992    470   -177   -325       O
ATOM    684  CB  VAL A 429     -19.628 -30.108 -29.426  1.00 12.81           C
ANISOU  684  CB  VAL A 429     1639   1582   1647    330    -32   -261       C
ATOM    685  CG1 VAL A 429     -19.759 -28.954 -28.434  1.00 14.26           C
ANISOU  685  CG1 VAL A 429     1799   1767   1851    258     52   -221       C
ATOM    686  CG2 VAL A 429     -18.853 -29.668 -30.672  1.00 13.81           C
ANISOU  686  CG2 VAL A 429     1783   1785   1679    414    -57   -254       C
ATOM    687  N   ALA A 430     -20.260 -33.143 -29.801  1.00 12.66           N
ANISOU  687  N   ALA A 430     1659   1449   1702    374   -207   -349       N
ATOM    688  CA  ALA A 430     -20.536 -34.194 -30.770  1.00 16.01           C
ANISOU  688  CA  ALA A 430     2112   1837   2135    447   -323   -402       C
ATOM    689  C   ALA A 430     -21.540 -33.645 -31.772  1.00 16.97           C
ANISOU  689  C   ALA A 430     2210   1945   2294    482   -363   -428       C
ATOM    690  O   ALA A 430     -22.653 -33.290 -31.404  1.00 17.50           O
ANISOU  690  O   ALA A 430     2232   1966   2452    418   -348   -423       O
ATOM    691  CB  ALA A 430     -21.086 -35.426 -30.079  1.00 16.93           C
ANISOU  691  CB  ALA A 430     2233   1864   2334    391   -381   -414       C
ATOM    692  N   VAL A 431     -21.122 -33.556 -33.030  1.00 14.34           N
ANISOU  692  N   VAL A 431     1904   1659   1884    587   -412   -455       N
ATOM    693  CA  VAL A 431     -21.903 -32.894 -34.069  1.00 16.29           C
ANISOU  693  CA  VAL A 431     2136   1907   2148    629   -446   -475       C
ATOM    694  C   VAL A 431     -22.497 -33.945 -34.989  1.00 14.09           C
ANISOU  694  C   VAL A 431     1886   1567   1899    700   -577   -538       C
ATOM    695  O   VAL A 431     -21.817 -34.899 -35.381  1.00 20.30           O
ANISOU  695  O   VAL A 431     2722   2363   2629    774   -644   -569       O
ATOM    696  CB  VAL A 431     -21.018 -31.947 -34.919  1.00 17.32           C
ANISOU  696  CB  VAL A 431     2277   2142   2161    699   -411   -453       C
ATOM    697  CG1 VAL A 431     -21.863 -31.155 -35.918  1.00 19.16           C
ANISOU  697  CG1 VAL A 431     2495   2371   2413    733   -441   -468       C
ATOM    698  CG2 VAL A 431     -20.214 -31.000 -34.016  1.00 16.24           C
ANISOU  698  CG2 VAL A 431     2122   2063   1985    634   -297   -387       C
ATOM    699  N   VAL A 432     -23.768 -33.761 -35.339  1.00 16.59           N
ANISOU  699  N   VAL A 432     2174   1822   2308    682   -622   -558       N
ATOM    700  CA  VAL A 432     -24.432 -34.621 -36.314  1.00 18.87           C
ANISOU  700  CA  VAL A 432     2490   2046   2632    750   -757   -617       C
ATOM    701  C   VAL A 432     -25.149 -33.761 -37.347  1.00 20.06           C
ANISOU  701  C   VAL A 432     2625   2210   2786    785   -774   -631       C
ATOM    702  O   VAL A 432     -25.284 -32.546 -37.178  1.00 17.71           O
ANISOU  702  O   VAL A 432     2290   1948   2490    756   -693   -601       O
ATOM    703  CB  VAL A 432     -25.469 -35.543 -35.656  1.00 19.48           C
ANISOU  703  CB  VAL A 432     2545   2014   2844    671   -820   -623       C
ATOM    704  CG1 VAL A 432     -24.800 -36.496 -34.660  1.00 21.20           C
ANISOU  704  CG1 VAL A 432     2784   2213   3057    626   -815   -606       C
ATOM    705  CG2 VAL A 432     -26.561 -34.714 -34.980  1.00 19.12           C
ANISOU  705  CG2 VAL A 432     2420   1945   2897    568   -750   -590       C
ATOM    706  N   LYS A 433     -25.629 -34.391 -38.417  1.00 19.71           N
ANISOU  706  N   LYS A 433     2612   2146   2730    820   -875   -668       N
ATOM    707  CA  LYS A 433     -26.427 -33.673 -39.393  1.00 20.93           C
ANISOU  707  CA  LYS A 433     2756   2305   2891    833   -896   -681       C
ATOM    708  C   LYS A 433     -27.880 -33.594 -38.920  1.00 20.83           C
ANISOU  708  C   LYS A 433     2683   2199   3034    762   -921   -684       C
ATOM    709  O   LYS A 433     -28.425 -34.568 -38.398  1.00 25.55           O
ANISOU  709  O   LYS A 433     3268   2716   3724    721   -983   -693       O
ATOM    710  CB  LYS A 433     -26.330 -34.354 -40.766  1.00 22.41           C
ANISOU  710  CB  LYS A 433     3008   2511   2996    902   -988   -728       C
ATOM    711  CG  LYS A 433     -24.925 -34.286 -41.365  1.00 30.52           C
ANISOU  711  CG  LYS A 433     4087   3646   3862    981   -952   -728       C
ATOM    712  CD  LYS A 433     -24.840 -34.878 -42.766  1.00 31.25           C
ANISOU  712  CD  LYS A 433     4248   3760   3867   1057  -1031   -787       C
ATOM    713  CE  LYS A 433     -24.998 -36.387 -42.751  1.00 40.68           C
ANISOU  713  CE  LYS A 433     5485   4885   5086   1063  -1137   -840       C
ATOM    714  NZ  LYS A 433     -23.875 -37.061 -42.034  1.00 39.53           N
ANISOU  714  NZ  LYS A 433     5361   4769   4888   1077  -1114   -834       N
ATOM    715  N   LYS A 434     -28.500 -32.434 -39.094  1.00 19.34           N
ANISOU  715  N   LYS A 434     2454   2020   2875    747   -878   -674       N
ATOM    716  CA  LYS A 434     -29.888 -32.263 -38.673  1.00 26.62           C
ANISOU  716  CA  LYS A 434     3309   2865   3940    685   -896   -678       C
ATOM    717  C   LYS A 434     -30.791 -33.244 -39.416  1.00 32.17           C
ANISOU  717  C   LYS A 434     4024   3502   4697    688  -1023   -714       C
ATOM    718  O   LYS A 434     -31.828 -33.668 -38.902  1.00 35.15           O
ANISOU  718  O   LYS A 434     4347   3800   5208    632  -1066   -714       O
ATOM    719  CB  LYS A 434     -30.361 -30.825 -38.902  1.00 28.94           C
ANISOU  719  CB  LYS A 434     3567   3187   4240    681   -839   -669       C
ATOM    720  CG  LYS A 434     -31.785 -30.572 -38.430  1.00 33.43           C
ANISOU  720  CG  LYS A 434     4058   3690   4955    623   -848   -677       C
ATOM    721  CD  LYS A 434     -32.184 -29.121 -38.602  1.00 34.52           C
ANISOU  721  CD  LYS A 434     4166   3859   5090    622   -793   -671       C
ATOM    722  CE  LYS A 434     -33.535 -28.862 -37.955  1.00 50.85           C
ANISOU  722  CE  LYS A 434     6143   5874   7302    568   -788   -680       C
ATOM    723  NZ  LYS A 434     -33.880 -27.413 -37.918  1.00 55.06           N
ANISOU  723  NZ  LYS A 434     6648   6440   7833    566   -729   -677       N
ATOM    724  N   SER A 435     -30.380 -33.613 -40.624  1.00 30.33           N
ANISOU  724  N   SER A 435     3861   3303   4361    753  -1086   -744       N
ATOM    725  CA  SER A 435     -31.182 -34.486 -41.470  1.00 34.92           C
ANISOU  725  CA  SER A 435     4467   3825   4977    763  -1213   -787       C
ATOM    726  C   SER A 435     -31.191 -35.925 -40.961  1.00 37.99           C
ANISOU  726  C   SER A 435     4868   4146   5420    738  -1298   -796       C
ATOM    727  O   SER A 435     -32.034 -36.728 -41.365  1.00 37.64           O
ANISOU  727  O   SER A 435     4827   4030   5444    724  -1415   -823       O
ATOM    728  CB  SER A 435     -30.669 -34.450 -42.909  1.00 39.69           C
ANISOU  728  CB  SER A 435     5149   4486   5447    845  -1248   -825       C
ATOM    729  OG  SER A 435     -29.345 -34.935 -42.992  1.00 37.62           O
ANISOU  729  OG  SER A 435     4947   4284   5065    898  -1230   -830       O
ATOM    730  N   ALA A 436     -30.254 -36.253 -40.076  1.00 35.72           N
ANISOU  730  N   ALA A 436     4589   3877   5103    731  -1248   -771       N
ATOM    731  CA  ALA A 436     -30.108 -37.627 -39.595  1.00 36.68           C
ANISOU  731  CA  ALA A 436     4734   3938   5262    711  -1334   -777       C
ATOM    732  C   ALA A 436     -31.259 -38.026 -38.685  1.00 47.56           C
ANISOU  732  C   ALA A 436     6038   5214   6818    621  -1377   -746       C
ATOM    733  O   ALA A 436     -31.582 -37.323 -37.728  1.00 44.63           O
ANISOU  733  O   ALA A 436     5598   4831   6528    565  -1286   -709       O
ATOM    734  CB  ALA A 436     -28.778 -37.813 -38.888  1.00 40.33           C
ANISOU  734  CB  ALA A 436     5228   4451   5645    728  -1266   -758       C
ATOM    735  N   SER A 437     -31.859 -39.174 -38.980  1.00 57.07           N
ANISOU  735  N   SER A 437     7255   6343   8084    606  -1520   -762       N
ATOM    736  CA  SER A 437     -33.002 -39.660 -38.219  1.00 63.56           C
ANISOU  736  CA  SER A 437     7999   7068   9083    520  -1580   -717       C
ATOM    737  C   SER A 437     -32.591 -40.565 -37.056  1.00 61.40           C
ANISOU  737  C   SER A 437     7726   6748   8854    465  -1584   -667       C
ATOM    738  O   SER A 437     -31.763 -41.462 -37.216  1.00 58.82           O
ANISOU  738  O   SER A 437     7469   6430   8449    508  -1648   -682       O
ATOM    739  CB  SER A 437     -33.964 -40.410 -39.121  1.00  0.00           C
ATOM    740  OG  SER A 437     -35.039 -40.930 -38.335  1.00  0.00           O
ATOM    741  N   ASP A 438     -33.171 -40.305 -35.886  1.00 55.08           N
ANISOU  741  N   ASP A 438     6850   5912   8166    353  -1506   -614       N
ATOM    742  CA  ASP A 438     -33.068 -41.205 -34.739  1.00 55.58           C
ANISOU  742  CA  ASP A 438     6903   5941   8275    254  -1504   -553       C
ATOM    743  C   ASP A 438     -31.697 -41.227 -34.056  1.00 50.69           C
ANISOU  743  C   ASP A 438     6338   5366   7556    258  -1426   -558       C
ATOM    744  O   ASP A 438     -31.448 -42.064 -33.193  1.00 61.40           O
ANISOU  744  O   ASP A 438     7701   6699   8928    190  -1435   -511       O
ATOM    745  CB  ASP A 438     -33.447 -42.621 -35.134  1.00  0.00           C
ATOM    746  CG  ASP A 438     -34.833 -42.625 -35.776  1.00  0.00           C
ATOM    747  OD1 ASP A 438     -35.738 -41.969 -35.195  1.00  0.00           O
ATOM    748  OD2 ASP A 438     -34.972 -43.284 -36.841  1.00  0.00           O
ATOM    749  N   LEU A 439     -30.817 -40.307 -34.430  1.00 35.22           N
ANISOU  749  N   LEU A 439     4417   3477   5490    341  -1342   -604       N
ATOM    750  CA  LEU A 439     -29.453 -40.311 -33.910  1.00 32.03           C
ANISOU  750  CA  LEU A 439     4062   3135   4971    364  -1262   -599       C
ATOM    751  C   LEU A 439     -29.354 -39.499 -32.617  1.00 25.00           C
ANISOU  751  C   LEU A 439     3103   2317   4077    261  -1085   -534       C
ATOM    752  O   LEU A 439     -29.645 -38.304 -32.615  1.00 28.79           O
ANISOU  752  O   LEU A 439     3533   2860   4547    256   -980   -525       O
ATOM    753  CB  LEU A 439     -28.511 -39.737 -34.967  1.00 39.06           C
ANISOU  753  CB  LEU A 439     5015   4100   5724    504  -1245   -654       C
ATOM    754  CG  LEU A 439     -27.006 -39.932 -34.817  1.00 37.36           C
ANISOU  754  CG  LEU A 439     4865   3954   5377    563  -1203   -663       C
ATOM    755  CD1 LEU A 439     -26.667 -41.412 -34.663  1.00 35.08           C
ANISOU  755  CD1 LEU A 439     4627   3617   5084    562  -1319   -666       C
ATOM    756  CD2 LEU A 439     -26.303 -39.348 -36.034  1.00 34.42           C
ANISOU  756  CD2 LEU A 439     4529   3691   4858    675  -1182   -697       C
ATOM    757  N   THR A 440     -28.956 -40.147 -31.519  1.00 26.60           N
ANISOU  757  N   THR A 440     3310   2508   4289    182  -1061   -490       N
ATOM    758  CA  THR A 440     -28.743 -39.447 -30.252  1.00 25.99           C
ANISOU  758  CA  THR A 440     3180   2500   4195     95   -899   -432       C
ATOM    759  C   THR A 440     -27.520 -40.012 -29.529  1.00 22.41           C
ANISOU  759  C   THR A 440     2787   2060   3669     87   -874   -418       C
ATOM    760  O   THR A 440     -26.947 -41.016 -29.953  1.00 26.12           O
ANISOU  760  O   THR A 440     3331   2480   4113    141   -988   -451       O
ATOM    761  CB  THR A 440     -29.964 -39.553 -29.302  1.00 31.11           C
ANISOU  761  CB  THR A 440     3732   3125   4965    -38   -871   -367       C
ATOM    762  OG1 THR A 440     -29.916 -40.798 -28.599  1.00 34.65           O
ANISOU  762  OG1 THR A 440     4197   3510   5460   -114   -942   -328       O
ATOM    763  CG2 THR A 440     -31.278 -39.469 -30.073  1.00 36.71           C
ANISOU  763  CG2 THR A 440     4387   3790   5772    -36   -950   -381       C
ATOM    764  N   TRP A 441     -27.132 -39.368 -28.433  1.00 19.61           N
ANISOU  764  N   TRP A 441     2401   1769   3281     24   -730   -372       N
ATOM    765  CA  TRP A 441     -26.025 -39.862 -27.619  1.00 22.35           C
ANISOU  765  CA  TRP A 441     2798   2128   3567      4   -699   -353       C
ATOM    766  C   TRP A 441     -26.252 -41.313 -27.204  1.00 29.15           C
ANISOU  766  C   TRP A 441     3682   2897   4496    -56   -817   -333       C
ATOM    767  O   TRP A 441     -25.310 -42.101 -27.116  1.00 27.89           O
ANISOU  767  O   TRP A 441     3596   2714   4286    -25   -872   -349       O
ATOM    768  CB  TRP A 441     -25.865 -38.989 -26.375  1.00 24.72           C
ANISOU  768  CB  TRP A 441     3050   2496   3846    -73   -537   -299       C
ATOM    769  CG  TRP A 441     -24.732 -39.400 -25.498  1.00 23.82           C
ANISOU  769  CG  TRP A 441     2986   2396   3669    -96   -498   -277       C
ATOM    770  CD1 TRP A 441     -24.815 -40.030 -24.290  1.00 22.99           C
ANISOU  770  CD1 TRP A 441     2869   2264   3601   -198   -480   -224       C
ATOM    771  CD2 TRP A 441     -23.334 -39.208 -25.757  1.00 22.85           C
ANISOU  771  CD2 TRP A 441     2930   2320   3433    -15   -474   -305       C
ATOM    772  NE1 TRP A 441     -23.551 -40.242 -23.781  1.00 28.55           N
ANISOU  772  NE1 TRP A 441     3635   2989   4224   -183   -448   -222       N
ATOM    773  CE2 TRP A 441     -22.627 -39.747 -24.664  1.00 22.51           C
ANISOU  773  CE2 TRP A 441     2915   2270   3368    -72   -444   -271       C
ATOM    774  CE3 TRP A 441     -22.614 -38.631 -26.808  1.00 25.36           C
ANISOU  774  CE3 TRP A 441     3281   2691   3664     97   -474   -349       C
ATOM    775  CZ2 TRP A 441     -21.229 -39.726 -24.592  1.00 22.27           C
ANISOU  775  CZ2 TRP A 441     2943   2281   3236    -18   -416   -284       C
ATOM    776  CZ3 TRP A 441     -21.225 -38.619 -26.736  1.00 26.36           C
ANISOU  776  CZ3 TRP A 441     3460   2868   3688    149   -444   -355       C
ATOM    777  CH2 TRP A 441     -20.552 -39.162 -25.639  1.00 18.49           C
ANISOU  777  CH2 TRP A 441     2489   1860   2676     93   -416   -325       C
ATOM    778  N   ASP A 442     -27.512 -41.659 -26.964  1.00 30.77           N
ANISOU  778  N   ASP A 442     3823   3050   4818   -143   -862   -295       N
ATOM    779  CA  ASP A 442     -27.857 -42.958 -26.398  1.00 28.70           C
ANISOU  779  CA  ASP A 442     3568   2701   4635   -230   -967   -253       C
ATOM    780  C   ASP A 442     -27.728 -44.121 -27.370  1.00 32.50           C
ANISOU  780  C   ASP A 442     4128   3098   5122   -153  -1152   -298       C
ATOM    781  O   ASP A 442     -27.683 -45.271 -26.944  1.00 36.92           O
ANISOU  781  O   ASP A 442     4715   3620   5693   -187  -1222   -255       O
ATOM    782  CB  ASP A 442     -29.274 -42.929 -25.829  1.00 38.50           C
ANISOU  782  CB  ASP A 442     4701   3930   5996   -351   -951   -184       C
ATOM    783  CG  ASP A 442     -29.440 -41.893 -24.745  1.00 47.82           C
ANISOU  783  CG  ASP A 442     5804   5209   7157   -417   -765   -133       C
ATOM    784  OD1 ASP A 442     -28.503 -41.730 -23.934  1.00 49.91           O
ANISOU  784  OD1 ASP A 442     6102   5517   7346   -429   -675   -118       O
ATOM    785  OD2 ASP A 442     -30.502 -41.237 -24.708  1.00 49.87           O
ANISOU  785  OD2 ASP A 442     5970   5503   7475   -452   -713   -111       O
ATOM    786  N   ASN A 443     -27.690 -43.837 -28.669  1.00 31.42           N
ANISOU  786  N   ASN A 443     4024   2959   4956    -34  -1215   -372       N
ATOM    787  CA  ASN A 443     -27.589 -44.915 -29.647  1.00 32.89           C
ANISOU  787  CA  ASN A 443     4278   3098   5121     64  -1371   -403       C
ATOM    788  C   ASN A 443     -26.432 -44.768 -30.632  1.00 29.65           C
ANISOU  788  C   ASN A 443     3949   2730   4585    220  -1396   -486       C
ATOM    789  O   ASN A 443     -26.560 -45.114 -31.803  1.00 36.95           O
ANISOU  789  O   ASN A 443     4905   3645   5487    326  -1503   -529       O
ATOM    790  CB  ASN A 443     -28.919 -45.126 -30.385  1.00 39.52           C
ANISOU  790  CB  ASN A 443     5073   3888   6053     63  -1464   -392       C
ATOM    791  CG  ASN A 443     -29.309 -43.947 -31.255  1.00 45.52           C
ANISOU  791  CG  ASN A 443     5802   4682   6812    121  -1424   -445       C
ATOM    792  OD1 ASN A 443     -28.464 -43.162 -31.684  1.00 40.31           O
ANISOU  792  OD1 ASN A 443     5179   4079   6059    204  -1364   -504       O
ATOM    793  ND2 ASN A 443     -30.602 -43.824 -31.529  1.00 53.99           N
ANISOU  793  ND2 ASN A 443     6808   5724   7984     79  -1457   -421       N
ATOM    794  N   LEU A 444     -25.295 -44.279 -30.150  1.00 24.32           N
ANISOU  794  N   LEU A 444     3305   2112   3824    237  -1297   -503       N
ATOM    795  CA  LEU A 444     -24.124 -44.127 -31.006  1.00 25.23           C
ANISOU  795  CA  LEU A 444     3486   2295   3806    384  -1303   -567       C
ATOM    796  C   LEU A 444     -23.469 -45.463 -31.324  1.00 30.39           C
ANISOU  796  C   LEU A 444     4207   2932   4408    458  -1429   -581       C
ATOM    797  O   LEU A 444     -22.752 -45.584 -32.314  1.00 29.58           O
ANISOU  797  O   LEU A 444     4148   2887   4202    590  -1476   -634       O
ATOM    798  CB  LEU A 444     -23.098 -43.198 -30.351  1.00 21.76           C
ANISOU  798  CB  LEU A 444     3044   1940   3282    378  -1145   -559       C
ATOM    799  CG  LEU A 444     -23.469 -41.721 -30.383  1.00 24.02           C
ANISOU  799  CG  LEU A 444     3258   2310   3559    355   -998   -531       C
ATOM    800  CD1 LEU A 444     -22.406 -40.928 -29.628  1.00 26.04           C
ANISOU  800  CD1 LEU A 444     3506   2662   3725    339   -845   -497       C
ATOM    801  CD2 LEU A 444     -23.610 -41.242 -31.819  1.00 23.64           C
ANISOU  801  CD2 LEU A 444     3223   2292   3469    475  -1042   -587       C
ATOM    802  N   LYS A 445     -23.700 -46.461 -30.478  1.00 33.40           N
ANISOU  802  N   LYS A 445     4593   3243   4856    373  -1482   -529       N
ATOM    803  CA  LYS A 445     -23.108 -47.779 -30.702  1.00 37.04           C
ANISOU  803  CA  LYS A 445     5120   3673   5281    445  -1609   -537       C
ATOM    804  C   LYS A 445     -23.381 -48.234 -32.136  1.00 35.22           C
ANISOU  804  C   LYS A 445     4918   3434   5028    569  -1733   -585       C
ATOM    805  O   LYS A 445     -24.517 -48.182 -32.604  1.00 35.79           O
ANISOU  805  O   LYS A 445     4956   3462   5180    544  -1782   -576       O
ATOM    806  CB  LYS A 445     -23.661 -48.799 -29.707  1.00 40.39           C
ANISOU  806  CB  LYS A 445     5537   4011   5800    327  -1663   -463       C
ATOM    807  CG  LYS A 445     -22.906 -50.121 -29.688  1.00 47.34           C
ANISOU  807  CG  LYS A 445     6491   4853   6644    392  -1779   -465       C
ATOM    808  CD  LYS A 445     -23.590 -51.137 -28.786  1.00 54.85           C
ANISOU  808  CD  LYS A 445     7433   5717   7691    274  -1844   -384       C
ATOM    809  CE  LYS A 445     -22.585 -51.851 -27.891  1.00 61.48           C
ANISOU  809  CE  LYS A 445     8320   6553   8484    258  -1843   -364       C
ATOM    810  NZ  LYS A 445     -21.452 -52.437 -28.661  1.00 62.62           N
ANISOU  810  NZ  LYS A 445     8546   6708   8540    423  -1926   -427       N
ATOM    811  N   GLY A 446     -22.328 -48.647 -32.835  1.00 35.47           N
ANISOU  811  N   GLY A 446     5011   3526   4939    668  -1714   -639       N
ATOM    812  CA  GLY A 446     -22.459 -49.160 -34.189  1.00 35.54           C
ANISOU  812  CA  GLY A 446     5054   3547   4903    749  -1760   -688       C
ATOM    813  C   GLY A 446     -22.651 -48.130 -35.293  1.00 36.65           C
ANISOU  813  C   GLY A 446     5176   3772   4979    795  -1707   -738       C
ATOM    814  O   GLY A 446     -22.827 -48.499 -36.455  1.00 37.67           O
ANISOU  814  O   GLY A 446     5342   3910   5064    840  -1747   -796       O
ATOM    815  N   LYS A 447     -22.632 -46.845 -34.947  1.00 33.68           N
ANISOU  815  N   LYS A 447     4756   3447   4595    773  -1616   -731       N
ATOM    816  CA  LYS A 447     -22.759 -45.789 -35.951  1.00 29.14           C
ANISOU  816  CA  LYS A 447     4170   2947   3956    819  -1556   -775       C
ATOM    817  C   LYS A 447     -21.391 -45.495 -36.549  1.00 28.16           C
ANISOU  817  C   LYS A 447     4086   2936   3677    912  -1468   -815       C
ATOM    818  O   LYS A 447     -20.405 -46.108 -36.159  1.00 29.29           O
ANISOU  818  O   LYS A 447     4262   3097   3770    933  -1455   -816       O
ATOM    819  CB  LYS A 447     -23.345 -44.515 -35.339  1.00 27.84           C
ANISOU  819  CB  LYS A 447     3935   2787   3856    763  -1500   -745       C
ATOM    820  CG  LYS A 447     -24.728 -44.676 -34.729  1.00 33.15           C
ANISOU  820  CG  LYS A 447     4548   3350   4697    666  -1570   -698       C
ATOM    821  CD  LYS A 447     -25.796 -44.839 -35.797  1.00 40.05           C
ANISOU  821  CD  LYS A 447     5417   4190   5612    677  -1635   -718       C
ATOM    822  CE  LYS A 447     -26.753 -45.974 -35.460  1.00 46.73           C
ANISOU  822  CE  LYS A 447     6252   4918   6587    615  -1748   -670       C
ATOM    823  NZ  LYS A 447     -27.572 -45.710 -34.244  1.00 49.32           N
ANISOU  823  NZ  LYS A 447     6500   5177   7061    501  -1740   -597       N
ATOM    824  N   LYS A 448     -21.331 -44.554 -37.488  1.00 24.71           N
ANISOU  824  N   LYS A 448     3642   2576   3169    966  -1407   -840       N
ATOM    825  CA  LYS A 448     -20.080 -44.223 -38.168  1.00 24.28           C
ANISOU  825  CA  LYS A 448     3612   2637   2975   1057  -1319   -861       C
ATOM    826  C   LYS A 448     -19.497 -42.942 -37.587  1.00 26.87           C
ANISOU  826  C   LYS A 448     3898   3055   3254   1050  -1207   -825       C
ATOM    827  O   LYS A 448     -20.189 -41.929 -37.530  1.00 27.89           O
ANISOU  827  O   LYS A 448     3989   3190   3418   1019  -1184   -811       O
ATOM    828  CB  LYS A 448     -20.318 -44.017 -39.663  1.00 25.24           C
ANISOU  828  CB  LYS A 448     3753   2796   3042   1126  -1323   -900       C
ATOM    829  CG  LYS A 448     -20.837 -45.244 -40.410  1.00 31.10           C
ANISOU  829  CG  LYS A 448     4542   3456   3817   1149  -1432   -943       C
ATOM    830  CD  LYS A 448     -20.992 -44.921 -41.899  1.00 41.86           C
ANISOU  830  CD  LYS A 448     5923   4865   5116   1224  -1427   -979       C
ATOM    831  CE  LYS A 448     -21.464 -46.126 -42.703  1.00 56.42           C
ANISOU  831  CE  LYS A 448     7819   6631   6986   1257  -1536  -1027       C
ATOM    832  NZ  LYS A 448     -22.874 -46.487 -42.389  1.00 63.24           N
ANISOU  832  NZ  LYS A 448     8672   7377   7980   1174  -1636  -1017       N
ATOM    833  N   SER A 449     -18.224 -42.973 -37.190  1.00 21.83           N
ANISOU  833  N   SER A 449     3268   2487   2539   1082  -1137   -810       N
ATOM    834  CA  SER A 449     -17.654 -41.853 -36.433  1.00 23.19           C
ANISOU  834  CA  SER A 449     3401   2735   2674   1065  -1036   -767       C
ATOM    835  C   SER A 449     -16.480 -41.144 -37.112  1.00 24.59           C
ANISOU  835  C   SER A 449     3567   3050   2727   1137   -926   -750       C
ATOM    836  O   SER A 449     -15.737 -41.747 -37.887  1.00 27.73           O
ANISOU  836  O   SER A 449     3986   3484   3065   1204   -919   -772       O
ATOM    837  CB  SER A 449     -17.225 -42.334 -35.047  1.00 23.41           C
ANISOU  837  CB  SER A 449     3432   2721   2742   1016  -1042   -741       C
ATOM    838  OG  SER A 449     -16.176 -43.280 -35.158  1.00 24.31           O
ANISOU  838  OG  SER A 449     3582   2856   2800   1061  -1040   -755       O
ATOM    839  N   CYS A 450     -16.328 -39.859 -36.798  1.00 22.70           N
ANISOU  839  N   CYS A 450     3285   2882   2458   1122   -840   -707       N
ATOM    840  CA  CYS A 450     -15.233 -39.028 -37.292  1.00 17.70           C
ANISOU  840  CA  CYS A 450     2622   2379   1723   1171   -728   -667       C
ATOM    841  C   CYS A 450     -14.503 -38.408 -36.110  1.00 19.24           C
ANISOU  841  C   CYS A 450     2785   2621   1903   1135   -648   -610       C
ATOM    842  O   CYS A 450     -15.081 -37.615 -35.377  1.00 18.96           O
ANISOU  842  O   CYS A 450     2726   2567   1912   1084   -628   -583       O
ATOM    843  CB  CYS A 450     -15.775 -37.902 -38.177  1.00 19.53           C
ANISOU  843  CB  CYS A 450     2832   2659   1931   1185   -698   -657       C
ATOM    844  SG  CYS A 450     -16.709 -38.502 -39.609  1.00 26.77           S
ANISOU  844  SG  CYS A 450     3786   3519   2864   1228   -791   -721       S
ATOM    845  N   HIS A 451     -13.236 -38.769 -35.929  1.00 17.67           N
ANISOU  845  N   HIS A 451     2574   2475   1664   1168   -597   -586       N
ATOM    846  CA  HIS A 451     -12.433 -38.276 -34.807  1.00 17.62           C
ANISOU  846  CA  HIS A 451     2535   2516   1642   1137   -527   -524       C
ATOM    847  C   HIS A 451     -11.275 -37.441 -35.329  1.00 21.08           C
ANISOU  847  C   HIS A 451     2916   3086   2008   1169   -428   -462       C
ATOM    848  O   HIS A 451     -10.738 -37.734 -36.397  1.00 23.14           O
ANISOU  848  O   HIS A 451     3167   3395   2230   1230   -426   -473       O
ATOM    849  CB  HIS A 451     -11.873 -39.457 -34.015  1.00 17.77           C
ANISOU  849  CB  HIS A 451     2587   2483   1683   1134   -569   -543       C
ATOM    850  CG  HIS A 451     -12.908 -40.453 -33.611  1.00 25.80           C
ANISOU  850  CG  HIS A 451     3656   3364   2784   1100   -683   -596       C
ATOM    851  ND1 HIS A 451     -13.450 -40.491 -32.345  1.00 22.49           N
ANISOU  851  ND1 HIS A 451     3256   2864   2427   1012   -700   -597       N
ATOM    852  CD2 HIS A 451     -13.498 -41.457 -34.305  1.00 24.95           C
ANISOU  852  CD2 HIS A 451     3587   3177   2715   1119   -771   -654       C
ATOM    853  CE1 HIS A 451     -14.336 -41.471 -32.278  1.00 22.68           C
ANISOU  853  CE1 HIS A 451     3313   2767   2537    989   -814   -636       C
ATOM    854  NE2 HIS A 451     -14.377 -42.075 -33.452  1.00 24.89           N
ANISOU  854  NE2 HIS A 451     3604   3059   2792   1049   -870   -663       N
ATOM    855  N   THR A 452     -10.880 -36.413 -34.583  1.00 19.29           N
ANISOU  855  N   THR A 452     2650   2915   1766   1116   -348   -392       N
ATOM    856  CA  THR A 452      -9.778 -35.561 -35.023  1.00 22.29           C
ANISOU  856  CA  THR A 452     2963   3411   2094   1123   -263   -320       C
ATOM    857  C   THR A 452      -8.514 -36.398 -35.204  1.00 22.66           C
ANISOU  857  C   THR A 452     2994   3501   2114   1182   -263   -325       C
ATOM    858  O   THR A 452      -7.819 -36.286 -36.214  1.00 22.68           O
ANISOU  858  O   THR A 452     2962   3581   2075   1230   -242   -312       O
ATOM    859  CB  THR A 452      -9.519 -34.403 -34.051  1.00 18.01           C
ANISOU  859  CB  THR A 452     2394   2893   1555   1000   -177   -236       C
ATOM    860  OG1 THR A 452      -9.180 -34.925 -32.759  1.00 19.12           O
ANISOU  860  OG1 THR A 452     2561   2987   1716    938   -167   -236       O
ATOM    861  CG2 THR A 452     -10.761 -33.512 -33.944  1.00 19.24           C
ANISOU  861  CG2 THR A 452     2565   3013   1732    944   -169   -235       C
ATOM    862  N   ALA A 453      -8.236 -37.242 -34.219  1.00 21.71           N
ANISOU  862  N   ALA A 453     2906   3328   2016   1168   -289   -346       N
ATOM    863  CA  ALA A 453      -7.169 -38.241 -34.305  1.00 23.61           C
ANISOU  863  CA  ALA A 453     3149   3586   2236   1213   -305   -366       C
ATOM    864  C   ALA A 453      -7.231 -39.087 -33.048  1.00 22.98           C
ANISOU  864  C   ALA A 453     3117   3419   2193   1183   -346   -392       C
ATOM    865  O   ALA A 453      -7.762 -38.649 -32.041  1.00 20.40           O
ANISOU  865  O   ALA A 453     2811   3048   1894   1081   -325   -368       O
ATOM    866  CB  ALA A 453      -5.800 -37.577 -34.434  1.00 22.86           C
ANISOU  866  CB  ALA A 453     2978   3607   2099   1216   -229   -296       C
ATOM    867  N   VAL A 454      -6.701 -40.305 -33.092  1.00 19.41           N
ANISOU  867  N   VAL A 454     2697   2938   1741   1224   -396   -437       N
ATOM    868  CA  VAL A 454      -6.674 -41.114 -31.884  1.00 18.43           C
ANISOU  868  CA  VAL A 454     2620   2729   1652   1194   -438   -458       C
ATOM    869  C   VAL A 454      -5.811 -40.423 -30.828  1.00 21.41           C
ANISOU  869  C   VAL A 454     2964   3158   2014   1115   -353   -388       C
ATOM    870  O   VAL A 454      -4.750 -39.871 -31.138  1.00 22.77           O
ANISOU  870  O   VAL A 454     3073   3431   2148   1135   -289   -341       O
ATOM    871  CB  VAL A 454      -6.166 -42.550 -32.170  1.00 34.01           C
ANISOU  871  CB  VAL A 454     4632   4663   3626   1250   -508   -515       C
ATOM    872  CG1 VAL A 454      -4.815 -42.505 -32.853  1.00 41.59           C
ANISOU  872  CG1 VAL A 454     5539   5737   4526   1311   -458   -496       C
ATOM    873  CG2 VAL A 454      -6.094 -43.362 -30.882  1.00 36.10           C
ANISOU  873  CG2 VAL A 454     4948   4837   3933   1212   -554   -530       C
ATOM    874  N   GLY A 455      -6.289 -40.419 -29.589  1.00 19.15           N
ANISOU  874  N   GLY A 455     2720   2796   1760   1006   -348   -379       N
ATOM    875  CA  GLY A 455      -5.539 -39.857 -28.478  1.00 20.22           C
ANISOU  875  CA  GLY A 455     2839   2957   1886    912   -267   -319       C
ATOM    876  C   GLY A 455      -5.688 -38.357 -28.265  1.00 25.13           C
ANISOU  876  C   GLY A 455     3419   3627   2503    825   -171   -248       C
ATOM    877  O   GLY A 455      -5.150 -37.819 -27.290  1.00 25.21           O
ANISOU  877  O   GLY A 455     3419   3643   2517    739   -105   -197       O
ATOM    878  N   ARG A 456      -6.405 -37.675 -29.158  1.00 18.23           N
ANISOU  878  N   ARG A 456     2523   2779   1625    846   -166   -245       N
ATOM    879  CA  ARG A 456      -6.610 -36.232 -29.000  1.00 18.30           C
ANISOU  879  CA  ARG A 456     2495   2821   1638    765    -84   -178       C
ATOM    880  C   ARG A 456      -7.712 -35.976 -27.984  1.00 20.20           C
ANISOU  880  C   ARG A 456     2782   2980   1912    676    -61   -191       C
ATOM    881  O   ARG A 456      -8.617 -36.790 -27.818  1.00 18.95           O
ANISOU  881  O   ARG A 456     2678   2742   1779    689   -122   -261       O
ATOM    882  CB  ARG A 456      -6.977 -35.571 -30.327  1.00 21.81           C
ANISOU  882  CB  ARG A 456     2901   3322   2065    820    -89   -170       C
ATOM    883  CG  ARG A 456      -5.923 -35.711 -31.404  1.00 31.15           C
ANISOU  883  CG  ARG A 456     4029   4594   3211    912    -97   -159       C
ATOM    884  CD  ARG A 456      -4.935 -34.568 -31.377  1.00 44.75           C
ANISOU  884  CD  ARG A 456     5687   6392   4926    856    -26    -73       C
ATOM    885  NE  ARG A 456      -3.831 -34.813 -32.298  1.00 57.96           N
ANISOU  885  NE  ARG A 456     7304   8157   6561    945    -32    -66       N
ATOM    886  CZ  ARG A 456      -2.901 -33.918 -32.610  1.00 65.43           C
ANISOU  886  CZ  ARG A 456     8184   9183   7493    922     12      2       C
ATOM    887  NH1 ARG A 456      -2.942 -32.703 -32.077  1.00 68.28           N
ANISOU  887  NH1 ARG A 456     8533   9529   7883    810     56     66       N
ATOM    888  NH2 ARG A 456      -1.933 -34.240 -33.458  1.00 64.87           N
ANISOU  888  NH2 ARG A 456     8059   9206   7382   1015      7      3       N
ATOM    889  N   THR A 457      -7.649 -34.833 -27.313  1.00 15.02           N
ANISOU  889  N   THR A 457     2102   2334   1270    584     23   -126       N
ATOM    890  CA  THR A 457      -8.597 -34.556 -26.233  1.00 14.87           C
ANISOU  890  CA  THR A 457     2108   2224   1320    486     60   -124       C
ATOM    891  C   THR A 457     -10.051 -34.461 -26.725  1.00 17.37           C
ANISOU  891  C   THR A 457     2417   2472   1710    476     28   -159       C
ATOM    892  O   THR A 457     -10.919 -35.206 -26.261  1.00 18.41           O
ANISOU  892  O   THR A 457     2570   2505   1920    437    -11   -196       O
ATOM    893  CB  THR A 457      -8.186 -33.297 -25.450  1.00 18.30           C
ANISOU  893  CB  THR A 457     2517   2681   1755    398    150    -45       C
ATOM    894  OG1 THR A 457      -6.932 -33.552 -24.802  1.00 19.64           O
ANISOU  894  OG1 THR A 457     2684   2867   1912    374    161    -15       O
ATOM    895  CG2 THR A 457      -9.239 -32.934 -24.384  1.00 17.93           C
ANISOU  895  CG2 THR A 457     2477   2529   1809    290    186    -39       C
ATOM    896  N   ALA A 458     -10.317 -33.555 -27.662  1.00 17.16           N
ANISOU  896  N   ALA A 458     2360   2501   1660    507     39   -142       N
ATOM    897  CA  ALA A 458     -11.686 -33.362 -28.148  1.00 18.59           C
ANISOU  897  CA  ALA A 458     2531   2620   1911    499      9   -172       C
ATOM    898  C   ALA A 458     -12.153 -34.529 -29.018  1.00 15.90           C
ANISOU  898  C   ALA A 458     2216   2250   1575    586    -93   -247       C
ATOM    899  O   ALA A 458     -13.316 -34.921 -28.972  1.00 17.33           O
ANISOU  899  O   ALA A 458     2402   2339   1842    557   -137   -283       O
ATOM    900  CB  ALA A 458     -11.793 -32.062 -28.932  1.00 21.95           C
ANISOU  900  CB  ALA A 458     2922   3111   2306    511     42   -133       C
ATOM    901  N   GLY A 459     -11.243 -35.081 -29.808  1.00 15.92           N
ANISOU  901  N   GLY A 459     2235   2332   1483    695   -136   -271       N
ATOM    902  CA  GLY A 459     -11.643 -36.042 -30.828  1.00 17.29           C
ANISOU  902  CA  GLY A 459     2438   2488   1645    800   -243   -345       C
ATOM    903  C   GLY A 459     -11.729 -37.478 -30.341  1.00 19.52           C
ANISOU  903  C   GLY A 459     2769   2680   1966    809   -327   -402       C
ATOM    904  O   GLY A 459     -12.287 -38.340 -31.014  1.00 21.92           O
ANISOU  904  O   GLY A 459     3105   2932   2290    876   -433   -466       O
ATOM    905  N   TRP A 460     -11.188 -37.743 -29.163  1.00 14.09           N
ANISOU  905  N   TRP A 460     2093   1967   1295    738   -289   -375       N
ATOM    906  CA  TRP A 460     -11.040 -39.124 -28.721  1.00 16.72           C
ANISOU  906  CA  TRP A 460     2478   2227   1649    753   -375   -423       C
ATOM    907  C   TRP A 460     -11.179 -39.285 -27.219  1.00 18.62           C
ANISOU  907  C   TRP A 460     2725   2385   1965    621   -331   -387       C
ATOM    908  O   TRP A 460     -12.068 -39.985 -26.745  1.00 16.70           O
ANISOU  908  O   TRP A 460     2501   2031   1813    561   -386   -403       O
ATOM    909  CB  TRP A 460      -9.681 -39.667 -29.168  1.00 16.82           C
ANISOU  909  CB  TRP A 460     2501   2327   1564    862   -399   -435       C
ATOM    910  CG  TRP A 460      -9.514 -41.127 -28.904  1.00 19.74           C
ANISOU  910  CG  TRP A 460     2918   2615   1966    891   -500   -480       C
ATOM    911  CD1 TRP A 460      -8.939 -41.704 -27.801  1.00 23.09           C
ANISOU  911  CD1 TRP A 460     3373   3000   2401    840   -499   -473       C
ATOM    912  CD2 TRP A 460      -9.930 -42.205 -29.751  1.00 21.36           C
ANISOU  912  CD2 TRP A 460     3150   2760   2205    979   -621   -535       C
ATOM    913  NE1 TRP A 460      -8.974 -43.069 -27.916  1.00 22.26           N
ANISOU  913  NE1 TRP A 460     3309   2815   2333    887   -613   -516       N
ATOM    914  CE2 TRP A 460      -9.578 -43.403 -29.100  1.00 22.66           C
ANISOU  914  CE2 TRP A 460     3358   2848   2401    974   -689   -555       C
ATOM    915  CE3 TRP A 460     -10.571 -42.271 -30.993  1.00 24.76           C
ANISOU  915  CE3 TRP A 460     3575   3187   2647   1063   -678   -569       C
ATOM    916  CZ2 TRP A 460      -9.833 -44.658 -29.657  1.00 24.80           C
ANISOU  916  CZ2 TRP A 460     3669   3038   2717   1052   -811   -604       C
ATOM    917  CZ3 TRP A 460     -10.827 -43.517 -31.544  1.00 28.63           C
ANISOU  917  CZ3 TRP A 460     4102   3602   3172   1102   -777   -619       C
ATOM    918  CH2 TRP A 460     -10.455 -44.693 -30.875  1.00 24.10           C
ANISOU  918  CH2 TRP A 460     3572   2955   2631   1092   -840   -634       C
ATOM    919  N   ASN A 461     -10.290 -38.645 -26.467  1.00 15.04           N
ANISOU  919  N   ASN A 461     2255   1988   1472    576   -236   -332       N
ATOM    920  CA  ASN A 461     -10.264 -38.864 -25.022  1.00 17.82           C
ANISOU  920  CA  ASN A 461     2622   2271   1879    464   -198   -300       C
ATOM    921  C   ASN A 461     -11.584 -38.522 -24.327  1.00 17.28           C
ANISOU  921  C   ASN A 461     2531   2116   1919    347   -165   -276       C
ATOM    922  O   ASN A 461     -12.111 -39.312 -23.537  1.00 15.66           O
ANISOU  922  O   ASN A 461     2347   1819   1782    279   -200   -280       O
ATOM    923  CB  ASN A 461      -9.116 -38.098 -24.372  1.00 15.87           C
ANISOU  923  CB  ASN A 461     2359   2099   1572    436   -102   -244       C
ATOM    924  CG  ASN A 461      -7.758 -38.605 -24.812  1.00 22.08           C
ANISOU  924  CG  ASN A 461     3162   2970   2256    539   -133   -263       C
ATOM    925  OD1 ASN A 461      -7.650 -39.632 -25.486  1.00 20.21           O
ANISOU  925  OD1 ASN A 461     2959   2728   1993    635   -231   -326       O
ATOM    926  ND2 ASN A 461      -6.709 -37.890 -24.419  1.00 26.86           N
ANISOU  926  ND2 ASN A 461     3746   3654   2804    524    -56   -208       N
ATOM    927  N   ILE A 462     -12.120 -37.345 -24.623  1.00 15.09           N
ANISOU  927  N   ILE A 462     2208   1871   1653    326   -101   -249       N
ATOM    928  CA  ILE A 462     -13.365 -36.918 -23.996  1.00 15.28           C
ANISOU  928  CA  ILE A 462     2203   1830   1772    228    -64   -228       C
ATOM    929  C   ILE A 462     -14.551 -37.804 -24.387  1.00 16.40           C
ANISOU  929  C   ILE A 462     2349   1890   1994    227   -157   -269       C
ATOM    930  O   ILE A 462     -15.214 -38.354 -23.519  1.00 14.66           O
ANISOU  930  O   ILE A 462     2128   1595   1848    143   -167   -256       O
ATOM    931  CB  ILE A 462     -13.648 -35.424 -24.236  1.00 13.44           C
ANISOU  931  CB  ILE A 462     1925   1648   1532    213     16   -194       C
ATOM    932  CG1 ILE A 462     -12.713 -34.594 -23.348  1.00 13.51           C
ANISOU  932  CG1 ILE A 462     1934   1702   1498    168    107   -140       C
ATOM    933  CG2 ILE A 462     -15.112 -35.089 -23.920  1.00 13.81           C
ANISOU  933  CG2 ILE A 462     1937   1634   1676    144     31   -192       C
ATOM    934  CD1 ILE A 462     -12.740 -33.065 -23.617  1.00 15.03           C
ANISOU  934  CD1 ILE A 462     2091   1947   1670    161    171   -102       C
ATOM    935  N   PRO A 463     -14.826 -37.955 -25.692  1.00 15.68           N
ANISOU  935  N   PRO A 463     2258   1812   1887    318   -230   -313       N
ATOM    936  CA  PRO A 463     -15.996 -38.785 -26.000  1.00 18.14           C
ANISOU  936  CA  PRO A 463     2573   2034   2286    307   -327   -347       C
ATOM    937  C   PRO A 463     -15.828 -40.247 -25.572  1.00 15.75           C
ANISOU  937  C   PRO A 463     2321   1654   2008    298   -425   -370       C
ATOM    938  O   PRO A 463     -16.772 -40.826 -25.055  1.00 18.06           O
ANISOU  938  O   PRO A 463     2606   1860   2395    219   -466   -359       O
ATOM    939  CB  PRO A 463     -16.131 -38.664 -27.526  1.00 18.58           C
ANISOU  939  CB  PRO A 463     2631   2124   2303    422   -392   -394       C
ATOM    940  CG  PRO A 463     -14.810 -38.176 -28.006  1.00 20.38           C
ANISOU  940  CG  PRO A 463     2870   2464   2410    507   -349   -390       C
ATOM    941  CD  PRO A 463     -14.249 -37.333 -26.896  1.00 16.57           C
ANISOU  941  CD  PRO A 463     2365   2019   1914    422   -227   -327       C
ATOM    942  N   MET A 464     -14.651 -40.836 -25.761  1.00 18.26           N
ANISOU  942  N   MET A 464     2689   2005   2246    376   -464   -397       N
ATOM    943  CA  MET A 464     -14.480 -42.234 -25.371  1.00 19.05           C
ANISOU  943  CA  MET A 464     2845   2023   2371    373   -572   -423       C
ATOM    944  C   MET A 464     -14.582 -42.404 -23.856  1.00 19.41           C
ANISOU  944  C   MET A 464     2888   2018   2472    238   -517   -367       C
ATOM    945  O   MET A 464     -15.203 -43.351 -23.372  1.00 20.85           O
ANISOU  945  O   MET A 464     3089   2103   2730    174   -596   -362       O
ATOM    946  CB  MET A 464     -13.163 -42.805 -25.901  1.00 21.48           C
ANISOU  946  CB  MET A 464     3204   2384   2573    498   -627   -470       C
ATOM    947  CG  MET A 464     -13.126 -42.917 -27.416  1.00 23.06           C
ANISOU  947  CG  MET A 464     3417   2628   2716    643   -707   -534       C
ATOM    948  SD  MET A 464     -14.494 -43.932 -28.043  1.00 43.43           S
ANISOU  948  SD  MET A 464     6026   5075   5398    652   -874   -585       S
ATOM    949  CE  MET A 464     -13.990 -44.165 -29.746  1.00 55.94           C
ANISOU  949  CE  MET A 464     7620   6748   6887    841   -949   -633       C
ATOM    950  N   GLY A 465     -13.996 -41.472 -23.107  1.00 17.38           N
ANISOU  950  N   GLY A 465     2605   1823   2174    193   -387   -320       N
ATOM    951  CA  GLY A 465     -14.124 -41.477 -21.661  1.00 15.86           C
ANISOU  951  CA  GLY A 465     2408   1594   2026     70   -322   -265       C
ATOM    952  C   GLY A 465     -15.567 -41.373 -21.185  1.00 19.63           C
ANISOU  952  C   GLY A 465     2839   2014   2606    -33   -306   -232       C
ATOM    953  O   GLY A 465     -15.946 -41.992 -20.195  1.00 22.08           O
ANISOU  953  O   GLY A 465     3154   2264   2972   -127   -316   -198       O
ATOM    954  N   LEU A 466     -16.387 -40.593 -21.882  1.00 15.85           N
ANISOU  954  N   LEU A 466     2310   1560   2153    -17   -282   -237       N
ATOM    955  CA  LEU A 466     -17.789 -40.466 -21.480  1.00 13.90           C
ANISOU  955  CA  LEU A 466     2008   1270   2003   -107   -266   -207       C
ATOM    956  C   LEU A 466     -18.665 -41.624 -21.977  1.00 18.97           C
ANISOU  956  C   LEU A 466     2658   1824   2724   -114   -405   -228       C
ATOM    957  O   LEU A 466     -19.744 -41.879 -21.434  1.00 20.09           O
ANISOU  957  O   LEU A 466     2758   1920   2955   -208   -412   -190       O
ATOM    958  CB  LEU A 466     -18.363 -39.128 -21.938  1.00 14.36           C
ANISOU  958  CB  LEU A 466     2008   1385   2063    -92   -186   -204       C
ATOM    959  CG  LEU A 466     -17.679 -37.968 -21.211  1.00 14.82           C
ANISOU  959  CG  LEU A 466     2056   1512   2062   -112    -56   -170       C
ATOM    960  CD1 LEU A 466     -18.243 -36.651 -21.714  1.00 19.62           C
ANISOU  960  CD1 LEU A 466     2615   2167   2673    -92      5   -170       C
ATOM    961  CD2 LEU A 466     -17.885 -38.067 -19.696  1.00 16.77           C
ANISOU  961  CD2 LEU A 466     2293   1738   2341   -220     11   -119       C
ATOM    962  N   LEU A 467     -18.207 -42.313 -23.013  1.00 19.68           N
ANISOU  962  N   LEU A 467     2801   1896   2783    -12   -520   -286       N
ATOM    963  CA  LEU A 467     -18.923 -43.479 -23.533  1.00 17.83           C
ANISOU  963  CA  LEU A 467     2590   1566   2620     -6   -676   -313       C
ATOM    964  C   LEU A 467     -18.545 -44.737 -22.764  1.00 22.38           C
ANISOU  964  C   LEU A 467     3221   2066   3215    -55   -760   -300       C
ATOM    965  O   LEU A 467     -19.062 -45.816 -23.031  1.00 25.52           O
ANISOU  965  O   LEU A 467     3649   2371   3678    -63   -905   -314       O
ATOM    966  CB  LEU A 467     -18.630 -43.661 -25.026  1.00 17.86           C
ANISOU  966  CB  LEU A 467     2631   1581   2574    139   -774   -389       C
ATOM    967  CG  LEU A 467     -19.332 -42.648 -25.935  1.00 23.22           C
ANISOU  967  CG  LEU A 467     3257   2305   3260    179   -734   -402       C
ATOM    968  CD1 LEU A 467     -18.709 -42.635 -27.333  1.00 21.35           C
ANISOU  968  CD1 LEU A 467     3062   2113   2937    335   -798   -472       C
ATOM    969  CD2 LEU A 467     -20.833 -42.950 -26.012  1.00 23.06           C
ANISOU  969  CD2 LEU A 467     3194   2205   3363    108   -799   -386       C
ATOM    970  N   TYR A 468     -17.647 -44.576 -21.800  1.00 21.26           N
ANISOU  970  N   TYR A 468     3097   1959   3021    -88   -676   -271       N
ATOM    971  CA  TYR A 468     -17.012 -45.691 -21.102  1.00 20.77           C
ANISOU  971  CA  TYR A 468     3100   1836   2956   -116   -750   -266       C
ATOM    972  C   TYR A 468     -17.987 -46.773 -20.624  1.00 23.32           C
ANISOU  972  C   TYR A 468     3415   2067   3377   -214   -846   -221       C
ATOM    973  O   TYR A 468     -17.729 -47.969 -20.779  1.00 21.08           O
ANISOU  973  O   TYR A 468     3173   1750   3086   -175   -958   -229       O
ATOM    974  CB  TYR A 468     -16.207 -45.159 -19.917  1.00 22.54           C
ANISOU  974  CB  TYR A 468     3322   2113   3128   -172   -618   -221       C
ATOM    975  CG  TYR A 468     -15.731 -46.231 -18.964  1.00 23.76           C
ANISOU  975  CG  TYR A 468     3535   2201   3293   -231   -679   -200       C
ATOM    976  CD1 TYR A 468     -14.697 -47.087 -19.319  1.00 24.68           C
ANISOU  976  CD1 TYR A 468     3721   2304   3351   -138   -775   -250       C
ATOM    977  CD2 TYR A 468     -16.304 -46.376 -17.705  1.00 27.30           C
ANISOU  977  CD2 TYR A 468     3950   2630   3793   -365   -622   -121       C
ATOM    978  CE1 TYR A 468     -14.252 -48.066 -18.451  1.00 27.03           C
ANISOU  978  CE1 TYR A 468     4047   2580   3645   -177   -807   -216       C
ATOM    979  CE2 TYR A 468     -15.862 -47.357 -16.827  1.00 31.49           C
ANISOU  979  CE2 TYR A 468     4508   3146   4312   -398   -649    -90       C
ATOM    980  CZ  TYR A 468     -14.836 -48.196 -17.209  1.00 29.11           C
ANISOU  980  CZ  TYR A 468     4275   2829   3957   -308   -746   -137       C
ATOM    981  OH  TYR A 468     -14.390 -49.168 -16.341  1.00 30.16           O
ANISOU  981  OH  TYR A 468     4436   2944   4081   -340   -779   -105       O
ATOM    982  N   ASN A 469     -19.094 -46.355 -20.026  1.00 24.89           N
ANISOU  982  N   ASN A 469     3541   2265   3652   -327   -778   -158       N
ATOM    983  CA  ASN A 469     -20.047 -47.320 -19.480  1.00 30.68           C
ANISOU  983  CA  ASN A 469     4240   2962   4453   -412   -827    -93       C
ATOM    984  C   ASN A 469     -20.602 -48.291 -20.518  1.00 31.69           C
ANISOU  984  C   ASN A 469     4384   3034   4621   -352   -988   -118       C
ATOM    985  O   ASN A 469     -21.035 -49.395 -20.175  1.00 33.98           O
ANISOU  985  O   ASN A 469     4678   3282   4950   -395  -1071    -74       O
ATOM    986  CB  ASN A 469     -21.185 -46.606 -18.748  1.00 38.80           C
ANISOU  986  CB  ASN A 469     5175   4024   5542   -526   -715    -24       C
ATOM    987  CG  ASN A 469     -20.781 -46.147 -17.363  1.00 50.04           C
ANISOU  987  CG  ASN A 469     6584   5501   6928   -601   -575     28       C
ATOM    988  OD1 ASN A 469     -19.978 -46.798 -16.695  1.00 50.31           O
ANISOU  988  OD1 ASN A 469     6668   5529   6918   -605   -585     37       O
ATOM    989  ND2 ASN A 469     -21.332 -45.019 -16.925  1.00 59.72           N
ANISOU  989  ND2 ASN A 469     7742   6783   8168   -651   -446     58       N
ATOM    990  N   LYS A 470     -20.581 -47.888 -21.786  1.00 24.54           N
ANISOU  990  N   LYS A 470     3491   2129   3702   -248  -1036   -189       N
ATOM    991  CA  LYS A 470     -21.114 -48.726 -22.858  1.00 28.83           C
ANISOU  991  CA  LYS A 470     4053   2623   4279   -177  -1188   -216       C
ATOM    992  C   LYS A 470     -20.008 -49.437 -23.629  1.00 29.36           C
ANISOU  992  C   LYS A 470     4203   2685   4266    -35  -1292   -283       C
ATOM    993  O   LYS A 470     -20.269 -50.145 -24.600  1.00 29.55           O
ANISOU  993  O   LYS A 470     4253   2672   4302     50  -1424   -312       O
ATOM    994  CB  LYS A 470     -21.975 -47.894 -23.807  1.00 34.83           C
ANISOU  994  CB  LYS A 470     4764   3391   5078   -148  -1180   -246       C
ATOM    995  CG  LYS A 470     -23.190 -47.280 -23.128  1.00 40.63           C
ANISOU  995  CG  LYS A 470     5405   4134   5900   -278  -1091   -177       C
ATOM    996  CD  LYS A 470     -24.057 -46.501 -24.104  1.00 52.57           C
ANISOU  996  CD  LYS A 470     6867   5650   7456   -244  -1095   -209       C
ATOM    997  CE  LYS A 470     -23.487 -45.114 -24.376  1.00 58.74           C
ANISOU  997  CE  LYS A 470     7645   6488   8186   -195   -986   -262       C
ATOM    998  NZ  LYS A 470     -24.379 -44.296 -25.259  1.00 55.32           N
ANISOU  998  NZ  LYS A 470     7153   6081   7784   -159   -968   -282       N
ATOM    999  N   ILE A 471     -18.767 -49.248 -23.195  1.00 26.01           N
ANISOU  999  N   ILE A 471     3819   2303   3759     -4  -1231   -304       N
ATOM   1000  CA  ILE A 471     -17.635 -49.853 -23.884  1.00 25.92           C
ANISOU 1000  CA  ILE A 471     3877   2309   3663    139  -1312   -364       C
ATOM   1001  C   ILE A 471     -17.359 -51.204 -23.258  1.00 31.33           C
ANISOU 1001  C   ILE A 471     4604   2938   4362    117  -1406   -327       C
ATOM   1002  O   ILE A 471     -17.374 -51.347 -22.033  1.00 31.58           O
ANISOU 1002  O   ILE A 471     4624   2958   4416      1  -1350   -267       O
ATOM   1003  CB  ILE A 471     -16.348 -48.995 -23.777  1.00 29.01           C
ANISOU 1003  CB  ILE A 471     4287   2783   3950    197  -1203   -403       C
ATOM   1004  CG1 ILE A 471     -16.545 -47.611 -24.412  1.00 26.87           C
ANISOU 1004  CG1 ILE A 471     3980   2573   3655    229  -1110   -438       C
ATOM   1005  CG2 ILE A 471     -15.171 -49.720 -24.422  1.00 29.83           C
ANISOU 1005  CG2 ILE A 471     4449   2916   3968    346  -1281   -452       C
ATOM   1006  CD1 ILE A 471     -16.784 -47.639 -25.906  1.00 26.96           C
ANISOU 1006  CD1 ILE A 471     3995   2605   3643    360  -1191   -494       C
ATOM   1007  N   ASN A 472     -17.099 -52.188 -24.109  1.00 30.76           N
ANISOU 1007  N   ASN A 472     4582   2831   4275    235  -1549   -362       N
ATOM   1008  CA  ASN A 472     -16.812 -53.543 -23.668  1.00 36.78           C
ANISOU 1008  CA  ASN A 472     5394   3529   5052    236  -1661   -333       C
ATOM   1009  C   ASN A 472     -15.320 -53.783 -23.553  1.00 29.59           C
ANISOU 1009  C   ASN A 472     4537   2656   4051    330  -1650   -369       C
ATOM   1010  O   ASN A 472     -14.603 -53.695 -24.554  1.00 28.87           O
ANISOU 1010  O   ASN A 472     4470   2602   3897    483  -1672   -433       O
ATOM   1011  CB  ASN A 472     -17.403 -54.535 -24.668  1.00 34.31           C
ANISOU 1011  CB  ASN A 472     5112   3139   4784    321  -1835   -345       C
ATOM   1012  CG  ASN A 472     -18.922 -54.457 -24.737  1.00 48.65           C
ANISOU 1012  CG  ASN A 472     6875   4910   6700    223  -1863   -298       C
ATOM   1013  OD1 ASN A 472     -19.600 -54.462 -23.706  1.00 57.07           O
ANISOU 1013  OD1 ASN A 472     7898   5961   7825     73  -1814   -225       O
ATOM   1014  ND2 ASN A 472     -19.463 -54.370 -25.953  1.00 43.84           N
ANISOU 1014  ND2 ASN A 472     6263   4284   6108    312  -1935   -338       N
ATOM   1015  N   HIS A 473     -14.855 -54.075 -22.338  1.00 22.74           N
ANISOU 1015  N   HIS A 473     3680   1782   3178    244  -1610   -326       N
ATOM   1016  CA  HIS A 473     -13.468 -54.488 -22.121  1.00 22.46           C
ANISOU 1016  CA  HIS A 473     3695   1769   3070    326  -1615   -352       C
ATOM   1017  C   HIS A 473     -12.450 -53.521 -22.713  1.00 29.18           C
ANISOU 1017  C   HIS A 473     4540   2718   3830    433  -1518   -414       C
ATOM   1018  O   HIS A 473     -11.428 -53.939 -23.264  1.00 25.79           O
ANISOU 1018  O   HIS A 473     4146   2306   3346    573  -1555   -458       O
ATOM   1019  CB  HIS A 473     -13.238 -55.897 -22.678  1.00 23.63           C
ANISOU 1019  CB  HIS A 473     3907   1839   3233    437  -1787   -366       C
ATOM   1020  CG  HIS A 473     -13.911 -56.970 -21.885  1.00 27.48           C
ANISOU 1020  CG  HIS A 473     4411   2238   3793    333  -1886   -297       C
ATOM   1021  ND1 HIS A 473     -15.108 -57.540 -22.264  1.00 32.11           N
ANISOU 1021  ND1 HIS A 473     4991   2749   4458    303  -1997   -266       N
ATOM   1022  CD2 HIS A 473     -13.556 -57.573 -20.726  1.00 23.82           C
ANISOU 1022  CD2 HIS A 473     3969   1751   3332    253  -1889   -247       C
ATOM   1023  CE1 HIS A 473     -15.455 -58.454 -21.375  1.00 24.62           C
ANISOU 1023  CE1 HIS A 473     4057   1739   3557    207  -2066   -197       C
ATOM   1024  NE2 HIS A 473     -14.533 -58.492 -20.432  1.00 31.10           N
ANISOU 1024  NE2 HIS A 473     4896   2591   4330    176  -2001   -186       N
ATOM   1025  N   CYS A 474     -12.748 -52.232 -22.595  1.00 24.69           N
ANISOU 1025  N   CYS A 474     3923   2209   3251    371  -1389   -413       N
ATOM   1026  CA  CYS A 474     -11.832 -51.172 -23.000  1.00 27.26           C
ANISOU 1026  CA  CYS A 474     4234   2637   3487    449  -1282   -456       C
ATOM   1027  C   CYS A 474     -11.571 -51.147 -24.503  1.00 25.71           C
ANISOU 1027  C   CYS A 474     4040   2485   3245    620  -1329   -516       C
ATOM   1028  O   CYS A 474     -10.569 -50.590 -24.955  1.00 35.10           O
ANISOU 1028  O   CYS A 474     5220   3767   4351    717  -1258   -549       O
ATOM   1029  CB  CYS A 474     -10.515 -51.276 -22.217  1.00 28.36           C
ANISOU 1029  CB  CYS A 474     4397   2812   3565    458  -1229   -450       C
ATOM   1030  SG  CYS A 474     -10.721 -51.084 -20.427  1.00 31.71           S
ANISOU 1030  SG  CYS A 474     4816   3200   4030    264  -1143   -378       S
ATOM   1031  N   ARG A 475     -12.468 -51.749 -25.277  1.00 21.23           N
ANISOU 1031  N   ARG A 475     3481   1853   2734    656  -1442   -526       N
ATOM   1032  CA  ARG A 475     -12.304 -51.811 -26.727  1.00 22.87           C
ANISOU 1032  CA  ARG A 475     3682   2109   2898    784  -1448   -590       C
ATOM   1033  C   ARG A 475     -12.945 -50.601 -27.397  1.00 22.53           C
ANISOU 1033  C   ARG A 475     3595   2121   2845    793  -1392   -601       C
ATOM   1034  O   ARG A 475     -13.991 -50.705 -28.051  1.00 25.38           O
ANISOU 1034  O   ARG A 475     3945   2443   3257    784  -1448   -609       O
ATOM   1035  CB  ARG A 475     -12.904 -53.103 -27.280  1.00 30.10           C
ANISOU 1035  CB  ARG A 475     4627   2941   3868    797  -1567   -605       C
ATOM   1036  CG  ARG A 475     -12.320 -54.365 -26.661  1.00 34.15           C
ANISOU 1036  CG  ARG A 475     5186   3394   4393    791  -1632   -595       C
ATOM   1037  CD  ARG A 475     -11.247 -54.976 -27.542  1.00 43.08           C
ANISOU 1037  CD  ARG A 475     6340   4572   5458    919  -1623   -664       C
ATOM   1038  NE  ARG A 475     -10.739 -56.236 -26.996  1.00 45.42           N
ANISOU 1038  NE  ARG A 475     6683   4804   5772    918  -1696   -660       N
ATOM   1039  CZ  ARG A 475     -11.091 -57.443 -27.431  1.00 52.39           C
ANISOU 1039  CZ  ARG A 475     7605   5607   6693    942  -1805   -679       C
ATOM   1040  NH1 ARG A 475     -11.954 -57.569 -28.432  1.00 59.88           N
ANISOU 1040  NH1 ARG A 475     8555   6530   7669    969  -1853   -704       N
ATOM   1041  NH2 ARG A 475     -10.571 -58.527 -26.870  1.00 53.12           N
ANISOU 1041  NH2 ARG A 475     7740   5645   6799    940  -1868   -674       N
ATOM   1042  N   PHE A 476     -12.321 -49.446 -27.214  1.00 25.55           N
ANISOU 1042  N   PHE A 476     3951   2594   3162    810  -1282   -599       N
ATOM   1043  CA  PHE A 476     -12.854 -48.204 -27.768  1.00 26.10           C
ANISOU 1043  CA  PHE A 476     3975   2730   3212    802  -1205   -608       C
ATOM   1044  C   PHE A 476     -12.937 -48.258 -29.291  1.00 31.75           C
ANISOU 1044  C   PHE A 476     4680   3493   3892    912  -1220   -654       C
ATOM   1045  O   PHE A 476     -13.813 -47.643 -29.895  1.00 29.80           O
ANISOU 1045  O   PHE A 476     4407   3252   3664    906  -1220   -661       O
ATOM   1046  CB  PHE A 476     -12.006 -47.018 -27.314  1.00 26.56           C
ANISOU 1046  CB  PHE A 476     4005   2898   3189    780  -1053   -596       C
ATOM   1047  CG  PHE A 476     -11.958 -46.848 -25.819  1.00 30.70           C
ANISOU 1047  CG  PHE A 476     4537   3383   3745    634   -989   -557       C
ATOM   1048  CD1 PHE A 476     -13.077 -46.429 -25.121  1.00 31.64           C
ANISOU 1048  CD1 PHE A 476     4639   3429   3952    495   -958   -530       C
ATOM   1049  CD2 PHE A 476     -10.797 -47.109 -25.113  1.00 36.69           C
ANISOU 1049  CD2 PHE A 476     5315   4172   4454    639   -953   -543       C
ATOM   1050  CE1 PHE A 476     -13.038 -46.271 -23.744  1.00 36.71           C
ANISOU 1050  CE1 PHE A 476     5286   4030   4631    364   -890   -486       C
ATOM   1051  CE2 PHE A 476     -10.750 -46.954 -23.741  1.00 35.45           C
ANISOU 1051  CE2 PHE A 476     5170   3975   4326    508   -894   -506       C
ATOM   1052  CZ  PHE A 476     -11.871 -46.536 -23.054  1.00 37.16           C
ANISOU 1052  CZ  PHE A 476     5372   4118   4629    371   -861   -475       C
ATOM   1053  N   ASP A 477     -12.029 -49.005 -29.910  1.00 37.03           N
ANISOU 1053  N   ASP A 477     5367   4195   4509    998  -1220   -688       N
ATOM   1054  CA  ASP A 477     -12.013 -49.121 -31.369  1.00 46.38           C
ANISOU 1054  CA  ASP A 477     6546   5423   5652   1088  -1216   -736       C
ATOM   1055  C   ASP A 477     -13.058 -50.090 -31.926  1.00 44.67           C
ANISOU 1055  C   ASP A 477     6363   5102   5509   1081  -1333   -759       C
ATOM   1056  O   ASP A 477     -13.136 -50.298 -33.136  1.00 48.94           O
ANISOU 1056  O   ASP A 477     6914   5660   6019   1152  -1344   -808       O
ATOM   1057  CB  ASP A 477     -10.614 -49.496 -31.872  1.00 58.19           C
ANISOU 1057  CB  ASP A 477     8046   7000   7064   1184  -1171   -767       C
ATOM   1058  CG  ASP A 477     -10.064 -50.743 -31.202  1.00 71.04           C
ANISOU 1058  CG  ASP A 477     9716   8560   8717   1182  -1237   -773       C
ATOM   1059  OD1 ASP A 477     -10.866 -51.586 -30.743  1.00 71.16           O
ANISOU 1059  OD1 ASP A 477     9767   8456   8813   1125  -1338   -763       O
ATOM   1060  OD2 ASP A 477      -8.824 -50.881 -31.138  1.00 78.19           O
ANISOU 1060  OD2 ASP A 477    10614   9532   9562   1236  -1189   -781       O
ATOM   1061  N   GLU A 478     -13.864 -50.677 -31.048  1.00 41.66           N
ANISOU 1061  N   GLU A 478     5998   4612   5219    991  -1422   -722       N
ATOM   1062  CA  GLU A 478     -14.910 -51.602 -31.484  1.00 41.98           C
ANISOU 1062  CA  GLU A 478     6063   4551   5337    974  -1539   -729       C
ATOM   1063  C   GLU A 478     -16.316 -51.067 -31.214  1.00 39.05           C
ANISOU 1063  C   GLU A 478     5657   4129   5051    880  -1577   -690       C
ATOM   1064  O   GLU A 478     -17.304 -51.743 -31.483  1.00 36.94           O
ANISOU 1064  O   GLU A 478     5399   3778   4859    850  -1676   -682       O
ATOM   1065  CB  GLU A 478     -14.739 -52.972 -30.816  1.00 48.41           C
ANISOU 1065  CB  GLU A 478     6923   5274   6197    947  -1633   -714       C
ATOM   1066  CG  GLU A 478     -13.455 -53.703 -31.193  1.00 61.37           C
ANISOU 1066  CG  GLU A 478     8600   6948   7768   1046  -1619   -764       C
ATOM   1067  CD  GLU A 478     -13.329 -55.066 -30.517  1.00 68.64           C
ANISOU 1067  CD  GLU A 478     9569   7775   8737   1019  -1719   -748       C
ATOM   1068  OE1 GLU A 478     -14.340 -55.564 -29.974  1.00 69.69           O
ANISOU 1068  OE1 GLU A 478     9710   7812   8959    930  -1810   -700       O
ATOM   1069  OE2 GLU A 478     -12.217 -55.638 -30.528  1.00 66.18           O
ANISOU 1069  OE2 GLU A 478     9284   7487   8375   1084  -1707   -780       O
ATOM   1070  N   PHE A 479     -16.408 -49.851 -30.686  1.00 35.94           N
ANISOU 1070  N   PHE A 479     5222   3784   4650    833  -1501   -666       N
ATOM   1071  CA  PHE A 479     -17.706 -49.279 -30.352  1.00 28.16           C
ANISOU 1071  CA  PHE A 479     4197   2745   3758    742  -1530   -632       C
ATOM   1072  C   PHE A 479     -18.488 -48.856 -31.591  1.00 29.97           C
ANISOU 1072  C   PHE A 479     4404   2996   3988    782  -1538   -665       C
ATOM   1073  O   PHE A 479     -19.671 -49.190 -31.751  1.00 28.72           O
ANISOU 1073  O   PHE A 479     4231   2758   3923    733  -1620   -649       O
ATOM   1074  CB  PHE A 479     -17.533 -48.086 -29.413  1.00 24.56           C
ANISOU 1074  CB  PHE A 479     3705   2331   3295    669  -1418   -605       C
ATOM   1075  CG  PHE A 479     -18.826 -47.480 -28.954  1.00 26.65           C
ANISOU 1075  CG  PHE A 479     3916   2546   3665    531  -1374   -570       C
ATOM   1076  CD1 PHE A 479     -19.274 -46.280 -29.486  1.00 24.94           C
ANISOU 1076  CD1 PHE A 479     3658   2375   3443    540  -1298   -590       C
ATOM   1077  CD2 PHE A 479     -19.590 -48.099 -27.981  1.00 34.42           C
ANISOU 1077  CD2 PHE A 479     4883   3441   4753    396  -1403   -510       C
ATOM   1078  CE1 PHE A 479     -20.460 -45.706 -29.051  1.00 29.73           C
ANISOU 1078  CE1 PHE A 479     4208   2933   4155    421  -1253   -556       C
ATOM   1079  CE2 PHE A 479     -20.779 -47.531 -27.541  1.00 36.07           C
ANISOU 1079  CE2 PHE A 479     5028   3616   5060    273  -1351   -467       C
ATOM   1080  CZ  PHE A 479     -21.212 -46.330 -28.075  1.00 29.03           C
ANISOU 1080  CZ  PHE A 479     4095   2765   4171    287  -1277   -493       C
ATOM   1081  N   PHE A 480     -17.838 -48.099 -32.463  1.00 27.65           N
ANISOU 1081  N   PHE A 480     4103   2813   3591    867  -1452   -703       N
ATOM   1082  CA  PHE A 480     -18.484 -47.679 -33.699  1.00 30.74           C
ANISOU 1082  CA  PHE A 480     4478   3238   3963    905  -1459   -735       C
ATOM   1083  C   PHE A 480     -18.331 -48.767 -34.748  1.00 33.98           C
ANISOU 1083  C   PHE A 480     4951   3587   4372    991  -1495   -790       C
ATOM   1084  O   PHE A 480     -17.396 -49.560 -34.683  1.00 31.06           O
ANISOU 1084  O   PHE A 480     4623   3222   3958   1033  -1499   -814       O
ATOM   1085  CB  PHE A 480     -17.892 -46.362 -34.177  1.00 29.02           C
ANISOU 1085  CB  PHE A 480     4240   3150   3638    943  -1342   -760       C
ATOM   1086  CG  PHE A 480     -18.168 -45.223 -33.241  1.00 23.12           C
ANISOU 1086  CG  PHE A 480     3448   2405   2932    886  -1281   -722       C
ATOM   1087  CD1 PHE A 480     -19.413 -44.623 -33.221  1.00 24.39           C
ANISOU 1087  CD1 PHE A 480     3570   2514   3183    829  -1307   -715       C
ATOM   1088  CD2 PHE A 480     -17.203 -44.788 -32.351  1.00 26.64           C
ANISOU 1088  CD2 PHE A 480     3892   2899   3332    883  -1202   -699       C
ATOM   1089  CE1 PHE A 480     -19.683 -43.580 -32.353  1.00 24.02           C
ANISOU 1089  CE1 PHE A 480     3479   2457   3190    747  -1187   -678       C
ATOM   1090  CE2 PHE A 480     -17.467 -43.748 -31.474  1.00 29.33           C
ANISOU 1090  CE2 PHE A 480     4198   3232   3716    797  -1095   -669       C
ATOM   1091  CZ  PHE A 480     -18.713 -43.143 -31.475  1.00 23.84           C
ANISOU 1091  CZ  PHE A 480     3461   2479   3119    726  -1075   -658       C
ATOM   1092  N   SER A 481     -19.256 -48.818 -35.703  1.00 36.79           N
ANISOU 1092  N   SER A 481     5323   3935   4721    961  -1558   -851       N
ATOM   1093  CA  SER A 481     -19.176 -49.832 -36.752  1.00 40.20           C
ANISOU 1093  CA  SER A 481     5811   4326   5137   1041  -1618   -904       C
ATOM   1094  C   SER A 481     -17.927 -49.594 -37.587  1.00 43.46           C
ANISOU 1094  C   SER A 481     6239   4854   5420   1154  -1539   -944       C
ATOM   1095  O   SER A 481     -17.178 -50.522 -37.896  1.00 43.63           O
ANISOU 1095  O   SER A 481     6302   4870   5407   1222  -1564   -976       O
ATOM   1096  CB  SER A 481     -20.424 -49.812 -37.638  1.00 40.49           C
ANISOU 1096  CB  SER A 481     5845   4322   5219   1026  -1692   -923       C
ATOM   1097  OG  SER A 481     -20.583 -48.554 -38.273  1.00 41.17           O
ANISOU 1097  OG  SER A 481     5892   4497   5252   1050  -1622   -928       O
ATOM   1098  N   GLU A 482     -17.715 -48.332 -37.943  1.00 35.35           N
ANISOU 1098  N   GLU A 482     5172   3933   4325   1173  -1446   -936       N
ATOM   1099  CA  GLU A 482     -16.530 -47.909 -38.673  1.00 29.10           C
ANISOU 1099  CA  GLU A 482     4377   3265   3415   1270  -1355   -953       C
ATOM   1100  C   GLU A 482     -16.406 -46.403 -38.516  1.00 29.70           C
ANISOU 1100  C   GLU A 482     4398   3437   3449   1251  -1248   -914       C
ATOM   1101  O   GLU A 482     -17.309 -45.757 -37.983  1.00 28.96           O
ANISOU 1101  O   GLU A 482     4276   3311   3417   1174  -1257   -886       O
ATOM   1102  CB  GLU A 482     -16.627 -48.280 -40.153  1.00 31.47           C
ANISOU 1102  CB  GLU A 482     4708   3580   3667   1357  -1392  -1007       C
ATOM   1103  CG  GLU A 482     -17.782 -47.624 -40.895  1.00 33.49           C
ANISOU 1103  CG  GLU A 482     4953   3826   3947   1337  -1416  -1013       C
ATOM   1104  CD  GLU A 482     -17.844 -48.027 -42.364  1.00 48.76           C
ANISOU 1104  CD  GLU A 482     6923   5773   5830   1427  -1456  -1067       C
ATOM   1105  OE1 GLU A 482     -18.819 -47.651 -43.044  1.00 53.03           O
ANISOU 1105  OE1 GLU A 482     7463   6292   6394   1417  -1490  -1077       O
ATOM   1106  OE2 GLU A 482     -16.919 -48.719 -42.842  1.00 52.02           O
ANISOU 1106  OE2 GLU A 482     7365   6218   6182   1512  -1455  -1099       O
ATOM   1107  N   GLY A 483     -15.289 -45.850 -38.972  1.00 29.51           N
ANISOU 1107  N   GLY A 483     4354   3532   3327   1321  -1152   -906       N
ATOM   1108  CA  GLY A 483     -15.066 -44.422 -38.860  1.00 29.98           C
ANISOU 1108  CA  GLY A 483     4362   3688   3343   1307  -1047   -862       C
ATOM   1109  C   GLY A 483     -13.735 -43.991 -39.428  1.00 28.23           C
ANISOU 1109  C   GLY A 483     4111   3595   3021   1387   -949   -844       C
ATOM   1110  O   GLY A 483     -13.068 -44.752 -40.132  1.00 28.14           O
ANISOU 1110  O   GLY A 483     4120   3606   2967   1464   -966   -876       O
ATOM   1111  N   CYS A 484     -13.371 -42.746 -39.149  1.00 23.47           N
ANISOU 1111  N   CYS A 484     3456   3078   2383   1368   -851   -790       N
ATOM   1112  CA  CYS A 484     -12.045 -42.249 -39.450  1.00 23.96           C
ANISOU 1112  CA  CYS A 484     3472   3265   2367   1423   -755   -750       C
ATOM   1113  C   CYS A 484     -11.467 -41.657 -38.188  1.00 28.78           C
ANISOU 1113  C   CYS A 484     4043   3907   2986   1369   -687   -690       C
ATOM   1114  O   CYS A 484     -11.967 -40.651 -37.683  1.00 25.41           O
ANISOU 1114  O   CYS A 484     3591   3485   2577   1311   -649   -653       O
ATOM   1115  CB  CYS A 484     -12.075 -41.168 -40.530  1.00 26.22           C
ANISOU 1115  CB  CYS A 484     3723   3642   2599   1459   -697   -727       C
ATOM   1116  SG  CYS A 484     -10.407 -40.554 -40.913  1.00 30.54           S
ANISOU 1116  SG  CYS A 484     4197   4347   3060   1518   -590   -664       S
ATOM   1117  N   ALA A 485     -10.422 -42.292 -37.674  1.00 24.47           N
ANISOU 1117  N   ALA A 485     3493   3378   2426   1388   -677   -682       N
ATOM   1118  CA  ALA A 485      -9.682 -41.749 -36.548  1.00 24.57           C
ANISOU 1118  CA  ALA A 485     3467   3435   2435   1344   -610   -623       C
ATOM   1119  C   ALA A 485      -8.206 -41.859 -36.876  1.00 22.57           C
ANISOU 1119  C   ALA A 485     3174   3283   2117   1403   -558   -599       C
ATOM   1120  O   ALA A 485      -7.571 -42.890 -36.609  1.00 27.50           O
ANISOU 1120  O   ALA A 485     3822   3885   2742   1432   -593   -627       O
ATOM   1121  CB  ALA A 485     -10.022 -42.493 -35.262  1.00 22.75           C
ANISOU 1121  CB  ALA A 485     3278   3098   2270   1288   -668   -637       C
ATOM   1122  N   PRO A 486      -7.657 -40.809 -37.498  1.00 24.22           N
ANISOU 1122  N   PRO A 486     3321   3607   2275   1420   -479   -548       N
ATOM   1123  CA  PRO A 486      -6.258 -40.858 -37.933  1.00 29.02           C
ANISOU 1123  CA  PRO A 486     3881   4320   2823   1476   -435   -522       C
ATOM   1124  C   PRO A 486      -5.324 -41.274 -36.804  1.00 29.38           C
ANISOU 1124  C   PRO A 486     3919   4367   2877   1452   -421   -504       C
ATOM   1125  O   PRO A 486      -5.429 -40.785 -35.675  1.00 25.37           O
ANISOU 1125  O   PRO A 486     3403   3836   2399   1379   -392   -466       O
ATOM   1126  CB  PRO A 486      -5.981 -39.423 -38.376  1.00 27.90           C
ANISOU 1126  CB  PRO A 486     3668   4284   2647   1459   -352   -449       C
ATOM   1127  CG  PRO A 486      -7.329 -38.936 -38.874  1.00 31.42           C
ANISOU 1127  CG  PRO A 486     4141   4682   3116   1443   -375   -468       C
ATOM   1128  CD  PRO A 486      -8.344 -39.581 -37.953  1.00 24.68           C
ANISOU 1128  CD  PRO A 486     3352   3698   2328   1394   -440   -514       C
ATOM   1129  N   GLY A 487      -4.416 -42.190 -37.117  1.00 29.87           N
ANISOU 1129  N   GLY A 487     3986   4455   2909   1519   -443   -534       N
ATOM   1130  CA  GLY A 487      -3.507 -42.734 -36.125  1.00 30.65           C
ANISOU 1130  CA  GLY A 487     4084   4548   3013   1507   -441   -527       C
ATOM   1131  C   GLY A 487      -3.875 -44.159 -35.772  1.00 28.90           C
ANISOU 1131  C   GLY A 487     3940   4211   2828   1526   -534   -601       C
ATOM   1132  O   GLY A 487      -3.109 -44.860 -35.106  1.00 32.85           O
ANISOU 1132  O   GLY A 487     4452   4700   3331   1534   -548   -611       O
ATOM   1133  N   SER A 488      -5.053 -44.589 -36.212  1.00 28.36           N
ANISOU 1133  N   SER A 488     3926   4055   2793   1529   -601   -650       N
ATOM   1134  CA  SER A 488      -5.500 -45.957 -36.001  1.00 23.72           C
ANISOU 1134  CA  SER A 488     3414   3350   2250   1542   -703   -716       C
ATOM   1135  C   SER A 488      -4.702 -46.918 -36.883  1.00 31.92           C
ANISOU 1135  C   SER A 488     4464   4422   3242   1644   -737   -765       C
ATOM   1136  O   SER A 488      -4.035 -46.499 -37.831  1.00 33.36           O
ANISOU 1136  O   SER A 488     4601   4715   3361   1709   -689   -753       O
ATOM   1137  CB  SER A 488      -6.997 -46.096 -36.294  1.00 31.48           C
ANISOU 1137  CB  SER A 488     4444   4232   3285   1512   -770   -750       C
ATOM   1138  OG  SER A 488      -7.775 -45.334 -35.376  1.00 29.85           O
ANISOU 1138  OG  SER A 488     4231   3984   3127   1419   -751   -712       O
ATOM   1139  N   LYS A 489      -4.779 -48.202 -36.560  1.00 33.59           N
ANISOU 1139  N   LYS A 489     4738   4538   3488   1660   -824   -817       N
ATOM   1140  CA  LYS A 489      -4.098 -49.229 -37.338  1.00 43.28           C
ANISOU 1140  CA  LYS A 489     5987   5783   4675   1761   -870   -872       C
ATOM   1141  C   LYS A 489      -4.669 -49.275 -38.752  1.00 46.63           C
ANISOU 1141  C   LYS A 489     6427   6220   5071   1827   -898   -913       C
ATOM   1142  O   LYS A 489      -5.882 -49.196 -38.944  1.00 45.05           O
ANISOU 1142  O   LYS A 489     6260   5943   4914   1788   -940   -927       O
ATOM   1143  CB  LYS A 489      -4.209 -50.587 -36.642  1.00 46.23           C
ANISOU 1143  CB  LYS A 489     6429   6034   5101   1754   -967   -917       C
ATOM   1144  CG  LYS A 489      -3.539 -50.606 -35.272  1.00 53.43           C
ANISOU 1144  CG  LYS A 489     7330   6936   6034   1698   -942   -880       C
ATOM   1145  CD  LYS A 489      -3.800 -51.894 -34.507  1.00 61.27           C
ANISOU 1145  CD  LYS A 489     8395   7796   7090   1676  -1044   -914       C
ATOM   1146  CE  LYS A 489      -3.170 -51.828 -33.119  1.00 63.99           C
ANISOU 1146  CE  LYS A 489     8730   8131   7454   1616  -1016   -874       C
ATOM   1147  NZ  LYS A 489      -3.442 -53.042 -32.299  1.00 66.45           N
ANISOU 1147  NZ  LYS A 489     9109   8308   7830   1584  -1117   -896       N
ATOM   1148  N   LYS A 490      -3.782 -49.387 -39.736  1.00 55.59           N
ANISOU 1148  N   LYS A 490     7535   7455   6131   1928   -876   -929       N
ATOM   1149  CA  LYS A 490      -4.167 -49.328 -41.144  1.00 61.13           C
ANISOU 1149  CA  LYS A 490     8245   8191   6793   2002   -892   -963       C
ATOM   1150  C   LYS A 490      -5.330 -50.259 -41.490  1.00 58.17           C
ANISOU 1150  C   LYS A 490     7954   7683   6466   2006  -1002  -1032       C
ATOM   1151  O   LYS A 490      -6.107 -49.975 -42.402  1.00 60.72           O
ANISOU 1151  O   LYS A 490     8291   8001   6781   2023  -1018  -1050       O
ATOM   1152  CB  LYS A 490      -2.984 -49.647 -42.037  1.00  0.00           C
ATOM   1153  CG  LYS A 490      -1.937 -48.544 -41.925  1.00  0.00           C
ATOM   1154  CD  LYS A 490      -0.756 -48.870 -42.832  1.00  0.00           C
ATOM   1155  CE  LYS A 490       0.309 -47.788 -42.689  1.00  0.00           C
ATOM   1156  NZ  LYS A 490       1.450 -48.105 -43.559  1.00  0.00           N
ATOM   1157  N   ASP A 491      -5.450 -51.362 -40.759  1.00 53.72           N
ANISOU 1157  N   ASP A 491     7447   7010   5955   1986  -1083  -1066       N
ATOM   1158  CA  ASP A 491      -6.488 -52.349 -41.039  1.00 61.90           C
ANISOU 1158  CA  ASP A 491     8562   7914   7044   1986  -1200  -1125       C
ATOM   1159  C   ASP A 491      -7.654 -52.305 -40.050  1.00 68.08           C
ANISOU 1159  C   ASP A 491     9370   8574   7925   1863  -1242  -1101       C
ATOM   1160  O   ASP A 491      -8.412 -53.267 -39.940  1.00 70.87           O
ANISOU 1160  O   ASP A 491     9785   8803   8340   1844  -1348  -1137       O
ATOM   1161  CB  ASP A 491      -5.903 -53.750 -41.056  1.00  0.00           C
ATOM   1162  CG  ASP A 491      -5.385 -54.097 -39.662  1.00  0.00           C
ATOM   1163  OD2 ASP A 491      -4.938 -55.262 -39.487  1.00  0.00           O
ATOM   1164  OD1 ASP A 491      -5.441 -53.194 -38.785  1.00  0.00           O
ATOM   1165  N   SER A 492      -7.798 -51.191 -39.334  1.00 61.01           N
ANISOU 1165  N   SER A 492     8425   7713   7044   1782  -1162  -1037       N
ATOM   1166  CA  SER A 492      -8.867 -51.049 -38.344  1.00 53.63           C
ANISOU 1166  CA  SER A 492     7506   6673   6198   1668  -1195  -1009       C
ATOM   1167  C   SER A 492     -10.151 -50.514 -38.971  1.00 39.09           C
ANISOU 1167  C   SER A 492     5670   4799   4383   1635  -1216  -1015       C
ATOM   1168  O   SER A 492     -10.121 -49.866 -40.015  1.00 37.60           O
ANISOU 1168  O   SER A 492     5459   4692   4136   1686  -1172  -1022       O
ATOM   1169  CB  SER A 492      -8.428 -50.125 -37.204  1.00 51.51           C
ANISOU 1169  CB  SER A 492     7185   6452   5933   1598  -1107   -941       C
ATOM   1170  OG  SER A 492      -9.442 -50.004 -36.216  1.00 56.41           O
ANISOU 1170  OG  SER A 492     7820   6975   6639   1493  -1142   -914       O
ATOM   1171  N   SER A 493     -11.279 -50.784 -38.324  1.00 35.39           N
ANISOU 1171  N   SER A 493     5229   4211   4006   1548  -1286  -1008       N
ATOM   1172  CA  SER A 493     -12.550 -50.252 -38.787  1.00 36.70           C
ANISOU 1172  CA  SER A 493     5396   4341   4207   1505  -1311  -1010       C
ATOM   1173  C   SER A 493     -12.526 -48.732 -38.703  1.00 35.15           C
ANISOU 1173  C   SER A 493     5139   4240   3975   1475  -1201   -963       C
ATOM   1174  O   SER A 493     -13.299 -48.056 -39.378  1.00 33.37           O
ANISOU 1174  O   SER A 493     4904   4028   3746   1467  -1195   -967       O
ATOM   1175  CB  SER A 493     -13.708 -50.806 -37.953  1.00 41.93           C
ANISOU 1175  CB  SER A 493     6086   4861   4985   1408  -1405   -998       C
ATOM   1176  OG  SER A 493     -13.604 -50.410 -36.597  1.00 50.91           O
ANISOU 1176  OG  SER A 493     7195   5984   6163   1328  -1368   -941       O
ATOM   1177  N   LEU A 494     -11.636 -48.197 -37.870  1.00 32.51           N
ANISOU 1177  N   LEU A 494     4765   3971   3616   1459  -1118   -917       N
ATOM   1178  CA  LEU A 494     -11.564 -46.747 -37.683  1.00 31.86           C
ANISOU 1178  CA  LEU A 494     4625   3976   3503   1427  -1015   -865       C
ATOM   1179  C   LEU A 494     -10.618 -46.080 -38.685  1.00 33.93           C
ANISOU 1179  C   LEU A 494     4845   4378   3669   1508   -928   -855       C
ATOM   1180  O   LEU A 494     -10.251 -44.915 -38.538  1.00 26.90           O
ANISOU 1180  O   LEU A 494     3899   3576   2744   1491   -835   -801       O
ATOM   1181  CB  LEU A 494     -11.196 -46.395 -36.237  1.00 28.57           C
ANISOU 1181  CB  LEU A 494     4185   3556   3115   1359   -972   -813       C
ATOM   1182  CG  LEU A 494     -12.322 -46.563 -35.209  1.00 29.32           C
ANISOU 1182  CG  LEU A 494     4300   3530   3309   1261  -1038   -801       C
ATOM   1183  CD1 LEU A 494     -11.868 -46.120 -33.817  1.00 28.34           C
ANISOU 1183  CD1 LEU A 494     4154   3416   3199   1202   -990   -748       C
ATOM   1184  CD2 LEU A 494     -13.587 -45.804 -35.606  1.00 33.73           C
ANISOU 1184  CD2 LEU A 494     4849   4066   3901   1218  -1050   -804       C
ATOM   1185  N   CYS A 495     -10.227 -46.823 -39.716  1.00 34.59           N
ANISOU 1185  N   CYS A 495     4952   4480   3710   1598   -964   -902       N
ATOM   1186  CA  CYS A 495      -9.493 -46.232 -40.832  1.00 27.35           C
ANISOU 1186  CA  CYS A 495     3995   3689   2707   1679   -896   -893       C
ATOM   1187  C   CYS A 495     -10.332 -46.280 -42.108  1.00 28.98           C
ANISOU 1187  C   CYS A 495     4233   3879   2901   1722   -944   -937       C
ATOM   1188  O   CYS A 495      -9.974 -45.680 -43.121  1.00 31.81           O
ANISOU 1188  O   CYS A 495     4559   4333   3193   1784   -894   -928       O
ATOM   1189  CB  CYS A 495      -8.159 -46.953 -41.060  1.00 38.86           C
ANISOU 1189  CB  CYS A 495     5445   5209   4110   1764   -888   -908       C
ATOM   1190  SG  CYS A 495      -6.815 -46.403 -39.970  1.00 39.22           S
ANISOU 1190  SG  CYS A 495     5423   5344   4133   1735   -793   -837       S
ATOM   1191  N   LYS A 496     -11.452 -46.990 -42.044  1.00 31.62           N
ANISOU 1191  N   LYS A 496     4624   4089   3301   1687  -1044   -981       N
ATOM   1192  CA  LYS A 496     -12.268 -47.251 -43.232  1.00 32.33           C
ANISOU 1192  CA  LYS A 496     4752   4146   3385   1729  -1109  -1030       C
ATOM   1193  C   LYS A 496     -12.792 -45.994 -43.930  1.00 36.15           C
ANISOU 1193  C   LYS A 496     5204   4691   3842   1722  -1055  -1005       C
ATOM   1194  O   LYS A 496     -12.935 -45.976 -45.155  1.00 35.78           O
ANISOU 1194  O   LYS A 496     5170   4675   3751   1793  -1070  -1035       O
ATOM   1195  CB  LYS A 496     -13.430 -48.186 -42.887  1.00 36.96           C
ANISOU 1195  CB  LYS A 496     5396   4582   4063   1674  -1230  -1067       C
ATOM   1196  CG  LYS A 496     -12.997 -49.629 -42.617  1.00 48.88           C
ANISOU 1196  CG  LYS A 496     6954   6023   5593   1707  -1309  -1107       C
ATOM   1197  CD  LYS A 496     -14.194 -50.538 -42.358  1.00 56.90           C
ANISOU 1197  CD  LYS A 496     8023   6889   6707   1649  -1435  -1134       C
ATOM   1198  CE  LYS A 496     -13.764 -51.989 -42.198  1.00 65.67           C
ANISOU 1198  CE  LYS A 496     9186   7929   7837   1689  -1519  -1174       C
ATOM   1199  NZ  LYS A 496     -13.183 -52.544 -43.455  1.00 71.65           N
ANISOU 1199  NZ  LYS A 496     9973   8732   8517   1814  -1541  -1234       N
ATOM   1200  N   LEU A 497     -13.069 -44.942 -43.165  1.00 28.23           N
ANISOU 1200  N   LEU A 497     4159   3704   2863   1642   -995   -950       N
ATOM   1201  CA  LEU A 497     -13.688 -43.746 -43.735  1.00 27.43           C
ANISOU 1201  CA  LEU A 497     4031   3644   2747   1627   -954   -926       C
ATOM   1202  C   LEU A 497     -12.679 -42.662 -44.085  1.00 29.22           C
ANISOU 1202  C   LEU A 497     4193   4012   2896   1666   -838   -870       C
ATOM   1203  O   LEU A 497     -13.048 -41.627 -44.621  1.00 33.56           O
ANISOU 1203  O   LEU A 497     4718   4608   3426   1662   -798   -845       O
ATOM   1204  CB  LEU A 497     -14.734 -43.167 -42.777  1.00 29.15           C
ANISOU 1204  CB  LEU A 497     4241   3794   3042   1519   -968   -902       C
ATOM   1205  CG  LEU A 497     -16.021 -43.967 -42.582  1.00 35.80           C
ANISOU 1205  CG  LEU A 497     5129   4499   3976   1468  -1088   -943       C
ATOM   1206  CD1 LEU A 497     -17.046 -43.158 -41.803  1.00 37.50           C
ANISOU 1206  CD1 LEU A 497     5317   4669   4263   1372  -1092   -911       C
ATOM   1207  CD2 LEU A 497     -16.584 -44.381 -43.931  1.00 41.14           C
ANISOU 1207  CD2 LEU A 497     5842   5153   4638   1528  -1154   -994       C
ATOM   1208  N   CYS A 498     -11.408 -42.884 -43.763  1.00 27.81           N
ANISOU 1208  N   CYS A 498     3984   3901   2680   1700   -788   -846       N
ATOM   1209  CA  CYS A 498     -10.390 -41.864 -44.009  1.00 30.80           C
ANISOU 1209  CA  CYS A 498     4290   4417   2996   1726   -684   -780       C
ATOM   1210  C   CYS A 498     -10.203 -41.636 -45.519  1.00 33.94           C
ANISOU 1210  C   CYS A 498     4677   4894   3326   1819   -674   -793       C
ATOM   1211  O   CYS A 498     -10.617 -42.462 -46.323  1.00 37.38           O
ANISOU 1211  O   CYS A 498     5165   5283   3754   1878   -747   -858       O
ATOM   1212  CB  CYS A 498      -9.081 -42.219 -43.289  1.00 32.85           C
ANISOU 1212  CB  CYS A 498     4515   4728   3238   1736   -645   -751       C
ATOM   1213  SG  CYS A 498      -9.223 -42.142 -41.446  1.00 35.59           S
ANISOU 1213  SG  CYS A 498     4861   5003   3657   1622   -635   -717       S
ATOM   1214  N   MET A 499      -9.623 -40.502 -45.901  1.00 33.24           N
ANISOU 1214  N   MET A 499     4520   4922   3189   1831   -590   -727       N
ATOM   1215  CA  MET A 499      -9.626 -40.101 -47.306  1.00 37.52           C
ANISOU 1215  CA  MET A 499     5049   5537   3670   1910   -580   -732       C
ATOM   1216  C   MET A 499      -8.225 -39.936 -47.892  1.00 40.55           C
ANISOU 1216  C   MET A 499     5367   6064   3976   1988   -522   -692       C
ATOM   1217  O   MET A 499      -8.075 -39.634 -49.076  1.00 37.04           O
ANISOU 1217  O   MET A 499     4904   5697   3471   2065   -511   -691       O
ATOM   1218  CB  MET A 499     -10.430 -38.805 -47.500  1.00 31.73           C
ANISOU 1218  CB  MET A 499     4297   4814   2947   1861   -546   -693       C
ATOM   1219  CG  MET A 499      -9.657 -37.526 -47.194  1.00 30.25           C
ANISOU 1219  CG  MET A 499     4023   4739   2733   1827   -447   -597       C
ATOM   1220  SD  MET A 499     -10.579 -36.020 -47.610  1.00 37.95           S
ANISOU 1220  SD  MET A 499     4979   5730   3710   1787   -414   -556       S
ATOM   1221  CE  MET A 499      -9.318 -35.079 -48.471  1.00 54.93           C
ANISOU 1221  CE  MET A 499     7035   8062   5775   1844   -329   -473       C
ATOM   1222  N   GLY A 500      -7.206 -40.135 -47.065  1.00 34.30           N
ANISOU 1222  N   GLY A 500     4538   5310   3184   1970   -488   -658       N
ATOM   1223  CA  GLY A 500      -5.834 -39.972 -47.502  1.00 31.68           C
ANISOU 1223  CA  GLY A 500     4137   5118   2783   2034   -437   -615       C
ATOM   1224  C   GLY A 500      -5.478 -40.809 -48.719  1.00 34.41           C
ANISOU 1224  C   GLY A 500     4501   5506   3066   2162   -478   -672       C
ATOM   1225  O   GLY A 500      -5.688 -42.019 -48.743  1.00 35.93           O
ANISOU 1225  O   GLY A 500     4760   5618   3272   2204   -551   -748       O
ATOM   1226  N   SER A 501      -4.917 -40.155 -49.725  1.00 39.15           N
ANISOU 1226  N   SER A 501     5043   6238   3596   2227   -434   -633       N
ATOM   1227  CA  SER A 501      -4.542 -40.838 -50.959  1.00 46.04           C
ANISOU 1227  CA  SER A 501     5926   7170   4397   2361   -468   -682       C
ATOM   1228  C   SER A 501      -3.166 -41.469 -50.820  1.00 45.16           C
ANISOU 1228  C   SER A 501     5774   7143   4241   2422   -457   -676       C
ATOM   1229  O   SER A 501      -2.346 -41.033 -50.009  1.00 41.48           O
ANISOU 1229  O   SER A 501     5247   6731   3782   2366   -404   -610       O
ATOM   1230  CB  SER A 501      -4.553 -39.863 -52.133  1.00 44.15           C
ANISOU 1230  CB  SER A 501     5638   7042   4094   2411   -428   -641       C
ATOM   1231  OG  SER A 501      -3.529 -38.896 -51.982  1.00 48.05           O
ANISOU 1231  OG  SER A 501     6031   7675   4553   2388   -346   -544       O
ATOM   1232  N   GLY A 502      -2.909 -42.501 -51.615  1.00 52.75           N
ANISOU 1232  N   GLY A 502     6771   8116   5157   2541   -512   -745       N
ATOM   1233  CA  GLY A 502      -1.666 -43.231 -51.495  1.00 51.49           C
ANISOU 1233  CA  GLY A 502     6582   8028   4955   2610   -514   -753       C
ATOM   1234  C   GLY A 502      -1.509 -43.779 -50.092  1.00 54.51           C
ANISOU 1234  C   GLY A 502     6990   8317   5405   2528   -528   -760       C
ATOM   1235  O   GLY A 502      -2.470 -44.274 -49.503  1.00 57.99           O
ANISOU 1235  O   GLY A 502     7507   8611   5916   2469   -579   -807       O
ATOM   1236  N   LEU A 503      -0.299 -43.678 -49.551  1.00 47.75           N
ANISOU 1236  N   LEU A 503     6069   7550   4526   2523   -483   -711       N
ATOM   1237  CA  LEU A 503      -0.005 -44.219 -48.233  1.00 45.80           C
ANISOU 1237  CA  LEU A 503     5841   7226   4333   2456   -494   -717       C
ATOM   1238  C   LEU A 503      -0.326 -43.233 -47.103  1.00 44.43           C
ANISOU 1238  C   LEU A 503     5641   7015   4224   2311   -441   -646       C
ATOM   1239  O   LEU A 503      -0.036 -43.505 -45.941  1.00 41.15           O
ANISOU 1239  O   LEU A 503     5233   6549   3853   2247   -440   -638       O
ATOM   1240  CB  LEU A 503       1.446 -44.642 -48.134  1.00  0.00           C
ATOM   1241  CG  LEU A 503       1.755 -45.685 -49.202  1.00  0.00           C
ATOM   1242  CD1 LEU A 503       3.238 -46.036 -49.156  1.00  0.00           C
ATOM   1243  CD2 LEU A 503       0.928 -46.940 -48.941  1.00  0.00           C
ATOM   1244  N   ASN A 504      -0.921 -42.095 -47.444  1.00 43.14           N
ANISOU 1244  N   ASN A 504     5450   6876   4065   2264   -400   -596       N
ATOM   1245  CA  ASN A 504      -1.323 -41.122 -46.427  1.00 38.16           C
ANISOU 1245  CA  ASN A 504     4799   6206   3495   2133   -354   -533       C
ATOM   1246  C   ASN A 504      -2.607 -41.532 -45.708  1.00 40.81           C
ANISOU 1246  C   ASN A 504     5219   6377   3909   2064   -405   -584       C
ATOM   1247  O   ASN A 504      -2.969 -40.954 -44.682  1.00 38.47           O
ANISOU 1247  O   ASN A 504     4919   6031   3668   1960   -379   -544       O
ATOM   1248  CB  ASN A 504      -1.486 -39.734 -47.042  1.00 40.64           C
ANISOU 1248  CB  ASN A 504     5052   6607   3784   2108   -294   -461       C
ATOM   1249  CG  ASN A 504      -0.190 -39.191 -47.595  1.00 47.15           C
ANISOU 1249  CG  ASN A 504     5779   7599   4536   2155   -239   -393       C
ATOM   1250  OD1 ASN A 504       0.878 -39.422 -47.034  1.00 48.03           O
ANISOU 1250  OD1 ASN A 504     5851   7761   4636   2152   -221   -368       O
ATOM   1251  ND2 ASN A 504      -0.275 -38.465 -48.705  1.00 51.52           N
ANISOU 1251  ND2 ASN A 504     6293   8245   5039   2200   -214   -363       N
ATOM   1252  N   LEU A 505      -3.280 -42.541 -46.248  1.00 36.90           N
ANISOU 1252  N   LEU A 505     4801   5801   3420   2124   -482   -670       N
ATOM   1253  CA  LEU A 505      -4.537 -43.030 -45.699  1.00 30.94           C
ANISOU 1253  CA  LEU A 505     4127   4891   2737   2066   -544   -722       C
ATOM   1254  C   LEU A 505      -4.469 -43.246 -44.186  1.00 33.57           C
ANISOU 1254  C   LEU A 505     4470   5151   3133   1974   -543   -706       C
ATOM   1255  O   LEU A 505      -3.701 -44.080 -43.705  1.00 31.53           O
ANISOU 1255  O   LEU A 505     4219   4888   2871   1999   -562   -726       O
ATOM   1256  CB  LEU A 505      -4.914 -44.346 -46.370  1.00 36.62           C
ANISOU 1256  CB  LEU A 505     4924   5538   3451   2149   -637   -818       C
ATOM   1257  CG  LEU A 505      -6.163 -45.041 -45.837  1.00 39.49           C
ANISOU 1257  CG  LEU A 505     5373   5738   3891   2091   -718   -875       C
ATOM   1258  CD1 LEU A 505      -7.389 -44.151 -46.009  1.00 38.56           C
ANISOU 1258  CD1 LEU A 505     5264   5579   3806   2027   -712   -860       C
ATOM   1259  CD2 LEU A 505      -6.354 -46.367 -46.545  1.00 42.78           C
ANISOU 1259  CD2 LEU A 505     5863   6095   4298   2179   -813   -965       C
ATOM   1260  N   CYS A 506      -5.287 -42.499 -43.449  1.00 36.27           N
ANISOU 1260  N   CYS A 506     4814   5438   3529   1874   -523   -673       N
ATOM   1261  CA  CYS A 506      -5.442 -42.691 -42.006  1.00 34.22           C
ANISOU 1261  CA  CYS A 506     4573   5097   3332   1786   -530   -662       C
ATOM   1262  C   CYS A 506      -4.251 -42.220 -41.179  1.00 35.00           C
ANISOU 1262  C   CYS A 506     4607   5275   3416   1753   -461   -595       C
ATOM   1263  O   CYS A 506      -4.164 -42.511 -39.983  1.00 36.78           O
ANISOU 1263  O   CYS A 506     4847   5443   3683   1695   -467   -589       O
ATOM   1264  CB  CYS A 506      -5.760 -44.154 -41.680  1.00 37.30           C
ANISOU 1264  CB  CYS A 506     5041   5372   3759   1805   -623   -740       C
ATOM   1265  SG  CYS A 506      -6.581 -44.384 -40.074  1.00 36.54           S
ANISOU 1265  SG  CYS A 506     4988   5141   3755   1690   -658   -739       S
ATOM   1266  N   GLU A 507      -3.348 -41.472 -41.801  1.00 33.23           N
ANISOU 1266  N   GLU A 507     4310   5183   3135   1786   -398   -541       N
ATOM   1267  CA  GLU A 507      -2.199 -40.936 -41.078  1.00 36.20           C
ANISOU 1267  CA  GLU A 507     4618   5638   3498   1748   -334   -471       C
ATOM   1268  C   GLU A 507      -2.590 -39.711 -40.261  1.00 29.88           C
ANISOU 1268  C   GLU A 507     3785   4830   2736   1641   -280   -400       C
ATOM   1269  O   GLU A 507      -3.345 -38.865 -40.732  1.00 30.79           O
ANISOU 1269  O   GLU A 507     3893   4951   2855   1619   -262   -380       O
ATOM   1270  CB  GLU A 507      -1.067 -40.589 -42.044  1.00 42.24           C
ANISOU 1270  CB  GLU A 507     5311   6549   4188   1820   -293   -434       C
ATOM   1271  CG  GLU A 507      -0.354 -41.812 -42.614  1.00 55.86           C
ANISOU 1271  CG  GLU A 507     7055   8300   5868   1929   -339   -495       C
ATOM   1272  CD  GLU A 507       0.320 -42.651 -41.535  1.00 66.16           C
ANISOU 1272  CD  GLU A 507     8378   9564   7196   1915   -358   -514       C
ATOM   1273  OE1 GLU A 507       1.277 -42.150 -40.903  1.00 67.89           O
ANISOU 1273  OE1 GLU A 507     8538   9851   7407   1876   -306   -452       O
ATOM   1274  OE2 GLU A 507      -0.110 -43.806 -41.313  1.00 66.40           O
ANISOU 1274  OE2 GLU A 507     8483   9492   7252   1940   -428   -589       O
ATOM   1275  N   PRO A 508      -2.063 -39.608 -39.032  1.00 28.26           N
ANISOU 1275  N   PRO A 508     3564   4614   2559   1577   -254   -365       N
ATOM   1276  CA  PRO A 508      -2.384 -38.474 -38.160  1.00 31.91           C
ANISOU 1276  CA  PRO A 508     3998   5067   3058   1477   -204   -299       C
ATOM   1277  C   PRO A 508      -1.568 -37.240 -38.531  1.00 30.04           C
ANISOU 1277  C   PRO A 508     3672   4952   2789   1457   -134   -211       C
ATOM   1278  O   PRO A 508      -0.731 -36.784 -37.754  1.00 32.84           O
ANISOU 1278  O   PRO A 508     3981   5346   3152   1405    -94   -152       O
ATOM   1279  CB  PRO A 508      -1.984 -38.983 -36.775  1.00 31.33           C
ANISOU 1279  CB  PRO A 508     3944   4941   3018   1431   -210   -300       C
ATOM   1280  CG  PRO A 508      -0.830 -39.900 -37.057  1.00 29.24           C
ANISOU 1280  CG  PRO A 508     3671   4725   2715   1503   -226   -325       C
ATOM   1281  CD  PRO A 508      -1.129 -40.553 -38.395  1.00 27.24           C
ANISOU 1281  CD  PRO A 508     3444   4480   2426   1599   -272   -386       C
ATOM   1282  N   ASN A 509      -1.827 -36.709 -39.721  1.00 36.28           N
ANISOU 1282  N   ASN A 509     4439   5800   3546   1496   -125   -201       N
ATOM   1283  CA  ASN A 509      -1.165 -35.502 -40.192  1.00 30.54           C
ANISOU 1283  CA  ASN A 509     3627   5188   2790   1477    -67   -116       C
ATOM   1284  C   ASN A 509      -1.980 -34.873 -41.315  1.00 33.77           C
ANISOU 1284  C   ASN A 509     4034   5618   3178   1504    -65   -115       C
ATOM   1285  O   ASN A 509      -2.947 -35.468 -41.792  1.00 33.81           O
ANISOU 1285  O   ASN A 509     4104   5555   3188   1547   -112   -187       O
ATOM   1286  CB  ASN A 509       0.250 -35.822 -40.679  1.00 47.34           C
ANISOU 1286  CB  ASN A 509     5699   7426   4861   1538    -54    -96       C
ATOM   1287  CG  ASN A 509       0.256 -36.703 -41.913  1.00 52.65           C
ANISOU 1287  CG  ASN A 509     6396   8130   5479   1656    -92   -161       C
ATOM   1288  OD1 ASN A 509      -0.006 -36.236 -43.019  1.00 57.94           O
ANISOU 1288  OD1 ASN A 509     7046   8858   6113   1699    -85   -152       O
ATOM   1289  ND2 ASN A 509       0.557 -37.983 -41.731  1.00 54.84           N
ANISOU 1289  ND2 ASN A 509     6718   8368   5750   1712   -137   -228       N
ATOM   1290  N   ASN A 510      -1.582 -33.677 -41.737  1.00 42.34           N
ANISOU 1290  N   ASN A 510     5046   6799   4244   1478    -17    -35       N
ATOM   1291  CA  ASN A 510      -2.352 -32.903 -42.711  1.00 46.53           C
ANISOU 1291  CA  ASN A 510     5569   7354   4758   1493    -10    -23       C
ATOM   1292  C   ASN A 510      -2.491 -33.528 -44.097  1.00 42.95           C
ANISOU 1292  C   ASN A 510     5135   6937   4245   1606    -40    -79       C
ATOM   1293  O   ASN A 510      -3.274 -33.049 -44.919  1.00 40.64           O
ANISOU 1293  O   ASN A 510     4853   6650   3940   1628    -44    -86       O
ATOM   1294  CB  ASN A 510      -1.796 -31.481 -42.837  1.00 56.12           C
ANISOU 1294  CB  ASN A 510     6693   8668   5964   1436     46     83       C
ATOM   1295  CG  ASN A 510      -2.587 -30.472 -42.027  1.00 72.66           C
ANISOU 1295  CG  ASN A 510     8790  10701   8117   1336     64    122       C
ATOM   1296  OD1 ASN A 510      -3.246 -30.824 -41.046  1.00 74.03           O
ANISOU 1296  OD1 ASN A 510     9021  10769   8340   1295     46     85       O
ATOM   1297  ND2 ASN A 510      -2.531 -29.210 -42.438  1.00 79.42           N
ANISOU 1297  ND2 ASN A 510     9590  11620   8966   1289     96    200       N
ATOM   1298  N   LYS A 511      -1.734 -34.587 -44.366  1.00 42.86           N
ANISOU 1298  N   LYS A 511     5131   6954   4198   1681    -64   -121       N
ATOM   1299  CA  LYS A 511      -1.833 -35.258 -45.655  1.00 39.90           C
ANISOU 1299  CA  LYS A 511     4779   6613   3767   1796    -98   -179       C
ATOM   1300  C   LYS A 511      -3.090 -36.117 -45.692  1.00 42.06           C
ANISOU 1300  C   LYS A 511     5154   6751   4075   1817   -164   -275       C
ATOM   1301  O   LYS A 511      -3.512 -36.571 -46.751  1.00 38.11           O
ANISOU 1301  O   LYS A 511     4688   6250   3540   1900   -200   -330       O
ATOM   1302  CB  LYS A 511      -0.614 -36.112 -45.936  1.00  0.00           C
ATOM   1303  CG  LYS A 511       0.619 -35.230 -46.096  1.00  0.00           C
ATOM   1304  CD  LYS A 511       1.837 -36.105 -46.373  1.00  0.00           C
ATOM   1305  CE  LYS A 511       3.070 -35.222 -46.540  1.00  0.00           C
ATOM   1306  NZ  LYS A 511       4.250 -36.068 -46.769  1.00  0.00           N
ATOM   1307  N   GLU A 512      -3.686 -36.330 -44.520  1.00 36.84           N
ANISOU 1307  N   GLU A 512     4539   5976   3482   1739   -181   -293       N
ATOM   1308  CA  GLU A 512      -4.962 -37.028 -44.411  1.00 32.05           C
ANISOU 1308  CA  GLU A 512     4023   5236   2918   1738   -246   -374       C
ATOM   1309  C   GLU A 512      -6.077 -35.985 -44.274  1.00 31.20           C
ANISOU 1309  C   GLU A 512     3922   5086   2847   1670   -231   -350       C
ATOM   1310  O   GLU A 512      -6.108 -35.232 -43.312  1.00 30.02           O
ANISOU 1310  O   GLU A 512     3746   4926   2732   1584   -193   -296       O
ATOM   1311  CB  GLU A 512      -4.939 -37.979 -43.209  1.00 31.76           C
ANISOU 1311  CB  GLU A 512     4032   5105   2932   1701   -281   -411       C
ATOM   1312  CG  GLU A 512      -6.292 -38.468 -42.722  1.00 32.11           C
ANISOU 1312  CG  GLU A 512     4156   5006   3038   1661   -342   -471       C
ATOM   1313  CD  GLU A 512      -7.108 -39.149 -43.802  1.00 31.16           C
ANISOU 1313  CD  GLU A 512     4096   4836   2908   1730   -410   -549       C
ATOM   1314  OE1 GLU A 512      -6.654 -40.181 -44.349  1.00 32.79           O
ANISOU 1314  OE1 GLU A 512     4327   5048   3085   1810   -451   -600       O
ATOM   1315  OE2 GLU A 512      -8.216 -38.648 -44.104  1.00 29.30           O
ANISOU 1315  OE2 GLU A 512     3885   4555   2694   1705   -425   -561       O
ATOM   1316  N   GLY A 513      -6.978 -35.938 -45.252  1.00 32.15           N
ANISOU 1316  N   GLY A 513     4078   5183   2954   1712   -263   -391       N
ATOM   1317  CA  GLY A 513      -7.991 -34.895 -45.311  1.00 33.09           C
ANISOU 1317  CA  GLY A 513     4200   5275   3096   1662   -250   -370       C
ATOM   1318  C   GLY A 513      -8.953 -34.814 -44.134  1.00 33.28           C
ANISOU 1318  C   GLY A 513     4266   5186   3193   1574   -270   -384       C
ATOM   1319  O   GLY A 513      -9.524 -33.753 -43.870  1.00 34.23           O
ANISOU 1319  O   GLY A 513     4370   5304   3333   1518   -241   -344       O
ATOM   1320  N   TYR A 514      -9.143 -35.921 -43.421  1.00 28.37           N
ANISOU 1320  N   TYR A 514     3696   4473   2610   1563   -321   -438       N
ATOM   1321  CA  TYR A 514     -10.077 -35.921 -42.293  1.00 20.46           C
ANISOU 1321  CA  TYR A 514     2732   3366   1676   1483   -347   -453       C
ATOM   1322  C   TYR A 514      -9.377 -35.763 -40.940  1.00 28.55           C
ANISOU 1322  C   TYR A 514     3724   4400   2722   1420   -304   -402       C
ATOM   1323  O   TYR A 514      -9.996 -35.907 -39.882  1.00 27.48           O
ANISOU 1323  O   TYR A 514     3619   4183   2640   1361   -326   -414       O
ATOM   1324  CB  TYR A 514     -10.952 -37.176 -42.306  1.00 24.35           C
ANISOU 1324  CB  TYR A 514     3305   3739   2208   1498   -442   -544       C
ATOM   1325  CG  TYR A 514     -11.889 -37.267 -43.490  1.00 25.27           C
ANISOU 1325  CG  TYR A 514     3462   3824   2317   1541   -495   -598       C
ATOM   1326  CD1 TYR A 514     -12.150 -36.158 -44.287  1.00 27.75           C
ANISOU 1326  CD1 TYR A 514     3747   4197   2599   1554   -458   -566       C
ATOM   1327  CD2 TYR A 514     -12.520 -38.461 -43.801  1.00 27.12           C
ANISOU 1327  CD2 TYR A 514     3763   3965   2577   1567   -588   -677       C
ATOM   1328  CE1 TYR A 514     -13.014 -36.249 -45.376  1.00 26.78           C
ANISOU 1328  CE1 TYR A 514     3664   4043   2469   1596   -510   -617       C
ATOM   1329  CE2 TYR A 514     -13.383 -38.560 -44.880  1.00 31.61           C
ANISOU 1329  CE2 TYR A 514     4369   4501   3141   1604   -643   -725       C
ATOM   1330  CZ  TYR A 514     -13.624 -37.454 -45.660  1.00 26.88           C
ANISOU 1330  CZ  TYR A 514     3743   3962   2509   1620   -603   -696       C
ATOM   1331  OH  TYR A 514     -14.481 -37.570 -46.730  1.00 29.67           O
ANISOU 1331  OH  TYR A 514     4135   4279   2857   1659   -661   -745       O
ATOM   1332  N   TYR A 515      -8.091 -35.439 -40.983  1.00 24.86           N
ANISOU 1332  N   TYR A 515     3194   4036   2216   1432   -246   -342       N
ATOM   1333  CA  TYR A 515      -7.318 -35.216 -39.769  1.00 25.16           C
ANISOU 1333  CA  TYR A 515     3196   4090   2271   1372   -203   -288       C
ATOM   1334  C   TYR A 515      -7.596 -33.834 -39.190  1.00 26.83           C
ANISOU 1334  C   TYR A 515     3369   4323   2504   1295   -148   -216       C
ATOM   1335  O   TYR A 515      -7.734 -32.858 -39.928  1.00 27.76           O
ANISOU 1335  O   TYR A 515     3450   4498   2600   1298   -118   -178       O
ATOM   1336  CB  TYR A 515      -5.827 -35.386 -40.079  1.00 27.95           C
ANISOU 1336  CB  TYR A 515     3494   4545   2578   1412   -170   -253       C
ATOM   1337  CG  TYR A 515      -4.891 -34.906 -38.997  1.00 26.92           C
ANISOU 1337  CG  TYR A 515     3313   4454   2462   1347   -119   -183       C
ATOM   1338  CD1 TYR A 515      -4.715 -35.635 -37.830  1.00 29.03           C
ANISOU 1338  CD1 TYR A 515     3612   4658   2761   1317   -136   -204       C
ATOM   1339  CD2 TYR A 515      -4.166 -33.732 -39.151  1.00 32.83           C
ANISOU 1339  CD2 TYR A 515     3982   5300   3193   1314    -58    -96       C
ATOM   1340  CE1 TYR A 515      -3.852 -35.202 -36.840  1.00 28.13           C
ANISOU 1340  CE1 TYR A 515     3453   4574   2659   1260    -92   -142       C
ATOM   1341  CE2 TYR A 515      -3.301 -33.290 -38.167  1.00 36.17           C
ANISOU 1341  CE2 TYR A 515     4358   5750   3633   1250    -19    -33       C
ATOM   1342  CZ  TYR A 515      -3.147 -34.031 -37.014  1.00 38.96           C
ANISOU 1342  CZ  TYR A 515     4747   6039   4017   1225    -35    -58       C
ATOM   1343  OH  TYR A 515      -2.284 -33.598 -36.032  1.00 40.26           O
ANISOU 1343  OH  TYR A 515     4873   6225   4201   1157      2      3       O
ATOM   1344  N   GLY A 516      -7.698 -33.750 -37.867  1.00 21.38           N
ANISOU 1344  N   GLY A 516     2685   3584   1854   1228   -138   -198       N
ATOM   1345  CA  GLY A 516      -7.850 -32.467 -37.207  1.00 21.31           C
ANISOU 1345  CA  GLY A 516     2651   3581   1866   1120    -86   -122       C
ATOM   1346  C   GLY A 516      -9.307 -32.075 -37.016  1.00 20.62           C
ANISOU 1346  C   GLY A 516     2611   3415   1808   1079   -110   -148       C
ATOM   1347  O   GLY A 516     -10.207 -32.801 -37.433  1.00 21.77           O
ANISOU 1347  O   GLY A 516     2802   3504   1964   1143   -173   -227       O
ATOM   1348  N   TYR A 517      -9.541 -30.930 -36.384  1.00 21.99           N
ANISOU 1348  N   TYR A 517     2774   3581   2000    974    -66    -85       N
ATOM   1349  CA  TYR A 517     -10.911 -30.456 -36.163  1.00 21.33           C
ANISOU 1349  CA  TYR A 517     2730   3434   1942    938    -86   -107       C
ATOM   1350  C   TYR A 517     -11.679 -30.256 -37.457  1.00 22.26           C
ANISOU 1350  C   TYR A 517     2853   3562   2044   1008   -125   -142       C
ATOM   1351  O   TYR A 517     -12.795 -30.752 -37.602  1.00 20.95           O
ANISOU 1351  O   TYR A 517     2732   3326   1901   1043   -190   -216       O
ATOM   1352  CB  TYR A 517     -10.919 -29.138 -35.403  1.00 20.46           C
ANISOU 1352  CB  TYR A 517     2603   3324   1849    826    -26    -29       C
ATOM   1353  CG  TYR A 517     -10.426 -29.240 -33.994  1.00 21.13           C
ANISOU 1353  CG  TYR A 517     2695   3375   1961    744     15     -3       C
ATOM   1354  CD1 TYR A 517     -11.197 -29.854 -33.014  1.00 21.87           C
ANISOU 1354  CD1 TYR A 517     2836   3391   2081    722      8    -58       C
ATOM   1355  CD2 TYR A 517      -9.199 -28.703 -33.627  1.00 21.12           C
ANISOU 1355  CD2 TYR A 517     2651   3410   1963    685     60     70       C
ATOM   1356  CE1 TYR A 517     -10.757 -29.941 -31.715  1.00 22.85           C
ANISOU 1356  CE1 TYR A 517     2968   3480   2232    645     54    -35       C
ATOM   1357  CE2 TYR A 517      -8.751 -28.781 -32.313  1.00 24.37           C
ANISOU 1357  CE2 TYR A 517     3074   3779   2406    608     92     89       C
ATOM   1358  CZ  TYR A 517      -9.541 -29.405 -31.366  1.00 29.05           C
ANISOU 1358  CZ  TYR A 517     3716   4300   3021    589     93     40       C
ATOM   1359  OH  TYR A 517      -9.118 -29.494 -30.060  1.00 32.65           O
ANISOU 1359  OH  TYR A 517     4185   4712   3509    513    130     59       O
ATOM   1360  N   THR A 518     -11.103 -29.493 -38.382  1.00 23.75           N
ANISOU 1360  N   THR A 518     2996   3830   2197   1020    -91    -90       N
ATOM   1361  CA  THR A 518     -11.791 -29.212 -39.634  1.00 25.43           C
ANISOU 1361  CA  THR A 518     3218   4055   2389   1078   -120   -118       C
ATOM   1362  C   THR A 518     -11.947 -30.502 -40.422  1.00 25.73           C
ANISOU 1362  C   THR A 518     3288   4076   2412   1194   -174   -213       C
ATOM   1363  O   THR A 518     -12.951 -30.717 -41.090  1.00 25.01           O
ANISOU 1363  O   THR A 518     3239   3935   2328   1237   -227   -278       O
ATOM   1364  CB  THR A 518     -11.044 -28.170 -40.492  1.00 34.80           C
ANISOU 1364  CB  THR A 518     4349   5337   3536   1065    -74    -39       C
ATOM   1365  OG1 THR A 518      -9.781 -28.710 -40.897  1.00 39.20           O
ANISOU 1365  OG1 THR A 518     4863   5975   4057   1119    -51    -27       O
ATOM   1366  CG2 THR A 518     -10.821 -26.887 -39.702  1.00 30.06           C
ANISOU 1366  CG2 THR A 518     3725   4738   2958    943    -31     53       C
ATOM   1367  N   GLY A 519     -10.946 -31.370 -40.335  1.00 25.35           N
ANISOU 1367  N   GLY A 519     3223   4061   2347   1244   -165   -223       N
ATOM   1368  CA  GLY A 519     -10.994 -32.634 -41.042  1.00 22.54           C
ANISOU 1368  CA  GLY A 519     2911   3675   1979   1321   -224   -303       C
ATOM   1369  C   GLY A 519     -12.116 -33.526 -40.552  1.00 23.45           C
ANISOU 1369  C   GLY A 519     3101   3663   2148   1304   -303   -384       C
ATOM   1370  O   GLY A 519     -12.790 -34.175 -41.343  1.00 24.04           O
ANISOU 1370  O   GLY A 519     3223   3686   2226   1345   -368   -452       O
ATOM   1371  N   ALA A 520     -12.314 -33.576 -39.239  1.00 19.29           N
ANISOU 1371  N   ALA A 520     2581   3083   1664   1242   -303   -375       N
ATOM   1372  CA  ALA A 520     -13.357 -34.433 -38.694  1.00 18.55           C
ANISOU 1372  CA  ALA A 520     2549   2870   1628   1219   -385   -447       C
ATOM   1373  C   ALA A 520     -14.726 -33.892 -39.068  1.00 18.72           C
ANISOU 1373  C   ALA A 520     2594   2840   1680   1203   -430   -481       C
ATOM   1374  O   ALA A 520     -15.666 -34.648 -39.280  1.00 21.14           O
ANISOU 1374  O   ALA A 520     2944   3056   2031   1203   -522   -549       O
ATOM   1375  CB  ALA A 520     -13.224 -34.564 -37.168  1.00 17.72           C
ANISOU 1375  CB  ALA A 520     2443   2730   1561   1159   -375   -427       C
ATOM   1376  N   PHE A 521     -14.840 -32.571 -39.143  1.00 19.58           N
ANISOU 1376  N   PHE A 521     2664   3001   1774   1179   -375   -423       N
ATOM   1377  CA  PHE A 521     -16.088 -31.976 -39.576  1.00 19.77           C
ANISOU 1377  CA  PHE A 521     2693   2972   1848   1154   -420   -435       C
ATOM   1378  C   PHE A 521     -16.316 -32.308 -41.050  1.00 22.85           C
ANISOU 1378  C   PHE A 521     3115   3372   2194   1232   -458   -493       C
ATOM   1379  O   PHE A 521     -17.424 -32.648 -41.451  1.00 21.72           O
ANISOU 1379  O   PHE A 521     3002   3144   2105   1227   -539   -548       O
ATOM   1380  CB  PHE A 521     -16.089 -30.467 -39.326  1.00 17.10           C
ANISOU 1380  CB  PHE A 521     2306   2682   1511   1101   -359   -347       C
ATOM   1381  CG  PHE A 521     -17.347 -29.775 -39.785  1.00 16.94           C
ANISOU 1381  CG  PHE A 521     2279   2599   1560   1084   -398   -359       C
ATOM   1382  CD1 PHE A 521     -18.596 -30.284 -39.449  1.00 18.89           C
ANISOU 1382  CD1 PHE A 521     2532   2714   1931   1056   -458   -419       C
ATOM   1383  CD2 PHE A 521     -17.281 -28.617 -40.535  1.00 20.74           C
ANISOU 1383  CD2 PHE A 521     2741   3143   1994   1084   -370   -309       C
ATOM   1384  CE1 PHE A 521     -19.754 -29.658 -39.872  1.00 21.97           C
ANISOU 1384  CE1 PHE A 521     2910   3043   2394   1036   -487   -433       C
ATOM   1385  CE2 PHE A 521     -18.449 -27.973 -40.958  1.00 21.71           C
ANISOU 1385  CE2 PHE A 521     2860   3203   2185   1071   -410   -324       C
ATOM   1386  CZ  PHE A 521     -19.681 -28.503 -40.627  1.00 18.36           C
ANISOU 1386  CZ  PHE A 521     2441   2651   1884   1050   -466   -390       C
ATOM   1387  N   ARG A 522     -15.254 -32.258 -41.851  1.00 21.80           N
ANISOU 1387  N   ARG A 522     2961   3335   1985   1296   -403   -468       N
ATOM   1388  CA  ARG A 522     -15.389 -32.601 -43.259  1.00 23.65           C
ANISOU 1388  CA  ARG A 522     3219   3582   2187   1366   -438   -508       C
ATOM   1389  C   ARG A 522     -15.854 -34.042 -43.380  1.00 22.84           C
ANISOU 1389  C   ARG A 522     3173   3385   2118   1381   -530   -588       C
ATOM   1390  O   ARG A 522     -16.681 -34.369 -44.218  1.00 22.37           O
ANISOU 1390  O   ARG A 522     3152   3275   2073   1407   -598   -642       O
ATOM   1391  CB  ARG A 522     -14.060 -32.434 -43.991  1.00 21.60           C
ANISOU 1391  CB  ARG A 522     2910   3443   1853   1425   -370   -457       C
ATOM   1392  CG  ARG A 522     -14.172 -32.629 -45.493  1.00 22.01           C
ANISOU 1392  CG  ARG A 522     2979   3524   1859   1506   -397   -492       C
ATOM   1393  CD  ARG A 522     -12.840 -32.372 -46.156  1.00 24.65           C
ANISOU 1393  CD  ARG A 522     3253   3991   2123   1563   -331   -435       C
ATOM   1394  NE  ARG A 522     -12.905 -32.584 -47.599  1.00 27.53           N
ANISOU 1394  NE  ARG A 522     3633   4391   2437   1651   -356   -468       N
ATOM   1395  CZ  ARG A 522     -11.876 -32.421 -48.420  1.00 28.97           C
ANISOU 1395  CZ  ARG A 522     3763   4692   2550   1716   -312   -429       C
ATOM   1396  NH1 ARG A 522     -10.699 -32.044 -47.940  1.00 32.15           N
ANISOU 1396  NH1 ARG A 522     4094   5189   2933   1695   -245   -354       N
ATOM   1397  NH2 ARG A 522     -12.030 -32.623 -49.728  1.00 30.22           N
ANISOU 1397  NH2 ARG A 522     3940   4879   2661   1802   -339   -465       N
ATOM   1398  N   CYS A 523     -15.303 -34.897 -42.524  1.00 21.28           N
ANISOU 1398  N   CYS A 523     2981   3166   1939   1363   -535   -592       N
ATOM   1399  CA  CYS A 523     -15.680 -36.303 -42.471  1.00 22.89           C
ANISOU 1399  CA  CYS A 523     3237   3277   2182   1370   -627   -660       C
ATOM   1400  C   CYS A 523     -17.177 -36.461 -42.224  1.00 25.72           C
ANISOU 1400  C   CYS A 523     3626   3520   2625   1318   -719   -706       C
ATOM   1401  O   CYS A 523     -17.839 -37.281 -42.853  1.00 24.51           O
ANISOU 1401  O   CYS A 523     3512   3298   2502   1337   -805   -761       O
ATOM   1402  CB  CYS A 523     -14.873 -37.019 -41.376  1.00 24.22           C
ANISOU 1402  CB  CYS A 523     3402   3438   2363   1347   -613   -648       C
ATOM   1403  SG  CYS A 523     -15.313 -38.753 -41.092  1.00 28.87           S
ANISOU 1403  SG  CYS A 523     4054   3905   3011   1344   -730   -721       S
ATOM   1404  N   LEU A 524     -17.712 -35.664 -41.304  1.00 20.16           N
ANISOU 1404  N   LEU A 524     2897   2794   1967   1253   -704   -681       N
ATOM   1405  CA  LEU A 524     -19.131 -35.725 -40.993  1.00 17.86           C
ANISOU 1405  CA  LEU A 524     2609   2392   1784   1196   -786   -711       C
ATOM   1406  C   LEU A 524     -19.953 -35.351 -42.220  1.00 24.29           C
ANISOU 1406  C   LEU A 524     3437   3195   2596   1225   -824   -741       C
ATOM   1407  O   LEU A 524     -20.943 -36.000 -42.551  1.00 21.15           O
ANISOU 1407  O   LEU A 524     3062   2706   2266   1213   -919   -791       O
ATOM   1408  CB  LEU A 524     -19.464 -34.756 -39.851  1.00 17.08           C
ANISOU 1408  CB  LEU A 524     2443   2273   1775   1110   -721   -638       C
ATOM   1409  CG  LEU A 524     -20.966 -34.545 -39.652  1.00 20.17           C
ANISOU 1409  CG  LEU A 524     2804   2552   2306   1045   -762   -645       C
ATOM   1410  CD1 LEU A 524     -21.657 -35.839 -39.219  1.00 21.10           C
ANISOU 1410  CD1 LEU A 524     2941   2558   2519   1011   -857   -687       C
ATOM   1411  CD2 LEU A 524     -21.225 -33.445 -38.642  1.00 19.99           C
ANISOU 1411  CD2 LEU A 524     2719   2516   2358    978   -675   -589       C
ATOM   1412  N   VAL A 525     -19.530 -34.278 -42.873  1.00 20.36           N
ANISOU 1412  N   VAL A 525     2922   2789   2025   1261   -751   -706       N
ATOM   1413  CA  VAL A 525     -20.232 -33.737 -44.024  1.00 19.44           C
ANISOU 1413  CA  VAL A 525     2816   2671   1901   1289   -776   -725       C
ATOM   1414  C   VAL A 525     -20.225 -34.740 -45.176  1.00 21.18           C
ANISOU 1414  C   VAL A 525     3083   2876   2089   1357   -834   -779       C
ATOM   1415  O   VAL A 525     -21.209 -34.870 -45.898  1.00 27.09           O
ANISOU 1415  O   VAL A 525     3854   3564   2875   1361   -905   -820       O
ATOM   1416  CB  VAL A 525     -19.584 -32.415 -44.475  1.00 22.26           C
ANISOU 1416  CB  VAL A 525     3138   3137   2184   1315   -679   -660       C
ATOM   1417  CG1 VAL A 525     -20.161 -31.949 -45.819  1.00 27.91           C
ANISOU 1417  CG1 VAL A 525     3872   3858   2874   1362   -706   -684       C
ATOM   1418  CG2 VAL A 525     -19.776 -31.346 -43.397  1.00 24.21           C
ANISOU 1418  CG2 VAL A 525     3324   3378   2497   1227   -628   -582       C
ATOM   1419  N   GLU A 526     -19.118 -35.463 -45.325  1.00 23.21           N
ANISOU 1419  N   GLU A 526     3347   3185   2285   1405   -803   -773       N
ATOM   1420  CA  GLU A 526     -18.918 -36.300 -46.511  1.00 27.74           C
ANISOU 1420  CA  GLU A 526     3957   3765   2818   1483   -842   -815       C
ATOM   1421  C   GLU A 526     -19.248 -37.780 -46.332  1.00 32.39           C
ANISOU 1421  C   GLU A 526     4590   4259   3459   1477   -937   -869       C
ATOM   1422  O   GLU A 526     -19.692 -38.426 -47.277  1.00 30.08           O
ANISOU 1422  O   GLU A 526     4335   3927   3166   1520  -1005   -917       O
ATOM   1423  CB  GLU A 526     -17.497 -36.118 -47.061  1.00 25.11           C
ANISOU 1423  CB  GLU A 526     3598   3557   2385   1558   -753   -779       C
ATOM   1424  CG  GLU A 526     -17.214 -34.683 -47.495  1.00 30.69           C
ANISOU 1424  CG  GLU A 526     4260   4360   3040   1573   -670   -722       C
ATOM   1425  CD  GLU A 526     -15.853 -34.481 -48.131  1.00 34.91           C
ANISOU 1425  CD  GLU A 526     4752   5026   3486   1648   -591   -677       C
ATOM   1426  OE1 GLU A 526     -15.020 -35.414 -48.102  1.00 37.73           O
ANISOU 1426  OE1 GLU A 526     5111   5404   3822   1685   -592   -689       O
ATOM   1427  OE2 GLU A 526     -15.615 -33.372 -48.659  1.00 33.57           O
ANISOU 1427  OE2 GLU A 526     4542   4941   3272   1668   -532   -628       O
ATOM   1428  N   LYS A 527     -19.045 -38.318 -45.130  1.00 30.20           N
ANISOU 1428  N   LYS A 527     4306   3941   3226   1424   -945   -861       N
ATOM   1429  CA  LYS A 527     -19.130 -39.770 -44.947  1.00 28.57           C
ANISOU 1429  CA  LYS A 527     4139   3654   3061   1426  -1030   -904       C
ATOM   1430  C   LYS A 527     -19.745 -40.268 -43.633  1.00 32.82           C
ANISOU 1430  C   LYS A 527     4674   4094   3704   1337  -1086   -902       C
ATOM   1431  O   LYS A 527     -20.411 -41.303 -43.615  1.00 30.85           O
ANISOU 1431  O   LYS A 527     4455   3746   3523   1318  -1184   -937       O
ATOM   1432  CB  LYS A 527     -17.737 -40.394 -45.080  1.00 31.97           C
ANISOU 1432  CB  LYS A 527     4577   4154   3415   1493   -985   -902       C
ATOM   1433  CG  LYS A 527     -17.044 -40.196 -46.421  1.00 37.09           C
ANISOU 1433  CG  LYS A 527     5226   4897   3970   1593   -943   -909       C
ATOM   1434  CD  LYS A 527     -15.733 -40.975 -46.427  1.00 39.75           C
ANISOU 1434  CD  LYS A 527     5563   5289   4253   1656   -915   -912       C
ATOM   1435  CE  LYS A 527     -14.964 -40.828 -47.729  1.00 45.64           C
ANISOU 1435  CE  LYS A 527     6297   6135   4907   1764   -875   -915       C
ATOM   1436  NZ  LYS A 527     -13.699 -41.633 -47.676  1.00 46.85           N
ANISOU 1436  NZ  LYS A 527     6443   6340   5016   1827   -856   -920       N
ATOM   1437  N   GLY A 528     -19.498 -39.560 -42.534  1.00 29.69           N
ANISOU 1437  N   GLY A 528     4238   3721   3320   1284  -1025   -857       N
ATOM   1438  CA  GLY A 528     -19.814 -40.091 -41.217  1.00 26.65           C
ANISOU 1438  CA  GLY A 528     3847   3255   3025   1210  -1068   -850       C
ATOM   1439  C   GLY A 528     -21.179 -39.734 -40.656  1.00 27.69           C
ANISOU 1439  C   GLY A 528     3950   3297   3275   1130  -1123   -849       C
ATOM   1440  O   GLY A 528     -21.968 -39.044 -41.303  1.00 29.49           O
ANISOU 1440  O   GLY A 528     4164   3521   3520   1129  -1133   -858       O
ATOM   1441  N   ASP A 529     -21.453 -40.218 -39.445  1.00 23.60           N
ANISOU 1441  N   ASP A 529     3417   2705   2847   1062  -1161   -837       N
ATOM   1442  CA  ASP A 529     -22.703 -39.925 -38.737  1.00 24.68           C
ANISOU 1442  CA  ASP A 529     3500   2751   3128    973  -1190   -812       C
ATOM   1443  C   ASP A 529     -22.496 -38.924 -37.603  1.00 18.40           C
ANISOU 1443  C   ASP A 529     2639   1977   2374    918  -1064   -741       C
ATOM   1444  O   ASP A 529     -23.398 -38.146 -37.281  1.00 22.03           O
ANISOU 1444  O   ASP A 529     3043   2398   2929    862  -1024   -713       O
ATOM   1445  CB  ASP A 529     -23.294 -41.196 -38.129  1.00 27.16           C
ANISOU 1445  CB  ASP A 529     3825   2948   3546    919  -1308   -825       C
ATOM   1446  CG  ASP A 529     -23.723 -42.204 -39.178  1.00 33.50           C
ANISOU 1446  CG  ASP A 529     4674   3704   4352    953  -1396   -860       C
ATOM   1447  OD1 ASP A 529     -23.461 -43.414 -38.983  1.00 36.60           O
ANISOU 1447  OD1 ASP A 529     5103   4048   4756    953  -1454   -865       O
ATOM   1448  OD2 ASP A 529     -24.325 -41.784 -40.187  1.00 31.57           O
ANISOU 1448  OD2 ASP A 529     4431   3468   4098    979  -1409   -882       O
ATOM   1449  N   VAL A 530     -21.328 -38.965 -36.980  1.00 21.83           N
ANISOU 1449  N   VAL A 530     3086   2467   2741    935  -1003   -721       N
ATOM   1450  CA  VAL A 530     -21.047 -38.070 -35.861  1.00 18.19           C
ANISOU 1450  CA  VAL A 530     2577   2020   2314    884   -882   -665       C
ATOM   1451  C   VAL A 530     -19.591 -37.624 -35.899  1.00 23.21           C
ANISOU 1451  C   VAL A 530     3225   2779   2813    941   -800   -644       C
ATOM   1452  O   VAL A 530     -18.706 -38.403 -36.247  1.00 22.35           O
ANISOU 1452  O   VAL A 530     3164   2718   2612    999   -840   -671       O
ATOM   1453  CB  VAL A 530     -21.366 -38.733 -34.502  1.00 17.90           C
ANISOU 1453  CB  VAL A 530     2534   1878   2390    796   -892   -651       C
ATOM   1454  CG1 VAL A 530     -20.532 -39.994 -34.297  1.00 20.53           C
ANISOU 1454  CG1 VAL A 530     2924   2201   2674    827   -964   -672       C
ATOM   1455  CG2 VAL A 530     -21.137 -37.757 -33.344  1.00 17.48           C
ANISOU 1455  CG2 VAL A 530     2428   1871   2343    685   -736   -580       C
ATOM   1456  N   ALA A 531     -19.347 -36.365 -35.555  1.00 19.74           N
ANISOU 1456  N   ALA A 531     2744   2397   2361    921   -686   -597       N
ATOM   1457  CA  ALA A 531     -17.980 -35.864 -35.485  1.00 17.55           C
ANISOU 1457  CA  ALA A 531     2466   2241   1962    954   -601   -558       C
ATOM   1458  C   ALA A 531     -17.694 -35.323 -34.092  1.00 14.92           C
ANISOU 1458  C   ALA A 531     2100   1906   1663    829   -488   -494       C
ATOM   1459  O   ALA A 531     -18.520 -34.623 -33.510  1.00 18.21           O
ANISOU 1459  O   ALA A 531     2477   2278   2163    732   -436   -464       O
ATOM   1460  CB  ALA A 531     -17.749 -34.780 -36.529  1.00 21.57           C
ANISOU 1460  CB  ALA A 531     2957   2851   2387   1012   -564   -536       C
ATOM   1461  N   PHE A 532     -16.511 -35.638 -33.581  1.00 14.90           N
ANISOU 1461  N   PHE A 532     2114   1957   1590    839   -453   -475       N
ATOM   1462  CA  PHE A 532     -16.120 -35.195 -32.252  1.00 16.22           C
ANISOU 1462  CA  PHE A 532     2258   2124   1780    729   -353   -417       C
ATOM   1463  C   PHE A 532     -15.110 -34.071 -32.393  1.00 17.58           C
ANISOU 1463  C   PHE A 532     2408   2415   1857    740   -263   -358       C
ATOM   1464  O   PHE A 532     -13.939 -34.302 -32.717  1.00 15.97           O
ANISOU 1464  O   PHE A 532     2216   2300   1550    812   -261   -352       O
ATOM   1465  CB  PHE A 532     -15.580 -36.384 -31.461  1.00 15.16           C
ANISOU 1465  CB  PHE A 532     2160   1948   1650    718   -387   -434       C
ATOM   1466  CG  PHE A 532     -16.609 -37.452 -31.253  1.00 16.41           C
ANISOU 1466  CG  PHE A 532     2339   1983   1912    688   -483   -477       C
ATOM   1467  CD1 PHE A 532     -17.648 -37.260 -30.355  1.00 17.03           C
ANISOU 1467  CD1 PHE A 532     2385   1983   2104    567   -450   -450       C
ATOM   1468  CD2 PHE A 532     -16.562 -38.632 -31.973  1.00 19.70           C
ANISOU 1468  CD2 PHE A 532     2806   2366   2312    784   -611   -543       C
ATOM   1469  CE1 PHE A 532     -18.625 -38.231 -30.170  1.00 17.12           C
ANISOU 1469  CE1 PHE A 532     2405   1886   2215    529   -541   -476       C
ATOM   1470  CE2 PHE A 532     -17.536 -39.605 -31.797  1.00 19.14           C
ANISOU 1470  CE2 PHE A 532     2755   2173   2345    748   -714   -574       C
ATOM   1471  CZ  PHE A 532     -18.568 -39.406 -30.895  1.00 16.12           C
ANISOU 1471  CZ  PHE A 532     2331   1715   2079    615   -677   -535       C
ATOM   1472  N   VAL A 533     -15.595 -32.849 -32.189  1.00 13.27           N
ANISOU 1472  N   VAL A 533     1825   1869   1347    672   -197   -314       N
ATOM   1473  CA  VAL A 533     -14.813 -31.638 -32.430  1.00 13.53           C
ANISOU 1473  CA  VAL A 533     1835   2003   1303    672   -128   -250       C
ATOM   1474  C   VAL A 533     -15.001 -30.656 -31.271  1.00 15.87           C
ANISOU 1474  C   VAL A 533     2108   2266   1656    555    -44   -196       C
ATOM   1475  O   VAL A 533     -15.333 -31.073 -30.165  1.00 17.64           O
ANISOU 1475  O   VAL A 533     2336   2417   1948    484    -25   -203       O
ATOM   1476  CB  VAL A 533     -15.163 -31.000 -33.806  1.00 13.63           C
ANISOU 1476  CB  VAL A 533     1836   2065   1276    743   -160   -255       C
ATOM   1477  CG1 VAL A 533     -14.720 -31.934 -34.943  1.00 16.84           C
ANISOU 1477  CG1 VAL A 533     2272   2529   1599    876   -237   -304       C
ATOM   1478  CG2 VAL A 533     -16.654 -30.709 -33.939  1.00 14.72           C
ANISOU 1478  CG2 VAL A 533     1964   2110   1520    707   -189   -286       C
ATOM   1479  N   LYS A 534     -14.757 -29.368 -31.503  1.00 15.51           N
ANISOU 1479  N   LYS A 534     2041   2275   1579    537      1   -141       N
ATOM   1480  CA  LYS A 534     -14.984 -28.390 -30.440  1.00 15.27           C
ANISOU 1480  CA  LYS A 534     1996   2207   1601    437     65    -98       C
ATOM   1481  C   LYS A 534     -16.039 -27.362 -30.817  1.00 12.14           C
ANISOU 1481  C   LYS A 534     1579   1777   1257    418     60    -99       C
ATOM   1482  O   LYS A 534     -16.529 -27.340 -31.946  1.00 15.55           O
ANISOU 1482  O   LYS A 534     2007   2220   1680    478      9   -126       O
ATOM   1483  CB  LYS A 534     -13.684 -27.712 -29.997  1.00 18.57           C
ANISOU 1483  CB  LYS A 534     2411   2695   1948    409    120    -23       C
ATOM   1484  CG  LYS A 534     -12.921 -26.982 -31.087  1.00 16.55           C
ANISOU 1484  CG  LYS A 534     2141   2548   1601    460    114     29       C
ATOM   1485  CD  LYS A 534     -11.593 -26.482 -30.507  1.00 19.57           C
ANISOU 1485  CD  LYS A 534     2516   2996   1923    422    164    109       C
ATOM   1486  CE  LYS A 534     -10.744 -25.753 -31.524  1.00 25.64           C
ANISOU 1486  CE  LYS A 534     3254   3861   2626    448    153    174       C
ATOM   1487  NZ  LYS A 534      -9.504 -25.263 -30.844  1.00 29.14           N
ANISOU 1487  NZ  LYS A 534     3677   4300   3096    371    175    233       N
ATOM   1488  N   HIS A 535     -16.396 -26.507 -29.867  1.00 14.02           N
ANISOU 1488  N   HIS A 535     1808   1974   1547    340    107    -75       N
ATOM   1489  CA  HIS A 535     -17.567 -25.651 -30.059  1.00 12.69           C
ANISOU 1489  CA  HIS A 535     1621   1759   1444    323     97    -91       C
ATOM   1490  C   HIS A 535     -17.419 -24.604 -31.159  1.00 14.98           C
ANISOU 1490  C   HIS A 535     1907   2098   1685    358     72    -58       C
ATOM   1491  O   HIS A 535     -18.421 -24.172 -31.733  1.00 16.77           O
ANISOU 1491  O   HIS A 535     2123   2292   1956    373     38    -87       O
ATOM   1492  CB  HIS A 535     -18.005 -25.004 -28.740  1.00 14.55           C
ANISOU 1492  CB  HIS A 535     1847   1941   1739    245    149    -80       C
ATOM   1493  CG  HIS A 535     -17.082 -23.934 -28.249  1.00 16.00           C
ANISOU 1493  CG  HIS A 535     2044   2157   1877    209    186    -14       C
ATOM   1494  ND1 HIS A 535     -15.944 -24.209 -27.526  1.00 15.42           N
ANISOU 1494  ND1 HIS A 535     1988   2112   1758    183    222     25       N
ATOM   1495  CD2 HIS A 535     -17.148 -22.584 -28.349  1.00 16.68           C
ANISOU 1495  CD2 HIS A 535     2132   2244   1962    192    183     20       C
ATOM   1496  CE1 HIS A 535     -15.338 -23.076 -27.212  1.00 22.02           C
ANISOU 1496  CE1 HIS A 535     2834   2966   2568    150    239     83       C
ATOM   1497  NE2 HIS A 535     -16.054 -22.076 -27.690  1.00 19.67           N
ANISOU 1497  NE2 HIS A 535     2528   2649   2297    153    213     82       N
ATOM   1498  N   GLN A 536     -16.187 -24.223 -31.486  1.00 13.00           N
ANISOU 1498  N   GLN A 536     1664   1932   1345    371     84      5       N
ATOM   1499  CA  GLN A 536     -15.991 -23.244 -32.553  1.00 15.45           C
ANISOU 1499  CA  GLN A 536     1969   2299   1604    398     58     49       C
ATOM   1500  C   GLN A 536     -15.996 -23.885 -33.938  1.00 14.40           C
ANISOU 1500  C   GLN A 536     1836   2221   1414    492      8     22       C
ATOM   1501  O   GLN A 536     -16.083 -23.195 -34.943  1.00 18.07           O
ANISOU 1501  O   GLN A 536     2297   2726   1843    523    -22     47       O
ATOM   1502  CB  GLN A 536     -14.665 -22.497 -32.389  1.00 20.22           C
ANISOU 1502  CB  GLN A 536     2571   2979   2132    368     87    144       C
ATOM   1503  CG  GLN A 536     -14.448 -21.861 -31.033  1.00 23.29           C
ANISOU 1503  CG  GLN A 536     2969   3318   2561    283    129    177       C
ATOM   1504  CD  GLN A 536     -13.625 -22.743 -30.113  1.00 30.21           C
ANISOU 1504  CD  GLN A 536     3853   4207   3420    266    170    179       C
ATOM   1505  OE1 GLN A 536     -13.779 -23.966 -30.109  1.00 20.66           O
ANISOU 1505  OE1 GLN A 536     2646   2988   2216    303    167    123       O
ATOM   1506  NE2 GLN A 536     -12.751 -22.126 -29.321  1.00 34.18           N
ANISOU 1506  NE2 GLN A 536     4361   4721   3903    210    200    245       N
ATOM   1507  N   THR A 537     -15.874 -25.201 -33.992  1.00 12.82           N
ANISOU 1507  N   THR A 537     1645   2023   1203    541     -7    -29       N
ATOM   1508  CA  THR A 537     -15.591 -25.859 -35.269  1.00 11.67           C
ANISOU 1508  CA  THR A 537     1507   1947    980    645    -57    -53       C
ATOM   1509  C   THR A 537     -16.656 -25.621 -36.348  1.00 14.37           C
ANISOU 1509  C   THR A 537     1851   2261   1349    692   -117    -93       C
ATOM   1510  O   THR A 537     -16.335 -25.233 -37.479  1.00 16.82           O
ANISOU 1510  O   THR A 537     2161   2652   1580    753   -141    -67       O
ATOM   1511  CB  THR A 537     -15.327 -27.368 -35.083  1.00 12.29           C
ANISOU 1511  CB  THR A 537     1604   2017   1049    694    -79   -110       C
ATOM   1512  OG1 THR A 537     -14.263 -27.552 -34.135  1.00 15.89           O
ANISOU 1512  OG1 THR A 537     2059   2505   1472    655    -26    -70       O
ATOM   1513  CG2 THR A 537     -14.933 -28.001 -36.427  1.00 16.90           C
ANISOU 1513  CG2 THR A 537     2201   2685   1537    819   -136   -138       C
ATOM   1514  N   VAL A 538     -17.921 -25.852 -36.022  1.00 15.61           N
ANISOU 1514  N   VAL A 538     2008   2310   1614    665   -142   -154       N
ATOM   1515  CA  VAL A 538     -18.952 -25.688 -37.038  1.00 13.81           C
ANISOU 1515  CA  VAL A 538     1781   2049   1417    712   -205   -197       C
ATOM   1516  C   VAL A 538     -19.117 -24.218 -37.455  1.00 18.20           C
ANISOU 1516  C   VAL A 538     2327   2625   1964    686   -198   -146       C
ATOM   1517  O   VAL A 538     -19.127 -23.905 -38.637  1.00 18.42           O
ANISOU 1517  O   VAL A 538     2362   2701   1936    746   -239   -139       O
ATOM   1518  CB  VAL A 538     -20.302 -26.339 -36.639  1.00 16.00           C
ANISOU 1518  CB  VAL A 538     2052   2209   1817    689   -241   -271       C
ATOM   1519  CG1 VAL A 538     -21.381 -26.013 -37.680  1.00 18.37           C
ANISOU 1519  CG1 VAL A 538     2352   2474   2156    732   -308   -310       C
ATOM   1520  CG2 VAL A 538     -20.132 -27.852 -36.520  1.00 21.65           C
ANISOU 1520  CG2 VAL A 538     2787   2904   2534    728   -278   -320       C
ATOM   1521  N   PRO A 539     -19.222 -23.308 -36.481  1.00 17.43           N
ANISOU 1521  N   PRO A 539     2216   2490   1915    599   -151   -110       N
ATOM   1522  CA  PRO A 539     -19.339 -21.895 -36.865  1.00 16.69           C
ANISOU 1522  CA  PRO A 539     2121   2408   1813    574   -159    -60       C
ATOM   1523  C   PRO A 539     -18.179 -21.400 -37.740  1.00 16.26           C
ANISOU 1523  C   PRO A 539     2071   2470   1638    605   -161     21       C
ATOM   1524  O   PRO A 539     -18.419 -20.642 -38.680  1.00 22.47           O
ANISOU 1524  O   PRO A 539     2861   3278   2399    626   -200     45       O
ATOM   1525  CB  PRO A 539     -19.376 -21.172 -35.511  1.00 21.75           C
ANISOU 1525  CB  PRO A 539     2755   2997   2512    484   -109    -35       C
ATOM   1526  CG  PRO A 539     -19.986 -22.177 -34.585  1.00 21.14           C
ANISOU 1526  CG  PRO A 539     2668   2852   2511    465    -88    -99       C
ATOM   1527  CD  PRO A 539     -19.433 -23.514 -35.037  1.00 18.92           C
ANISOU 1527  CD  PRO A 539     2397   2615   2179    524   -102   -122       C
ATOM   1528  N   GLN A 540     -16.952 -21.836 -37.458  1.00 19.59           N
ANISOU 1528  N   GLN A 540     2488   2971   1983    608   -121     66       N
ATOM   1529  CA  GLN A 540     -15.787 -21.386 -38.222  1.00 23.46           C
ANISOU 1529  CA  GLN A 540     2969   3589   2354    632   -115    155       C
ATOM   1530  C   GLN A 540     -15.627 -22.049 -39.585  1.00 22.96           C
ANISOU 1530  C   GLN A 540     2910   3613   2202    744   -154    133       C
ATOM   1531  O   GLN A 540     -14.775 -21.654 -40.381  1.00 24.74           O
ANISOU 1531  O   GLN A 540     3114   3918   2370    742   -133    191       O
ATOM   1532  CB  GLN A 540     -14.508 -21.560 -37.402  1.00 23.37           C
ANISOU 1532  CB  GLN A 540     2946   3639   2295    595    -58    216       C
ATOM   1533  CG  GLN A 540     -14.465 -20.630 -36.188  1.00 21.83           C
ANISOU 1533  CG  GLN A 540     2753   3378   2165    487    -26    260       C
ATOM   1534  CD  GLN A 540     -13.203 -20.784 -35.374  1.00 32.46           C
ANISOU 1534  CD  GLN A 540     4089   4778   3466    449     24    321       C
ATOM   1535  OE1 GLN A 540     -12.374 -21.653 -35.649  1.00 36.40           O
ANISOU 1535  OE1 GLN A 540     4571   5338   3921    489     41    312       O
ATOM   1536  NE2 GLN A 540     -13.048 -19.941 -34.356  1.00 31.08           N
ANISOU 1536  NE2 GLN A 540     3921   4551   3338    361     44    366       N
ATOM   1537  N   ASN A 541     -16.456 -23.046 -39.861  1.00 18.53           N
ANISOU 1537  N   ASN A 541     2366   2993   1683    806   -194     34       N
ATOM   1538  CA  ASN A 541     -16.337 -23.779 -41.116  1.00 20.85           C
ANISOU 1538  CA  ASN A 541     2669   3343   1909    909   -231     -6       C
ATOM   1539  C   ASN A 541     -17.637 -23.821 -41.895  1.00 24.03           C
ANISOU 1539  C   ASN A 541     3094   3677   2361    959   -307    -76       C
ATOM   1540  O   ASN A 541     -17.859 -24.718 -42.715  1.00 25.68           O
ANISOU 1540  O   ASN A 541     3323   3875   2558   1029   -338   -146       O
ATOM   1541  CB  ASN A 541     -15.787 -25.181 -40.869  1.00 19.85           C
ANISOU 1541  CB  ASN A 541     2550   3227   1764    958   -219    -61       C
ATOM   1542  CG  ASN A 541     -14.342 -25.156 -40.424  1.00 23.50           C
ANISOU 1542  CG  ASN A 541     2980   3765   2185    919   -143      6       C
ATOM   1543  OD1 ASN A 541     -13.441 -24.945 -41.238  1.00 23.77           O
ANISOU 1543  OD1 ASN A 541     2980   3877   2172    933   -111     47       O
ATOM   1544  ND2 ASN A 541     -14.109 -25.349 -39.122  1.00 20.68           N
ANISOU 1544  ND2 ASN A 541     2625   3382   1850    868   -117     18       N
ATOM   1545  N   THR A 542     -18.488 -22.832 -41.637  1.00 19.80           N
ANISOU 1545  N   THR A 542     2553   3067   1904    895   -318    -65       N
ATOM   1546  CA  THR A 542     -19.749 -22.690 -42.350  1.00 22.63           C
ANISOU 1546  CA  THR A 542     2925   3350   2325    926   -386   -125       C
ATOM   1547  C   THR A 542     -19.958 -21.234 -42.752  1.00 26.92           C
ANISOU 1547  C   THR A 542     3464   3899   2865    884   -395    -63       C
ATOM   1548  O   THR A 542     -19.236 -20.349 -42.302  1.00 25.74           O
ANISOU 1548  O   THR A 542     3302   3791   2686    818   -352     23       O
ATOM   1549  CB  THR A 542     -20.943 -23.161 -41.493  1.00 22.92           C
ANISOU 1549  CB  THR A 542     2956   3247   2505    882   -398   -205       C
ATOM   1550  OG1 THR A 542     -20.886 -22.534 -40.207  1.00 22.02           O
ANISOU 1550  OG1 THR A 542     2822   3093   2451    779   -336   -169       O
ATOM   1551  CG2 THR A 542     -20.905 -24.670 -41.308  1.00 23.92           C
ANISOU 1551  CG2 THR A 542     3094   3355   2641    930   -417   -270       C
ATOM   1552  N   GLY A 543     -20.938 -20.993 -43.616  1.00 33.68           N
ANISOU 1552  N   GLY A 543     4335   4710   3753    923   -460   -106       N
ATOM   1553  CA  GLY A 543     -21.292 -19.639 -43.997  1.00 35.19           C
ANISOU 1553  CA  GLY A 543     4528   4886   3955    884   -484    -58       C
ATOM   1554  C   GLY A 543     -20.179 -18.868 -44.685  1.00 37.01           C
ANISOU 1554  C   GLY A 543     4758   5235   4070    873   -463     50       C
ATOM   1555  O   GLY A 543     -20.176 -17.637 -44.683  1.00 39.00           O
ANISOU 1555  O   GLY A 543     5011   5483   4325    817   -477    118       O
ATOM   1556  N   GLY A 544     -19.229 -19.587 -45.271  1.00 28.92           N
ANISOU 1556  N   GLY A 544     3726   4297   2963    903   -417     62       N
ATOM   1557  CA  GLY A 544     -18.146 -18.960 -46.004  1.00 29.12           C
ANISOU 1557  CA  GLY A 544     3735   4422   2908    872   -376    156       C
ATOM   1558  C   GLY A 544     -16.927 -18.578 -45.186  1.00 28.71           C
ANISOU 1558  C   GLY A 544     3652   4425   2831    794   -312    244       C
ATOM   1559  O   GLY A 544     -15.935 -18.107 -45.746  1.00 34.41           O
ANISOU 1559  O   GLY A 544     4350   5225   3500    761   -280    320       O
ATOM   1560  N   LYS A 545     -16.982 -18.784 -43.871  1.00 24.64           N
ANISOU 1560  N   LYS A 545     3136   3868   2359    765   -296    234       N
ATOM   1561  CA  LYS A 545     -15.852 -18.438 -43.008  1.00 29.13           C
ANISOU 1561  CA  LYS A 545     3679   4475   2914    686   -238    312       C
ATOM   1562  C   LYS A 545     -14.600 -19.249 -43.353  1.00 32.97           C
ANISOU 1562  C   LYS A 545     4133   5051   3343    712   -178    321       C
ATOM   1563  O   LYS A 545     -13.476 -18.777 -43.186  1.00 37.85           O
ANISOU 1563  O   LYS A 545     4719   5719   3944    650   -137    396       O
ATOM   1564  CB  LYS A 545     -16.230 -18.587 -41.530  1.00 34.62           C
ANISOU 1564  CB  LYS A 545     4385   5107   3663    660   -233    292       C
ATOM   1565  CG  LYS A 545     -17.266 -17.555 -41.067  1.00 37.46           C
ANISOU 1565  CG  LYS A 545     4762   5362   4109    609   -276    287       C
ATOM   1566  CD  LYS A 545     -18.054 -18.060 -39.868  1.00 49.21           C
ANISOU 1566  CD  LYS A 545     6254   6730   5713    579   -252    197       C
ATOM   1567  CE  LYS A 545     -19.553 -17.784 -40.018  1.00 57.30           C
ANISOU 1567  CE  LYS A 545     7289   7643   6840    586   -302    117       C
ATOM   1568  NZ  LYS A 545     -20.404 -18.916 -39.515  1.00 49.66           N
ANISOU 1568  NZ  LYS A 545     6315   6602   5952    610   -293     11       N
ATOM   1569  N   ASN A 546     -14.802 -20.471 -43.839  1.00 30.36           N
ANISOU 1569  N   ASN A 546     3809   4733   2991    808   -182    237       N
ATOM   1570  CA  ASN A 546     -13.724 -21.258 -44.429  1.00 20.21           C
ANISOU 1570  CA  ASN A 546     2492   3536   1649    860   -140    234       C
ATOM   1571  C   ASN A 546     -13.938 -21.300 -45.935  1.00 26.55           C
ANISOU 1571  C   ASN A 546     3300   4382   2405    932   -164    215       C
ATOM   1572  O   ASN A 546     -14.950 -21.833 -46.404  1.00 26.28           O
ANISOU 1572  O   ASN A 546     3305   4296   2383   1001   -213    132       O
ATOM   1573  CB  ASN A 546     -13.729 -22.675 -43.848  1.00 17.32           C
ANISOU 1573  CB  ASN A 546     2139   3149   1294    923   -134    150       C
ATOM   1574  CG  ASN A 546     -12.662 -23.572 -44.456  1.00 24.70           C
ANISOU 1574  CG  ASN A 546     3041   4168   2175    996   -101    136       C
ATOM   1575  OD1 ASN A 546     -12.002 -23.212 -45.431  1.00 27.64           O
ANISOU 1575  OD1 ASN A 546     3379   4624   2499   1015    -82    180       O
ATOM   1576  ND2 ASN A 546     -12.493 -24.755 -43.878  1.00 24.92           N
ANISOU 1576  ND2 ASN A 546     3080   4176   2214   1042    -98     74       N
ATOM   1577  N   PRO A 547     -13.001 -20.718 -46.703  1.00 28.15           N
ANISOU 1577  N   PRO A 547     3462   4676   2557    916   -135    290       N
ATOM   1578  CA  PRO A 547     -13.173 -20.591 -48.157  1.00 25.79           C
ANISOU 1578  CA  PRO A 547     3166   4427   2207    977   -156    286       C
ATOM   1579  C   PRO A 547     -12.885 -21.867 -48.946  1.00 26.03           C
ANISOU 1579  C   PRO A 547     3190   4513   2186   1106   -145    211       C
ATOM   1580  O   PRO A 547     -13.120 -21.870 -50.153  1.00 32.16           O
ANISOU 1580  O   PRO A 547     3975   5326   2918   1171   -165    195       O
ATOM   1581  CB  PRO A 547     -12.137 -19.529 -48.532  1.00 30.81           C
ANISOU 1581  CB  PRO A 547     3753   5145   2808    906   -125    401       C
ATOM   1582  CG  PRO A 547     -11.049 -19.725 -47.529  1.00 36.09           C
ANISOU 1582  CG  PRO A 547     4378   5842   3492    861    -74    436       C
ATOM   1583  CD  PRO A 547     -11.759 -20.074 -46.239  1.00 31.73           C
ANISOU 1583  CD  PRO A 547     3866   5186   3006    833    -87    385       C
ATOM   1584  N   ASP A 548     -12.376 -22.913 -48.300  1.00 25.58           N
ANISOU 1584  N   ASP A 548     3122   4463   2135   1145   -119    167       N
ATOM   1585  CA  ASP A 548     -12.068 -24.157 -49.013  1.00 28.48           C
ANISOU 1585  CA  ASP A 548     3487   4876   2456   1276   -118     92       C
ATOM   1586  C   ASP A 548     -13.322 -24.725 -49.685  1.00 24.97           C
ANISOU 1586  C   ASP A 548     3110   4356   2019   1356   -182    -10       C
ATOM   1587  O   ASP A 548     -14.425 -24.619 -49.152  1.00 27.31           O
ANISOU 1587  O   ASP A 548     3455   4545   2377   1318   -228    -48       O
ATOM   1588  CB  ASP A 548     -11.464 -25.187 -48.061  1.00 33.34           C
ANISOU 1588  CB  ASP A 548     4092   5485   3092   1298    -96     55       C
ATOM   1589  CG  ASP A 548     -10.055 -24.818 -47.611  1.00 43.19           C
ANISOU 1589  CG  ASP A 548     5264   6820   4326   1244    -37    145       C
ATOM   1590  OD1 ASP A 548      -9.607 -23.685 -47.891  1.00 44.56           O
ANISOU 1590  OD1 ASP A 548     5399   7048   4484   1172    -15    239       O
ATOM   1591  OD2 ASP A 548      -9.399 -25.664 -46.972  1.00 41.94           O
ANISOU 1591  OD2 ASP A 548     5088   6670   4176   1271    -20    121       O
ATOM   1592  N   PRO A 549     -13.157 -25.335 -50.864  1.00 25.80           N
ANISOU 1592  N   PRO A 549     3219   4518   2066   1472   -191    -55       N
ATOM   1593  CA  PRO A 549     -14.321 -25.785 -51.634  1.00 25.81           C
ANISOU 1593  CA  PRO A 549     3289   4445   2074   1546   -258   -150       C
ATOM   1594  C   PRO A 549     -15.338 -26.608 -50.838  1.00 25.97           C
ANISOU 1594  C   PRO A 549     3372   4328   2167   1545   -314   -248       C
ATOM   1595  O   PRO A 549     -16.532 -26.372 -50.978  1.00 24.69           O
ANISOU 1595  O   PRO A 549     3257   4074   2051   1526   -374   -287       O
ATOM   1596  CB  PRO A 549     -13.690 -26.615 -52.757  1.00 27.26           C
ANISOU 1596  CB  PRO A 549     3462   4716   2180   1685   -249   -193       C
ATOM   1597  CG  PRO A 549     -12.381 -25.937 -52.989  1.00 28.89           C
ANISOU 1597  CG  PRO A 549     3581   5064   2330   1660   -180    -82       C
ATOM   1598  CD  PRO A 549     -11.899 -25.552 -51.596  1.00 30.82           C
ANISOU 1598  CD  PRO A 549     3792   5290   2626   1541   -143    -19       C
ATOM   1599  N   TRP A 550     -14.887 -27.547 -50.014  1.00 24.86           N
ANISOU 1599  N   TRP A 550     3232   4172   2043   1561   -302   -284       N
ATOM   1600  CA  TRP A 550     -15.823 -28.416 -49.310  1.00 23.14           C
ANISOU 1600  CA  TRP A 550     3076   3825   1891   1558   -364   -378       C
ATOM   1601  C   TRP A 550     -16.646 -27.678 -48.255  1.00 25.29           C
ANISOU 1601  C   TRP A 550     3353   4015   2243   1441   -381   -347       C
ATOM   1602  O   TRP A 550     -17.746 -28.105 -47.901  1.00 22.92           O
ANISOU 1602  O   TRP A 550     3098   3600   2009   1424   -448   -417       O
ATOM   1603  CB  TRP A 550     -15.081 -29.590 -48.660  1.00 26.23           C
ANISOU 1603  CB  TRP A 550     3469   4220   2279   1599   -351   -418       C
ATOM   1604  CG  TRP A 550     -14.177 -29.198 -47.526  1.00 23.42           C
ANISOU 1604  CG  TRP A 550     3055   3910   1935   1520   -286   -334       C
ATOM   1605  CD1 TRP A 550     -12.841 -28.936 -47.596  1.00 29.43           C
ANISOU 1605  CD1 TRP A 550     3745   4787   2648   1526   -218   -259       C
ATOM   1606  CD2 TRP A 550     -14.548 -29.030 -46.152  1.00 21.17           C
ANISOU 1606  CD2 TRP A 550     2776   3552   1716   1421   -289   -318       C
ATOM   1607  NE1 TRP A 550     -12.351 -28.615 -46.352  1.00 28.22           N
ANISOU 1607  NE1 TRP A 550     3561   4632   2531   1432   -180   -198       N
ATOM   1608  CE2 TRP A 550     -13.380 -28.663 -45.446  1.00 25.18           C
ANISOU 1608  CE2 TRP A 550     3224   4135   2211   1371   -219   -233       C
ATOM   1609  CE3 TRP A 550     -15.752 -29.152 -45.451  1.00 22.23           C
ANISOU 1609  CE3 TRP A 550     2957   3568   1923   1369   -348   -365       C
ATOM   1610  CZ2 TRP A 550     -13.381 -28.420 -44.072  1.00 25.64           C
ANISOU 1610  CZ2 TRP A 550     3275   4151   2318   1278   -202   -198       C
ATOM   1611  CZ3 TRP A 550     -15.752 -28.906 -44.077  1.00 25.44           C
ANISOU 1611  CZ3 TRP A 550     3348   3941   2379   1282   -330   -327       C
ATOM   1612  CH2 TRP A 550     -14.573 -28.542 -43.407  1.00 25.29           C
ANISOU 1612  CH2 TRP A 550     3277   3996   2335   1240   -255   -246       C
ATOM   1613  N   ALA A 551     -16.110 -26.573 -47.751  1.00 25.03           N
ANISOU 1613  N   ALA A 551     3268   4036   2207   1358   -326   -243       N
ATOM   1614  CA  ALA A 551     -16.736 -25.881 -46.621  1.00 17.83           C
ANISOU 1614  CA  ALA A 551     2354   3053   1366   1257   -336   -212       C
ATOM   1615  C   ALA A 551     -17.506 -24.633 -47.030  1.00 19.66           C
ANISOU 1615  C   ALA A 551     2587   3261   1621   1210   -362   -171       C
ATOM   1616  O   ALA A 551     -18.424 -24.212 -46.325  1.00 20.43           O
ANISOU 1616  O   ALA A 551     2694   3274   1796   1157   -398   -180       O
ATOM   1617  CB  ALA A 551     -15.675 -25.508 -45.591  1.00 20.05           C
ANISOU 1617  CB  ALA A 551     2590   3390   1639   1187   -267   -129       C
ATOM   1618  N   LYS A 552     -17.133 -24.039 -48.162  1.00 20.75           N
ANISOU 1618  N   LYS A 552     2712   3474   1699   1232   -347   -126       N
ATOM   1619  CA  LYS A 552     -17.552 -22.672 -48.452  1.00 24.02           C
ANISOU 1619  CA  LYS A 552     3118   3882   2125   1168   -363    -59       C
ATOM   1620  C   LYS A 552     -19.061 -22.463 -48.548  1.00 28.46           C
ANISOU 1620  C   LYS A 552     3720   4329   2764   1169   -441   -121       C
ATOM   1621  O   LYS A 552     -19.552 -21.373 -48.246  1.00 27.55           O
ANISOU 1621  O   LYS A 552     3599   4176   2692   1103   -461    -76       O
ATOM   1622  CB  LYS A 552     -16.846 -22.114 -49.692  1.00 27.50           C
ANISOU 1622  CB  LYS A 552     3536   4426   2486   1188   -338      4       C
ATOM   1623  CG  LYS A 552     -17.240 -22.768 -50.998  1.00 35.51           C
ANISOU 1623  CG  LYS A 552     4581   5448   3462   1296   -372    -69       C
ATOM   1624  CD  LYS A 552     -16.446 -22.171 -52.158  1.00 41.59           C
ANISOU 1624  CD  LYS A 552     5320   6335   4148   1314   -342      4       C
ATOM   1625  CE  LYS A 552     -16.590 -20.660 -52.203  1.00 45.85           C
ANISOU 1625  CE  LYS A 552     5848   6873   4700   1210   -352    103       C
ATOM   1626  NZ  LYS A 552     -15.848 -20.078 -53.358  1.00 51.83           N
ANISOU 1626  NZ  LYS A 552     6575   7740   5376   1220   -330    178       N
ATOM   1627  N   ASN A 553     -19.797 -23.495 -48.955  1.00 23.91           N
ANISOU 1627  N   ASN A 553     3181   3690   2213   1240   -491   -226       N
ATOM   1628  CA  ASN A 553     -21.246 -23.368 -49.099  1.00 20.51           C
ANISOU 1628  CA  ASN A 553     2780   3144   1868   1236   -569   -290       C
ATOM   1629  C   ASN A 553     -22.071 -24.105 -48.042  1.00 25.62           C
ANISOU 1629  C   ASN A 553     3433   3680   2619   1211   -607   -360       C
ATOM   1630  O   ASN A 553     -23.288 -24.238 -48.192  1.00 26.73           O
ANISOU 1630  O   ASN A 553     3591   3720   2844   1207   -672   -424       O
ATOM   1631  CB  ASN A 553     -21.692 -23.803 -50.504  1.00 27.08           C
ANISOU 1631  CB  ASN A 553     3651   3969   2667   1317   -614   -351       C
ATOM   1632  CG  ASN A 553     -21.016 -23.005 -51.603  1.00 37.33           C
ANISOU 1632  CG  ASN A 553     4936   5372   3874   1338   -583   -278       C
ATOM   1633  OD1 ASN A 553     -20.433 -23.570 -52.530  1.00 43.22           O
ANISOU 1633  OD1 ASN A 553     5691   6188   4541   1417   -566   -295       O
ATOM   1634  ND2 ASN A 553     -21.074 -21.687 -51.492  1.00 27.98           N
ANISOU 1634  ND2 ASN A 553     3730   4198   2702   1265   -578   -195       N
ATOM   1635  N   LEU A 554     -21.418 -24.575 -46.980  1.00 22.88           N
ANISOU 1635  N   LEU A 554     3068   3351   2273   1187   -566   -345       N
ATOM   1636  CA  LEU A 554     -22.123 -25.229 -45.875  1.00 20.32           C
ANISOU 1636  CA  LEU A 554     2739   2927   2055   1151   -595   -397       C
ATOM   1637  C   LEU A 554     -22.946 -24.238 -45.061  1.00 27.08           C
ANISOU 1637  C   LEU A 554     3561   3713   3016   1082   -602   -374       C
ATOM   1638  O   LEU A 554     -22.620 -23.055 -44.994  1.00 21.76           O
ANISOU 1638  O   LEU A 554     2869   3083   2316   1054   -576   -302       O
ATOM   1639  CB  LEU A 554     -21.141 -25.933 -44.942  1.00 19.41           C
ANISOU 1639  CB  LEU A 554     2613   2853   1909   1144   -547   -380       C
ATOM   1640  CG  LEU A 554     -20.308 -27.030 -45.611  1.00 19.66           C
ANISOU 1640  CG  LEU A 554     2676   2945   1849   1219   -539   -416       C
ATOM   1641  CD1 LEU A 554     -19.306 -27.623 -44.620  1.00 23.36           C
ANISOU 1641  CD1 LEU A 554     3130   3452   2292   1207   -490   -396       C
ATOM   1642  CD2 LEU A 554     -21.223 -28.107 -46.192  1.00 24.20           C
ANISOU 1642  CD2 LEU A 554     3299   3433   2464   1258   -623   -517       C
ATOM   1643  N   ASN A 555     -24.007 -24.736 -44.433  1.00 23.12           N
ANISOU 1643  N   ASN A 555     3047   3099   2637   1050   -637   -434       N
ATOM   1644  CA  ASN A 555     -24.861 -23.899 -43.592  1.00 25.26           C
ANISOU 1644  CA  ASN A 555     3279   3295   3024    989   -632   -429       C
ATOM   1645  C   ASN A 555     -24.856 -24.370 -42.146  1.00 19.81           C
ANISOU 1645  C   ASN A 555     2557   2559   2409    929   -584   -434       C
ATOM   1646  O   ASN A 555     -25.107 -25.538 -41.870  1.00 25.15           O
ANISOU 1646  O   ASN A 555     3237   3192   3128    934   -607   -481       O
ATOM   1647  CB  ASN A 555     -26.294 -23.893 -44.116  1.00 28.03           C
ANISOU 1647  CB  ASN A 555     3631   3552   3466    976   -693   -489       C
ATOM   1648  CG  ASN A 555     -26.377 -23.467 -45.565  1.00 46.21           C
ANISOU 1648  CG  ASN A 555     5972   5890   5698   1025   -735   -491       C
ATOM   1649  OD1 ASN A 555     -26.886 -24.201 -46.413  1.00 52.17           O
ANISOU 1649  OD1 ASN A 555     6756   6616   6449   1056   -788   -546       O
ATOM   1650  ND2 ASN A 555     -25.867 -22.275 -45.858  1.00 50.25           N
ANISOU 1650  ND2 ASN A 555     6482   6460   6150   1029   -715   -426       N
ATOM   1651  N   GLU A 556     -24.574 -23.451 -41.228  1.00 22.56           N
ANISOU 1651  N   GLU A 556     2884   2918   2772    846   -510   -380       N
ATOM   1652  CA  GLU A 556     -24.556 -23.753 -39.802  1.00 25.94           C
ANISOU 1652  CA  GLU A 556     3286   3309   3262    768   -447   -377       C
ATOM   1653  C   GLU A 556     -25.843 -24.444 -39.335  1.00 26.58           C
ANISOU 1653  C   GLU A 556     3339   3289   3472    744   -477   -443       C
ATOM   1654  O   GLU A 556     -25.809 -25.334 -38.489  1.00 21.69           O
ANISOU 1654  O   GLU A 556     2708   2644   2891    711   -456   -455       O
ATOM   1655  CB  GLU A 556     -24.308 -22.466 -39.003  1.00 32.65           C
ANISOU 1655  CB  GLU A 556     4121   4168   4117    692   -383   -319       C
ATOM   1656  CG  GLU A 556     -24.262 -22.649 -37.501  1.00 38.58           C
ANISOU 1656  CG  GLU A 556     4849   4887   4922    615   -314   -313       C
ATOM   1657  CD  GLU A 556     -23.619 -21.466 -36.780  1.00 42.41           C
ANISOU 1657  CD  GLU A 556     5336   5399   5380    556   -257   -248       C
ATOM   1658  OE1 GLU A 556     -23.166 -20.515 -37.451  1.00 43.88           O
ANISOU 1658  OE1 GLU A 556     5539   5627   5505    568   -274   -200       O
ATOM   1659  OE2 GLU A 556     -23.559 -21.492 -35.536  1.00 47.16           O
ANISOU 1659  OE2 GLU A 556     5923   5977   6018    497   -200   -242       O
ATOM   1660  N   LYS A 557     -26.977 -24.049 -39.905  1.00 24.85           N
ANISOU 1660  N   LYS A 557     3106   3016   3319    759   -532   -481       N
ATOM   1661  CA  LYS A 557     -28.260 -24.608 -39.493  1.00 22.53           C
ANISOU 1661  CA  LYS A 557     2773   2635   3153    731   -563   -534       C
ATOM   1662  C   LYS A 557     -28.463 -26.080 -39.863  1.00 24.06           C
ANISOU 1662  C   LYS A 557     2981   2796   3364    764   -630   -575       C
ATOM   1663  O   LYS A 557     -29.419 -26.704 -39.401  1.00 28.08           O
ANISOU 1663  O   LYS A 557     3455   3239   3976    722   -653   -603       O
ATOM   1664  CB  LYS A 557     -29.414 -23.769 -40.061  1.00 26.07           C
ANISOU 1664  CB  LYS A 557     3202   3039   3667    742   -609   -563       C
ATOM   1665  CG  LYS A 557     -29.578 -23.920 -41.570  1.00 26.80           C
ANISOU 1665  CG  LYS A 557     3338   3144   3700    793   -685   -578       C
ATOM   1666  CD  LYS A 557     -30.902 -23.320 -42.054  1.00 41.41           C
ANISOU 1666  CD  LYS A 557     5168   4943   5623    776   -729   -609       C
ATOM   1667  CE  LYS A 557     -31.020 -21.852 -41.694  1.00 51.21           C
ANISOU 1667  CE  LYS A 557     6390   6184   6881    759   -696   -588       C
ATOM   1668  NZ  LYS A 557     -32.291 -21.260 -42.215  1.00 63.24           N
ANISOU 1668  NZ  LYS A 557     7897   7663   8468    748   -744   -620       N
ATOM   1669  N   ASP A 558     -27.586 -26.639 -40.699  1.00 20.32           N
ANISOU 1669  N   ASP A 558     2562   2377   2783    822   -659   -571       N
ATOM   1670  CA  ASP A 558     -27.736 -28.035 -41.110  1.00 23.91           C
ANISOU 1670  CA  ASP A 558     3043   2803   3236    840   -727   -608       C
ATOM   1671  C   ASP A 558     -27.185 -29.035 -40.085  1.00 21.72           C
ANISOU 1671  C   ASP A 558     2763   2513   2975    819   -707   -605       C
ATOM   1672  O   ASP A 558     -27.275 -30.252 -40.291  1.00 20.98           O
ANISOU 1672  O   ASP A 558     2695   2389   2888    830   -772   -635       O
ATOM   1673  CB  ASP A 558     -27.082 -28.278 -42.477  1.00 22.85           C
ANISOU 1673  CB  ASP A 558     2972   2733   2976    918   -770   -619       C
ATOM   1674  CG  ASP A 558     -27.772 -27.516 -43.599  1.00 31.73           C
ANISOU 1674  CG  ASP A 558     4109   3855   4094    940   -809   -633       C
ATOM   1675  OD1 ASP A 558     -27.142 -27.300 -44.657  1.00 27.41           O
ANISOU 1675  OD1 ASP A 558     3605   3374   3435   1003   -818   -629       O
ATOM   1676  OD2 ASP A 558     -28.946 -27.128 -43.421  1.00 30.72           O
ANISOU 1676  OD2 ASP A 558     3943   3659   4069    894   -828   -648       O
ATOM   1677  N   TYR A 559     -26.630 -28.527 -38.984  1.00 19.27           N
ANISOU 1677  N   TYR A 559     2426   2223   2672    786   -621   -571       N
ATOM   1678  CA  TYR A 559     -25.981 -29.387 -37.987  1.00 18.00           C
ANISOU 1678  CA  TYR A 559     2270   2064   2507    745   -585   -555       C
ATOM   1679  C   TYR A 559     -26.573 -29.199 -36.607  1.00 16.75           C
ANISOU 1679  C   TYR A 559     2058   1864   2443    635   -517   -533       C
ATOM   1680  O   TYR A 559     -27.122 -28.141 -36.306  1.00 19.71           O
ANISOU 1680  O   TYR A 559     2396   2238   2856    594   -470   -517       O
ATOM   1681  CB  TYR A 559     -24.460 -29.134 -37.990  1.00 16.93           C
ANISOU 1681  CB  TYR A 559     2166   2028   2239    775   -526   -512       C
ATOM   1682  CG  TYR A 559     -23.990 -29.224 -39.413  1.00 19.18           C
ANISOU 1682  CG  TYR A 559     2493   2370   2425    890   -590   -532       C
ATOM   1683  CD1 TYR A 559     -23.859 -28.088 -40.195  1.00 21.78           C
ANISOU 1683  CD1 TYR A 559     2822   2757   2695    920   -575   -504       C
ATOM   1684  CD2 TYR A 559     -23.785 -30.462 -40.008  1.00 19.90           C
ANISOU 1684  CD2 TYR A 559     2628   2459   2473    930   -658   -569       C
ATOM   1685  CE1 TYR A 559     -23.495 -28.181 -41.535  1.00 21.47           C
ANISOU 1685  CE1 TYR A 559     2825   2781   2553    987   -615   -512       C
ATOM   1686  CE2 TYR A 559     -23.427 -30.566 -41.339  1.00 23.23           C
ANISOU 1686  CE2 TYR A 559     3095   2941   2790   1001   -698   -586       C
ATOM   1687  CZ  TYR A 559     -23.286 -29.422 -42.097  1.00 25.61           C
ANISOU 1687  CZ  TYR A 559     3394   3306   3032   1029   -670   -557       C
ATOM   1688  OH  TYR A 559     -22.934 -29.526 -43.427  1.00 25.65           O
ANISOU 1688  OH  TYR A 559     3442   3370   2932   1101   -698   -577       O
ATOM   1689  N   GLU A 560     -26.479 -30.240 -35.784  1.00 19.99           N
ANISOU 1689  N   GLU A 560     2466   2241   2889    593   -518   -532       N
ATOM   1690  CA  GLU A 560     -26.965 -30.174 -34.409  1.00 18.42           C
ANISOU 1690  CA  GLU A 560     2216   2015   2769    490   -449   -505       C
ATOM   1691  C   GLU A 560     -25.936 -30.813 -33.501  1.00 19.96           C
ANISOU 1691  C   GLU A 560     2435   2232   2918    457   -403   -476       C
ATOM   1692  O   GLU A 560     -25.021 -31.475 -33.975  1.00 18.17           O
ANISOU 1692  O   GLU A 560     2259   2028   2616    516   -442   -486       O
ATOM   1693  CB  GLU A 560     -28.317 -30.884 -34.278  1.00 19.17           C
ANISOU 1693  CB  GLU A 560     2266   2028   2989    451   -512   -529       C
ATOM   1694  CG  GLU A 560     -29.480 -30.098 -34.899  1.00 26.97           C
ANISOU 1694  CG  GLU A 560     3214   2994   4041    464   -540   -553       C
ATOM   1695  CD  GLU A 560     -30.839 -30.753 -34.682  1.00 34.91           C
ANISOU 1695  CD  GLU A 560     4160   3927   5178    416   -596   -566       C
ATOM   1696  OE1 GLU A 560     -30.912 -31.999 -34.652  1.00 34.88           O
ANISOU 1696  OE1 GLU A 560     4170   3874   5211    405   -669   -572       O
ATOM   1697  OE2 GLU A 560     -31.842 -30.015 -34.551  1.00 39.78           O
ANISOU 1697  OE2 GLU A 560     4716   4537   5862    389   -575   -569       O
ATOM   1698  N   LEU A 561     -26.086 -30.599 -32.198  1.00 17.37           N
ANISOU 1698  N   LEU A 561     2071   1900   2630    370   -322   -442       N
ATOM   1699  CA  LEU A 561     -25.216 -31.210 -31.201  1.00 15.28           C
ANISOU 1699  CA  LEU A 561     1826   1647   2333    327   -278   -413       C
ATOM   1700  C   LEU A 561     -25.969 -32.302 -30.443  1.00 17.67           C
ANISOU 1700  C   LEU A 561     2100   1884   2730    260   -308   -412       C
ATOM   1701  O   LEU A 561     -27.178 -32.187 -30.231  1.00 19.50           O
ANISOU 1701  O   LEU A 561     2274   2082   3054    216   -314   -413       O
ATOM   1702  CB  LEU A 561     -24.747 -30.141 -30.210  1.00 16.62           C
ANISOU 1702  CB  LEU A 561     1981   1863   2470    277   -164   -370       C
ATOM   1703  CG  LEU A 561     -24.041 -28.916 -30.809  1.00 17.26           C
ANISOU 1703  CG  LEU A 561     2083   2006   2468    323   -133   -354       C
ATOM   1704  CD1 LEU A 561     -23.638 -27.944 -29.711  1.00 19.47           C
ANISOU 1704  CD1 LEU A 561     2354   2316   2730    266    -36   -312       C
ATOM   1705  CD2 LEU A 561     -22.827 -29.333 -31.625  1.00 17.10           C
ANISOU 1705  CD2 LEU A 561     2116   2035   2347    395   -167   -353       C
ATOM   1706  N   LEU A 562     -25.258 -33.351 -30.038  1.00 15.16           N
ANISOU 1706  N   LEU A 562     1821   1552   2389    250   -332   -405       N
ATOM   1707  CA  LEU A 562     -25.817 -34.387 -29.168  1.00 13.98           C
ANISOU 1707  CA  LEU A 562     1648   1344   2320    171   -357   -388       C
ATOM   1708  C   LEU A 562     -25.569 -34.039 -27.710  1.00 17.71           C
ANISOU 1708  C   LEU A 562     2095   1845   2789     85   -244   -339       C
ATOM   1709  O   LEU A 562     -24.423 -33.886 -27.291  1.00 19.70           O
ANISOU 1709  O   LEU A 562     2388   2137   2962     93   -191   -322       O
ATOM   1710  CB  LEU A 562     -25.186 -35.751 -29.465  1.00 17.01           C
ANISOU 1710  CB  LEU A 562     2094   1686   2682    206   -457   -409       C
ATOM   1711  CG  LEU A 562     -25.298 -36.204 -30.914  1.00 19.72           C
ANISOU 1711  CG  LEU A 562     2477   2003   3014    307   -580   -465       C
ATOM   1712  CD1 LEU A 562     -24.632 -37.571 -31.101  1.00 19.88           C
ANISOU 1712  CD1 LEU A 562     2565   1981   3007    349   -684   -491       C
ATOM   1713  CD2 LEU A 562     -26.756 -36.249 -31.341  1.00 21.68           C
ANISOU 1713  CD2 LEU A 562     2676   2190   3372    285   -645   -479       C
ATOM   1714  N   CYS A 563     -26.645 -33.905 -26.944  1.00 17.88           N
ANISOU 1714  N   CYS A 563     2048   1852   2894      9   -207   -314       N
ATOM   1715  CA  CYS A 563     -26.545 -33.618 -25.518  1.00 21.54           C
ANISOU 1715  CA  CYS A 563     2484   2345   3355    -69   -102   -269       C
ATOM   1716  C   CYS A 563     -26.408 -34.921 -24.735  1.00 18.10           C
ANISOU 1716  C   CYS A 563     2060   1869   2949   -136   -134   -238       C
ATOM   1717  O   CYS A 563     -26.901 -35.971 -25.161  1.00 22.47           O
ANISOU 1717  O   CYS A 563     2614   2362   3563   -145   -238   -246       O
ATOM   1718  CB  CYS A 563     -27.774 -32.828 -25.061  1.00 22.72           C
ANISOU 1718  CB  CYS A 563     2549   2514   3571   -110    -44   -257       C
ATOM   1719  SG  CYS A 563     -28.226 -31.472 -26.207  1.00 26.56           S
ANISOU 1719  SG  CYS A 563     3021   3023   4049    -30    -49   -301       S
ATOM   1720  N   LEU A 564     -25.726 -34.868 -23.602  1.00 21.22           N
ANISOU 1720  N   LEU A 564     2470   2291   3301   -182    -54   -203       N
ATOM   1721  CA  LEU A 564     -25.488 -36.073 -22.815  1.00 24.72           C
ANISOU 1721  CA  LEU A 564     2932   2696   3763   -247    -83   -171       C
ATOM   1722  C   LEU A 564     -26.791 -36.729 -22.353  1.00 23.22           C
ANISOU 1722  C   LEU A 564     2671   2472   3680   -332   -113   -135       C
ATOM   1723  O   LEU A 564     -26.828 -37.936 -22.100  1.00 27.58           O
ANISOU 1723  O   LEU A 564     3238   2969   4270   -381   -188   -111       O
ATOM   1724  CB  LEU A 564     -24.587 -35.765 -21.615  1.00 24.04           C
ANISOU 1724  CB  LEU A 564     2871   2649   3612   -283     17   -137       C
ATOM   1725  CG  LEU A 564     -23.122 -35.493 -21.969  1.00 18.95           C
ANISOU 1725  CG  LEU A 564     2303   2031   2868   -214     26   -159       C
ATOM   1726  CD1 LEU A 564     -22.318 -34.986 -20.760  1.00 23.75           C
ANISOU 1726  CD1 LEU A 564     2929   2678   3418   -251    129   -124       C
ATOM   1727  CD2 LEU A 564     -22.500 -36.745 -22.588  1.00 21.56           C
ANISOU 1727  CD2 LEU A 564     2694   2314   3185   -176    -86   -183       C
ATOM   1728  N   ASP A 565     -27.854 -35.937 -22.251  1.00 24.73           N
ANISOU 1728  N   ASP A 565     2782   2698   3918   -349    -61   -127       N
ATOM   1729  CA  ASP A 565     -29.140 -36.466 -21.794  1.00 29.40           C
ANISOU 1729  CA  ASP A 565     3287   3275   4609   -432    -79    -84       C
ATOM   1730  C   ASP A 565     -29.956 -37.109 -22.919  1.00 35.60           C
ANISOU 1730  C   ASP A 565     4055   3995   5478   -416   -211   -106       C
ATOM   1731  O   ASP A 565     -31.094 -37.537 -22.705  1.00 33.18           O
ANISOU 1731  O   ASP A 565     3669   3673   5264   -483   -242    -68       O
ATOM   1732  CB  ASP A 565     -29.964 -35.381 -21.091  1.00 29.99           C
ANISOU 1732  CB  ASP A 565     3274   3425   4697   -456     37    -65       C
ATOM   1733  CG  ASP A 565     -30.412 -34.277 -22.032  1.00 35.15           C
ANISOU 1733  CG  ASP A 565     3905   4098   5352   -377     41   -118       C
ATOM   1734  OD1 ASP A 565     -30.224 -34.411 -23.261  1.00 33.68           O
ANISOU 1734  OD1 ASP A 565     3763   3868   5167   -313    -48   -163       O
ATOM   1735  OD2 ASP A 565     -30.967 -33.272 -21.536  1.00 40.96           O
ANISOU 1735  OD2 ASP A 565     4582   4894   6086   -376    130   -117       O
ATOM   1736  N   GLY A 566     -29.382 -37.173 -24.116  1.00 30.67           N
ANISOU 1736  N   GLY A 566     3501   3335   4818   -324   -292   -165       N
ATOM   1737  CA  GLY A 566     -30.049 -37.825 -25.234  1.00 30.05           C
ANISOU 1737  CA  GLY A 566     3423   3187   4809   -295   -431   -194       C
ATOM   1738  C   GLY A 566     -30.868 -36.921 -26.144  1.00 28.36           C
ANISOU 1738  C   GLY A 566     3164   2989   4624   -241   -434   -232       C
ATOM   1739  O   GLY A 566     -31.473 -37.397 -27.110  1.00 28.75           O
ANISOU 1739  O   GLY A 566     3213   2978   4733   -212   -552   -259       O
ATOM   1740  N   THR A 567     -30.887 -35.625 -25.844  1.00 25.14           N
ANISOU 1740  N   THR A 567     2722   2653   4175   -223   -315   -237       N
ATOM   1741  CA  THR A 567     -31.564 -34.645 -26.684  1.00 27.71           C
ANISOU 1741  CA  THR A 567     3014   2996   4519   -166   -315   -276       C
ATOM   1742  C   THR A 567     -30.577 -34.008 -27.666  1.00 24.14           C
ANISOU 1742  C   THR A 567     2644   2559   3971    -61   -323   -327       C
ATOM   1743  O   THR A 567     -29.390 -34.359 -27.679  1.00 20.38           O
ANISOU 1743  O   THR A 567     2243   2085   3417    -33   -327   -331       O
ATOM   1744  CB  THR A 567     -32.249 -33.553 -25.836  1.00 31.52           C
ANISOU 1744  CB  THR A 567     3411   3548   5015   -200   -194   -255       C
ATOM   1745  OG1 THR A 567     -31.263 -32.826 -25.093  1.00 30.77           O
ANISOU 1745  OG1 THR A 567     3356   3509   4827   -191    -87   -247       O
ATOM   1746  CG2 THR A 567     -33.233 -34.188 -24.859  1.00 36.84           C
ANISOU 1746  CG2 THR A 567     3993   4228   5776   -302   -178   -196       C
ATOM   1747  N   ARG A 568     -31.076 -33.095 -28.493  1.00 21.21           N
ANISOU 1747  N   ARG A 568     2254   2199   3606     -5   -329   -363       N
ATOM   1748  CA  ARG A 568     -30.256 -32.407 -29.486  1.00 21.43           C
ANISOU 1748  CA  ARG A 568     2349   2249   3546     89   -339   -402       C
ATOM   1749  C   ARG A 568     -30.516 -30.908 -29.491  1.00 23.68           C
ANISOU 1749  C   ARG A 568     2603   2583   3810    110   -262   -409       C
ATOM   1750  O   ARG A 568     -31.615 -30.458 -29.162  1.00 26.23           O
ANISOU 1750  O   ARG A 568     2851   2910   4205     79   -237   -407       O
ATOM   1751  CB  ARG A 568     -30.523 -32.982 -30.877  1.00 23.57           C
ANISOU 1751  CB  ARG A 568     2653   2466   3837    158   -471   -447       C
ATOM   1752  CG  ARG A 568     -30.018 -34.403 -31.049  1.00 28.16           C
ANISOU 1752  CG  ARG A 568     3290   2996   4415    165   -566   -452       C
ATOM   1753  CD  ARG A 568     -30.805 -35.122 -32.128  1.00 38.82           C
ANISOU 1753  CD  ARG A 568     4646   4272   5832    205   -710   -490       C
ATOM   1754  NE  ARG A 568     -30.691 -34.472 -33.430  1.00 36.41           N
ANISOU 1754  NE  ARG A 568     4377   3981   5475    308   -748   -539       N
ATOM   1755  CZ  ARG A 568     -30.389 -35.114 -34.554  1.00 40.77           C
ANISOU 1755  CZ  ARG A 568     4997   4499   5995    398   -865   -585       C
ATOM   1756  NH1 ARG A 568     -30.170 -36.422 -34.532  1.00 38.59           N
ANISOU 1756  NH1 ARG A 568     4763   4164   5736    399   -962   -593       N
ATOM   1757  NH2 ARG A 568     -30.307 -34.455 -35.703  1.00 39.68           N
ANISOU 1757  NH2 ARG A 568     4888   4385   5803    490   -890   -624       N
ATOM   1758  N   LYS A 569     -29.500 -30.133 -29.857  1.00 18.21           N
ANISOU 1758  N   LYS A 569     1968   1931   3021    164   -229   -416       N
ATOM   1759  CA  LYS A 569     -29.630 -28.677 -29.919  1.00 19.60           C
ANISOU 1759  CA  LYS A 569     2129   2144   3172    186   -173   -421       C
ATOM   1760  C   LYS A 569     -28.861 -28.105 -31.114  1.00 19.86           C
ANISOU 1760  C   LYS A 569     2225   2198   3124    266   -209   -438       C
ATOM   1761  O   LYS A 569     -27.960 -28.755 -31.647  1.00 20.11           O
ANISOU 1761  O   LYS A 569     2312   2235   3093    304   -248   -439       O
ATOM   1762  CB  LYS A 569     -29.113 -28.040 -28.628  1.00 18.60           C
ANISOU 1762  CB  LYS A 569     1997   2061   3007    140    -64   -386       C
ATOM   1763  CG  LYS A 569     -29.964 -28.302 -27.394  1.00 26.28           C
ANISOU 1763  CG  LYS A 569     2899   3036   4050     67    -10   -366       C
ATOM   1764  CD  LYS A 569     -29.627 -27.298 -26.299  1.00 44.66           C
ANISOU 1764  CD  LYS A 569     5223   5410   6334     47     92   -346       C
ATOM   1765  CE  LYS A 569     -30.458 -27.515 -25.038  1.00 56.63           C
ANISOU 1765  CE  LYS A 569     6665   6945   7905    -17    154   -325       C
ATOM   1766  NZ  LYS A 569     -29.929 -28.633 -24.201  1.00 57.43           N
ANISOU 1766  NZ  LYS A 569     6780   7043   7998    -78    175   -285       N
ATOM   1767  N   PRO A 570     -29.194 -26.871 -31.524  1.00 19.31           N
ANISOU 1767  N   PRO A 570     2145   2143   3048    294   -198   -449       N
ATOM   1768  CA  PRO A 570     -28.417 -26.205 -32.575  1.00 20.73           C
ANISOU 1768  CA  PRO A 570     2381   2353   3143    360   -224   -450       C
ATOM   1769  C   PRO A 570     -26.968 -26.025 -32.125  1.00 18.44           C
ANISOU 1769  C   PRO A 570     2137   2115   2754    352   -166   -406       C
ATOM   1770  O   PRO A 570     -26.703 -25.984 -30.917  1.00 18.60           O
ANISOU 1770  O   PRO A 570     2146   2145   2778    296    -96   -380       O
ATOM   1771  CB  PRO A 570     -29.095 -24.836 -32.700  1.00 22.53           C
ANISOU 1771  CB  PRO A 570     2583   2583   3395    367   -211   -459       C
ATOM   1772  CG  PRO A 570     -30.490 -25.059 -32.204  1.00 26.81           C
ANISOU 1772  CG  PRO A 570     3051   3087   4047    333   -213   -485       C
ATOM   1773  CD  PRO A 570     -30.364 -26.079 -31.109  1.00 18.86           C
ANISOU 1773  CD  PRO A 570     2023   2079   3064    271   -171   -462       C
ATOM   1774  N   VAL A 571     -26.044 -25.910 -33.075  1.00 15.21           N
ANISOU 1774  N   VAL A 571     1777   1744   2257    410   -196   -396       N
ATOM   1775  CA  VAL A 571     -24.624 -25.847 -32.713  1.00 14.31           C
ANISOU 1775  CA  VAL A 571     1700   1686   2049    404   -147   -351       C
ATOM   1776  C   VAL A 571     -24.270 -24.580 -31.937  1.00 17.66           C
ANISOU 1776  C   VAL A 571     2122   2134   2454    360    -77   -309       C
ATOM   1777  O   VAL A 571     -23.268 -24.555 -31.210  1.00 18.44           O
ANISOU 1777  O   VAL A 571     2241   2265   2502    331    -26   -269       O
ATOM   1778  CB  VAL A 571     -23.683 -26.023 -33.941  1.00 22.38           C
ANISOU 1778  CB  VAL A 571     2767   2765   2974    481   -192   -343       C
ATOM   1779  CG1 VAL A 571     -24.082 -27.254 -34.745  1.00 20.15           C
ANISOU 1779  CG1 VAL A 571     2496   2451   2709    539   -276   -394       C
ATOM   1780  CG2 VAL A 571     -23.706 -24.802 -34.808  1.00 23.72           C
ANISOU 1780  CG2 VAL A 571     2943   2964   3107    512   -207   -326       C
ATOM   1781  N   GLU A 572     -25.089 -23.539 -32.068  1.00 17.62           N
ANISOU 1781  N   GLU A 572     2096   2108   2489    359    -84   -321       N
ATOM   1782  CA  GLU A 572     -24.867 -22.313 -31.293  1.00 18.18           C
ANISOU 1782  CA  GLU A 572     2170   2189   2550    322    -34   -290       C
ATOM   1783  C   GLU A 572     -25.118 -22.534 -29.803  1.00 19.27           C
ANISOU 1783  C   GLU A 572     2282   2308   2731    265     32   -291       C
ATOM   1784  O   GLU A 572     -24.648 -21.758 -28.957  1.00 21.00           O
ANISOU 1784  O   GLU A 572     2515   2537   2926    235     78   -262       O
ATOM   1785  CB  GLU A 572     -25.773 -21.177 -31.780  1.00 25.47           C
ANISOU 1785  CB  GLU A 572     3079   3087   3512    342    -69   -311       C
ATOM   1786  CG  GLU A 572     -25.468 -20.685 -33.188  1.00 36.54           C
ANISOU 1786  CG  GLU A 572     4511   4510   4861    393   -131   -298       C
ATOM   1787  CD  GLU A 572     -26.264 -21.418 -34.268  1.00 46.40           C
ANISOU 1787  CD  GLU A 572     5747   5738   6144    443   -197   -347       C
ATOM   1788  OE1 GLU A 572     -26.789 -22.526 -34.001  1.00 31.17           O
ANISOU 1788  OE1 GLU A 572     3793   3782   4270    438   -201   -382       O
ATOM   1789  OE2 GLU A 572     -26.364 -20.875 -35.391  1.00 48.96           O
ANISOU 1789  OE2 GLU A 572     6090   6070   6444    487   -253   -348       O
ATOM   1790  N   GLU A 573     -25.878 -23.580 -29.489  1.00 14.84           N
ANISOU 1790  N   GLU A 573     1684   1719   2234    249     31   -321       N
ATOM   1791  CA  GLU A 573     -26.322 -23.818 -28.119  1.00 14.18           C
ANISOU 1791  CA  GLU A 573     1566   1625   2197    194     92   -321       C
ATOM   1792  C   GLU A 573     -25.492 -24.882 -27.396  1.00 16.12           C
ANISOU 1792  C   GLU A 573     1831   1880   2414    157    125   -294       C
ATOM   1793  O   GLU A 573     -26.018 -25.711 -26.661  1.00 19.25           O
ANISOU 1793  O   GLU A 573     2194   2259   2860    117    144   -299       O
ATOM   1794  CB  GLU A 573     -27.812 -24.172 -28.104  1.00 18.03           C
ANISOU 1794  CB  GLU A 573     1987   2083   2782    187     73   -360       C
ATOM   1795  CG  GLU A 573     -28.687 -23.023 -28.603  1.00 17.59           C
ANISOU 1795  CG  GLU A 573     1908   2018   2759    222     48   -390       C
ATOM   1796  CD  GLU A 573     -30.178 -23.325 -28.569  1.00 28.87           C
ANISOU 1796  CD  GLU A 573     3260   3424   4285    216     31   -426       C
ATOM   1797  OE1 GLU A 573     -30.626 -24.058 -27.660  1.00 29.97           O
ANISOU 1797  OE1 GLU A 573     3352   3568   4469    169     70   -418       O
ATOM   1798  OE2 GLU A 573     -30.904 -22.815 -29.451  1.00 29.24           O
ANISOU 1798  OE2 GLU A 573     3291   3452   4365    257    -23   -459       O
ATOM   1799  N   TYR A 574     -24.182 -24.830 -27.577  1.00 15.16           N
ANISOU 1799  N   TYR A 574     1761   1788   2210    169    130   -262       N
ATOM   1800  CA  TYR A 574     -23.292 -25.795 -26.945  1.00 14.84           C
ANISOU 1800  CA  TYR A 574     1745   1758   2136    142    155   -239       C
ATOM   1801  C   TYR A 574     -23.199 -25.660 -25.425  1.00 16.42           C
ANISOU 1801  C   TYR A 574     1938   1955   2345     81    230   -217       C
ATOM   1802  O   TYR A 574     -22.767 -26.588 -24.735  1.00 13.93           O
ANISOU 1802  O   TYR A 574     1634   1637   2024     48    250   -204       O
ATOM   1803  CB  TYR A 574     -21.896 -25.647 -27.536  1.00 16.09           C
ANISOU 1803  CB  TYR A 574     1953   1961   2200    175    145   -207       C
ATOM   1804  CG  TYR A 574     -21.235 -24.325 -27.218  1.00 14.62           C
ANISOU 1804  CG  TYR A 574     1786   1803   1967    163    181   -166       C
ATOM   1805  CD1 TYR A 574     -20.447 -24.181 -26.075  1.00 14.64           C
ANISOU 1805  CD1 TYR A 574     1808   1814   1941    119    237   -131       C
ATOM   1806  CD2 TYR A 574     -21.392 -23.224 -28.050  1.00 15.73           C
ANISOU 1806  CD2 TYR A 574     1929   1955   2094    193    151   -160       C
ATOM   1807  CE1 TYR A 574     -19.829 -22.984 -25.777  1.00 15.08           C
ANISOU 1807  CE1 TYR A 574     1885   1885   1958    105    256    -91       C
ATOM   1808  CE2 TYR A 574     -20.791 -22.013 -27.746  1.00 16.82           C
ANISOU 1808  CE2 TYR A 574     2088   2108   2195    176    169   -117       C
ATOM   1809  CZ  TYR A 574     -20.004 -21.906 -26.612  1.00 14.49           C
ANISOU 1809  CZ  TYR A 574     1813   1818   1874    132    219    -82       C
ATOM   1810  OH  TYR A 574     -19.399 -20.708 -26.320  1.00 17.63           O
ANISOU 1810  OH  TYR A 574     2237   2223   2240    114    223    -37       O
ATOM   1811  N   ALA A 575     -23.584 -24.503 -24.894  1.00 15.50           N
ANISOU 1811  N   ALA A 575     1809   1841   2239     72    266   -216       N
ATOM   1812  CA  ALA A 575     -23.418 -24.246 -23.458  1.00 14.17           C
ANISOU 1812  CA  ALA A 575     1642   1677   2065     27    336   -198       C
ATOM   1813  C   ALA A 575     -23.920 -25.376 -22.572  1.00 19.92           C
ANISOU 1813  C   ALA A 575     2338   2395   2837    -19    366   -199       C
ATOM   1814  O   ALA A 575     -23.204 -25.854 -21.689  1.00 21.05           O
ANISOU 1814  O   ALA A 575     2506   2543   2949    -56    404   -172       O
ATOM   1815  CB  ALA A 575     -24.097 -22.914 -23.061  1.00 13.36           C
ANISOU 1815  CB  ALA A 575     1522   1573   1980     39    356   -213       C
ATOM   1816  N   ASN A 576     -25.157 -25.800 -22.795  1.00 17.74           N
ANISOU 1816  N   ASN A 576     2004   2104   2633    -23    347   -225       N
ATOM   1817  CA  ASN A 576     -25.721 -26.904 -22.033  1.00 22.17           C
ANISOU 1817  CA  ASN A 576     2525   2657   3242    -76    365   -216       C
ATOM   1818  C   ASN A 576     -25.943 -28.135 -22.905  1.00 20.78           C
ANISOU 1818  C   ASN A 576     2343   2447   3104    -75    289   -225       C
ATOM   1819  O   ASN A 576     -26.792 -28.978 -22.618  1.00 21.79           O
ANISOU 1819  O   ASN A 576     2422   2558   3298   -115    276   -221       O
ATOM   1820  CB  ASN A 576     -27.031 -26.474 -21.373  1.00 29.46           C
ANISOU 1820  CB  ASN A 576     3374   3597   4223    -92    407   -227       C
ATOM   1821  CG  ASN A 576     -26.832 -25.347 -20.383  1.00 37.93           C
ANISOU 1821  CG  ASN A 576     4459   4701   5254    -86    476   -224       C
ATOM   1822  OD1 ASN A 576     -25.927 -25.394 -19.546  1.00 37.57           O
ANISOU 1822  OD1 ASN A 576     4457   4662   5155   -109    518   -197       O
ATOM   1823  ND2 ASN A 576     -27.668 -24.324 -20.477  1.00 37.90           N
ANISOU 1823  ND2 ASN A 576     4419   4710   5272    -48    481   -255       N
ATOM   1824  N   CYS A 577     -25.166 -28.231 -23.974  1.00 16.32           N
ANISOU 1824  N   CYS A 577     1639   1867   2694     86   -139   -282       N
ATOM   1825  CA  CYS A 577     -25.228 -29.380 -24.858  1.00 17.41           C
ANISOU 1825  CA  CYS A 577     1755   2002   2857     72   -173   -327       C
ATOM   1826  C   CYS A 577     -23.838 -29.686 -25.394  1.00 16.05           C
ANISOU 1826  C   CYS A 577     1626   1837   2635     76   -182   -338       C
ATOM   1827  O   CYS A 577     -23.625 -29.712 -26.602  1.00 17.82           O
ANISOU 1827  O   CYS A 577     1851   2095   2825     88   -223   -372       O
ATOM   1828  CB  CYS A 577     -26.197 -29.128 -26.008  1.00 16.41           C
ANISOU 1828  CB  CYS A 577     1591   1912   2734     85   -223   -361       C
ATOM   1829  SG  CYS A 577     -26.563 -30.599 -27.012  1.00 19.80           S
ANISOU 1829  SG  CYS A 577     1976   2338   3210     65   -269   -436       S
ATOM   1830  N   HIS A 578     -22.896 -29.904 -24.480  1.00 12.73           N
ANISOU 1830  N   HIS A 578     1239   1392   2208     67   -144   -309       N
ATOM   1831  CA  HIS A 578     -21.530 -30.273 -24.845  1.00 12.06           C
ANISOU 1831  CA  HIS A 578     1191   1308   2082     70   -147   -318       C
ATOM   1832  C   HIS A 578     -21.099 -31.499 -24.038  1.00 17.09           C
ANISOU 1832  C   HIS A 578     1826   1899   2769     47   -119   -312       C
ATOM   1833  O   HIS A 578     -21.802 -31.922 -23.129  1.00 19.08           O
ANISOU 1833  O   HIS A 578     2051   2121   3077     30    -94   -291       O
ATOM   1834  CB  HIS A 578     -20.573 -29.091 -24.642  1.00 11.60           C
ANISOU 1834  CB  HIS A 578     1180   1273   1956     88   -132   -280       C
ATOM   1835  CG  HIS A 578     -20.399 -28.686 -23.208  1.00 17.65           C
ANISOU 1835  CG  HIS A 578     1961   2018   2726     82    -87   -237       C
ATOM   1836  ND1 HIS A 578     -21.149 -27.692 -22.616  1.00 19.36           N
ANISOU 1836  ND1 HIS A 578     2169   2240   2946     90    -72   -216       N
ATOM   1837  CD2 HIS A 578     -19.557 -29.146 -22.248  1.00 16.36           C
ANISOU 1837  CD2 HIS A 578     1818   1836   2562     72    -54   -214       C
ATOM   1838  CE1 HIS A 578     -20.781 -27.557 -21.351  1.00 19.67           C
ANISOU 1838  CE1 HIS A 578     2223   2268   2981     85    -32   -187       C
ATOM   1839  NE2 HIS A 578     -19.817 -28.429 -21.103  1.00 19.04           N
ANISOU 1839  NE2 HIS A 578     2162   2177   2897     73    -22   -182       N
ATOM   1840  N   LEU A 579     -19.959 -32.088 -24.378  1.00 13.27           N
ANISOU 1840  N   LEU A 579     1365   1409   2267     49   -124   -327       N
ATOM   1841  CA  LEU A 579     -19.510 -33.277 -23.666  1.00 12.08           C
ANISOU 1841  CA  LEU A 579     1210   1210   2169     31   -101   -318       C
ATOM   1842  C   LEU A 579     -18.716 -32.894 -22.427  1.00 14.20           C
ANISOU 1842  C   LEU A 579     1511   1475   2409     32    -58   -257       C
ATOM   1843  O   LEU A 579     -19.090 -33.246 -21.313  1.00 15.53           O
ANISOU 1843  O   LEU A 579     1666   1619   2617     18    -26   -218       O
ATOM   1844  CB  LEU A 579     -18.681 -34.188 -24.584  1.00 13.68           C
ANISOU 1844  CB  LEU A 579     1416   1405   2377     35   -125   -369       C
ATOM   1845  CG  LEU A 579     -19.361 -34.560 -25.904  1.00 16.44           C
ANISOU 1845  CG  LEU A 579     1733   1771   2744     37   -172   -443       C
ATOM   1846  CD1 LEU A 579     -18.471 -35.540 -26.676  1.00 18.20           C
ANISOU 1846  CD1 LEU A 579     1956   1984   2974     43   -191   -500       C
ATOM   1847  CD2 LEU A 579     -20.744 -35.148 -25.671  1.00 20.69           C
ANISOU 1847  CD2 LEU A 579     2219   2274   3369     15   -178   -456       C
ATOM   1848  N   ALA A 580     -17.629 -32.150 -22.615  1.00 14.15           N
ANISOU 1848  N   ALA A 580     1545   1498   2331     49    -59   -249       N
ATOM   1849  CA  ALA A 580     -16.846 -31.678 -21.477  1.00 13.74           C
ANISOU 1849  CA  ALA A 580     1524   1452   2247     51    -24   -199       C
ATOM   1850  C   ALA A 580     -16.026 -30.454 -21.858  1.00 16.83           C
ANISOU 1850  C   ALA A 580     1950   1880   2564     68    -31   -196       C
ATOM   1851  O   ALA A 580     -15.779 -30.206 -23.041  1.00 15.17           O
ANISOU 1851  O   ALA A 580     1746   1693   2325     79    -60   -224       O
ATOM   1852  CB  ALA A 580     -15.913 -32.794 -20.970  1.00 12.44           C
ANISOU 1852  CB  ALA A 580     1364   1257   2107     44     -8   -184       C
ATOM   1853  N   ARG A 581     -15.603 -29.692 -20.855  1.00 13.40           N
ANISOU 1853  N   ARG A 581     1536   1455   2099     70     -5   -160       N
ATOM   1854  CA  ARG A 581     -14.704 -28.578 -21.105  1.00 11.86           C
ANISOU 1854  CA  ARG A 581     1373   1286   1846     82     -9   -154       C
ATOM   1855  C   ARG A 581     -13.257 -29.067 -21.098  1.00 13.46           C
ANISOU 1855  C   ARG A 581     1597   1491   2025     82     -5   -149       C
ATOM   1856  O   ARG A 581     -12.797 -29.676 -20.126  1.00 15.74           O
ANISOU 1856  O   ARG A 581     1889   1768   2325     76     16   -127       O
ATOM   1857  CB  ARG A 581     -14.893 -27.473 -20.059  1.00 16.00           C
ANISOU 1857  CB  ARG A 581     1906   1819   2354     84     14   -130       C
ATOM   1858  CG  ARG A 581     -14.018 -26.256 -20.337  1.00 15.61           C
ANISOU 1858  CG  ARG A 581     1884   1787   2260     93      7   -125       C
ATOM   1859  CD  ARG A 581     -14.299 -25.119 -19.376  1.00 16.19           C
ANISOU 1859  CD  ARG A 581     1962   1863   2328     97     26   -116       C
ATOM   1860  NE  ARG A 581     -14.060 -25.472 -17.977  1.00 13.99           N
ANISOU 1860  NE  ARG A 581     1683   1589   2044     90     55   -104       N
ATOM   1861  CZ  ARG A 581     -12.862 -25.522 -17.400  1.00 17.44           C
ANISOU 1861  CZ  ARG A 581     2138   2036   2450     87     65    -94       C
ATOM   1862  NH1 ARG A 581     -11.759 -25.290 -18.107  1.00 20.74           N
ANISOU 1862  NH1 ARG A 581     2577   2458   2847     88     49    -95       N
ATOM   1863  NH2 ARG A 581     -12.768 -25.829 -16.105  1.00 16.44           N
ANISOU 1863  NH2 ARG A 581     2008   1924   2314     84     90    -80       N
ATOM   1864  N   ALA A 582     -12.549 -28.817 -22.195  1.00 15.02           N
ANISOU 1864  N   ALA A 582     1807   1709   2190     91    -26   -166       N
ATOM   1865  CA  ALA A 582     -11.143 -29.198 -22.304  1.00 13.45           C
ANISOU 1865  CA  ALA A 582     1625   1518   1967     94    -23   -164       C
ATOM   1866  C   ALA A 582     -10.273 -28.015 -21.910  1.00 14.56           C
ANISOU 1866  C   ALA A 582     1790   1678   2063     96    -12   -138       C
ATOM   1867  O   ALA A 582     -10.385 -26.935 -22.494  1.00 18.96           O
ANISOU 1867  O   ALA A 582     2354   2253   2598    101    -22   -134       O
ATOM   1868  CB  ALA A 582     -10.817 -29.613 -23.729  1.00 16.62           C
ANISOU 1868  CB  ALA A 582     2022   1939   2353    104    -47   -200       C
ATOM   1869  N   PRO A 583      -9.378 -28.224 -20.942  1.00 12.53           N
ANISOU 1869  N   PRO A 583     1543   1417   1799     92      6   -119       N
ATOM   1870  CA  PRO A 583      -8.604 -27.085 -20.422  1.00 14.98           C
ANISOU 1870  CA  PRO A 583     1872   1744   2076     90     15   -100       C
ATOM   1871  C   PRO A 583      -7.347 -26.797 -21.236  1.00 15.27           C
ANISOU 1871  C   PRO A 583     1920   1802   2080     94      6   -101       C
ATOM   1872  O   PRO A 583      -6.849 -27.684 -21.930  1.00 15.13           O
ANISOU 1872  O   PRO A 583     1898   1790   2062    100      0   -115       O
ATOM   1873  CB  PRO A 583      -8.197 -27.574 -19.033  1.00 16.31           C
ANISOU 1873  CB  PRO A 583     2041   1909   2247     85     36    -81       C
ATOM   1874  CG  PRO A 583      -7.985 -29.075 -19.246  1.00 18.33           C
ANISOU 1874  CG  PRO A 583     2286   2149   2531     88     34    -83       C
ATOM   1875  CD  PRO A 583      -9.079 -29.484 -20.224  1.00 14.31           C
ANISOU 1875  CD  PRO A 583     1761   1624   2053     89     19   -110       C
ATOM   1876  N   ASN A 584      -6.833 -25.572 -21.154  1.00 13.10           N
ANISOU 1876  N   ASN A 584     1657   1538   1784     91      8    -87       N
ATOM   1877  CA  ASN A 584      -5.487 -25.315 -21.677  1.00 11.46           C
ANISOU 1877  CA  ASN A 584     1455   1350   1548     90      6    -80       C
ATOM   1878  C   ASN A 584      -4.467 -26.047 -20.801  1.00 14.08           C
ANISOU 1878  C   ASN A 584     1788   1685   1876     88     17    -76       C
ATOM   1879  O   ASN A 584      -4.764 -26.370 -19.649  1.00 15.04           O
ANISOU 1879  O   ASN A 584     1908   1795   2009     85     27    -71       O
ATOM   1880  CB  ASN A 584      -5.192 -23.819 -21.649  1.00 17.12           C
ANISOU 1880  CB  ASN A 584     2178   2068   2257     83      6    -63       C
ATOM   1881  CG  ASN A 584      -5.974 -23.040 -22.696  1.00 22.55           C
ANISOU 1881  CG  ASN A 584     2863   2757   2948     89     -7    -54       C
ATOM   1882  OD1 ASN A 584      -6.885 -23.568 -23.343  1.00 23.71           O
ANISOU 1882  OD1 ASN A 584     3003   2909   3098     98    -17    -66       O
ATOM   1883  ND2 ASN A 584      -5.608 -21.776 -22.877  1.00 17.06           N
ANISOU 1883  ND2 ASN A 584     2170   2057   2253     83     -7    -32       N
ATOM   1884  N   HIS A 585      -3.261 -26.299 -21.329  1.00 12.52           N
ANISOU 1884  N   HIS A 585     1590   1507   1660     91     16    -74       N
ATOM   1885  CA  HIS A 585      -2.194 -26.838 -20.489  1.00 12.41           C
ANISOU 1885  CA  HIS A 585     1574   1498   1643     91     25    -66       C
ATOM   1886  C   HIS A 585      -1.902 -25.864 -19.348  1.00 11.86           C
ANISOU 1886  C   HIS A 585     1510   1432   1564     78     30    -55       C
ATOM   1887  O   HIS A 585      -2.174 -24.666 -19.467  1.00 13.99           O
ANISOU 1887  O   HIS A 585     1785   1699   1833     70     28    -55       O
ATOM   1888  CB  HIS A 585      -0.926 -27.108 -21.318  1.00 13.57           C
ANISOU 1888  CB  HIS A 585     1715   1669   1771     97     23    -69       C
ATOM   1889  CG  HIS A 585      -1.102 -28.162 -22.370  1.00 17.00           C
ANISOU 1889  CG  HIS A 585     2140   2105   2212    113     18    -93       C
ATOM   1890  ND1 HIS A 585      -0.044 -28.739 -23.038  1.00 21.41           N
ANISOU 1890  ND1 HIS A 585     2689   2687   2759    124     19   -105       N
ATOM   1891  CD2 HIS A 585      -2.222 -28.742 -22.874  1.00 19.01           C
ANISOU 1891  CD2 HIS A 585     2391   2345   2486    119      9   -115       C
ATOM   1892  CE1 HIS A 585      -0.498 -29.629 -23.907  1.00 25.20           C
ANISOU 1892  CE1 HIS A 585     3160   3165   3249    139     12   -138       C
ATOM   1893  NE2 HIS A 585      -1.820 -29.642 -23.829  1.00 20.75           N
ANISOU 1893  NE2 HIS A 585     2600   2578   2706    134      4   -145       N
ATOM   1894  N   ALA A 586      -1.377 -26.385 -18.240  1.00 13.56           N
ANISOU 1894  N   ALA A 586     1721   1654   1776     79     36    -46       N
ATOM   1895  CA  ALA A 586      -1.109 -25.586 -17.039  1.00 12.63           C
ANISOU 1895  CA  ALA A 586     1604   1549   1643     70     39    -44       C
ATOM   1896  C   ALA A 586       0.244 -25.926 -16.438  1.00 14.94           C
ANISOU 1896  C   ALA A 586     1890   1869   1919     71     38    -35       C
ATOM   1897  O   ALA A 586       0.660 -27.079 -16.455  1.00 15.44           O
ANISOU 1897  O   ALA A 586     1945   1933   1986     83     39    -21       O
ATOM   1898  CB  ALA A 586      -2.198 -25.809 -15.986  1.00 11.79           C
ANISOU 1898  CB  ALA A 586     1498   1440   1541     72     48    -42       C
ATOM   1899  N   VAL A 587       0.909 -24.924 -15.872  1.00 12.80           N
ANISOU 1899  N   VAL A 587     1617   1615   1633     59     33    -43       N
ATOM   1900  CA  VAL A 587       2.128 -25.177 -15.109  1.00 10.01           C
ANISOU 1900  CA  VAL A 587     1250   1292   1259     60     28    -37       C
ATOM   1901  C   VAL A 587       1.692 -25.602 -13.722  1.00 14.04           C
ANISOU 1901  C   VAL A 587     1758   1825   1752     67     33    -29       C
ATOM   1902  O   VAL A 587       0.853 -24.934 -13.115  1.00 14.47           O
ANISOU 1902  O   VAL A 587     1817   1881   1801     62     37    -45       O
ATOM   1903  CB  VAL A 587       2.968 -23.907 -14.970  1.00 11.99           C
ANISOU 1903  CB  VAL A 587     1495   1555   1506     41     19    -55       C
ATOM   1904  CG1 VAL A 587       4.160 -24.153 -14.031  1.00 10.87           C
ANISOU 1904  CG1 VAL A 587     1336   1452   1341     42     10    -53       C
ATOM   1905  CG2 VAL A 587       3.449 -23.458 -16.337  1.00 14.69           C
ANISOU 1905  CG2 VAL A 587     1836   1882   1864     33     19    -50       C
ATOM   1906  N   VAL A 588       2.231 -26.719 -13.235  1.00 13.20           N
ANISOU 1906  N   VAL A 588     1642   1737   1638     81     33     -1       N
ATOM   1907  CA  VAL A 588       1.889 -27.191 -11.891  1.00 15.35           C
ANISOU 1907  CA  VAL A 588     1907   2040   1887     90     38     19       C
ATOM   1908  C   VAL A 588       3.127 -27.181 -11.002  1.00 15.20           C
ANISOU 1908  C   VAL A 588     1872   2071   1833     94     26     27       C
ATOM   1909  O   VAL A 588       4.258 -27.300 -11.487  1.00 15.57           O
ANISOU 1909  O   VAL A 588     1909   2120   1886     94     15     28       O
ATOM   1910  CB  VAL A 588       1.288 -28.603 -11.910  1.00 16.48           C
ANISOU 1910  CB  VAL A 588     2046   2160   2054    105     50     59       C
ATOM   1911  CG1 VAL A 588       0.066 -28.642 -12.837  1.00 16.09           C
ANISOU 1911  CG1 VAL A 588     2009   2065   2042    100     58     45       C
ATOM   1912  CG2 VAL A 588       2.346 -29.626 -12.343  1.00 22.13           C
ANISOU 1912  CG2 VAL A 588     2751   2868   2789    119     43     81       C
ATOM   1913  N   THR A 589       2.907 -27.031  -9.701  1.00 14.92           N
ANISOU 1913  N   THR A 589     1828   2082   1757     98     27     31       N
ATOM   1914  CA  THR A 589       4.004 -26.983  -8.733  1.00 12.79           C
ANISOU 1914  CA  THR A 589     1539   1873   1446    103     11     35       C
ATOM   1915  C   THR A 589       3.465 -27.390  -7.362  1.00 13.69           C
ANISOU 1915  C   THR A 589     1645   2043   1515    117     19     63       C
ATOM   1916  O   THR A 589       2.272 -27.655  -7.223  1.00 14.16           O
ANISOU 1916  O   THR A 589     1711   2088   1580    120     39     78       O
ATOM   1917  CB  THR A 589       4.663 -25.578  -8.682  1.00 16.35           C
ANISOU 1917  CB  THR A 589     1986   2340   1885     83     -6    -22       C
ATOM   1918  OG1 THR A 589       5.854 -25.621  -7.872  1.00 21.45           O
ANISOU 1918  OG1 THR A 589     2609   3046   2496     87    -26    -21       O
ATOM   1919  CG2 THR A 589       3.699 -24.536  -8.120  1.00 15.55           C
ANISOU 1919  CG2 THR A 589     1892   2247   1768     73     -1    -67       C
ATOM   1920  N   ARG A 590       4.336 -27.472  -6.360  1.00 15.57           N
ANISOU 1920  N   ARG A 590     1862   2349   1704    126      4     74       N
ATOM   1921  CA  ARG A 590       3.881 -27.634  -4.972  1.00 15.64           C
ANISOU 1921  CA  ARG A 590     1858   2431   1652    140     10     95       C
ATOM   1922  C   ARG A 590       3.237 -26.336  -4.493  1.00 21.28           C
ANISOU 1922  C   ARG A 590     2578   3172   2337    127     12     25       C
ATOM   1923  O   ARG A 590       3.699 -25.255  -4.840  1.00 20.72           O
ANISOU 1923  O   ARG A 590     2508   3086   2277    109     -4    -38       O
ATOM   1924  CB  ARG A 590       5.064 -27.988  -4.060  1.00 15.45           C
ANISOU 1924  CB  ARG A 590     1808   2485   1579    155    -12    121       C
ATOM   1925  CG  ARG A 590       5.770 -29.276  -4.454  1.00 18.43           C
ANISOU 1925  CG  ARG A 590     2176   2836   1991    172    -15    190       C
ATOM   1926  CD  ARG A 590       6.874 -29.658  -3.464  1.00 20.30           C
ANISOU 1926  CD  ARG A 590     2382   3154   2175    192    -38    225       C
ATOM   1927  NE  ARG A 590       7.924 -28.641  -3.369  1.00 19.32           N
ANISOU 1927  NE  ARG A 590     2246   3069   2026    179    -68    161       N
ATOM   1928  CZ  ARG A 590       8.868 -28.449  -4.284  1.00 23.49           C
ANISOU 1928  CZ  ARG A 590     2771   3557   2598    168    -82    137       C
ATOM   1929  NH1 ARG A 590       8.892 -29.190  -5.387  1.00 17.66           N
ANISOU 1929  NH1 ARG A 590     2043   2743   1924    172    -69    166       N
ATOM   1930  NH2 ARG A 590       9.790 -27.506  -4.101  1.00 22.66           N
ANISOU 1930  NH2 ARG A 590     2648   3488   2472    153   -108     81       N
ATOM   1931  N   LYS A 591       2.188 -26.442  -3.684  1.00 20.76           N
ANISOU 1931  N   LYS A 591     2509   3144   2236    136     33     37       N
ATOM   1932  CA  LYS A 591       1.462 -25.257  -3.217  1.00 18.46           C
ANISOU 1932  CA  LYS A 591     2220   2876   1920    129     38    -34       C
ATOM   1933  C   LYS A 591       2.400 -24.217  -2.604  1.00 21.58           C
ANISOU 1933  C   LYS A 591     2599   3325   2274    123      9   -104       C
ATOM   1934  O   LYS A 591       2.217 -23.014  -2.793  1.00 21.35           O
ANISOU 1934  O   LYS A 591     2575   3271   2266    107      3   -181       O
ATOM   1935  CB  LYS A 591       0.352 -25.648  -2.231  1.00 23.50           C
ANISOU 1935  CB  LYS A 591     2847   3569   2511    145     66     -4       C
ATOM   1936  CG  LYS A 591      -0.457 -24.468  -1.662  1.00 28.05           C
ANISOU 1936  CG  LYS A 591     3421   4178   3058    143     75    -83       C
ATOM   1937  CD  LYS A 591      -1.340 -23.793  -2.723  1.00 24.02           C
ANISOU 1937  CD  LYS A 591     2931   3574   2621    128     85   -123       C
ATOM   1938  CE  LYS A 591      -2.219 -22.711  -2.087  1.00 32.16           C
ANISOU 1938  CE  LYS A 591     3954   4635   3629    132     97   -197       C
ATOM   1939  NZ  LYS A 591      -3.175 -22.101  -3.062  1.00 28.63           N
ANISOU 1939  NZ  LYS A 591     3524   4101   3255    122    107   -226       N
ATOM   1940  N   ASP A 592       3.418 -24.669  -1.883  1.00 23.34           N
ANISOU 1940  N   ASP A 592     2802   3619   2448    134    -10    -79       N
ATOM   1941  CA  ASP A 592       4.308 -23.733  -1.203  1.00 28.23           C
ANISOU 1941  CA  ASP A 592     3400   4299   3025    128    -41   -151       C
ATOM   1942  C   ASP A 592       5.267 -23.022  -2.158  1.00 25.24           C
ANISOU 1942  C   ASP A 592     3024   3856   2708    102    -65   -195       C
ATOM   1943  O   ASP A 592       6.011 -22.147  -1.742  1.00 26.32           O
ANISOU 1943  O   ASP A 592     3142   4027   2830     91    -93   -261       O
ATOM   1944  CB  ASP A 592       5.101 -24.433  -0.101  1.00 35.78           C
ANISOU 1944  CB  ASP A 592     4328   5362   3903    150    -58   -109       C
ATOM   1945  CG  ASP A 592       6.234 -25.262  -0.650  1.00 55.59           C
ANISOU 1945  CG  ASP A 592     6832   7848   6442    153    -75    -50       C
ATOM   1946  OD1 ASP A 592       5.967 -26.384  -1.130  1.00 64.74           O
ANISOU 1946  OD1 ASP A 592     8001   8964   7634    164    -56     32       O
ATOM   1947  OD2 ASP A 592       7.391 -24.787  -0.611  1.00 61.28           O
ANISOU 1947  OD2 ASP A 592     7534   8590   7159    144   -108    -89       O
ATOM   1948  N   LYS A 593       5.248 -23.398  -3.434  1.00 20.49           N
ANISOU 1948  N   LYS A 593     2443   3167   2177     94    -55   -158       N
ATOM   1949  CA  LYS A 593       6.078 -22.732  -4.437  1.00 20.27           C
ANISOU 1949  CA  LYS A 593     2416   3079   2207     69    -71   -189       C
ATOM   1950  C   LYS A 593       5.249 -21.856  -5.367  1.00 22.62           C
ANISOU 1950  C   LYS A 593     2735   3293   2565     51    -57   -225       C
ATOM   1951  O   LYS A 593       5.784 -21.270  -6.309  1.00 22.70           O
ANISOU 1951  O   LYS A 593     2748   3249   2629     30    -65   -241       O
ATOM   1952  CB  LYS A 593       6.824 -23.758  -5.285  1.00 19.56           C
ANISOU 1952  CB  LYS A 593     2327   2958   2147     75    -71   -125       C
ATOM   1953  CG  LYS A 593       7.983 -24.421  -4.580  1.00 28.54           C
ANISOU 1953  CG  LYS A 593     3437   4165   3244     90    -93    -94       C
ATOM   1954  CD  LYS A 593       9.107 -23.419  -4.388  1.00 34.41           C
ANISOU 1954  CD  LYS A 593     4155   4935   3986     70   -124   -156       C
ATOM   1955  CE  LYS A 593      10.371 -24.091  -3.899  1.00 36.39           C
ANISOU 1955  CE  LYS A 593     4374   5248   4205     84   -148   -124       C
ATOM   1956  NZ  LYS A 593      11.465 -23.098  -3.750  1.00 28.55           N
ANISOU 1956  NZ  LYS A 593     3352   4278   3218     61   -180   -187       N
ATOM   1957  N   GLU A 594       3.947 -21.774  -5.109  1.00 20.02           N
ANISOU 1957  N   GLU A 594     2420   2959   2229     60    -36   -232       N
ATOM   1958  CA  GLU A 594       3.046 -21.011  -5.976  1.00 21.72           C
ANISOU 1958  CA  GLU A 594     2654   3098   2502     47    -23   -258       C
ATOM   1959  C   GLU A 594       3.516 -19.566  -6.219  1.00 20.57           C
ANISOU 1959  C   GLU A 594     2500   2917   2397     23    -41   -328       C
ATOM   1960  O   GLU A 594       3.599 -19.115  -7.365  1.00 19.60           O
ANISOU 1960  O   GLU A 594     2386   2723   2336      7    -41   -322       O
ATOM   1961  CB  GLU A 594       1.620 -21.036  -5.414  1.00 23.86           C
ANISOU 1961  CB  GLU A 594     2931   3382   2752     62      1   -265       C
ATOM   1962  CG  GLU A 594       0.585 -20.349  -6.292  1.00 22.95           C
ANISOU 1962  CG  GLU A 594     2832   3190   2696     54     14   -284       C
ATOM   1963  CD  GLU A 594      -0.825 -20.427  -5.710  1.00 35.35           C
ANISOU 1963  CD  GLU A 594     4403   4779   4247     70     39   -290       C
ATOM   1964  OE1 GLU A 594      -0.961 -20.584  -4.475  1.00 33.29           O
ANISOU 1964  OE1 GLU A 594     4128   4597   3924     84     45   -303       O
ATOM   1965  OE2 GLU A 594      -1.799 -20.335  -6.488  1.00 27.16           O
ANISOU 1965  OE2 GLU A 594     3379   3684   3255     70     53   -280       O
ATOM   1966  N   ALA A 595       3.813 -18.832  -5.148  1.00 18.49           N
ANISOU 1966  N   ALA A 595     2217   2706   2104     21    -58   -394       N
ATOM   1967  CA  ALA A 595       4.195 -17.425  -5.290  1.00 23.05           C
ANISOU 1967  CA  ALA A 595     2782   3244   2734     -4    -77   -467       C
ATOM   1968  C   ALA A 595       5.503 -17.280  -6.052  1.00 23.64           C
ANISOU 1968  C   ALA A 595     2845   3288   2849    -27    -95   -451       C
ATOM   1969  O   ALA A 595       5.657 -16.399  -6.903  1.00 23.82           O
ANISOU 1969  O   ALA A 595     2868   3237   2944    -50    -98   -465       O
ATOM   1970  CB  ALA A 595       4.305 -16.757  -3.925  1.00 25.32           C
ANISOU 1970  CB  ALA A 595     3044   3600   2977      0    -94   -552       C
ATOM   1971  N   CYS A 596       6.440 -18.159  -5.728  1.00 21.76           N
ANISOU 1971  N   CYS A 596     2594   3107   2565    -20   -106   -416       N
ATOM   1972  CA  CYS A 596       7.754 -18.189  -6.350  1.00 23.39           C
ANISOU 1972  CA  CYS A 596     2784   3300   2801    -38   -122   -396       C
ATOM   1973  C   CYS A 596       7.641 -18.434  -7.859  1.00 17.98           C
ANISOU 1973  C   CYS A 596     2120   2541   2171    -45   -102   -339       C
ATOM   1974  O   CYS A 596       8.196 -17.692  -8.677  1.00 19.28           O
ANISOU 1974  O   CYS A 596     2276   2657   2394    -70   -107   -345       O
ATOM   1975  CB  CYS A 596       8.577 -19.292  -5.685  1.00 27.77           C
ANISOU 1975  CB  CYS A 596     3323   3936   3293    -19   -134   -359       C
ATOM   1976  SG  CYS A 596      10.089 -19.745  -6.516  1.00 36.78           S
ANISOU 1976  SG  CYS A 596     4444   5068   4462    -30   -146   -316       S
ATOM   1977  N   VAL A 597       6.904 -19.471  -8.221  1.00 17.93           N
ANISOU 1977  N   VAL A 597     2137   2530   2146    -23    -81   -284       N
ATOM   1978  CA  VAL A 597       6.718 -19.796  -9.626  1.00 17.37           C
ANISOU 1978  CA  VAL A 597     2084   2401   2116    -25    -63   -237       C
ATOM   1979  C   VAL A 597       5.995 -18.663 -10.366  1.00 18.93           C
ANISOU 1979  C   VAL A 597     2293   2530   2369    -41    -56   -258       C
ATOM   1980  O   VAL A 597       6.389 -18.298 -11.469  1.00 18.03           O
ANISOU 1980  O   VAL A 597     2178   2374   2298    -57    -53   -238       O
ATOM   1981  CB  VAL A 597       6.028 -21.153  -9.792  1.00 18.75           C
ANISOU 1981  CB  VAL A 597     2277   2582   2264      2    -45   -184       C
ATOM   1982  CG1 VAL A 597       5.593 -21.375 -11.248  1.00 18.54           C
ANISOU 1982  CG1 VAL A 597     2269   2498   2278      1    -29   -151       C
ATOM   1983  CG2 VAL A 597       6.982 -22.258  -9.331  1.00 18.81           C
ANISOU 1983  CG2 VAL A 597     2269   2642   2236     18    -53   -149       C
ATOM   1984  N   HIS A 598       4.965 -18.082  -9.754  1.00 15.74           N
ANISOU 1984  N   HIS A 598     1897   2119   1965    -37    -53   -298       N
ATOM   1985  CA  HIS A 598       4.305 -16.922 -10.360  1.00 20.15           C
ANISOU 1985  CA  HIS A 598     2461   2610   2584    -51    -49   -321       C
ATOM   1986  C   HIS A 598       5.308 -15.824 -10.701  1.00 20.01           C
ANISOU 1986  C   HIS A 598     2422   2559   2623    -81    -65   -343       C
ATOM   1987  O   HIS A 598       5.330 -15.310 -11.818  1.00 20.55           O
ANISOU 1987  O   HIS A 598     2492   2571   2744    -95    -59   -314       O
ATOM   1988  CB  HIS A 598       3.264 -16.323  -9.413  1.00 20.31           C
ANISOU 1988  CB  HIS A 598     2483   2636   2599    -41    -47   -377       C
ATOM   1989  CG  HIS A 598       1.975 -17.078  -9.369  1.00 19.88           C
ANISOU 1989  CG  HIS A 598     2448   2590   2517    -16    -25   -351       C
ATOM   1990  ND1 HIS A 598       1.063 -16.925  -8.352  1.00 23.09           N
ANISOU 1990  ND1 HIS A 598     2852   3025   2895     -1    -17   -391       N
ATOM   1991  CD2 HIS A 598       1.449 -18.005 -10.211  1.00 18.45           C
ANISOU 1991  CD2 HIS A 598     2284   2391   2333     -5    -10   -291       C
ATOM   1992  CE1 HIS A 598       0.025 -17.718  -8.564  1.00 25.24           C
ANISOU 1992  CE1 HIS A 598     3140   3298   3153     17      3   -352       C
ATOM   1993  NE2 HIS A 598       0.239 -18.384  -9.689  1.00 19.72           N
ANISOU 1993  NE2 HIS A 598     2453   2569   2471     14      6   -294       N
ATOM   1994  N   LYS A 599       6.120 -15.454  -9.718  1.00 16.72           N
ANISOU 1994  N   LYS A 599     1980   2180   2193    -92    -86   -395       N
ATOM   1995  CA  LYS A 599       7.031 -14.325  -9.861  1.00 17.54           C
ANISOU 1995  CA  LYS A 599     2056   2249   2359   -125   -104   -428       C
ATOM   1996  C   LYS A 599       8.109 -14.588 -10.899  1.00 18.77           C
ANISOU 1996  C   LYS A 599     2201   2394   2537   -141   -101   -370       C
ATOM   1997  O   LYS A 599       8.359 -13.767 -11.776  1.00 17.71           O
ANISOU 1997  O   LYS A 599     2058   2201   2471   -165    -98   -353       O
ATOM   1998  CB  LYS A 599       7.676 -13.994  -8.509  1.00 19.43           C
ANISOU 1998  CB  LYS A 599     2267   2544   2573   -131   -130   -504       C
ATOM   1999  CG  LYS A 599       8.705 -12.882  -8.557  1.00 28.95           C
ANISOU 1999  CG  LYS A 599     3436   3715   3847   -168   -153   -546       C
ATOM   2000  CD  LYS A 599       9.374 -12.706  -7.199  1.00 40.84           C
ANISOU 2000  CD  LYS A 599     4911   5290   5316   -171   -184   -626       C
ATOM   2001  CE  LYS A 599      10.407 -11.590  -7.236  1.00 47.34           C
ANISOU 2001  CE  LYS A 599     5693   6075   6219   -212   -209   -675       C
ATOM   2002  NZ  LYS A 599       9.771 -10.272  -7.525  1.00 52.27           N
ANISOU 2002  NZ  LYS A 599     6315   6604   6940   -230   -207   -718       N
ATOM   2003  N   ILE A 600       8.756 -15.739 -10.792  1.00 16.09           N
ANISOU 2003  N   ILE A 600     1860   2113   2142   -127   -101   -337       N
ATOM   2004  CA  ILE A 600       9.868 -16.052 -11.677  1.00 16.11           C
ANISOU 2004  CA  ILE A 600     1846   2116   2158   -139    -98   -290       C
ATOM   2005  C   ILE A 600       9.399 -16.209 -13.119  1.00 16.35           C
ANISOU 2005  C   ILE A 600     1897   2103   2213   -136    -73   -229       C
ATOM   2006  O   ILE A 600      10.017 -15.670 -14.043  1.00 15.79           O
ANISOU 2006  O   ILE A 600     1810   2002   2186   -158    -67   -201       O
ATOM   2007  CB  ILE A 600      10.602 -17.323 -11.203  1.00 17.07           C
ANISOU 2007  CB  ILE A 600     1959   2309   2217   -118   -104   -269       C
ATOM   2008  CG1 ILE A 600      11.269 -17.083  -9.846  1.00 25.23           C
ANISOU 2008  CG1 ILE A 600     2964   3398   3224   -124   -134   -325       C
ATOM   2009  CG2 ILE A 600      11.640 -17.774 -12.234  1.00 16.85           C
ANISOU 2009  CG2 ILE A 600     1916   2284   2204   -124    -96   -219       C
ATOM   2010  CD1 ILE A 600      12.343 -16.024  -9.869  1.00 35.43           C
ANISOU 2010  CD1 ILE A 600     4216   4674   4571   -161   -154   -361       C
ATOM   2011  N   LEU A 601       8.297 -16.930 -13.322  1.00 14.39           N
ANISOU 2011  N   LEU A 601     1681   1854   1934   -109    -58   -208       N
ATOM   2012  CA  LEU A 601       7.834 -17.186 -14.682  1.00 13.35           C
ANISOU 2012  CA  LEU A 601     1567   1693   1815   -102    -38   -156       C
ATOM   2013  C   LEU A 601       7.281 -15.934 -15.346  1.00 17.05           C
ANISOU 2013  C   LEU A 601     2037   2099   2343   -120    -34   -153       C
ATOM   2014  O   LEU A 601       7.410 -15.775 -16.551  1.00 18.40           O
ANISOU 2014  O   LEU A 601     2207   2251   2534   -125    -22   -106       O
ATOM   2015  CB  LEU A 601       6.807 -18.315 -14.731  1.00 14.26           C
ANISOU 2015  CB  LEU A 601     1710   1821   1888    -70    -26   -139       C
ATOM   2016  CG  LEU A 601       7.416 -19.718 -14.827  1.00 21.86           C
ANISOU 2016  CG  LEU A 601     2671   2827   2810    -51    -22   -112       C
ATOM   2017  CD1 LEU A 601       7.999 -19.945 -16.221  1.00 27.85           C
ANISOU 2017  CD1 LEU A 601     3423   3580   3580    -52    -10    -73       C
ATOM   2018  CD2 LEU A 601       8.482 -19.943 -13.787  1.00 26.12           C
ANISOU 2018  CD2 LEU A 601     3186   3411   3327    -53    -39   -130       C
ATOM   2019  N   ARG A 602       6.669 -15.044 -14.578  1.00 17.10           N
ANISOU 2019  N   ARG A 602     2043   2075   2378   -126    -44   -200       N
ATOM   2020  CA  ARG A 602       6.225 -13.790 -15.176  1.00 15.62           C
ANISOU 2020  CA  ARG A 602     1852   1820   2261   -143    -42   -195       C
ATOM   2021  C   ARG A 602       7.414 -12.989 -15.705  1.00 19.45           C
ANISOU 2021  C   ARG A 602     2307   2282   2802   -177    -45   -175       C
ATOM   2022  O   ARG A 602       7.359 -12.440 -16.801  1.00 18.90           O
ANISOU 2022  O   ARG A 602     2233   2173   2774   -187    -34   -123       O
ATOM   2023  CB  ARG A 602       5.413 -12.939 -14.203  1.00 18.70           C
ANISOU 2023  CB  ARG A 602     2243   2179   2682   -142    -52   -260       C
ATOM   2024  CG  ARG A 602       4.960 -11.634 -14.857  1.00 20.97           C
ANISOU 2024  CG  ARG A 602     2525   2386   3057   -157    -51   -250       C
ATOM   2025  CD  ARG A 602       3.838 -10.981 -14.076  1.00 28.10           C
ANISOU 2025  CD  ARG A 602     3433   3256   3986   -144    -56   -310       C
ATOM   2026  NE  ARG A 602       2.574 -11.708 -14.209  1.00 24.38           N
ANISOU 2026  NE  ARG A 602     2990   2803   3470   -112    -42   -293       N
ATOM   2027  CZ  ARG A 602       1.431 -11.293 -13.674  1.00 24.83           C
ANISOU 2027  CZ  ARG A 602     3053   2838   3543    -95    -41   -335       C
ATOM   2028  NH1 ARG A 602       1.404 -10.161 -12.979  1.00 27.26           N
ANISOU 2028  NH1 ARG A 602     3342   3105   3910   -105    -52   -401       N
ATOM   2029  NH2 ARG A 602       0.317 -11.999 -13.826  1.00 25.00           N
ANISOU 2029  NH2 ARG A 602     3096   2877   3526    -68    -28   -316       N
ATOM   2030  N   GLN A 603       8.489 -12.925 -14.924  1.00 17.48           N
ANISOU 2030  N   GLN A 603     2030   2060   2552   -194    -61   -212       N
ATOM   2031  CA  GLN A 603       9.692 -12.234 -15.372  1.00 20.83           C
ANISOU 2031  CA  GLN A 603     2418   2465   3031   -229    -64   -194       C
ATOM   2032  C   GLN A 603      10.311 -12.936 -16.588  1.00 16.60           C
ANISOU 2032  C   GLN A 603     1880   1959   2469   -225    -43   -118       C
ATOM   2033  O   GLN A 603      10.750 -12.279 -17.536  1.00 18.08           O
ANISOU 2033  O   GLN A 603     2047   2115   2705   -248    -32    -69       O
ATOM   2034  CB  GLN A 603      10.706 -12.122 -14.225  1.00 18.64           C
ANISOU 2034  CB  GLN A 603     2109   2220   2752   -246    -89   -256       C
ATOM   2035  CG  GLN A 603      11.953 -11.326 -14.576  1.00 25.83           C
ANISOU 2035  CG  GLN A 603     2974   3107   3731   -287    -95   -246       C
ATOM   2036  CD  GLN A 603      11.687  -9.836 -14.618  1.00 40.11           C
ANISOU 2036  CD  GLN A 603     4766   4828   5644   -318   -102   -269       C
ATOM   2037  OE1 GLN A 603      10.561  -9.388 -14.390  1.00 39.91           O
ANISOU 2037  OE1 GLN A 603     4763   4761   5638   -305   -103   -296       O
ATOM   2038  NE2 GLN A 603      12.725  -9.054 -14.903  1.00 35.56           N
ANISOU 2038  NE2 GLN A 603     4146   4222   5144   -358   -107   -258       N
ATOM   2039  N   GLN A 604      10.330 -14.267 -16.570  1.00 13.58           N
ANISOU 2039  N   GLN A 604     1514   1635   2011   -196    -37   -107       N
ATOM   2040  CA  GLN A 604      10.893 -15.015 -17.682  1.00 16.72           C
ANISOU 2040  CA  GLN A 604     1907   2065   2380   -188    -18    -48       C
ATOM   2041  C   GLN A 604      10.152 -14.770 -18.985  1.00 14.40           C
ANISOU 2041  C   GLN A 604     1630   1746   2097   -181      2      7       C
ATOM   2042  O   GLN A 604      10.772 -14.640 -20.031  1.00 15.92           O
ANISOU 2042  O   GLN A 604     1804   1948   2297   -191     19     59       O
ATOM   2043  CB  GLN A 604      10.944 -16.505 -17.369  1.00 15.65           C
ANISOU 2043  CB  GLN A 604     1786   1987   2173   -154    -17    -53       C
ATOM   2044  CG  GLN A 604      11.989 -16.838 -16.302  1.00 16.35           C
ANISOU 2044  CG  GLN A 604     1850   2118   2246   -159    -36    -88       C
ATOM   2045  CD  GLN A 604      13.366 -16.364 -16.691  1.00 19.51           C
ANISOU 2045  CD  GLN A 604     2205   2526   2680   -187    -36    -72       C
ATOM   2046  OE1 GLN A 604      13.909 -16.791 -17.716  1.00 16.11           O
ANISOU 2046  OE1 GLN A 604     1764   2116   2240   -182    -16    -26       O
ATOM   2047  NE2 GLN A 604      13.946 -15.463 -15.880  1.00 18.63           N
ANISOU 2047  NE2 GLN A 604     2065   2403   2610   -217    -57   -113       N
ATOM   2048  N   GLN A 605       8.827 -14.709 -18.936  1.00 13.83           N
ANISOU 2048  N   GLN A 605     1589   1646   2021   -164      1     -2       N
ATOM   2049  CA  GLN A 605       8.097 -14.470 -20.174  1.00 13.26           C
ANISOU 2049  CA  GLN A 605     1529   1555   1955   -156     16     51       C
ATOM   2050  C   GLN A 605       8.195 -13.028 -20.639  1.00 16.00           C
ANISOU 2050  C   GLN A 605     1855   1845   2378   -185     18     84       C
ATOM   2051  O   GLN A 605       8.119 -12.761 -21.832  1.00 17.77           O
ANISOU 2051  O   GLN A 605     2075   2069   2608   -185     33    148       O
ATOM   2052  CB  GLN A 605       6.640 -14.937 -20.095  1.00 15.01           C
ANISOU 2052  CB  GLN A 605     1785   1769   2149   -126     15     37       C
ATOM   2053  CG  GLN A 605       5.734 -14.128 -19.194  1.00 16.84           C
ANISOU 2053  CG  GLN A 605     2026   1950   2422   -130      2     -6       C
ATOM   2054  CD  GLN A 605       4.383 -14.809 -19.068  1.00 18.84           C
ANISOU 2054  CD  GLN A 605     2308   2209   2640    -99      3    -19       C
ATOM   2055  OE1 GLN A 605       4.139 -15.822 -19.719  1.00 25.54           O
ANISOU 2055  OE1 GLN A 605     3170   3093   3442    -79     11      4       O
ATOM   2056  NE2 GLN A 605       3.516 -14.275 -18.222  1.00 22.25           N
ANISOU 2056  NE2 GLN A 605     2748   2609   3097    -96     -5    -62       N
ATOM   2057  N   HIS A 606       8.392 -12.094 -19.716  1.00 15.15           N
ANISOU 2057  N   HIS A 606     1731   1691   2332   -209      3     40       N
ATOM   2058  CA  HIS A 606       8.685 -10.727 -20.153  1.00 17.29           C
ANISOU 2058  CA  HIS A 606     1975   1900   2694   -241      4     74       C
ATOM   2059  C   HIS A 606       9.997 -10.680 -20.939  1.00 20.05           C
ANISOU 2059  C   HIS A 606     2290   2277   3051   -265     19    130       C
ATOM   2060  O   HIS A 606      10.116  -9.953 -21.926  1.00 20.88           O
ANISOU 2060  O   HIS A 606     2377   2356   3200   -280     34    201       O
ATOM   2061  CB  HIS A 606       8.738  -9.769 -18.962  1.00 17.27           C
ANISOU 2061  CB  HIS A 606     1957   1842   2762   -264    -18      2       C
ATOM   2062  CG  HIS A 606       7.395  -9.493 -18.361  1.00 19.07           C
ANISOU 2062  CG  HIS A 606     2212   2033   3002   -243    -28    -45       C
ATOM   2063  ND1 HIS A 606       7.233  -8.752 -17.208  1.00 21.65           N
ANISOU 2063  ND1 HIS A 606     2528   2320   3379   -253    -48   -126       N
ATOM   2064  CD2 HIS A 606       6.153  -9.853 -18.756  1.00 23.12           C
ANISOU 2064  CD2 HIS A 606     2755   2546   3481   -211    -20    -26       C
ATOM   2065  CE1 HIS A 606       5.946  -8.670 -16.922  1.00 21.61           C
ANISOU 2065  CE1 HIS A 606     2548   2292   3371   -227    -49   -153       C
ATOM   2066  NE2 HIS A 606       5.269  -9.337 -17.840  1.00 22.94           N
ANISOU 2066  NE2 HIS A 606     2741   2483   3490   -202    -33    -91       N
ATOM   2067  N   LEU A 607      10.973 -11.464 -20.501  1.00 17.95           N
ANISOU 2067  N   LEU A 607     2012   2067   2743   -266     17    104       N
ATOM   2068  CA  LEU A 607      12.278 -11.531 -21.167  1.00 21.59           C
ANISOU 2068  CA  LEU A 607     2435   2564   3206   -286     33    151       C
ATOM   2069  C   LEU A 607      12.248 -12.284 -22.493  1.00 21.45           C
ANISOU 2069  C   LEU A 607     2424   2601   3123   -262     60    218       C
ATOM   2070  O   LEU A 607      12.796 -11.821 -23.489  1.00 19.97           O
ANISOU 2070  O   LEU A 607     2209   2421   2956   -279     81    287       O
ATOM   2071  CB  LEU A 607      13.292 -12.236 -20.259  1.00 21.64           C
ANISOU 2071  CB  LEU A 607     2424   2618   3182   -289     19     98       C
ATOM   2072  CG  LEU A 607      13.907 -11.453 -19.103  1.00 28.22           C
ANISOU 2072  CG  LEU A 607     3226   3418   4077   -322     -8     37       C
ATOM   2073  CD1 LEU A 607      14.184 -12.341 -17.892  1.00 30.47           C
ANISOU 2073  CD1 LEU A 607     3517   3755   4305   -304    -30    -32       C
ATOM   2074  CD2 LEU A 607      15.175 -10.771 -19.596  1.00 31.24           C
ANISOU 2074  CD2 LEU A 607     3555   3793   4522   -363      2     76       C
ATOM   2075  N   PHE A 608      11.619 -13.457 -22.494  1.00 18.20           N
ANISOU 2075  N   PHE A 608     2048   2232   2636   -223     60    196       N
ATOM   2076  CA  PHE A 608      11.820 -14.431 -23.563  1.00 13.82           C
ANISOU 2076  CA  PHE A 608     1495   1744   2012   -197     82    234       C
ATOM   2077  C   PHE A 608      10.523 -14.885 -24.224  1.00 17.87           C
ANISOU 2077  C   PHE A 608     2045   2264   2481   -164     85    246       C
ATOM   2078  O   PHE A 608      10.534 -15.819 -25.035  1.00 19.92           O
ANISOU 2078  O   PHE A 608     2309   2580   2678   -137     99    259       O
ATOM   2079  CB  PHE A 608      12.526 -15.671 -22.991  1.00 12.32           C
ANISOU 2079  CB  PHE A 608     1302   1606   1772   -179     77    190       C
ATOM   2080  CG  PHE A 608      13.852 -15.370 -22.367  1.00 13.56           C
ANISOU 2080  CG  PHE A 608     1418   1770   1963   -207     71    176       C
ATOM   2081  CD1 PHE A 608      14.852 -14.777 -23.121  1.00 15.00           C
ANISOU 2081  CD1 PHE A 608     1559   1966   2176   -234     91    227       C
ATOM   2082  CD2 PHE A 608      14.108 -15.687 -21.035  1.00 15.24           C
ANISOU 2082  CD2 PHE A 608     1632   1982   2176   -208     46    115       C
ATOM   2083  CE1 PHE A 608      16.095 -14.504 -22.554  1.00 18.84           C
ANISOU 2083  CE1 PHE A 608     2001   2458   2698   -262     84    212       C
ATOM   2084  CE2 PHE A 608      15.341 -15.408 -20.465  1.00 18.12           C
ANISOU 2084  CE2 PHE A 608     1955   2359   2571   -233     37     99       C
ATOM   2085  CZ  PHE A 608      16.332 -14.818 -21.230  1.00 17.63           C
ANISOU 2085  CZ  PHE A 608     1850   2305   2546   -262     55    145       C
ATOM   2086  N   GLY A 609       9.428 -14.207 -23.896  1.00 17.17           N
ANISOU 2086  N   GLY A 609     1978   2119   2428   -165     72    237       N
ATOM   2087  CA  GLY A 609       8.098 -14.606 -24.343  1.00 16.03           C
ANISOU 2087  CA  GLY A 609     1867   1976   2249   -134     70    239       C
ATOM   2088  C   GLY A 609       7.704 -14.148 -25.739  1.00 23.88           C
ANISOU 2088  C   GLY A 609     2855   2983   3235   -128     84    312       C
ATOM   2089  O   GLY A 609       8.540 -13.959 -26.623  1.00 19.54           O
ANISOU 2089  O   GLY A 609     2278   2470   2675   -138    103    367       O
ATOM   2090  N   SER A 610       6.407 -13.966 -25.945  1.00 21.59           N
ANISOU 2090  N   SER A 610     2588   2669   2945   -111     75    316       N
ATOM   2091  CA  SER A 610       5.889 -13.833 -27.301  1.00 29.77           C
ANISOU 2091  CA  SER A 610     3622   3737   3950    -94     84    380       C
ATOM   2092  C   SER A 610       6.186 -12.481 -27.959  1.00 35.10           C
ANISOU 2092  C   SER A 610     4270   4383   4682   -117     94    463       C
ATOM   2093  O   SER A 610       5.945 -12.307 -29.155  1.00 38.68           O
ANISOU 2093  O   SER A 610     4715   4877   5104   -105    104    531       O
ATOM   2094  CB  SER A 610       4.385 -14.137 -27.326  1.00 34.29           C
ANISOU 2094  CB  SER A 610     4224   4299   4505    -66     68    358       C
ATOM   2095  OG  SER A 610       3.683 -13.198 -26.536  1.00 37.50           O
ANISOU 2095  OG  SER A 610     4638   4626   4984    -76     54    344       O
ATOM   2096  N   ASN A 611       6.718 -11.549 -27.195  1.00 32.95           N
ANISOU 2096  N   ASN A 611     3981   4045   4493   -151     90    459       N
ATOM   2097  CA  ASN A 611       7.051 -10.241 -27.734  1.00 41.50           C
ANISOU 2097  CA  ASN A 611     5033   5085   5648   -177    100    541       C
ATOM   2098  C   ASN A 611       8.497 -10.082 -28.163  1.00 39.78           C
ANISOU 2098  C   ASN A 611     4776   4902   5436   -205    123    588       C
ATOM   2099  O   ASN A 611       8.916  -9.031 -28.537  1.00 44.06           O
ANISOU 2099  O   ASN A 611     5286   5406   6049   -234    134    659       O
ATOM   2100  CB  ASN A 611       6.612  -9.088 -26.816  1.00 20.00           C
ATOM   2101  CG  ASN A 611       7.693  -8.597 -25.878  1.00 20.00           C
ATOM   2102  OD1 ASN A 611       7.571  -7.520 -25.324  1.00 20.00           O
ATOM   2103  ND2 ASN A 611       8.717  -9.386 -25.661  1.00 20.00           N
ATOM   2104  N   VAL A 612       9.255 -11.144 -28.111  1.00 24.99           N
ANISOU 2104  N   VAL A 612     2901   3098   3495   -198    132    550       N
ATOM   2105  CA  VAL A 612      10.633 -11.105 -28.584  1.00 27.98           C
ANISOU 2105  CA  VAL A 612     3238   3522   3870   -220    156    593       C
ATOM   2106  C   VAL A 612      10.607 -10.878 -30.089  1.00 37.69           C
ANISOU 2106  C   VAL A 612     4450   4811   5059   -209    182    694       C
ATOM   2107  O   VAL A 612       9.974 -11.636 -30.826  1.00 37.20           O
ANISOU 2107  O   VAL A 612     4408   4814   4911   -172    185    696       O
ATOM   2108  CB  VAL A 612      11.391 -12.405 -28.271  1.00 26.56           C
ANISOU 2108  CB  VAL A 612     3060   3410   3622   -205    160    532       C
ATOM   2109  CG1 VAL A 612      12.735 -12.420 -28.982  1.00 37.58           C
ANISOU 2109  CG1 VAL A 612     4410   4866   5002   -221    190    583       C
ATOM   2110  CG2 VAL A 612      11.586 -12.551 -26.769  1.00 26.87           C
ANISOU 2110  CG2 VAL A 612     3109   3401   3700   -218    135    445       C
ATOM   2111  N   THR A 613      11.291  -9.832 -30.544  1.00 41.09           N
ANISOU 2111  N   THR A 613     4840   5221   5552   -243    201    778       N
ATOM   2112  CA  THR A 613      11.188  -9.410 -31.939  1.00 42.65           C
ANISOU 2112  CA  THR A 613     5016   5470   5719   -235    226    891       C
ATOM   2113  C   THR A 613      11.920 -10.332 -32.918  1.00 45.08           C
ANISOU 2113  C   THR A 613     5305   5906   5917   -214    257    914       C
ATOM   2114  O   THR A 613      11.465 -10.527 -34.044  1.00 55.12           O
ANISOU 2114  O   THR A 613     6578   7254   7113   -185    269    968       O
ATOM   2115  CB  THR A 613      11.653  -7.944 -32.130  1.00 49.55           C
ANISOU 2115  CB  THR A 613     5847   6275   6706   -279    240    988       C
ATOM   2116  OG1 THR A 613      13.040  -7.827 -31.790  1.00 47.64           O
ANISOU 2116  OG1 THR A 613     5563   6034   6504   -317    256    985       O
ATOM   2117  CG2 THR A 613      10.840  -7.005 -31.245  1.00 54.74           C
ANISOU 2117  CG2 THR A 613     6520   6803   7474   -294    209    961       C
ATOM   2118  N   ASP A 614      13.044 -10.901 -32.492  1.00 37.05           N
ANISOU 2118  N   ASP A 614     4268   4917   4891   -226    267    868       N
ATOM   2119  CA  ASP A 614      13.823 -11.779 -33.365  1.00 43.55           C
ANISOU 2119  CA  ASP A 614     5068   5860   5618   -205    298    879       C
ATOM   2120  C   ASP A 614      14.250 -13.069 -32.671  1.00 38.15           C
ANISOU 2120  C   ASP A 614     4400   5206   4891   -186    288    771       C
ATOM   2121  O   ASP A 614      15.219 -13.080 -31.908  1.00 37.73           O
ANISOU 2121  O   ASP A 614     4324   5129   4884   -211    288    739       O
ATOM   2122  CB  ASP A 614      15.060 -11.049 -33.896  1.00 53.69           C
ANISOU 2122  CB  ASP A 614     6292   7171   6938   -242    335    970       C
ATOM   2123  CG  ASP A 614      15.863 -11.893 -34.870  1.00 64.41           C
ANISOU 2123  CG  ASP A 614     7619   8662   8192   -217    372    985       C
ATOM   2124  OD1 ASP A 614      15.289 -12.835 -35.459  1.00 64.76           O
ANISOU 2124  OD1 ASP A 614     7689   8783   8135   -170    371    950       O
ATOM   2125  OD2 ASP A 614      17.067 -11.611 -35.052  1.00 71.13           O
ANISOU 2125  OD2 ASP A 614     8418   9542   9067   -245    402   1029       O
ATOM   2126  N   CYS A 615      13.539 -14.157 -32.951  1.00 30.94           N
ANISOU 2126  N   CYS A 615     3520   4343   3894   -140    279    716       N
ATOM   2127  CA  CYS A 615      13.837 -15.438 -32.318  1.00 29.75           C
ANISOU 2127  CA  CYS A 615     3384   4211   3708   -118    268    617       C
ATOM   2128  C   CYS A 615      14.912 -16.238 -33.038  1.00 33.87           C
ANISOU 2128  C   CYS A 615     3869   4834   4164   -100    300    615       C
ATOM   2129  O   CYS A 615      15.282 -17.326 -32.596  1.00 33.87           O
ANISOU 2129  O   CYS A 615     3874   4853   4141    -78    294    540       O
ATOM   2130  CB  CYS A 615      12.575 -16.287 -32.183  1.00 35.22           C
ANISOU 2130  CB  CYS A 615     4126   4898   4358    -80    242    552       C
ATOM   2131  SG  CYS A 615      11.429 -15.648 -30.964  1.00 39.60           S
ANISOU 2131  SG  CYS A 615     4722   5333   4991    -97    204    523       S
ATOM   2132  N   SER A 616      15.417 -15.708 -34.144  1.00 34.51           N
ANISOU 2132  N   SER A 616     3911   4983   4217   -106    335    700       N
ATOM   2133  CA  SER A 616      16.469 -16.399 -34.872  1.00 29.72           C
ANISOU 2133  CA  SER A 616     3264   4481   3546    -88    369    699       C
ATOM   2134  C   SER A 616      17.786 -16.353 -34.093  1.00 27.65           C
ANISOU 2134  C   SER A 616     2965   4197   3344   -117    378    684       C
ATOM   2135  O   SER A 616      18.388 -15.288 -33.931  1.00 32.36           O
ANISOU 2135  O   SER A 616     3528   4758   4011   -163    389    749       O
ATOM   2136  CB  SER A 616      16.651 -15.787 -36.263  1.00 40.90           C
ANISOU 2136  CB  SER A 616     4644   5986   4912    -87    408    803       C
ATOM   2137  OG  SER A 616      17.758 -16.369 -36.929  1.00 43.35           O
ANISOU 2137  OG  SER A 616     4907   6401   5162    -72    446    803       O
ATOM   2138  N   GLY A 617      18.233 -17.505 -33.608  1.00 22.56           N
ANISOU 2138  N   GLY A 617     2324   3572   2678    -92    370    599       N
ATOM   2139  CA  GLY A 617      19.464 -17.557 -32.837  1.00 23.88           C
ANISOU 2139  CA  GLY A 617     2454   3723   2896   -115    373    579       C
ATOM   2140  C   GLY A 617      19.279 -17.156 -31.380  1.00 28.41           C
ANISOU 2140  C   GLY A 617     3051   4190   3555   -145    333    542       C
ATOM   2141  O   GLY A 617      20.073 -17.532 -30.526  1.00 33.77           O
ANISOU 2141  O   GLY A 617     3712   4855   4263   -152    322    498       O
ATOM   2142  N   ASN A 618      18.228 -16.397 -31.093  1.00 23.28           N
ANISOU 2142  N   ASN A 618     2437   3467   2940   -161    311    559       N
ATOM   2143  CA  ASN A 618      17.953 -15.976 -29.714  1.00 20.26           C
ANISOU 2143  CA  ASN A 618     2077   2989   2633   -187    273    516       C
ATOM   2144  C   ASN A 618      17.046 -16.962 -29.012  1.00 25.10           C
ANISOU 2144  C   ASN A 618     2742   3579   3215   -152    243    436       C
ATOM   2145  O   ASN A 618      16.282 -17.679 -29.657  1.00 28.66           O
ANISOU 2145  O   ASN A 618     3221   4065   3604   -115    246    423       O
ATOM   2146  CB  ASN A 618      17.322 -14.589 -29.694  1.00 23.53           C
ANISOU 2146  CB  ASN A 618     2498   3330   3115   -223    266    571       C
ATOM   2147  CG  ASN A 618      18.283 -13.519 -30.156  1.00 35.28           C
ANISOU 2147  CG  ASN A 618     3928   4818   4659   -267    293    653       C
ATOM   2148  OD1 ASN A 618      19.224 -13.175 -29.445  1.00 31.51           O
ANISOU 2148  OD1 ASN A 618     3415   4312   4244   -301    287    638       O
ATOM   2149  ND2 ASN A 618      18.063 -12.996 -31.358  1.00 41.25           N
ANISOU 2149  ND2 ASN A 618     4670   5610   5394   -267    322    743       N
ATOM   2150  N   PHE A 619      17.134 -17.012 -27.689  1.00 18.16           N
ANISOU 2150  N   PHE A 619     1874   2645   2380   -165    213    383       N
ATOM   2151  CA  PHE A 619      16.260 -17.899 -26.951  1.00 16.24           C
ANISOU 2151  CA  PHE A 619     1677   2380   2113   -134    186    317       C
ATOM   2152  C   PHE A 619      14.844 -17.353 -26.867  1.00 18.02           C
ANISOU 2152  C   PHE A 619     1945   2549   2351   -136    170    320       C
ATOM   2153  O   PHE A 619      14.633 -16.204 -26.481  1.00 19.42           O
ANISOU 2153  O   PHE A 619     2121   2668   2589   -169    161    340       O
ATOM   2154  CB  PHE A 619      16.777 -18.154 -25.545  1.00 17.53           C
ANISOU 2154  CB  PHE A 619     1837   2516   2309   -143    160    263       C
ATOM   2155  CG  PHE A 619      15.849 -18.985 -24.735  1.00 17.24           C
ANISOU 2155  CG  PHE A 619     1845   2455   2251   -115    135    208       C
ATOM   2156  CD1 PHE A 619      15.663 -20.321 -25.044  1.00 20.06           C
ANISOU 2156  CD1 PHE A 619     2216   2850   2557    -72    139    182       C
ATOM   2157  CD2 PHE A 619      15.130 -18.433 -23.692  1.00 13.74           C
ANISOU 2157  CD2 PHE A 619     1426   1952   1841   -131    108    182       C
ATOM   2158  CE1 PHE A 619      14.788 -21.101 -24.316  1.00 16.23           C
ANISOU 2158  CE1 PHE A 619     1768   2338   2060    -49    119    140       C
ATOM   2159  CE2 PHE A 619      14.254 -19.209 -22.949  1.00 15.41           C
ANISOU 2159  CE2 PHE A 619     1675   2148   2031   -105     90    139       C
ATOM   2160  CZ  PHE A 619      14.081 -20.551 -23.268  1.00 16.49           C
ANISOU 2160  CZ  PHE A 619     1825   2318   2121    -65     95    123       C
ATOM   2161  N   CYS A 620      13.880 -18.198 -27.222  1.00 16.63           N
ANISOU 2161  N   CYS A 620     1805   2390   2124    -99    166    297       N
ATOM   2162  CA  CYS A 620      12.461 -17.842 -27.137  1.00 15.76           C
ANISOU 2162  CA  CYS A 620     1734   2232   2021    -94    150    294       C
ATOM   2163  C   CYS A 620      11.735 -18.957 -26.408  1.00 15.54           C
ANISOU 2163  C   CYS A 620     1741   2193   1971    -65    130    229       C
ATOM   2164  O   CYS A 620      11.797 -20.113 -26.809  1.00 18.03           O
ANISOU 2164  O   CYS A 620     2059   2551   2240    -33    136    204       O
ATOM   2165  CB  CYS A 620      11.874 -17.628 -28.525  1.00 18.06           C
ANISOU 2165  CB  CYS A 620     2027   2561   2273    -80    167    345       C
ATOM   2166  SG  CYS A 620      12.462 -16.068 -29.263  1.00 29.05           S
ANISOU 2166  SG  CYS A 620     3380   3948   3709   -119    189    442       S
ATOM   2167  N   LEU A 621      11.063 -18.592 -25.326  1.00 13.86           N
ANISOU 2167  N   LEU A 621     1551   1921   1794    -76    108    202       N
ATOM   2168  CA  LEU A 621      10.465 -19.565 -24.424  1.00 15.17           C
ANISOU 2168  CA  LEU A 621     1745   2074   1947    -54     91    148       C
ATOM   2169  C   LEU A 621       9.385 -20.404 -25.094  1.00 13.62           C
ANISOU 2169  C   LEU A 621     1574   1891   1712    -22     91    137       C
ATOM   2170  O   LEU A 621       9.198 -21.574 -24.748  1.00 18.47           O
ANISOU 2170  O   LEU A 621     2199   2511   2306      2     86    100       O
ATOM   2171  CB  LEU A 621       9.885 -18.834 -23.210  1.00 17.55           C
ANISOU 2171  CB  LEU A 621     2061   2317   2290    -73     71    126       C
ATOM   2172  CG  LEU A 621       9.480 -19.669 -22.000  1.00 16.49           C
ANISOU 2172  CG  LEU A 621     1946   2173   2145    -57     54     77       C
ATOM   2173  CD1 LEU A 621      10.640 -20.554 -21.545  1.00 17.41           C
ANISOU 2173  CD1 LEU A 621     2042   2327   2246    -49     54     62       C
ATOM   2174  CD2 LEU A 621       9.019 -18.728 -20.887  1.00 20.14           C
ANISOU 2174  CD2 LEU A 621     2417   2590   2646    -78     38     54       C
ATOM   2175  N   PHE A 622       8.672 -19.809 -26.052  1.00 15.04           N
ANISOU 2175  N   PHE A 622     1760   2072   1883    -21     97    171       N
ATOM   2176  CA  PHE A 622       7.513 -20.459 -26.653  1.00 15.93           C
ANISOU 2176  CA  PHE A 622     1894   2194   1963      6     92    156       C
ATOM   2177  C   PHE A 622       7.755 -20.854 -28.111  1.00 16.70           C
ANISOU 2177  C   PHE A 622     1977   2361   2008     26    107    175       C
ATOM   2178  O   PHE A 622       6.812 -20.985 -28.892  1.00 21.65           O
ANISOU 2178  O   PHE A 622     2614   3005   2606     44    103    177       O
ATOM   2179  CB  PHE A 622       6.263 -19.565 -26.517  1.00 15.18           C
ANISOU 2179  CB  PHE A 622     1820   2052   1896     -2     79    170       C
ATOM   2180  CG  PHE A 622       5.988 -19.117 -25.107  1.00 14.83           C
ANISOU 2180  CG  PHE A 622     1787   1948   1898    -19     65    145       C
ATOM   2181  CD1 PHE A 622       5.729 -17.779 -24.831  1.00 16.55           C
ANISOU 2181  CD1 PHE A 622     2004   2119   2165    -42     61    168       C
ATOM   2182  CD2 PHE A 622       5.964 -20.032 -24.057  1.00 15.42           C
ANISOU 2182  CD2 PHE A 622     1873   2015   1969     -9     57     98       C
ATOM   2183  CE1 PHE A 622       5.479 -17.362 -23.533  1.00 16.76           C
ANISOU 2183  CE1 PHE A 622     2038   2098   2231    -54     48    133       C
ATOM   2184  CE2 PHE A 622       5.711 -19.624 -22.760  1.00 15.63           C
ANISOU 2184  CE2 PHE A 622     1908   2002   2028    -22     46     73       C
ATOM   2185  CZ  PHE A 622       5.469 -18.280 -22.494  1.00 20.35           C
ANISOU 2185  CZ  PHE A 622     2504   2559   2669    -44     41     85       C
ATOM   2186  N   ARG A 623       9.026 -21.036 -28.471  1.00 14.01           N
ANISOU 2186  N   ARG A 623     1606   2065   1650     25    126    186       N
ATOM   2187  CA  ARG A 623       9.399 -21.619 -29.760  1.00 14.14           C
ANISOU 2187  CA  ARG A 623     1604   2160   1608     49    144    189       C
ATOM   2188  C   ARG A 623      10.218 -22.884 -29.516  1.00 19.81           C
ANISOU 2188  C   ARG A 623     2309   2902   2315     71    149    138       C
ATOM   2189  O   ARG A 623      10.859 -23.023 -28.473  1.00 19.50           O
ANISOU 2189  O   ARG A 623     2266   2832   2312     60    144    124       O
ATOM   2190  CB  ARG A 623      10.220 -20.633 -30.588  1.00 23.32           C
ANISOU 2190  CB  ARG A 623     2734   3366   2761     31    169    258       C
ATOM   2191  CG  ARG A 623       9.583 -19.262 -30.730  1.00 29.33           C
ANISOU 2191  CG  ARG A 623     3501   4090   3552      7    164    321       C
ATOM   2192  CD  ARG A 623       8.547 -19.224 -31.841  1.00 43.29           C
ANISOU 2192  CD  ARG A 623     5280   5898   5272     29    161    343       C
ATOM   2193  NE  ARG A 623       8.182 -17.849 -32.178  1.00 51.36           N
ANISOU 2193  NE  ARG A 623     6297   6896   6323      8    163    422       N
ATOM   2194  CZ  ARG A 623       8.734 -17.141 -33.160  1.00 57.32           C
ANISOU 2194  CZ  ARG A 623     7020   7702   7057      0    186    500       C
ATOM   2195  NH1 ARG A 623       9.682 -17.674 -33.921  1.00 51.66           N
ANISOU 2195  NH1 ARG A 623     6274   7072   6283     12    212    506       N
ATOM   2196  NH2 ARG A 623       8.335 -15.895 -33.384  1.00 61.04           N
ANISOU 2196  NH2 ARG A 623     7486   8137   7568    -19    185    577       N
ATOM   2197  N   SER A 624      10.195 -23.802 -30.479  1.00 20.16           N
ANISOU 2197  N   SER A 624     2346   3005   2311    104    157    107       N
ATOM   2198  CA  SER A 624      10.835 -25.105 -30.313  1.00 22.49           C
ANISOU 2198  CA  SER A 624     2628   3314   2603    131    161     51       C
ATOM   2199  C   SER A 624      11.570 -25.530 -31.580  1.00 26.45           C
ANISOU 2199  C   SER A 624     3095   3905   3048    156    185     42       C
ATOM   2200  O   SER A 624      11.080 -25.324 -32.689  1.00 22.32           O
ANISOU 2200  O   SER A 624     2570   3436   2474    167    192     52       O
ATOM   2201  CB  SER A 624       9.791 -26.174 -29.953  1.00 18.98           C
ANISOU 2201  CB  SER A 624     2210   2829   2172    153    138     -8       C
ATOM   2202  OG  SER A 624       9.164 -25.899 -28.704  1.00 19.42           O
ANISOU 2202  OG  SER A 624     2294   2811   2276    133    119     -1       O
ATOM   2203  N   GLU A 625      12.740 -26.135 -31.405  1.00 24.88           N
ANISOU 2203  N   GLU A 625     2869   3728   2857    168    199     21       N
ATOM   2204  CA  GLU A 625      13.507 -26.664 -32.532  1.00 27.28           C
ANISOU 2204  CA  GLU A 625     3136   4119   3109    197    226      0       C
ATOM   2205  C   GLU A 625      12.709 -27.770 -33.221  1.00 29.95           C
ANISOU 2205  C   GLU A 625     3484   4478   3417    237    215    -72       C
ATOM   2206  O   GLU A 625      12.732 -27.897 -34.445  1.00 30.52           O
ANISOU 2206  O   GLU A 625     3537   4634   3426    259    231    -87       O
ATOM   2207  CB  GLU A 625      14.871 -27.181 -32.056  1.00 34.83           C
ANISOU 2207  CB  GLU A 625     4059   5084   4092    204    239    -14       C
ATOM   2208  CG  GLU A 625      15.830 -27.543 -33.176  1.00 56.83           C
ANISOU 2208  CG  GLU A 625     6799   7967   6826    232    273    -28       C
ATOM   2209  CD  GLU A 625      15.919 -29.041 -33.407  1.00 75.32           C
ANISOU 2209  CD  GLU A 625     9132  10319   9168    281    270   -117       C
ATOM   2210  OE1 GLU A 625      16.073 -29.789 -32.416  1.00 80.75           O
ANISOU 2210  OE1 GLU A 625     9826  10941   9915    289    252   -148       O
ATOM   2211  OE2 GLU A 625      15.833 -29.468 -34.580  1.00 79.26           O
ANISOU 2211  OE2 GLU A 625     9614  10894   9609    312    285   -156       O
ATOM   2212  N   THR A 626      12.001 -28.571 -32.431  1.00 24.29           N
ANISOU 2212  N   THR A 626     2794   3688   2747    245    189   -119       N
ATOM   2213  CA  THR A 626      11.036 -29.512 -32.992  1.00 24.04           C
ANISOU 2213  CA  THR A 626     2774   3658   2703    275    173   -187       C
ATOM   2214  C   THR A 626       9.613 -28.994 -32.802  1.00 28.55           C
ANISOU 2214  C   THR A 626     3381   4186   3280    256    149   -169       C
ATOM   2215  O   THR A 626       9.153 -28.134 -33.559  1.00 27.93           O
ANISOU 2215  O   THR A 626     3306   4152   3155    247    152   -132       O
ATOM   2216  CB  THR A 626      11.195 -30.929 -32.421  1.00 31.18           C
ANISOU 2216  CB  THR A 626     3675   4512   3662    301    163   -256       C
ATOM   2217  OG1 THR A 626      11.048 -30.900 -30.997  1.00 29.76           O
ANISOU 2217  OG1 THR A 626     3517   4245   3546    280    147   -229       O
ATOM   2218  CG2 THR A 626      12.580 -31.481 -32.761  1.00 36.01           C
ANISOU 2218  CG2 THR A 626     4245   5174   4266    327    187   -280       C
ATOM   2219  N   LYS A 627       8.920 -29.502 -31.791  1.00 24.49           N
ANISOU 2219  N   LYS A 627     2892   3587   2825    251    127   -190       N
ATOM   2220  CA  LYS A 627       7.536 -29.109 -31.571  1.00 25.05           C
ANISOU 2220  CA  LYS A 627     2994   3618   2907    236    105   -179       C
ATOM   2221  C   LYS A 627       7.138 -29.160 -30.096  1.00 23.70           C
ANISOU 2221  C   LYS A 627     2846   3357   2801    216     91   -166       C
ATOM   2222  O   LYS A 627       7.393 -30.148 -29.411  1.00 22.24           O
ANISOU 2222  O   LYS A 627     2659   3132   2659    228     87   -196       O
ATOM   2223  CB  LYS A 627       6.620 -30.011 -32.399  1.00 32.70           C
ANISOU 2223  CB  LYS A 627     3961   4603   3860    263     89   -248       C
ATOM   2224  CG  LYS A 627       5.150 -29.900 -32.077  1.00 45.97           C
ANISOU 2224  CG  LYS A 627     5668   6233   5565    251     64   -250       C
ATOM   2225  CD  LYS A 627       4.329 -30.758 -33.029  1.00 56.62           C
ANISOU 2225  CD  LYS A 627     7008   7609   6896    277     47   -324       C
ATOM   2226  CE  LYS A 627       2.846 -30.442 -32.916  1.00 62.68           C
ANISOU 2226  CE  LYS A 627     7795   8344   7677    264     22   -318       C
ATOM   2227  NZ  LYS A 627       2.566 -28.999 -33.177  1.00 65.05           N
ANISOU 2227  NZ  LYS A 627     8105   8674   7936    246     25   -244       N
ATOM   2228  N   ASP A 628       6.534 -28.075 -29.615  1.00 19.41           N
ANISOU 2228  N   ASP A 628     2325   2786   2266    188     84   -118       N
ATOM   2229  CA  ASP A 628       5.898 -28.049 -28.301  1.00 18.49           C
ANISOU 2229  CA  ASP A 628     2231   2596   2199    171     70   -109       C
ATOM   2230  C   ASP A 628       6.814 -28.519 -27.174  1.00 18.37           C
ANISOU 2230  C   ASP A 628     2210   2552   2219    170     74   -107       C
ATOM   2231  O   ASP A 628       6.399 -29.301 -26.315  1.00 17.98           O
ANISOU 2231  O   ASP A 628     2169   2454   2207    175     64   -124       O
ATOM   2232  CB  ASP A 628       4.615 -28.898 -28.327  1.00 21.02           C
ANISOU 2232  CB  ASP A 628     2564   2883   2540    184     53   -152       C
ATOM   2233  CG  ASP A 628       3.597 -28.391 -29.336  1.00 27.14           C
ANISOU 2233  CG  ASP A 628     3344   3687   3281    186     43   -153       C
ATOM   2234  OD1 ASP A 628       3.608 -27.184 -29.670  1.00 23.21           O
ANISOU 2234  OD1 ASP A 628     2849   3214   2756    171     48   -105       O
ATOM   2235  OD2 ASP A 628       2.770 -29.206 -29.798  1.00 31.72           O
ANISOU 2235  OD2 ASP A 628     3922   4265   3866    202     29   -201       O
ATOM   2236  N   LEU A 629       8.058 -28.042 -27.168  1.00 16.58           N
ANISOU 2236  N   LEU A 629     1964   2357   1980    162     88    -82       N
ATOM   2237  CA  LEU A 629       8.998 -28.392 -26.101  1.00 15.81           C
ANISOU 2237  CA  LEU A 629     1856   2241   1912    161     88    -77       C
ATOM   2238  C   LEU A 629       8.794 -27.492 -24.875  1.00 15.86           C
ANISOU 2238  C   LEU A 629     1877   2210   1939    131     79    -44       C
ATOM   2239  O   LEU A 629       8.880 -26.275 -24.987  1.00 14.08           O
ANISOU 2239  O   LEU A 629     1653   1993   1705    106     82    -14       O
ATOM   2240  CB  LEU A 629      10.445 -28.285 -26.601  1.00 15.66           C
ANISOU 2240  CB  LEU A 629     1803   2274   1874    165    106    -68       C
ATOM   2241  CG  LEU A 629      10.753 -29.149 -27.831  1.00 19.34           C
ANISOU 2241  CG  LEU A 629     2247   2787   2313    199    119   -107       C
ATOM   2242  CD1 LEU A 629      12.133 -28.844 -28.401  1.00 19.12           C
ANISOU 2242  CD1 LEU A 629     2183   2822   2260    201    142    -92       C
ATOM   2243  CD2 LEU A 629      10.627 -30.639 -27.473  1.00 20.04           C
ANISOU 2243  CD2 LEU A 629     2334   2840   2440    230    110   -156       C
ATOM   2244  N   LEU A 630       8.536 -28.116 -23.725  1.00 14.40           N
ANISOU 2244  N   LEU A 630     1702   1987   1782    135     67    -51       N
ATOM   2245  CA  LEU A 630       8.273 -27.447 -22.446  1.00 14.02           C
ANISOU 2245  CA  LEU A 630     1667   1912   1748    113     57    -32       C
ATOM   2246  C   LEU A 630       6.890 -26.774 -22.404  1.00 13.91           C
ANISOU 2246  C   LEU A 630     1680   1871   1736     99     51    -29       C
ATOM   2247  O   LEU A 630       6.135 -26.960 -21.439  1.00 16.95           O
ANISOU 2247  O   LEU A 630     2079   2226   2136     97     43    -31       O
ATOM   2248  CB  LEU A 630       9.370 -26.440 -22.085  1.00 13.52           C
ANISOU 2248  CB  LEU A 630     1586   1870   1680     90     59    -10       C
ATOM   2249  CG  LEU A 630      10.800 -26.976 -22.022  1.00 15.45           C
ANISOU 2249  CG  LEU A 630     1800   2147   1926    101     63    -10       C
ATOM   2250  CD1 LEU A 630      11.731 -25.846 -21.612  1.00 16.82           C
ANISOU 2250  CD1 LEU A 630     1954   2336   2101     72     62      9       C
ATOM   2251  CD2 LEU A 630      10.900 -28.123 -21.037  1.00 18.12           C
ANISOU 2251  CD2 LEU A 630     2135   2469   2280    123     53    -17       C
ATOM   2252  N   PHE A 631       6.571 -26.000 -23.442  1.00 12.82           N
ANISOU 2252  N   PHE A 631     1544   1745   1581     91     56    -21       N
ATOM   2253  CA  PHE A 631       5.271 -25.342 -23.582  1.00 14.97           C
ANISOU 2253  CA  PHE A 631     1836   1994   1857     83     50    -17       C
ATOM   2254  C   PHE A 631       4.756 -25.592 -24.993  1.00 18.02           C
ANISOU 2254  C   PHE A 631     2222   2406   2221     98     52    -25       C
ATOM   2255  O   PHE A 631       5.548 -25.836 -25.893  1.00 15.68           O
ANISOU 2255  O   PHE A 631     1908   2151   1899    108     61    -27       O
ATOM   2256  CB  PHE A 631       5.427 -23.823 -23.391  1.00 15.30           C
ANISOU 2256  CB  PHE A 631     1878   2028   1907     55     50     11       C
ATOM   2257  CG  PHE A 631       6.020 -23.448 -22.072  1.00 12.88           C
ANISOU 2257  CG  PHE A 631     1568   1707   1619     39     45     10       C
ATOM   2258  CD1 PHE A 631       5.238 -23.467 -20.921  1.00 11.51           C
ANISOU 2258  CD1 PHE A 631     1410   1506   1459     37     36     -5       C
ATOM   2259  CD2 PHE A 631       7.360 -23.122 -21.969  1.00 13.84           C
ANISOU 2259  CD2 PHE A 631     1667   1850   1741     27     49     21       C
ATOM   2260  CE1 PHE A 631       5.774 -23.147 -19.696  1.00 14.94           C
ANISOU 2260  CE1 PHE A 631     1837   1938   1899     25     30    -12       C
ATOM   2261  CE2 PHE A 631       7.913 -22.813 -20.741  1.00 14.51           C
ANISOU 2261  CE2 PHE A 631     1744   1929   1839     13     40     12       C
ATOM   2262  CZ  PHE A 631       7.122 -22.821 -19.605  1.00 14.93           C
ANISOU 2262  CZ  PHE A 631     1814   1959   1898     13     29     -5       C
ATOM   2263  N   ARG A 632       3.444 -25.509 -25.203  1.00 16.12           N
ANISOU 2263  N   ARG A 632     1996   2145   1983    100     42    -32       N
ATOM   2264  CA  ARG A 632       2.936 -25.515 -26.575  1.00 20.13           C
ANISOU 2264  CA  ARG A 632     2500   2687   2462    113     40    -37       C
ATOM   2265  C   ARG A 632       3.486 -24.310 -27.338  1.00 16.40           C
ANISOU 2265  C   ARG A 632     2017   2248   1964    102     49      7       C
ATOM   2266  O   ARG A 632       3.558 -23.202 -26.798  1.00 18.50           O
ANISOU 2266  O   ARG A 632     2288   2489   2253     79     50     41       O
ATOM   2267  CB  ARG A 632       1.406 -25.476 -26.595  1.00 21.59           C
ANISOU 2267  CB  ARG A 632     2699   2845   2659    116     25    -48       C
ATOM   2268  CG  ARG A 632       0.757 -26.792 -26.232  1.00 29.74           C
ANISOU 2268  CG  ARG A 632     3732   3851   3715    129     18    -90       C
ATOM   2269  CD  ARG A 632      -0.065 -27.340 -27.386  1.00 51.82           C
ANISOU 2269  CD  ARG A 632     6522   6671   6495    146      5   -123       C
ATOM   2270  NE  ARG A 632      -1.496 -27.364 -27.090  1.00 61.39           N
ANISOU 2270  NE  ARG A 632     7742   7849   7734    143     -9   -132       N
ATOM   2271  CZ  ARG A 632      -2.375 -26.471 -27.537  1.00 67.01           C
ANISOU 2271  CZ  ARG A 632     8457   8569   8434    140    -18   -113       C
ATOM   2272  NH1 ARG A 632      -1.982 -25.468 -28.311  1.00 61.65           N
ANISOU 2272  NH1 ARG A 632     7776   7929   7719    139    -16    -78       N
ATOM   2273  NH2 ARG A 632      -3.657 -26.584 -27.212  1.00 71.51           N
ANISOU 2273  NH2 ARG A 632     9029   9107   9032    138    -30   -125       N
ATOM   2274  N   ASP A 633       3.846 -24.515 -28.603  1.00 17.42           N
ANISOU 2274  N   ASP A 633     2131   2437   2051    117     56      8       N
ATOM   2275  CA  ASP A 633       4.387 -23.422 -29.408  1.00 20.64           C
ANISOU 2275  CA  ASP A 633     2524   2884   2433    107     69     62       C
ATOM   2276  C   ASP A 633       3.337 -22.332 -29.654  1.00 22.70           C
ANISOU 2276  C   ASP A 633     2796   3127   2702     97     58    101       C
ATOM   2277  O   ASP A 633       3.671 -21.199 -30.001  1.00 23.59           O
ANISOU 2277  O   ASP A 633     2898   3246   2817     82     67    159       O
ATOM   2278  CB  ASP A 633       4.954 -23.950 -30.732  1.00 27.42           C
ANISOU 2278  CB  ASP A 633     3361   3825   3233    129     81     53       C
ATOM   2279  CG  ASP A 633       6.187 -24.819 -30.533  1.00 27.32           C
ANISOU 2279  CG  ASP A 633     3330   3831   3218    139     96     23       C
ATOM   2280  OD1 ASP A 633       6.401 -25.756 -31.339  1.00 26.18           O
ANISOU 2280  OD1 ASP A 633     3171   3738   3038    166    100    -19       O
ATOM   2281  OD2 ASP A 633       6.944 -24.571 -29.567  1.00 26.79           O
ANISOU 2281  OD2 ASP A 633     3261   3731   3187    120    101     37       O
ATOM   2282  N   ASP A 634       2.072 -22.687 -29.448  1.00 20.31           N
ANISOU 2282  N   ASP A 634     2510   2796   2412    107     40     72       N
ATOM   2283  CA  ASP A 634       0.952 -21.755 -29.593  1.00 22.51           C
ANISOU 2283  CA  ASP A 634     2797   3052   2704    102     27    103       C
ATOM   2284  C   ASP A 634       0.815 -20.813 -28.406  1.00 20.71           C
ANISOU 2284  C   ASP A 634     2580   2754   2534     79     27    121       C
ATOM   2285  O   ASP A 634       0.003 -19.893 -28.427  1.00 16.18           O
ANISOU 2285  O   ASP A 634     2010   2152   1984     75     18    149       O
ATOM   2286  CB  ASP A 634      -0.363 -22.532 -29.721  1.00 31.58           C
ANISOU 2286  CB  ASP A 634     3953   4194   3850    120      7     59       C
ATOM   2287  CG  ASP A 634      -0.591 -23.068 -31.111  1.00 52.06           C
ANISOU 2287  CG  ASP A 634     6534   6861   6386    145      0     44       C
ATOM   2288  OD1 ASP A 634      -0.032 -22.495 -32.069  1.00 53.03           O
ANISOU 2288  OD1 ASP A 634     6642   7042   6466    149      9     87       O
ATOM   2289  OD2 ASP A 634      -1.341 -24.059 -31.246  1.00 65.83           O
ANISOU 2289  OD2 ASP A 634     8278   8607   8128    160    -16    -11       O
ATOM   2290  N   THR A 635       1.572 -21.064 -27.347  1.00 17.93           N
ANISOU 2290  N   THR A 635     2230   2376   2205     66     34    101       N
ATOM   2291  CA  THR A 635       1.454 -20.258 -26.140  1.00 14.49           C
ANISOU 2291  CA  THR A 635     1804   1883   1820     46     31    103       C
ATOM   2292  C   THR A 635       1.834 -18.799 -26.378  1.00 17.06           C
ANISOU 2292  C   THR A 635     2118   2192   2173     26     36    154       C
ATOM   2293  O   THR A 635       2.904 -18.512 -26.914  1.00 17.79           O
ANISOU 2293  O   THR A 635     2192   2312   2254     16     49    186       O
ATOM   2294  CB  THR A 635       2.334 -20.835 -25.027  1.00 14.72           C
ANISOU 2294  CB  THR A 635     1832   1903   1858     38     36     74       C
ATOM   2295  OG1 THR A 635       1.954 -22.197 -24.795  1.00 15.98           O
ANISOU 2295  OG1 THR A 635     1999   2070   2003     56     33     35       O
ATOM   2296  CG2 THR A 635       2.167 -20.041 -23.742  1.00 14.98           C
ANISOU 2296  CG2 THR A 635     1871   1888   1932     19     32     65       C
ATOM   2297  N   VAL A 636       0.954 -17.885 -25.972  1.00 15.04           N
ANISOU 2297  N   VAL A 636     1870   1887   1959     20     27    162       N
ATOM   2298  CA  VAL A 636       1.210 -16.454 -26.071  1.00 17.32           C
ANISOU 2298  CA  VAL A 636     2146   2140   2294      0     29    208       C
ATOM   2299  C   VAL A 636       1.768 -15.921 -24.758  1.00 18.92           C
ANISOU 2299  C   VAL A 636     2348   2297   2546    -24     29    178       C
ATOM   2300  O   VAL A 636       2.661 -15.075 -24.753  1.00 19.17           O
ANISOU 2300  O   VAL A 636     2360   2311   2611    -47     35    205       O
ATOM   2301  CB  VAL A 636      -0.086 -15.684 -26.416  1.00 20.71           C
ANISOU 2301  CB  VAL A 636     2579   2538   2751     10     18    231       C
ATOM   2302  CG1 VAL A 636       0.146 -14.194 -26.318  1.00 27.72           C
ANISOU 2302  CG1 VAL A 636     3454   3372   3707    -10     19    273       C
ATOM   2303  CG2 VAL A 636      -0.579 -16.074 -27.814  1.00 25.38           C
ANISOU 2303  CG2 VAL A 636     3167   3186   3290     33     14    265       C
ATOM   2304  N   CYS A 637       1.239 -16.418 -23.644  1.00 15.03           N
ANISOU 2304  N   CYS A 637     1870   1787   2056    -18     22    124       N
ATOM   2305  CA  CYS A 637       1.747 -16.053 -22.326  1.00 16.49           C
ANISOU 2305  CA  CYS A 637     2051   1943   2272    -36     20     86       C
ATOM   2306  C   CYS A 637       1.282 -17.074 -21.297  1.00 15.63           C
ANISOU 2306  C   CYS A 637     1957   1846   2136    -22     17     35       C
ATOM   2307  O   CYS A 637       0.433 -17.919 -21.590  1.00 16.62           O
ANISOU 2307  O   CYS A 637     2094   1986   2235     -2     17     31       O
ATOM   2308  CB  CYS A 637       1.261 -14.664 -21.921  1.00 21.67           C
ANISOU 2308  CB  CYS A 637     2701   2537   2994    -48     13     84       C
ATOM   2309  SG  CYS A 637      -0.391 -14.659 -21.217  1.00 24.97           S
ANISOU 2309  SG  CYS A 637     3136   2925   3424    -27      6     44       S
ATOM   2310  N   LEU A 638       1.851 -16.999 -20.100  1.00 14.87           N
ANISOU 2310  N   LEU A 638     1856   1746   2047    -34     14      0       N
ATOM   2311  CA  LEU A 638       1.419 -17.831 -18.986  1.00 14.86           C
ANISOU 2311  CA  LEU A 638     1866   1760   2022    -22     13    -39       C
ATOM   2312  C   LEU A 638       0.634 -16.952 -18.040  1.00 12.75           C
ANISOU 2312  C   LEU A 638     1599   1459   1785    -25      8    -74       C
ATOM   2313  O   LEU A 638       1.147 -15.948 -17.552  1.00 15.57           O
ANISOU 2313  O   LEU A 638     1945   1794   2178    -43      2    -93       O
ATOM   2314  CB  LEU A 638       2.632 -18.430 -18.264  1.00 14.11           C
ANISOU 2314  CB  LEU A 638     1761   1699   1902    -28     12    -53       C
ATOM   2315  CG  LEU A 638       3.552 -19.290 -19.144  1.00 16.89           C
ANISOU 2315  CG  LEU A 638     2106   2085   2227    -23     18    -24       C
ATOM   2316  CD1 LEU A 638       4.822 -19.663 -18.391  1.00 17.23           C
ANISOU 2316  CD1 LEU A 638     2133   2157   2256    -30     14    -36       C
ATOM   2317  CD2 LEU A 638       2.841 -20.548 -19.626  1.00 16.39           C
ANISOU 2317  CD2 LEU A 638     2055   2035   2135      2     22    -19       C
ATOM   2318  N   ALA A 639      -0.621 -17.317 -17.794  1.00 11.43           N
ANISOU 2318  N   ALA A 639     1444   1288   1612     -7     11    -86       N
ATOM   2319  CA  ALA A 639      -1.532 -16.454 -17.064  1.00 10.99           C
ANISOU 2319  CA  ALA A 639     1387   1201   1588     -5     10   -120       C
ATOM   2320  C   ALA A 639      -1.760 -16.943 -15.633  1.00 15.50           C
ANISOU 2320  C   ALA A 639     1959   1802   2129      2     14   -162       C
ATOM   2321  O   ALA A 639      -2.050 -18.114 -15.413  1.00 15.17           O
ANISOU 2321  O   ALA A 639     1923   1792   2049     15     21   -153       O
ATOM   2322  CB  ALA A 639      -2.861 -16.380 -17.809  1.00 13.85           C
ANISOU 2322  CB  ALA A 639     1755   1541   1966     12     11   -101       C
ATOM   2323  N   LYS A 640      -1.654 -16.035 -14.669  1.00 15.23           N
ANISOU 2323  N   LYS A 640     1914   1758   2114     -5     10   -208       N
ATOM   2324  CA  LYS A 640      -1.790 -16.377 -13.258  1.00 13.44           C
ANISOU 2324  CA  LYS A 640     1683   1573   1850      3     13   -251       C
ATOM   2325  C   LYS A 640      -3.197 -16.866 -12.936  1.00 17.11           C
ANISOU 2325  C   LYS A 640     2153   2046   2300     24     28   -253       C
ATOM   2326  O   LYS A 640      -4.184 -16.210 -13.270  1.00 17.89           O
ANISOU 2326  O   LYS A 640     2252   2108   2437     31     30   -261       O
ATOM   2327  CB  LYS A 640      -1.453 -15.141 -12.425  1.00 18.81           C
ANISOU 2327  CB  LYS A 640     2348   2240   2560     -8      3   -311       C
ATOM   2328  CG  LYS A 640      -1.478 -15.329 -10.929  1.00 19.78           C
ANISOU 2328  CG  LYS A 640     2462   2418   2635      0      5   -363       C
ATOM   2329  CD  LYS A 640      -1.126 -13.985 -10.273  1.00 28.87           C
ANISOU 2329  CD  LYS A 640     3594   3548   3826    -12     -9   -435       C
ATOM   2330  CE  LYS A 640      -1.194 -14.034  -8.760  1.00 38.06           C
ANISOU 2330  CE  LYS A 640     4746   4779   4938     -1     -9   -499       C
ATOM   2331  NZ  LYS A 640      -0.891 -12.688  -8.176  1.00 36.02           N
ANISOU 2331  NZ  LYS A 640     4465   4495   4724    -12    -26   -583       N
ATOM   2332  N   LEU A 641      -3.282 -18.032 -12.303  1.00 15.68           N
ANISOU 2332  N   LEU A 641     1975   1915   2069     33     38   -242       N
ATOM   2333  CA  LEU A 641      -4.557 -18.557 -11.841  1.00 13.30           C
ANISOU 2333  CA  LEU A 641     1672   1627   1753     50     54   -241       C
ATOM   2334  C   LEU A 641      -4.909 -17.985 -10.457  1.00 18.61           C
ANISOU 2334  C   LEU A 641     2332   2333   2405     58     62   -295       C
ATOM   2335  O   LEU A 641      -4.054 -17.858  -9.583  1.00 20.61           O
ANISOU 2335  O   LEU A 641     2578   2627   2627     53     55   -322       O
ATOM   2336  CB  LEU A 641      -4.532 -20.099 -11.817  1.00 13.46           C
ANISOU 2336  CB  LEU A 641     1696   1679   1738     57     63   -197       C
ATOM   2337  CG  LEU A 641      -4.427 -20.714 -13.216  1.00 13.28           C
ANISOU 2337  CG  LEU A 641     1683   1625   1736     54     57   -157       C
ATOM   2338  CD1 LEU A 641      -4.048 -22.209 -13.149  1.00 13.04           C
ANISOU 2338  CD1 LEU A 641     1653   1620   1682     59     62   -121       C
ATOM   2339  CD2 LEU A 641      -5.749 -20.511 -13.974  1.00 15.68           C
ANISOU 2339  CD2 LEU A 641     1989   1895   2075     61     61   -153       C
ATOM   2340  N   HIS A 642      -6.173 -17.629 -10.274  1.00 18.53           N
ANISOU 2340  N   HIS A 642     2316   2312   2413     71     75   -315       N
ATOM   2341  CA  HIS A 642      -6.628 -17.082  -9.003  1.00 19.94           C
ANISOU 2341  CA  HIS A 642     2479   2527   2570     82     86   -372       C
ATOM   2342  C   HIS A 642      -7.552 -18.087  -8.307  1.00 22.73           C
ANISOU 2342  C   HIS A 642     2824   2932   2879     98    112   -349       C
ATOM   2343  O   HIS A 642      -7.122 -18.824  -7.416  1.00 30.25           O
ANISOU 2343  O   HIS A 642     3771   3949   3773    100    119   -336       O
ATOM   2344  CB  HIS A 642      -7.295 -15.720  -9.223  1.00 24.13           C
ANISOU 2344  CB  HIS A 642     3002   3004   3163     87     82   -421       C
ATOM   2345  CG  HIS A 642      -6.491 -14.796 -10.091  1.00 31.27           C
ANISOU 2345  CG  HIS A 642     3911   3846   4124     70     59   -424       C
ATOM   2346  ND1 HIS A 642      -6.600 -14.783 -11.467  1.00 37.14           N
ANISOU 2346  ND1 HIS A 642     4666   4536   4911     65     51   -372       N
ATOM   2347  CD2 HIS A 642      -5.539 -13.883  -9.780  1.00 37.46           C
ANISOU 2347  CD2 HIS A 642     4687   4615   4930     56     42   -468       C
ATOM   2348  CE1 HIS A 642      -5.763 -13.889 -11.964  1.00 39.41           C
ANISOU 2348  CE1 HIS A 642     4952   4779   5242     48     34   -376       C
ATOM   2349  NE2 HIS A 642      -5.104 -13.333 -10.963  1.00 39.78           N
ANISOU 2349  NE2 HIS A 642     4987   4844   5283     41     28   -435       N
ATOM   2350  N   ASP A 643      -8.809 -18.148  -8.727  1.00 18.69           N
ANISOU 2350  N   ASP A 643     2308   2394   2398    107    125   -338       N
ATOM   2351  CA  ASP A 643      -9.744 -19.101  -8.145  1.00 23.62           C
ANISOU 2351  CA  ASP A 643     2920   3061   2992    118    152   -310       C
ATOM   2352  C   ASP A 643      -9.493 -20.527  -8.621  1.00 22.53           C
ANISOU 2352  C   ASP A 643     2791   2926   2845    110    153   -239       C
ATOM   2353  O   ASP A 643      -9.765 -21.484  -7.901  1.00 26.97           O
ANISOU 2353  O   ASP A 643     3341   3533   3372    115    174   -206       O
ATOM   2354  CB  ASP A 643     -11.190 -18.708  -8.465  1.00 35.21           C
ANISOU 2354  CB  ASP A 643     4375   4499   4503    130    165   -322       C
ATOM   2355  CG  ASP A 643     -11.592 -17.387  -7.832  1.00 57.27           C
ANISOU 2355  CG  ASP A 643     7155   7295   7311    144    169   -396       C
ATOM   2356  OD1 ASP A 643     -11.182 -17.123  -6.680  1.00 59.81           O
ANISOU 2356  OD1 ASP A 643     7467   7674   7585    150    176   -439       O
ATOM   2357  OD2 ASP A 643     -12.318 -16.612  -8.490  1.00 70.82           O
ANISOU 2357  OD2 ASP A 643     8866   8955   9086    152    164   -414       O
ATOM   2358  N   ARG A 644      -8.980 -20.678  -9.835  1.00 16.99           N
ANISOU 2358  N   ARG A 644     2106   2174   2176     99    133   -216       N
ATOM   2359  CA  ARG A 644      -8.872 -22.013 -10.410  1.00 14.27           C
ANISOU 2359  CA  ARG A 644     1766   1822   1835     94    133   -161       C
ATOM   2360  C   ARG A 644      -7.511 -22.648 -10.142  1.00 18.15           C
ANISOU 2360  C   ARG A 644     2264   2340   2292     88    124   -138       C
ATOM   2361  O   ARG A 644      -6.937 -23.275 -11.013  1.00 18.35           O
ANISOU 2361  O   ARG A 644     2299   2340   2333     83    112   -111       O
ATOM   2362  CB  ARG A 644      -9.199 -21.974 -11.908  1.00 18.51           C
ANISOU 2362  CB  ARG A 644     2311   2302   2419     90    117   -150       C
ATOM   2363  CG  ARG A 644     -10.683 -21.738 -12.179  1.00 29.34           C
ANISOU 2363  CG  ARG A 644     3669   3652   3825     98    126   -158       C
ATOM   2364  CD  ARG A 644     -10.913 -20.912 -13.428  1.00 36.13           C
ANISOU 2364  CD  ARG A 644     4537   4466   4726     99    105   -167       C
ATOM   2365  NE  ARG A 644     -10.218 -21.458 -14.580  1.00 35.47           N
ANISOU 2365  NE  ARG A 644     4466   4365   4646     91     86   -141       N
ATOM   2366  CZ  ARG A 644      -9.865 -20.747 -15.646  1.00 39.47           C
ANISOU 2366  CZ  ARG A 644     4982   4846   5170     89     67   -140       C
ATOM   2367  NH1 ARG A 644     -10.139 -19.450 -15.708  1.00 49.79           N
ANISOU 2367  NH1 ARG A 644     6286   6130   6502     94     62   -158       N
ATOM   2368  NH2 ARG A 644      -9.229 -21.332 -16.650  1.00 30.23           N
ANISOU 2368  NH2 ARG A 644     3820   3673   3994     84     54   -118       N
ATOM   2369  N   ASN A 645      -7.006 -22.495  -8.923  1.00 16.61           N
ANISOU 2369  N   ASN A 645     2061   2200   2049     92    130   -152       N
ATOM   2370  CA  ASN A 645      -5.674 -23.008  -8.604  1.00 18.06           C
ANISOU 2370  CA  ASN A 645     2248   2415   2199     89    119   -131       C
ATOM   2371  C   ASN A 645      -5.706 -24.316  -7.820  1.00 18.42           C
ANISOU 2371  C   ASN A 645     2282   2504   2213     98    135    -76       C
ATOM   2372  O   ASN A 645      -4.848 -24.573  -6.972  1.00 18.53           O
ANISOU 2372  O   ASN A 645     2289   2571   2180    102    131    -64       O
ATOM   2373  CB  ASN A 645      -4.835 -21.949  -7.875  1.00 19.94           C
ANISOU 2373  CB  ASN A 645     2483   2687   2407     87    105   -183       C
ATOM   2374  CG  ASN A 645      -5.403 -21.580  -6.519  1.00 26.25           C
ANISOU 2374  CG  ASN A 645     3265   3550   3160     99    122   -216       C
ATOM   2375  OD1 ASN A 645      -6.536 -21.935  -6.187  1.00 24.97           O
ANISOU 2375  OD1 ASN A 645     3093   3401   2992    109    146   -201       O
ATOM   2376  ND2 ASN A 645      -4.619 -20.846  -5.731  1.00 26.79           N
ANISOU 2376  ND2 ASN A 645     3326   3662   3192     99    108   -265       N
ATOM   2377  N   THR A 646      -6.713 -25.140  -8.105  1.00 18.45           N
ANISOU 2377  N   THR A 646     2280   2485   2246    100    152    -40       N
ATOM   2378  CA  THR A 646      -6.712 -26.537  -7.681  1.00 18.90           C
ANISOU 2378  CA  THR A 646     2325   2559   2298    104    166     26       C
ATOM   2379  C   THR A 646      -7.200 -27.339  -8.881  1.00 15.22           C
ANISOU 2379  C   THR A 646     1862   2022   1897     97    163     49       C
ATOM   2380  O   THR A 646      -7.860 -26.790  -9.761  1.00 17.30           O
ANISOU 2380  O   THR A 646     2133   2246   2196     92    157     17       O
ATOM   2381  CB  THR A 646      -7.672 -26.776  -6.509  1.00 23.22           C
ANISOU 2381  CB  THR A 646     2849   3158   2814    112    197     50       C
ATOM   2382  OG1 THR A 646      -9.016 -26.525  -6.945  1.00 24.15           O
ANISOU 2382  OG1 THR A 646     2961   3242   2972    109    211     33       O
ATOM   2383  CG2 THR A 646      -7.341 -25.852  -5.354  1.00 26.02           C
ANISOU 2383  CG2 THR A 646     3198   3590   3099    122    199     10       C
ATOM   2384  N   TYR A 647      -6.886 -28.627  -8.936  1.00 16.88           N
ANISOU 2384  N   TYR A 647     2066   2220   2129     99    166    101       N
ATOM   2385  CA  TYR A 647      -7.299 -29.398 -10.096  1.00 18.11           C
ANISOU 2385  CA  TYR A 647     2221   2309   2350     93    159    109       C
ATOM   2386  C   TYR A 647      -8.816 -29.471 -10.200  1.00 15.55           C
ANISOU 2386  C   TYR A 647     1882   1965   2060     87    176    108       C
ATOM   2387  O   TYR A 647      -9.354 -29.500 -11.300  1.00 17.35           O
ANISOU 2387  O   TYR A 647     2112   2145   2333     82    165     85       O
ATOM   2388  CB  TYR A 647      -6.669 -30.798 -10.105  1.00 15.95           C
ANISOU 2388  CB  TYR A 647     1938   2016   2104     97    158    160       C
ATOM   2389  CG  TYR A 647      -7.390 -31.820  -9.262  1.00 17.68           C
ANISOU 2389  CG  TYR A 647     2132   2241   2344     98    184    223       C
ATOM   2390  CD1 TYR A 647      -8.361 -32.637  -9.826  1.00 27.05           C
ANISOU 2390  CD1 TYR A 647     3303   3371   3602     89    191    236       C
ATOM   2391  CD2 TYR A 647      -7.094 -31.978  -7.917  1.00 24.95           C
ANISOU 2391  CD2 TYR A 647     3042   3225   3215    107    200    271       C
ATOM   2392  CE1 TYR A 647      -9.027 -33.578  -9.074  1.00 28.24           C
ANISOU 2392  CE1 TYR A 647     3426   3521   3782     86    217    300       C
ATOM   2393  CE2 TYR A 647      -7.759 -32.922  -7.149  1.00 29.29           C
ANISOU 2393  CE2 TYR A 647     3564   3783   3783    107    227    341       C
ATOM   2394  CZ  TYR A 647      -8.726 -33.716  -7.737  1.00 33.79           C
ANISOU 2394  CZ  TYR A 647     4117   4287   4433     96    237    358       C
ATOM   2395  OH  TYR A 647      -9.401 -34.666  -6.998  1.00 38.22           O
ANISOU 2395  OH  TYR A 647     4647   4850   5024     93    265    434       O
ATOM   2396  N   GLU A 648      -9.506 -29.503  -9.061  1.00 18.22           N
ANISOU 2396  N   GLU A 648     2202   2345   2374     90    203    134       N
ATOM   2397  CA  GLU A 648     -10.955 -29.654  -9.091  1.00 23.59           C
ANISOU 2397  CA  GLU A 648     2861   3010   3091     85    223    139       C
ATOM   2398  C   GLU A 648     -11.641 -28.391  -9.585  1.00 20.68           C
ANISOU 2398  C   GLU A 648     2500   2635   2723     85    216     78       C
ATOM   2399  O   GLU A 648     -12.727 -28.453 -10.164  1.00 20.36           O
ANISOU 2399  O   GLU A 648     2446   2562   2728     80    218     69       O
ATOM   2400  CB  GLU A 648     -11.498 -30.091  -7.725  1.00 33.00           C
ANISOU 2400  CB  GLU A 648     4025   4256   4255     89    259    192       C
ATOM   2401  CG  GLU A 648     -11.725 -31.602  -7.648  1.00 52.34           C
ANISOU 2401  CG  GLU A 648     6452   6675   6760     81    272    264       C
ATOM   2402  CD  GLU A 648     -11.495 -32.183  -6.262  1.00 67.80           C
ANISOU 2402  CD  GLU A 648     8390   8697   8674     89    300    338       C
ATOM   2403  OE1 GLU A 648     -10.804 -31.535  -5.445  1.00 68.88           O
ANISOU 2403  OE1 GLU A 648     8536   8904   8731    102    300    329       O
ATOM   2404  OE2 GLU A 648     -12.003 -33.296  -5.995  1.00 71.60           O
ANISOU 2404  OE2 GLU A 648     8843   9158   9204     82    321    407       O
ATOM   2405  N   LYS A 649     -10.995 -27.247  -9.369  1.00 17.19           N
ANISOU 2405  N   LYS A 649     2075   2220   2236     92    205     37       N
ATOM   2406  CA  LYS A 649     -11.528 -25.982  -9.854  1.00 16.53           C
ANISOU 2406  CA  LYS A 649     1999   2122   2161     95    196    -18       C
ATOM   2407  C   LYS A 649     -11.024 -25.686 -11.265  1.00 17.46           C
ANISOU 2407  C   LYS A 649     2137   2188   2308     89    164    -39       C
ATOM   2408  O   LYS A 649     -11.726 -25.065 -12.059  1.00 17.93           O
ANISOU 2408  O   LYS A 649     2196   2217   2398     90    154    -65       O
ATOM   2409  CB  LYS A 649     -11.173 -24.838  -8.896  1.00 19.12           C
ANISOU 2409  CB  LYS A 649     2329   2498   2437    104    201    -57       C
ATOM   2410  CG  LYS A 649     -11.997 -24.869  -7.595  1.00 27.31           C
ANISOU 2410  CG  LYS A 649     3340   3595   3441    113    235    -51       C
ATOM   2411  CD  LYS A 649     -11.634 -23.730  -6.641  1.00 33.81           C
ANISOU 2411  CD  LYS A 649     4163   4472   4210    125    238   -104       C
ATOM   2412  CE  LYS A 649     -10.219 -23.872  -6.092  1.00 45.27           C
ANISOU 2412  CE  LYS A 649     5626   5964   5611    124    225    -98       C
ATOM   2413  NZ  LYS A 649      -9.887 -22.783  -5.119  1.00 54.17           N
ANISOU 2413  NZ  LYS A 649     6748   7149   6686    134    224   -160       N
ATOM   2414  N   TYR A 650      -9.811 -26.139 -11.575  1.00 12.50           N
ANISOU 2414  N   TYR A 650     1524   1556   1670     86    149    -26       N
ATOM   2415  CA  TYR A 650      -9.242 -25.890 -12.901  1.00 11.40           C
ANISOU 2415  CA  TYR A 650     1401   1380   1550     82    123    -42       C
ATOM   2416  C   TYR A 650      -9.919 -26.755 -13.981  1.00 12.83           C
ANISOU 2416  C   TYR A 650     1576   1523   1778     80    115    -34       C
ATOM   2417  O   TYR A 650     -10.090 -26.322 -15.121  1.00 17.57           O
ANISOU 2417  O   TYR A 650     2182   2100   2394     80     96    -54       O
ATOM   2418  CB  TYR A 650      -7.723 -26.142 -12.886  1.00 11.64           C
ANISOU 2418  CB  TYR A 650     1444   1422   1555     81    112    -32       C
ATOM   2419  CG  TYR A 650      -7.023 -25.745 -14.176  1.00 12.60           C
ANISOU 2419  CG  TYR A 650     1580   1519   1687     78     89    -49       C
ATOM   2420  CD1 TYR A 650      -6.612 -26.701 -15.100  1.00 13.08           C
ANISOU 2420  CD1 TYR A 650     1643   1562   1767     79     80    -37       C
ATOM   2421  CD2 TYR A 650      -6.794 -24.408 -14.469  1.00 13.52           C
ANISOU 2421  CD2 TYR A 650     1706   1633   1798     75     80    -75       C
ATOM   2422  CE1 TYR A 650      -5.995 -26.328 -16.289  1.00 13.18           C
ANISOU 2422  CE1 TYR A 650     1665   1564   1779     78     62    -51       C
ATOM   2423  CE2 TYR A 650      -6.189 -24.030 -15.646  1.00 13.71           C
ANISOU 2423  CE2 TYR A 650     1740   1641   1829     72     63    -79       C
ATOM   2424  CZ  TYR A 650      -5.784 -24.983 -16.545  1.00 13.65           C
ANISOU 2424  CZ  TYR A 650     1733   1626   1828     74     55    -66       C
ATOM   2425  OH  TYR A 650      -5.178 -24.576 -17.716  1.00 14.01           O
ANISOU 2425  OH  TYR A 650     1785   1668   1872     73     42    -69       O
ATOM   2426  N   LEU A 651     -10.260 -27.991 -13.623  1.00 13.95           N
ANISOU 2426  N   LEU A 651     1700   1658   1941     77    128     -2       N
ATOM   2427  CA  LEU A 651     -10.810 -28.957 -14.581  1.00 15.20           C
ANISOU 2427  CA  LEU A 651     1848   1777   2152     73    118     -1       C
ATOM   2428  C   LEU A 651     -12.330 -29.060 -14.474  1.00 15.73           C
ANISOU 2428  C   LEU A 651     1889   1832   2254     68    130     -1       C
ATOM   2429  O   LEU A 651     -12.874 -29.074 -13.375  1.00 17.66           O
ANISOU 2429  O   LEU A 651     2118   2099   2491     68    156     22       O
ATOM   2430  CB  LEU A 651     -10.202 -30.342 -14.336  1.00 14.53           C
ANISOU 2430  CB  LEU A 651     1755   1678   2089     71    123     33       C
ATOM   2431  CG  LEU A 651      -8.677 -30.435 -14.436  1.00 14.48           C
ANISOU 2431  CG  LEU A 651     1766   1682   2054     78    112     36       C
ATOM   2432  CD1 LEU A 651      -8.227 -31.849 -14.094  1.00 17.20           C
ANISOU 2432  CD1 LEU A 651     2097   2006   2430     80    118     75       C
ATOM   2433  CD2 LEU A 651      -8.192 -30.038 -15.832  1.00 14.94           C
ANISOU 2433  CD2 LEU A 651     1840   1727   2111     80     87     -4       C
ATOM   2434  N   GLY A 652     -13.013 -29.160 -15.610  1.00 14.71           N
ANISOU 2434  N   GLY A 652     1753   1675   2162     66    110    -26       N
ATOM   2435  CA  GLY A 652     -14.462 -29.307 -15.605  1.00 16.94           C
ANISOU 2435  CA  GLY A 652     2006   1946   2484     61    118    -29       C
ATOM   2436  C   GLY A 652     -14.912 -30.617 -14.979  1.00 16.02           C
ANISOU 2436  C   GLY A 652     1862   1812   2413     49    138      8       C
ATOM   2437  O   GLY A 652     -14.151 -31.584 -14.925  1.00 17.40           O
ANISOU 2437  O   GLY A 652     2039   1970   2603     46    138     29       O
ATOM   2438  N   GLU A 653     -16.157 -30.658 -14.507  1.00 16.32           N
ANISOU 2438  N   GLU A 653     2250   2338   1611   -528    419    436       N
ATOM   2439  CA  GLU A 653     -16.674 -31.854 -13.834  1.00 16.84           C
ANISOU 2439  CA  GLU A 653     2319   2336   1743   -595    394    501       C
ATOM   2440  C   GLU A 653     -16.758 -33.053 -14.783  1.00 15.55           C
ANISOU 2440  C   GLU A 653     2112   2100   1696   -626    361    433       C
ATOM   2441  O   GLU A 653     -16.318 -34.158 -14.440  1.00 18.45           O
ANISOU 2441  O   GLU A 653     2490   2357   2163   -654    308    455       O
ATOM   2442  CB  GLU A 653     -18.060 -31.593 -13.233  1.00 28.12           C
ANISOU 2442  CB  GLU A 653     3729   3822   3133   -581    416    538       C
ATOM   2443  CG  GLU A 653     -18.238 -30.224 -12.595  1.00 51.48           C
ANISOU 2443  CG  GLU A 653     6704   6822   6035   -464    427    521       C
ATOM   2444  CD  GLU A 653     -17.290 -29.971 -11.437  1.00 72.84           C
ANISOU 2444  CD  GLU A 653     9458   9480   8737   -423    404    564       C
ATOM   2445  OE1 GLU A 653     -17.234 -28.815 -10.960  1.00 78.60           O
ANISOU 2445  OE1 GLU A 653    10210  10223   9432   -333    411    538       O
ATOM   2446  OE2 GLU A 653     -16.604 -30.922 -11.001  1.00 79.54           O
ANISOU 2446  OE2 GLU A 653    10329  10264   9630   -480    376    619       O
ATOM   2447  N   GLU A 654     -17.328 -32.847 -15.967  1.00 15.76           N
ANISOU 2447  N   GLU A 654     2091   2187   1712   -620    388    349       N
ATOM   2448  CA  GLU A 654     -17.425 -33.930 -16.942  1.00 19.34           C
ANISOU 2448  CA  GLU A 654     2501   2576   2270   -642    354    273       C
ATOM   2449  C   GLU A 654     -16.055 -34.272 -17.481  1.00 17.45           C
ANISOU 2449  C   GLU A 654     2266   2261   2104   -592    309    201       C
ATOM   2450  O   GLU A 654     -15.787 -35.428 -17.811  1.00 16.42           O
ANISOU 2450  O   GLU A 654     2123   2034   2083   -609    257    164       O
ATOM   2451  CB  GLU A 654     -18.377 -33.598 -18.093  1.00 20.09           C
ANISOU 2451  CB  GLU A 654     2541   2761   2330   -644    395    199       C
ATOM   2452  CG  GLU A 654     -19.842 -33.554 -17.683  1.00 20.51           C
ANISOU 2452  CG  GLU A 654     2580   2879   2334   -703    432    264       C
ATOM   2453  CD  GLU A 654     -20.355 -34.888 -17.164  1.00 34.45           C
ANISOU 2453  CD  GLU A 654     4341   4554   4193   -777    388    322       C
ATOM   2454  OE1 GLU A 654     -20.058 -35.928 -17.789  1.00 31.45           O
ANISOU 2454  OE1 GLU A 654     3942   4082   3924   -790    336    262       O
ATOM   2455  OE2 GLU A 654     -21.054 -34.897 -16.128  1.00 46.67           O
ANISOU 2455  OE2 GLU A 654     5905   6125   5703   -821    402    429       O
ATOM   2456  N   TYR A 655     -15.184 -33.270 -17.564  1.00 14.34           N
ANISOU 2456  N   TYR A 655     1889   1910   1650   -529    325    183       N
ATOM   2457  CA  TYR A 655     -13.816 -33.541 -17.983  1.00 16.56           C
ANISOU 2457  CA  TYR A 655     2174   2126   1993   -479    283    126       C
ATOM   2458  C   TYR A 655     -13.165 -34.531 -17.018  1.00 18.12           C
ANISOU 2458  C   TYR A 655     2413   2197   2275   -503    226    187       C
ATOM   2459  O   TYR A 655     -12.571 -35.512 -17.438  1.00 14.92           O
ANISOU 2459  O   TYR A 655     1996   1702   1970   -497    175    137       O
ATOM   2460  CB  TYR A 655     -12.974 -32.271 -18.080  1.00 12.79           C
ANISOU 2460  CB  TYR A 655     1710   1715   1436   -414    307    117       C
ATOM   2461  CG  TYR A 655     -11.596 -32.566 -18.647  1.00 13.02           C
ANISOU 2461  CG  TYR A 655     1732   1689   1528   -361    265     55       C
ATOM   2462  CD1 TYR A 655     -11.422 -32.847 -20.005  1.00 15.90           C
ANISOU 2462  CD1 TYR A 655     2041   2071   1930   -329    259    -54       C
ATOM   2463  CD2 TYR A 655     -10.484 -32.619 -17.821  1.00 16.29           C
ANISOU 2463  CD2 TYR A 655     2193   2034   1964   -341    230    105       C
ATOM   2464  CE1 TYR A 655     -10.157 -33.150 -20.522  1.00 15.54           C
ANISOU 2464  CE1 TYR A 655     1985   1981   1937   -275    221   -110       C
ATOM   2465  CE2 TYR A 655      -9.216 -32.904 -18.331  1.00 16.90           C
ANISOU 2465  CE2 TYR A 655     2261   2064   2097   -291    192     51       C
ATOM   2466  CZ  TYR A 655      -9.060 -33.171 -19.670  1.00 16.07           C
ANISOU 2466  CZ  TYR A 655     2099   1983   2025   -257    188    -54       C
ATOM   2467  OH  TYR A 655      -7.801 -33.468 -20.158  1.00 16.85           O
ANISOU 2467  OH  TYR A 655     2186   2043   2175   -203    150   -106       O
ATOM   2468  N   VAL A 656     -13.281 -34.268 -15.723  1.00 14.81           N
ANISOU 2468  N   VAL A 656     2040   1774   1814   -527    233    294       N
ATOM   2469  CA  VAL A 656     -12.685 -35.147 -14.724  1.00 14.93           C
ANISOU 2469  CA  VAL A 656     2094   1675   1902   -551    181    362       C
ATOM   2470  C   VAL A 656     -13.288 -36.547 -14.802  1.00 18.69           C
ANISOU 2470  C   VAL A 656     2549   2067   2485   -613    140    365       C
ATOM   2471  O   VAL A 656     -12.583 -37.552 -14.655  1.00 18.63           O
ANISOU 2471  O   VAL A 656     2552   1944   2580   -619     80    362       O
ATOM   2472  CB  VAL A 656     -12.854 -34.570 -13.298  1.00 15.34           C
ANISOU 2472  CB  VAL A 656     2195   1755   1878   -566    200    481       C
ATOM   2473  CG1 VAL A 656     -12.585 -35.632 -12.262  1.00 20.47           C
ANISOU 2473  CG1 VAL A 656     2875   2295   2606   -609    149    562       C
ATOM   2474  CG2 VAL A 656     -11.928 -33.366 -13.103  1.00 16.87           C
ANISOU 2474  CG2 VAL A 656     2421   1996   1994   -501    215    480       C
ATOM   2475  N   LYS A 657     -14.592 -36.625 -15.041  1.00 16.01           N
ANISOU 2475  N   LYS A 657     2178   1781   2124   -659    169    371       N
ATOM   2476  CA  LYS A 657     -15.230 -37.934 -15.204  1.00 18.04           C
ANISOU 2476  CA  LYS A 657     2410   1959   2487   -721    126    372       C
ATOM   2477  C   LYS A 657     -14.634 -38.699 -16.396  1.00 18.21           C
ANISOU 2477  C   LYS A 657     2402   1910   2609   -692     79    251       C
ATOM   2478  O   LYS A 657     -14.329 -39.893 -16.306  1.00 18.33           O
ANISOU 2478  O   LYS A 657     2420   1806   2741   -717     12    248       O
ATOM   2479  CB  LYS A 657     -16.733 -37.757 -15.406  1.00 17.98           C
ANISOU 2479  CB  LYS A 657     2366   2035   2429   -771    169    390       C
ATOM   2480  CG  LYS A 657     -17.486 -39.072 -15.564  1.00 25.38           C
ANISOU 2480  CG  LYS A 657     3274   2894   3473   -842    122    398       C
ATOM   2481  CD  LYS A 657     -18.985 -38.827 -15.658  1.00 36.28           C
ANISOU 2481  CD  LYS A 657     4621   4368   4797   -893    168    431       C
ATOM   2482  CE  LYS A 657     -19.738 -40.133 -15.891  1.00 52.54           C
ANISOU 2482  CE  LYS A 657     6647   6347   6969   -965    116    438       C
ATOM   2483  NZ  LYS A 657     -21.215 -39.952 -15.825  1.00 54.88           N
ANISOU 2483  NZ  LYS A 657     6909   6732   7211  -1023    158    490       N
ATOM   2484  N   ALA A 658     -14.470 -38.001 -17.514  1.00 16.64           N
ANISOU 2484  N   ALA A 658     2172   1787   2364   -637    111    151       N
ATOM   2485  CA  ALA A 658     -13.949 -38.612 -18.729  1.00 20.03           C
ANISOU 2485  CA  ALA A 658     2567   2173   2871   -599     72     28       C
ATOM   2486  C   ALA A 658     -12.522 -39.118 -18.550  1.00 18.14           C
ANISOU 2486  C   ALA A 658     2354   1834   2703   -556     16     10       C
ATOM   2487  O   ALA A 658     -12.220 -40.264 -18.891  1.00 20.83           O
ANISOU 2487  O   ALA A 658     2686   2071   3156   -560    -48    -38       O
ATOM   2488  CB  ALA A 658     -14.008 -37.626 -19.890  1.00 17.55           C
ANISOU 2488  CB  ALA A 658     2214   1978   2478   -544    124    -64       C
ATOM   2489  N   VAL A 659     -11.644 -38.268 -18.029  1.00 16.43           N
ANISOU 2489  N   VAL A 659     2172   1648   2425   -513     37     48       N
ATOM   2490  CA  VAL A 659     -10.256 -38.688 -17.842  1.00 18.20           C
ANISOU 2490  CA  VAL A 659     2420   1785   2711   -470    -14     35       C
ATOM   2491  C   VAL A 659     -10.146 -39.773 -16.780  1.00 22.27           C
ANISOU 2491  C   VAL A 659     2973   2173   3317   -522    -71    116       C
ATOM   2492  O   VAL A 659      -9.343 -40.697 -16.912  1.00 21.37           O
ANISOU 2492  O   VAL A 659     2864   1955   3303   -505   -133     80       O
ATOM   2493  CB  VAL A 659      -9.295 -37.513 -17.543  1.00 25.08           C
ANISOU 2493  CB  VAL A 659     3316   2715   3496   -413     16     59       C
ATOM   2494  CG1 VAL A 659      -9.301 -36.516 -18.697  1.00 23.69           C
ANISOU 2494  CG1 VAL A 659     3098   2659   3245   -359     63    -25       C
ATOM   2495  CG2 VAL A 659      -9.645 -36.848 -16.247  1.00 26.13           C
ANISOU 2495  CG2 VAL A 659     3495   2877   3555   -447     47    179       C
ATOM   2496  N   GLY A 660     -10.968 -39.684 -15.738  1.00 19.25           N
ANISOU 2496  N   GLY A 660     2613   1801   2900   -584    -51    225       N
ATOM   2497  CA  GLY A 660     -11.015 -40.731 -14.736  1.00 20.96           C
ANISOU 2497  CA  GLY A 660     2857   1905   3201   -642   -103    312       C
ATOM   2498  C   GLY A 660     -11.395 -42.078 -15.341  1.00 25.39           C
ANISOU 2498  C   GLY A 660     3388   2371   3889   -678   -165    259       C
ATOM   2499  O   GLY A 660     -10.787 -43.107 -15.033  1.00 23.73           O
ANISOU 2499  O   GLY A 660     3194   2036   3786   -688   -234    268       O
ATOM   2500  N   ASN A 661     -12.399 -42.082 -16.214  1.00 20.24           N
ANISOU 2500  N   ASN A 661     2691   1772   3227   -697   -144    201       N
ATOM   2501  CA  ASN A 661     -12.801 -43.323 -16.874  1.00 20.30           C
ANISOU 2501  CA  ASN A 661     2668   1689   3354   -728   -207    141       C
ATOM   2502  C   ASN A 661     -11.707 -43.885 -17.780  1.00 20.80           C
ANISOU 2502  C   ASN A 661     2723   1683   3499   -660   -261     20       C
ATOM   2503  O   ASN A 661     -11.478 -45.093 -17.805  1.00 22.89           O
ANISOU 2503  O   ASN A 661     2988   1821   3886   -677   -340      0       O
ATOM   2504  CB  ASN A 661     -14.097 -43.127 -17.662  1.00 20.27           C
ANISOU 2504  CB  ASN A 661     2618   1768   3317   -758   -171     99       C
ATOM   2505  CG  ASN A 661     -15.296 -42.950 -16.765  1.00 25.43           C
ANISOU 2505  CG  ASN A 661     3274   2466   3921   -837   -136    222       C
ATOM   2506  OD1 ASN A 661     -15.227 -43.215 -15.561  1.00 24.10           O
ANISOU 2506  OD1 ASN A 661     3139   2251   3766   -878   -152    338       O
ATOM   2507  ND2 ASN A 661     -16.421 -42.537 -17.349  1.00 22.29           N
ANISOU 2507  ND2 ASN A 661     2839   2163   3468   -859    -90    198       N
ATOM   2508  N   LEU A 662     -11.018 -43.018 -18.516  1.00 21.61           N
ANISOU 2508  N   LEU A 662     2813   1866   3532   -581   -223    -59       N
ATOM   2509  CA  LEU A 662      -9.926 -43.499 -19.367  1.00 19.95           C
ANISOU 2509  CA  LEU A 662     2589   1603   3387   -508   -272   -171       C
ATOM   2510  C   LEU A 662      -8.864 -44.180 -18.528  1.00 24.25           C
ANISOU 2510  C   LEU A 662     3177   2027   4009   -501   -332   -123       C
ATOM   2511  O   LEU A 662      -8.245 -45.155 -18.962  1.00 26.04           O
ANISOU 2511  O   LEU A 662     3398   2155   4340   -473   -402   -193       O
ATOM   2512  CB  LEU A 662      -9.274 -42.354 -20.129  1.00 27.46           C
ANISOU 2512  CB  LEU A 662     3520   2671   4241   -426   -218   -239       C
ATOM   2513  CG  LEU A 662     -10.016 -41.825 -21.344  1.00 26.54           C
ANISOU 2513  CG  LEU A 662     3350   2667   4067   -406   -173   -329       C
ATOM   2514  CD1 LEU A 662      -9.121 -40.817 -22.056  1.00 32.64           C
ANISOU 2514  CD1 LEU A 662     4102   3538   4760   -319   -134   -391       C
ATOM   2515  CD2 LEU A 662     -10.400 -42.962 -22.269  1.00 30.96           C
ANISOU 2515  CD2 LEU A 662     3874   3162   4728   -409   -230   -430       C
ATOM   2516  N   ARG A 663      -8.644 -43.663 -17.324  1.00 20.00           N
ANISOU 2516  N   ARG A 663     2682   1496   3420   -524   -306     -5       N
ATOM   2517  CA  ARG A 663      -7.634 -44.243 -16.433  1.00 28.18           C
ANISOU 2517  CA  ARG A 663     3761   2423   4522   -521   -359     52       C
ATOM   2518  C   ARG A 663      -7.993 -45.642 -15.923  1.00 31.57           C
ANISOU 2518  C   ARG A 663     4201   2714   5082   -587   -435     95       C
ATOM   2519  O   ARG A 663      -7.126 -46.385 -15.466  1.00 28.93           O
ANISOU 2519  O   ARG A 663     3893   2269   4831   -578   -496    113       O
ATOM   2520  CB  ARG A 663      -7.300 -43.297 -15.272  1.00 29.78           C
ANISOU 2520  CB  ARG A 663     4008   2675   4633   -525   -313    166       C
ATOM   2521  CG  ARG A 663      -6.338 -42.180 -15.671  1.00 32.52           C
ANISOU 2521  CG  ARG A 663     4356   3106   4893   -444   -273    122       C
ATOM   2522  CD  ARG A 663      -5.232 -42.752 -16.536  1.00 41.92           C
ANISOU 2522  CD  ARG A 663     5528   4241   6158   -375   -323     16       C
ATOM   2523  NE  ARG A 663      -4.182 -41.791 -16.847  1.00 55.57           N
ANISOU 2523  NE  ARG A 663     7257   6041   7817   -299   -294    -14       N
ATOM   2524  CZ  ARG A 663      -3.116 -42.079 -17.589  1.00 62.77           C
ANISOU 2524  CZ  ARG A 663     8149   6930   8770   -228   -328    -99       C
ATOM   2525  NH1 ARG A 663      -2.970 -43.299 -18.094  1.00 65.73           N
ANISOU 2525  NH1 ARG A 663     8508   7210   9256   -219   -393   -171       N
ATOM   2526  NH2 ARG A 663      -2.198 -41.152 -17.831  1.00 56.30           N
ANISOU 2526  NH2 ARG A 663     7326   6184   7882   -164   -300   -113       N
ATOM   2527  N   LYS A 664      -9.267 -46.002 -16.000  1.00 21.94           N
ANISOU 2527  N   LYS A 664     2958   1498   3879   -655   -434    116       N
ATOM   2528  CA  LYS A 664      -9.679 -47.361 -15.669  1.00 23.10           C
ANISOU 2528  CA  LYS A 664     3106   1512   4157   -721   -514    150       C
ATOM   2529  C   LYS A 664      -9.209 -48.364 -16.724  1.00 29.58           C
ANISOU 2529  C   LYS A 664     3905   2239   5096   -679   -591     18       C
ATOM   2530  O   LYS A 664      -9.118 -49.570 -16.460  1.00 30.81           O
ANISOU 2530  O   LYS A 664     4068   2275   5363   -706   -669     31       O
ATOM   2531  CB  LYS A 664     -11.195 -47.423 -15.521  1.00 30.37           C
ANISOU 2531  CB  LYS A 664     4002   2473   5062   -805   -492    209       C
ATOM   2532  CG  LYS A 664     -11.720 -46.484 -14.457  1.00 32.28           C
ANISOU 2532  CG  LYS A 664     4264   2812   5188   -844   -419    339       C
ATOM   2533  CD  LYS A 664     -13.222 -46.572 -14.341  1.00 41.78           C
ANISOU 2533  CD  LYS A 664     5439   4061   6374   -924   -397    397       C
ATOM   2534  CE  LYS A 664     -13.726 -45.657 -13.237  1.00 48.96           C
ANISOU 2534  CE  LYS A 664     6367   5071   7163   -955   -327    527       C
ATOM   2535  NZ  LYS A 664     -15.193 -45.796 -13.020  1.00 56.71           N
ANISOU 2535  NZ  LYS A 664     7319   6100   8129  -1035   -307    598       N
ATOM   2536  N   CYS A 665      -8.919 -47.868 -17.923  1.00 24.80           N
ANISOU 2536  N   CYS A 665     3269   1709   4446   -604   -565   -110       N
ATOM   2537  CA  CYS A 665      -8.493 -48.739 -19.016  1.00 27.04           C
ANISOU 2537  CA  CYS A 665     3527   1922   4826   -552   -634   -248       C
ATOM   2538  C   CYS A 665      -6.990 -48.698 -19.271  1.00 30.33           C
ANISOU 2538  C   CYS A 665     3955   2316   5252   -458   -655   -312       C
ATOM   2539  O   CYS A 665      -6.440 -49.573 -19.934  1.00 40.59           O
ANISOU 2539  O   CYS A 665     5244   3534   6645   -412   -727   -411       O
ATOM   2540  CB  CYS A 665      -9.252 -48.395 -20.297  1.00 29.32           C
ANISOU 2540  CB  CYS A 665     3764   2306   5071   -530   -601   -357       C
ATOM   2541  SG  CYS A 665     -10.928 -49.045 -20.305  1.00 39.53           S
ANISOU 2541  SG  CYS A 665     5034   3570   6417   -635   -623   -322       S
ATOM   2542  N   SER A 666      -6.329 -47.670 -18.758  1.00 24.19           N
ANISOU 2542  N   SER A 666     3200   1615   4376   -428   -595   -256       N
ATOM   2543  CA  SER A 666      -4.875 -47.580 -18.873  1.00 30.31           C
ANISOU 2543  CA  SER A 666     3988   2374   5156   -344   -613   -298       C
ATOM   2544  C   SER A 666      -4.356 -46.949 -17.597  1.00 34.82           C
ANISOU 2544  C   SER A 666     4607   2953   5671   -363   -580   -169       C
ATOM   2545  O   SER A 666      -4.383 -45.725 -17.438  1.00 32.88           O
ANISOU 2545  O   SER A 666     4364   2823   5306   -351   -505   -131       O
ATOM   2546  CB  SER A 666      -4.464 -46.763 -20.098  1.00 37.96           C
ANISOU 2546  CB  SER A 666     4913   3464   6044   -256   -568   -411       C
ATOM   2547  OG  SER A 666      -4.923 -45.430 -19.999  1.00 54.89           O
ANISOU 2547  OG  SER A 666     7053   5747   8057   -266   -477   -364       O
ATOM   2548  N   THR A 667      -3.901 -47.795 -16.680  1.00 30.82           N
ANISOU 2548  N   THR A 667     4137   2319   5253   -393   -641   -100       N
ATOM   2549  CA  THR A 667      -3.655 -47.353 -15.310  1.00 35.13           C
ANISOU 2549  CA  THR A 667     4731   2862   5756   -430   -617     39       C
ATOM   2550  C   THR A 667      -2.270 -46.751 -15.090  1.00 39.81           C
ANISOU 2550  C   THR A 667     5347   3475   6305   -359   -605     42       C
ATOM   2551  O   THR A 667      -1.368 -46.886 -15.928  1.00 28.81           O
ANISOU 2551  O   THR A 667     3934   2077   4935   -281   -628    -59       O
ATOM   2552  CB  THR A 667      -3.874 -48.500 -14.304  1.00 32.65           C
ANISOU 2552  CB  THR A 667     4434   2485   5488   -482   -652    124       C
ATOM   2553  OG1 THR A 667      -2.906 -49.531 -14.539  1.00 35.90           O
ANISOU 2553  OG1 THR A 667     4842   2826   5971   -431   -713     66       O
ATOM   2554  CG2 THR A 667      -5.291 -49.070 -14.450  1.00 36.58           C
ANISOU 2554  CG2 THR A 667     4908   2970   6023   -556   -663    137       C
ATOM   2555  N   SER A 668      -2.123 -46.099 -13.940  1.00 44.15           N
ANISOU 2555  N   SER A 668     5935   4053   6786   -385   -568    160       N
ATOM   2556  CA  SER A 668      -0.916 -45.357 -13.602  1.00 37.23           C
ANISOU 2556  CA  SER A 668     5083   3208   5854   -328   -550    181       C
ATOM   2557  C   SER A 668      -0.429 -45.717 -12.198  1.00 35.37           C
ANISOU 2557  C   SER A 668     4882   2964   5592   -346   -546    285       C
ATOM   2558  O   SER A 668      -1.186 -45.613 -11.238  1.00 35.66           O
ANISOU 2558  O   SER A 668     4935   3029   5585   -404   -516    378       O
ATOM   2559  CB  SER A 668      -1.209 -43.860 -13.684  1.00 45.04           C
ANISOU 2559  CB  SER A 668     6067   4342   6703   -314   -466    199       C
ATOM   2560  OG  SER A 668      -0.211 -43.102 -13.025  1.00 41.46           O
ANISOU 2560  OG  SER A 668     5649   3913   6193   -280   -450    256       O
ATOM   2561  N   SER A 669       0.826 -46.148 -12.084  1.00 30.81           N
ANISOU 2561  N   SER A 669     4311   2355   5039   -294   -575    264       N
ATOM   2562  CA  SER A 669       1.404 -46.443 -10.780  1.00 26.10           C
ANISOU 2562  CA  SER A 669     3744   1757   4417   -305   -570    350       C
ATOM   2563  C   SER A 669       1.447 -45.193  -9.899  1.00 27.72           C
ANISOU 2563  C   SER A 669     3977   2046   4508   -310   -508    432       C
ATOM   2564  O   SER A 669       1.263 -45.268  -8.685  1.00 26.76           O
ANISOU 2564  O   SER A 669     3875   1944   4347   -343   -486    514       O
ATOM   2565  CB  SER A 669       2.790 -47.085 -10.911  1.00 30.83           C
ANISOU 2565  CB  SER A 669     4340   2310   5062   -247   -612    306       C
ATOM   2566  OG  SER A 669       3.765 -46.174 -11.388  1.00 34.51           O
ANISOU 2566  OG  SER A 669     4807   2819   5486   -182   -596    272       O
ATOM   2567  N   LEU A 670       1.681 -44.038 -10.511  1.00 24.96           N
ANISOU 2567  N   LEU A 670     3627   1750   4107   -273   -481    405       N
ATOM   2568  CA  LEU A 670       1.672 -42.786  -9.767  1.00 22.65           C
ANISOU 2568  CA  LEU A 670     3361   1544   3703   -273   -425    475       C
ATOM   2569  C   LEU A 670       0.281 -42.477  -9.217  1.00 27.81           C
ANISOU 2569  C   LEU A 670     4019   2240   4306   -337   -387    539       C
ATOM   2570  O   LEU A 670       0.119 -42.146  -8.042  1.00 27.77           O
ANISOU 2570  O   LEU A 670     4035   2284   4232   -353   -352    613       O
ATOM   2571  CB  LEU A 670       2.144 -41.636 -10.656  1.00 23.13           C
ANISOU 2571  CB  LEU A 670     3416   1650   3722   -222   -412    432       C
ATOM   2572  CG  LEU A 670       2.169 -40.284  -9.956  1.00 23.74           C
ANISOU 2572  CG  LEU A 670     3519   1822   3681   -216   -359    498       C
ATOM   2573  CD1 LEU A 670       3.143 -40.308  -8.811  1.00 21.71           C
ANISOU 2573  CD1 LEU A 670     3280   1580   3387   -196   -348    543       C
ATOM   2574  CD2 LEU A 670       2.532 -39.193 -10.961  1.00 26.53           C
ANISOU 2574  CD2 LEU A 670     3864   2216   4001   -169   -354    457       C
ATOM   2575  N   LEU A 671      -0.727 -42.593 -10.072  1.00 31.51           N
ANISOU 2575  N   LEU A 671     4467   2696   4811   -370   -394    503       N
ATOM   2576  CA  LEU A 671      -2.096 -42.349  -9.648  1.00 28.29           C
ANISOU 2576  CA  LEU A 671     4058   2334   4357   -433   -358    563       C
ATOM   2577  C   LEU A 671      -2.464 -43.274  -8.482  1.00 33.60           C
ANISOU 2577  C   LEU A 671     4736   2986   5046   -474   -364    630       C
ATOM   2578  O   LEU A 671      -3.071 -42.844  -7.500  1.00 31.89           O
ANISOU 2578  O   LEU A 671     4531   2833   4753   -499   -322    706       O
ATOM   2579  CB  LEU A 671      -3.053 -42.557 -10.820  1.00 34.50           C
ANISOU 2579  CB  LEU A 671     4811   3099   5197   -464   -371    502       C
ATOM   2580  CG  LEU A 671      -4.499 -42.130 -10.582  1.00 37.49           C
ANISOU 2580  CG  LEU A 671     5179   3560   5506   -522   -320    551       C
ATOM   2581  CD1 LEU A 671      -4.558 -40.670 -10.190  1.00 37.56           C
ANISOU 2581  CD1 LEU A 671     5206   3689   5375   -499   -254    592       C
ATOM   2582  CD2 LEU A 671      -5.325 -42.396 -11.832  1.00 46.57           C
ANISOU 2582  CD2 LEU A 671     6276   4739   6679   -527   -312    452       C
ATOM   2583  N   GLU A 672      -2.070 -44.538  -8.588  1.00 29.45           N
ANISOU 2583  N   GLU A 672     4199   2374   4618   -475   -417    600       N
ATOM   2584  CA  GLU A 672      -2.325 -45.510  -7.523  1.00 27.67           C
ANISOU 2584  CA  GLU A 672     3976   2118   4418   -513   -433    662       C
ATOM   2585  C   GLU A 672      -1.659 -45.089  -6.223  1.00 31.37           C
ANISOU 2585  C   GLU A 672     4474   2633   4814   -491   -403    726       C
ATOM   2586  O   GLU A 672      -2.298 -45.066  -5.174  1.00 34.43           O
ANISOU 2586  O   GLU A 672     4867   3059   5156   -524   -377    800       O
ATOM   2587  CB  GLU A 672      -1.837 -46.898  -7.931  1.00 25.57           C
ANISOU 2587  CB  GLU A 672     3695   1751   4268   -509   -502    611       C
ATOM   2588  CG  GLU A 672      -2.031 -47.979  -6.855  1.00 28.97           C
ANISOU 2588  CG  GLU A 672     4127   2144   4736   -548   -527    678       C
ATOM   2589  CD  GLU A 672      -3.489 -48.336  -6.642  1.00 43.78           C
ANISOU 2589  CD  GLU A 672     5984   4028   6621   -618   -523    727       C
ATOM   2590  OE1 GLU A 672      -4.328 -47.918  -7.469  1.00 47.13           O
ANISOU 2590  OE1 GLU A 672     6391   4475   7040   -638   -508    697       O
ATOM   2591  OE2 GLU A 672      -3.793 -49.039  -5.652  1.00 45.99           O
ANISOU 2591  OE2 GLU A 672     6263   4296   6916   -654   -535    797       O
ATOM   2592  N   ALA A 673      -0.371 -44.757  -6.297  1.00 27.26           N
ANISOU 2592  N   ALA A 673     3967   2109   4281   -434   -406    695       N
ATOM   2593  CA  ALA A 673       0.380 -44.334  -5.124  1.00 34.04           C
ANISOU 2593  CA  ALA A 673     4850   3010   5075   -408   -379    742       C
ATOM   2594  C   ALA A 673      -0.281 -43.145  -4.436  1.00 36.16           C
ANISOU 2594  C   ALA A 673     5131   3376   5232   -412   -318    794       C
ATOM   2595  O   ALA A 673      -0.251 -43.034  -3.211  1.00 36.76           O
ANISOU 2595  O   ALA A 673     5221   3486   5260   -413   -295    848       O
ATOM   2596  CB  ALA A 673       1.807 -43.987  -5.503  1.00 29.04           C
ANISOU 2596  CB  ALA A 673     4225   2371   4440   -345   -388    695       C
ATOM   2597  N   CYS A 674      -0.875 -42.259  -5.227  1.00 32.89           N
ANISOU 2597  N   CYS A 674     4711   3008   4778   -412   -293    773       N
ATOM   2598  CA  CYS A 674      -1.449 -41.029  -4.687  1.00 38.36           C
ANISOU 2598  CA  CYS A 674     5414   3800   5359   -405   -236    811       C
ATOM   2599  C   CYS A 674      -2.901 -41.154  -4.229  1.00 43.87           C
ANISOU 2599  C   CYS A 674     6103   4535   6032   -459   -213    863       C
ATOM   2600  O   CYS A 674      -3.373 -40.335  -3.442  1.00 47.32           O
ANISOU 2600  O   CYS A 674     6549   5053   6378   -450   -168    902       O
ATOM   2601  CB  CYS A 674      -1.336 -39.896  -5.709  1.00 35.67           C
ANISOU 2601  CB  CYS A 674     5072   3505   4975   -375   -218    768       C
ATOM   2602  SG  CYS A 674       0.362 -39.438  -6.107  1.00 33.89           S
ANISOU 2602  SG  CYS A 674     4856   3268   4753   -304   -234    719       S
ATOM   2603  N   THR A 675      -3.612 -42.162  -4.723  1.00 48.45           N
ANISOU 2603  N   THR A 675     6661   5057   6691   -510   -245    860       N
ATOM   2604  CA  THR A 675      -5.028 -42.297  -4.396  1.00 54.58           C
ANISOU 2604  CA  THR A 675     7421   5871   7445   -564   -225    910       C
ATOM   2605  C   THR A 675      -5.280 -43.299  -3.274  1.00 61.91           C
ANISOU 2605  C   THR A 675     8346   6773   8405   -597   -243    971       C
ATOM   2606  O   THR A 675      -6.426 -43.555  -2.911  1.00 62.12           O
ANISOU 2606  O   THR A 675     8355   6828   8420   -643   -232   1019       O
ATOM   2607  CB  THR A 675      -5.877 -42.661  -5.630  1.00 60.43           C
ANISOU 2607  CB  THR A 675     8133   6582   8245   -609   -243    874       C
ATOM   2608  OG1 THR A 675      -5.382 -43.870  -6.221  1.00 62.04           O
ANISOU 2608  OG1 THR A 675     8325   6677   8571   -617   -306    827       O
ATOM   2609  CG2 THR A 675      -5.836 -41.535  -6.657  1.00 64.94           C
ANISOU 2609  CG2 THR A 675     8706   7199   8768   -584   -217    825       C
ATOM   2610  N   PHE A 676      -4.209 -43.860  -2.725  1.00 67.82           N
ANISOU 2610  N   PHE A 676     9108   7469   9190   -573   -271    970       N
ATOM   2611  CA  PHE A 676      -4.330 -44.723  -1.559  1.00 72.30           C
ANISOU 2611  CA  PHE A 676     9675   8017   9779   -599   -288   1031       C
ATOM   2612  C   PHE A 676      -4.643 -43.867  -0.339  1.00 76.43           C
ANISOU 2612  C   PHE A 676    10213   8632  10195   -583   -236   1086       C
ATOM   2613  O   PHE A 676      -4.660 -42.637  -0.424  1.00 72.20           O
ANISOU 2613  O   PHE A 676     9690   8169   9574   -546   -192   1069       O
ATOM   2614  CB  PHE A 676      -3.052 -45.503  -1.317  1.00  0.00           C
ATOM   2615  CG  PHE A 676      -3.089 -46.419  -0.117  1.00  0.00           C
ATOM   2616  CD1 PHE A 676      -3.739 -47.656  -0.201  1.00  0.00           C
ATOM   2617  CD2 PHE A 676      -2.474 -46.031   1.079  1.00  0.00           C
ATOM   2618  CE2 PHE A 676      -2.508 -46.881   2.192  1.00  0.00           C
ATOM   2619  CZ  PHE A 676      -3.158 -48.118   2.108  1.00  0.00           C
ATOM   2620  CE1 PHE A 676      -3.773 -48.506   0.912  1.00  0.00           C
END


A second structure was input as follows:


HELIX    1   1 SER A  348  ASN A  361  1                                  14
HELIX    2   2 THR A  374  ASN A  383  1                                  10
HELIX    3   3 GLY A  393  LYS A  401  1                                   9
HELIX    4   4 CYS A  418  ASP A  420  1                                   3
HELIX    5   5 THR A  457  ILE A  471  1                                  15
HELIX    6   6 PHE A  476  PHE A  479  1                                   4
HELIX    7   7 SER A  493  CYS A  495  1                                   3
HELIX    8   8 GLY A  502  ASN A  504  1                                   3
HELIX    9   9 GLY A  516  GLU A  526  1                                  11
HELIX   10  10 THR A  537  ASN A  541  1                                   5
HELIX   11  11 GLU A  556  ASP A  558  1                                   3
HELIX   12  12 VAL A  571  ASN A  576  1                                   6
HELIX   13  13 LYS A  591  PHE A  608  1                                  18
HELIX   14  14 TYR A  647  LEU A  651  1                                   5
HELIX   15  15 GLU A  653  LEU A  662  1                                  10
HELIX   16  16 SER A  669  THR A  675  1                                   7
SHEET    1   1 1 VAL A 342  LEU A 347  0
SHEET    2   2 1 ILE A 366  ALA A 371  0
SHEET    3   3 1 ALA A 388  LEU A 391  0
SHEET    4   4 1 VAL A 405  ASN A 411  0
SHEET    5   5 1 TYR A 426  LYS A 433  0
SHEET    6   6 1 LYS A 448  HIS A 451  0
SHEET    7   7 1 GLU A 482  CYS A 484  0
SHEET    8   8 1 VAL A 530  LYS A 534  0
SHEET    9   9 1 TYR A 559  LEU A 561  0
SHEET   10  10 1 ALA A 580  ALA A 582  0
SHEET   11  11 1 ALA A 586  THR A 589  0
SHEET   12  12 1 CYS A 637  LYS A 640  0
ATOM      1  N   CYS A 339     -75.180  12.808 -37.613  1.00 77.68           N
ANISOU    1  N   CYS A 339     6801  10879  11834    -92   1774  -2441       N
ATOM      2  CA  CYS A 339     -74.265  11.770 -38.093  1.00 72.01           C
ANISOU    2  CA  CYS A 339     6319  10141  10900   -188   1807  -2187       C
ATOM      3  C   CYS A 339     -73.917  11.968 -39.568  1.00 62.31           C
ANISOU    3  C   CYS A 339     5025   8863   9788     41   1466  -2127       C
ATOM      4  O   CYS A 339     -74.617  11.492 -40.458  1.00 64.46           O
ANISOU    4  O   CYS A 339     5091   9145  10256     40   1307  -2252       O
ATOM      5  CB  CYS A 339     -74.819  10.364 -37.836  1.00 76.72           C
ANISOU    5  CB  CYS A 339     6920  10778  11450   -504   2036  -2231       C
ATOM      6  SG  CYS A 339     -73.621   9.230 -37.103  1.00 82.18           S
ANISOU    6  SG  CYS A 339     8080  11421  11724   -744   2284  -1914       S
ATOM      7  N   LYS A 340     -72.821  12.677 -39.805  1.00 62.76           N
ANISOU    7  N   LYS A 340     5271   8857   9719    233   1345  -1944       N
ATOM      8  CA  LYS A 340     -72.386  13.050 -41.145  1.00 59.26           C
ANISOU    8  CA  LYS A 340     4865   8326   9325    463    986  -1854       C
ATOM      9  C   LYS A 340     -71.671  11.885 -41.823  1.00 57.77           C
ANISOU    9  C   LYS A 340     4976   8089   8886    327    973  -1600       C
ATOM     10  O   LYS A 340     -71.441  10.855 -41.190  1.00 54.53           O
ANISOU   10  O   LYS A 340     4664   7724   8329     93   1263  -1538       O
ATOM     11  CB  LYS A 340     -71.458  14.267 -41.057  1.00 50.42           C
ANISOU   11  CB  LYS A 340     3965   7108   8085    670    853  -1697       C
ATOM     12  N   PRO A 341     -71.342  12.030 -43.121  1.00 54.47           N
ANISOU   12  N   PRO A 341     4723   7562   8411    465    633  -1465       N
ATOM     13  CA  PRO A 341     -70.461  11.038 -43.748  1.00 51.14           C
ANISOU   13  CA  PRO A 341     4618   7086   7727    357    642  -1228       C
ATOM     14  C   PRO A 341     -69.079  11.032 -43.089  1.00 45.43           C
ANISOU   14  C   PRO A 341     4193   6331   6737    319    840   -999       C
ATOM     15  O   PRO A 341     -68.651  12.060 -42.556  1.00 41.34           O
ANISOU   15  O   PRO A 341     3710   5796   6203    433    851   -971       O
ATOM     16  CB  PRO A 341     -70.351  11.537 -45.191  1.00 49.58           C
ANISOU   16  CB  PRO A 341     4564   6773   7501    527    249  -1153       C
ATOM     17  CG  PRO A 341     -71.622  12.267 -45.420  1.00 53.26           C
ANISOU   17  CG  PRO A 341     4708   7241   8287    672     -3  -1408       C
ATOM     18  CD  PRO A 341     -71.925  12.946 -44.118  1.00 54.04           C
ANISOU   18  CD  PRO A 341     4567   7423   8543    697    217  -1564       C
ATOM     19  N   VAL A 342     -68.400   9.888 -43.117  1.00 39.72           N
ANISOU   19  N   VAL A 342     3674   5586   5831    170    970   -858       N
ATOM     20  CA  VAL A 342     -67.083   9.772 -42.492  1.00 35.96           C
ANISOU   20  CA  VAL A 342     3458   5063   5142    143   1118   -671       C
ATOM     21  C   VAL A 342     -65.977  10.198 -43.452  1.00 30.31           C
ANISOU   21  C   VAL A 342     2972   4256   4289    267    950   -504       C
ATOM     22  O   VAL A 342     -65.816   9.613 -44.517  1.00 30.72           O
ANISOU   22  O   VAL A 342     3129   4266   4276    249    841   -459       O
ATOM     23  CB  VAL A 342     -66.802   8.334 -42.019  1.00 37.04           C
ANISOU   23  CB  VAL A 342     3724   5184   5165    -62   1307   -611       C
ATOM     24  CG1 VAL A 342     -65.465   8.269 -41.304  1.00 33.22           C
ANISOU   24  CG1 VAL A 342     3490   4629   4502    -58   1402   -447       C
ATOM     25  CG2 VAL A 342     -67.930   7.836 -41.105  1.00 36.81           C
ANISOU   25  CG2 VAL A 342     3506   5239   5241   -251   1516   -777       C
ATOM     26  N   LYS A 343     -65.226  11.224 -43.071  1.00 27.84           N
ANISOU   26  N   LYS A 343     2740   3910   3926    374    947   -431       N
ATOM     27  CA  LYS A 343     -64.102  11.694 -43.866  1.00 33.37           C
ANISOU   27  CA  LYS A 343     3658   4528   4495    449    846   -287       C
ATOM     28  C   LYS A 343     -62.874  10.860 -43.524  1.00 32.62           C
ANISOU   28  C   LYS A 343     3726   4399   4268    369    999   -179       C
ATOM     29  O   LYS A 343     -62.241  11.075 -42.497  1.00 31.91           O
ANISOU   29  O   LYS A 343     3668   4300   4155    372   1108   -142       O
ATOM     30  CB  LYS A 343     -63.843  13.183 -43.583  1.00 34.58           C
ANISOU   30  CB  LYS A 343     3818   4645   4675    582    770   -270       C
ATOM     31  CG  LYS A 343     -64.831  14.104 -44.283  1.00 40.78           C
ANISOU   31  CG  LYS A 343     4512   5399   5582    704    519   -359       C
ATOM     32  CD  LYS A 343     -64.768  15.533 -43.793  1.00 49.61           C
ANISOU   32  CD  LYS A 343     5611   6469   6769    839    443   -376       C
ATOM     33  CE  LYS A 343     -65.783  15.756 -42.679  1.00 59.83           C
ANISOU   33  CE  LYS A 343     6619   7850   8265    874    530   -573       C
ATOM     34  NZ  LYS A 343     -65.883  17.184 -42.276  1.00 64.21           N
ANISOU   34  NZ  LYS A 343     7132   8345   8922   1032    419   -633       N
ATOM     35  N   TRP A 344     -62.566   9.881 -44.368  1.00 32.45           N
ANISOU   35  N   TRP A 344     3805   4349   4176    306    986   -150       N
ATOM     36  CA  TRP A 344     -61.419   9.015 -44.139  1.00 29.11           C
ANISOU   36  CA  TRP A 344     3513   3874   3674    255   1094    -86       C
ATOM     37  C   TRP A 344     -60.133   9.737 -44.544  1.00 34.90           C
ANISOU   37  C   TRP A 344     4360   4559   4343    322   1090    -19       C
ATOM     38  O   TRP A 344     -60.123  10.487 -45.528  1.00 39.58           O
ANISOU   38  O   TRP A 344     5012   5141   4886    354   1002     -2       O
ATOM     39  CB  TRP A 344     -61.560   7.715 -44.933  1.00 29.83           C
ANISOU   39  CB  TRP A 344     3659   3942   3734    171   1082   -113       C
ATOM     40  CG  TRP A 344     -60.813   6.593 -44.302  1.00 31.09           C
ANISOU   40  CG  TRP A 344     3905   4033   3873    114   1175    -90       C
ATOM     41  CD1 TRP A 344     -59.558   6.168 -44.610  1.00 31.98           C
ANISOU   41  CD1 TRP A 344     4125   4072   3954    144   1194    -72       C
ATOM     42  CD2 TRP A 344     -61.263   5.775 -43.217  1.00 31.85           C
ANISOU   42  CD2 TRP A 344     4003   4108   3989     13   1248    -96       C
ATOM     43  NE1 TRP A 344     -59.204   5.116 -43.799  1.00 37.60           N
ANISOU   43  NE1 TRP A 344     4905   4698   4682    101   1223    -65       N
ATOM     44  CE2 TRP A 344     -60.236   4.860 -42.932  1.00 34.87           C
ANISOU   44  CE2 TRP A 344     4532   4376   4342      6   1257    -60       C
ATOM     45  CE3 TRP A 344     -62.445   5.716 -42.474  1.00 31.64           C
ANISOU   45  CE3 TRP A 344     3876   4141   4005    -89   1314   -145       C
ATOM     46  CZ2 TRP A 344     -60.352   3.899 -41.931  1.00 34.52           C
ANISOU   46  CZ2 TRP A 344     4596   4245   4274    -99   1293    -38       C
ATOM     47  CZ3 TRP A 344     -62.560   4.762 -41.476  1.00 32.81           C
ANISOU   47  CZ3 TRP A 344     4125   4228   4114   -229   1410   -129       C
ATOM     48  CH2 TRP A 344     -61.519   3.869 -41.212  1.00 36.25           C
ANISOU   48  CH2 TRP A 344     4767   4522   4486   -234   1380    -59       C
ATOM     49  N   CYS A 345     -59.057   9.525 -43.787  1.00 29.57           N
ANISOU   49  N   CYS A 345     3728   3839   3667    329   1174     12       N
ATOM     50  CA  CYS A 345     -57.773  10.118 -44.136  1.00 24.99           C
ANISOU   50  CA  CYS A 345     3212   3217   3065    368   1197     40       C
ATOM     51  C   CYS A 345     -56.873   9.063 -44.773  1.00 26.76           C
ANISOU   51  C   CYS A 345     3494   3396   3279    331   1251     -2       C
ATOM     52  O   CYS A 345     -56.464   8.109 -44.122  1.00 29.59           O
ANISOU   52  O   CYS A 345     3853   3702   3690    331   1266    -24       O
ATOM     53  CB  CYS A 345     -57.094  10.789 -42.925  1.00 22.78           C
ANISOU   53  CB  CYS A 345     2910   2912   2835    421   1221     65       C
ATOM     54  SG  CYS A 345     -55.744  11.987 -43.418  1.00 31.14           S
ANISOU   54  SG  CYS A 345     4003   3931   3897    449   1245     81       S
ATOM     55  N   ALA A 346     -56.591   9.246 -46.060  1.00 26.92           N
ANISOU   55  N   ALA A 346     3584   3421   3223    296   1270    -22       N
ATOM     56  CA  ALA A 346     -55.788   8.313 -46.846  1.00 30.95           C
ANISOU   56  CA  ALA A 346     4140   3899   3719    254   1349   -104       C
ATOM     57  C   ALA A 346     -54.326   8.726 -46.824  1.00 31.12           C
ANISOU   57  C   ALA A 346     4133   3892   3800    263   1458   -157       C
ATOM     58  O   ALA A 346     -54.009   9.909 -46.942  1.00 26.85           O
ANISOU   58  O   ALA A 346     3614   3363   3224    247   1488   -117       O
ATOM     59  CB  ALA A 346     -56.294   8.257 -48.296  1.00 28.57           C
ANISOU   59  CB  ALA A 346     3961   3620   3272    181   1333   -122       C
ATOM     60  N   LEU A 347     -53.443   7.746 -46.677  1.00 33.22           N
ANISOU   60  N   LEU A 347     4340   4105   4175    287   1506   -264       N
ATOM     61  CA  LEU A 347     -52.013   8.005 -46.677  1.00 33.12           C
ANISOU   61  CA  LEU A 347     4240   4065   4280    299   1609   -372       C
ATOM     62  C   LEU A 347     -51.509   8.112 -48.117  1.00 36.21           C
ANISOU   62  C   LEU A 347     4688   4493   4576    185   1786   -476       C
ATOM     63  O   LEU A 347     -51.264   7.093 -48.773  1.00 37.51           O
ANISOU   63  O   LEU A 347     4855   4642   4755    166   1849   -607       O
ATOM     64  CB  LEU A 347     -51.288   6.878 -45.954  1.00 31.89           C
ANISOU   64  CB  LEU A 347     3990   3813   4315    394   1546   -480       C
ATOM     65  CG  LEU A 347     -49.816   7.093 -45.657  1.00 36.08           C
ANISOU   65  CG  LEU A 347     4364   4297   5050    446   1592   -625       C
ATOM     66  CD1 LEU A 347     -49.679   8.236 -44.688  1.00 39.08           C
ANISOU   66  CD1 LEU A 347     4713   4679   5455    476   1530   -525       C
ATOM     67  CD2 LEU A 347     -49.181   5.819 -45.103  1.00 37.37           C
ANISOU   67  CD2 LEU A 347     4455   4328   5416    564   1465   -755       C
ATOM     68  N   SER A 348     -51.386   9.346 -48.603  1.00 33.58           N
ANISOU   68  N   SER A 348     4434   4195   4129     94   1866   -421       N
ATOM     69  CA  SER A 348     -50.894   9.632 -49.956  1.00 31.91           C
ANISOU   69  CA  SER A 348     4347   4010   3768    -67   2061   -502       C
ATOM     70  C   SER A 348     -51.749   8.996 -51.074  1.00 34.43           C
ANISOU   70  C   SER A 348     4857   4344   3878   -135   2041   -497       C
ATOM     71  O   SER A 348     -52.829   8.466 -50.807  1.00 40.22           O
ANISOU   71  O   SER A 348     5608   5075   4599    -58   1860   -418       O
ATOM     72  CB  SER A 348     -49.411   9.251 -50.089  1.00 29.65           C
ANISOU   72  CB  SER A 348     3882   3717   3668    -98   2164   -698       C
ATOM     73  OG  SER A 348     -48.910   9.559 -51.377  1.00 36.80           O
ANISOU   73  OG  SER A 348     4906   4648   4429   -282   2315   -766       O
ATOM     74  N   HIS A 349     -51.250   9.044 -52.311  1.00 37.01           N
ANISOU   74  N   HIS A 349     5324   4686   4054   -294   2198   -587       N
ATOM     75  CA  HIS A 349     -52.055   8.743 -53.494  1.00 38.65           C
ANISOU   75  CA  HIS A 349     5802   4897   3986   -393   2195   -571       C
ATOM     76  C   HIS A 349     -52.439   7.281 -53.688  1.00 37.23           C
ANISOU   76  C   HIS A 349     5578   4715   3854   -331   2148   -677       C
ATOM     77  O   HIS A 349     -53.481   7.001 -54.270  1.00 40.61           O
ANISOU   77  O   HIS A 349     6175   5136   4120   -349   1998   -612       O
ATOM     78  CB  HIS A 349     -51.421   9.329 -54.771  1.00 44.76           C
ANISOU   78  CB  HIS A 349     6778   5664   4565   -602   2317   -607       C
ATOM     79  CG  HIS A 349     -50.371   8.463 -55.402  1.00 46.15           C
ANISOU   79  CG  HIS A 349     6841   5857   4838   -668   2478   -822       C
ATOM     80  ND1 HIS A 349     -49.022   8.717 -55.275  1.00 50.88           N
ANISOU   80  ND1 HIS A 349     7246   6462   5623   -720   2622   -949       N
ATOM     81  CD2 HIS A 349     -50.474   7.369 -56.197  1.00 49.89           C
ANISOU   81  CD2 HIS A 349     7374   6336   5245   -697   2520   -951       C
ATOM     82  CE1 HIS A 349     -48.338   7.810 -55.952  1.00 55.93           C
ANISOU   82  CE1 HIS A 349     7817   7113   6320   -770   2751  -1150       C
ATOM     83  NE2 HIS A 349     -49.196   6.979 -56.518  1.00 55.57           N
ANISOU   83  NE2 HIS A 349     7926   7066   6121   -754   2694  -1151       N
ATOM     84  N   HIS A 350     -51.608   6.359 -53.206  1.00 36.45           N
ANISOU   84  N   HIS A 350     5249   4601   3998   -249   2219   -839       N
ATOM     85  CA  HIS A 350     -51.920   4.936 -53.281  1.00 41.74           C
ANISOU   85  CA  HIS A 350     5887   5237   4736   -181   2170   -948       C
ATOM     86  C   HIS A 350     -53.196   4.656 -52.503  1.00 36.77           C
ANISOU   86  C   HIS A 350     5250   4584   4138    -84   1901   -773       C
ATOM     87  O   HIS A 350     -54.114   3.995 -52.991  1.00 34.30           O
ANISOU   87  O   HIS A 350     5044   4261   3727   -106   1792   -759       O
ATOM     88  CB  HIS A 350     -50.797   4.087 -52.682  1.00 43.35           C
ANISOU   88  CB  HIS A 350     5841   5389   5243    -72   2208  -1132       C
ATOM     89  CG  HIS A 350     -49.582   3.975 -53.546  1.00 46.26           C
ANISOU   89  CG  HIS A 350     6141   5781   5656   -160   2350  -1314       C
ATOM     90  ND1 HIS A 350     -48.501   4.823 -53.423  1.00 53.12           N
ANISOU   90  ND1 HIS A 350     6879   6676   6626   -211   2432  -1345       N
ATOM     91  CD2 HIS A 350     -49.264   3.101 -54.531  1.00 45.92           C
ANISOU   91  CD2 HIS A 350     6134   5734   5582   -216   2440  -1491       C
ATOM     92  CE1 HIS A 350     -47.574   4.481 -54.302  1.00 50.46           C
ANISOU   92  CE1 HIS A 350     6495   6354   6323   -305   2583  -1537       C
ATOM     93  NE2 HIS A 350     -48.012   3.438 -54.985  1.00 46.03           N
ANISOU   93  NE2 HIS A 350     6031   5777   5681   -303   2591  -1626       N
ATOM     94  N   GLU A 351     -53.246   5.151 -51.277  1.00 36.10           N
ANISOU   94  N   GLU A 351     5033   4490   4192      9   1807   -661       N
ATOM     95  CA  GLU A 351     -54.433   4.954 -50.459  1.00 29.46           C
ANISOU   95  CA  GLU A 351     4173   3639   3381     69   1607   -521       C
ATOM     96  C   GLU A 351     -55.592   5.826 -50.943  1.00 35.10           C
ANISOU   96  C   GLU A 351     5007   4406   3923     19   1498   -392       C
ATOM     97  O   GLU A 351     -56.751   5.416 -50.865  1.00 38.58           O
ANISOU   97  O   GLU A 351     5451   4851   4355     23   1355   -348       O
ATOM     98  CB  GLU A 351     -54.137   5.202 -48.984  1.00 27.63           C
ANISOU   98  CB  GLU A 351     3800   3377   3322    168   1551   -458       C
ATOM     99  CG  GLU A 351     -53.313   4.102 -48.332  1.00 36.13           C
ANISOU   99  CG  GLU A 351     4787   4352   4587    249   1537   -568       C
ATOM    100  CD  GLU A 351     -53.417   4.111 -46.817  1.00 37.56           C
ANISOU  100  CD  GLU A 351     4921   4475   4875    326   1411   -471       C
ATOM    101  OE1 GLU A 351     -53.965   5.097 -46.265  1.00 32.26           O
ANISOU  101  OE1 GLU A 351     4247   3863   4147    319   1385   -344       O
ATOM    102  OE2 GLU A 351     -52.947   3.133 -46.184  1.00 28.84           O
ANISOU  102  OE2 GLU A 351     3808   3249   3902    393   1327   -530       O
ATOM    103  N   ARG A 352     -55.280   7.021 -51.446  1.00 31.78           N
ANISOU  103  N   ARG A 352     4684   4009   3381    -34   1552   -346       N
ATOM    104  CA  ARG A 352     -56.331   7.943 -51.863  1.00 32.74           C
ANISOU  104  CA  ARG A 352     4938   4141   3362    -53   1389   -227       C
ATOM    105  C   ARG A 352     -57.174   7.333 -52.978  1.00 36.13           C
ANISOU  105  C   ARG A 352     5529   4561   3637   -114   1279   -259       C
ATOM    106  O   ARG A 352     -58.392   7.468 -52.964  1.00 39.36           O
ANISOU  106  O   ARG A 352     5935   4971   4050    -77   1066   -203       O
ATOM    107  CB  ARG A 352     -55.769   9.306 -52.271  1.00 31.46           C
ANISOU  107  CB  ARG A 352     4918   3964   3073   -118   1450   -165       C
ATOM    108  CG  ARG A 352     -56.822  10.288 -52.841  1.00 38.58           C
ANISOU  108  CG  ARG A 352     6014   4828   3817   -126   1223    -48       C
ATOM    109  CD  ARG A 352     -58.027  10.511 -51.914  1.00 42.22           C
ANISOU  109  CD  ARG A 352     6297   5302   4442     15   1001     10       C
ATOM    110  NE  ARG A 352     -58.142  11.921 -51.548  1.00 52.15           N
ANISOU  110  NE  ARG A 352     7586   6520   5709     65    903    104       N
ATOM    111  CZ  ARG A 352     -59.130  12.730 -51.915  1.00 48.28           C
ANISOU  111  CZ  ARG A 352     7201   5972   5172    115    645    160       C
ATOM    112  NH1 ARG A 352     -60.132  12.281 -52.647  1.00 49.43           N
ANISOU  112  NH1 ARG A 352     7415   6100   5264    122    444    130       N
ATOM    113  NH2 ARG A 352     -59.118  13.993 -51.528  1.00 51.65           N
ANISOU  113  NH2 ARG A 352     7658   6341   5626    171    559    231       N
ATOM    114  N   LEU A 353     -56.533   6.645 -53.920  1.00 35.41           N
ANISOU  114  N   LEU A 353     5563   4459   3431   -206   1421   -375       N
ATOM    115  CA  LEU A 353     -57.269   5.999 -55.004  1.00 42.61           C
ANISOU  115  CA  LEU A 353     6656   5353   4179   -272   1313   -421       C
ATOM    116  C   LEU A 353     -58.202   4.891 -54.502  1.00 41.90           C
ANISOU  116  C   LEU A 353     6410   5261   4250   -205   1168   -448       C
ATOM    117  O   LEU A 353     -59.363   4.831 -54.907  1.00 44.27           O
ANISOU  117  O   LEU A 353     6767   5553   4499   -212    953   -421       O
ATOM    118  CB  LEU A 353     -56.323   5.462 -56.075  1.00 47.13           C
ANISOU  118  CB  LEU A 353     7397   5919   4591   -395   1535   -572       C
ATOM    119  CG  LEU A 353     -55.701   6.512 -57.005  1.00 49.99           C
ANISOU  119  CG  LEU A 353     8036   6274   4685   -547   1672   -552       C
ATOM    120  CD1 LEU A 353     -55.058   5.836 -58.200  1.00 39.85           C
ANISOU  120  CD1 LEU A 353     6953   4988   3199   -701   1889   -731       C
ATOM    121  CD2 LEU A 353     -56.725   7.549 -57.458  1.00 52.66           C
ANISOU  121  CD2 LEU A 353     8621   6562   4827   -568   1396   -381       C
ATOM    122  N   LYS A 354     -57.706   4.023 -53.622  1.00 36.93           N
ANISOU  122  N   LYS A 354     5594   4620   3816   -151   1268   -506       N
ATOM    123  CA  LYS A 354     -58.554   2.980 -53.042  1.00 35.31           C
ANISOU  123  CA  LYS A 354     5275   4391   3751   -126   1153   -518       C
ATOM    124  C   LYS A 354     -59.708   3.603 -52.261  1.00 37.82           C
ANISOU  124  C   LYS A 354     5470   4748   4154    -91    998   -408       C
ATOM    125  O   LYS A 354     -60.852   3.143 -52.322  1.00 41.88           O
ANISOU  125  O   LYS A 354     5939   5265   4708   -120    857   -422       O
ATOM    126  CB  LYS A 354     -57.756   2.037 -52.137  1.00 31.78           C
ANISOU  126  CB  LYS A 354     4708   3884   3484    -75   1253   -578       C
ATOM    127  CG  LYS A 354     -58.644   1.003 -51.426  1.00 34.70           C
ANISOU  127  CG  LYS A 354     5010   4202   3972    -88   1142   -563       C
ATOM    128  CD  LYS A 354     -57.859  -0.024 -50.607  1.00 33.71           C
ANISOU  128  CD  LYS A 354     4849   3964   3996    -42   1184   -615       C
ATOM    129  CE  LYS A 354     -58.808  -0.862 -49.750  1.00 29.89           C
ANISOU  129  CE  LYS A 354     4348   3416   3592   -101   1086   -560       C
ATOM    130  NZ  LYS A 354     -58.167  -2.047 -49.092  1.00 29.75           N
ANISOU  130  NZ  LYS A 354     4383   3233   3689    -73   1063   -605       N
ATOM    131  N   CYS A 355     -59.408   4.668 -51.536  1.00 35.01           N
ANISOU  131  N   CYS A 355     5041   4421   3841    -33   1033   -324       N
ATOM    132  CA  CYS A 355     -60.420   5.326 -50.726  1.00 35.09           C
ANISOU  132  CA  CYS A 355     4911   4471   3950     10    918   -256       C
ATOM    133  C   CYS A 355     -61.542   5.909 -51.603  1.00 37.39           C
ANISOU  133  C   CYS A 355     5260   4775   4171      7    704   -255       C
ATOM    134  O   CYS A 355     -62.718   5.818 -51.247  1.00 41.89           O
ANISOU  134  O   CYS A 355     5680   5373   4865     16    577   -284       O
ATOM    135  CB  CYS A 355     -59.770   6.392 -49.835  1.00 36.24           C
ANISOU  135  CB  CYS A 355     4994   4632   4143     78    995   -182       C
ATOM    136  SG  CYS A 355     -60.879   7.221 -48.688  1.00 48.80           S
ANISOU  136  SG  CYS A 355     6398   6273   5870    138    903   -139       S
ATOM    137  N   ASP A 356     -61.181   6.502 -52.740  1.00 32.62           N
ANISOU  137  N   ASP A 356     4882   4139   3373    -17    656   -236       N
ATOM    138  CA  ASP A 356     -62.163   7.073 -53.666  1.00 41.16           C
ANISOU  138  CA  ASP A 356     6090   5190   4360    -10    389   -229       C
ATOM    139  C   ASP A 356     -63.098   6.009 -54.227  1.00 41.74           C
ANISOU  139  C   ASP A 356     6148   5257   4456    -55    244   -324       C
ATOM    140  O   ASP A 356     -64.302   6.232 -54.344  1.00 39.26           O
ANISOU  140  O   ASP A 356     5742   4937   4237    -14     -6   -359       O
ATOM    141  CB  ASP A 356     -61.477   7.780 -54.838  1.00 44.88           C
ANISOU  141  CB  ASP A 356     6903   5598   4551    -74    384   -181       C
ATOM    142  CG  ASP A 356     -60.816   9.081 -54.438  1.00 50.96           C
ANISOU  142  CG  ASP A 356     7717   6351   5295    -45    451    -81       C
ATOM    143  OD1 ASP A 356     -61.238   9.696 -53.433  1.00 51.13           O
ANISOU  143  OD1 ASP A 356     7530   6394   5505     61    387    -46       O
ATOM    144  OD2 ASP A 356     -59.874   9.491 -55.151  1.00 53.26           O
ANISOU  144  OD2 ASP A 356     8261   6604   5372   -146    583    -53       O
ATOM    145  N   GLU A 357     -62.534   4.860 -54.590  1.00 44.57           N
ANISOU  145  N   GLU A 357     6581   5605   4750   -133    389   -388       N
ATOM    146  CA  GLU A 357     -63.343   3.725 -55.019  1.00 47.08           C
ANISOU  146  CA  GLU A 357     6876   5906   5106   -188    273   -486       C
ATOM    147  C   GLU A 357     -64.293   3.329 -53.912  1.00 45.07           C
ANISOU  147  C   GLU A 357     6315   5692   5118   -176    240   -514       C
ATOM    148  O   GLU A 357     -65.462   3.034 -54.162  1.00 50.15           O
ANISOU  148  O   GLU A 357     6862   6337   5857   -200     45   -589       O
ATOM    149  CB  GLU A 357     -62.473   2.527 -55.399  1.00 53.05           C
ANISOU  149  CB  GLU A 357     7742   6629   5784   -259    458   -565       C
ATOM    150  CG  GLU A 357     -63.285   1.274 -55.697  1.00 59.57           C
ANISOU  150  CG  GLU A 357     8536   7421   6675   -323    347   -668       C
ATOM    151  CD  GLU A 357     -62.469   0.195 -56.368  1.00 67.75           C
ANISOU  151  CD  GLU A 357     9738   8402   7602   -381    481   -772       C
ATOM    152  OE1 GLU A 357     -63.069  -0.721 -56.973  1.00 69.17           O
ANISOU  152  OE1 GLU A 357     9979   8537   7766   -443    363   -866       O
ATOM    153  OE2 GLU A 357     -61.225   0.262 -56.292  1.00 72.82           O
ANISOU  153  OE2 GLU A 357    10432   9040   8195   -361    702   -784       O
ATOM    154  N   TRP A 358     -63.784   3.333 -52.683  1.00 45.82           N
ANISOU  154  N   TRP A 358     6264   5814   5330   -154    435   -466       N
ATOM    155  CA  TRP A 358     -64.595   3.028 -51.514  1.00 41.06           C
ANISOU  155  CA  TRP A 358     5413   5250   4939   -181    464   -488       C
ATOM    156  C   TRP A 358     -65.700   4.056 -51.386  1.00 41.72           C
ANISOU  156  C   TRP A 358     5325   5388   5138   -121    291   -515       C
ATOM    157  O   TRP A 358     -66.849   3.721 -51.089  1.00 43.78           O
ANISOU  157  O   TRP A 358     5378   5683   5573   -172    220   -613       O
ATOM    158  CB  TRP A 358     -63.734   3.040 -50.249  1.00 36.81           C
ANISOU  158  CB  TRP A 358     4827   4712   4448   -163    677   -417       C
ATOM    159  CG  TRP A 358     -64.481   2.668 -49.006  1.00 34.98           C
ANISOU  159  CG  TRP A 358     4411   4507   4372   -235    750   -435       C
ATOM    160  CD1 TRP A 358     -65.721   2.095 -48.929  1.00 38.26           C
ANISOU  160  CD1 TRP A 358     4683   4946   4908   -342    697   -527       C
ATOM    161  CD2 TRP A 358     -64.032   2.831 -47.655  1.00 34.73           C
ANISOU  161  CD2 TRP A 358     4340   4475   4379   -234    905   -371       C
ATOM    162  NE1 TRP A 358     -66.071   1.900 -47.614  1.00 41.76           N
ANISOU  162  NE1 TRP A 358     5008   5412   5448   -432    849   -527       N
ATOM    163  CE2 TRP A 358     -65.051   2.341 -46.813  1.00 35.41           C
ANISOU  163  CE2 TRP A 358     4290   4587   4577   -364    966   -423       C
ATOM    164  CE3 TRP A 358     -62.865   3.340 -47.076  1.00 31.28           C
ANISOU  164  CE3 TRP A 358     3978   4015   3892   -151    996   -287       C
ATOM    165  CZ2 TRP A 358     -64.939   2.345 -45.425  1.00 37.33           C
ANISOU  165  CZ2 TRP A 358     4520   4827   4836   -422   1121   -380       C
ATOM    166  CZ3 TRP A 358     -62.761   3.348 -45.700  1.00 33.14           C
ANISOU  166  CZ3 TRP A 358     4183   4241   4168   -180   1105   -245       C
ATOM    167  CH2 TRP A 358     -63.793   2.854 -44.886  1.00 29.67           C
ANISOU  167  CH2 TRP A 358     3656   3822   3794   -320   1170   -285       C
ATOM    168  N   SER A 359     -65.342   5.314 -51.618  1.00 38.16           N
ANISOU  168  N   SER A 359     4956   4934   4609    -17    223   -446       N
ATOM    169  CA  SER A 359     -66.288   6.406 -51.476  1.00 41.06           C
ANISOU  169  CA  SER A 359     5172   5323   5106     78     29   -481       C
ATOM    170  C   SER A 359     -67.446   6.203 -52.453  1.00 45.94           C
ANISOU  170  C   SER A 359     5765   5912   5778     78   -275   -594       C
ATOM    171  O   SER A 359     -68.611   6.239 -52.067  1.00 36.87           O
ANISOU  171  O   SER A 359     4334   4806   4870     93   -386   -723       O
ATOM    172  CB  SER A 359     -65.597   7.755 -51.696  1.00 37.62           C
ANISOU  172  CB  SER A 359     4904   4846   4544    179    -21   -374       C
ATOM    173  OG  SER A 359     -66.472   8.830 -51.384  1.00 40.54           O
ANISOU  173  OG  SER A 359     5111   5217   5076    296   -213   -420       O
ATOM    174  N   VAL A 360     -67.107   5.960 -53.711  1.00 49.41           N
ANISOU  174  N   VAL A 360     6499   6280   5997     49   -400   -565       N
ATOM    175  CA  VAL A 360     -68.094   5.648 -54.739  1.00 51.74           C
ANISOU  175  CA  VAL A 360     6834   6524   6301     40   -718   -668       C
ATOM    176  C   VAL A 360     -69.019   4.493 -54.327  1.00 51.10           C
ANISOU  176  C   VAL A 360     6467   6496   6454    -55   -693   -815       C
ATOM    177  O   VAL A 360     -70.237   4.613 -54.414  1.00 56.01           O
ANISOU  177  O   VAL A 360     6862   7124   7293    -24   -935   -956       O
ATOM    178  CB  VAL A 360     -67.406   5.353 -56.100  1.00 61.02           C
ANISOU  178  CB  VAL A 360     8429   7615   7141    -22   -780   -616       C
ATOM    179  CG1 VAL A 360     -68.316   4.544 -57.008  1.00 65.96           C
ANISOU  179  CG1 VAL A 360     9092   8195   7774    -75  -1042   -741       C
ATOM    180  CG2 VAL A 360     -66.988   6.654 -56.781  1.00 56.51           C
ANISOU  180  CG2 VAL A 360     8167   6958   6345     44   -936   -505       C
ATOM    181  N   ASN A 361     -68.441   3.396 -53.847  1.00 49.72           N
ANISOU  181  N   ASN A 361     6295   6343   6253   -173   -408   -797       N
ATOM    182  CA  ASN A 361     -69.226   2.229 -53.444  1.00 50.71           C
ANISOU  182  CA  ASN A 361     6209   6492   6565   -306   -355   -917       C
ATOM    183  C   ASN A 361     -70.080   2.413 -52.184  1.00 51.43           C
ANISOU  183  C   ASN A 361     5928   6671   6942   -342   -246  -1001       C
ATOM    184  O   ASN A 361     -71.100   1.748 -52.021  1.00 52.05           O
ANISOU  184  O   ASN A 361     5780   6774   7221   -457   -276  -1149       O
ATOM    185  CB  ASN A 361     -68.325   1.003 -53.285  1.00 49.21           C
ANISOU  185  CB  ASN A 361     6180   6260   6259   -418   -114   -867       C
ATOM    186  CG  ASN A 361     -67.945   0.385 -54.616  1.00 49.89           C
ANISOU  186  CG  ASN A 361     6551   6265   6138   -442   -230   -890       C
ATOM    187  OD1 ASN A 361     -68.743  -0.316 -55.230  1.00 56.51           O
ANISOU  187  OD1 ASN A 361     7371   7072   7028   -516   -401  -1003       O
ATOM    188  ND2 ASN A 361     -66.726   0.639 -55.067  1.00 47.11           N
ANISOU  188  ND2 ASN A 361     6459   5883   5557   -393   -123   -806       N
ATOM    189  N   SER A 362     -69.665   3.310 -51.294  1.00 46.26           N
ANISOU  189  N   SER A 362     5211   6063   6303   -262   -102   -926       N
ATOM    190  CA  SER A 362     -70.393   3.542 -50.048  1.00 42.73           C
ANISOU  190  CA  SER A 362     4440   5705   6090   -309     50  -1020       C
ATOM    191  C   SER A 362     -71.619   4.406 -50.280  1.00 46.96           C
ANISOU  191  C   SER A 362     4688   6280   6874   -206   -205  -1197       C
ATOM    192  O   SER A 362     -72.398   4.638 -49.360  1.00 49.25           O
ANISOU  192  O   SER A 362     4654   6656   7402   -246    -88  -1341       O
ATOM    193  CB  SER A 362     -69.501   4.242 -49.019  1.00 37.12           C
ANISOU  193  CB  SER A 362     3784   5021   5301   -249    273   -891       C
ATOM    194  OG  SER A 362     -69.221   5.582 -49.406  1.00 35.82           O
ANISOU  194  OG  SER A 362     3680   4840   5089    -59    106   -839       O
ATOM    195  N   VAL A 363     -71.772   4.868 -51.519  1.00 49.20           N
ANISOU  195  N   VAL A 363     5107   6489   7096    -78   -560  -1202       N
ATOM    196  CA  VAL A 363     -72.751   5.890 -51.901  1.00 54.87           C
ANISOU  196  CA  VAL A 363     5630   7190   8027     87   -909  -1349       C
ATOM    197  C   VAL A 363     -72.979   6.978 -50.842  1.00 55.69           C
ANISOU  197  C   VAL A 363     5479   7360   8322    195   -812  -1409       C
ATOM    198  O   VAL A 363     -74.069   7.123 -50.301  1.00 53.62           O
ANISOU  198  O   VAL A 363     4812   7169   8391    195   -826  -1643       O
ATOM    199  CB  VAL A 363     -74.090   5.281 -52.435  1.00 76.96           C
ANISOU  199  CB  VAL A 363     8161   9989  11089     33  -1163  -1592       C
ATOM    200  CG1 VAL A 363     -73.851   4.570 -53.765  1.00 76.78           C
ANISOU  200  CG1 VAL A 363     8472   9863  10837     -7  -1389  -1527       C
ATOM    201  CG2 VAL A 363     -74.734   4.331 -51.427  1.00 78.15           C
ANISOU  201  CG2 VAL A 363     7964  10255  11475   -185   -843  -1749       C
ATOM    202  N   GLY A 364     -71.926   7.729 -50.536  1.00 60.93           N
ANISOU  202  N   GLY A 364     6368   7999   8784    276   -696  -1220       N
ATOM    203  CA  GLY A 364     -72.053   8.874 -49.649  1.00 64.15           C
ANISOU  203  CA  GLY A 364     6592   8441   9340    402   -646  -1268       C
ATOM    204  C   GLY A 364     -71.796   8.646 -48.167  1.00 60.92           C
ANISOU  204  C   GLY A 364     6029   8147   8971    285   -216  -1273       C
ATOM    205  O   GLY A 364     -71.805   9.595 -47.384  1.00 62.62           O
ANISOU  205  O   GLY A 364     6123   8392   9278    382   -146  -1311       O
ATOM    206  N   LYS A 365     -71.573   7.399 -47.772  1.00 54.96           N
ANISOU  206  N   LYS A 365     5310   7436   8136     74     55  -1237       N
ATOM    207  CA  LYS A 365     -71.289   7.090 -46.373  1.00 49.05           C
ANISOU  207  CA  LYS A 365     4505   6762   7369    -65    440  -1218       C
ATOM    208  C   LYS A 365     -69.857   7.494 -46.025  1.00 42.75           C
ANISOU  208  C   LYS A 365     4012   5915   6315     -1    556   -984       C
ATOM    209  O   LYS A 365     -69.576   7.957 -44.920  1.00 38.51           O
ANISOU  209  O   LYS A 365     3441   5419   5772     -3    756   -968       O
ATOM    210  CB  LYS A 365     -71.489   5.594 -46.103  1.00 49.42           C
ANISOU  210  CB  LYS A 365     4559   6826   7394   -321    646  -1238       C
ATOM    211  CG  LYS A 365     -72.919   5.108 -46.265  1.00 55.07           C
ANISOU  211  CG  LYS A 365     4931   7601   8391   -440    596  -1497       C
ATOM    212  CD  LYS A 365     -73.844   5.772 -45.258  1.00 57.29           C
ANISOU  212  CD  LYS A 365     4834   7999   8936   -463    755  -1730       C
ATOM    213  CE  LYS A 365     -75.287   5.307 -45.446  1.00 63.97           C
ANISOU  213  CE  LYS A 365     5275   8913  10117   -590    714  -2038       C
ATOM    214  NZ  LYS A 365     -76.240   6.090 -44.601  1.00 65.44           N
ANISOU  214  NZ  LYS A 365     5031   9220  10614   -579    848  -2330       N
ATOM    215  N   ILE A 366     -68.961   7.315 -46.990  1.00 42.31           N
ANISOU  215  N   ILE A 366     4247   5773   6054     47    434   -825       N
ATOM    216  CA  ILE A 366     -67.538   7.559 -46.800  1.00 36.42           C
ANISOU  216  CA  ILE A 366     3767   4978   5092     88    545   -633       C
ATOM    217  C   ILE A 366     -67.062   8.684 -47.714  1.00 36.74           C
ANISOU  217  C   ILE A 366     3971   4952   5035    249    327   -552       C
ATOM    218  O   ILE A 366     -67.398   8.709 -48.899  1.00 38.68           O
ANISOU  218  O   ILE A 366     4306   5146   5243    283     88   -570       O
ATOM    219  CB  ILE A 366     -66.721   6.287 -47.134  1.00 35.81           C
ANISOU  219  CB  ILE A 366     3906   4847   4852    -25    645   -540       C
ATOM    220  CG1 ILE A 366     -67.132   5.125 -46.227  1.00 33.89           C
ANISOU  220  CG1 ILE A 366     3578   4625   4672   -208    842   -592       C
ATOM    221  CG2 ILE A 366     -65.211   6.556 -47.041  1.00 28.91           C
ANISOU  221  CG2 ILE A 366     3261   3920   3805     32    739   -387       C
ATOM    222  CD1 ILE A 366     -66.809   5.341 -44.758  1.00 37.41           C
ANISOU  222  CD1 ILE A 366     4009   5095   5110   -251   1064   -553       C
ATOM    223  N   GLU A 367     -66.286   9.613 -47.162  1.00 36.44           N
ANISOU  223  N   GLU A 367     4005   4901   4941    329    401   -462       N
ATOM    224  CA  GLU A 367     -65.604  10.616 -47.972  1.00 39.80           C
ANISOU  224  CA  GLU A 367     4652   5242   5230    430    248   -356       C
ATOM    225  C   GLU A 367     -64.097  10.539 -47.739  1.00 40.20           C
ANISOU  225  C   GLU A 367     4896   5268   5110    390    451   -218       C
ATOM    226  O   GLU A 367     -63.648   9.988 -46.733  1.00 43.04           O
ANISOU  226  O   GLU A 367     5196   5665   5493    337    658   -206       O
ATOM    227  CB  GLU A 367     -66.130  12.011 -47.657  1.00 43.92           C
ANISOU  227  CB  GLU A 367     5065   5742   5881    577     92   -404       C
ATOM    228  CG  GLU A 367     -67.622  12.161 -47.915  1.00 55.83           C
ANISOU  228  CG  GLU A 367     6334   7261   7618    648   -147   -588       C
ATOM    229  CD  GLU A 367     -68.145  13.558 -47.626  1.00 63.86           C
ANISOU  229  CD  GLU A 367     7232   8231   8801    826   -337   -669       C
ATOM    230  OE1 GLU A 367     -67.463  14.329 -46.911  1.00 67.61           O
ANISOU  230  OE1 GLU A 367     7758   8694   9234    871   -216   -597       O
ATOM    231  OE2 GLU A 367     -69.246  13.884 -48.119  1.00 65.28           O
ANISOU  231  OE2 GLU A 367     7260   8372   9172    931   -634   -821       O
ATOM    232  N   CYS A 368     -63.322  11.101 -48.662  1.00 33.27           N
ANISOU  232  N   CYS A 368     4259   4316   4065    405    381   -126       N
ATOM    233  CA  CYS A 368     -61.873  10.980 -48.619  1.00 36.55           C
ANISOU  233  CA  CYS A 368     4825   4712   4352    352    576    -41       C
ATOM    234  C   CYS A 368     -61.112  12.297 -48.483  1.00 36.98           C
ANISOU  234  C   CYS A 368     4981   4715   4356    400    582     40       C
ATOM    235  O   CYS A 368     -61.465  13.311 -49.088  1.00 43.06           O
ANISOU  235  O   CYS A 368     5868   5415   5076    447    394     72       O
ATOM    236  CB  CYS A 368     -61.383  10.226 -49.855  1.00 45.58           C
ANISOU  236  CB  CYS A 368     6171   5823   5326    259    594    -37       C
ATOM    237  SG  CYS A 368     -61.951   8.516 -49.879  1.00 56.43           S
ANISOU  237  SG  CYS A 368     7445   7235   6761    186    631   -130       S
ATOM    238  N   VAL A 369     -60.060  12.260 -47.672  1.00 30.69           N
ANISOU  238  N   VAL A 369     4152   3932   3578    386    774     68       N
ATOM    239  CA  VAL A 369     -59.101  13.352 -47.563  1.00 30.99           C
ANISOU  239  CA  VAL A 369     4285   3919   3571    396    820    133       C
ATOM    240  C   VAL A 369     -57.709  12.693 -47.595  1.00 31.39           C
ANISOU  240  C   VAL A 369     4370   3971   3584    317   1029    124       C
ATOM    241  O   VAL A 369     -57.582  11.534 -47.216  1.00 27.40           O
ANISOU  241  O   VAL A 369     3776   3498   3137    305   1108     73       O
ATOM    242  CB  VAL A 369     -59.347  14.154 -46.258  1.00 37.90           C
ANISOU  242  CB  VAL A 369     5011   4807   4583    494    805    130       C
ATOM    243  CG1 VAL A 369     -58.181  15.070 -45.939  1.00 40.23           C
ANISOU  243  CG1 VAL A 369     5378   5050   4858    490    882    186       C
ATOM    244  CG2 VAL A 369     -60.628  14.968 -46.391  1.00 33.69           C
ANISOU  244  CG2 VAL A 369     4430   4252   4117    589    588     98       C
ATOM    245  N   SER A 370     -56.677  13.377 -48.084  1.00 34.87           N
ANISOU  245  N   SER A 370     4940   4367   3943    254   1112    152       N
ATOM    246  CA  SER A 370     -55.344  12.769 -48.033  1.00 37.14           C
ANISOU  246  CA  SER A 370     5188   4662   4263    193   1314     88       C
ATOM    247  C   SER A 370     -54.261  13.612 -47.370  1.00 32.31           C
ANISOU  247  C   SER A 370     4522   4022   3733    194   1402     92       C
ATOM    248  O   SER A 370     -54.396  14.825 -47.200  1.00 27.67           O
ANISOU  248  O   SER A 370     3995   3395   3125    207   1332    163       O
ATOM    249  CB  SER A 370     -54.886  12.217 -49.396  1.00 44.00           C
ANISOU  249  CB  SER A 370     6208   5526   4983     65   1424     30       C
ATOM    250  OG  SER A 370     -55.280  13.022 -50.490  1.00 48.22           O
ANISOU  250  OG  SER A 370     6995   6015   5314    -19   1348     98       O
ATOM    251  N   ALA A 371     -53.198  12.940 -46.957  1.00 32.53           N
ANISOU  251  N   ALA A 371     4425   4055   3879    192   1529      0       N
ATOM    252  CA  ALA A 371     -52.039  13.612 -46.395  1.00 28.68           C
ANISOU  252  CA  ALA A 371     3855   3538   3503    184   1608    -35       C
ATOM    253  C   ALA A 371     -50.854  12.723 -46.701  1.00 30.36           C
ANISOU  253  C   ALA A 371     3962   3752   3820    139   1765   -194       C
ATOM    254  O   ALA A 371     -51.031  11.557 -47.064  1.00 32.70           O
ANISOU  254  O   ALA A 371     4247   4063   4115    152   1778   -260       O
ATOM    255  CB  ALA A 371     -52.202  13.791 -44.894  1.00 26.91           C
ANISOU  255  CB  ALA A 371     3515   3300   3408    312   1492     -2       C
ATOM    256  N   GLU A 372     -49.648  13.256 -46.546  1.00 33.29           N
ANISOU  256  N   GLU A 372     4236   4101   4310     92   1876   -280       N
ATOM    257  CA  GLU A 372     -48.461  12.519 -46.954  1.00 35.04           C
ANISOU  257  CA  GLU A 372     4316   4327   4672     43   2025   -481       C
ATOM    258  C   GLU A 372     -47.828  11.642 -45.871  1.00 37.94           C
ANISOU  258  C   GLU A 372     4469   4647   5300    201   1914   -594       C
ATOM    259  O   GLU A 372     -47.037  10.754 -46.198  1.00 36.18           O
ANISOU  259  O   GLU A 372     4128   4414   5206    203   1935   -763       O
ATOM    260  CB  GLU A 372     -47.429  13.449 -47.608  1.00 39.41           C
ANISOU  260  CB  GLU A 372     4869   4881   5223   -135   2177   -552       C
ATOM    261  CG  GLU A 372     -47.903  14.047 -48.947  1.00 47.39           C
ANISOU  261  CG  GLU A 372     6159   5904   5942   -324   2285   -468       C
ATOM    262  CD  GLU A 372     -48.465  12.993 -49.911  1.00 55.87           C
ANISOU  262  CD  GLU A 372     7344   7012   6872   -346   2294   -498       C
ATOM    263  OE1 GLU A 372     -49.658  13.096 -50.299  1.00 53.18           O
ANISOU  263  OE1 GLU A 372     7223   6669   6315   -344   2227   -359       O
ATOM    264  OE2 GLU A 372     -47.711  12.062 -50.276  1.00 59.13           O
ANISOU  264  OE2 GLU A 372     7625   7444   7397   -361   2362   -672       O
ATOM    265  N   THR A 373     -48.168  11.877 -44.600  1.00 25.58           N
ANISOU  265  N   THR A 373     2887   3039   3792    326   1736   -495       N
ATOM    266  CA  THR A 373     -47.696  11.008 -43.512  1.00 29.15           C
ANISOU  266  CA  THR A 373     3224   3409   4441    475   1570   -571       C
ATOM    267  C   THR A 373     -48.823  10.701 -42.534  1.00 29.16           C
ANISOU  267  C   THR A 373     3360   3387   4333    557   1386   -407       C
ATOM    268  O   THR A 373     -49.809  11.428 -42.479  1.00 27.95           O
ANISOU  268  O   THR A 373     3314   3289   4018    523   1385   -264       O
ATOM    269  CB  THR A 373     -46.551  11.650 -42.688  1.00 37.51           C
ANISOU  269  CB  THR A 373     4126   4409   5717    522   1509   -663       C
ATOM    270  OG1 THR A 373     -47.084  12.703 -41.868  1.00 33.57           O
ANISOU  270  OG1 THR A 373     3724   3910   5119    536   1413   -502       O
ATOM    271  CG2 THR A 373     -45.440  12.196 -43.595  1.00 32.51           C
ANISOU  271  CG2 THR A 373     3349   3816   5188    385   1714   -827       C
ATOM    272  N   THR A 374     -48.665   9.628 -41.761  1.00 27.92           N
ANISOU  272  N   THR A 374     3205   3135   4270    657   1231   -444       N
ATOM    273  CA  THR A 374     -49.632   9.247 -40.749  1.00 25.91           C
ANISOU  273  CA  THR A 374     3104   2843   3898    692   1088   -306       C
ATOM    274  C   THR A 374     -49.856  10.368 -39.724  1.00 30.61           C
ANISOU  274  C   THR A 374     3745   3447   4437    707   1029   -209       C
ATOM    275  O   THR A 374     -50.997  10.662 -39.347  1.00 29.12           O
ANISOU  275  O   THR A 374     3661   3312   4091    673   1039    -94       O
ATOM    276  CB  THR A 374     -49.216   7.937 -40.041  1.00 27.77           C
ANISOU  276  CB  THR A 374     3391   2925   4236    780    902   -363       C
ATOM    277  OG1 THR A 374     -49.254   6.862 -40.986  1.00 25.21           O
ANISOU  277  OG1 THR A 374     3049   2589   3942    765    957   -447       O
ATOM    278  CG2 THR A 374     -50.165   7.605 -38.875  1.00 24.24           C
ANISOU  278  CG2 THR A 374     3159   2422   3627    765    781   -214       C
ATOM    279  N   GLU A 375     -48.766  10.998 -39.293  1.00 30.07           N
ANISOU  279  N   GLU A 375     3579   3329   4517    754    973   -283       N
ATOM    280  CA  GLU A 375     -48.856  12.120 -38.362  1.00 29.72           C
ANISOU  280  CA  GLU A 375     3579   3283   4431    770    912   -213       C
ATOM    281  C   GLU A 375     -49.695  13.258 -38.946  1.00 28.99           C
ANISOU  281  C   GLU A 375     3508   3302   4203    695   1051   -124       C
ATOM    282  O   GLU A 375     -50.606  13.744 -38.278  1.00 27.60           O
ANISOU  282  O   GLU A 375     3426   3152   3908    702   1021    -36       O
ATOM    283  CB  GLU A 375     -47.462  12.592 -37.880  1.00 31.61           C
ANISOU  283  CB  GLU A 375     3688   3438   4883    828    810   -332       C
ATOM    284  CG  GLU A 375     -46.780  11.573 -36.925  1.00 27.42           C
ANISOU  284  CG  GLU A 375     3191   2749   4479    944    558   -405       C
ATOM    285  CD  GLU A 375     -45.534  12.104 -36.194  1.00 37.24           C
ANISOU  285  CD  GLU A 375     4318   3890   5940   1023    381   -524       C
ATOM    286  OE1 GLU A 375     -45.044  13.213 -36.522  1.00 39.57           O
ANISOU  286  OE1 GLU A 375     4467   4245   6323    969    492   -575       O
ATOM    287  OE2 GLU A 375     -45.052  11.401 -35.272  1.00 37.33           O
ANISOU  287  OE2 GLU A 375     4409   3742   6033   1132    106   -567       O
ATOM    288  N   ASP A 376     -49.430  13.637 -40.199  1.00 22.42           N
ANISOU  288  N   ASP A 376     2610   2524   3386    618   1196   -160       N
ATOM    289  CA  ASP A 376     -50.191  14.704 -40.854  1.00 23.49           C
ANISOU  289  CA  ASP A 376     2816   2722   3388    551   1273    -71       C
ATOM    290  C   ASP A 376     -51.681  14.379 -40.863  1.00 22.51           C
ANISOU  290  C   ASP A 376     2783   2652   3119    565   1244     17       C
ATOM    291  O   ASP A 376     -52.510  15.240 -40.617  1.00 30.26           O
ANISOU  291  O   ASP A 376     3809   3656   4033    583   1209     80       O
ATOM    292  CB  ASP A 376     -49.715  14.948 -42.291  1.00 22.86           C
ANISOU  292  CB  ASP A 376     2729   2667   3287    431   1432   -116       C
ATOM    293  CG  ASP A 376     -48.325  15.574 -42.360  1.00 37.76           C
ANISOU  293  CG  ASP A 376     4506   4515   5324    369   1513   -222       C
ATOM    294  OD1 ASP A 376     -47.795  16.017 -41.319  1.00 32.03           O
ANISOU  294  OD1 ASP A 376     3710   3738   4723    433   1411   -246       O
ATOM    295  OD2 ASP A 376     -47.761  15.638 -43.471  1.00 40.44           O
ANISOU  295  OD2 ASP A 376     4835   4875   5655    236   1689   -296       O
ATOM    296  N   CYS A 377     -51.999  13.121 -41.149  1.00 25.41           N
ANISOU  296  N   CYS A 377     3157   3032   3465    558   1254     -3       N
ATOM    297  CA  CYS A 377     -53.372  12.637 -41.131  1.00 21.12           C
ANISOU  297  CA  CYS A 377     2668   2539   2818    550   1235     51       C
ATOM    298  C   CYS A 377     -53.997  12.689 -39.729  1.00 23.38           C
ANISOU  298  C   CYS A 377     2986   2819   3078    586   1176     83       C
ATOM    299  O   CYS A 377     -55.164  13.050 -39.581  1.00 28.08           O
ANISOU  299  O   CYS A 377     3580   3474   3614    577   1186    105       O
ATOM    300  CB  CYS A 377     -53.416  11.199 -41.645  1.00 21.15           C
ANISOU  300  CB  CYS A 377     2683   2533   2821    520   1254     10       C
ATOM    301  SG  CYS A 377     -53.943  11.001 -43.355  1.00 32.61           S
ANISOU  301  SG  CYS A 377     4166   4044   4180    443   1324     -2       S
ATOM    302  N   ILE A 378     -53.235  12.304 -38.708  1.00 25.90           N
ANISOU  302  N   ILE A 378     3340   3058   3443    620   1110     67       N
ATOM    303  CA  ILE A 378     -53.753  12.340 -37.339  1.00 23.59           C
ANISOU  303  CA  ILE A 378     3142   2745   3075    622   1069     96       C
ATOM    304  C   ILE A 378     -54.063  13.783 -36.958  1.00 27.81           C
ANISOU  304  C   ILE A 378     3647   3323   3596    653   1083    102       C
ATOM    305  O   ILE A 378     -55.129  14.060 -36.425  1.00 23.33           O
ANISOU  305  O   ILE A 378     3097   2811   2955    633   1129     99       O
ATOM    306  CB  ILE A 378     -52.775  11.742 -36.309  1.00 21.79           C
ANISOU  306  CB  ILE A 378     3017   2384   2876    658    936     84       C
ATOM    307  CG1 ILE A 378     -52.659  10.229 -36.488  1.00 22.37           C
ANISOU  307  CG1 ILE A 378     3164   2380   2956    636    886     77       C
ATOM    308  CG2 ILE A 378     -53.238  12.044 -34.880  1.00 22.31           C
ANISOU  308  CG2 ILE A 378     3238   2425   2814    637    905    116       C
ATOM    309  CD1 ILE A 378     -51.487   9.624 -35.741  1.00 23.46           C
ANISOU  309  CD1 ILE A 378     3389   2346   3179    710    687     41       C
ATOM    310  N   ALA A 379     -53.145  14.701 -37.259  1.00 26.63           N
ANISOU  310  N   ALA A 379     3442   3143   3532    693   1053     88       N
ATOM    311  CA  ALA A 379     -53.395  16.125 -37.009  1.00 27.82           C
ANISOU  311  CA  ALA A 379     3581   3308   3682    725   1046     93       C
ATOM    312  C   ALA A 379     -54.697  16.615 -37.657  1.00 27.91           C
ANISOU  312  C   ALA A 379     3559   3395   3650    723   1087    103       C
ATOM    313  O   ALA A 379     -55.416  17.440 -37.069  1.00 25.94           O
ANISOU  313  O   ALA A 379     3302   3163   3389    765   1076     77       O
ATOM    314  CB  ALA A 379     -52.217  16.969 -37.472  1.00 22.60           C
ANISOU  314  CB  ALA A 379     2873   2592   3121    727   1026     79       C
ATOM    315  N   LYS A 380     -55.006  16.100 -38.853  1.00 32.91           N
ANISOU  315  N   LYS A 380     4170   4063   4270    684   1117    120       N
ATOM    316  CA  LYS A 380     -56.237  16.490 -39.568  1.00 24.70           C
ANISOU  316  CA  LYS A 380     3102   3072   3209    696   1096    117       C
ATOM    317  C   LYS A 380     -57.475  15.940 -38.905  1.00 32.55           C
ANISOU  317  C   LYS A 380     4036   4138   4193    691   1131     63       C
ATOM    318  O   LYS A 380     -58.528  16.592 -38.907  1.00 36.48           O
ANISOU  318  O   LYS A 380     4459   4672   4731    738   1098      6       O
ATOM    319  CB  LYS A 380     -56.231  16.030 -41.032  1.00 30.68           C
ANISOU  319  CB  LYS A 380     3890   3837   3931    642   1097    144       C
ATOM    320  CG  LYS A 380     -55.164  16.674 -41.923  1.00 37.61           C
ANISOU  320  CG  LYS A 380     4847   4652   4790    597   1109    180       C
ATOM    321  CD  LYS A 380     -55.501  16.484 -43.409  1.00 38.34           C
ANISOU  321  CD  LYS A 380     5032   4747   4791    532   1098    204       C
ATOM    322  CE  LYS A 380     -54.476  17.153 -44.309  1.00 43.21           C
ANISOU  322  CE  LYS A 380     5771   5299   5347    434   1157    233       C
ATOM    323  NZ  LYS A 380     -55.026  17.426 -45.664  1.00 50.14           N
ANISOU  323  NZ  LYS A 380     6829   6143   6080    369   1092    282       N
ATOM    324  N   ILE A 381     -57.363  14.728 -38.362  1.00 26.26           N
ANISOU  324  N   ILE A 381     3173   3306   3498    892   1038     39       N
ATOM    325  CA  ILE A 381     -58.464  14.148 -37.610  1.00 25.01           C
ANISOU  325  CA  ILE A 381     2960   3198   3343    929   1096     23       C
ATOM    326  C   ILE A 381     -58.703  14.972 -36.355  1.00 30.67           C
ANISOU  326  C   ILE A 381     3716   3934   4003   1029   1049     34       C
ATOM    327  O   ILE A 381     -59.862  15.258 -35.997  1.00 28.32           O
ANISOU  327  O   ILE A 381     3390   3689   3680   1086   1054      2       O
ATOM    328  CB  ILE A 381     -58.229  12.652 -37.259  1.00 25.04           C
ANISOU  328  CB  ILE A 381     2920   3180   3412    886   1224     54       C
ATOM    329  CG1 ILE A 381     -58.274  11.794 -38.536  1.00 24.06           C
ANISOU  329  CG1 ILE A 381     2757   3040   3345    789   1277     14       C
ATOM    330  CG2 ILE A 381     -59.295  12.165 -36.276  1.00 24.45           C
ANISOU  330  CG2 ILE A 381     2804   3142   3343    928   1307     57       C
ATOM    331  CD1 ILE A 381     -57.932  10.313 -38.323  1.00 24.13           C
ANISOU  331  CD1 ILE A 381     2738   2996   3434    743   1410     41       C
ATOM    332  N   MET A 382     -57.608  15.374 -35.704  1.00 31.39           N
ANISOU  332  N   MET A 382     3866   3985   4076   1054    999     66       N
ATOM    333  CA  MET A 382     -57.685  16.209 -34.497  1.00 28.65           C
ANISOU  333  CA  MET A 382     3577   3650   3659   1153    936     60       C
ATOM    334  C   MET A 382     -58.440  17.500 -34.767  1.00 24.53           C
ANISOU  334  C   MET A 382     3090   3134   3096   1201    855     10       C
ATOM    335  O   MET A 382     -59.264  17.921 -33.961  1.00 27.97           O
ANISOU  335  O   MET A 382     3541   3607   3477   1293    854    -14       O
ATOM    336  CB  MET A 382     -56.289  16.573 -33.989  1.00 33.54           C
ANISOU  336  CB  MET A 382     4243   4223   4279   1157    857     76       C
ATOM    337  CG  MET A 382     -55.511  15.439 -33.362  1.00 31.64           C
ANISOU  337  CG  MET A 382     3982   3984   4057   1162    911    129       C
ATOM    338  SD  MET A 382     -53.784  15.923 -33.137  1.00 26.40           S
ANISOU  338  SD  MET A 382     3325   3273   3431   1146    792    125       S
ATOM    339  CE  MET A 382     -53.939  17.177 -31.866  1.00 25.53           C
ANISOU  339  CE  MET A 382     3303   3179   3218   1251    660     66       C
ATOM    340  N   ASN A 383     -58.157  18.135 -35.901  1.00 24.33           N
ANISOU  340  N   ASN A 383     3086   3066   3092   1151    798      0       N
ATOM    341  CA  ASN A 383     -58.737  19.445 -36.162  1.00 31.88           C
ANISOU  341  CA  ASN A 383     4099   4006   4008   1212    715    -34       C
ATOM    342  C   ASN A 383     -60.048  19.450 -36.951  1.00 30.75           C
ANISOU  342  C   ASN A 383     3908   3924   3852   1242    722    -62       C
ATOM    343  O   ASN A 383     -60.644  20.497 -37.123  1.00 33.50           O
ANISOU  343  O   ASN A 383     4300   4264   4163   1319    653    -86       O
ATOM    344  CB  ASN A 383     -57.710  20.428 -36.755  1.00 31.85           C
ANISOU  344  CB  ASN A 383     4177   3903   4022   1167    642    -21       C
ATOM    345  CG  ASN A 383     -57.336  20.116 -38.206  1.00 34.31           C
ANISOU  345  CG  ASN A 383     4482   4192   4364   1078    675     10       C
ATOM    346  OD1 ASN A 383     -58.104  19.512 -38.962  1.00 29.06           O
ANISOU  346  OD1 ASN A 383     3772   3587   3685   1071    711      1       O
ATOM    347  ND2 ASN A 383     -56.144  20.553 -38.601  1.00 28.56           N
ANISOU  347  ND2 ASN A 383     3797   3376   3678   1008    664     37       N
ATOM    348  N   GLY A 384     -60.481  18.285 -37.427  1.00 28.89           N
ANISOU  348  N   GLY A 384     3579   3745   3654   1186    797    -67       N
ATOM    349  CA  GLY A 384     -61.761  18.164 -38.095  1.00 26.37           C
ANISOU  349  CA  GLY A 384     3183   3500   3336   1210    792   -115       C
ATOM    350  C   GLY A 384     -61.693  18.159 -39.619  1.00 30.79           C
ANISOU  350  C   GLY A 384     3756   4059   3885   1159    746   -126       C
ATOM    351  O   GLY A 384     -62.727  18.069 -40.282  1.00 33.00           O
ANISOU  351  O   GLY A 384     3969   4411   4158   1185    713   -178       O
ATOM    352  N   GLU A 385     -60.494  18.271 -40.182  1.00 29.91           N
ANISOU  352  N   GLU A 385     3727   3871   3766   1096    744    -81       N
ATOM    353  CA  GLU A 385     -60.328  18.149 -41.631  1.00 38.80           C
ANISOU  353  CA  GLU A 385     4886   4995   4861   1049    727    -83       C
ATOM    354  C   GLU A 385     -60.607  16.721 -42.088  1.00 38.73           C
ANISOU  354  C   GLU A 385     4781   5039   4895    969    798   -129       C
ATOM    355  O   GLU A 385     -61.067  16.504 -43.206  1.00 39.29           O
ANISOU  355  O   GLU A 385     4846   5154   4928    958    765   -174       O
ATOM    356  CB  GLU A 385     -58.933  18.587 -42.087  1.00 44.33           C
ANISOU  356  CB  GLU A 385     5691   5595   5556    994    741    -20       C
ATOM    357  CG  GLU A 385     -58.692  20.088 -42.041  1.00 56.68           C
ANISOU  357  CG  GLU A 385     7369   7082   7083   1054    669     16       C
ATOM    358  CD  GLU A 385     -57.295  20.470 -42.507  1.00 68.53           C
ANISOU  358  CD  GLU A 385     8953   8477   8610    976    707     76       C
ATOM    359  OE1 GLU A 385     -56.707  21.408 -41.919  1.00 73.83           O
ANISOU  359  OE1 GLU A 385     9679   9061   9313    982    678     98       O
ATOM    360  OE2 GLU A 385     -56.789  19.832 -43.461  1.00 68.01           O
ANISOU  360  OE2 GLU A 385     8891   8410   8538    907    772     93       O
ATOM    361  N   ALA A 386     -60.312  15.750 -41.228  1.00 34.95           N
ANISOU  361  N   ALA A 386     4239   4550   4490    921    893   -119       N
ATOM    362  CA  ALA A 386     -60.737  14.373 -41.473  1.00 34.48           C
ANISOU  362  CA  ALA A 386     4085   4523   4494    848    975   -169       C
ATOM    363  C   ALA A 386     -61.449  13.844 -40.233  1.00 32.11           C
ANISOU  363  C   ALA A 386     3695   4249   4255    867   1047   -174       C
ATOM    364  O   ALA A 386     -61.519  14.536 -39.219  1.00 30.45           O
ANISOU  364  O   ALA A 386     3509   4041   4020    944   1030   -139       O
ATOM    365  CB  ALA A 386     -59.548  13.484 -41.841  1.00 28.91           C
ANISOU  365  CB  ALA A 386     3409   3750   3827    761   1059   -138       C
ATOM    366  N   ASP A 387     -61.968  12.621 -40.308  1.00 32.05           N
ANISOU  366  N   ASP A 387     3594   4255   4329    796   1138   -219       N
ATOM    367  CA  ASP A 387     -62.676  12.028 -39.173  1.00 28.14           C
ANISOU  367  CA  ASP A 387     3017   3773   3901    804   1242   -212       C
ATOM    368  C   ASP A 387     -62.061  10.749 -38.645  1.00 28.61           C
ANISOU  368  C   ASP A 387     3080   3757   4032    740   1387   -162       C
ATOM    369  O   ASP A 387     -62.161  10.470 -37.461  1.00 27.21           O
ANISOU  369  O   ASP A 387     2904   3565   3870    777   1478   -104       O
ATOM    370  CB  ASP A 387     -64.138  11.765 -39.527  1.00 30.25           C
ANISOU  370  CB  ASP A 387     3143   4120   4232    782   1242   -313       C
ATOM    371  CG  ASP A 387     -64.892  13.045 -39.880  1.00 35.10           C
ANISOU  371  CG  ASP A 387     3743   4817   4777    881   1098   -357       C
ATOM    372  OD1 ASP A 387     -64.633  14.097 -39.233  1.00 31.10           O
ANISOU  372  OD1 ASP A 387     3318   4303   4197    981   1051   -300       O
ATOM    373  OD2 ASP A 387     -65.730  12.989 -40.812  1.00 39.52           O
ANISOU  373  OD2 ASP A 387     4214   5446   5356    865   1025   -453       O
ATOM    374  N   ALA A 388     -61.429   9.960 -39.505  1.00 32.52           N
ANISOU  374  N   ALA A 388     3592   4201   4565    656   1417   -180       N
ATOM    375  CA  ALA A 388     -61.035   8.626 -39.069  1.00 31.20           C
ANISOU  375  CA  ALA A 388     3419   3951   4486    601   1567   -142       C
ATOM    376  C   ALA A 388     -59.978   7.980 -39.957  1.00 31.34           C
ANISOU  376  C   ALA A 388     3486   3899   4522    540   1588   -146       C
ATOM    377  O   ALA A 388     -59.843   8.334 -41.133  1.00 30.65           O
ANISOU  377  O   ALA A 388     3417   3837   4392    512   1508   -207       O
ATOM    378  CB  ALA A 388     -62.272   7.726 -38.984  1.00 34.24           C
ANISOU  378  CB  ALA A 388     3688   4340   4981    530   1670   -210       C
ATOM    379  N   MET A 389     -59.239   7.030 -39.381  1.00 25.76           N
ANISOU  379  N   MET A 389     2810   3105   3873    534   1705    -76       N
ATOM    380  CA  MET A 389     -58.271   6.212 -40.122  1.00 25.76           C
ANISOU  380  CA  MET A 389     2846   3026   3916    485   1759    -80       C
ATOM    381  C   MET A 389     -57.899   5.008 -39.277  1.00 26.27           C
ANISOU  381  C   MET A 389     2926   2990   4065    492   1909     -5       C
ATOM    382  O   MET A 389     -58.150   4.990 -38.078  1.00 31.71           O
ANISOU  382  O   MET A 389     3626   3678   4744    549   1943     73       O
ATOM    383  CB  MET A 389     -57.013   7.015 -40.474  1.00 26.92           C
ANISOU  383  CB  MET A 389     3056   3180   3992    529   1674    -35       C
ATOM    384  CG  MET A 389     -56.125   7.320 -39.291  1.00 27.25           C
ANISOU  384  CG  MET A 389     3131   3205   4016    617   1663     75       C
ATOM    385  SD  MET A 389     -54.868   8.569 -39.630  1.00 25.35           S
ANISOU  385  SD  MET A 389     2929   2985   3717    650   1543    104       S
ATOM    386  CE  MET A 389     -53.861   7.666 -40.817  1.00 24.23           C
ANISOU  386  CE  MET A 389     2790   2775   3640    587   1633     84       C
ATOM    387  N   SER A 390     -57.312   3.994 -39.897  1.00 26.66           N
ANISOU  387  N   SER A 390     2995   2949   4185    441   1991    -25       N
ATOM    388  CA  SER A 390     -56.810   2.855 -39.147  1.00 27.28           C
ANISOU  388  CA  SER A 390     3122   2916   4326    455   2082     64       C
ATOM    389  C   SER A 390     -55.315   3.038 -38.874  1.00 32.79           C
ANISOU  389  C   SER A 390     3872   3597   4990    545   2045    156       C
ATOM    390  O   SER A 390     -54.570   3.482 -39.747  1.00 29.34           O
ANISOU  390  O   SER A 390     3432   3184   4533    538   1996    120       O
ATOM    391  CB  SER A 390     -57.069   1.562 -39.907  1.00 28.28           C
ANISOU  391  CB  SER A 390     3243   2935   4566    353   2193    -16       C
ATOM    392  OG  SER A 390     -56.823   0.458 -39.066  1.00 31.52           O
ANISOU  392  OG  SER A 390     3706   3219   5049    374   2306     78       O
ATOM    393  N   LEU A 391     -54.879   2.713 -37.659  1.00 30.16           N
ANISOU  393  N   LEU A 391     3580   3227   4651    636   2076    274       N
ATOM    394  CA  LEU A 391     -53.514   3.030 -37.230  1.00 26.86           C
ANISOU  394  CA  LEU A 391     3182   2821   4205    744   2027    354       C
ATOM    395  C   LEU A 391     -52.833   1.839 -36.600  1.00 30.58           C
ANISOU  395  C   LEU A 391     3701   3186   4733    814   2123    451       C
ATOM    396  O   LEU A 391     -53.469   1.069 -35.888  1.00 33.99           O
ANISOU  396  O   LEU A 391     4178   3551   5185    826   2223    506       O
ATOM    397  CB  LEU A 391     -53.541   4.149 -36.185  1.00 35.08           C
ANISOU  397  CB  LEU A 391     4224   3955   5148    848   1943    405       C
ATOM    398  CG  LEU A 391     -53.982   5.528 -36.640  1.00 33.60           C
ANISOU  398  CG  LEU A 391     4006   3867   4893    812   1819    331       C
ATOM    399  CD1 LEU A 391     -53.898   6.507 -35.492  1.00 25.45           C
ANISOU  399  CD1 LEU A 391     3002   2904   3762    911   1709    378       C
ATOM    400  CD2 LEU A 391     -53.068   5.946 -37.769  1.00 32.48           C
ANISOU  400  CD2 LEU A 391     3841   3728   4773    766   1761    285       C
ATOM    401  N   ASP A 392     -51.532   1.695 -36.842  1.00 29.69           N
ANISOU  401  N   ASP A 392     3576   3053   4651    870   2103    478       N
ATOM    402  CA  ASP A 392     -50.726   0.769 -36.053  1.00 34.09           C
ANISOU  402  CA  ASP A 392     4175   3533   5247    990   2169    589       C
ATOM    403  C   ASP A 392     -50.738   1.203 -34.569  1.00 34.60           C
ANISOU  403  C   ASP A 392     4273   3655   5217   1142   2132    693       C
ATOM    404  O   ASP A 392     -50.833   2.393 -34.256  1.00 32.33           O
ANISOU  404  O   ASP A 392     3960   3479   4845   1164   2009    669       O
ATOM    405  CB  ASP A 392     -49.293   0.685 -36.616  1.00 34.00           C
ANISOU  405  CB  ASP A 392     4114   3514   5290   1029   2131    585       C
ATOM    406  CG  ASP A 392     -48.310   0.078 -35.631  1.00 30.24           C
ANISOU  406  CG  ASP A 392     3655   3004   4832   1200   2141    704       C
ATOM    407  OD1 ASP A 392     -48.217  -1.150 -35.568  1.00 31.35           O
ANISOU  407  OD1 ASP A 392     3853   3025   5034   1226   2257    756       O
ATOM    408  OD2 ASP A 392     -47.631   0.825 -34.902  1.00 37.10           O
ANISOU  408  OD2 ASP A 392     4482   3961   5655   1319   2027    745       O
ATOM    409  N   GLY A 393     -50.660   0.235 -33.662  1.00 34.06           N
ANISOU  409  N   GLY A 393     4284   3506   5152   1250   2231    808       N
ATOM    410  CA  GLY A 393     -50.686   0.505 -32.232  1.00 34.48           C
ANISOU  410  CA  GLY A 393     4405   3609   5085   1409   2194    914       C
ATOM    411  C   GLY A 393     -49.739   1.583 -31.724  1.00 37.47           C
ANISOU  411  C   GLY A 393     4747   4117   5373   1508   1976    912       C
ATOM    412  O   GLY A 393     -50.065   2.295 -30.781  1.00 37.20           O
ANISOU  412  O   GLY A 393     4760   4167   5207   1577   1888    934       O
ATOM    413  N   GLY A 394     -48.563   1.697 -32.339  1.00 41.28           N
ANISOU  413  N   GLY A 394     5141   4611   5931   1515   1895    875       N
ATOM    414  CA  GLY A 394     -47.640   2.775 -32.026  1.00 30.59           C
ANISOU  414  CA  GLY A 394     3718   3372   4533   1571   1688    844       C
ATOM    415  C   GLY A 394     -48.248   4.151 -32.282  1.00 31.47           C
ANISOU  415  C   GLY A 394     3802   3571   4584   1464   1585    748       C
ATOM    416  O   GLY A 394     -48.005   5.088 -31.519  1.00 33.20           O
ANISOU  416  O   GLY A 394     4024   3879   4713   1527   1426    735       O
ATOM    417  N   PHE A 395     -49.027   4.284 -33.354  1.00 28.33           N
ANISOU  417  N   PHE A 395     3384   3148   4232   1312   1665    674       N
ATOM    418  CA  PHE A 395     -49.701   5.554 -33.641  1.00 27.30           C
ANISOU  418  CA  PHE A 395     3240   3090   4043   1226   1577    592       C
ATOM    419  C   PHE A 395     -51.094   5.675 -33.008  1.00 33.39           C
ANISOU  419  C   PHE A 395     4083   3881   4721   1229   1623    602       C
ATOM    420  O   PHE A 395     -51.602   6.782 -32.865  1.00 30.03           O
ANISOU  420  O   PHE A 395     3662   3525   4224   1211   1529    552       O
ATOM    421  CB  PHE A 395     -49.735   5.866 -35.143  1.00 30.15           C
ANISOU  421  CB  PHE A 395     3541   3436   4478   1082   1603    504       C
ATOM    422  CG  PHE A 395     -48.380   6.206 -35.704  1.00 34.05           C
ANISOU  422  CG  PHE A 395     3955   3935   5047   1072   1541    484       C
ATOM    423  CD1 PHE A 395     -47.887   7.495 -35.613  1.00 26.33           C
ANISOU  423  CD1 PHE A 395     2938   3019   4049   1059   1396    446       C
ATOM    424  CD2 PHE A 395     -47.581   5.225 -36.272  1.00 32.93           C
ANISOU  424  CD2 PHE A 395     3774   3729   5010   1078   1639    501       C
ATOM    425  CE1 PHE A 395     -46.631   7.805 -36.095  1.00 38.60           C
ANISOU  425  CE1 PHE A 395     4399   4571   5695   1039   1357    428       C
ATOM    426  CE2 PHE A 395     -46.311   5.530 -36.764  1.00 33.89           C
ANISOU  426  CE2 PHE A 395     3802   3860   5215   1073   1600    483       C
ATOM    427  CZ  PHE A 395     -45.836   6.814 -36.672  1.00 36.18           C
ANISOU  427  CZ  PHE A 395     4038   4213   5495   1047   1462    448       C
ATOM    428  N   VAL A 396     -51.700   4.542 -32.642  1.00 36.79           N
ANISOU  428  N   VAL A 396     4569   4243   5167   1251   1780    667       N
ATOM    429  CA  VAL A 396     -52.873   4.554 -31.768  1.00 37.78           C
ANISOU  429  CA  VAL A 396     4760   4386   5208   1283   1846    702       C
ATOM    430  C   VAL A 396     -52.445   5.238 -30.480  1.00 36.94           C
ANISOU  430  C   VAL A 396     4719   4359   4959   1433   1717    751       C
ATOM    431  O   VAL A 396     -53.169   6.068 -29.936  1.00 35.69           O
ANISOU  431  O   VAL A 396     4592   4269   4700   1454   1671    725       O
ATOM    432  CB  VAL A 396     -53.396   3.127 -31.451  1.00 30.90           C
ANISOU  432  CB  VAL A 396     3946   3404   4390   1292   2058    787       C
ATOM    433  CG1 VAL A 396     -54.445   3.170 -30.351  1.00 31.81           C
ANISOU  433  CG1 VAL A 396     4136   3541   4408   1349   2141    846       C
ATOM    434  CG2 VAL A 396     -53.972   2.473 -32.696  1.00 29.14           C
ANISOU  434  CG2 VAL A 396     3664   3103   4306   1123   2164    708       C
ATOM    435  N   TYR A 397     -51.240   4.908 -30.021  1.00 29.61           N
ANISOU  435  N   TYR A 397     3804   3424   4020   1545   1648    811       N
ATOM    436  CA  TYR A 397     -50.681   5.516 -28.819  1.00 37.42           C
ANISOU  436  CA  TYR A 397     4851   4496   4870   1698   1493    840       C
ATOM    437  C   TYR A 397     -50.548   7.036 -28.965  1.00 36.06           C
ANISOU  437  C   TYR A 397     4628   4413   4661   1652   1306    726       C
ATOM    438  O   TYR A 397     -51.044   7.795 -28.139  1.00 33.19           O
ANISOU  438  O   TYR A 397     4333   4113   4165   1714   1238    707       O
ATOM    439  CB  TYR A 397     -49.322   4.891 -28.506  1.00 37.57           C
ANISOU  439  CB  TYR A 397     4859   4500   4916   1819   1426    903       C
ATOM    440  CG  TYR A 397     -48.596   5.503 -27.323  1.00 41.77           C
ANISOU  440  CG  TYR A 397     5433   5130   5308   1983   1227    912       C
ATOM    441  CD1 TYR A 397     -48.701   4.946 -26.055  1.00 45.14           C
ANISOU  441  CD1 TYR A 397     6003   5568   5581   2167   1250   1025       C
ATOM    442  CD2 TYR A 397     -47.791   6.627 -27.477  1.00 40.89           C
ANISOU  442  CD2 TYR A 397     5225   5095   5218   1955   1016    804       C
ATOM    443  CE1 TYR A 397     -48.035   5.496 -24.976  1.00 45.22           C
ANISOU  443  CE1 TYR A 397     6061   5679   5442   2329   1047   1019       C
ATOM    444  CE2 TYR A 397     -47.127   7.184 -26.400  1.00 43.14           C
ANISOU  444  CE2 TYR A 397     5539   5469   5382   2097    816    786       C
ATOM    445  CZ  TYR A 397     -47.246   6.612 -25.156  1.00 45.95           C
ANISOU  445  CZ  TYR A 397     6040   5851   5568   2290    820    888       C
ATOM    446  OH  TYR A 397     -46.571   7.164 -24.086  1.00 51.88           O
ANISOU  446  OH  TYR A 397     6829   6704   6180   2444    599    857       O
ATOM    447  N   ILE A 398     -49.863   7.469 -30.015  1.00 34.13           N
ANISOU  447  N   ILE A 398     4273   4160   4533   1548   1238    651       N
ATOM    448  CA  ILE A 398     -49.683   8.891 -30.287  1.00 31.73           C
ANISOU  448  CA  ILE A 398     3924   3910   4221   1487   1083    549       C
ATOM    449  C   ILE A 398     -51.025   9.590 -30.495  1.00 32.33           C
ANISOU  449  C   ILE A 398     4039   4002   4243   1420   1121    500       C
ATOM    450  O   ILE A 398     -51.257  10.663 -29.940  1.00 33.48           O
ANISOU  450  O   ILE A 398     4222   4198   4300   1455   1008    449       O
ATOM    451  CB  ILE A 398     -48.758   9.106 -31.499  1.00 29.62           C
ANISOU  451  CB  ILE A 398     3540   3613   4103   1375   1055    497       C
ATOM    452  CG1 ILE A 398     -47.369   8.540 -31.206  1.00 28.66           C
ANISOU  452  CG1 ILE A 398     3352   3490   4046   1457    998    534       C
ATOM    453  CG2 ILE A 398     -48.622  10.573 -31.842  1.00 27.15           C
ANISOU  453  CG2 ILE A 398     3194   3328   3795   1300    925    404       C
ATOM    454  CD1 ILE A 398     -46.416   8.711 -32.368  1.00 28.39           C
ANISOU  454  CD1 ILE A 398     3192   3428   4168   1352    999    487       C
ATOM    455  N   ALA A 399     -51.911   8.975 -31.275  1.00 31.74           N
ANISOU  455  N   ALA A 399     3950   3885   4225   1332   1274    506       N
ATOM    456  CA  ALA A 399     -53.260   9.509 -31.467  1.00 31.82           C
ANISOU  456  CA  ALA A 399     3974   3918   4196   1283   1315    459       C
ATOM    457  C   ALA A 399     -53.973   9.712 -30.122  1.00 36.27           C
ANISOU  457  C   ALA A 399     4626   4529   4624   1400   1324    492       C
ATOM    458  O   ALA A 399     -54.627  10.727 -29.910  1.00 39.69           O
ANISOU  458  O   ALA A 399     5080   5010   4991   1412   1264    435       O
ATOM    459  CB  ALA A 399     -54.083   8.593 -32.375  1.00 26.00           C
ANISOU  459  CB  ALA A 399     3197   3132   3549   1181   1476    456       C
ATOM    460  N   GLY A 400     -53.830   8.739 -29.224  1.00 33.43           N
ANISOU  460  N   GLY A 400     4331   4152   4219   1497   1409    589       N
ATOM    461  CA  GLY A 400     -54.365   8.829 -27.880  1.00 29.14           C
ANISOU  461  CA  GLY A 400     3896   3652   3523   1629   1436    638       C
ATOM    462  C   GLY A 400     -53.841  10.044 -27.138  1.00 31.93           C
ANISOU  462  C   GLY A 400     4299   4079   3753   1722   1235    580       C
ATOM    463  O   GLY A 400     -54.625  10.817 -26.596  1.00 34.85           O
ANISOU  463  O   GLY A 400     4722   4497   4022   1766   1221    540       O
ATOM    464  N   LYS A 401     -52.521  10.223 -27.131  1.00 31.11           N
ANISOU  464  N   LYS A 401     4168   3981   3669   1749   1079    563       N
ATOM    465  CA  LYS A 401     -51.891  11.382 -26.492  1.00 30.37           C
ANISOU  465  CA  LYS A 401     4104   3949   3489   1816    867    483       C
ATOM    466  C   LYS A 401     -52.435  12.676 -27.093  1.00 30.52           C
ANISOU  466  C   LYS A 401     4091   3969   3536   1719    805    372       C
ATOM    467  O   LYS A 401     -52.560  13.689 -26.403  1.00 35.04           O
ANISOU  467  O   LYS A 401     4728   4581   4003   1782    689    302       O
ATOM    468  CB  LYS A 401     -50.374  11.343 -26.663  1.00 30.77           C
ANISOU  468  CB  LYS A 401     4075   3997   3619   1818    719    465       C
ATOM    469  CG  LYS A 401     -49.679  10.283 -25.829  1.00 34.32           C
ANISOU  469  CG  LYS A 401     4571   4461   4008   1967    719    565       C
ATOM    470  CD  LYS A 401     -49.617  10.705 -24.376  1.00 36.50           C
ANISOU  470  CD  LYS A 401     4976   4818   4074   2143    590    557       C
ATOM    471  CE  LYS A 401     -48.884   9.665 -23.524  1.00 37.12           C
ANISOU  471  CE  LYS A 401     5116   4917   4069   2319    571    666       C
ATOM    472  NZ  LYS A 401     -48.530  10.254 -22.210  1.00 36.77           N
ANISOU  472  NZ  LYS A 401     5181   4970   3819   2492    378    623       N
ATOM    473  N   CYS A 402     -52.758  12.618 -28.381  1.00 27.98           N
ANISOU  473  N   CYS A 402     3681   3601   3349   1578    881    356       N
ATOM    474  CA  CYS A 402     -53.377  13.728 -29.103  1.00 27.19           C
ANISOU  474  CA  CYS A 402     3559   3493   3278   1494    844    272       C
ATOM    475  C   CYS A 402     -54.880  13.868 -28.850  1.00 27.21           C
ANISOU  475  C   CYS A 402     3603   3524   3211   1525    948    268       C
ATOM    476  O   CYS A 402     -55.519  14.731 -29.437  1.00 30.65           O
ANISOU  476  O   CYS A 402     4021   3957   3666   1478    922    205       O
ATOM    477  CB  CYS A 402     -53.145  13.566 -30.607  1.00 26.17           C
ANISOU  477  CB  CYS A 402     3334   3312   3296   1350    886    262       C
ATOM    478  SG  CYS A 402     -51.408  13.669 -31.080  1.00 35.47           S
ANISOU  478  SG  CYS A 402     4437   4456   4585   1296    779    249       S
ATOM    479  N   GLY A 403     -55.451  13.017 -28.000  1.00 27.94           N
ANISOU  479  N   GLY A 403     3747   3639   3228   1608   1074    340       N
ATOM    480  CA  GLY A 403     -56.846  13.186 -27.608  1.00 33.14           C
ANISOU  480  CA  GLY A 403     4433   4333   3826   1647   1183    334       C
ATOM    481  C   GLY A 403     -57.852  12.384 -28.417  1.00 31.52           C
ANISOU  481  C   GLY A 403     4137   4107   3732   1548   1355    355       C
ATOM    482  O   GLY A 403     -59.053  12.455 -28.169  1.00 32.59           O
ANISOU  482  O   GLY A 403     4260   4274   3849   1567   1459    344       O
ATOM    483  N   LEU A 404     -57.363  11.623 -29.389  1.00 29.92           N
ANISOU  483  N   LEU A 404     3864   3853   3653   1442   1385    373       N
ATOM    484  CA  LEU A 404     -58.215  10.758 -30.191  1.00 33.14           C
ANISOU  484  CA  LEU A 404     4186   4233   4175   1338   1535    375       C
ATOM    485  C   LEU A 404     -58.435   9.430 -29.468  1.00 30.77           C
ANISOU  485  C   LEU A 404     3918   3892   3880   1368   1720    474       C
ATOM    486  O   LEU A 404     -57.636   9.049 -28.622  1.00 37.42           O
ANISOU  486  O   LEU A 404     4850   4719   4649   1464   1714    554       O
ATOM    487  CB  LEU A 404     -57.589  10.518 -31.571  1.00 28.23           C
ANISOU  487  CB  LEU A 404     3493   3565   3667   1217   1493    340       C
ATOM    488  CG  LEU A 404     -57.227  11.766 -32.369  1.00 33.67           C
ANISOU  488  CG  LEU A 404     4167   4272   4353   1183   1331    264       C
ATOM    489  CD1 LEU A 404     -56.755  11.378 -33.771  1.00 24.71           C
ANISOU  489  CD1 LEU A 404     2974   3095   3319   1067   1335    240       C
ATOM    490  CD2 LEU A 404     -58.404  12.753 -32.421  1.00 25.39           C
ANISOU  490  CD2 LEU A 404     3106   3277   3265   1205   1297    200       C
ATOM    491  N   VAL A 405     -59.515   8.731 -29.809  1.00 29.93           N
ANISOU  491  N   VAL A 405     3741   3763   3867   1285   1875    468       N
ATOM    492  CA  VAL A 405     -59.867   7.471 -29.149  1.00 31.33           C
ANISOU  492  CA  VAL A 405     3960   3874   4071   1266   2034    561       C
ATOM    493  C   VAL A 405     -60.023   6.343 -30.167  1.00 34.17           C
ANISOU  493  C   VAL A 405     4240   4142   4598   1108   2110    539       C
ATOM    494  O   VAL A 405     -60.389   6.591 -31.315  1.00 31.06           O
ANISOU  494  O   VAL A 405     3743   3768   4290   1000   2056    434       O
ATOM    495  CB  VAL A 405     -61.207   7.602 -28.372  1.00 46.52           C
ANISOU  495  CB  VAL A 405     5881   5833   5963   1273   2121    562       C
ATOM    496  CG1 VAL A 405     -61.078   8.585 -27.203  1.00 42.34           C
ANISOU  496  CG1 VAL A 405     5461   5381   5245   1445   2066    587       C
ATOM    497  CG2 VAL A 405     -62.333   8.011 -29.310  1.00 30.50           C
ANISOU  497  CG2 VAL A 405     3702   3847   4038   1154   2095    440       C
ATOM    498  N   PRO A 406     -59.758   5.092 -29.754  1.00 30.62           N
ANISOU  498  N   PRO A 406     3852   3590   4191   1106   2239    637       N
ATOM    499  CA  PRO A 406     -59.974   3.990 -30.697  1.00 36.69           C
ANISOU  499  CA  PRO A 406     4558   4257   5126    956   2319    601       C
ATOM    500  C   PRO A 406     -61.456   3.637 -30.771  1.00 37.63           C
ANISOU  500  C   PRO A 406     4592   4364   5340    842   2416    545       C
ATOM    501  O   PRO A 406     -62.145   3.735 -29.761  1.00 37.66           O
ANISOU  501  O   PRO A 406     4630   4389   5291    894   2491    599       O
ATOM    502  CB  PRO A 406     -59.169   2.839 -30.079  1.00 34.84           C
ANISOU  502  CB  PRO A 406     4437   3904   4898   1025   2434    737       C
ATOM    503  CG  PRO A 406     -59.183   3.116 -28.621  1.00 33.06           C
ANISOU  503  CG  PRO A 406     4327   3716   4518   1187   2474    851       C
ATOM    504  CD  PRO A 406     -59.226   4.625 -28.462  1.00 31.73           C
ANISOU  504  CD  PRO A 406     4135   3697   4224   1255   2320    782       C
ATOM    505  N   VAL A 407     -61.944   3.237 -31.940  1.00 37.93           N
ANISOU  505  N   VAL A 407     4518   4377   5516    696   2420    434       N
ATOM    506  CA  VAL A 407     -63.368   2.941 -32.096  1.00 36.87           C
ANISOU  506  CA  VAL A 407     4270   4247   5492    585   2502    358       C
ATOM    507  C   VAL A 407     -63.638   1.473 -32.481  1.00 38.52           C
ANISOU  507  C   VAL A 407     4460   4303   5874    457   2650    346       C
ATOM    508  O   VAL A 407     -64.578   0.857 -31.974  1.00 38.17           O
ANISOU  508  O   VAL A 407     4385   4202   5917    400   2790    360       O
ATOM    509  CB  VAL A 407     -64.047   3.937 -33.075  1.00 47.58           C
ANISOU  509  CB  VAL A 407     5481   5735   6861    539   2377    208       C
ATOM    510  CG1 VAL A 407     -63.062   4.430 -34.082  1.00 45.53           C
ANISOU  510  CG1 VAL A 407     5235   5502   6562    552   2243    161       C
ATOM    511  CG2 VAL A 407     -65.222   3.301 -33.785  1.00 53.56           C
ANISOU  511  CG2 VAL A 407     6086   6476   7787    391   2448     92       C
ATOM    512  N   LEU A 408     -62.802   0.922 -33.361  1.00 39.78           N
ANISOU  512  N   LEU A 408     4640   4387   6088    412   2629    315       N
ATOM    513  CA  LEU A 408     -62.863  -0.489 -33.747  1.00 44.15           C
ANISOU  513  CA  LEU A 408     5200   4770   6804    305   2772    299       C
ATOM    514  C   LEU A 408     -61.452  -1.037 -33.938  1.00 44.55           C
ANISOU  514  C   LEU A 408     5367   4723   6838    365   2774    370       C
ATOM    515  O   LEU A 408     -60.518  -0.281 -34.201  1.00 32.86           O
ANISOU  515  O   LEU A 408     3909   3325   5249    444   2640    379       O
ATOM    516  CB  LEU A 408     -63.630  -0.665 -35.058  1.00 46.23           C
ANISOU  516  CB  LEU A 408     5312   5049   7205    145   2752    111       C
ATOM    517  CG  LEU A 408     -65.086  -0.214 -35.105  1.00 46.31           C
ANISOU  517  CG  LEU A 408     5161   5160   7274     72   2748      9       C
ATOM    518  CD1 LEU A 408     -65.600  -0.264 -36.533  1.00 42.65           C
ANISOU  518  CD1 LEU A 408     4545   4737   6925    -60   2691   -192       C
ATOM    519  CD2 LEU A 408     -65.944  -1.086 -34.187  1.00 48.12           C
ANISOU  519  CD2 LEU A 408     5389   5279   7613     20   2934     67       C
ATOM    520  N   ALA A 409     -61.302  -2.354 -33.829  1.00 40.24           N
ANISOU  520  N   ALA A 409     4885   3993   6412    330   2935    416       N
ATOM    521  CA  ALA A 409     -60.004  -2.979 -34.008  1.00 39.20           C
ANISOU  521  CA  ALA A 409     4854   3755   6283    398   2960    484       C
ATOM    522  C   ALA A 409     -60.011  -3.790 -35.295  1.00 41.69           C
ANISOU  522  C   ALA A 409     5120   3967   6752    259   3006    345       C
ATOM    523  O   ALA A 409     -61.031  -4.392 -35.636  1.00 40.88           O
ANISOU  523  O   ALA A 409     4948   3791   6792    119   3102    244       O
ATOM    524  CB  ALA A 409     -59.684  -3.882 -32.810  1.00 42.06           C
ANISOU  524  CB  ALA A 409     5360   3970   6651    507   3126    665       C
ATOM    525  N   GLU A 410     -58.896  -3.790 -36.025  1.00 35.00           N
ANISOU  525  N   GLU A 410     4301   3115   5881    294   2942    325       N
ATOM    526  CA  GLU A 410     -58.731  -4.782 -37.075  1.00 43.24           C
ANISOU  526  CA  GLU A 410     5340   4021   7067    192   3030    217       C
ATOM    527  C   GLU A 410     -58.543  -6.123 -36.365  1.00 45.90           C
ANISOU  527  C   GLU A 410     5789   4134   7518    226   3239    331       C
ATOM    528  O   GLU A 410     -57.824  -6.203 -35.369  1.00 41.46           O
ANISOU  528  O   GLU A 410     5330   3542   6882    383   3271    508       O
ATOM    529  CB  GLU A 410     -57.514  -4.484 -37.959  1.00 34.59           C
ANISOU  529  CB  GLU A 410     4260   2971   5910    240   2928    182       C
ATOM    530  CG  GLU A 410     -57.528  -3.122 -38.658  1.00 39.90           C
ANISOU  530  CG  GLU A 410     4852   3849   6459    232   2733     92       C
ATOM    531  CD  GLU A 410     -56.278  -2.900 -39.521  1.00 41.89           C
ANISOU  531  CD  GLU A 410     5130   4127   6660    278   2656     68       C
ATOM    532  OE1 GLU A 410     -55.339  -3.724 -39.446  1.00 39.51           O
ANISOU  532  OE1 GLU A 410     4898   3704   6408    335   2736    134       O
ATOM    533  OE2 GLU A 410     -56.234  -1.905 -40.275  1.00 38.56           O
ANISOU  533  OE2 GLU A 410     4658   3841   6150    264   2526    -12       O
ATOM    534  N   ASN A 411     -59.203  -7.163 -36.861  1.00 39.18           N
ANISOU  534  N   ASN A 411     4918   3121   6848     87   3389    226       N
ATOM    535  CA  ASN A 411     -58.977  -8.519 -36.379  1.00 41.12           C
ANISOU  535  CA  ASN A 411     5279   3120   7224    116   3606    314       C
ATOM    536  C   ASN A 411     -58.339  -9.340 -37.478  1.00 41.61           C
ANISOU  536  C   ASN A 411     5364   3043   7401     60   3680    207       C
ATOM    537  O   ASN A 411     -58.605  -9.103 -38.651  1.00 45.27           O
ANISOU  537  O   ASN A 411     5732   3572   7896    -68   3610     15       O
ATOM    538  CB  ASN A 411     -60.291  -9.163 -35.962  1.00 45.80           C
ANISOU  538  CB  ASN A 411     5840   3606   7957     -1   3751    273       C
ATOM    539  CG  ASN A 411     -60.553  -9.043 -34.476  1.00 48.99           C
ANISOU  539  CG  ASN A 411     6320   4015   8278    122   3809    465       C
ATOM    540  OD1 ASN A 411     -59.808  -8.382 -33.756  1.00 45.04           O
ANISOU  540  OD1 ASN A 411     5891   3618   7606    291   3724    616       O
ATOM    541  ND2 ASN A 411     -61.617  -9.690 -34.007  1.00 45.78           N
ANISOU  541  ND2 ASN A 411     5899   3501   7994     39   3961    452       N
ATOM    542  N   TYR A 412     -57.507 -10.311 -37.114  1.00 42.73           N
ANISOU  542  N   TYR A 412     5635   2995   7604    168   3833    325       N
ATOM    543  CA  TYR A 412     -56.772 -11.065 -38.128  1.00 43.24           C
ANISOU  543  CA  TYR A 412     5733   2924   7771    138   3915    234       C
ATOM    544  C   TYR A 412     -57.050 -12.547 -38.081  1.00 48.89           C
ANISOU  544  C   TYR A 412     6522   3369   8686     97   4168    203       C
ATOM    545  O   TYR A 412     -56.651 -13.282 -38.982  1.00 51.49           O
ANISOU  545  O   TYR A 412     6865   3583   9118     48   4267     85       O
ATOM    546  CB  TYR A 412     -55.271 -10.811 -38.001  1.00 42.23           C
ANISOU  546  CB  TYR A 412     5671   2849   7525    322   3840    376       C
ATOM    547  CG  TYR A 412     -54.959  -9.352 -37.861  1.00 39.98           C
ANISOU  547  CG  TYR A 412     5313   2843   7036    391   3586    405       C
ATOM    548  CD1 TYR A 412     -55.252  -8.465 -38.890  1.00 38.58           C
ANISOU  548  CD1 TYR A 412     5027   2837   6796    285   3418    231       C
ATOM    549  CD2 TYR A 412     -54.393  -8.848 -36.698  1.00 39.47           C
ANISOU  549  CD2 TYR A 412     5293   2862   6841    568   3526    601       C
ATOM    550  CE1 TYR A 412     -54.981  -7.124 -38.771  1.00 43.83           C
ANISOU  550  CE1 TYR A 412     5635   3730   7290    347   3207    257       C
ATOM    551  CE2 TYR A 412     -54.122  -7.492 -36.569  1.00 37.59           C
ANISOU  551  CE2 TYR A 412     4987   2862   6434    621   3305    607       C
ATOM    552  CZ  TYR A 412     -54.417  -6.641 -37.611  1.00 36.22           C
ANISOU  552  CZ  TYR A 412     4709   2834   6218    506   3152    438       C
ATOM    553  OH  TYR A 412     -54.161  -5.293 -37.508  1.00 34.53           O
ANISOU  553  OH  TYR A 412     4438   2830   5853    556   2956    444       O
ATOM    554  N   ASN A 413     -57.740 -12.987 -37.034  1.00 58.05           N
ANISOU  554  N   ASN A 413     7716   4464   9875    124   4273    297       N
ATOM    555  CA  ASN A 413     -58.024 -14.404 -36.863  1.00 64.21           C
ANISOU  555  CA  ASN A 413     8553   5038  10807     94   4500    283       C
ATOM    556  C   ASN A 413     -59.420 -14.766 -37.359  1.00 69.32           C
ANISOU  556  C   ASN A 413     9091   5631  11614   -146   4546     79       C
ATOM    557  O   ASN A 413     -60.424 -14.258 -36.863  1.00 76.41           O
ANISOU  557  O   ASN A 413     9918   6609  12504   -212   4500     78       O
ATOM    558  CB  ASN A 413     -57.841 -14.823 -35.399  1.00 67.41           C
ANISOU  558  CB  ASN A 413     9079   5389  11146    279   4617    525       C
ATOM    559  CG  ASN A 413     -57.477 -16.294 -35.252  1.00 72.75           C
ANISOU  559  CG  ASN A 413     9851   5875  11916    320   4834    576       C
ATOM    560  OD1 ASN A 413     -56.344 -16.636 -34.900  1.00 68.87           O
ANISOU  560  OD1 ASN A 413     9453   5378  11337    496   4866    733       O
ATOM    561  ND2 ASN A 413     -58.441 -17.170 -35.515  1.00 78.84           N
ANISOU  561  ND2 ASN A 413    10594   6498  12863    149   4971    448       N
ATOM    562  N   LYS A 414     -59.471 -15.635 -38.357  1.00 68.83           N
ANISOU  562  N   LYS A 414     9006   5450  11694   -278   4630   -100       N
ATOM    563  CA  LYS A 414     -60.733 -16.136 -38.867  1.00 73.53           C
ANISOU  563  CA  LYS A 414     9492   5980  12465   -508   4682   -310       C
ATOM    564  C   LYS A 414     -61.386 -17.049 -37.822  1.00 80.30           C
ANISOU  564  C   LYS A 414    10400   6686  13424   -501   4877   -204       C
ATOM    565  O   LYS A 414     -60.667 -17.763 -37.127  1.00 84.94           O
ANISOU  565  O   LYS A 414    11130   7159  13983   -344   5014    -25       O
ATOM    566  CB  LYS A 414     -60.476 -16.922 -40.154  1.00 74.83           C
ANISOU  566  CB  LYS A 414     9645   6048  12738   -633   4717   -517       C
ATOM    567  N   SER A 415     -62.716 -17.044 -37.663  1.00 82.40           N
ANISOU  567  N   SER A 415    10551   6954  13803   -659   4899   -301       N
ATOM    568  CA  SER A 415     -63.682 -16.126 -38.277  1.00 84.27           C
ANISOU  568  CA  SER A 415    10600   7361  14059   -826   4731   -486       C
ATOM    569  C   SER A 415     -65.047 -16.360 -37.630  1.00 89.63           C
ANISOU  569  C   SER A 415    11183   8007  14866   -940   4824   -504       C
ATOM    570  O   SER A 415     -66.065 -15.979 -38.205  1.00 93.60           O
ANISOU  570  O   SER A 415    11501   8608  15456  -1116   4732   -698       O
ATOM    571  CB  SER A 415     -63.845 -16.362 -39.784  1.00 83.95           C
ANISOU  571  CB  SER A 415    10454   7318  14125  -1013   4661   -775       C
ATOM    572  N   ASP A 416     -65.061 -16.999 -36.456  1.00 89.78           N
ANISOU  572  N   ASP A 416    11322   7890  14898   -836   5011   -307       N
ATOM    573  CA  ASP A 416     -66.302 -17.432 -35.784  1.00 93.03           C
ANISOU  573  CA  ASP A 416    11667   8225  15455   -942   5158   -308       C
ATOM    574  C   ASP A 416     -67.377 -16.344 -35.706  1.00 88.33           C
ANISOU  574  C   ASP A 416    10887   7834  14840  -1035   5017   -378       C
ATOM    575  O   ASP A 416     -68.289 -16.287 -36.535  1.00 92.95           O
ANISOU  575  O   ASP A 416    11278   8470  15569  -1235   4952   -612       O
ATOM    576  CB  ASP A 416     -65.992 -17.961 -34.379  1.00 96.93           C
ANISOU  576  CB  ASP A 416    12347   8592  15891   -763   5354    -35       C
ATOM    577  N   ASN A 417     -67.289 -15.509 -34.680  1.00 76.30           N
ANISOU  577  N   ASN A 417     9421   6431  13139   -883   4974   -176       N
ATOM    578  CA  ASN A 417     -67.937 -14.215 -34.712  1.00 71.05           C
ANISOU  578  CA  ASN A 417     8602   6012  12382   -917   4787   -221       C
ATOM    579  C   ASN A 417     -66.826 -13.210 -34.474  1.00 64.14           C
ANISOU  579  C   ASN A 417     7835   5291  11245   -719   4619    -70       C
ATOM    580  O   ASN A 417     -66.612 -12.752 -33.350  1.00 60.04           O
ANISOU  580  O   ASN A 417     7416   4826  10569   -559   4631    138       O
ATOM    581  CB  ASN A 417     -69.031 -14.103 -33.653  1.00 77.65           C
ANISOU  581  CB  ASN A 417     9385   6863  13255   -935   4899   -134       C
ATOM    582  N   CYS A 418     -66.094 -12.914 -35.543  1.00 59.51           N
ANISOU  582  N   CYS A 418     7231   4766  10615   -732   4473   -180       N
ATOM    583  CA  CYS A 418     -64.902 -12.089 -35.473  1.00 52.79           C
ANISOU  583  CA  CYS A 418     6480   4037   9542   -556   4324    -54       C
ATOM    584  C   CYS A 418     -65.167 -10.724 -34.819  1.00 53.83           C
ANISOU  584  C   CYS A 418     6563   4406   9484   -471   4170     43       C
ATOM    585  O   CYS A 418     -64.402 -10.281 -33.963  1.00 55.14           O
ANISOU  585  O   CYS A 418     6858   4622   9471   -283   4137    239       O
ATOM    586  CB  CYS A 418     -64.305 -11.936 -36.872  1.00 51.96           C
ANISOU  586  CB  CYS A 418     6325   3972   9444   -624   4201   -227       C
ATOM    587  SG  CYS A 418     -63.278 -10.479 -37.074  1.00 69.45           S
ANISOU  587  SG  CYS A 418     8559   6432  11398   -477   3956   -147       S
ATOM    588  N   GLU A 419     -66.273 -10.087 -35.196  1.00 52.88           N
ANISOU  588  N   GLU A 419     6252   4433   9408   -602   4080   -102       N
ATOM    589  CA  GLU A 419     -66.654  -8.780 -34.652  1.00 59.88           C
ANISOU  589  CA  GLU A 419     7072   5551  10128   -528   3941    -38       C
ATOM    590  C   GLU A 419     -66.892  -8.759 -33.133  1.00 58.82           C
ANISOU  590  C   GLU A 419     7042   5394   9915   -406   4059    171       C
ATOM    591  O   GLU A 419     -66.847  -7.698 -32.505  1.00 52.55           O
ANISOU  591  O   GLU A 419     6256   4773   8938   -291   3953    266       O
ATOM    592  CB  GLU A 419     -67.910  -8.273 -35.356  1.00 66.45           C
ANISOU  592  CB  GLU A 419     7664   6524  11062   -692   3854   -245       C
ATOM    593  CG  GLU A 419     -67.827  -8.313 -36.863  1.00 73.18           C
ANISOU  593  CG  GLU A 419     8402   7407  11996   -820   3744   -475       C
ATOM    594  CD  GLU A 419     -69.181  -8.120 -37.511  1.00 79.27           C
ANISOU  594  CD  GLU A 419     8923   8277  12919   -993   3691   -697       C
ATOM    595  OE1 GLU A 419     -69.886  -7.156 -37.137  1.00 79.84           O
ANISOU  595  OE1 GLU A 419     8881   8533  12920   -958   3603   -681       O
ATOM    596  OE2 GLU A 419     -69.541  -8.941 -38.383  1.00 82.67           O
ANISOU  596  OE2 GLU A 419     9266   8603  13543  -1159   3735   -896       O
ATOM    597  N   ASP A 420     -67.148  -9.923 -32.551  1.00 52.52           N
ANISOU  597  N   ASP A 420     6325   4380   9251   -427   4286    236       N
ATOM    598  CA  ASP A 420     -67.425 -10.021 -31.121  1.00 61.02           C
ANISOU  598  CA  ASP A 420     7509   5416  10259   -314   4430    429       C
ATOM    599  C   ASP A 420     -66.220 -10.537 -30.346  1.00 65.95           C
ANISOU  599  C   ASP A 420     8375   5917  10768   -113   4515    638       C
ATOM    600  O   ASP A 420     -66.231 -10.563 -29.116  1.00 71.19           O
ANISOU  600  O   ASP A 420     9162   6559  11329     23   4621    819       O
ATOM    601  CB  ASP A 420     -68.598 -10.970 -30.871  1.00 60.23           C
ANISOU  601  CB  ASP A 420     7340   5160  10383   -458   4652    377       C
ATOM    602  CG  ASP A 420     -69.928 -10.376 -31.271  1.00 64.64           C
ANISOU  602  CG  ASP A 420     7654   5865  11042   -621   4588    210       C
ATOM    603  OD1 ASP A 420     -70.137  -9.166 -31.041  1.00 60.08           O
ANISOU  603  OD1 ASP A 420     7010   5508  10310   -557   4441    229       O
ATOM    604  OD2 ASP A 420     -70.771 -11.130 -31.807  1.00 72.35           O
ANISOU  604  OD2 ASP A 420     8498   6734  12256   -806   4689     53       O
ATOM    605  N   THR A 421     -65.189 -10.964 -31.065  1.00 61.23           N
ANISOU  605  N   THR A 421     7840   5240  10184    -85   4476    611       N
ATOM    606  CA  THR A 421     -64.050 -11.622 -30.437  1.00 64.50           C
ANISOU  606  CA  THR A 421     8463   5520  10523    105   4574    793       C
ATOM    607  C   THR A 421     -62.798 -10.744 -30.447  1.00 65.36           C
ANISOU  607  C   THR A 421     8637   5775  10421    274   4381    879       C
ATOM    608  O   THR A 421     -62.106 -10.661 -31.457  1.00 74.09           O
ANISOU  608  O   THR A 421     9706   6898  11546    242   4275    785       O
ATOM    609  CB  THR A 421     -63.731 -12.952 -31.152  1.00 65.32           C
ANISOU  609  CB  THR A 421     8603   5397  10819     34   4718    714       C
ATOM    610  OG1 THR A 421     -64.916 -13.754 -31.226  1.00 64.94           O
ANISOU  610  OG1 THR A 421     8475   5216  10985   -144   4890    610       O
ATOM    611  CG2 THR A 421     -62.634 -13.722 -30.418  1.00 65.75           C
ANISOU  611  CG2 THR A 421     8867   5315  10802    248   4846    912       C
ATOM    612  N   PRO A 422     -62.502 -10.083 -29.317  1.00 58.91           N
ANISOU  612  N   PRO A 422     7916   5066   9402    454   4343   1053       N
ATOM    613  CA  PRO A 422     -61.277  -9.280 -29.221  1.00 54.88           C
ANISOU  613  CA  PRO A 422     7467   4691   8694    624   4170   1140       C
ATOM    614  C   PRO A 422     -60.042 -10.169 -29.237  1.00 59.38           C
ANISOU  614  C   PRO A 422     8172   5114   9277    764   4251   1239       C
ATOM    615  O   PRO A 422     -60.025 -11.195 -28.564  1.00 67.21           O
ANISOU  615  O   PRO A 422     9286   5941  10312    846   4448   1347       O
ATOM    616  CB  PRO A 422     -61.410  -8.600 -27.859  1.00 53.57           C
ANISOU  616  CB  PRO A 422     7388   4639   8328    786   4162   1298       C
ATOM    617  CG  PRO A 422     -62.333  -9.490 -27.080  1.00 57.90           C
ANISOU  617  CG  PRO A 422     7995   5034   8969    761   4397   1359       C
ATOM    618  CD  PRO A 422     -63.298 -10.038 -28.079  1.00 57.31           C
ANISOU  618  CD  PRO A 422     7767   4867   9142    509   4463   1168       C
ATOM    619  N   GLU A 423     -59.023  -9.784 -29.998  1.00 56.64           N
ANISOU  619  N   GLU A 423     7798   4833   8890    797   4109   1203       N
ATOM    620  CA  GLU A 423     -57.805 -10.579 -30.087  1.00 49.41           C
ANISOU  620  CA  GLU A 423     6987   3795   7991    937   4183   1291       C
ATOM    621  C   GLU A 423     -56.710 -10.038 -29.170  1.00 46.83           C
ANISOU  621  C   GLU A 423     6763   3583   7446   1195   4106   1482       C
ATOM    622  O   GLU A 423     -56.607  -8.829 -28.957  1.00 45.12           O
ANISOU  622  O   GLU A 423     6504   3564   7077   1230   3930   1493       O
ATOM    623  CB  GLU A 423     -57.334 -10.648 -31.538  1.00 46.42           C
ANISOU  623  CB  GLU A 423     6515   3394   7728    814   4111   1130       C
ATOM    624  CG  GLU A 423     -58.465 -10.988 -32.478  1.00 48.01           C
ANISOU  624  CG  GLU A 423     6600   3531   8113    560   4151    916       C
ATOM    625  CD  GLU A 423     -58.015 -11.241 -33.894  1.00 53.01           C
ANISOU  625  CD  GLU A 423     7169   4118   8855    449   4116    751       C
ATOM    626  OE1 GLU A 423     -58.790 -11.895 -34.627  1.00 53.60           O
ANISOU  626  OE1 GLU A 423     7179   4085   9100    268   4204    582       O
ATOM    627  OE2 GLU A 423     -56.905 -10.792 -34.280  1.00 55.93           O
ANISOU  627  OE2 GLU A 423     7548   4560   9142    539   4007    783       O
ATOM    628  N   ALA A 424     -55.917 -10.945 -28.607  1.00 48.52           N
ANISOU  628  N   ALA A 424     7104   3697   7633   1377   4237   1622       N
ATOM    629  CA  ALA A 424     -54.801 -10.575 -27.739  1.00 56.90           C
ANISOU  629  CA  ALA A 424     8257   4888   8473   1633   4162   1798       C
ATOM    630  C   ALA A 424     -53.704  -9.822 -28.504  1.00 54.06           C
ANISOU  630  C   ALA A 424     7812   4658   8072   1659   3982   1766       C
ATOM    631  O   ALA A 424     -52.961  -9.034 -27.922  1.00 55.42           O
ANISOU  631  O   ALA A 424     8010   4996   8051   1814   3822   1864       O
ATOM    632  CB  ALA A 424     -54.226 -11.825 -27.054  1.00 55.05           C
ANISOU  632  CB  ALA A 424     8163   4550   8203   1785   4316   1941       C
ATOM    633  N   GLY A 425     -53.600 -10.074 -29.806  1.00 49.19           N
ANISOU  633  N   GLY A 425     7094   3963   7632   1502   3991   1619       N
ATOM    634  CA  GLY A 425     -52.670  -9.340 -30.641  1.00 44.65           C
ANISOU  634  CA  GLY A 425     6429   3508   7029   1471   3790   1568       C
ATOM    635  C   GLY A 425     -51.773 -10.225 -31.490  1.00 48.35           C
ANISOU  635  C   GLY A 425     6877   3896   7598   1445   3789   1514       C
ATOM    636  O   GLY A 425     -51.615 -11.420 -31.218  1.00 50.21           O
ANISOU  636  O   GLY A 425     7198   4000   7881   1492   3947   1582       O
ATOM    637  N   TYR A 426     -51.191  -9.638 -32.530  1.00 42.41           N
ANISOU  637  N   TYR A 426     6008   3236   6869   1375   3605   1374       N
ATOM    638  CA  TYR A 426     -50.232 -10.346 -33.374  1.00 42.90           C
ANISOU  638  CA  TYR A 426     6046   3242   7011   1367   3589   1319       C
ATOM    639  C   TYR A 426     -48.854 -10.338 -32.711  1.00 53.38           C
ANISOU  639  C   TYR A 426     7390   4668   8224   1591   3450   1440       C
ATOM    640  O   TYR A 426     -48.707  -9.875 -31.574  1.00 56.02           O
ANISOU  640  O   TYR A 426     7771   5103   8413   1747   3372   1562       O
ATOM    641  CB  TYR A 426     -50.188  -9.765 -34.793  1.00 41.20           C
ANISOU  641  CB  TYR A 426     5705   3090   6858   1204   3471   1113       C
ATOM    642  CG  TYR A 426     -49.826  -8.297 -34.872  1.00 44.28           C
ANISOU  642  CG  TYR A 426     5988   3712   7123   1229   3229   1060       C
ATOM    643  CD1 TYR A 426     -50.761  -7.316 -34.557  1.00 46.80           C
ANISOU  643  CD1 TYR A 426     6272   4141   7369   1172   3168   1027       C
ATOM    644  CD2 TYR A 426     -48.562  -7.888 -35.284  1.00 38.59           C
ANISOU  644  CD2 TYR A 426     5192   3104   6367   1300   3071   1034       C
ATOM    645  CE1 TYR A 426     -50.445  -5.974 -34.630  1.00 47.03           C
ANISOU  645  CE1 TYR A 426     6208   4377   7285   1187   2957    975       C
ATOM    646  CE2 TYR A 426     -48.235  -6.535 -35.366  1.00 41.89           C
ANISOU  646  CE2 TYR A 426     5508   3719   6690   1309   2872    982       C
ATOM    647  CZ  TYR A 426     -49.184  -5.591 -35.038  1.00 43.63           C
ANISOU  647  CZ  TYR A 426     5710   4036   6833   1253   2818    954       C
ATOM    648  OH  TYR A 426     -48.887  -4.256 -35.089  1.00 34.35           O
ANISOU  648  OH  TYR A 426     4443   3041   5567   1260   2635    904       O
ATOM    649  N   PHE A 427     -47.848 -10.856 -33.406  1.00 49.76           N
ANISOU  649  N   PHE A 427     6894   4182   7830   1612   3414   1396       N
ATOM    650  CA  PHE A 427     -46.524 -10.952 -32.818  1.00 51.28           C
ANISOU  650  CA  PHE A 427     7084   4454   7945   1824   3285   1495       C
ATOM    651  C   PHE A 427     -45.486 -10.130 -33.574  1.00 49.51           C
ANISOU  651  C   PHE A 427     6706   4379   7728   1826   3083   1387       C
ATOM    652  O   PHE A 427     -45.421 -10.158 -34.802  1.00 50.38           O
ANISOU  652  O   PHE A 427     6748   4460   7935   1686   3104   1250       O
ATOM    653  CB  PHE A 427     -46.073 -12.416 -32.740  1.00 47.88           C
ANISOU  653  CB  PHE A 427     6748   3857   7586   1901   3434   1571       C
ATOM    654  CG  PHE A 427     -46.883 -13.257 -31.797  1.00 49.15           C
ANISOU  654  CG  PHE A 427     7067   3885   7724   1940   3632   1702       C
ATOM    655  CD1 PHE A 427     -46.653 -13.209 -30.433  1.00 54.88           C
ANISOU  655  CD1 PHE A 427     7885   4676   8290   2143   3583   1869       C
ATOM    656  CD2 PHE A 427     -47.869 -14.106 -32.275  1.00 59.90           C
ANISOU  656  CD2 PHE A 427     8480   5058   9220   1775   3867   1647       C
ATOM    657  CE1 PHE A 427     -47.392 -13.992 -29.554  1.00 60.03           C
ANISOU  657  CE1 PHE A 427     8692   5209   8909   2185   3781   1991       C
ATOM    658  CE2 PHE A 427     -48.614 -14.889 -31.404  1.00 64.01           C
ANISOU  658  CE2 PHE A 427     9132   5456   9733   1806   4068   1757       C
ATOM    659  CZ  PHE A 427     -48.373 -14.832 -30.040  1.00 62.84           C
ANISOU  659  CZ  PHE A 427     9087   5374   9416   2014   4031   1935       C
ATOM    660  N   ALA A 428     -44.678  -9.391 -32.824  1.00 47.23           N
ANISOU  660  N   ALA A 428     6362   4249   7332   1985   2892   1444       N
ATOM    661  CA  ALA A 428     -43.515  -8.729 -33.390  1.00 46.35           C
ANISOU  661  CA  ALA A 428     6095   4269   7248   2013   2717   1358       C
ATOM    662  C   ALA A 428     -42.369  -9.742 -33.435  1.00 50.23           C
ANISOU  662  C   ALA A 428     6583   4696   7807   2147   2735   1404       C
ATOM    663  O   ALA A 428     -41.972 -10.305 -32.409  1.00 49.67           O
ANISOU  663  O   ALA A 428     6589   4608   7677   2332   2717   1536       O
ATOM    664  CB  ALA A 428     -43.133  -7.521 -32.553  1.00 46.37           C
ANISOU  664  CB  ALA A 428     6024   4461   7132   2122   2502   1381       C
ATOM    665  N   VAL A 429     -41.860 -10.002 -34.629  1.00 53.69           N
ANISOU  665  N   VAL A 429     6944   5095   8361   2060   2774   1295       N
ATOM    666  CA  VAL A 429     -40.756 -10.941 -34.771  1.00 46.67           C
ANISOU  666  CA  VAL A 429     6039   4145   7549   2186   2797   1324       C
ATOM    667  C   VAL A 429     -39.579 -10.240 -35.418  1.00 47.17           C
ANISOU  667  C   VAL A 429     5914   4342   7665   2203   2658   1227       C
ATOM    668  O   VAL A 429     -39.719  -9.132 -35.954  1.00 44.43           O
ANISOU  668  O   VAL A 429     5468   4106   7307   2082   2582   1129       O
ATOM    669  CB  VAL A 429     -41.147 -12.154 -35.629  1.00 47.58           C
ANISOU  669  CB  VAL A 429     6248   4059   7770   2085   3014   1284       C
ATOM    670  CG1 VAL A 429     -42.383 -12.835 -35.060  1.00 48.12           C
ANISOU  670  CG1 VAL A 429     6486   3983   7816   2037   3180   1364       C
ATOM    671  CG2 VAL A 429     -41.370 -11.734 -37.072  1.00 46.06           C
ANISOU  671  CG2 VAL A 429     5984   3875   7641   1883   3044   1112       C
ATOM    672  N   ALA A 430     -38.417 -10.884 -35.348  1.00 48.20           N
ANISOU  672  N   ALA A 430     5993   4459   7859   2358   2634   1257       N
ATOM    673  CA  ALA A 430     -37.217 -10.411 -36.024  1.00 51.95           C
ANISOU  673  CA  ALA A 430     6281   5040   8418   2378   2542   1164       C
ATOM    674  C   ALA A 430     -36.802 -11.450 -37.056  1.00 54.32           C
ANISOU  674  C   ALA A 430     6599   5209   8830   2352   2699   1111       C
ATOM    675  O   ALA A 430     -36.419 -12.565 -36.701  1.00 51.68           O
ANISOU  675  O   ALA A 430     6336   4768   8533   2491   2762   1187       O
ATOM    676  CB  ALA A 430     -36.097 -10.176 -35.025  1.00 52.32           C
ANISOU  676  CB  ALA A 430     6214   5208   8456   2601   2351   1226       C
ATOM    677  N   VAL A 431     -36.888 -11.090 -38.333  1.00 52.49           N
ANISOU  677  N   VAL A 431     6318   4984   8643   2180   2762    981       N
ATOM    678  CA  VAL A 431     -36.621 -12.048 -39.396  1.00 49.56           C
ANISOU  678  CA  VAL A 431     5986   4485   8360   2142   2920    914       C
ATOM    679  C   VAL A 431     -35.208 -11.916 -39.943  1.00 50.71           C
ANISOU  679  C   VAL A 431     5963   4713   8592   2224   2880    858       C
ATOM    680  O   VAL A 431     -34.737 -10.815 -40.225  1.00 49.75           O
ANISOU  680  O   VAL A 431     5690   4741   8471   2178   2780    799       O
ATOM    681  CB  VAL A 431     -37.643 -11.943 -40.539  1.00 48.09           C
ANISOU  681  CB  VAL A 431     5881   4233   8159   1913   3035    798       C
ATOM    682  CG1 VAL A 431     -37.397 -13.046 -41.553  1.00 49.63           C
ANISOU  682  CG1 VAL A 431     6139   4282   8435   1892   3198    727       C
ATOM    683  CG2 VAL A 431     -39.058 -12.050 -39.983  1.00 47.15           C
ANISOU  683  CG2 VAL A 431     5902   4036   7976   1828   3079    842       C
ATOM    684  N   VAL A 432     -34.530 -13.052 -40.060  1.00 52.98           N
ANISOU  684  N   VAL A 432     6274   4896   8960   2349   2965    880       N
ATOM    685  CA  VAL A 432     -33.185 -13.093 -40.614  1.00 57.04           C
ANISOU  685  CA  VAL A 432     6630   5472   9573   2438   2955    825       C
ATOM    686  C   VAL A 432     -33.115 -14.179 -41.684  1.00 60.05           C
ANISOU  686  C   VAL A 432     7103   5696  10019   2405   3148    759       C
ATOM    687  O   VAL A 432     -33.941 -15.096 -41.701  1.00 61.61           O
ANISOU  687  O   VAL A 432     7480   5724  10203   2367   3270    781       O
ATOM    688  CB  VAL A 432     -32.133 -13.350 -39.517  1.00 56.56           C
ANISOU  688  CB  VAL A 432     6463   5471   9556   2690   2824    916       C
ATOM    689  CG1 VAL A 432     -32.133 -12.210 -38.498  1.00 55.45           C
ANISOU  689  CG1 VAL A 432     6221   5498   9349   2726   2615    958       C
ATOM    690  CG2 VAL A 432     -32.395 -14.678 -38.830  1.00 58.39           C
ANISOU  690  CG2 VAL A 432     6868   5534   9782   2828   2898   1028       C
ATOM    691  N   LYS A 433     -32.150 -14.064 -42.589  1.00 56.70           N
ANISOU  691  N   LYS A 433     6553   5324   9665   2413   3185    672       N
ATOM    692  CA  LYS A 433     -32.002 -15.040 -43.662  1.00 58.15           C
ANISOU  692  CA  LYS A 433     6820   5370   9903   2393   3366    596       C
ATOM    693  C   LYS A 433     -31.285 -16.275 -43.138  1.00 60.98           C
ANISOU  693  C   LYS A 433     7198   5621  10349   2610   3407    668       C
ATOM    694  O   LYS A 433     -30.295 -16.162 -42.415  1.00 62.29           O
ANISOU  694  O   LYS A 433     7218   5882  10567   2792   3291    726       O
ATOM    695  CB  LYS A 433     -31.222 -14.444 -44.830  1.00 58.27           C
ANISOU  695  CB  LYS A 433     6704   5486   9951   2330   3405    483       C
ATOM    696  CG  LYS A 433     -31.627 -13.026 -45.206  1.00 55.83           C
ANISOU  696  CG  LYS A 433     6332   5317   9562   2156   3331    432       C
ATOM    697  CD  LYS A 433     -31.110 -12.705 -46.592  1.00 56.23           C
ANISOU  697  CD  LYS A 433     6334   5408   9623   2070   3434    319       C
ATOM    698  CE  LYS A 433     -30.929 -11.219 -46.815  1.00 56.07           C
ANISOU  698  CE  LYS A 433     6181   5557   9565   1963   3347    293       C
ATOM    699  NZ  LYS A 433     -29.938 -10.599 -45.892  1.00 57.02           N
ANISOU  699  NZ  LYS A 433     6079   5817   9769   2081   3207    352       N
ATOM    700  N   LYS A 434     -31.788 -17.455 -43.484  1.00 62.12           N
ANISOU  700  N   LYS A 434     7522   5566  10513   2598   3565    658       N
ATOM    701  CA  LYS A 434     -31.155 -18.681 -43.013  1.00 68.58           C
ANISOU  701  CA  LYS A 434     8382   6260  11414   2807   3617    730       C
ATOM    702  C   LYS A 434     -29.768 -18.812 -43.621  1.00 70.99           C
ANISOU  702  C   LYS A 434     8527   6628  11820   2935   3636    668       C
ATOM    703  O   LYS A 434     -29.551 -18.454 -44.780  1.00 68.84           O
ANISOU  703  O   LYS A 434     8202   6399  11555   2823   3710    547       O
ATOM    704  CB  LYS A 434     -31.998 -19.926 -43.314  1.00 69.09           C
ANISOU  704  CB  LYS A 434     8675   6082  11493   2752   3800    721       C
ATOM    705  CG  LYS A 434     -31.450 -21.166 -42.627  1.00 74.30           C
ANISOU  705  CG  LYS A 434     9402   6601  12227   2978   3847    825       C
ATOM    706  CD  LYS A 434     -32.386 -22.363 -42.659  1.00 79.60           C
ANISOU  706  CD  LYS A 434    10308   7021  12915   2921   4021    841       C
ATOM    707  CE  LYS A 434     -31.664 -23.604 -42.114  1.00 83.54           C
ANISOU  707  CE  LYS A 434    10869   7376  13498   3164   4077    938       C
ATOM    708  NZ  LYS A 434     -32.543 -24.803 -41.979  1.00 84.67           N
ANISOU  708  NZ  LYS A 434    11244   7260  13668   3122   4252    974       N
ATOM    709  N   SER A 435     -28.829 -19.293 -42.812  1.00 77.86           N
ANISOU  709  N   SER A 435     9314   7509  12759   3176   3563    751       N
ATOM    710  CA  SER A 435     -27.454 -19.544 -43.251  1.00 84.61           C
ANISOU  710  CA  SER A 435    10001   8417  13731   3333   3579    699       C
ATOM    711  C   SER A 435     -26.712 -18.287 -43.706  1.00 83.28           C
ANISOU  711  C   SER A 435     9588   8470  13583   3273   3495    618       C
ATOM    712  O   SER A 435     -25.867 -18.340 -44.592  1.00 86.98           O
ANISOU  712  O   SER A 435     9945   8974  14131   3295   3582    529       O
ATOM    713  CB  SER A 435     -27.396 -20.633 -44.336  1.00 86.47           C
ANISOU  713  CB  SER A 435    10358   8474  14023   3322   3797    616       C
ATOM    714  N   ALA A 436     -27.021 -17.157 -43.090  1.00 79.41           N
ANISOU  714  N   ALA A 436     9018   8127  13027   3200   3335    648       N
ATOM    715  CA  ALA A 436     -26.216 -15.968 -43.317  1.00 77.68           C
ANISOU  715  CA  ALA A 436     8549   8117  12849   3167   3239    586       C
ATOM    716  C   ALA A 436     -26.066 -15.066 -42.074  1.00 81.56           C
ANISOU  716  C   ALA A 436     8903   8768  13320   3235   3001    650       C
ATOM    717  O   ALA A 436     -26.422 -13.890 -42.130  1.00 79.94           O
ANISOU  717  O   ALA A 436     8635   8679  13059   3080   2929    620       O
ATOM    718  CB  ALA A 436     -26.771 -15.181 -44.503  1.00 66.02           C
ANISOU  718  CB  ALA A 436     7107   6669  11308   2911   3341    489       C
ATOM    719  N   SER A 437     -25.540 -15.579 -40.957  1.00 82.92           N
ANISOU  719  N   SER A 437     9030   8945  13529   3471   2870    732       N
ATOM    720  CA  SER A 437     -25.132 -16.969 -40.761  1.00 87.07           C
ANISOU  720  CA  SER A 437     9641   9325  14117   3677   2940    783       C
ATOM    721  C   SER A 437     -25.127 -17.207 -39.264  1.00 90.99           C
ANISOU  721  C   SER A 437    10168   9831  14574   3878   2753    909       C
ATOM    722  O   SER A 437     -25.899 -18.012 -38.738  1.00 91.12           O
ANISOU  722  O   SER A 437    10417   9688  14516   3916   2803   1014       O
ATOM    723  CB  SER A 437     -23.729 -17.232 -41.332  1.00 85.93           C
ANISOU  723  CB  SER A 437     9282   9241  14126   3815   2976    703       C
ATOM    724  OG  SER A 437     -23.395 -18.612 -41.279  1.00 79.86           O
ANISOU  724  OG  SER A 437     8615   8310  13418   4004   3068    744       O
ATOM    725  N   ASP A 438     -24.241 -16.486 -38.583  1.00 91.82           N
ANISOU  725  N   ASP A 438    10035  10125  14729   4006   2537    894       N
ATOM    726  CA  ASP A 438     -24.232 -16.450 -37.131  1.00 89.56           C
ANISOU  726  CA  ASP A 438     9760   9886  14384   4187   2315    998       C
ATOM    727  C   ASP A 438     -24.909 -15.175 -36.663  1.00 88.03           C
ANISOU  727  C   ASP A 438     9543   9821  14082   4037   2178    997       C
ATOM    728  O   ASP A 438     -24.645 -14.688 -35.563  1.00 87.39           O
ANISOU  728  O   ASP A 438     9376   9858  13970   4166   1945   1034       O
ATOM    729  CB  ASP A 438     -22.810 -16.520 -36.588  1.00 90.05           C
ANISOU  729  CB  ASP A 438     9568  10072  14575   4450   2129    970       C
ATOM    730  N   LEU A 439     -25.771 -14.627 -37.514  1.00 86.65           N
ANISOU  730  N   LEU A 439     9447   9625  13853   3770   2316    947       N
ATOM    731  CA  LEU A 439     -26.612 -13.504 -37.122  1.00 82.27           C
ANISOU  731  CA  LEU A 439     8916   9159  13185   3616   2218    954       C
ATOM    732  C   LEU A 439     -27.556 -14.028 -36.055  1.00 77.80           C
ANISOU  732  C   LEU A 439     8591   8489  12479   3687   2185   1096       C
ATOM    733  O   LEU A 439     -28.519 -14.727 -36.360  1.00 78.44           O
ANISOU  733  O   LEU A 439     8903   8402  12499   3591   2365   1146       O
ATOM    734  CB  LEU A 439     -27.404 -12.985 -38.324  1.00 81.26           C
ANISOU  734  CB  LEU A 439     8853   8998  13023   3329   2391    877       C
ATOM    735  CG  LEU A 439     -27.796 -11.509 -38.310  1.00 80.53           C
ANISOU  735  CG  LEU A 439     8669   9052  12878   3158   2289    827       C
ATOM    736  CD1 LEU A 439     -28.943 -11.239 -37.368  1.00 77.07           C
ANISOU  736  CD1 LEU A 439     8399   8595  12291   3128   2207    916       C
ATOM    737  CD2 LEU A 439     -26.588 -10.700 -37.903  1.00 84.76           C
ANISOU  737  CD2 LEU A 439     8910   9781  13514   3262   2099    771       C
ATOM    738  N   THR A 440     -27.268 -13.714 -34.801  1.00 75.35           N
ANISOU  738  N   THR A 440     8229   8280  12121   3857   1958   1160       N
ATOM    739  CA  THR A 440     -28.020 -14.297 -33.701  1.00 78.93           C
ANISOU  739  CA  THR A 440     8918   8640  12432   3961   1931   1314       C
ATOM    740  C   THR A 440     -28.110 -13.333 -32.532  1.00 83.97           C
ANISOU  740  C   THR A 440     9507   9434  12965   4025   1681   1348       C
ATOM    741  O   THR A 440     -27.479 -13.551 -31.497  1.00 87.54           O
ANISOU  741  O   THR A 440     9924   9940  13398   4259   1493   1412       O
ATOM    742  CB  THR A 440     -27.385 -15.622 -33.217  1.00 78.53           C
ANISOU  742  CB  THR A 440     8940   8476  12422   4217   1941   1408       C
ATOM    743  N   TRP A 441     -28.895 -12.270 -32.712  1.00 82.90           N
ANISOU  743  N   TRP A 441     9371   9369  12758   3821   1674   1302       N
ATOM    744  CA  TRP A 441     -29.108 -11.257 -31.683  1.00 85.68           C
ANISOU  744  CA  TRP A 441     9689   9864  13000   3854   1451   1322       C
ATOM    745  C   TRP A 441     -27.747 -10.724 -31.249  1.00 89.74           C
ANISOU  745  C   TRP A 441     9921  10552  13625   4018   1194   1244       C
ATOM    746  O   TRP A 441     -26.854 -10.594 -32.088  1.00 90.74           O
ANISOU  746  O   TRP A 441     9828  10727  13921   3990   1219   1128       O
ATOM    747  CB  TRP A 441     -29.902 -11.843 -30.506  1.00 87.38           C
ANISOU  747  CB  TRP A 441    10170  10000  13028   3971   1440   1490       C
ATOM    748  CG  TRP A 441     -30.592 -10.831 -29.639  1.00 86.96           C
ANISOU  748  CG  TRP A 441    10168  10058  12815   3936   1294   1517       C
ATOM    749  CD1 TRP A 441     -30.171 -10.372 -28.426  1.00 92.42           C
ANISOU  749  CD1 TRP A 441    10817  10882  13415   4114   1032   1554       C
ATOM    750  CD2 TRP A 441     -31.829 -10.161 -29.912  1.00 83.31           C
ANISOU  750  CD2 TRP A 441     9812   9583  12259   3717   1397   1505       C
ATOM    751  NE1 TRP A 441     -31.064  -9.455 -27.928  1.00 94.00           N
ANISOU  751  NE1 TRP A 441    11100  11154  13463   4020    974   1564       N
ATOM    752  CE2 TRP A 441     -32.092  -9.308 -28.821  1.00 86.78           C
ANISOU  752  CE2 TRP A 441    10272  10151  12550   3780   1197   1536       C
ATOM    753  CE3 TRP A 441     -32.737 -10.197 -30.972  1.00 81.47           C
ANISOU  753  CE3 TRP A 441     9657   9246  12054   3479   1628   1463       C
ATOM    754  CZ2 TRP A 441     -33.222  -8.499 -28.760  1.00 82.47           C
ANISOU  754  CZ2 TRP A 441     9818   9628  11887   3620   1234   1531       C
ATOM    755  CZ3 TRP A 441     -33.858  -9.394 -30.910  1.00 79.04           C
ANISOU  755  CZ3 TRP A 441     9431   8963  11639   3319   1653   1457       C
ATOM    756  CH2 TRP A 441     -34.092  -8.556 -29.812  1.00 80.79           C
ANISOU  756  CH2 TRP A 441     9668   9310  11718   3393   1464   1493       C
ATOM    757  N   ASP A 442     -27.602 -10.430 -29.955  1.00 91.41           N
ANISOU  757  N   ASP A 442    10137  10855  13740   4184    953   1304       N
ATOM    758  CA  ASP A 442     -26.331 -10.023 -29.343  1.00 91.85           C
ANISOU  758  CA  ASP A 442     9931  11068  13902   4367    670   1237       C
ATOM    759  C   ASP A 442     -25.459  -9.171 -30.257  1.00 89.79           C
ANISOU  759  C   ASP A 442     9339  10931  13846   4255    638   1051       C
ATOM    760  O   ASP A 442     -25.491  -7.936 -30.202  1.00 83.73           O
ANISOU  760  O   ASP A 442     8427  10298  13090   4141    515    960       O
ATOM    761  CB  ASP A 442     -25.539 -11.256 -28.891  1.00 94.95           C
ANISOU  761  CB  ASP A 442    10346  11389  14340   4628    632   1318       C
ATOM    762  CG  ASP A 442     -26.158 -11.942 -27.684  1.00 96.85           C
ANISOU  762  CG  ASP A 442    10880  11555  14365   4788    595   1508       C
ATOM    763  OD1 ASP A 442     -27.377 -11.781 -27.463  1.00 93.37           O
ANISOU  763  OD1 ASP A 442    10672  11061  13742   4668    702   1587       O
ATOM    764  OD2 ASP A 442     -25.423 -12.645 -26.955  1.00103.30           O
ANISOU  764  OD2 ASP A 442    11692  12367  15189   5038    466   1582       O
ATOM    765  N   ASN A 443     -24.704  -9.864 -31.112  1.00 90.65           N
ANISOU  765  N   ASN A 443     9342  10992  14110   4286    771    999       N
ATOM    766  CA  ASN A 443     -23.809  -9.252 -32.090  1.00 88.48           C
ANISOU  766  CA  ASN A 443     8769  10828  14022   4188    801    836       C
ATOM    767  C   ASN A 443     -24.559  -8.596 -33.250  1.00 86.22           C
ANISOU  767  C   ASN A 443     8528  10517  13716   3886   1025    786       C
ATOM    768  O   ASN A 443     -24.149  -8.695 -34.408  1.00 87.36           O
ANISOU  768  O   ASN A 443     8578  10646  13970   3779   1208    715       O
ATOM    769  CB  ASN A 443     -22.839 -10.304 -32.631  1.00 87.00           C
ANISOU  769  CB  ASN A 443     8491  10584  13979   4328    900    815       C
ATOM    770  N   LEU A 444     -25.658  -7.924 -32.929  1.00 82.16           N
ANISOU  770  N   LEU A 444     8163   9997  13056   3753   1008    827       N
ATOM    771  CA  LEU A 444     -26.492  -7.281 -33.928  1.00 77.15           C
ANISOU  771  CA  LEU A 444     7596   9329  12390   3474   1196    790       C
ATOM    772  C   LEU A 444     -25.898  -5.926 -34.288  1.00 76.29           C
ANISOU  772  C   LEU A 444     7212   9387  12389   3348   1109    662       C
ATOM    773  O   LEU A 444     -26.170  -5.380 -35.355  1.00 73.60           O
ANISOU  773  O   LEU A 444     6855   9032  12078   3123   1276    609       O
ATOM    774  CB  LEU A 444     -27.915  -7.126 -33.391  1.00 74.92           C
ANISOU  774  CB  LEU A 444     7578   8976  11913   3399   1210    885       C
ATOM    775  CG  LEU A 444     -29.062  -7.108 -34.401  1.00 73.88           C
ANISOU  775  CG  LEU A 444     7626   8728  11718   3154   1455    888       C
ATOM    776  CD1 LEU A 444     -28.716  -7.913 -35.647  1.00 76.91           C
ANISOU  776  CD1 LEU A 444     8013   9009  12202   3090   1680    849       C
ATOM    777  CD2 LEU A 444     -30.329  -7.638 -33.755  1.00 71.23           C
ANISOU  777  CD2 LEU A 444     7581   8277  11207   3164   1507   1011       C
ATOM    778  N   LYS A 445     -25.074  -5.397 -33.390  1.00 76.95           N
ANISOU  778  N   LYS A 445     7081   9625  12531   3494    845    613       N
ATOM    779  CA  LYS A 445     -24.430  -4.105 -33.594  1.00 75.96           C
ANISOU  779  CA  LYS A 445     6673   9670  12520   3385    745    492       C
ATOM    780  C   LYS A 445     -23.641  -4.083 -34.898  1.00 74.72           C
ANISOU  780  C   LYS A 445     6341   9525  12523   3258    947    417       C
ATOM    781  O   LYS A 445     -22.926  -5.028 -35.218  1.00 79.40           O
ANISOU  781  O   LYS A 445     6888  10085  13196   3381   1023    416       O
ATOM    782  CB  LYS A 445     -23.515  -3.783 -32.408  1.00 78.45           C
ANISOU  782  CB  LYS A 445     6770  10154  12886   3600    413    437       C
ATOM    783  CG  LYS A 445     -23.018  -2.347 -32.358  1.00 79.26           C
ANISOU  783  CG  LYS A 445     6598  10447  13068   3485    276    327       C
ATOM    784  CD  LYS A 445     -22.502  -2.003 -30.966  1.00 78.42           C
ANISOU  784  CD  LYS A 445     6359  10506  12931   3704    -92    285       C
ATOM    785  CE  LYS A 445     -20.994  -1.811 -30.943  1.00 77.51           C
ANISOU  785  CE  LYS A 445     5884  10615  12951   3813   -200    210       C
ATOM    786  NZ  LYS A 445     -20.554  -0.554 -31.609  1.00 75.35           N
ANISOU  786  NZ  LYS A 445     5355  10442  12831   3538   -123    164       N
ATOM    787  N   GLY A 446     -23.790  -3.004 -35.658  1.00 72.65           N
ANISOU  787  N   GLY A 446     5998   9299  12308   3010   1041    362       N
ATOM    788  CA  GLY A 446     -23.068  -2.855 -36.906  1.00 63.27           C
ANISOU  788  CA  GLY A 446     4661   8114  11266   2866   1241    301       C
ATOM    789  C   GLY A 446     -23.751  -3.523 -38.084  1.00 61.62           C
ANISOU  789  C   GLY A 446     4688   7732  10991   2739   1529    339       C
ATOM    790  O   GLY A 446     -23.302  -3.377 -39.215  1.00 61.97           O
ANISOU  790  O   GLY A 446     4660   7761  11125   2606   1714    294       O
ATOM    791  N   LYS A 447     -24.833  -4.252 -37.824  1.00 60.01           N
ANISOU  791  N   LYS A 447     4771   7400  10630   2778   1566    421       N
ATOM    792  CA  LYS A 447     -25.598  -4.903 -38.890  1.00 60.71           C
ANISOU  792  CA  LYS A 447     5096   7328  10644   2654   1818    450       C
ATOM    793  C   LYS A 447     -26.561  -3.963 -39.618  1.00 61.63           C
ANISOU  793  C   LYS A 447     5325   7413  10679   2396   1918    431       C
ATOM    794  O   LYS A 447     -26.609  -2.761 -39.337  1.00 60.54           O
ANISOU  794  O   LYS A 447     5078   7370  10556   2302   1810    400       O
ATOM    795  CB  LYS A 447     -26.365  -6.110 -38.349  1.00 60.34           C
ANISOU  795  CB  LYS A 447     5303   7146  10477   2785   1834    545       C
ATOM    796  CG  LYS A 447     -25.583  -7.410 -38.406  1.00 67.00           C
ANISOU  796  CG  LYS A 447     6132   7927  11397   2977   1891    563       C
ATOM    797  CD  LYS A 447     -24.421  -7.427 -37.436  1.00 70.41           C
ANISOU  797  CD  LYS A 447     6331   8490  11931   3209   1672    548       C
ATOM    798  CE  LYS A 447     -23.467  -8.570 -37.741  1.00 69.64           C
ANISOU  798  CE  LYS A 447     6169   8346  11943   3383   1749    541       C
ATOM    799  NZ  LYS A 447     -22.270  -8.501 -36.864  1.00 74.49           N
ANISOU  799  NZ  LYS A 447     6524   9110  12670   3611   1520    504       N
ATOM    800  N   LYS A 448     -27.328  -4.522 -40.554  1.00 54.37           N
ANISOU  800  N   LYS A 448     4624   6359   9674   2288   2116    445       N
ATOM    801  CA  LYS A 448     -28.232  -3.727 -41.378  1.00 51.98           C
ANISOU  801  CA  LYS A 448     4442   6024   9285   2059   2214    420       C
ATOM    802  C   LYS A 448     -29.687  -4.081 -41.076  1.00 52.40           C
ANISOU  802  C   LYS A 448     4758   5978   9172   2025   2222    476       C
ATOM    803  O   LYS A 448     -30.089  -5.237 -41.186  1.00 54.59           O
ANISOU  803  O   LYS A 448     5199   6138   9403   2083   2313    512       O
ATOM    804  CB  LYS A 448     -27.930  -3.934 -42.863  1.00 55.54           C
ANISOU  804  CB  LYS A 448     4920   6417   9765   1944   2430    368       C
ATOM    805  CG  LYS A 448     -26.505  -3.550 -43.278  1.00 56.42           C
ANISOU  805  CG  LYS A 448     4771   6620  10045   1956   2460    315       C
ATOM    806  CD  LYS A 448     -26.208  -3.970 -44.712  1.00 59.17           C
ANISOU  806  CD  LYS A 448     5180   6898  10404   1880   2689    276       C
ATOM    807  CE  LYS A 448     -24.946  -3.298 -45.240  1.00 65.54           C
ANISOU  807  CE  LYS A 448     5739   7797  11366   1838   2745    226       C
ATOM    808  NZ  LYS A 448     -24.420  -3.968 -46.467  1.00 69.02           N
ANISOU  808  NZ  LYS A 448     6214   8175  11834   1835   2963    194       N
ATOM    809  N   SER A 449     -30.478  -3.082 -40.706  1.00 47.94           N
ANISOU  809  N   SER A 449     4229   5456   8528   1928   2135    480       N
ATOM    810  CA  SER A 449     -31.832  -3.331 -40.217  1.00 47.15           C
ANISOU  810  CA  SER A 449     4349   5286   8280   1912   2121    535       C
ATOM    811  C   SER A 449     -32.921  -2.799 -41.151  1.00 45.94           C
ANISOU  811  C   SER A 449     4343   5086   8026   1705   2224    497       C
ATOM    812  O   SER A 449     -32.754  -1.771 -41.812  1.00 43.43           O
ANISOU  812  O   SER A 449     3950   4825   7728   1575   2240    443       O
ATOM    813  CB  SER A 449     -32.000  -2.728 -38.823  1.00 45.89           C
ANISOU  813  CB  SER A 449     4137   5213   8086   2010   1915    579       C
ATOM    814  OG  SER A 449     -31.891  -1.310 -38.873  1.00 45.08           O
ANISOU  814  OG  SER A 449     3901   5213   8015   1900   1833    526       O
ATOM    815  N   CYS A 450     -34.040  -3.515 -41.200  1.00 45.30           N
ANISOU  815  N   CYS A 450     4473   4900   7841   1679   2293    525       N
ATOM    816  CA  CYS A 450     -35.195  -3.085 -41.976  1.00 43.19           C
ANISOU  816  CA  CYS A 450     4349   4594   7466   1503   2361    483       C
ATOM    817  C   CYS A 450     -36.394  -2.918 -41.044  1.00 44.69           C
ANISOU  817  C   CYS A 450     4652   4776   7551   1506   2284    533       C
ATOM    818  O   CYS A 450     -36.726  -3.825 -40.270  1.00 46.33           O
ANISOU  818  O   CYS A 450     4947   4918   7739   1610   2285    602       O
ATOM    819  CB  CYS A 450     -35.502  -4.079 -43.092  1.00 41.47           C
ANISOU  819  CB  CYS A 450     4270   4257   7230   1444   2528    441       C
ATOM    820  SG  CYS A 450     -34.100  -4.342 -44.229  1.00 43.41           S
ANISOU  820  SG  CYS A 450     4401   4508   7586   1456   2643    384       S
ATOM    821  N   HIS A 451     -37.027  -1.749 -41.119  1.00 41.74           N
ANISOU  821  N   HIS A 451     4280   4467   7112   1396   2227    503       N
ATOM    822  CA  HIS A 451     -38.150  -1.407 -40.253  1.00 38.20           C
ANISOU  822  CA  HIS A 451     3921   4030   6564   1396   2152    542       C
ATOM    823  C   HIS A 451     -39.377  -1.017 -41.083  1.00 38.13           C
ANISOU  823  C   HIS A 451     4037   3993   6456   1230   2211    484       C
ATOM    824  O   HIS A 451     -39.235  -0.430 -42.152  1.00 34.87           O
ANISOU  824  O   HIS A 451     3606   3603   6040   1120   2251    417       O
ATOM    825  CB  HIS A 451     -37.746  -0.229 -39.369  1.00 42.86           C
ANISOU  825  CB  HIS A 451     4373   4740   7170   1447   1994    557       C
ATOM    826  CG  HIS A 451     -36.447  -0.427 -38.658  1.00 38.43           C
ANISOU  826  CG  HIS A 451     3652   4234   6717   1605   1902    587       C
ATOM    827  ND1 HIS A 451     -36.373  -0.863 -37.353  1.00 39.27           N
ANISOU  827  ND1 HIS A 451     3770   4356   6796   1782   1793    664       N
ATOM    828  CD2 HIS A 451     -35.169  -0.258 -39.072  1.00 39.80           C
ANISOU  828  CD2 HIS A 451     3646   4454   7021   1619   1898    547       C
ATOM    829  CE1 HIS A 451     -35.106  -0.945 -36.992  1.00 47.54           C
ANISOU  829  CE1 HIS A 451     4648   5465   7951   1906   1703    663       C
ATOM    830  NE2 HIS A 451     -34.355  -0.586 -38.018  1.00 41.40           N
ANISOU  830  NE2 HIS A 451     3740   4708   7283   1804   1770    588       N
ATOM    831  N   THR A 452     -40.578  -1.324 -40.597  1.00 34.41           N
ANISOU  831  N   THR A 452     3692   3477   5905   1219   2216    510       N
ATOM    832  CA  THR A 452     -41.783  -0.957 -41.331  1.00 33.11           C
ANISOU  832  CA  THR A 452     3627   3299   5653   1074   2249    443       C
ATOM    833  C   THR A 452     -41.846   0.557 -41.459  1.00 32.03           C
ANISOU  833  C   THR A 452     3425   3273   5473   1010   2160    411       C
ATOM    834  O   THR A 452     -42.090   1.076 -42.538  1.00 31.53           O
ANISOU  834  O   THR A 452     3388   3222   5370    898   2191    343       O
ATOM    835  CB  THR A 452     -43.068  -1.470 -40.657  1.00 32.64           C
ANISOU  835  CB  THR A 452     3685   3183   5536   1073   2268    475       C
ATOM    836  OG1 THR A 452     -43.167  -0.915 -39.337  1.00 37.13           O
ANISOU  836  OG1 THR A 452     4223   3817   6067   1169   2167    551       O
ATOM    837  CG2 THR A 452     -43.073  -2.993 -40.584  1.00 33.90           C
ANISOU  837  CG2 THR A 452     3923   3205   5752   1122   2386    509       C
ATOM    838  N   ALA A 453     -41.622   1.245 -40.340  1.00 35.62           N
ANISOU  838  N   ALA A 453     3803   3799   5933   1093   2049    463       N
ATOM    839  CA  ALA A 453     -41.458   2.697 -40.289  1.00 34.82           C
ANISOU  839  CA  ALA A 453     3614   3789   5826   1054   1963    439       C
ATOM    840  C   ALA A 453     -41.159   3.115 -38.855  1.00 35.19           C
ANISOU  840  C   ALA A 453     3583   3898   5891   1189   1834    497       C
ATOM    841  O   ALA A 453     -41.519   2.415 -37.909  1.00 33.85           O
ANISOU  841  O   ALA A 453     3478   3705   5678   1296   1813    559       O
ATOM    842  CB  ALA A 453     -42.703   3.413 -40.778  1.00 36.05           C
ANISOU  842  CB  ALA A 453     3865   3958   5873    940   1966    394       C
ATOM    843  N   VAL A 454     -40.512   4.264 -38.699  1.00 31.96           N
ANISOU  843  N   VAL A 454     3038   3560   5545   1186   1749    475       N
ATOM    844  CA  VAL A 454     -40.284   4.830 -37.383  1.00 32.37           C
ANISOU  844  CA  VAL A 454     3042   3686   5572   1279   1559    500       C
ATOM    845  C   VAL A 454     -41.616   5.003 -36.669  1.00 35.56           C
ANISOU  845  C   VAL A 454     3604   4098   5808   1281   1502    522       C
ATOM    846  O   VAL A 454     -42.553   5.576 -37.231  1.00 32.93           O
ANISOU  846  O   VAL A 454     3351   3759   5401   1161   1534    483       O
ATOM    847  CB  VAL A 454     -39.611   6.210 -37.482  1.00 32.31           C
ANISOU  847  CB  VAL A 454     2909   3743   5625   1191   1440    439       C
ATOM    848  CG1 VAL A 454     -39.633   6.911 -36.132  1.00 32.56           C
ANISOU  848  CG1 VAL A 454     2934   3850   5586   1261   1217    436       C
ATOM    849  CG2 VAL A 454     -38.173   6.081 -38.026  1.00 33.71           C
ANISOU  849  CG2 VAL A 454     2889   3924   5995   1196   1493    419       C
ATOM    850  N   GLY A 455     -41.706   4.503 -35.441  1.00 32.89           N
ANISOU  850  N   GLY A 455     3314   3776   5406   1427   1425    587       N
ATOM    851  CA  GLY A 455     -42.902   4.706 -34.637  1.00 32.65           C
ANISOU  851  CA  GLY A 455     3427   3762   5218   1443   1381    613       C
ATOM    852  C   GLY A 455     -43.918   3.580 -34.646  1.00 34.74           C
ANISOU  852  C   GLY A 455     3825   3939   5434   1459   1543    670       C
ATOM    853  O   GLY A 455     -44.875   3.600 -33.862  1.00 37.71           O
ANISOU  853  O   GLY A 455     4312   4326   5692   1490   1531    707       O
ATOM    854  N   ARG A 456     -43.729   2.597 -35.521  1.00 35.63           N
ANISOU  854  N   ARG A 456     3931   3962   5647   1434   1705    672       N
ATOM    855  CA  ARG A 456     -44.637   1.447 -35.561  1.00 36.66           C
ANISOU  855  CA  ARG A 456     4188   3990   5751   1419   1852    711       C
ATOM    856  C   ARG A 456     -44.250   0.336 -34.569  1.00 37.65           C
ANISOU  856  C   ARG A 456     4373   4060   5872   1584   1873    824       C
ATOM    857  O   ARG A 456     -43.078   0.188 -34.216  1.00 39.95           O
ANISOU  857  O   ARG A 456     4587   4381   6212   1705   1793    857       O
ATOM    858  CB  ARG A 456     -44.792   0.918 -36.994  1.00 32.90           C
ANISOU  858  CB  ARG A 456     3725   3442   5335   1262   1968    635       C
ATOM    859  CG  ARG A 456     -45.614   1.867 -37.871  1.00 33.22           C
ANISOU  859  CG  ARG A 456     3769   3526   5328   1109   1957    541       C
ATOM    860  CD  ARG A 456     -45.664   1.476 -39.341  1.00 35.93           C
ANISOU  860  CD  ARG A 456     4130   3817   5704    976   2040    457       C
ATOM    861  NE  ARG A 456     -46.276   0.172 -39.594  1.00 29.80           N
ANISOU  861  NE  ARG A 456     3443   2928   4951    943   2154    451       N
ATOM    862  CZ  ARG A 456     -46.714  -0.225 -40.790  1.00 32.01           C
ANISOU  862  CZ  ARG A 456     3765   3158   5239    828   2222    360       C
ATOM    863  NH1 ARG A 456     -46.649   0.590 -41.837  1.00 29.20           N
ANISOU  863  NH1 ARG A 456     3387   2864   4844    747   2190    281       N
ATOM    864  NH2 ARG A 456     -47.238  -1.433 -40.947  1.00 33.48           N
ANISOU  864  NH2 ARG A 456     4023   3228   5471    801   2331    346       N
ATOM    865  N   THR A 457     -45.247  -0.438 -34.137  1.00 37.59           N
ANISOU  865  N   THR A 457     4498   3971   5813   1589   1983    884       N
ATOM    866  CA  THR A 457     -45.084  -1.425 -33.070  1.00 40.41           C
ANISOU  866  CA  THR A 457     4951   4266   6136   1753   2021   1015       C
ATOM    867  C   THR A 457     -44.022  -2.486 -33.338  1.00 41.92           C
ANISOU  867  C   THR A 457     5121   4384   6422   1820   2061   1050       C
ATOM    868  O   THR A 457     -43.003  -2.536 -32.649  1.00 44.88           O
ANISOU  868  O   THR A 457     5453   4812   6788   1983   1947   1106       O
ATOM    869  CB  THR A 457     -46.411  -2.143 -32.733  1.00 34.48           C
ANISOU  869  CB  THR A 457     4345   3410   5345   1713   2187   1072       C
ATOM    870  OG1 THR A 457     -47.409  -1.182 -32.369  1.00 33.44           O
ANISOU  870  OG1 THR A 457     4230   3356   5119   1671   2153   1043       O
ATOM    871  CG2 THR A 457     -46.204  -3.083 -31.567  1.00 38.04           C
ANISOU  871  CG2 THR A 457     4916   3795   5742   1895   2236   1228       C
ATOM    872  N   ALA A 458     -44.264  -3.344 -34.324  1.00 43.33           N
ANISOU  872  N   ALA A 458     5330   4444   6691   1701   2212   1009       N
ATOM    873  CA  ALA A 458     -43.320  -4.419 -34.639  1.00 42.11           C
ANISOU  873  CA  ALA A 458     5166   4205   6629   1764   2270   1036       C
ATOM    874  C   ALA A 458     -42.061  -3.888 -35.314  1.00 39.69           C
ANISOU  874  C   ALA A 458     4697   3986   6396   1766   2169    959       C
ATOM    875  O   ALA A 458     -40.964  -4.430 -35.133  1.00 40.27           O
ANISOU  875  O   ALA A 458     4718   4056   6528   1891   2139    996       O
ATOM    876  CB  ALA A 458     -43.986  -5.484 -35.521  1.00 37.40           C
ANISOU  876  CB  ALA A 458     4657   3446   6109   1635   2464   1000       C
ATOM    877  N   GLY A 459     -42.223  -2.829 -36.098  1.00 35.68           N
ANISOU  877  N   GLY A 459     4110   3556   5892   1629   2124    853       N
ATOM    878  CA  GLY A 459     -41.130  -2.317 -36.903  1.00 37.21           C
ANISOU  878  CA  GLY A 459     4156   3814   6167   1596   2073    777       C
ATOM    879  C   GLY A 459     -40.160  -1.441 -36.135  1.00 40.23           C
ANISOU  879  C   GLY A 459     4396   4326   6565   1716   1899    793       C
ATOM    880  O   GLY A 459     -39.020  -1.251 -36.571  1.00 36.97           O
ANISOU  880  O   GLY A 459     3839   3957   6252   1730   1864    751       O
ATOM    881  N   TRP A 460     -40.596  -0.917 -34.990  1.00 36.02           N
ANISOU  881  N   TRP A 460     3897   3853   5937   1804   1791    847       N
ATOM    882  CA  TRP A 460     -39.786   0.050 -34.247  1.00 44.61           C
ANISOU  882  CA  TRP A 460     4847   5068   7033   1910   1599    841       C
ATOM    883  C   TRP A 460     -39.894  -0.034 -32.717  1.00 47.94           C
ANISOU  883  C   TRP A 460     5343   5534   7336   2105   1471    938       C
ATOM    884  O   TRP A 460     -38.918  -0.342 -32.033  1.00 50.76           O
ANISOU  884  O   TRP A 460     5637   5937   7713   2271   1353    977       O
ATOM    885  CB  TRP A 460     -40.121   1.469 -34.707  1.00 36.77           C
ANISOU  885  CB  TRP A 460     3783   4148   6042   1776   1552    755       C
ATOM    886  CG  TRP A 460     -39.211   2.525 -34.165  1.00 38.65           C
ANISOU  886  CG  TRP A 460     3854   4504   6326   1836   1358    721       C
ATOM    887  CD1 TRP A 460     -39.423   3.310 -33.064  1.00 40.66           C
ANISOU  887  CD1 TRP A 460     4140   4849   6459   1884   1163    719       C
ATOM    888  CD2 TRP A 460     -37.945   2.928 -34.706  1.00 36.55           C
ANISOU  888  CD2 TRP A 460     3375   4282   6228   1810   1320    658       C
ATOM    889  NE1 TRP A 460     -38.374   4.184 -32.896  1.00 36.62           N
ANISOU  889  NE1 TRP A 460     3449   4432   6035   1882    990    648       N
ATOM    890  CE2 TRP A 460     -37.453   3.968 -33.888  1.00 45.00           C
ANISOU  890  CE2 TRP A 460     4347   5466   7284   1832   1088    613       C
ATOM    891  CE3 TRP A 460     -37.184   2.515 -35.807  1.00 37.05           C
ANISOU  891  CE3 TRP A 460     3347   4308   6424   1736   1441    618       C
ATOM    892  CZ2 TRP A 460     -36.227   4.591 -34.130  1.00 43.29           C
ANISOU  892  CZ2 TRP A 460     3900   5313   7236   1800   1000    540       C
ATOM    893  CZ3 TRP A 460     -35.974   3.131 -36.047  1.00 38.16           C
ANISOU  893  CZ3 TRP A 460     3263   4515   6723   1720   1375    559       C
ATOM    894  CH2 TRP A 460     -35.506   4.161 -35.213  1.00 47.04           C
ANISOU  894  CH2 TRP A 460     4249   5741   7884   1756   1165    525       C
ATOM    895  N   ASN A 461     -41.072   0.254 -32.180  1.00 43.71           N
ANISOU  895  N   ASN A 461     4946   4995   6666   2091   1489    972       N
ATOM    896  CA  ASN A 461     -41.225   0.359 -30.736  1.00 39.68           C
ANISOU  896  CA  ASN A 461     4527   4545   6007   2271   1363   1057       C
ATOM    897  C   ASN A 461     -40.768  -0.883 -29.975  1.00 42.18           C
ANISOU  897  C   ASN A 461     4933   4810   6283   2446   1373   1172       C
ATOM    898  O   ASN A 461     -39.995  -0.779 -29.028  1.00 42.22           O
ANISOU  898  O   ASN A 461     4909   4903   6230   2625   1192   1207       O
ATOM    899  CB  ASN A 461     -42.665   0.734 -30.361  1.00 39.29           C
ANISOU  899  CB  ASN A 461     4630   4486   5813   2207   1421   1074       C
ATOM    900  CG  ASN A 461     -43.044   2.125 -30.837  1.00 38.89           C
ANISOU  900  CG  ASN A 461     4512   4521   5745   2027   1329    948       C
ATOM    901  OD1 ASN A 461     -42.179   2.940 -31.158  1.00 45.25           O
ANISOU  901  OD1 ASN A 461     5168   5401   6625   1985   1196    864       O
ATOM    902  ND2 ASN A 461     -44.338   2.401 -30.888  1.00 35.77           N
ANISOU  902  ND2 ASN A 461     4221   4107   5262   1921   1408    935       N
ATOM    903  N   ILE A 462     -41.244  -2.052 -30.392  1.00 40.89           N
ANISOU  903  N   ILE A 462     4881   4505   6149   2394   1576   1227       N
ATOM    904  CA  ILE A 462     -40.861  -3.293 -29.736  1.00 45.84           C
ANISOU  904  CA  ILE A 462     5610   5061   6746   2554   1616   1345       C
ATOM    905  C   ILE A 462     -39.344  -3.566 -29.800  1.00 52.12           C
ANISOU  905  C   ILE A 462     6255   5902   7645   2674   1491   1325       C
ATOM    906  O   ILE A 462     -38.713  -3.730 -28.755  1.00 54.32           O
ANISOU  906  O   ILE A 462     6549   6244   7845   2873   1341   1391       O
ATOM    907  CB  ILE A 462     -41.661  -4.508 -30.265  1.00 46.42           C
ANISOU  907  CB  ILE A 462     5821   4952   6863   2459   1876   1396       C
ATOM    908  CG1 ILE A 462     -43.149  -4.329 -29.980  1.00 42.47           C
ANISOU  908  CG1 ILE A 462     5461   4409   6268   2371   1995   1429       C
ATOM    909  CG2 ILE A 462     -41.147  -5.791 -29.634  1.00 46.80           C
ANISOU  909  CG2 ILE A 462     5970   4917   6896   2629   1923   1521       C
ATOM    910  CD1 ILE A 462     -43.452  -4.202 -28.505  1.00 49.90           C
ANISOU  910  CD1 ILE A 462     6537   5406   7018   2544   1927   1547       C
ATOM    911  N   PRO A 463     -38.752  -3.601 -31.014  1.00 46.78           N
ANISOU  911  N   PRO A 463     5433   5202   7140   2558   1548   1228       N
ATOM    912  CA  PRO A 463     -37.320  -3.921 -31.065  1.00 51.97           C
ANISOU  912  CA  PRO A 463     5936   5900   7910   2679   1448   1208       C
ATOM    913  C   PRO A 463     -36.443  -2.819 -30.482  1.00 52.15           C
ANISOU  913  C   PRO A 463     5775   6094   7944   2772   1190   1149       C
ATOM    914  O   PRO A 463     -35.560  -3.117 -29.681  1.00 49.52           O
ANISOU  914  O   PRO A 463     5392   5819   7604   2965   1035   1185       O
ATOM    915  CB  PRO A 463     -37.039  -4.050 -32.567  1.00 52.42           C
ANISOU  915  CB  PRO A 463     5890   5899   8128   2508   1591   1108       C
ATOM    916  CG  PRO A 463     -38.377  -4.171 -33.216  1.00 47.17           C
ANISOU  916  CG  PRO A 463     5372   5133   7419   2323   1775   1099       C
ATOM    917  CD  PRO A 463     -39.300  -3.393 -32.365  1.00 46.01           C
ANISOU  917  CD  PRO A 463     5307   5044   7130   2327   1701   1133       C
ATOM    918  N   MET A 464     -36.678  -1.569 -30.880  1.00 53.50           N
ANISOU  918  N   MET A 464     5846   6343   8141   2636   1141   1056       N
ATOM    919  CA  MET A 464     -35.875  -0.458 -30.377  1.00 51.04           C
ANISOU  919  CA  MET A 464     5343   6186   7864   2702    901    987       C
ATOM    920  C   MET A 464     -36.062  -0.308 -28.876  1.00 54.13           C
ANISOU  920  C   MET A 464     5846   6657   8064   2891    709   1057       C
ATOM    921  O   MET A 464     -35.119   0.026 -28.161  1.00 59.56           O
ANISOU  921  O   MET A 464     6404   7463   8764   3034    476   1026       O
ATOM    922  CB  MET A 464     -36.209   0.844 -31.104  1.00 49.03           C
ANISOU  922  CB  MET A 464     4984   5976   7671   2510    912    885       C
ATOM    923  CG  MET A 464     -35.863   0.803 -32.568  1.00 41.65           C
ANISOU  923  CG  MET A 464     3937   4983   6905   2329   1079    809       C
ATOM    924  SD  MET A 464     -34.330  -0.134 -32.810  1.00 59.27           S
ANISOU  924  SD  MET A 464     6004   7216   9299   2443   1068    797       S
ATOM    925  CE  MET A 464     -33.694   0.638 -34.288  1.00 57.69           C
ANISOU  925  CE  MET A 464     5597   7033   9290   2226   1173    672       C
ATOM    926  N   GLY A 465     -37.280  -0.571 -28.407  1.00 48.87           N
ANISOU  926  N   GLY A 465     5420   5930   7218   2888    807   1144       N
ATOM    927  CA  GLY A 465     -37.545  -0.639 -26.980  1.00 47.23           C
ANISOU  927  CA  GLY A 465     5375   5781   6792   3070    673   1230       C
ATOM    928  C   GLY A 465     -36.574  -1.598 -26.298  1.00 51.16           C
ANISOU  928  C   GLY A 465     5875   6285   7279   3277    577   1300       C
ATOM    929  O   GLY A 465     -35.854  -1.201 -25.386  1.00 50.44           O
ANISOU  929  O   GLY A 465     5723   6323   7121   3433    324   1279       O
ATOM    930  N   LEU A 466     -36.547  -2.852 -26.751  1.00 49.63           N
ANISOU  930  N   LEU A 466     5751   5952   7153   3280    769   1374       N
ATOM    931  CA  LEU A 466     -35.675  -3.882 -26.171  1.00 56.57           C
ANISOU  931  CA  LEU A 466     6651   6814   8031   3482    707   1453       C
ATOM    932  C   LEU A 466     -34.205  -3.550 -26.366  1.00 61.70           C
ANISOU  932  C   LEU A 466     7019   7568   8855   3553    503   1348       C
ATOM    933  O   LEU A 466     -33.370  -3.832 -25.506  1.00 71.25           O
ANISOU  933  O   LEU A 466     8196   8848  10028   3755    313   1378       O
ATOM    934  CB  LEU A 466     -35.974  -5.242 -26.795  1.00 52.12           C
ANISOU  934  CB  LEU A 466     6207   6065   7533   3444    975   1535       C
ATOM    935  CG  LEU A 466     -37.396  -5.754 -26.581  1.00 57.79           C
ANISOU  935  CG  LEU A 466     7186   6660   8110   3376   1199   1645       C
ATOM    936  CD1 LEU A 466     -37.650  -6.983 -27.429  1.00 58.03           C
ANISOU  936  CD1 LEU A 466     7290   6502   8258   3294   1462   1686       C
ATOM    937  CD2 LEU A 466     -37.631  -6.061 -25.112  1.00 59.99           C
ANISOU  937  CD2 LEU A 466     7665   6971   8156   3576   1125   1779       C
ATOM    938  N   LEU A 467     -33.901  -2.953 -27.513  1.00 63.51           N
ANISOU  938  N   LEU A 467     7043   7808   9279   3383    553   1224       N
ATOM    939  CA  LEU A 467     -32.543  -2.552 -27.862  1.00 64.42           C
ANISOU  939  CA  LEU A 467     6857   8019   9599   3411    401   1108       C
ATOM    940  C   LEU A 467     -32.041  -1.440 -26.934  1.00 63.43           C
ANISOU  940  C   LEU A 467     6596   8073   9433   3498     88   1039       C
ATOM    941  O   LEU A 467     -30.891  -1.453 -26.480  1.00 67.72           O
ANISOU  941  O   LEU A 467     6956   8707  10066   3636   -121    996       O
ATOM    942  CB  LEU A 467     -32.517  -2.065 -29.313  1.00 61.51           C
ANISOU  942  CB  LEU A 467     6336   7621   9415   3180    565   1000       C
ATOM    943  CG  LEU A 467     -31.249  -2.284 -30.138  1.00 64.16           C
ANISOU  943  CG  LEU A 467     6420   7974   9984   3173    581    910       C
ATOM    944  CD1 LEU A 467     -31.347  -3.585 -30.930  1.00 64.28           C
ANISOU  944  CD1 LEU A 467     6553   7833  10037   3152    829    964       C
ATOM    945  CD2 LEU A 467     -30.981  -1.092 -31.054  1.00 57.03           C
ANISOU  945  CD2 LEU A 467     5299   7141   9230   2973    600    778       C
ATOM    946  N   TYR A 468     -32.920  -0.481 -26.663  1.00 61.88           N
ANISOU  946  N   TYR A 468     6484   7925   9104   3412     53   1020       N
ATOM    947  CA  TYR A 468     -32.581   0.692 -25.872  1.00 68.43           C
ANISOU  947  CA  TYR A 468     7200   8921   9878   3461   -236    931       C
ATOM    948  C   TYR A 468     -32.224   0.322 -24.437  1.00 74.61           C
ANISOU  948  C   TYR A 468     8091   9785  10474   3694   -464    992       C
ATOM    949  O   TYR A 468     -31.382   0.973 -23.814  1.00 77.62           O
ANISOU  949  O   TYR A 468     8305  10311  10875   3769   -747    900       O
ATOM    950  CB  TYR A 468     -33.747   1.681 -25.892  1.00 70.10           C
ANISOU  950  CB  TYR A 468     7531   9147   9955   3330   -195    906       C
ATOM    951  CG  TYR A 468     -33.532   2.935 -25.080  1.00 74.21           C
ANISOU  951  CG  TYR A 468     7973   9834  10390   3368   -490    793       C
ATOM    952  CD1 TYR A 468     -32.445   3.766 -25.322  1.00 77.01           C
ANISOU  952  CD1 TYR A 468     8012  10302  10947   3325   -681    638       C
ATOM    953  CD2 TYR A 468     -34.432   3.302 -24.086  1.00 72.06           C
ANISOU  953  CD2 TYR A 468     7941   9601   9836   3431   -572    822       C
ATOM    954  CE1 TYR A 468     -32.249   4.922 -24.586  1.00 76.89           C
ANISOU  954  CE1 TYR A 468     7938  10416  10860   3301   -963    495       C
ATOM    955  CE2 TYR A 468     -34.248   4.459 -23.346  1.00 73.92           C
ANISOU  955  CE2 TYR A 468     8125   9981   9979   3455   -853    690       C
ATOM    956  CZ  TYR A 468     -33.155   5.266 -23.601  1.00 75.72           C
ANISOU  956  CZ  TYR A 468     8051  10301  10417   3369  -1053    517       C
ATOM    957  OH  TYR A 468     -32.964   6.419 -22.865  1.00 74.95           O
ANISOU  957  OH  TYR A 468     7911  10323  10243   3346  -1335    358       O
ATOM    958  N   ASN A 469     -32.870  -0.724 -23.922  1.00 74.37           N
ANISOU  958  N   ASN A 469     8341   9657  10258   3797   -334   1146       N
ATOM    959  CA  ASN A 469     -32.606  -1.215 -22.574  1.00 76.09           C
ANISOU  959  CA  ASN A 469     8706   9937  10269   4027   -505   1232       C
ATOM    960  C   ASN A 469     -31.140  -1.572 -22.394  1.00 78.79           C
ANISOU  960  C   ASN A 469     8824  10345  10768   4169   -699   1195       C
ATOM    961  O   ASN A 469     -30.569  -1.367 -21.320  1.00 84.80           O
ANISOU  961  O   ASN A 469     9574  11237  11408   4329   -963   1181       O
ATOM    962  CB  ASN A 469     -33.473  -2.438 -22.257  1.00 78.07           C
ANISOU  962  CB  ASN A 469     9272  10043  10347   4098   -269   1415       C
ATOM    963  CG  ASN A 469     -34.949  -2.105 -22.185  1.00 81.42           C
ANISOU  963  CG  ASN A 469     9924  10416  10594   3983    -96   1461       C
ATOM    964  OD1 ASN A 469     -35.485  -1.817 -21.116  1.00 83.96           O
ANISOU  964  OD1 ASN A 469    10435  10807  10661   4076   -178   1504       O
ATOM    965  ND2 ASN A 469     -35.616  -2.141 -23.327  1.00 81.77           N
ANISOU  965  ND2 ASN A 469     9953  10345  10773   3782    148   1448       N
ATOM    966  N   LYS A 470     -30.535  -2.098 -23.455  1.00 74.85           N
ANISOU  966  N   LYS A 470     8145   9761  10535   4109   -565   1170       N
ATOM    967  CA  LYS A 470     -29.152  -2.548 -23.392  1.00 80.77           C
ANISOU  967  CA  LYS A 470     8667  10554  11467   4245   -712   1140       C
ATOM    968  C   LYS A 470     -28.178  -1.384 -23.481  1.00 83.82           C
ANISOU  968  C   LYS A 470     8703  11100  12043   4184   -955    972       C
ATOM    969  O   LYS A 470     -27.447  -1.107 -22.532  1.00 84.87           O
ANISOU  969  O   LYS A 470     8746  11374  12125   4319  -1235    944       O
ATOM    970  CB  LYS A 470     -28.859  -3.561 -24.502  1.00 77.80           C
ANISOU  970  CB  LYS A 470     8235  10026  11298   4208   -467   1162       C
ATOM    971  N   ILE A 471     -28.186  -0.698 -24.620  1.00 82.51           N
ANISOU  971  N   ILE A 471     8345  10917  12089   3973   -837    860       N
ATOM    972  CA  ILE A 471     -27.180   0.324 -24.917  1.00 79.53           C
ANISOU  972  CA  ILE A 471     7595  10669  11955   3883  -1004    707       C
ATOM    973  C   ILE A 471     -27.339   1.637 -24.132  1.00 82.21           C
ANISOU  973  C   ILE A 471     7909  11172  12155   3838  -1258    611       C
ATOM    974  O   ILE A 471     -26.366   2.370 -23.939  1.00 83.08           O
ANISOU  974  O   ILE A 471     7742  11426  12399   3812  -1470    492       O
ATOM    975  CB  ILE A 471     -27.092   0.602 -26.436  1.00 68.62           C
ANISOU  975  CB  ILE A 471     6020   9212  10840   3672   -770    612       C
ATOM    976  CG1 ILE A 471     -28.376   1.251 -26.952  1.00 62.81           C
ANISOU  976  CG1 ILE A 471     5460   8429   9975   3490   -600    604       C
ATOM    977  CG2 ILE A 471     -26.811  -0.688 -27.185  1.00 65.25           C
ANISOU  977  CG2 ILE A 471     5631   8654  10509   3725   -553    649       C
ATOM    978  CD1 ILE A 471     -28.411   1.406 -28.462  1.00 60.08           C
ANISOU  978  CD1 ILE A 471     5005   8017   9807   3283   -331    533       C
ATOM    979  N   ASN A 472     -28.559   1.926 -23.687  1.00 82.64           N
ANISOU  979  N   ASN A 472     8257  11206  11937   3820  -1229    649       N
ATOM    980  CA  ASN A 472     -28.833   3.106 -22.859  1.00 79.92           C
ANISOU  980  CA  ASN A 472     7951  10998  11418   3794  -1472    539       C
ATOM    981  C   ASN A 472     -28.494   4.476 -23.478  1.00 78.83           C
ANISOU  981  C   ASN A 472     7536  10935  11481   3579  -1556    340       C
ATOM    982  O   ASN A 472     -28.235   5.441 -22.753  1.00 79.03           O
ANISOU  982  O   ASN A 472     7501  11086  11440   3559  -1828    198       O
ATOM    983  CB  ASN A 472     -28.181   2.962 -21.478  1.00 77.13           C
ANISOU  983  CB  ASN A 472     7634  10777  10895   4000  -1775    536       C
ATOM    984  N   HIS A 473     -28.486   4.552 -24.808  1.00 76.34           N
ANISOU  984  N   HIS A 473     7063  10534  11408   3410  -1319    319       N
ATOM    985  CA  HIS A 473     -28.485   5.841 -25.510  1.00 74.47           C
ANISOU  985  CA  HIS A 473     6636  10320  11340   3171  -1329    142       C
ATOM    986  C   HIS A 473     -29.429   5.776 -26.705  1.00 71.54           C
ANISOU  986  C   HIS A 473     6390   9791  11002   2977   -980    205       C
ATOM    987  O   HIS A 473     -29.761   4.685 -27.176  1.00 69.33           O
ANISOU  987  O   HIS A 473     6229   9411  10702   3053   -742    352       O
ATOM    988  CB  HIS A 473     -27.076   6.270 -25.945  1.00 73.83           C
ANISOU  988  CB  HIS A 473     6169  10311  11573   3057  -1412     12       C
ATOM    989  CG  HIS A 473     -26.414   5.322 -26.896  1.00 72.22           C
ANISOU  989  CG  HIS A 473     5818  10050  11572   3074  -1167    105       C
ATOM    990  ND1 HIS A 473     -26.974   4.959 -28.102  1.00 64.23           N
ANISOU  990  ND1 HIS A 473     4866   8901  10637   2965   -834    166       N
ATOM    991  CD2 HIS A 473     -25.227   4.672 -26.823  1.00 78.75           C
ANISOU  991  CD2 HIS A 473     6450  10946  12525   3190  -1207    139       C
ATOM    992  CE1 HIS A 473     -26.170   4.115 -28.724  1.00 71.65           C
ANISOU  992  CE1 HIS A 473     5684   9842  11699   3022   -679    214       C
ATOM    993  NE2 HIS A 473     -25.101   3.926 -27.970  1.00 76.51           N
ANISOU  993  NE2 HIS A 473     6128  10581  12360   3167   -894    213       N
ATOM    994  N   CYS A 474     -29.834   6.941 -27.207  1.00 74.39           N
ANISOU  994  N   CYS A 474     6742  10114  11409   2701   -939     98       N
ATOM    995  CA  CYS A 474     -30.903   7.033 -28.208  1.00 71.15           C
ANISOU  995  CA  CYS A 474     6513   9561  10962   2495   -636    160       C
ATOM    996  C   CYS A 474     -30.438   6.986 -29.660  1.00 71.53           C
ANISOU  996  C   CYS A 474     6379   9524  11275   2310   -385    147       C
ATOM    997  O   CYS A 474     -31.220   7.259 -30.574  1.00 71.90           O
ANISOU  997  O   CYS A 474     6549   9465  11305   2118   -162    168       O
ATOM    998  CB  CYS A 474     -31.716   8.314 -27.993  1.00 69.29           C
ANISOU  998  CB  CYS A 474     6407   9317  10603   2317   -711     70       C
ATOM    999  SG  CYS A 474     -32.725   8.312 -26.500  1.00 95.62           S
ANISOU  999  SG  CYS A 474    10059  12711  13562   2507   -890    116       S
ATOM   1000  N   ARG A 475     -29.177   6.636 -29.881  1.00 68.64           N
ANISOU 1000  N   ARG A 475     5724   9208  11147   2378   -417    110       N
ATOM   1001  CA  ARG A 475     -28.608   6.744 -31.215  1.00 69.65           C
ANISOU 1001  CA  ARG A 475     5654   9271  11539   2197   -186     78       C
ATOM   1002  C   ARG A 475     -28.627   5.421 -31.967  1.00 70.41           C
ANISOU 1002  C   ARG A 475     5819   9283  11650   2288     81    201       C
ATOM   1003  O   ARG A 475     -27.575   4.857 -32.261  1.00 76.24           O
ANISOU 1003  O   ARG A 475     6403  10066  12497   2341    111    181       O
ATOM   1004  CB  ARG A 475     -27.186   7.287 -31.124  1.00 77.14           C
ANISOU 1004  CB  ARG A 475     6230  10324  12758   2167   -350    -59       C
ATOM   1005  CG  ARG A 475     -26.954   8.140 -29.890  1.00 82.76           C
ANISOU 1005  CG  ARG A 475     6866  11154  13424   2214   -719   -184       C
ATOM   1006  CD  ARG A 475     -25.689   8.965 -30.014  1.00 88.64           C
ANISOU 1006  CD  ARG A 475     7282  11975  14422   2063   -833   -339       C
ATOM   1007  NE  ARG A 475     -25.422   9.739 -28.804  1.00 93.62           N
ANISOU 1007  NE  ARG A 475     7850  12722  15000   2106  -1201   -476       N
ATOM   1008  CZ  ARG A 475     -24.625  10.802 -28.758  1.00 95.91           C
ANISOU 1008  CZ  ARG A 475     7901  13051  15488   1923  -1339   -648       C
ATOM   1009  NH1 ARG A 475     -24.018  11.226 -29.861  1.00 94.24           N
ANISOU 1009  NH1 ARG A 475     7494  12770  15543   1687  -1123   -687       N
ATOM   1010  NH2 ARG A 475     -24.440  11.445 -27.612  1.00 98.19           N
ANISOU 1010  NH2 ARG A 475     8170  13442  15697   1971  -1682   -781       N
ATOM   1011  N   PHE A 476     -29.825   4.935 -32.285  1.00 70.81           N
ANISOU 1011  N   PHE A 476     6156   9224  11526   2272    269    306       N
ATOM   1012  CA  PHE A 476     -29.965   3.665 -32.993  1.00 69.22           C
ANISOU 1012  CA  PHE A 476     6102   8930  11270   2310    506    387       C
ATOM   1013  C   PHE A 476     -29.293   3.730 -34.354  1.00 66.34           C
ANISOU 1013  C   PHE A 476     5607   8528  11072   2129    711    326       C
ATOM   1014  O   PHE A 476     -28.766   2.728 -34.843  1.00 66.48           O
ANISOU 1014  O   PHE A 476     5626   8515  11120   2190    831    347       O
ATOM   1015  CB  PHE A 476     -31.434   3.291 -33.187  1.00 65.70           C
ANISOU 1015  CB  PHE A 476     5972   8369  10624   2268    669    479       C
ATOM   1016  CG  PHE A 476     -32.270   3.420 -31.948  1.00 67.44           C
ANISOU 1016  CG  PHE A 476     6361   8621  10643   2401    508    544       C
ATOM   1017  CD1 PHE A 476     -32.192   2.472 -30.939  1.00 71.01           C
ANISOU 1017  CD1 PHE A 476     6922   9090  10967   2641    405    629       C
ATOM   1018  CD2 PHE A 476     -33.158   4.478 -31.806  1.00 64.14           C
ANISOU 1018  CD2 PHE A 476     6066   8214  10090   2240    449    494       C
ATOM   1019  CE1 PHE A 476     -32.973   2.586 -29.802  1.00 73.48           C
ANISOU 1019  CE1 PHE A 476     7426   9439  11055   2763    274    695       C
ATOM   1020  CE2 PHE A 476     -33.942   4.599 -30.678  1.00 64.31           C
ANISOU 1020  CE2 PHE A 476     6284   8273   9879   2335    307    533       C
ATOM   1021  CZ  PHE A 476     -33.850   3.652 -29.672  1.00 70.46           C
ANISOU 1021  CZ  PHE A 476     7154   9074  10543   2595    225    634       C
ATOM   1022  N   ASP A 477     -29.306   4.915 -34.958  1.00 61.18           N
ANISOU 1022  N   ASP A 477     4853   7870  10521   1910    753    254       N
ATOM   1023  CA  ASP A 477     -28.707   5.107 -36.276  1.00 63.25           C
ANISOU 1023  CA  ASP A 477     5020   8093  10918   1727    962    209       C
ATOM   1024  C   ASP A 477     -27.195   4.847 -36.293  1.00 63.31           C
ANISOU 1024  C   ASP A 477     4760   8186  11110   1788    912    154       C
ATOM   1025  O   ASP A 477     -26.571   4.846 -37.353  1.00 68.67           O
ANISOU 1025  O   ASP A 477     5359   8835  11897   1668   1095    128       O
ATOM   1026  CB  ASP A 477     -29.015   6.504 -36.823  1.00 68.52           C
ANISOU 1026  CB  ASP A 477     5650   8731  11656   1488   1010    150       C
ATOM   1027  CG  ASP A 477     -28.309   7.604 -36.053  1.00 75.19           C
ANISOU 1027  CG  ASP A 477     6241   9665  12664   1451    774     49       C
ATOM   1028  OD1 ASP A 477     -28.464   7.665 -34.814  1.00 78.75           O
ANISOU 1028  OD1 ASP A 477     6674  10186  13062   1600    519     37       O
ATOM   1029  OD2 ASP A 477     -27.594   8.406 -36.692  1.00 76.28           O
ANISOU 1029  OD2 ASP A 477     6209   9796  12978   1270    839    -23       O
ATOM   1030  N   GLU A 478     -26.602   4.633 -35.126  1.00 58.78           N
ANISOU 1030  N   GLU A 478     4053   7724  10557   1984    662    137       N
ATOM   1031  CA  GLU A 478     -25.203   4.228 -35.085  1.00 66.11           C
ANISOU 1031  CA  GLU A 478     4735   8746  11639   2079    608     92       C
ATOM   1032  C   GLU A 478     -24.984   2.958 -34.276  1.00 68.18           C
ANISOU 1032  C   GLU A 478     5054   9050  11800   2379    498    154       C
ATOM   1033  O   GLU A 478     -23.856   2.481 -34.157  1.00 72.96           O
ANISOU 1033  O   GLU A 478     5467   9742  12511   2505    441    126       O
ATOM   1034  CB  GLU A 478     -24.282   5.363 -34.627  1.00 72.78           C
ANISOU 1034  CB  GLU A 478     5278   9707  12669   1995    405    -24       C
ATOM   1035  CG  GLU A 478     -24.782   6.172 -33.454  1.00 81.04           C
ANISOU 1035  CG  GLU A 478     6336  10811  13647   2025    121    -65       C
ATOM   1036  CD  GLU A 478     -24.177   7.567 -33.426  1.00 88.53           C
ANISOU 1036  CD  GLU A 478     7044  11801  14792   1814      0   -206       C
ATOM   1037  OE1 GLU A 478     -23.685   7.981 -32.356  1.00 92.28           O
ANISOU 1037  OE1 GLU A 478     7376  12393  15294   1892   -305   -290       O
ATOM   1038  OE2 GLU A 478     -24.193   8.249 -34.477  1.00 88.12           O
ANISOU 1038  OE2 GLU A 478     6966  11658  14858   1568    210   -235       O
ATOM   1039  N   PHE A 479     -26.061   2.401 -33.729  1.00 62.36           N
ANISOU 1039  N   PHE A 479     4587   8246  10859   2495    478    243       N
ATOM   1040  CA  PHE A 479     -25.994   1.018 -33.278  1.00 61.94           C
ANISOU 1040  CA  PHE A 479     4662   8161  10710   2740    466    318       C
ATOM   1041  C   PHE A 479     -25.871   0.144 -34.529  1.00 58.58           C
ANISOU 1041  C   PHE A 479     4306   7617  10332   2666    758    339       C
ATOM   1042  O   PHE A 479     -24.850  -0.506 -34.749  1.00 59.50           O
ANISOU 1042  O   PHE A 479     4282   7767  10558   2770    780    315       O
ATOM   1043  CB  PHE A 479     -27.220   0.621 -32.455  1.00 60.21           C
ANISOU 1043  CB  PHE A 479     4742   7866  10270   2844    412    419       C
ATOM   1044  CG  PHE A 479     -27.249  -0.838 -32.097  1.00 60.44           C
ANISOU 1044  CG  PHE A 479     4943   7808  10215   3049    444    511       C
ATOM   1045  CD1 PHE A 479     -27.988  -1.736 -32.847  1.00 59.26           C
ANISOU 1045  CD1 PHE A 479     5026   7495   9994   2978    706    588       C
ATOM   1046  CD2 PHE A 479     -26.507  -1.313 -31.036  1.00 64.60           C
ANISOU 1046  CD2 PHE A 479     5395   8407  10745   3304    209    516       C
ATOM   1047  CE1 PHE A 479     -28.003  -3.080 -32.532  1.00 61.00           C
ANISOU 1047  CE1 PHE A 479     5404   7618  10155   3147    750    679       C
ATOM   1048  CE2 PHE A 479     -26.514  -2.657 -30.718  1.00 68.04           C
ANISOU 1048  CE2 PHE A 479     5997   8736  11121   3479    252    616       C
ATOM   1049  CZ  PHE A 479     -27.264  -3.541 -31.467  1.00 65.38           C
ANISOU 1049  CZ  PHE A 479     5893   8232  10716   3398    533    701       C
ATOM   1050  N   PHE A 480     -26.912   0.146 -35.359  1.00 57.41           N
ANISOU 1050  N   PHE A 480     4376   7340  10098   2490    974    378       N
ATOM   1051  CA  PHE A 480     -26.835  -0.486 -36.672  1.00 59.27           C
ANISOU 1051  CA  PHE A 480     4679   7472  10370   2384   1243    379       C
ATOM   1052  C   PHE A 480     -25.885   0.326 -37.545  1.00 61.07           C
ANISOU 1052  C   PHE A 480     4664   7761  10777   2226   1318    291       C
ATOM   1053  O   PHE A 480     -25.651   1.507 -37.279  1.00 61.52           O
ANISOU 1053  O   PHE A 480     4558   7904  10913   2128   1202    236       O
ATOM   1054  CB  PHE A 480     -28.227  -0.576 -37.315  1.00 56.92           C
ANISOU 1054  CB  PHE A 480     4668   7040   9920   2232   1421    427       C
ATOM   1055  CG  PHE A 480     -29.197  -1.403 -36.524  1.00 58.04           C
ANISOU 1055  CG  PHE A 480     5053   7105   9895   2358   1385    521       C
ATOM   1056  CD1 PHE A 480     -29.166  -2.786 -36.598  1.00 59.76           C
ANISOU 1056  CD1 PHE A 480     5398   7223  10084   2478   1481    579       C
ATOM   1057  CD2 PHE A 480     -30.123  -0.798 -35.684  1.00 60.24           C
ANISOU 1057  CD2 PHE A 480     5434   7403  10049   2358   1263    557       C
ATOM   1058  CE1 PHE A 480     -30.049  -3.556 -35.857  1.00 64.08           C
ANISOU 1058  CE1 PHE A 480     6174   7684  10488   2580   1468    677       C
ATOM   1059  CE2 PHE A 480     -31.011  -1.562 -34.940  1.00 61.16           C
ANISOU 1059  CE2 PHE A 480     5783   7447  10008   2468   1251    655       C
ATOM   1060  CZ  PHE A 480     -30.976  -2.943 -35.029  1.00 62.85           C
ANISOU 1060  CZ  PHE A 480     6125   7555  10202   2571   1359    718       C
ATOM   1061  N   SER A 481     -25.321  -0.296 -38.574  1.00 56.30           N
ANISOU 1061  N   SER A 481     4041   7107  10243   2196   1515    279       N
ATOM   1062  CA  SER A 481     -24.414   0.434 -39.450  1.00 58.83           C
ANISOU 1062  CA  SER A 481     4152   7473  10728   2043   1616    209       C
ATOM   1063  C   SER A 481     -25.244   1.318 -40.359  1.00 55.17           C
ANISOU 1063  C   SER A 481     3828   6934  10202   1793   1765    205       C
ATOM   1064  O   SER A 481     -24.890   2.468 -40.631  1.00 55.46           O
ANISOU 1064  O   SER A 481     3720   7011  10343   1634   1764    156       O
ATOM   1065  CB  SER A 481     -23.540  -0.514 -40.271  1.00 61.96           C
ANISOU 1065  CB  SER A 481     4492   7841  11210   2106   1786    199       C
ATOM   1066  OG  SER A 481     -24.332  -1.367 -41.076  1.00 63.59           O
ANISOU 1066  OG  SER A 481     4973   7904  11286   2076   1982    243       O
ATOM   1067  N   GLU A 482     -26.363   0.763 -40.808  1.00 56.62           N
ANISOU 1067  N   GLU A 482     4297   7001  10213   1761   1885    256       N
ATOM   1068  CA  GLU A 482     -27.318   1.481 -41.642  1.00 57.31           C
ANISOU 1068  CA  GLU A 482     4558   7018  10200   1555   2009    257       C
ATOM   1069  C   GLU A 482     -28.591   0.655 -41.732  1.00 55.61           C
ANISOU 1069  C   GLU A 482     4639   6699   9792   1580   2069    310       C
ATOM   1070  O   GLU A 482     -28.623  -0.499 -41.306  1.00 56.88           O
ANISOU 1070  O   GLU A 482     4869   6822   9919   1736   2055    348       O
ATOM   1071  CB  GLU A 482     -26.740   1.694 -43.038  1.00 57.13           C
ANISOU 1071  CB  GLU A 482     4504   6960  10241   1417   2221    223       C
ATOM   1072  CG  GLU A 482     -26.111   0.447 -43.614  1.00 64.82           C
ANISOU 1072  CG  GLU A 482     5488   7895  11246   1524   2352    224       C
ATOM   1073  CD  GLU A 482     -25.320   0.735 -44.860  1.00 73.82           C
ANISOU 1073  CD  GLU A 482     6552   9023  12472   1413   2545    188       C
ATOM   1074  OE1 GLU A 482     -25.744   1.631 -45.622  1.00 73.71           O
ANISOU 1074  OE1 GLU A 482     6625   8978  12406   1238   2636    181       O
ATOM   1075  OE2 GLU A 482     -24.273   0.078 -45.069  1.00 80.02           O
ANISOU 1075  OE2 GLU A 482     7195   9833  13375   1511   2607    169       O
ATOM   1076  N   GLY A 483     -29.645   1.243 -42.279  1.00 53.69           N
ANISOU 1076  N   GLY A 483     4568   6405   9428   1426   2135    312       N
ATOM   1077  CA  GLY A 483     -30.855   0.486 -42.513  1.00 49.16           C
ANISOU 1077  CA  GLY A 483     4260   5733   8685   1422   2204    346       C
ATOM   1078  C   GLY A 483     -31.883   1.275 -43.282  1.00 43.72           C
ANISOU 1078  C   GLY A 483     3728   5009   7877   1246   2273    329       C
ATOM   1079  O   GLY A 483     -31.578   2.342 -43.820  1.00 43.05           O
ANISOU 1079  O   GLY A 483     3566   4956   7837   1125   2304    298       O
ATOM   1080  N   CYS A 484     -33.099   0.740 -43.350  1.00 44.99           N
ANISOU 1080  N   CYS A 484     4107   5098   7888   1233   2300    348       N
ATOM   1081  CA  CYS A 484     -34.240   1.505 -43.841  1.00 40.25           C
ANISOU 1081  CA  CYS A 484     3653   4482   7158   1095   2319    332       C
ATOM   1082  C   CYS A 484     -35.332   1.592 -42.785  1.00 38.06           C
ANISOU 1082  C   CYS A 484     3462   4210   6788   1133   2201    368       C
ATOM   1083  O   CYS A 484     -35.917   0.579 -42.407  1.00 38.66           O
ANISOU 1083  O   CYS A 484     3656   4228   6806   1204   2209    399       O
ATOM   1084  CB  CYS A 484     -34.828   0.901 -45.109  1.00 39.21           C
ANISOU 1084  CB  CYS A 484     3708   4268   6923   1019   2465    298       C
ATOM   1085  SG  CYS A 484     -36.158   1.936 -45.750  1.00 41.57           S
ANISOU 1085  SG  CYS A 484     4166   4568   7060    868   2464    269       S
ATOM   1086  N   ALA A 485     -35.596   2.805 -42.314  1.00 37.21           N
ANISOU 1086  N   ALA A 485     3297   4165   6675   1086   2104    366       N
ATOM   1087  CA  ALA A 485     -36.631   3.034 -41.326  1.00 42.28           C
ANISOU 1087  CA  ALA A 485     4018   4821   7224   1124   1997    397       C
ATOM   1088  C   ALA A 485     -37.380   4.306 -41.690  1.00 41.54           C
ANISOU 1088  C   ALA A 485     3970   4750   7065    994   1988    368       C
ATOM   1089  O   ALA A 485     -37.087   5.372 -41.144  1.00 42.92           O
ANISOU 1089  O   ALA A 485     4021   4982   7306    987   1895    362       O
ATOM   1090  CB  ALA A 485     -36.030   3.134 -39.921  1.00 36.79           C
ANISOU 1090  CB  ALA A 485     3178   4193   6606   1274   1837    432       C
ATOM   1091  N   PRO A 486     -38.329   4.193 -42.636  1.00 36.81           N
ANISOU 1091  N   PRO A 486     3541   4102   6342    897   2078    345       N
ATOM   1092  CA  PRO A 486     -39.146   5.301 -43.155  1.00 37.85           C
ANISOU 1092  CA  PRO A 486     3749   4248   6385    783   2082    319       C
ATOM   1093  C   PRO A 486     -39.675   6.210 -42.051  1.00 39.14           C
ANISOU 1093  C   PRO A 486     3875   4461   6536    814   1958    337       C
ATOM   1094  O   PRO A 486     -40.229   5.725 -41.064  1.00 37.65           O
ANISOU 1094  O   PRO A 486     3725   4278   6303    907   1887    367       O
ATOM   1095  CB  PRO A 486     -40.303   4.580 -43.847  1.00 34.47           C
ANISOU 1095  CB  PRO A 486     3512   3770   5816    742   2143    294       C
ATOM   1096  CG  PRO A 486     -39.656   3.330 -44.379  1.00 41.06           C
ANISOU 1096  CG  PRO A 486     4355   4547   6698    777   2235    285       C
ATOM   1097  CD  PRO A 486     -38.620   2.927 -43.335  1.00 37.35           C
ANISOU 1097  CD  PRO A 486     3738   4096   6359    898   2181    332       C
ATOM   1098  N   GLY A 487     -39.487   7.515 -42.222  1.00 38.18           N
ANISOU 1098  N   GLY A 487     3687   4365   6456    739   1940    321       N
ATOM   1099  CA  GLY A 487     -39.843   8.472 -41.197  1.00 39.01           C
ANISOU 1099  CA  GLY A 487     3797   4515   6511    735   1743    319       C
ATOM   1100  C   GLY A 487     -38.625   8.966 -40.438  1.00 41.77           C
ANISOU 1100  C   GLY A 487     3954   4904   7011    764   1623    307       C
ATOM   1101  O   GLY A 487     -38.729   9.834 -39.573  1.00 44.41           O
ANISOU 1101  O   GLY A 487     4277   5275   7322    759   1449    286       O
ATOM   1102  N   SER A 488     -37.460   8.408 -40.749  1.00 39.87           N
ANISOU 1102  N   SER A 488     3556   4662   6932    798   1711    308       N
ATOM   1103  CA  SER A 488     -36.236   8.845 -40.089  1.00 39.04           C
ANISOU 1103  CA  SER A 488     3232   4604   6998    823   1592    281       C
ATOM   1104  C   SER A 488     -35.750  10.157 -40.690  1.00 42.65           C
ANISOU 1104  C   SER A 488     3607   5043   7554    659   1618    239       C
ATOM   1105  O   SER A 488     -36.206  10.556 -41.765  1.00 40.35           O
ANISOU 1105  O   SER A 488     3430   4698   7203    549   1766    250       O
ATOM   1106  CB  SER A 488     -35.152   7.766 -40.175  1.00 43.84           C
ANISOU 1106  CB  SER A 488     3676   5220   7761    933   1675    295       C
ATOM   1107  OG  SER A 488     -35.219   6.893 -39.054  1.00 43.96           O
ANISOU 1107  OG  SER A 488     3703   5270   7732   1111   1549    330       O
ATOM   1108  N   LYS A 489     -34.848  10.836 -39.985  1.00 47.00           N
ANISOU 1108  N   LYS A 489     3969   5633   8253    645   1470    190       N
ATOM   1109  CA  LYS A 489     -34.183  12.010 -40.538  1.00 50.51           C
ANISOU 1109  CA  LYS A 489     4300   6042   8849    481   1517    149       C
ATOM   1110  C   LYS A 489     -33.547  11.636 -41.870  1.00 53.33           C
ANISOU 1110  C   LYS A 489     4591   6354   9317    421   1792    177       C
ATOM   1111  O   LYS A 489     -32.915  10.587 -41.991  1.00 53.53           O
ANISOU 1111  O   LYS A 489     4513   6406   9422    520   1869    189       O
ATOM   1112  CB  LYS A 489     -33.125  12.541 -39.566  1.00 56.51           C
ANISOU 1112  CB  LYS A 489     4816   6857   9798    485   1319     72       C
ATOM   1113  CG  LYS A 489     -33.517  13.832 -38.876  1.00 58.28           C
ANISOU 1113  CG  LYS A 489     5095   7068   9981    401   1128     11       C
ATOM   1114  CD  LYS A 489     -32.602  14.972 -39.289  1.00 65.49           C
ANISOU 1114  CD  LYS A 489     5833   7926  11125    221   1167    -52       C
ATOM   1115  CE  LYS A 489     -31.623  15.333 -38.174  1.00 71.98           C
ANISOU 1115  CE  LYS A 489     6406   8816  12127    240    924   -164       C
ATOM   1116  NZ  LYS A 489     -32.305  15.976 -37.006  1.00 69.25           N
ANISOU 1116  NZ  LYS A 489     6184   8495  11632    279    658   -226       N
ATOM   1117  N   LYS A 490     -33.726  12.489 -42.870  1.00 55.14           N
ANISOU 1117  N   LYS A 490     4904   6513   9533    272   1940    190       N
ATOM   1118  CA  LYS A 490     -33.329  12.159 -44.237  1.00 58.65           C
ANISOU 1118  CA  LYS A 490     5393   6912   9980    217   2188    224       C
ATOM   1119  C   LYS A 490     -31.837  11.895 -44.423  1.00 62.98           C
ANISOU 1119  C   LYS A 490     5732   7477  10720    206   2228    197       C
ATOM   1120  O   LYS A 490     -31.435  11.231 -45.379  1.00 63.37           O
ANISOU 1120  O   LYS A 490     5846   7508  10723    215   2375    216       O
ATOM   1121  CB  LYS A 490     -33.790  13.253 -45.199  1.00 60.15           C
ANISOU 1121  CB  LYS A 490     5735   7020  10098     71   2319    254       C
ATOM   1122  CG  LYS A 490     -35.303  13.344 -45.319  1.00 57.31           C
ANISOU 1122  CG  LYS A 490     5634   6649   9492     95   2290    284       C
ATOM   1123  CD  LYS A 490     -35.906  11.970 -45.598  1.00 55.69           C
ANISOU 1123  CD  LYS A 490     5560   6475   9123    212   2324    295       C
ATOM   1124  CE  LYS A 490     -37.360  12.082 -46.012  1.00 55.06           C
ANISOU 1124  CE  LYS A 490     5725   6382   8812    213   2333    314       C
ATOM   1125  NZ  LYS A 490     -37.509  12.971 -47.207  1.00 59.22           N
ANISOU 1125  NZ  LYS A 490     6390   6851   9260    108   2468    346       N
ATOM   1126  N   ASP A 491     -31.021  12.412 -43.512  1.00 63.89           N
ANISOU 1126  N   ASP A 491     5590   7631  11053    190   2090    141       N
ATOM   1127  CA  ASP A 491     -29.576  12.223 -43.603  1.00 66.46           C
ANISOU 1127  CA  ASP A 491     5688   7987  11578    179   2110    103       C
ATOM   1128  C   ASP A 491     -29.108  11.016 -42.789  1.00 67.53           C
ANISOU 1128  C   ASP A 491     5700   8216  11742    367   1979     87       C
ATOM   1129  O   ASP A 491     -27.969  10.575 -42.923  1.00 74.30           O
ANISOU 1129  O   ASP A 491     6387   9110  12734    398   2007     64       O
ATOM   1130  CB  ASP A 491     -28.837  13.493 -43.166  1.00 65.70           C
ANISOU 1130  CB  ASP A 491     5367   7877  11718     39   2027     34       C
ATOM   1131  CG  ASP A 491     -29.151  13.887 -41.735  1.00 65.63           C
ANISOU 1131  CG  ASP A 491     5235   7925  11778     91   1755    -32       C
ATOM   1132  OD1 ASP A 491     -28.332  14.602 -41.118  1.00 61.63           O
ANISOU 1132  OD1 ASP A 491     4490   7438  11488     20   1614   -123       O
ATOM   1133  OD2 ASP A 491     -30.217  13.477 -41.224  1.00 67.15           O
ANISOU 1133  OD2 ASP A 491     5594   8140  11778    205   1661     -2       O
ATOM   1134  N   SER A 492     -29.997  10.479 -41.957  1.00 62.78           N
ANISOU 1134  N   SER A 492     5195   7649  11010    502   1846    106       N
ATOM   1135  CA  SER A 492     -29.670   9.335 -41.108  1.00 57.34           C
ANISOU 1135  CA  SER A 492     4433   7036  10318    701   1716    109       C
ATOM   1136  C   SER A 492     -29.222   8.107 -41.904  1.00 52.60           C
ANISOU 1136  C   SER A 492     3893   6420   9674    769   1875    144       C
ATOM   1137  O   SER A 492     -29.614   7.915 -43.055  1.00 45.33           O
ANISOU 1137  O   SER A 492     3154   5428   8641    695   2068    175       O
ATOM   1138  CB  SER A 492     -30.861   8.973 -40.220  1.00 54.06           C
ANISOU 1138  CB  SER A 492     4174   6632   9732    828   1589    145       C
ATOM   1139  OG  SER A 492     -30.683   7.699 -39.631  1.00 62.75           O
ANISOU 1139  OG  SER A 492     5286   7774  10782   1023   1522    178       O
ATOM   1140  N   SER A 493     -28.390   7.280 -41.283  1.00 51.14           N
ANISOU 1140  N   SER A 493     3554   6303   9572    922   1780    133       N
ATOM   1141  CA  SER A 493     -27.942   6.043 -41.908  1.00 55.00           C
ANISOU 1141  CA  SER A 493     4088   6774  10035   1010   1915    159       C
ATOM   1142  C   SER A 493     -29.113   5.068 -41.979  1.00 52.40           C
ANISOU 1142  C   SER A 493     4038   6384   9488   1092   1961    217       C
ATOM   1143  O   SER A 493     -29.090   4.102 -42.745  1.00 53.80           O
ANISOU 1143  O   SER A 493     4329   6507   9605   1122   2107    236       O
ATOM   1144  CB  SER A 493     -26.796   5.432 -41.105  1.00 59.92           C
ANISOU 1144  CB  SER A 493     4475   7490  10801   1174   1781    133       C
ATOM   1145  OG  SER A 493     -27.183   5.273 -39.749  1.00 61.08           O
ANISOU 1145  OG  SER A 493     4613   7698  10898   1326   1548    144       O
ATOM   1146  N   LEU A 494     -30.140   5.332 -41.177  1.00 48.25           N
ANISOU 1146  N   LEU A 494     3618   5861   8853   1121   1837    239       N
ATOM   1147  CA  LEU A 494     -31.347   4.522 -41.202  1.00 47.26           C
ANISOU 1147  CA  LEU A 494     3754   5673   8531   1173   1881    290       C
ATOM   1148  C   LEU A 494     -32.242   4.905 -42.369  1.00 47.06           C
ANISOU 1148  C   LEU A 494     3928   5573   8378   1012   2037    289       C
ATOM   1149  O   LEU A 494     -33.373   4.437 -42.474  1.00 47.45           O
ANISOU 1149  O   LEU A 494     4189   5573   8266   1018   2066    314       O
ATOM   1150  CB  LEU A 494     -32.105   4.643 -39.891  1.00 48.92           C
ANISOU 1150  CB  LEU A 494     4006   5916   8664   1277   1698    319       C
ATOM   1151  CG  LEU A 494     -31.377   4.001 -38.716  1.00 49.42           C
ANISOU 1151  CG  LEU A 494     3938   6047   8792   1483   1531    335       C
ATOM   1152  CD1 LEU A 494     -32.280   4.018 -37.498  1.00 42.49           C
ANISOU 1152  CD1 LEU A 494     3169   5188   7788   1599   1373    382       C
ATOM   1153  CD2 LEU A 494     -30.913   2.580 -39.050  1.00 50.21           C
ANISOU 1153  CD2 LEU A 494     4083   6105   8890   1592   1631    365       C
ATOM   1154  N   CYS A 495     -31.729   5.766 -43.241  1.00 45.80           N
ANISOU 1154  N   CYS A 495     3703   5407   8293    873   2133    259       N
ATOM   1155  CA  CYS A 495     -32.373   6.048 -44.517  1.00 45.88           C
ANISOU 1155  CA  CYS A 495     3904   5350   8176    744   2291    261       C
ATOM   1156  C   CYS A 495     -31.550   5.483 -45.674  1.00 45.08           C
ANISOU 1156  C   CYS A 495     3801   5217   8111    726   2462    249       C
ATOM   1157  O   CYS A 495     -32.042   5.366 -46.799  1.00 42.09           O
ANISOU 1157  O   CYS A 495     3605   4784   7605    663   2593    247       O
ATOM   1158  CB  CYS A 495     -32.569   7.553 -44.711  1.00 47.39           C
ANISOU 1158  CB  CYS A 495     4075   5540   8391    601   2289    252       C
ATOM   1159  SG  CYS A 495     -34.086   8.200 -44.000  1.00 53.07           S
ANISOU 1159  SG  CYS A 495     4934   6261   8968    590   2172    266       S
ATOM   1160  N   LYS A 496     -30.300   5.126 -45.391  1.00 44.58           N
ANISOU 1160  N   LYS A 496     3528   5193   8217    795   2454    235       N
ATOM   1161  CA  LYS A 496     -29.360   4.737 -46.441  1.00 48.62           C
ANISOU 1161  CA  LYS A 496     3996   5682   8793    778   2624    221       C
ATOM   1162  C   LYS A 496     -29.785   3.519 -47.271  1.00 48.67           C
ANISOU 1162  C   LYS A 496     4205   5623   8664    831   2747    223       C
ATOM   1163  O   LYS A 496     -29.385   3.382 -48.423  1.00 55.46           O
ANISOU 1163  O   LYS A 496     5113   6449   9512    788   2913    209       O
ATOM   1164  CB  LYS A 496     -27.953   4.533 -45.861  1.00 55.08           C
ANISOU 1164  CB  LYS A 496     4529   6570   9829    860   2573    199       C
ATOM   1165  CG  LYS A 496     -27.147   5.819 -45.698  1.00 59.72           C
ANISOU 1165  CG  LYS A 496     4893   7202  10594    748   2541    170       C
ATOM   1166  CD  LYS A 496     -25.701   5.514 -45.310  1.00 70.33           C
ANISOU 1166  CD  LYS A 496     5945   8620  12156    827   2505    135       C
ATOM   1167  CE  LYS A 496     -24.806   6.746 -45.440  1.00 78.17           C
ANISOU 1167  CE  LYS A 496     6719   9638  13346    682   2523     96       C
ATOM   1168  NZ  LYS A 496     -25.304   7.911 -44.642  1.00 78.55           N
ANISOU 1168  NZ  LYS A 496     6726   9697  13422    592   2360     77       N
ATOM   1169  N   LEU A 497     -30.604   2.648 -46.697  1.00 48.13           N
ANISOU 1169  N   LEU A 497     4258   5531   8499    921   2671    238       N
ATOM   1170  CA  LEU A 497     -30.988   1.410 -47.372  1.00 49.15           C
ANISOU 1170  CA  LEU A 497     4561   5585   8529    970   2776    230       C
ATOM   1171  C   LEU A 497     -32.347   1.489 -48.050  1.00 48.29           C
ANISOU 1171  C   LEU A 497     4701   5421   8224    883   2812    217       C
ATOM   1172  O   LEU A 497     -32.759   0.539 -48.711  1.00 48.57           O
ANISOU 1172  O   LEU A 497     4886   5391   8176    903   2898    192       O
ATOM   1173  CB  LEU A 497     -30.989   0.236 -46.387  1.00 45.96           C
ANISOU 1173  CB  LEU A 497     4140   5167   8156   1126   2695    254       C
ATOM   1174  CG  LEU A 497     -29.830  -0.755 -46.428  1.00 51.27           C
ANISOU 1174  CG  LEU A 497     4692   5835   8955   1253   2756    249       C
ATOM   1175  CD1 LEU A 497     -28.479  -0.050 -46.376  1.00 56.52           C
ANISOU 1175  CD1 LEU A 497     5092   6587   9796   1250   2750    233       C
ATOM   1176  CD2 LEU A 497     -29.962  -1.741 -45.286  1.00 53.08           C
ANISOU 1176  CD2 LEU A 497     4923   6047   9198   1415   2650    290       C
ATOM   1177  N   CYS A 498     -33.049   2.605 -47.868  1.00 44.10           N
ANISOU 1177  N   CYS A 498     4208   4920   7629    794   2740    226       N
ATOM   1178  CA  CYS A 498     -34.384   2.770 -48.441  1.00 42.91           C
ANISOU 1178  CA  CYS A 498     4276   4736   7292    722   2751    209       C
ATOM   1179  C   CYS A 498     -34.314   2.824 -49.978  1.00 46.34           C
ANISOU 1179  C   CYS A 498     4828   5139   7641    656   2909    174       C
ATOM   1180  O   CYS A 498     -33.231   3.008 -50.534  1.00 49.21           O
ANISOU 1180  O   CYS A 498     5096   5510   8093    647   3013    175       O
ATOM   1181  CB  CYS A 498     -35.070   4.002 -47.840  1.00 38.50           C
ANISOU 1181  CB  CYS A 498     3714   4220   6695    658   2639    230       C
ATOM   1182  SG  CYS A 498     -35.459   3.837 -46.044  1.00 47.95           S
ANISOU 1182  SG  CYS A 498     4827   5453   7938    755   2452    265       S
ATOM   1183  N   MET A 499     -35.444   2.637 -50.665  1.00 41.23           N
ANISOU 1183  N   MET A 499     4381   4462   6821    618   2929    140       N
ATOM   1184  CA  MET A 499     -35.429   2.527 -52.134  1.00 46.65           C
ANISOU 1184  CA  MET A 499     5198   5125   7403    582   3075     99       C
ATOM   1185  C   MET A 499     -36.229   3.604 -52.884  1.00 47.23           C
ANISOU 1185  C   MET A 499     5407   5222   7317    496   3084     96       C
ATOM   1186  O   MET A 499     -36.237   3.620 -54.119  1.00 45.55           O
ANISOU 1186  O   MET A 499     5314   4999   6994    475   3204     67       O
ATOM   1187  CB  MET A 499     -35.913   1.142 -52.592  1.00 45.25           C
ANISOU 1187  CB  MET A 499     5147   4888   7157    630   3125     37       C
ATOM   1188  CG  MET A 499     -37.425   0.939 -52.438  1.00 41.78           C
ANISOU 1188  CG  MET A 499     4853   4437   6584    603   3038     -2       C
ATOM   1189  SD  MET A 499     -38.078  -0.556 -53.242  1.00 58.73           S
ANISOU 1189  SD  MET A 499     7163   6504   8647    625   3120   -103       S
ATOM   1190  CE  MET A 499     -38.789   0.116 -54.741  1.00 54.82           C
ANISOU 1190  CE  MET A 499     6844   6052   7935    556   3183   -171       C
ATOM   1191  N   GLY A 500     -36.897   4.491 -52.148  1.00 47.83           N
ANISOU 1191  N   GLY A 500     5471   5330   7373    460   2964    126       N
ATOM   1192  CA  GLY A 500     -37.724   5.525 -52.753  1.00 50.75           C
ANISOU 1192  CA  GLY A 500     5972   5721   7591    394   2963    131       C
ATOM   1193  C   GLY A 500     -36.978   6.488 -53.670  1.00 54.35           C
ANISOU 1193  C   GLY A 500     6435   6174   8041    341   3090    168       C
ATOM   1194  O   GLY A 500     -35.831   6.860 -53.398  1.00 55.31           O
ANISOU 1194  O   GLY A 500     6398   6291   8327    326   3133    205       O
ATOM   1195  N   SER A 501     -37.639   6.902 -54.751  1.00 55.53           N
ANISOU 1195  N   SER A 501     6768   6328   8003    315   3153    159       N
ATOM   1196  CA  SER A 501     -37.031   7.773 -55.762  1.00 56.99           C
ANISOU 1196  CA  SER A 501     7007   6499   8148    272   3296    204       C
ATOM   1197  C   SER A 501     -37.112   9.257 -55.417  1.00 55.45           C
ANISOU 1197  C   SER A 501     6792   6299   7979    205   3266    277       C
ATOM   1198  O   SER A 501     -38.154   9.746 -54.982  1.00 53.72           O
ANISOU 1198  O   SER A 501     6639   6098   7674    197   3156    282       O
ATOM   1199  CB  SER A 501     -37.681   7.544 -57.126  1.00 56.97           C
ANISOU 1199  CB  SER A 501     7232   6505   7909    291   3383    167       C
ATOM   1200  OG  SER A 501     -37.439   6.229 -57.578  1.00 65.37           O
ANISOU 1200  OG  SER A 501     8315   7559   8963    344   3443     95       O
ATOM   1201  N   GLY A 502     -36.006   9.966 -55.632  1.00 55.64           N
ANISOU 1201  N   GLY A 502     6722   6290   8128    156   3376    329       N
ATOM   1202  CA  GLY A 502     -35.948  11.399 -55.403  1.00 54.51           C
ANISOU 1202  CA  GLY A 502     6562   6117   8032     79   3377    397       C
ATOM   1203  C   GLY A 502     -36.362  11.793 -53.997  1.00 53.74           C
ANISOU 1203  C   GLY A 502     6345   6036   8039     62   3205    397       C
ATOM   1204  O   GLY A 502     -35.791  11.320 -53.016  1.00 54.01           O
ANISOU 1204  O   GLY A 502     6184   6088   8248     79   3129    370       O
ATOM   1205  N   LEU A 503     -37.371  12.652 -53.900  1.00 51.49           N
ANISOU 1205  N   LEU A 503     6184   5745   7636     40   3145    428       N
ATOM   1206  CA  LEU A 503     -37.835  13.141 -52.607  1.00 52.80           C
ANISOU 1206  CA  LEU A 503     6253   5921   7886     25   2996    430       C
ATOM   1207  C   LEU A 503     -38.671  12.116 -51.845  1.00 52.67           C
ANISOU 1207  C   LEU A 503     6227   5964   7820    104   2856    372       C
ATOM   1208  O   LEU A 503     -39.095  12.367 -50.713  1.00 48.87           O
ANISOU 1208  O   LEU A 503     5668   5502   7399    111   2732    369       O
ATOM   1209  CB  LEU A 503     -38.625  14.438 -52.777  1.00 56.26           C
ANISOU 1209  CB  LEU A 503     6836   6323   8218    -20   2994    489       C
ATOM   1210  CG  LEU A 503     -37.773  15.682 -53.039  1.00 58.83           C
ANISOU 1210  CG  LEU A 503     7127   6562   8663   -119   3101    556       C
ATOM   1211  CD1 LEU A 503     -38.647  16.922 -53.228  1.00 56.73           C
ANISOU 1211  CD1 LEU A 503     7042   6241   8273   -149   3099    626       C
ATOM   1212  CD2 LEU A 503     -36.786  15.884 -51.901  1.00 56.82           C
ANISOU 1212  CD2 LEU A 503     6600   6295   8695   -177   3045    531       C
ATOM   1213  N   ASN A 504     -38.899  10.962 -52.466  1.00 54.22           N
ANISOU 1213  N   ASN A 504     6506   6182   7912    161   2883    324       N
ATOM   1214  CA  ASN A 504     -39.641   9.885 -51.822  1.00 49.91           C
ANISOU 1214  CA  ASN A 504     5957   5673   7334    226   2771    268       C
ATOM   1215  C   ASN A 504     -38.781   9.029 -50.899  1.00 40.92           C
ANISOU 1215  C   ASN A 504     4633   4536   6380    267   2727    254       C
ATOM   1216  O   ASN A 504     -39.310   8.278 -50.078  1.00 36.08           O
ANISOU 1216  O   ASN A 504     3998   3940   5772    321   2626    229       O
ATOM   1217  CB  ASN A 504     -40.317   9.005 -52.872  1.00 52.18           C
ANISOU 1217  CB  ASN A 504     6414   5969   7442    259   2819    211       C
ATOM   1218  CG  ASN A 504     -41.365   9.753 -53.656  1.00 51.00           C
ANISOU 1218  CG  ASN A 504     6454   5839   7083    246   2829    217       C
ATOM   1219  OD1 ASN A 504     -41.961  10.706 -53.148  1.00 47.21           O
ANISOU 1219  OD1 ASN A 504     5989   5369   6579    228   2761    255       O
ATOM   1220  ND2 ASN A 504     -41.598   9.333 -54.900  1.00 51.78           N
ANISOU 1220  ND2 ASN A 504     6707   5946   7022    264   2915    177       N
ATOM   1221  N   LEU A 505     -37.461   9.139 -51.045  1.00 38.89           N
ANISOU 1221  N   LEU A 505     4245   4259   6271    248   2810    274       N
ATOM   1222  CA  LEU A 505     -36.539   8.343 -50.240  1.00 40.21           C
ANISOU 1222  CA  LEU A 505     4229   4437   6613    303   2775    263       C
ATOM   1223  C   LEU A 505     -36.846   8.487 -48.753  1.00 38.84           C
ANISOU 1223  C   LEU A 505     3943   4295   6518    337   2614    270       C
ATOM   1224  O   LEU A 505     -36.917   9.600 -48.227  1.00 39.09           O
ANISOU 1224  O   LEU A 505     3915   4336   6603    288   2561    292       O
ATOM   1225  CB  LEU A 505     -35.083   8.720 -50.517  1.00 43.17           C
ANISOU 1225  CB  LEU A 505     4447   4799   7158    266   2876    280       C
ATOM   1226  CG  LEU A 505     -34.083   7.755 -49.864  1.00 51.03           C
ANISOU 1226  CG  LEU A 505     5256   5813   8318    344   2852    263       C
ATOM   1227  CD1 LEU A 505     -33.940   6.468 -50.678  1.00 49.74           C
ANISOU 1227  CD1 LEU A 505     5183   5627   8090    407   2953    234       C
ATOM   1228  CD2 LEU A 505     -32.722   8.412 -49.638  1.00 55.08           C
ANISOU 1228  CD2 LEU A 505     5541   6336   9049    300   2888    272       C
ATOM   1229  N   CYS A 506     -37.083   7.350 -48.106  1.00 40.34           N
ANISOU 1229  N   CYS A 506     4124   4495   6708    426   2546    254       N
ATOM   1230  CA  CYS A 506     -37.324   7.282 -46.669  1.00 39.93           C
ANISOU 1230  CA  CYS A 506     3977   4476   6718    490   2401    267       C
ATOM   1231  C   CYS A 506     -38.651   7.906 -46.212  1.00 39.70           C
ANISOU 1231  C   CYS A 506     4051   4463   6571    473   2313    271       C
ATOM   1232  O   CYS A 506     -38.864   8.086 -45.014  1.00 43.00           O
ANISOU 1232  O   CYS A 506     4393   4912   7034    526   2199    284       O
ATOM   1233  CB  CYS A 506     -36.152   7.897 -45.900  1.00 41.30           C
ANISOU 1233  CB  CYS A 506     3917   4682   7094    494   2353    278       C
ATOM   1234  SG  CYS A 506     -35.813   7.151 -44.287  1.00 41.28           S
ANISOU 1234  SG  CYS A 506     3760   4727   7198    642   2197    288       S
ATOM   1235  N   GLU A 507     -39.536   8.238 -47.150  1.00 35.02           N
ANISOU 1235  N   GLU A 507     3627   3856   5823    415   2364    257       N
ATOM   1236  CA  GLU A 507     -40.873   8.709 -46.787  1.00 37.10           C
ANISOU 1236  CA  GLU A 507     3990   4139   5965    411   2287    254       C
ATOM   1237  C   GLU A 507     -41.708   7.595 -46.150  1.00 35.50           C
ANISOU 1237  C   GLU A 507     3839   3941   5709    480   2218    235       C
ATOM   1238  O   GLU A 507     -41.780   6.485 -46.668  1.00 33.36           O
ANISOU 1238  O   GLU A 507     3631   3640   5405    495   2268    206       O
ATOM   1239  CB  GLU A 507     -41.619   9.275 -48.000  1.00 38.80           C
ANISOU 1239  CB  GLU A 507     4373   4348   6022    350   2355    242       C
ATOM   1240  CG  GLU A 507     -41.218  10.690 -48.395  1.00 41.43           C
ANISOU 1240  CG  GLU A 507     4699   4665   6378    278   2411    284       C
ATOM   1241  CD  GLU A 507     -41.245  11.649 -47.222  1.00 50.98           C
ANISOU 1241  CD  GLU A 507     5817   5884   7669    267   2277    306       C
ATOM   1242  OE1 GLU A 507     -40.264  12.399 -47.053  1.00 53.44           O
ANISOU 1242  OE1 GLU A 507     6012   6170   8123    214   2292    328       O
ATOM   1243  OE2 GLU A 507     -42.243  11.663 -46.467  1.00 56.11           O
ANISOU 1243  OE2 GLU A 507     6523   6564   8233    306   2122    291       O
ATOM   1244  N   PRO A 508     -42.347   7.888 -45.014  1.00 33.01           N
ANISOU 1244  N   PRO A 508     3498   3655   5389    523   2113    251       N
ATOM   1245  CA  PRO A 508     -43.252   6.919 -44.373  1.00 31.98           C
ANISOU 1245  CA  PRO A 508     3430   3520   5202    579   2063    243       C
ATOM   1246  C   PRO A 508     -44.572   6.740 -45.136  1.00 30.46           C
ANISOU 1246  C   PRO A 508     3384   3324   4866    530   2081    193       C
ATOM   1247  O   PRO A 508     -45.639   6.878 -44.542  1.00 30.02           O
ANISOU 1247  O   PRO A 508     3365   3291   4750    544   2018    187       O
ATOM   1248  CB  PRO A 508     -43.534   7.554 -43.008  1.00 37.78           C
ANISOU 1248  CB  PRO A 508     4112   4294   5948    632   1932    276       C
ATOM   1249  CG  PRO A 508     -43.352   9.036 -43.245  1.00 39.01           C
ANISOU 1249  CG  PRO A 508     4261   4473   6089    558   1864    273       C
ATOM   1250  CD  PRO A 508     -42.196   9.124 -44.227  1.00 34.66           C
ANISOU 1250  CD  PRO A 508     3638   3894   5637    511   2001    274       C
ATOM   1251  N   ASN A 509     -44.499   6.471 -46.433  1.00 28.47           N
ANISOU 1251  N   ASN A 509     3205   3050   4561    480   2167    150       N
ATOM   1252  CA  ASN A 509     -45.672   6.074 -47.204  1.00 36.15           C
ANISOU 1252  CA  ASN A 509     4298   4024   5413    447   2185     80       C
ATOM   1253  C   ASN A 509     -45.279   5.157 -48.355  1.00 29.30           C
ANISOU 1253  C   ASN A 509     3489   3114   4529    428   2288     27       C
ATOM   1254  O   ASN A 509     -44.099   4.832 -48.522  1.00 30.14           O
ANISOU 1254  O   ASN A 509     3543   3190   4721    445   2347     53       O
ATOM   1255  CB  ASN A 509     -46.472   7.283 -47.704  1.00 38.58           C
ANISOU 1255  CB  ASN A 509     4676   4384   5600    416   2166     67       C
ATOM   1256  CG  ASN A 509     -45.662   8.181 -48.605  1.00 34.52           C
ANISOU 1256  CG  ASN A 509     4185   3868   5063    384   2240     98       C
ATOM   1257  OD1 ASN A 509     -45.183   7.750 -49.645  1.00 33.20           O
ANISOU 1257  OD1 ASN A 509     4069   3680   4865    366   2330     72       O
ATOM   1258  ND2 ASN A 509     -45.521   9.445 -48.218  1.00 34.39           N
ANISOU 1258  ND2 ASN A 509     4145   3866   5055    370   2181    153       N
ATOM   1259  N   ASN A 510     -46.259   4.737 -49.146  1.00 29.43           N
ANISOU 1259  N   ASN A 510     3607   3133   4441    400   2312    -58       N
ATOM   1260  CA  ASN A 510     -46.015   3.708 -50.144  1.00 33.10           C
ANISOU 1260  CA  ASN A 510     4135   3551   4890    390   2409   -129       C
ATOM   1261  C   ASN A 510     -45.198   4.172 -51.342  1.00 37.30           C
ANISOU 1261  C   ASN A 510     4718   4095   5359    380   2500   -128       C
ATOM   1262  O   ASN A 510     -44.781   3.359 -52.165  1.00 37.63           O
ANISOU 1262  O   ASN A 510     4808   4098   5391    384   2592   -180       O
ATOM   1263  CB  ASN A 510     -47.318   3.035 -50.587  1.00 34.13           C
ANISOU 1263  CB  ASN A 510     4348   3677   4943    361   2411   -246       C
ATOM   1264  CG  ASN A 510     -47.934   2.201 -49.492  1.00 42.23           C
ANISOU 1264  CG  ASN A 510     5323   4654   6067    365   2372   -246       C
ATOM   1265  OD1 ASN A 510     -47.402   1.154 -49.125  1.00 45.53           O
ANISOU 1265  OD1 ASN A 510     5719   4988   6591    387   2420   -228       O
ATOM   1266  ND2 ASN A 510     -49.063   2.662 -48.954  1.00 43.56           N
ANISOU 1266  ND2 ASN A 510     5481   4870   6202    350   2297   -260       N
ATOM   1267  N   LYS A 511     -44.950   5.472 -51.439  1.00 31.34           N
ANISOU 1267  N   LYS A 511     3960   3384   4566    367   2489    -66       N
ATOM   1268  CA  LYS A 511     -43.993   5.951 -52.436  1.00 34.36           C
ANISOU 1268  CA  LYS A 511     4376   3762   4918    355   2595    -38       C
ATOM   1269  C   LYS A 511     -42.584   5.471 -52.077  1.00 33.25           C
ANISOU 1269  C   LYS A 511     4110   3577   4948    374   2645      7       C
ATOM   1270  O   LYS A 511     -41.700   5.452 -52.924  1.00 34.69           O
ANISOU 1270  O   LYS A 511     4305   3742   5134    370   2757     13       O
ATOM   1271  CB  LYS A 511     -44.038   7.479 -52.586  1.00 35.05           C
ANISOU 1271  CB  LYS A 511     4493   3883   4940    330   2590     30       C
ATOM   1272  CG  LYS A 511     -45.293   7.983 -53.287  1.00 44.90           C
ANISOU 1272  CG  LYS A 511     5899   5180   5981    333   2570    -13       C
ATOM   1273  CD  LYS A 511     -45.224   9.468 -53.622  1.00 50.10           C
ANISOU 1273  CD  LYS A 511     6626   5850   6560    319   2597     71       C
ATOM   1274  CE  LYS A 511     -45.380  10.320 -52.383  1.00 54.08           C
ANISOU 1274  CE  LYS A 511     7030   6354   7165    311   2505    133       C
ATOM   1275  NZ  LYS A 511     -45.653  11.737 -52.733  1.00 57.53           N
ANISOU 1275  NZ  LYS A 511     7570   6790   7497    297   2455    201       N
ATOM   1276  N   GLU A 512     -42.385   5.084 -50.816  1.00 37.96           N
ANISOU 1276  N   GLU A 512     4586   4158   5678    405   2568     38       N
ATOM   1277  CA  GLU A 512     -41.149   4.422 -50.389  1.00 36.33           C
ANISOU 1277  CA  GLU A 512     4259   3915   5629    447   2604     68       C
ATOM   1278  C   GLU A 512     -41.389   2.924 -50.438  1.00 37.40           C
ANISOU 1278  C   GLU A 512     4439   3994   5777    486   2634     15       C
ATOM   1279  O   GLU A 512     -42.189   2.390 -49.665  1.00 42.43           O
ANISOU 1279  O   GLU A 512     5089   4614   6420    503   2565      6       O
ATOM   1280  CB  GLU A 512     -40.766   4.847 -48.969  1.00 39.28           C
ANISOU 1280  CB  GLU A 512     4487   4310   6129    478   2504    133       C
ATOM   1281  CG  GLU A 512     -39.721   3.983 -48.300  1.00 33.62           C
ANISOU 1281  CG  GLU A 512     3645   3566   5562    551   2512    159       C
ATOM   1282  CD  GLU A 512     -38.419   3.942 -49.090  1.00 41.55           C
ANISOU 1282  CD  GLU A 512     4583   4559   6645    548   2628    159       C
ATOM   1283  OE1 GLU A 512     -37.871   5.020 -49.399  1.00 36.56           O
ANISOU 1283  OE1 GLU A 512     3895   3954   6043    496   2657    182       O
ATOM   1284  OE2 GLU A 512     -37.947   2.832 -49.406  1.00 41.42           O
ANISOU 1284  OE2 GLU A 512     4571   4499   6668    596   2701    138       O
ATOM   1285  N   GLY A 513     -40.713   2.249 -51.361  1.00 39.67           N
ANISOU 1285  N   GLY A 513     4758   4245   6072    498   2752    -20       N
ATOM   1286  CA  GLY A 513     -40.925   0.833 -51.585  1.00 35.86           C
ANISOU 1286  CA  GLY A 513     4334   3690   5599    529   2806    -82       C
ATOM   1287  C   GLY A 513     -40.680  -0.068 -50.388  1.00 41.68           C
ANISOU 1287  C   GLY A 513     4990   4374   6473    594   2767    -39       C
ATOM   1288  O   GLY A 513     -41.227  -1.168 -50.321  1.00 36.00           O
ANISOU 1288  O   GLY A 513     4335   3581   5761    607   2792    -82       O
ATOM   1289  N   TYR A 514     -39.864   0.375 -49.437  1.00 37.79           N
ANISOU 1289  N   TYR A 514     4358   3913   6088    639   2711     44       N
ATOM   1290  CA  TYR A 514     -39.622  -0.445 -48.245  1.00 39.78           C
ANISOU 1290  CA  TYR A 514     4541   4124   6449    724   2670     96       C
ATOM   1291  C   TYR A 514     -40.555  -0.135 -47.053  1.00 34.32           C
ANISOU 1291  C   TYR A 514     3851   3455   5734    731   2549    137       C
ATOM   1292  O   TYR A 514     -40.479  -0.794 -46.013  1.00 36.37           O
ANISOU 1292  O   TYR A 514     4078   3681   6060    811   2519    191       O
ATOM   1293  CB  TYR A 514     -38.158  -0.368 -47.806  1.00 36.88           C
ANISOU 1293  CB  TYR A 514     4011   3782   6219    799   2677    152       C
ATOM   1294  CG  TYR A 514     -37.184  -1.034 -48.746  1.00 38.64           C
ANISOU 1294  CG  TYR A 514     4221   3966   6495    825   2810    120       C
ATOM   1295  CD1 TYR A 514     -37.629  -1.890 -49.750  1.00 39.21           C
ANISOU 1295  CD1 TYR A 514     4435   3966   6497    802   2914     49       C
ATOM   1296  CD2 TYR A 514     -35.812  -0.811 -48.628  1.00 39.96           C
ANISOU 1296  CD2 TYR A 514     4224   4170   6787    875   2835    153       C
ATOM   1297  CE1 TYR A 514     -36.732  -2.504 -50.620  1.00 46.97           C
ANISOU 1297  CE1 TYR A 514     5412   4913   7521    835   3046     16       C
ATOM   1298  CE2 TYR A 514     -34.903  -1.429 -49.487  1.00 41.77           C
ANISOU 1298  CE2 TYR A 514     4435   4367   7068    907   2969    123       C
ATOM   1299  CZ  TYR A 514     -35.372  -2.270 -50.482  1.00 46.63           C
ANISOU 1299  CZ  TYR A 514     5208   4909   7600    889   3076     58       C
ATOM   1300  OH  TYR A 514     -34.485  -2.876 -51.338  1.00 47.75           O
ANISOU 1300  OH  TYR A 514     5339   5019   7786    928   3216     25       O
ATOM   1301  N   TYR A 515     -41.418   0.864 -47.195  1.00 33.11           N
ANISOU 1301  N   TYR A 515     3741   3359   5482    659   2489    117       N
ATOM   1302  CA  TYR A 515     -42.384   1.184 -46.130  1.00 31.87           C
ANISOU 1302  CA  TYR A 515     3591   3227   5292    665   2386    149       C
ATOM   1303  C   TYR A 515     -43.383   0.041 -45.905  1.00 31.84           C
ANISOU 1303  C   TYR A 515     3681   3144   5274    666   2414    122       C
ATOM   1304  O   TYR A 515     -43.910  -0.528 -46.864  1.00 34.59           O
ANISOU 1304  O   TYR A 515     4118   3444   5579    610   2486     39       O
ATOM   1305  CB  TYR A 515     -43.102   2.498 -46.446  1.00 30.81           C
ANISOU 1305  CB  TYR A 515     3485   3166   5055    593   2329    127       C
ATOM   1306  CG  TYR A 515     -44.254   2.830 -45.519  1.00 39.04           C
ANISOU 1306  CG  TYR A 515     4549   4238   6048    594   2237    142       C
ATOM   1307  CD1 TYR A 515     -44.027   3.359 -44.251  1.00 34.75           C
ANISOU 1307  CD1 TYR A 515     3922   3733   5549    655   2152    212       C
ATOM   1308  CD2 TYR A 515     -45.567   2.617 -45.912  1.00 29.18           C
ANISOU 1308  CD2 TYR A 515     3394   2981   4711    540   2239     77       C
ATOM   1309  CE1 TYR A 515     -45.083   3.661 -43.397  1.00 34.16           C
ANISOU 1309  CE1 TYR A 515     3874   3685   5418    666   2080    227       C
ATOM   1310  CE2 TYR A 515     -46.635   2.918 -45.057  1.00 28.29           C
ANISOU 1310  CE2 TYR A 515     3290   2899   4562    542   2166     90       C
ATOM   1311  CZ  TYR A 515     -46.380   3.436 -43.805  1.00 27.85           C
ANISOU 1311  CZ  TYR A 515     3167   2877   4539    606   2092    170       C
ATOM   1312  OH  TYR A 515     -47.423   3.732 -42.961  1.00 38.64           O
ANISOU 1312  OH  TYR A 515     4548   4273   5860    618   2032    184       O
ATOM   1313  N   GLY A 516     -43.624  -0.309 -44.639  1.00 32.96           N
ANISOU 1313  N   GLY A 516     3802   3265   5456    731   2370    190       N
ATOM   1314  CA  GLY A 516     -44.652  -1.284 -44.286  1.00 31.69           C
ANISOU 1314  CA  GLY A 516     3725   3020   5295    721   2410    180       C
ATOM   1315  C   GLY A 516     -44.121  -2.690 -44.035  1.00 39.47           C
ANISOU 1315  C   GLY A 516     4732   3885   6378    793   2506    216       C
ATOM   1316  O   GLY A 516     -42.909  -2.920 -44.079  1.00 36.37           O
ANISOU 1316  O   GLY A 516     4278   3490   6050    866   2527    251       O
ATOM   1317  N   TYR A 517     -45.022  -3.635 -43.770  1.00 33.39           N
ANISOU 1317  N   TYR A 517     4045   3012   5631    773   2574    207       N
ATOM   1318  CA  TYR A 517     -44.624  -5.012 -43.476  1.00 34.86           C
ANISOU 1318  CA  TYR A 517     4271   3060   5913    843   2684    252       C
ATOM   1319  C   TYR A 517     -43.935  -5.656 -44.670  1.00 35.98           C
ANISOU 1319  C   TYR A 517     4432   3144   6095    825   2775    173       C
ATOM   1320  O   TYR A 517     -42.815  -6.150 -44.565  1.00 43.10           O
ANISOU 1320  O   TYR A 517     5294   4017   7063    922   2810    225       O
ATOM   1321  CB  TYR A 517     -45.839  -5.862 -43.136  1.00 35.20           C
ANISOU 1321  CB  TYR A 517     4405   2983   5987    793   2770    240       C
ATOM   1322  CG  TYR A 517     -46.589  -5.485 -41.883  1.00 36.93           C
ANISOU 1322  CG  TYR A 517     4626   3231   6175    822   2721    328       C
ATOM   1323  CD1 TYR A 517     -45.973  -5.525 -40.633  1.00 34.87           C
ANISOU 1323  CD1 TYR A 517     4345   2984   5919    967   2690    474       C
ATOM   1324  CD2 TYR A 517     -47.940  -5.138 -41.943  1.00 35.81           C
ANISOU 1324  CD2 TYR A 517     4507   3106   5995    715   2713    262       C
ATOM   1325  CE1 TYR A 517     -46.682  -5.213 -39.475  1.00 36.55           C
ANISOU 1325  CE1 TYR A 517     4580   3223   6085   1008   2662    557       C
ATOM   1326  CE2 TYR A 517     -48.648  -4.823 -40.793  1.00 33.35           C
ANISOU 1326  CE2 TYR A 517     4199   2819   5653    745   2686    344       C
ATOM   1327  CZ  TYR A 517     -48.018  -4.864 -39.569  1.00 33.69           C
ANISOU 1327  CZ  TYR A 517     4241   2870   5688    892   2668    494       C
ATOM   1328  OH  TYR A 517     -48.739  -4.558 -38.449  1.00 36.44           O
ANISOU 1328  OH  TYR A 517     4612   3246   5987    932   2656    574       O
ATOM   1329  N   THR A 518     -44.629  -5.663 -45.802  1.00 41.10           N
ANISOU 1329  N   THR A 518     5140   3781   6697    711   2814     42       N
ATOM   1330  CA  THR A 518     -44.105  -6.222 -47.042  1.00 44.73           C
ANISOU 1330  CA  THR A 518     5637   4192   7165    690   2907    -52       C
ATOM   1331  C   THR A 518     -42.838  -5.504 -47.524  1.00 44.56           C
ANISOU 1331  C   THR A 518     5537   4269   7123    737   2878    -28       C
ATOM   1332  O   THR A 518     -41.912  -6.132 -48.029  1.00 41.68           O
ANISOU 1332  O   THR A 518     5167   3857   6811    787   2962    -39       O
ATOM   1333  CB  THR A 518     -45.168  -6.168 -48.151  1.00 40.89           C
ANISOU 1333  CB  THR A 518     5229   3706   6600    567   2931   -210       C
ATOM   1334  OG1 THR A 518     -46.288  -6.978 -47.773  1.00 39.59           O
ANISOU 1334  OG1 THR A 518     5120   3430   6491    511   2985   -253       O
ATOM   1335  CG2 THR A 518     -44.600  -6.675 -49.463  1.00 38.35           C
ANISOU 1335  CG2 THR A 518     4961   3350   6260    558   3025   -312       C
ATOM   1336  N   GLY A 519     -42.807  -4.187 -47.361  1.00 35.89           N
ANISOU 1336  N   GLY A 519     4375   3302   5960    719   2771      1       N
ATOM   1337  CA  GLY A 519     -41.667  -3.400 -47.774  1.00 36.09           C
ANISOU 1337  CA  GLY A 519     4316   3413   5984    744   2757     24       C
ATOM   1338  C   GLY A 519     -40.443  -3.717 -46.941  1.00 38.02           C
ANISOU 1338  C   GLY A 519     4449   3652   6346    862   2753    119       C
ATOM   1339  O   GLY A 519     -39.331  -3.796 -47.455  1.00 47.24           O
ANISOU 1339  O   GLY A 519     5553   4829   7566    901   2809    116       O
ATOM   1340  N   ALA A 520     -40.649  -3.897 -45.643  1.00 38.67           N
ANISOU 1340  N   ALA A 520     4504   3723   6466    930   2688    203       N
ATOM   1341  CA  ALA A 520     -39.552  -4.232 -44.745  1.00 41.57           C
ANISOU 1341  CA  ALA A 520     4766   4095   6932   1067   2666    293       C
ATOM   1342  C   ALA A 520     -38.982  -5.612 -45.076  1.00 41.58           C
ANISOU 1342  C   ALA A 520     4804   3981   7015   1137   2788    289       C
ATOM   1343  O   ALA A 520     -37.775  -5.847 -44.940  1.00 43.66           O
ANISOU 1343  O   ALA A 520     4963   4261   7363   1239   2798    323       O
ATOM   1344  CB  ALA A 520     -40.011  -4.167 -43.297  1.00 40.89           C
ANISOU 1344  CB  ALA A 520     4675   4023   6840   1140   2576    385       C
ATOM   1345  N   PHE A 521     -39.854  -6.515 -45.523  1.00 39.62           N
ANISOU 1345  N   PHE A 521     4693   3613   6748   1081   2881    236       N
ATOM   1346  CA  PHE A 521     -39.434  -7.848 -45.935  1.00 41.43           C
ANISOU 1346  CA  PHE A 521     4976   3713   7052   1134   3012    216       C
ATOM   1347  C   PHE A 521     -38.665  -7.745 -47.230  1.00 43.39           C
ANISOU 1347  C   PHE A 521     5201   3988   7298   1107   3082    131       C
ATOM   1348  O   PHE A 521     -37.707  -8.490 -47.460  1.00 43.97           O
ANISOU 1348  O   PHE A 521     5243   4013   7451   1196   3162    137       O
ATOM   1349  CB  PHE A 521     -40.635  -8.781 -46.117  1.00 41.61           C
ANISOU 1349  CB  PHE A 521     5148   3593   7068   1059   3101    163       C
ATOM   1350  CG  PHE A 521     -40.259 -10.207 -46.451  1.00 44.36           C
ANISOU 1350  CG  PHE A 521     5564   3787   7503   1114   3243    143       C
ATOM   1351  CD1 PHE A 521     -39.387 -10.922 -45.640  1.00 45.03           C
ANISOU 1351  CD1 PHE A 521     5611   3823   7676   1269   3265    252       C
ATOM   1352  CD2 PHE A 521     -40.784 -10.834 -47.570  1.00 50.12           C
ANISOU 1352  CD2 PHE A 521     6398   4424   8221   1020   3350      7       C
ATOM   1353  CE1 PHE A 521     -39.037 -12.232 -45.948  1.00 47.07           C
ANISOU 1353  CE1 PHE A 521     5937   3932   8015   1328   3399    235       C
ATOM   1354  CE2 PHE A 521     -40.444 -12.152 -47.878  1.00 54.69           C
ANISOU 1354  CE2 PHE A 521     7045   4852   8883   1070   3486    -20       C
ATOM   1355  CZ  PHE A 521     -39.571 -12.848 -47.063  1.00 47.74           C
ANISOU 1355  CZ  PHE A 521     6129   3915   8096   1223   3514     99       C
ATOM   1356  N   ARG A 522     -39.081  -6.827 -48.091  1.00 41.26           N
ANISOU 1356  N   ARG A 522     4951   3795   6930    995   3059     55       N
ATOM   1357  CA  ARG A 522     -38.365  -6.651 -49.340  1.00 42.20           C
ANISOU 1357  CA  ARG A 522     5062   3945   7027    974   3139    -16       C
ATOM   1358  C   ARG A 522     -36.975  -6.091 -49.049  1.00 42.83           C
ANISOU 1358  C   ARG A 522     4974   4112   7186   1054   3114     53       C
ATOM   1359  O   ARG A 522     -35.983  -6.499 -49.657  1.00 44.48           O
ANISOU 1359  O   ARG A 522     5141   4307   7453   1106   3210     32       O
ATOM   1360  CB  ARG A 522     -39.136  -5.742 -50.294  1.00 41.17           C
ANISOU 1360  CB  ARG A 522     5002   3883   6756    851   3120   -100       C
ATOM   1361  CG  ARG A 522     -38.433  -5.549 -51.616  1.00 42.35           C
ANISOU 1361  CG  ARG A 522     5167   4064   6860    837   3219   -164       C
ATOM   1362  CD  ARG A 522     -39.248  -4.713 -52.580  1.00 47.58           C
ANISOU 1362  CD  ARG A 522     5924   4792   7360    736   3206   -241       C
ATOM   1363  NE  ARG A 522     -38.570  -4.624 -53.871  1.00 44.40           N
ANISOU 1363  NE  ARG A 522     5560   4411   6898    736   3322   -296       N
ATOM   1364  CZ  ARG A 522     -39.049  -3.990 -54.937  1.00 44.64           C
ANISOU 1364  CZ  ARG A 522     5691   4499   6771    674   3345   -363       C
ATOM   1365  NH1 ARG A 522     -40.224  -3.373 -54.881  1.00 42.94           N
ANISOU 1365  NH1 ARG A 522     5539   4331   6446    606   3250   -392       N
ATOM   1366  NH2 ARG A 522     -38.343  -3.970 -56.062  1.00 44.69           N
ANISOU 1366  NH2 ARG A 522     5738   4521   6722    690   3467   -399       N
ATOM   1367  N   CYS A 523     -36.917  -5.154 -48.108  1.00 41.69           N
ANISOU 1367  N   CYS A 523     4727   4059   7052   1064   2987    125       N
ATOM   1368  CA  CYS A 523     -35.650  -4.618 -47.625  1.00 43.52           C
ANISOU 1368  CA  CYS A 523     4776   4378   7384   1140   2943    181       C
ATOM   1369  C   CYS A 523     -34.696  -5.742 -47.163  1.00 48.26           C
ANISOU 1369  C   CYS A 523     5306   4922   8108   1290   2987    221       C
ATOM   1370  O   CYS A 523     -33.523  -5.768 -47.542  1.00 50.72           O
ANISOU 1370  O   CYS A 523     5500   5266   8506   1343   3041    212       O
ATOM   1371  CB  CYS A 523     -35.902  -3.620 -46.496  1.00 41.03           C
ANISOU 1371  CB  CYS A 523     4377   4152   7062   1141   2788    243       C
ATOM   1372  SG  CYS A 523     -34.428  -2.962 -45.685  1.00 44.10           S
ANISOU 1372  SG  CYS A 523     4514   4651   7591   1240   2701    296       S
ATOM   1373  N   LEU A 524     -35.207  -6.663 -46.350  1.00 44.39           N
ANISOU 1373  N   LEU A 524     4891   4346   7629   1362   2971    268       N
ATOM   1374  CA  LEU A 524     -34.424  -7.807 -45.891  1.00 48.60           C
ANISOU 1374  CA  LEU A 524     5389   4811   8266   1517   3015    314       C
ATOM   1375  C   LEU A 524     -33.892  -8.626 -47.061  1.00 53.75           C
ANISOU 1375  C   LEU A 524     6082   5385   8955   1524   3175    242       C
ATOM   1376  O   LEU A 524     -32.692  -8.865 -47.158  1.00 49.80           O
ANISOU 1376  O   LEU A 524     5457   4911   8552   1626   3209    248       O
ATOM   1377  CB  LEU A 524     -35.257  -8.706 -44.984  1.00 49.16           C
ANISOU 1377  CB  LEU A 524     5584   4773   8323   1572   3007    378       C
ATOM   1378  CG  LEU A 524     -34.596  -9.987 -44.479  1.00 48.37           C
ANISOU 1378  CG  LEU A 524     5487   4576   8316   1742   3061    437       C
ATOM   1379  CD1 LEU A 524     -33.376  -9.676 -43.635  1.00 49.48           C
ANISOU 1379  CD1 LEU A 524     5438   4828   8536   1904   2947    502       C
ATOM   1380  CD2 LEU A 524     -35.606 -10.771 -43.680  1.00 48.19           C
ANISOU 1380  CD2 LEU A 524     5616   4430   8262   1762   3078    505       C
ATOM   1381  N   VAL A 525     -34.796  -9.036 -47.944  1.00 49.61           N
ANISOU 1381  N   VAL A 525     5725   4771   8354   1418   3267    163       N
ATOM   1382  CA  VAL A 525     -34.457  -9.845 -49.108  1.00 51.16           C
ANISOU 1382  CA  VAL A 525     5991   4886   8563   1419   3422     78       C
ATOM   1383  C   VAL A 525     -33.398  -9.184 -50.004  1.00 52.12           C
ANISOU 1383  C   VAL A 525     6002   5105   8697   1414   3474     38       C
ATOM   1384  O   VAL A 525     -32.460  -9.838 -50.466  1.00 53.99           O
ANISOU 1384  O   VAL A 525     6196   5308   9008   1500   3580     17       O
ATOM   1385  CB  VAL A 525     -35.735 -10.180 -49.922  1.00 48.66           C
ANISOU 1385  CB  VAL A 525     5866   4482   8142   1289   3485    -23       C
ATOM   1386  CG1 VAL A 525     -35.396 -10.596 -51.336  1.00 50.83           C
ANISOU 1386  CG1 VAL A 525     6208   4720   8386   1267   3626   -137       C
ATOM   1387  CG2 VAL A 525     -36.525 -11.269 -49.221  1.00 48.89           C
ANISOU 1387  CG2 VAL A 525     6003   4364   8209   1312   3506      2       C
ATOM   1388  N   GLU A 526     -33.534  -7.882 -50.216  1.00 48.81           N
ANISOU 1388  N   GLU A 526     5533   4801   8211   1316   3407     34       N
ATOM   1389  CA  GLU A 526     -32.681  -7.170 -51.157  1.00 49.67           C
ANISOU 1389  CA  GLU A 526     5563   4991   8319   1284   3478      0       C
ATOM   1390  C   GLU A 526     -31.414  -6.563 -50.536  1.00 50.50           C
ANISOU 1390  C   GLU A 526     5434   5198   8557   1357   3428     64       C
ATOM   1391  O   GLU A 526     -30.348  -6.546 -51.173  1.00 52.32           O
ANISOU 1391  O   GLU A 526     5566   5458   8857   1390   3530     42       O
ATOM   1392  CB  GLU A 526     -33.488  -6.089 -51.895  1.00 48.13           C
ANISOU 1392  CB  GLU A 526     5458   4853   7977   1138   3460    -43       C
ATOM   1393  CG  GLU A 526     -34.627  -6.647 -52.745  1.00 47.82           C
ANISOU 1393  CG  GLU A 526     5631   4735   7804   1068   3518   -136       C
ATOM   1394  CD  GLU A 526     -35.421  -5.572 -53.494  1.00 54.23           C
ANISOU 1394  CD  GLU A 526     6531   5616   8456    946   3490   -180       C
ATOM   1395  OE1 GLU A 526     -35.371  -4.380 -53.103  1.00 45.38           O
ANISOU 1395  OE1 GLU A 526     5328   4588   7327    903   3401   -123       O
ATOM   1396  OE2 GLU A 526     -36.104  -5.925 -54.484  1.00 51.36           O
ANISOU 1396  OE2 GLU A 526     6325   5217   7973    899   3557   -278       O
ATOM   1397  N   LYS A 527     -31.518  -6.068 -49.306  1.00 49.40           N
ANISOU 1397  N   LYS A 527     5198   5115   8456   1384   3273    133       N
ATOM   1398  CA  LYS A 527     -30.443  -5.246 -48.746  1.00 51.94           C
ANISOU 1398  CA  LYS A 527     5288   5554   8895   1425   3201    171       C
ATOM   1399  C   LYS A 527     -30.050  -5.543 -47.301  1.00 54.55           C
ANISOU 1399  C   LYS A 527     5487   5915   9323   1568   3062    238       C
ATOM   1400  O   LYS A 527     -28.888  -5.380 -46.936  1.00 54.88           O
ANISOU 1400  O   LYS A 527     5321   6034   9497   1657   3028    248       O
ATOM   1401  CB  LYS A 527     -30.774  -3.751 -48.886  1.00 50.90           C
ANISOU 1401  CB  LYS A 527     5127   5508   8704   1286   3139    169       C
ATOM   1402  CG  LYS A 527     -30.798  -3.249 -50.320  1.00 54.84           C
ANISOU 1402  CG  LYS A 527     5709   6004   9123   1170   3276    115       C
ATOM   1403  CD  LYS A 527     -31.237  -1.791 -50.416  1.00 59.69           C
ANISOU 1403  CD  LYS A 527     6324   6686   9670   1040   3216    125       C
ATOM   1404  CE  LYS A 527     -31.538  -1.412 -51.872  1.00 63.25           C
ANISOU 1404  CE  LYS A 527     6921   7119   9992    941   3350     78       C
ATOM   1405  NZ  LYS A 527     -32.013  -0.005 -52.061  1.00 58.13           N
ANISOU 1405  NZ  LYS A 527     6300   6522   9266    823   3306     94       N
ATOM   1406  N   GLY A 528     -31.000  -5.970 -46.474  1.00 49.24           N
ANISOU 1406  N   GLY A 528     4934   5189   8586   1598   2980    281       N
ATOM   1407  CA  GLY A 528     -30.756  -6.000 -45.042  1.00 49.44           C
ANISOU 1407  CA  GLY A 528     4855   5264   8668   1731   2825    353       C
ATOM   1408  C   GLY A 528     -30.286  -7.301 -44.417  1.00 51.29           C
ANISOU 1408  C   GLY A 528     5088   5429   8972   1921   2831    400       C
ATOM   1409  O   GLY A 528     -30.166  -8.323 -45.083  1.00 52.48           O
ANISOU 1409  O   GLY A 528     5326   5474   9140   1953   2969    376       O
ATOM   1410  N   ASP A 529     -30.028  -7.250 -43.114  1.00 51.69           N
ANISOU 1410  N   ASP A 529     5047   5537   9055   2058   2674    465       N
ATOM   1411  CA  ASP A 529     -29.664  -8.434 -42.346  1.00 53.50           C
ANISOU 1411  CA  ASP A 529     5297   5701   9330   2261   2652    529       C
ATOM   1412  C   ASP A 529     -30.815  -8.864 -41.449  1.00 54.27           C
ANISOU 1412  C   ASP A 529     5584   5715   9320   2286   2606    612       C
ATOM   1413  O   ASP A 529     -30.923 -10.032 -41.081  1.00 53.58           O
ANISOU 1413  O   ASP A 529     5611   5511   9237   2404   2655    671       O
ATOM   1414  CB  ASP A 529     -28.447  -8.137 -41.472  1.00 60.55           C
ANISOU 1414  CB  ASP A 529     5948   6726  10333   2433   2493    543       C
ATOM   1415  CG  ASP A 529     -27.230  -7.737 -42.280  1.00 62.07           C
ANISOU 1415  CG  ASP A 529     5923   7006  10655   2414   2548    464       C
ATOM   1416  OD1 ASP A 529     -27.013  -8.336 -43.357  1.00 57.67           O
ANISOU 1416  OD1 ASP A 529     5419   6370  10124   2377   2728    423       O
ATOM   1417  OD2 ASP A 529     -26.502  -6.820 -41.838  1.00 59.92           O
ANISOU 1417  OD2 ASP A 529     5426   6879  10461   2433   2415    440       O
ATOM   1418  N   VAL A 530     -31.669  -7.910 -41.083  1.00 53.34           N
ANISOU 1418  N   VAL A 530     5502   5654   9110   2178   2520    621       N
ATOM   1419  CA  VAL A 530     -32.757  -8.200 -40.167  1.00 51.68           C
ANISOU 1419  CA  VAL A 530     5458   5381   8797   2201   2478    703       C
ATOM   1420  C   VAL A 530     -33.967  -7.318 -40.439  1.00 52.57           C
ANISOU 1420  C   VAL A 530     5661   5509   8803   2010   2479    672       C
ATOM   1421  O   VAL A 530     -33.839  -6.100 -40.623  1.00 51.86           O
ANISOU 1421  O   VAL A 530     5459   5536   8708   1922   2403    624       O
ATOM   1422  CB  VAL A 530     -32.304  -8.074 -38.692  1.00 55.57           C
ANISOU 1422  CB  VAL A 530     5871   5957   9288   2397   2290    787       C
ATOM   1423  CG1 VAL A 530     -31.805  -6.674 -38.397  1.00 49.66           C
ANISOU 1423  CG1 VAL A 530     4922   5384   8562   2373   2125    741       C
ATOM   1424  CG2 VAL A 530     -33.427  -8.472 -37.739  1.00 49.55           C
ANISOU 1424  CG2 VAL A 530     5306   5118   8404   2432   2276    890       C
ATOM   1425  N   ALA A 531     -35.140  -7.948 -40.488  1.00 48.81           N
ANISOU 1425  N   ALA A 531     5383   4909   8255   1944   2572    696       N
ATOM   1426  CA  ALA A 531     -36.382  -7.220 -40.725  1.00 43.99           C
ANISOU 1426  CA  ALA A 531     4862   4307   7545   1775   2573    662       C
ATOM   1427  C   ALA A 531     -37.309  -7.319 -39.527  1.00 44.47           C
ANISOU 1427  C   ALA A 531     5028   4343   7526   1824   2520    755       C
ATOM   1428  O   ALA A 531     -37.647  -8.413 -39.065  1.00 44.10           O
ANISOU 1428  O   ALA A 531     5104   4174   7479   1896   2597    827       O
ATOM   1429  CB  ALA A 531     -37.074  -7.714 -41.981  1.00 43.25           C
ANISOU 1429  CB  ALA A 531     4893   4104   7437   1624   2727    577       C
ATOM   1430  N   PHE A 532     -37.714  -6.160 -39.024  1.00 41.63           N
ANISOU 1430  N   PHE A 532     4624   4095   7097   1785   2398    757       N
ATOM   1431  CA  PHE A 532     -38.615  -6.113 -37.895  1.00 46.25           C
ANISOU 1431  CA  PHE A 532     5309   4673   7590   1831   2350    843       C
ATOM   1432  C   PHE A 532     -40.050  -5.995 -38.374  1.00 39.51           C
ANISOU 1432  C   PHE A 532     4581   3757   6672   1658   2438    799       C
ATOM   1433  O   PHE A 532     -40.481  -4.949 -38.834  1.00 43.53           O
ANISOU 1433  O   PHE A 532     5054   4347   7140   1536   2390    727       O
ATOM   1434  CB  PHE A 532     -38.206  -4.989 -36.949  1.00 43.25           C
ANISOU 1434  CB  PHE A 532     4813   4448   7171   1918   2158    868       C
ATOM   1435  CG  PHE A 532     -36.824  -5.175 -36.370  1.00 42.71           C
ANISOU 1435  CG  PHE A 532     4609   4443   7174   2104   2048    902       C
ATOM   1436  CD1 PHE A 532     -36.606  -6.079 -35.346  1.00 44.41           C
ANISOU 1436  CD1 PHE A 532     4897   4614   7363   2294   2019   1012       C
ATOM   1437  CD2 PHE A 532     -35.748  -4.464 -36.867  1.00 43.05           C
ANISOU 1437  CD2 PHE A 532     4452   4589   7316   2090   1978    823       C
ATOM   1438  CE1 PHE A 532     -35.341  -6.261 -34.809  1.00 46.42           C
ANISOU 1438  CE1 PHE A 532     5021   4935   7680   2480   1895   1033       C
ATOM   1439  CE2 PHE A 532     -34.481  -4.633 -36.335  1.00 53.04           C
ANISOU 1439  CE2 PHE A 532     5566   5921   8664   2262   1866    839       C
ATOM   1440  CZ  PHE A 532     -34.276  -5.533 -35.304  1.00 46.74           C
ANISOU 1440  CZ  PHE A 532     4838   5087   7834   2464   1812    939       C
ATOM   1441  N   VAL A 533     -40.783  -7.097 -38.282  1.00 49.25           N
ANISOU 1441  N   VAL A 533     5959   4843   7910   1649   2571    839       N
ATOM   1442  CA  VAL A 533     -42.104  -7.189 -38.883  1.00 39.08           C
ANISOU 1442  CA  VAL A 533     4773   3478   6599   1478   2670    773       C
ATOM   1443  C   VAL A 533     -43.046  -8.039 -38.026  1.00 47.98           C
ANISOU 1443  C   VAL A 533     6039   4479   7712   1509   2772    867       C
ATOM   1444  O   VAL A 533     -42.684  -8.468 -36.930  1.00 40.95           O
ANISOU 1444  O   VAL A 533     5182   3574   6801   1670   2757    995       O
ATOM   1445  CB  VAL A 533     -42.021  -7.798 -40.297  1.00 41.80           C
ANISOU 1445  CB  VAL A 533     5140   3733   7010   1368   2785    659       C
ATOM   1446  CG1 VAL A 533     -41.330  -6.847 -41.260  1.00 38.74           C
ANISOU 1446  CG1 VAL A 533     4639   3465   6614   1307   2714    564       C
ATOM   1447  CG2 VAL A 533     -41.292  -9.119 -40.256  1.00 41.56           C
ANISOU 1447  CG2 VAL A 533     5147   3577   7066   1477   2889    708       C
ATOM   1448  N   LYS A 534     -44.254  -8.266 -38.539  1.00 39.21           N
ANISOU 1448  N   LYS A 534     5006   3280   6613   1354   2875    798       N
ATOM   1449  CA  LYS A 534     -45.255  -9.082 -37.868  1.00 40.38           C
ANISOU 1449  CA  LYS A 534     5276   3288   6777   1346   3011    869       C
ATOM   1450  C   LYS A 534     -45.009 -10.534 -38.245  1.00 42.46           C
ANISOU 1450  C   LYS A 534     5619   3369   7148   1357   3177    874       C
ATOM   1451  O   LYS A 534     -44.324 -10.812 -39.233  1.00 42.30           O
ANISOU 1451  O   LYS A 534     5560   3331   7180   1332   3187    787       O
ATOM   1452  CB  LYS A 534     -46.673  -8.657 -38.280  1.00 40.71           C
ANISOU 1452  CB  LYS A 534     5337   3319   6810   1167   3046    769       C
ATOM   1453  CG  LYS A 534     -46.994  -8.919 -39.746  1.00 38.69           C
ANISOU 1453  CG  LYS A 534     5076   3006   6619   1001   3101    594       C
ATOM   1454  CD  LYS A 534     -48.374  -8.415 -40.130  1.00 39.15           C
ANISOU 1454  CD  LYS A 534     5132   3083   6662    839   3100    479       C
ATOM   1455  CE  LYS A 534     -48.624  -8.572 -41.622  1.00 41.16           C
ANISOU 1455  CE  LYS A 534     5378   3313   6949    696   3124    290       C
ATOM   1456  NZ  LYS A 534     -49.970  -8.040 -41.978  1.00 43.79           N
ANISOU 1456  NZ  LYS A 534     5689   3689   7258    552   3100    167       N
ATOM   1457  N   HIS A 535     -45.577 -11.453 -37.471  1.00 43.30           N
ANISOU 1457  N   HIS A 535     5838   3333   7282   1394   3318    976       N
ATOM   1458  CA  HIS A 535     -45.245 -12.871 -37.604  1.00 50.64           C
ANISOU 1458  CA  HIS A 535     6851   4085   8306   1437   3475   1008       C
ATOM   1459  C   HIS A 535     -45.780 -13.514 -38.882  1.00 51.38           C
ANISOU 1459  C   HIS A 535     6968   4043   8510   1256   3605    842       C
ATOM   1460  O   HIS A 535     -45.327 -14.587 -39.281  1.00 58.61           O
ANISOU 1460  O   HIS A 535     7934   4829   9508   1282   3714    827       O
ATOM   1461  CB  HIS A 535     -45.719 -13.666 -36.375  1.00 53.13           C
ANISOU 1461  CB  HIS A 535     7292   4285   8610   1529   3605   1171       C
ATOM   1462  CG  HIS A 535     -47.203 -13.876 -36.319  1.00 51.80           C
ANISOU 1462  CG  HIS A 535     7186   4006   8491   1368   3761   1135       C
ATOM   1463  ND1 HIS A 535     -48.047 -13.046 -35.611  1.00 49.35           N
ANISOU 1463  ND1 HIS A 535     6871   3775   8103   1345   3728   1179       N
ATOM   1464  CD2 HIS A 535     -47.993 -14.821 -36.885  1.00 54.43           C
ANISOU 1464  CD2 HIS A 535     7573   4156   8954   1220   3955   1047       C
ATOM   1465  CE1 HIS A 535     -49.292 -13.471 -35.742  1.00 53.49           C
ANISOU 1465  CE1 HIS A 535     7435   4169   8719   1191   3901   1122       C
ATOM   1466  NE2 HIS A 535     -49.286 -14.546 -36.510  1.00 56.90           N
ANISOU 1466  NE2 HIS A 535     7897   4443   9280   1108   4037   1035       N
ATOM   1467  N   GLN A 536     -46.747 -12.873 -39.524  1.00 49.75           N
ANISOU 1467  N   GLN A 536     6729   3871   8302   1080   3586    707       N
ATOM   1468  CA  GLN A 536     -47.358 -13.487 -40.693  1.00 57.25           C
ANISOU 1468  CA  GLN A 536     7705   4699   9347    910   3697    530       C
ATOM   1469  C   GLN A 536     -46.777 -12.932 -42.004  1.00 52.83           C
ANISOU 1469  C   GLN A 536     7077   4246   8751    858   3592    378       C
ATOM   1470  O   GLN A 536     -47.205 -13.320 -43.096  1.00 44.58           O
ANISOU 1470  O   GLN A 536     6055   3132   7753    728   3655    209       O
ATOM   1471  CB  GLN A 536     -48.888 -13.346 -40.645  1.00 59.53           C
ANISOU 1471  CB  GLN A 536     8007   4935   9677    744   3767    451       C
ATOM   1472  CG  GLN A 536     -49.654 -14.479 -41.339  1.00 66.31           C
ANISOU 1472  CG  GLN A 536     8919   5599  10677    593   3948    310       C
ATOM   1473  CD  GLN A 536     -49.785 -15.741 -40.494  1.00 70.80           C
ANISOU 1473  CD  GLN A 536     9582   5981  11339    646   4147    433       C
ATOM   1474  OE1 GLN A 536     -48.791 -16.391 -40.151  1.00 66.45           O
ANISOU 1474  OE1 GLN A 536     9083   5384  10780    798   4176    552       O
ATOM   1475  NE2 GLN A 536     -51.023 -16.096 -40.158  1.00 77.21           N
ANISOU 1475  NE2 GLN A 536    10409   6688  12240    525   4286    398       N
ATOM   1476  N   THR A 537     -45.787 -12.049 -41.889  1.00 44.11           N
ANISOU 1476  N   THR A 537     5891   3309   7562    964   3440    434       N
ATOM   1477  CA  THR A 537     -45.194 -11.405 -43.059  1.00 42.26           C
ANISOU 1477  CA  THR A 537     5589   3188   7281    923   3353    312       C
ATOM   1478  C   THR A 537     -44.487 -12.402 -43.991  1.00 48.85           C
ANISOU 1478  C   THR A 537     6461   3916   8184    937   3458    237       C
ATOM   1479  O   THR A 537     -44.748 -12.429 -45.195  1.00 48.26           O
ANISOU 1479  O   THR A 537     6405   3833   8099    827   3485     76       O
ATOM   1480  CB  THR A 537     -44.221 -10.279 -42.659  1.00 41.11           C
ANISOU 1480  CB  THR A 537     5333   3230   7056   1030   3189    391       C
ATOM   1481  OG1 THR A 537     -44.941  -9.262 -41.958  1.00 43.63           O
ANISOU 1481  OG1 THR A 537     5622   3656   7298   1003   3085    429       O
ATOM   1482  CG2 THR A 537     -43.564  -9.651 -43.904  1.00 40.63           C
ANISOU 1482  CG2 THR A 537     5208   3272   6956    984   3135    276       C
ATOM   1483  N   VAL A 538     -43.598 -13.218 -43.435  1.00 45.51           N
ANISOU 1483  N   VAL A 538     6053   3418   7819   1083   3514    351       N
ATOM   1484  CA  VAL A 538     -42.904 -14.221 -44.243  1.00 47.36           C
ANISOU 1484  CA  VAL A 538     6326   3545   8125   1115   3621    287       C
ATOM   1485  C   VAL A 538     -43.861 -15.205 -44.935  1.00 53.09           C
ANISOU 1485  C   VAL A 538     7161   4091   8919    976   3772    153       C
ATOM   1486  O   VAL A 538     -43.747 -15.407 -46.140  1.00 49.11           O
ANISOU 1486  O   VAL A 538     6676   3570   8414    909   3808     -1       O
ATOM   1487  CB  VAL A 538     -41.762 -14.951 -43.477  1.00 49.06           C
ANISOU 1487  CB  VAL A 538     6534   3714   8394   1317   3647    433       C
ATOM   1488  CG1 VAL A 538     -41.068 -15.961 -44.384  1.00 51.08           C
ANISOU 1488  CG1 VAL A 538     6827   3856   8724   1350   3762    354       C
ATOM   1489  CG2 VAL A 538     -40.741 -13.951 -42.943  1.00 48.16           C
ANISOU 1489  CG2 VAL A 538     6285   3789   8224   1445   3484    522       C
ATOM   1490  N   PRO A 539     -44.822 -15.798 -44.191  1.00 53.94           N
ANISOU 1490  N   PRO A 539     7339   4069   9086    929   3865    201       N
ATOM   1491  CA  PRO A 539     -45.794 -16.646 -44.893  1.00 53.45           C
ANISOU 1491  CA  PRO A 539     7357   3846   9107    772   4000     42       C
ATOM   1492  C   PRO A 539     -46.539 -15.886 -45.989  1.00 52.37           C
ANISOU 1492  C   PRO A 539     7187   3802   8908    606   3927   -161       C
ATOM   1493  O   PRO A 539     -46.731 -16.436 -47.069  1.00 53.97           O
ANISOU 1493  O   PRO A 539     7437   3933   9138    519   3987   -338       O
ATOM   1494  CB  PRO A 539     -46.770 -17.055 -43.784  1.00 54.75           C
ANISOU 1494  CB  PRO A 539     7567   3902   9335    738   4094    140       C
ATOM   1495  CG  PRO A 539     -45.963 -17.002 -42.542  1.00 56.18           C
ANISOU 1495  CG  PRO A 539     7744   4123   9477    937   4059    371       C
ATOM   1496  CD  PRO A 539     -45.036 -15.826 -42.732  1.00 53.87           C
ANISOU 1496  CD  PRO A 539     7347   4046   9077   1020   3870    390       C
ATOM   1497  N   GLN A 540     -46.924 -14.638 -45.721  1.00 46.98           N
ANISOU 1497  N   GLN A 540     6433   3283   8135    578   3792   -140       N
ATOM   1498  CA  GLN A 540     -47.697 -13.849 -46.680  1.00 45.87           C
ANISOU 1498  CA  GLN A 540     6263   3246   7919    438   3711   -323       C
ATOM   1499  C   GLN A 540     -46.914 -13.485 -47.946  1.00 45.81           C
ANISOU 1499  C   GLN A 540     6248   3339   7817    453   3654   -432       C
ATOM   1500  O   GLN A 540     -47.496 -13.237 -49.001  1.00 50.73           O
ANISOU 1500  O   GLN A 540     6889   4006   8379    345   3629   -617       O
ATOM   1501  CB  GLN A 540     -48.277 -12.592 -46.011  1.00 43.73           C
ANISOU 1501  CB  GLN A 540     5919   3126   7570    422   3581   -260       C
ATOM   1502  CG  GLN A 540     -49.543 -12.887 -45.203  1.00 50.76           C
ANISOU 1502  CG  GLN A 540     6823   3918   8547    336   3658   -247       C
ATOM   1503  CD  GLN A 540     -49.872 -11.843 -44.139  1.00 53.69           C
ANISOU 1503  CD  GLN A 540     7136   4413   8852    381   3555   -114       C
ATOM   1504  OE1 GLN A 540     -50.551 -12.149 -43.148  1.00 53.20           O
ANISOU 1504  OE1 GLN A 540     7093   4265   8857    375   3639    -25       O
ATOM   1505  NE2 GLN A 540     -49.418 -10.609 -44.344  1.00 40.49           N
ANISOU 1505  NE2 GLN A 540     5397   2941   7045    425   3385   -102       N
ATOM   1506  N   ASN A 541     -45.594 -13.459 -47.854  1.00 45.99           N
ANISOU 1506  N   ASN A 541     6244   3404   7826    593   3639   -323       N
ATOM   1507  CA  ASN A 541     -44.815 -13.015 -49.002  1.00 52.72           C
ANISOU 1507  CA  ASN A 541     7081   4362   8590    611   3602   -409       C
ATOM   1508  C   ASN A 541     -43.900 -14.074 -49.618  1.00 56.57           C
ANISOU 1508  C   ASN A 541     7619   4740   9136    683   3720   -444       C
ATOM   1509  O   ASN A 541     -42.926 -13.746 -50.299  1.00 48.34           O
ANISOU 1509  O   ASN A 541     6546   3783   8039    745   3707   -457       O
ATOM   1510  CB  ASN A 541     -44.046 -11.747 -48.652  1.00 46.54           C
ANISOU 1510  CB  ASN A 541     6192   3765   7726    689   3469   -293       C
ATOM   1511  CG  ASN A 541     -44.957 -10.542 -48.521  1.00 42.34           C
ANISOU 1511  CG  ASN A 541     5622   3366   7097    603   3346   -315       C
ATOM   1512  OD1 ASN A 541     -45.183  -9.820 -49.489  1.00 44.51           O
ANISOU 1512  OD1 ASN A 541     5902   3746   7265    538   3297   -425       O
ATOM   1513  ND2 ASN A 541     -45.490 -10.325 -47.326  1.00 41.44           N
ANISOU 1513  ND2 ASN A 541     5481   3250   7013    613   3302   -207       N
ATOM   1514  N   THR A 542     -44.226 -15.344 -49.387  1.00 57.73           N
ANISOU 1514  N   THR A 542     7845   4694   9398    672   3846   -462       N
ATOM   1515  CA  THR A 542     -43.472 -16.442 -49.984  1.00 58.73           C
ANISOU 1515  CA  THR A 542     8033   4697   9584    737   3967   -511       C
ATOM   1516  C   THR A 542     -44.404 -17.451 -50.654  1.00 64.18           C
ANISOU 1516  C   THR A 542     8834   5221  10330    611   4073   -697       C
ATOM   1517  O   THR A 542     -45.623 -17.371 -50.498  1.00 59.68           O
ANISOU 1517  O   THR A 542     8278   4622   9777    476   4060   -770       O
ATOM   1518  CB  THR A 542     -42.592 -17.165 -48.944  1.00 55.01           C
ANISOU 1518  CB  THR A 542     7549   4136   9217    900   4025   -325       C
ATOM   1519  OG1 THR A 542     -43.410 -17.634 -47.866  1.00 54.45           O
ANISOU 1519  OG1 THR A 542     7515   3951   9222    873   4069   -235       O
ATOM   1520  CG2 THR A 542     -41.511 -16.230 -48.398  1.00 52.02           C
ANISOU 1520  CG2 THR A 542     7046   3928   8791   1034   3909   -175       C
ATOM   1521  N   GLY A 543     -43.820 -18.388 -51.404  1.00 66.26           N
ANISOU 1521  N   GLY A 543     9169   5379  10630    656   4176   -783       N
ATOM   1522  CA  GLY A 543     -44.566 -19.446 -52.064  1.00 65.95           C
ANISOU 1522  CA  GLY A 543     9238   5169  10652    548   4277   -971       C
ATOM   1523  C   GLY A 543     -45.588 -18.975 -53.085  1.00 68.50           C
ANISOU 1523  C   GLY A 543     9588   5564  10874    388   4207  -1201       C
ATOM   1524  O   GLY A 543     -46.645 -19.585 -53.245  1.00 74.68           O
ANISOU 1524  O   GLY A 543    10421   6228  11725    253   4244  -1348       O
ATOM   1525  N   GLY A 544     -45.279 -17.885 -53.778  1.00 64.14           N
ANISOU 1525  N   GLY A 544     9000   5209  10161    405   4104  -1237       N
ATOM   1526  CA  GLY A 544     -46.190 -17.338 -54.765  1.00 64.34           C
ANISOU 1526  CA  GLY A 544     9058   5331  10057    281   4021  -1447       C
ATOM   1527  C   GLY A 544     -47.379 -16.582 -54.187  1.00 66.31           C
ANISOU 1527  C   GLY A 544     9243   5650  10300    166   3919  -1450       C
ATOM   1528  O   GLY A 544     -48.240 -16.115 -54.935  1.00 67.46           O
ANISOU 1528  O   GLY A 544     9407   5882  10343     64   3834  -1631       O
ATOM   1529  N   LYS A 545     -47.447 -16.464 -52.864  1.00 67.26           N
ANISOU 1529  N   LYS A 545     9292   5740  10524    190   3925  -1257       N
ATOM   1530  CA  LYS A 545     -48.519 -15.684 -52.246  1.00 65.24           C
ANISOU 1530  CA  LYS A 545     8967   5558  10263     97   3838  -1245       C
ATOM   1531  C   LYS A 545     -48.400 -14.236 -52.698  1.00 62.60           C
ANISOU 1531  C   LYS A 545     8583   5457   9745    118   3692  -1245       C
ATOM   1532  O   LYS A 545     -49.395 -13.591 -53.013  1.00 62.78           O
ANISOU 1532  O   LYS A 545     8587   5571   9695     20   3603  -1369       O
ATOM   1533  CB  LYS A 545     -48.483 -15.780 -50.720  1.00 65.78           C
ANISOU 1533  CB  LYS A 545     8982   5562  10450    149   3876  -1017       C
ATOM   1534  CG  LYS A 545     -48.895 -17.136 -50.166  1.00 72.62           C
ANISOU 1534  CG  LYS A 545     9901   6195  11496    106   4030  -1010       C
ATOM   1535  CD  LYS A 545     -50.275 -17.542 -50.656  1.00 77.02           C
ANISOU 1535  CD  LYS A 545    10473   6672  12120    -86   4051  -1239       C
ATOM   1536  CE  LYS A 545     -51.167 -17.979 -49.507  1.00 75.49           C
ANISOU 1536  CE  LYS A 545    10249   6350  12083   -159   4142  -1156       C
ATOM   1537  NZ  LYS A 545     -50.601 -19.133 -48.754  1.00 78.08           N
ANISOU 1537  NZ  LYS A 545    10641   6491  12535    -71   4303   -998       N
ATOM   1538  N   ASN A 546     -47.170 -13.734 -52.736  1.00 61.13           N
ANISOU 1538  N   ASN A 546     8371   5366   9488    247   3672  -1111       N
ATOM   1539  CA  ASN A 546     -46.894 -12.462 -53.383  1.00 54.86           C
ANISOU 1539  CA  ASN A 546     7549   4777   8517    269   3564  -1120       C
ATOM   1540  C   ASN A 546     -46.467 -12.714 -54.830  1.00 55.33           C
ANISOU 1540  C   ASN A 546     7700   4857   8465    282   3606  -1277       C
ATOM   1541  O   ASN A 546     -45.396 -13.270 -55.082  1.00 50.23           O
ANISOU 1541  O   ASN A 546     7076   4157   7851    373   3694  -1233       O
ATOM   1542  CB  ASN A 546     -45.830 -11.670 -52.617  1.00 53.05           C
ANISOU 1542  CB  ASN A 546     7225   4647   8283    386   3514   -897       C
ATOM   1543  CG  ASN A 546     -45.772 -10.206 -53.040  1.00 53.47           C
ANISOU 1543  CG  ASN A 546     7237   4904   8175    383   3396   -886       C
ATOM   1544  OD1 ASN A 546     -46.230  -9.849 -54.127  1.00 51.65           O
ANISOU 1544  OD1 ASN A 546     7068   4748   7809    330   3373  -1035       O
ATOM   1545  ND2 ASN A 546     -45.208  -9.352 -52.182  1.00 42.81           N
ANISOU 1545  ND2 ASN A 546     5789   3645   6832    447   3320   -712       N
ATOM   1546  N   PRO A 547     -47.318 -12.314 -55.787  1.00 57.85           N
ANISOU 1546  N   PRO A 547     8078   5259   8644    200   3541  -1466       N
ATOM   1547  CA  PRO A 547     -47.082 -12.538 -57.219  1.00 56.93           C
ANISOU 1547  CA  PRO A 547     8074   5171   8385    213   3570  -1637       C
ATOM   1548  C   PRO A 547     -46.070 -11.571 -57.832  1.00 57.42           C
ANISOU 1548  C   PRO A 547     8135   5393   8290    309   3560  -1549       C
ATOM   1549  O   PRO A 547     -45.674 -11.781 -58.977  1.00 62.22           O
ANISOU 1549  O   PRO A 547     8840   6021   8778    345   3611  -1659       O
ATOM   1550  CB  PRO A 547     -48.458 -12.287 -57.831  1.00 59.05           C
ANISOU 1550  CB  PRO A 547     8392   5496   8548     98   3469  -1856       C
ATOM   1551  CG  PRO A 547     -49.059 -11.232 -56.923  1.00 61.63           C
ANISOU 1551  CG  PRO A 547     8611   5925   8881     65   3365  -1744       C
ATOM   1552  CD  PRO A 547     -48.579 -11.588 -55.539  1.00 58.19           C
ANISOU 1552  CD  PRO A 547     8082   5383   8643    102   3428  -1530       C
ATOM   1553  N   ASP A 548     -45.670 -10.534 -57.096  1.00 57.06           N
ANISOU 1553  N   ASP A 548     7983   5451   8246    347   3500  -1361       N
ATOM   1554  CA  ASP A 548     -44.718  -9.540 -57.605  1.00 56.76           C
ANISOU 1554  CA  ASP A 548     7926   5554   8085    419   3497  -1268       C
ATOM   1555  C   ASP A 548     -43.346 -10.158 -57.851  1.00 64.45           C
ANISOU 1555  C   ASP A 548     8893   6466   9128    516   3623  -1207       C
ATOM   1556  O   ASP A 548     -42.910 -11.024 -57.091  1.00 68.69           O
ANISOU 1556  O   ASP A 548     9384   6878   9839    555   3680  -1137       O
ATOM   1557  CB  ASP A 548     -44.583  -8.367 -56.635  1.00 50.10           C
ANISOU 1557  CB  ASP A 548     6959   4813   7264    428   3401  -1086       C
ATOM   1558  CG  ASP A 548     -45.775  -7.439 -56.673  1.00 48.20           C
ANISOU 1558  CG  ASP A 548     6731   4680   6903    355   3281  -1143       C
ATOM   1559  OD1 ASP A 548     -46.811  -7.814 -57.272  1.00 49.82           O
ANISOU 1559  OD1 ASP A 548     7023   4868   7036    289   3261  -1329       O
ATOM   1560  OD2 ASP A 548     -45.675  -6.340 -56.089  1.00 43.34           O
ANISOU 1560  OD2 ASP A 548     6035   4163   6269    365   3200  -1012       O
ATOM   1561  N   PRO A 549     -42.660  -9.704 -58.913  1.00 63.04           N
ANISOU 1561  N   PRO A 549     8763   6377   8811    562   3675  -1230       N
ATOM   1562  CA  PRO A 549     -41.399 -10.315 -59.356  1.00 61.92           C
ANISOU 1562  CA  PRO A 549     8622   6184   8720    654   3811  -1206       C
ATOM   1563  C   PRO A 549     -40.343 -10.471 -58.262  1.00 57.42           C
ANISOU 1563  C   PRO A 549     7901   5567   8347    728   3836  -1024       C
ATOM   1564  O   PRO A 549     -39.646 -11.472 -58.264  1.00 64.14           O
ANISOU 1564  O   PRO A 549     8753   6313   9305    798   3940  -1028       O
ATOM   1565  CB  PRO A 549     -40.918  -9.365 -60.459  1.00 63.32           C
ANISOU 1565  CB  PRO A 549     8846   6502   8709    679   3843  -1213       C
ATOM   1566  CG  PRO A 549     -42.180  -8.781 -61.007  1.00 65.49           C
ANISOU 1566  CG  PRO A 549     9226   6863   8793    604   3742  -1332       C
ATOM   1567  CD  PRO A 549     -43.091  -8.619 -59.814  1.00 61.11           C
ANISOU 1567  CD  PRO A 549     8590   6286   8344    535   3618  -1287       C
ATOM   1568  N   TRP A 550     -40.233  -9.532 -57.332  1.00 55.85           N
ANISOU 1568  N   TRP A 550     7580   5447   8193    721   3737   -877       N
ATOM   1569  CA  TRP A 550     -39.211  -9.664 -56.294  1.00 54.17           C
ANISOU 1569  CA  TRP A 550     7224   5206   8152    804   3742   -721       C
ATOM   1570  C   TRP A 550     -39.508 -10.783 -55.298  1.00 59.39           C
ANISOU 1570  C   TRP A 550     7881   5720   8964    828   3747   -694       C
ATOM   1571  O   TRP A 550     -38.618 -11.219 -54.567  1.00 50.27           O
ANISOU 1571  O   TRP A 550     6636   4518   7944    924   3774   -587       O
ATOM   1572  CB  TRP A 550     -39.007  -8.348 -55.542  1.00 48.77           C
ANISOU 1572  CB  TRP A 550     6413   4646   7472    793   3625   -586       C
ATOM   1573  CG  TRP A 550     -40.159  -7.952 -54.649  1.00 45.58           C
ANISOU 1573  CG  TRP A 550     6003   4254   7059    726   3493   -560       C
ATOM   1574  CD1 TRP A 550     -41.221  -7.163 -54.988  1.00 44.40           C
ANISOU 1574  CD1 TRP A 550     5914   4183   6774    638   3415   -620       C
ATOM   1575  CD2 TRP A 550     -40.346  -8.308 -53.269  1.00 44.72           C
ANISOU 1575  CD2 TRP A 550     5828   4086   7079    753   3432   -463       C
ATOM   1576  NE1 TRP A 550     -42.064  -7.013 -53.905  1.00 43.44           N
ANISOU 1576  NE1 TRP A 550     5755   4051   6699    603   3312   -573       N
ATOM   1577  CE2 TRP A 550     -41.549  -7.705 -52.839  1.00 43.02           C
ANISOU 1577  CE2 TRP A 550     5631   3912   6802    671   3325   -473       C
ATOM   1578  CE3 TRP A 550     -39.621  -9.081 -52.360  1.00 45.42           C
ANISOU 1578  CE3 TRP A 550     5848   4092   7317    850   3460   -368       C
ATOM   1579  CZ2 TRP A 550     -42.040  -7.856 -51.544  1.00 45.72           C
ANISOU 1579  CZ2 TRP A 550     5930   4213   7228    677   3258   -389       C
ATOM   1580  CZ3 TRP A 550     -40.104  -9.221 -51.074  1.00 49.38           C
ANISOU 1580  CZ3 TRP A 550     6317   4556   7889    863   3388   -278       C
ATOM   1581  CH2 TRP A 550     -41.307  -8.613 -50.675  1.00 47.86           C
ANISOU 1581  CH2 TRP A 550     6149   4403   7632    775   3293   -288       C
ATOM   1582  N   ALA A 551     -40.757 -11.241 -55.258  1.00 60.71           N
ANISOU 1582  N   ALA A 551     8142   5815   9111    744   3724   -790       N
ATOM   1583  CA  ALA A 551     -41.166 -12.191 -54.221  1.00 58.71           C
ANISOU 1583  CA  ALA A 551     7888   5416   9002    750   3735   -746       C
ATOM   1584  C   ALA A 551     -41.723 -13.510 -54.754  1.00 58.43           C
ANISOU 1584  C   ALA A 551     7981   5215   9005    712   3840   -897       C
ATOM   1585  O   ALA A 551     -41.760 -14.505 -54.031  1.00 53.99           O
ANISOU 1585  O   ALA A 551     7430   4502   8581    741   3899   -852       O
ATOM   1586  CB  ALA A 551     -42.161 -11.544 -53.274  1.00 55.73           C
ANISOU 1586  CB  ALA A 551     7471   5080   8624    680   3616   -687       C
ATOM   1587  N   LYS A 552     -42.148 -13.499 -56.015  1.00 65.27           N
ANISOU 1587  N   LYS A 552     8948   6109   9741    652   3862  -1077       N
ATOM   1588  CA  LYS A 552     -42.770 -14.650 -56.674  1.00 72.18           C
ANISOU 1588  CA  LYS A 552     9952   6841  10631    599   3941  -1263       C
ATOM   1589  C   LYS A 552     -42.030 -15.968 -56.424  1.00 75.57           C
ANISOU 1589  C   LYS A 552    10405   7094  11215    687   4074  -1232       C
ATOM   1590  O   LYS A 552     -42.657 -17.015 -56.240  1.00 77.03           O
ANISOU 1590  O   LYS A 552    10658   7110  11498    637   4130  -1310       O
ATOM   1591  CB  LYS A 552     -42.876 -14.378 -58.180  1.00 75.58           C
ANISOU 1591  CB  LYS A 552    10487   7359  10870    577   3949  -1445       C
ATOM   1592  CG  LYS A 552     -43.873 -15.243 -58.935  1.00 77.59           C
ANISOU 1592  CG  LYS A 552    10876   7513  11091    489   3966  -1686       C
ATOM   1593  CD  LYS A 552     -44.248 -14.577 -60.257  1.00 79.25           C
ANISOU 1593  CD  LYS A 552    11183   7868  11060    463   3910  -1852       C
ATOM   1594  CE  LYS A 552     -44.733 -15.577 -61.298  1.00 81.58           C
ANISOU 1594  CE  LYS A 552    11630   8069  11299    429   3948  -2108       C
ATOM   1595  NZ  LYS A 552     -43.612 -16.347 -61.909  1.00 84.54           N
ANISOU 1595  NZ  LYS A 552    12066   8371  11685    540   4092  -2122       N
ATOM   1596  N   ASN A 553     -40.700 -15.908 -56.398  1.00 75.76           N
ANISOU 1596  N   ASN A 553    10363   7154  11267    816   4126  -1119       N
ATOM   1597  CA  ASN A 553     -39.886 -17.107 -56.200  1.00 74.99           C
ANISOU 1597  CA  ASN A 553    10282   6904  11308    925   4250  -1085       C
ATOM   1598  C   ASN A 553     -39.135 -17.180 -54.862  1.00 70.17           C
ANISOU 1598  C   ASN A 553     9550   6272  10838   1037   4236   -867       C
ATOM   1599  O   ASN A 553     -38.140 -17.888 -54.742  1.00 75.94           O
ANISOU 1599  O   ASN A 553    10259   6931  11662   1167   4323   -813       O
ATOM   1600  CB  ASN A 553     -38.912 -17.289 -57.369  1.00 76.06           C
ANISOU 1600  CB  ASN A 553    10454   7070  11377   1008   4350  -1167       C
ATOM   1601  CG  ASN A 553     -39.625 -17.477 -58.697  1.00 74.14           C
ANISOU 1601  CG  ASN A 553    10360   6823  10986    924   4375  -1399       C
ATOM   1602  OD1 ASN A 553     -40.596 -18.233 -58.794  1.00 71.36           O
ANISOU 1602  OD1 ASN A 553    10108   6345  10660    839   4380  -1534       O
ATOM   1603  ND2 ASN A 553     -39.149 -16.781 -59.727  1.00 71.98           N
ANISOU 1603  ND2 ASN A 553    10104   6690  10556    950   4389  -1450       N
ATOM   1604  N   LEU A 554     -39.605 -16.450 -53.859  1.00 62.67           N
ANISOU 1604  N   LEU A 554     8525   5390   9898   1000   4122   -749       N
ATOM   1605  CA  LEU A 554     -39.058 -16.586 -52.514  1.00 60.70           C
ANISOU 1605  CA  LEU A 554     8183   5116   9764   1109   4095   -555       C
ATOM   1606  C   LEU A 554     -39.748 -17.759 -51.842  1.00 62.01           C
ANISOU 1606  C   LEU A 554     8439   5081  10041   1095   4167   -542       C
ATOM   1607  O   LEU A 554     -40.859 -18.125 -52.230  1.00 65.08           O
ANISOU 1607  O   LEU A 554     8926   5384  10418    962   4197   -674       O
ATOM   1608  CB  LEU A 554     -39.320 -15.326 -51.694  1.00 53.38           C
ANISOU 1608  CB  LEU A 554     7152   4341   8789   1079   3944   -441       C
ATOM   1609  CG  LEU A 554     -38.669 -14.019 -52.135  1.00 54.33           C
ANISOU 1609  CG  LEU A 554     7169   4659   8815   1085   3863   -425       C
ATOM   1610  CD1 LEU A 554     -39.174 -12.868 -51.282  1.00 49.74           C
ANISOU 1610  CD1 LEU A 554     6511   4199   8190   1037   3714   -333       C
ATOM   1611  CD2 LEU A 554     -37.145 -14.128 -52.066  1.00 55.09           C
ANISOU 1611  CD2 LEU A 554     7156   4791   8983   1235   3902   -344       C
ATOM   1612  N   ASN A 555     -39.109 -18.353 -50.838  1.00 58.67           N
ANISOU 1612  N   ASN A 555     7982   4583   9726   1231   4195   -389       N
ATOM   1613  CA  ASN A 555     -39.799 -19.375 -50.050  1.00 67.57           C
ANISOU 1613  CA  ASN A 555     9199   5522  10954   1221   4269   -342       C
ATOM   1614  C   ASN A 555     -39.461 -19.410 -48.560  1.00 67.06           C
ANISOU 1614  C   ASN A 555     9078   5455  10946   1350   4226   -124       C
ATOM   1615  O   ASN A 555     -38.348 -19.079 -48.139  1.00 64.05           O
ANISOU 1615  O   ASN A 555     8592   5173  10569   1503   4166    -13       O
ATOM   1616  CB  ASN A 555     -39.692 -20.771 -50.681  1.00 73.57           C
ANISOU 1616  CB  ASN A 555    10078   6079  11796   1240   4428   -449       C
ATOM   1617  CG  ASN A 555     -38.271 -21.191 -50.915  1.00 70.22           C
ANISOU 1617  CG  ASN A 555     9615   5654  11413   1422   4480   -408       C
ATOM   1618  OD1 ASN A 555     -37.548 -21.510 -49.975  1.00 71.66           O
ANISOU 1618  OD1 ASN A 555     9748   5812  11668   1580   4478   -246       O
ATOM   1619  ND2 ASN A 555     -37.859 -21.203 -52.176  1.00 64.47           N
ANISOU 1619  ND2 ASN A 555     8908   4956  10633   1410   4529   -558       N
ATOM   1620  N   GLU A 556     -40.452 -19.838 -47.787  1.00 64.99           N
ANISOU 1620  N   GLU A 556     8888   5078  10726   1288   4263    -75       N
ATOM   1621  CA  GLU A 556     -40.462 -19.698 -46.338  1.00 62.26           C
ANISOU 1621  CA  GLU A 556     8513   4748  10393   1382   4213    126       C
ATOM   1622  C   GLU A 556     -39.258 -20.321 -45.643  1.00 59.99           C
ANISOU 1622  C   GLU A 556     8205   4425  10163   1610   4229    274       C
ATOM   1623  O   GLU A 556     -38.775 -19.795 -44.642  1.00 59.17           O
ANISOU 1623  O   GLU A 556     8022   4431  10027   1735   4120    425       O
ATOM   1624  CB  GLU A 556     -41.754 -20.299 -45.782  1.00 62.49           C
ANISOU 1624  CB  GLU A 556     8647   4623  10474   1271   4305    136       C
ATOM   1625  CG  GLU A 556     -41.984 -20.013 -44.315  1.00 64.97           C
ANISOU 1625  CG  GLU A 556     8947   4970  10768   1348   4257    335       C
ATOM   1626  CD  GLU A 556     -43.439 -20.164 -43.924  1.00 67.85           C
ANISOU 1626  CD  GLU A 556     9379   5241  11159   1190   4331    316       C
ATOM   1627  OE1 GLU A 556     -43.721 -20.277 -42.714  1.00 67.27           O
ANISOU 1627  OE1 GLU A 556     9336   5140  11084   1257   4352    480       O
ATOM   1628  OE2 GLU A 556     -44.301 -20.161 -44.829  1.00 68.37           O
ANISOU 1628  OE2 GLU A 556     9462   5269  11245   1004   4368    131       O
ATOM   1629  N   LYS A 557     -38.790 -21.442 -46.181  1.00 62.33           N
ANISOU 1629  N   LYS A 557     8573   4569  10540   1671   4357    219       N
ATOM   1630  CA  LYS A 557     -37.698 -22.204 -45.586  1.00 68.90           C
ANISOU 1630  CA  LYS A 557     9400   5339  11439   1897   4388    344       C
ATOM   1631  C   LYS A 557     -36.402 -21.397 -45.418  1.00 67.26           C
ANISOU 1631  C   LYS A 557     9023   5333  11201   2053   4250    409       C
ATOM   1632  O   LYS A 557     -35.591 -21.696 -44.539  1.00 65.57           O
ANISOU 1632  O   LYS A 557     8768   5126  11021   2254   4209    547       O
ATOM   1633  CB  LYS A 557     -37.414 -23.438 -46.443  1.00 73.96           C
ANISOU 1633  CB  LYS A 557    10142   5792  12169   1919   4548    235       C
ATOM   1634  CG  LYS A 557     -38.599 -23.905 -47.291  1.00 79.23           C
ANISOU 1634  CG  LYS A 557    10932   6319  12854   1703   4660     58       C
ATOM   1635  CD  LYS A 557     -38.205 -25.113 -48.149  1.00 83.45           C
ANISOU 1635  CD  LYS A 557    11564   6670  13472   1743   4809    -61       C
ATOM   1636  CE  LYS A 557     -39.316 -25.535 -49.103  1.00 83.03           C
ANISOU 1636  CE  LYS A 557    11622   6493  13432   1528   4897   -274       C
ATOM   1637  NZ  LYS A 557     -38.902 -26.676 -49.975  1.00 84.98           N
ANISOU 1637  NZ  LYS A 557    11971   6567  13752   1572   5033   -406       N
ATOM   1638  N   ASP A 558     -36.214 -20.379 -46.257  1.00 67.26           N
ANISOU 1638  N   ASP A 558     8921   5496  11139   1963   4178    304       N
ATOM   1639  CA  ASP A 558     -34.953 -19.631 -46.287  1.00 68.38           C
ANISOU 1639  CA  ASP A 558     8887   5821  11274   2086   4074    333       C
ATOM   1640  C   ASP A 558     -34.833 -18.561 -45.208  1.00 70.19           C
ANISOU 1640  C   ASP A 558     8994   6224  11451   2133   3896    456       C
ATOM   1641  O   ASP A 558     -33.803 -17.893 -45.110  1.00 71.65           O
ANISOU 1641  O   ASP A 558     9014   6565  11644   2231   3796    479       O
ATOM   1642  CB  ASP A 558     -34.737 -18.977 -47.654  1.00 61.45           C
ANISOU 1642  CB  ASP A 558     7957   5043  10350   1974   4089    177       C
ATOM   1643  CG  ASP A 558     -34.612 -19.985 -48.769  1.00 67.86           C
ANISOU 1643  CG  ASP A 558     8872   5708  11202   1963   4253     45       C
ATOM   1644  OD1 ASP A 558     -34.223 -21.146 -48.492  1.00 71.29           O
ANISOU 1644  OD1 ASP A 558     9368   5989  11729   2093   4346     84       O
ATOM   1645  OD2 ASP A 558     -34.900 -19.611 -49.926  1.00 63.03           O
ANISOU 1645  OD2 ASP A 558     8289   5136  10522   1833   4288   -101       O
ATOM   1646  N   TYR A 559     -35.875 -18.393 -44.401  1.00 59.07           N
ANISOU 1646  N   TYR A 559     7661   4790   9994   2064   3860    527       N
ATOM   1647  CA  TYR A 559     -35.859 -17.349 -43.378  1.00 58.32           C
ANISOU 1647  CA  TYR A 559     7466   4858   9834   2105   3690    632       C
ATOM   1648  C   TYR A 559     -36.108 -17.931 -41.996  1.00 60.50           C
ANISOU 1648  C   TYR A 559     7823   5057  10108   2234   3678    796       C
ATOM   1649  O   TYR A 559     -36.781 -18.950 -41.851  1.00 59.51           O
ANISOU 1649  O   TYR A 559     7854   4744  10015   2211   3814    821       O
ATOM   1650  CB  TYR A 559     -36.861 -16.233 -43.726  1.00 54.64           C
ANISOU 1650  CB  TYR A 559     6994   4488   9277   1901   3630    559       C
ATOM   1651  CG  TYR A 559     -36.692 -15.789 -45.156  1.00 56.53           C
ANISOU 1651  CG  TYR A 559     7195   4782   9500   1779   3662    401       C
ATOM   1652  CD1 TYR A 559     -35.697 -14.886 -45.506  1.00 57.86           C
ANISOU 1652  CD1 TYR A 559     7205   5120   9659   1817   3577    379       C
ATOM   1653  CD2 TYR A 559     -37.484 -16.318 -46.170  1.00 56.73           C
ANISOU 1653  CD2 TYR A 559     7345   4688   9522   1635   3785    268       C
ATOM   1654  CE1 TYR A 559     -35.510 -14.502 -46.824  1.00 59.79           C
ANISOU 1654  CE1 TYR A 559     7431   5410   9875   1717   3626    247       C
ATOM   1655  CE2 TYR A 559     -37.305 -15.937 -47.496  1.00 57.02           C
ANISOU 1655  CE2 TYR A 559     7366   4780   9519   1544   3814    123       C
ATOM   1656  CZ  TYR A 559     -36.314 -15.031 -47.815  1.00 60.02           C
ANISOU 1656  CZ  TYR A 559     7603   5327   9876   1590   3741    123       C
ATOM   1657  OH  TYR A 559     -36.122 -14.650 -49.127  1.00 62.01           O
ANISOU 1657  OH  TYR A 559     7853   5633  10075   1509   3786     -6       O
ATOM   1658  N   GLU A 560     -35.537 -17.287 -40.985  1.00 60.17           N
ANISOU 1658  N   GLU A 560     7676   5159  10027   2373   3516    902       N
ATOM   1659  CA  GLU A 560     -35.690 -17.733 -39.611  1.00 61.35           C
ANISOU 1659  CA  GLU A 560     7905   5262  10143   2521   3483   1066       C
ATOM   1660  C   GLU A 560     -36.016 -16.558 -38.715  1.00 57.18           C
ANISOU 1660  C   GLU A 560     7314   4901   9509   2516   3313   1128       C
ATOM   1661  O   GLU A 560     -35.939 -15.405 -39.134  1.00 55.24           O
ANISOU 1661  O   GLU A 560     6943   4812   9235   2420   3211   1047       O
ATOM   1662  CB  GLU A 560     -34.405 -18.385 -39.102  1.00 68.30           C
ANISOU 1662  CB  GLU A 560     8730   6138  11081   2779   3436   1145       C
ATOM   1663  CG  GLU A 560     -33.935 -19.587 -39.887  1.00 74.25           C
ANISOU 1663  CG  GLU A 560     9541   6726  11944   2825   3598   1093       C
ATOM   1664  CD  GLU A 560     -32.605 -20.090 -39.387  1.00 79.95           C
ANISOU 1664  CD  GLU A 560    10179   7469  12727   3094   3527   1163       C
ATOM   1665  OE1 GLU A 560     -32.601 -20.993 -38.525  1.00 82.29           O
ANISOU 1665  OE1 GLU A 560    10597   7646  13023   3251   3558   1292       O
ATOM   1666  OE2 GLU A 560     -31.567 -19.568 -39.843  1.00 82.40           O
ANISOU 1666  OE2 GLU A 560    10300   7919  13089   3150   3443   1089       O
ATOM   1667  N   LEU A 561     -36.354 -16.868 -37.469  1.00 57.95           N
ANISOU 1667  N   LEU A 561     7511   4964   9543   2631   3289   1275       N
ATOM   1668  CA  LEU A 561     -36.715 -15.863 -36.484  1.00 64.19           C
ANISOU 1668  CA  LEU A 561     8272   5899  10217   2650   3136   1345       C
ATOM   1669  C   LEU A 561     -35.618 -15.700 -35.452  1.00 62.16           C
ANISOU 1669  C   LEU A 561     7928   5763   9929   2901   2951   1440       C
ATOM   1670  O   LEU A 561     -35.026 -16.675 -35.001  1.00 62.84           O
ANISOU 1670  O   LEU A 561     8069   5763  10045   3085   2977   1525       O
ATOM   1671  CB  LEU A 561     -38.006 -16.264 -35.781  1.00 56.37           C
ANISOU 1671  CB  LEU A 561     7470   4793   9157   2592   3248   1440       C
ATOM   1672  CG  LEU A 561     -39.196 -16.411 -36.717  1.00 56.24           C
ANISOU 1672  CG  LEU A 561     7527   4659   9183   2340   3416   1334       C
ATOM   1673  CD1 LEU A 561     -40.454 -16.691 -35.923  1.00 55.08           C
ANISOU 1673  CD1 LEU A 561     7532   4417   8980   2286   3523   1426       C
ATOM   1674  CD2 LEU A 561     -39.332 -15.149 -37.557  1.00 52.47           C
ANISOU 1674  CD2 LEU A 561     6915   4331   8688   2179   3317   1193       C
ATOM   1675  N   LEU A 562     -35.354 -14.462 -35.070  1.00 56.62           N
ANISOU 1675  N   LEU A 562     7087   5257   9168   2912   2757   1418       N
ATOM   1676  CA  LEU A 562     -34.436 -14.213 -33.980  1.00 62.17           C
ANISOU 1676  CA  LEU A 562     7707   6086   9830   3144   2552   1495       C
ATOM   1677  C   LEU A 562     -35.187 -14.339 -32.666  1.00 68.54           C
ANISOU 1677  C   LEU A 562     8685   6872  10486   3231   2525   1644       C
ATOM   1678  O   LEU A 562     -36.143 -13.605 -32.419  1.00 69.06           O
ANISOU 1678  O   LEU A 562     8799   6984  10456   3110   2517   1646       O
ATOM   1679  CB  LEU A 562     -33.842 -12.821 -34.099  1.00 63.19           C
ANISOU 1679  CB  LEU A 562     7611   6429   9970   3114   2355   1396       C
ATOM   1680  CG  LEU A 562     -32.326 -12.812 -34.132  1.00 68.00           C
ANISOU 1680  CG  LEU A 562     8014   7135  10688   3282   2222   1352       C
ATOM   1681  CD1 LEU A 562     -31.814 -11.382 -34.124  1.00 66.38           C
ANISOU 1681  CD1 LEU A 562     7584   7138  10500   3241   2030   1257       C
ATOM   1682  CD2 LEU A 562     -31.801 -13.609 -32.947  1.00 76.43           C
ANISOU 1682  CD2 LEU A 562     9147   8176  11716   3553   2128   1483       C
ATOM   1683  N   CYS A 563     -34.759 -15.277 -31.827  1.00 68.90           N
ANISOU 1683  N   CYS A 563     8829   6847  10502   3448   2519   1771       N
ATOM   1684  CA  CYS A 563     -35.355 -15.437 -30.510  1.00 64.22           C
ANISOU 1684  CA  CYS A 563     8412   6244   9745   3559   2495   1926       C
ATOM   1685  C   CYS A 563     -34.702 -14.510 -29.492  1.00 66.15           C
ANISOU 1685  C   CYS A 563     8551   6698   9884   3726   2209   1948       C
ATOM   1686  O   CYS A 563     -33.565 -14.064 -29.668  1.00 65.88           O
ANISOU 1686  O   CYS A 563     8307   6790   9934   3813   2029   1866       O
ATOM   1687  CB  CYS A 563     -35.254 -16.887 -30.051  1.00 66.88           C
ANISOU 1687  CB  CYS A 563     8929   6400  10082   3717   2632   2061       C
ATOM   1688  SG  CYS A 563     -36.152 -18.044 -31.105  1.00 76.81           S
ANISOU 1688  SG  CYS A 563    10335   7389  11462   3517   2975   2034       S
ATOM   1689  N   LEU A 564     -35.432 -14.215 -28.425  1.00 68.43           N
ANISOU 1689  N   LEU A 564     8983   7026   9993   3768   2171   2051       N
ATOM   1690  CA  LEU A 564     -34.919 -13.349 -27.372  1.00 71.16           C
ANISOU 1690  CA  LEU A 564     9260   7567  10212   3928   1894   2071       C
ATOM   1691  C   LEU A 564     -33.708 -13.944 -26.640  1.00 75.44           C
ANISOU 1691  C   LEU A 564     9771   8142  10750   4213   1732   2139       C
ATOM   1692  O   LEU A 564     -32.930 -13.213 -26.026  1.00 74.25           O
ANISOU 1692  O   LEU A 564     9483   8169  10561   4345   1462   2105       O
ATOM   1693  CB  LEU A 564     -36.033 -13.005 -26.386  1.00 70.85           C
ANISOU 1693  CB  LEU A 564     9412   7550   9959   3917   1918   2171       C
ATOM   1694  CG  LEU A 564     -37.042 -11.989 -26.925  1.00 67.15           C
ANISOU 1694  CG  LEU A 564     8907   7123   9483   3672   1971   2078       C
ATOM   1695  CD1 LEU A 564     -38.242 -11.862 -25.995  1.00 70.35           C
ANISOU 1695  CD1 LEU A 564     9523   7516   9691   3663   2053   2186       C
ATOM   1696  CD2 LEU A 564     -36.366 -10.639 -27.138  1.00 61.48           C
ANISOU 1696  CD2 LEU A 564     7951   6606   8804   3646   1721   1938       C
ATOM   1697  N   ASP A 565     -33.543 -15.263 -26.722  1.00 76.94           N
ANISOU 1697  N   ASP A 565    10083   8161  10991   4306   1891   2228       N
ATOM   1698  CA  ASP A 565     -32.456 -15.937 -26.010  1.00 83.52           C
ANISOU 1698  CA  ASP A 565    10910   9006  11818   4592   1753   2308       C
ATOM   1699  C   ASP A 565     -31.257 -16.304 -26.896  1.00 85.64           C
ANISOU 1699  C   ASP A 565    10967   9261  12312   4645   1719   2204       C
ATOM   1700  O   ASP A 565     -30.293 -16.913 -26.429  1.00 88.90           O
ANISOU 1700  O   ASP A 565    11349   9676  12755   4885   1608   2257       O
ATOM   1701  CB  ASP A 565     -32.981 -17.180 -25.281  1.00 87.45           C
ANISOU 1701  CB  ASP A 565    11700   9327  12199   4715   1933   2499       C
ATOM   1702  CG  ASP A 565     -33.692 -18.150 -26.212  1.00 88.23           C
ANISOU 1702  CG  ASP A 565    11918   9188  12415   4547   2263   2506       C
ATOM   1703  OD1 ASP A 565     -33.565 -18.003 -27.445  1.00 89.01           O
ANISOU 1703  OD1 ASP A 565    11870   9261  12689   4377   2332   2363       O
ATOM   1704  OD2 ASP A 565     -34.373 -19.071 -25.711  1.00 86.81           O
ANISOU 1704  OD2 ASP A 565    11982   8847  12155   4585   2458   2648       O
ATOM   1705  N   GLY A 566     -31.314 -15.938 -28.172  1.00 80.78           N
ANISOU 1705  N   GLY A 566    10208   8635  11850   4430   1818   2057       N
ATOM   1706  CA  GLY A 566     -30.229 -16.251 -29.083  1.00 75.33           C
ANISOU 1706  CA  GLY A 566     9320   7936  11365   4466   1816   1950       C
ATOM   1707  C   GLY A 566     -30.590 -17.334 -30.080  1.00 73.93           C
ANISOU 1707  C   GLY A 566     9259   7540  11290   4361   2109   1947       C
ATOM   1708  O   GLY A 566     -30.015 -17.401 -31.169  1.00 73.68           O
ANISOU 1708  O   GLY A 566     9078   7499  11420   4294   2170   1823       O
ATOM   1709  N   THR A 567     -31.545 -18.182 -29.702  1.00 75.11           N
ANISOU 1709  N   THR A 567     9677   7516  11345   4346   2296   2078       N
ATOM   1710  CA  THR A 567     -32.057 -19.237 -30.572  1.00 78.92           C
ANISOU 1710  CA  THR A 567    10295   7771  11921   4228   2582   2075       C
ATOM   1711  C   THR A 567     -32.549 -18.662 -31.890  1.00 79.02           C
ANISOU 1711  C   THR A 567    10214   7788  12022   3941   2693   1912       C
ATOM   1712  O   THR A 567     -32.822 -17.464 -31.995  1.00 74.95           O
ANISOU 1712  O   THR A 567     9587   7426  11462   3811   2585   1836       O
ATOM   1713  CB  THR A 567     -33.253 -19.954 -29.919  1.00 82.31           C
ANISOU 1713  CB  THR A 567    11011   8033  12231   4196   2770   2224       C
ATOM   1714  OG1 THR A 567     -33.044 -20.047 -28.506  1.00 86.37           O
ANISOU 1714  OG1 THR A 567    11623   8604  12588   4431   2632   2381       O
ATOM   1715  CG2 THR A 567     -33.450 -21.350 -30.501  1.00 84.82           C
ANISOU 1715  CG2 THR A 567    11476   8094  12658   4176   3032   2251       C
ATOM   1716  N   ARG A 568     -32.664 -19.519 -32.898  1.00 79.79           N
ANISOU 1716  N   ARG A 568    10365   7714  12238   3847   2905   1857       N
ATOM   1717  CA  ARG A 568     -33.225 -19.112 -34.177  1.00 75.83           C
ANISOU 1717  CA  ARG A 568     9814   7194  11803   3575   3027   1706       C
ATOM   1718  C   ARG A 568     -34.202 -20.161 -34.709  1.00 77.28           C
ANISOU 1718  C   ARG A 568    10201   7135  12028   3435   3296   1712       C
ATOM   1719  O   ARG A 568     -33.901 -20.874 -35.664  1.00 80.38           O
ANISOU 1719  O   ARG A 568    10594   7408  12538   3401   3428   1630       O
ATOM   1720  CB  ARG A 568     -32.109 -18.830 -35.187  1.00 72.43           C
ANISOU 1720  CB  ARG A 568     9166   6852  11504   3582   2976   1562       C
ATOM   1721  CG  ARG A 568     -31.247 -17.628 -34.823  1.00 66.98           C
ANISOU 1721  CG  ARG A 568     8239   6407  10801   3662   2722   1519       C
ATOM   1722  CD  ARG A 568     -29.987 -17.545 -35.672  1.00 72.46           C
ANISOU 1722  CD  ARG A 568     8713   7176  11642   3715   2690   1397       C
ATOM   1723  NE  ARG A 568     -30.253 -17.781 -37.091  1.00 73.62           N
ANISOU 1723  NE  ARG A 568     8879   7229  11863   3520   2892   1279       N
ATOM   1724  CZ  ARG A 568     -29.573 -17.227 -38.094  1.00 70.92           C
ANISOU 1724  CZ  ARG A 568     8354   6986  11607   3446   2894   1144       C
ATOM   1725  NH1 ARG A 568     -28.581 -16.380 -37.853  1.00 68.73           N
ANISOU 1725  NH1 ARG A 568     7837   6903  11373   3534   2714   1102       N
ATOM   1726  NH2 ARG A 568     -29.894 -17.515 -39.347  1.00 70.44           N
ANISOU 1726  NH2 ARG A 568     8349   6830  11586   3279   3080   1045       N
ATOM   1727  N   LYS A 569     -35.372 -20.253 -34.082  1.00 72.85           N
ANISOU 1727  N   LYS A 569     9807   6501  11374   3354   3382   1800       N
ATOM   1728  CA  LYS A 569     -36.412 -21.179 -34.527  1.00 70.29           C
ANISOU 1728  CA  LYS A 569     9657   5948  11100   3197   3638   1792       C
ATOM   1729  C   LYS A 569     -36.888 -20.785 -35.928  1.00 68.20           C
ANISOU 1729  C   LYS A 569     9320   5677  10916   2936   3715   1601       C
ATOM   1730  O   LYS A 569     -36.604 -19.677 -36.385  1.00 63.27           O
ANISOU 1730  O   LYS A 569     8534   5233  10275   2866   3577   1504       O
ATOM   1731  CB  LYS A 569     -37.574 -21.193 -33.529  1.00 67.39           C
ANISOU 1731  CB  LYS A 569     9452   5533  10621   3156   3708   1916       C
ATOM   1732  N   PRO A 570     -37.582 -21.699 -36.634  1.00 69.75           N
ANISOU 1732  N   PRO A 570     9636   5665  11200   2794   3933   1538       N
ATOM   1733  CA  PRO A 570     -38.094 -21.317 -37.955  1.00 67.21           C
ANISOU 1733  CA  PRO A 570     9259   5344  10935   2550   3990   1347       C
ATOM   1734  C   PRO A 570     -39.287 -20.395 -37.835  1.00 64.05           C
ANISOU 1734  C   PRO A 570     8856   5020  10461   2358   3966   1317       C
ATOM   1735  O   PRO A 570     -39.790 -20.175 -36.735  1.00 61.85           O
ANISOU 1735  O   PRO A 570     8635   4769  10096   2405   3940   1446       O
ATOM   1736  CB  PRO A 570     -38.534 -22.646 -38.568  1.00 72.11           C
ANISOU 1736  CB  PRO A 570    10021   5708  11667   2474   4219   1292       C
ATOM   1737  CG  PRO A 570     -38.787 -23.527 -37.418  1.00 76.57           C
ANISOU 1737  CG  PRO A 570    10741   6134  12218   2603   4311   1468       C
ATOM   1738  CD  PRO A 570     -37.786 -23.131 -36.368  1.00 76.86           C
ANISOU 1738  CD  PRO A 570    10717   6324  12164   2861   4125   1618       C
ATOM   1739  N   VAL A 571     -39.729 -19.877 -38.974  1.00 66.04           N
ANISOU 1739  N   VAL A 571     9047   5304  10741   2152   3978   1146       N
ATOM   1740  CA  VAL A 571     -40.776 -18.863 -39.039  1.00 61.56           C
ANISOU 1740  CA  VAL A 571     8449   4830  10111   1970   3931   1089       C
ATOM   1741  C   VAL A 571     -42.069 -19.264 -38.321  1.00 62.70           C
ANISOU 1741  C   VAL A 571     8722   4853  10249   1886   4060   1158       C
ATOM   1742  O   VAL A 571     -42.658 -18.466 -37.588  1.00 56.06           O
ANISOU 1742  O   VAL A 571     7868   4114   9320   1867   3990   1221       O
ATOM   1743  CB  VAL A 571     -41.065 -18.497 -40.511  1.00 57.48           C
ANISOU 1743  CB  VAL A 571     7877   4330   9632   1770   3947    880       C
ATOM   1744  CG1 VAL A 571     -42.422 -17.859 -40.658  1.00 58.33           C
ANISOU 1744  CG1 VAL A 571     7997   4457   9707   1564   3956    805       C
ATOM   1745  CG2 VAL A 571     -39.968 -17.589 -41.047  1.00 54.83           C
ANISOU 1745  CG2 VAL A 571     7387   4182   9262   1827   3792    827       C
ATOM   1746  N   GLU A 572     -42.492 -20.508 -38.507  1.00 64.44           N
ANISOU 1746  N   GLU A 572     9063   4854  10567   1843   4257   1143       N
ATOM   1747  CA  GLU A 572     -43.774 -20.956 -37.973  1.00 68.87           C
ANISOU 1747  CA  GLU A 572     9731   5283  11153   1733   4414   1179       C
ATOM   1748  C   GLU A 572     -43.797 -21.137 -36.453  1.00 67.22           C
ANISOU 1748  C   GLU A 572     9609   5072  10859   1906   4427   1400       C
ATOM   1749  O   GLU A 572     -44.849 -21.394 -35.869  1.00 68.86           O
ANISOU 1749  O   GLU A 572     9898   5193  11071   1831   4559   1448       O
ATOM   1750  CB  GLU A 572     -44.228 -22.234 -38.682  1.00 78.12           C
ANISOU 1750  CB  GLU A 572    10997   6215  12471   1620   4624   1073       C
ATOM   1751  CG  GLU A 572     -44.663 -21.997 -40.124  1.00 83.56           C
ANISOU 1751  CG  GLU A 572    11623   6902  13224   1403   4625    830       C
ATOM   1752  CD  GLU A 572     -45.902 -21.113 -40.230  1.00 83.90           C
ANISOU 1752  CD  GLU A 572    11609   7025  13243   1204   4595    739       C
ATOM   1753  OE1 GLU A 572     -46.839 -21.294 -39.416  1.00 91.44           O
ANISOU 1753  OE1 GLU A 572    12614   7915  14215   1159   4695    811       O
ATOM   1754  OE2 GLU A 572     -45.941 -20.240 -41.125  1.00 73.70           O
ANISOU 1754  OE2 GLU A 572    10225   5861  11916   1101   4477    595       O
ATOM   1755  N   GLU A 573     -42.647 -20.984 -35.811  1.00 66.18           N
ANISOU 1755  N   GLU A 573     9456   5042  10645   2139   4288   1526       N
ATOM   1756  CA  GLU A 573     -42.583 -21.134 -34.364  1.00 68.15           C
ANISOU 1756  CA  GLU A 573     9801   5307  10786   2328   4276   1733       C
ATOM   1757  C   GLU A 573     -42.557 -19.773 -33.680  1.00 67.09           C
ANISOU 1757  C   GLU A 573     9582   5409  10502   2377   4071   1782       C
ATOM   1758  O   GLU A 573     -41.974 -19.608 -32.611  1.00 65.79           O
ANISOU 1758  O   GLU A 573     9444   5335  10217   2589   3955   1927       O
ATOM   1759  CB  GLU A 573     -41.369 -21.974 -33.978  1.00 73.43           C
ANISOU 1759  CB  GLU A 573    10519   5921  11459   2577   4252   1842       C
ATOM   1760  CG  GLU A 573     -41.223 -23.217 -34.843  1.00 81.80           C
ANISOU 1760  CG  GLU A 573    11642   6761  12676   2532   4430   1764       C
ATOM   1761  CD  GLU A 573     -40.246 -24.226 -34.274  1.00 93.02           C
ANISOU 1761  CD  GLU A 573    13153   8083  14105   2788   4450   1900       C
ATOM   1762  OE1 GLU A 573     -39.777 -24.024 -33.134  1.00 98.22           O
ANISOU 1762  OE1 GLU A 573    13841   8838  14641   2999   4334   2062       O
ATOM   1763  OE2 GLU A 573     -39.948 -25.225 -34.966  1.00 95.67           O
ANISOU 1763  OE2 GLU A 573    13537   8246  14568   2786   4577   1840       O
ATOM   1764  N   TYR A 574     -43.213 -18.804 -34.311  1.00 68.10           N
ANISOU 1764  N   TYR A 574     9612   5630  10633   2184   4022   1652       N
ATOM   1765  CA  TYR A 574     -43.283 -17.434 -33.809  1.00 64.74           C
ANISOU 1765  CA  TYR A 574     9100   5419  10079   2201   3832   1671       C
ATOM   1766  C   TYR A 574     -43.814 -17.365 -32.377  1.00 68.01           C
ANISOU 1766  C   TYR A 574     9626   5854  10359   2311   3851   1841       C
ATOM   1767  O   TYR A 574     -43.405 -16.501 -31.597  1.00 71.21           O
ANISOU 1767  O   TYR A 574     9994   6437  10627   2443   3665   1910       O
ATOM   1768  CB  TYR A 574     -44.146 -16.572 -34.744  1.00 58.96           C
ANISOU 1768  CB  TYR A 574     8277   4739   9386   1957   3824   1505       C
ATOM   1769  CG  TYR A 574     -45.521 -17.149 -35.014  1.00 57.98           C
ANISOU 1769  CG  TYR A 574     8233   4446   9350   1763   4042   1447       C
ATOM   1770  CD1 TYR A 574     -45.758 -17.933 -36.133  1.00 58.68           C
ANISOU 1770  CD1 TYR A 574     8330   4383   9584   1615   4176   1303       C
ATOM   1771  CD2 TYR A 574     -46.581 -16.914 -34.144  1.00 56.77           C
ANISOU 1771  CD2 TYR A 574     8139   4289   9141   1730   4116   1522       C
ATOM   1772  CE1 TYR A 574     -47.006 -18.470 -36.376  1.00 55.26           C
ANISOU 1772  CE1 TYR A 574     7948   3799   9250   1432   4364   1225       C
ATOM   1773  CE2 TYR A 574     -47.831 -17.447 -34.380  1.00 54.52           C
ANISOU 1773  CE2 TYR A 574     7899   3854   8963   1550   4320   1450       C
ATOM   1774  CZ  TYR A 574     -48.037 -18.224 -35.497  1.00 55.14           C
ANISOU 1774  CZ  TYR A 574     7970   3784   9197   1398   4436   1296       C
ATOM   1775  OH  TYR A 574     -49.283 -18.752 -35.736  1.00 59.84           O
ANISOU 1775  OH  TYR A 574     8587   4236   9912   1215   4622   1198       O
ATOM   1776  N   ALA A 575     -44.713 -18.288 -32.040  1.00 64.79           N
ANISOU 1776  N   ALA A 575     9358   5266   9993   2259   4081   1897       N
ATOM   1777  CA  ALA A 575     -45.362 -18.303 -30.733  1.00 65.07           C
ANISOU 1777  CA  ALA A 575     9517   5304   9904   2346   4147   2051       C
ATOM   1778  C   ALA A 575     -44.378 -18.565 -29.595  1.00 65.04           C
ANISOU 1778  C   ALA A 575     9598   5357   9757   2636   4039   2228       C
ATOM   1779  O   ALA A 575     -44.643 -18.206 -28.450  1.00 62.64           O
ANISOU 1779  O   ALA A 575     9375   5135   9291   2751   4003   2350       O
ATOM   1780  CB  ALA A 575     -46.497 -19.324 -30.708  1.00 65.10           C
ANISOU 1780  CB  ALA A 575     9635   5086  10014   2218   4438   2053       C
ATOM   1781  N   ASN A 576     -43.250 -19.190 -29.913  1.00 67.83           N
ANISOU 1781  N   ASN A 576     9934   5670  10167   2760   3986   2235       N
ATOM   1782  CA  ASN A 576     -42.193 -19.412 -28.932  1.00 73.13           C
ANISOU 1782  CA  ASN A 576    10661   6409  10717   3048   3848   2381       C
ATOM   1783  C   ASN A 576     -40.914 -18.646 -29.271  1.00 73.64           C
ANISOU 1783  C   ASN A 576    10543   6659  10776   3149   3571   2309       C
ATOM   1784  O   ASN A 576     -39.872 -18.845 -28.639  1.00 80.77           O
ANISOU 1784  O   ASN A 576    11450   7623  11617   3387   3429   2394       O
ATOM   1785  CB  ASN A 576     -41.874 -20.903 -28.811  1.00 76.02           C
ANISOU 1785  CB  ASN A 576    11168   6561  11156   3159   4020   2472       C
ATOM   1786  CG  ASN A 576     -43.115 -21.766 -28.850  1.00 75.47           C
ANISOU 1786  CG  ASN A 576    11238   6270  11167   3002   4325   2487       C
ATOM   1787  OD1 ASN A 576     -43.464 -22.321 -29.895  1.00 76.40           O
ANISOU 1787  OD1 ASN A 576    11329   6238  11461   2822   4474   2362       O
ATOM   1788  ND2 ASN A 576     -43.796 -21.882 -27.711  1.00 70.86           N
ANISOU 1788  ND2 ASN A 576    10800   5667  10458   3070   4420   2626       N
ATOM   1789  N   CYS A 577     -40.997 -17.770 -30.266  1.00 64.53           N
ANISOU 1789  N   CYS A 577     9226   5596   9695   2970   3498   2146       N
ATOM   1790  CA  CYS A 577     -39.832 -17.034 -30.728  1.00 60.29           C
ANISOU 1790  CA  CYS A 577     8497   5224   9186   3034   3268   2055       C
ATOM   1791  C   CYS A 577     -40.228 -15.657 -31.269  1.00 62.82           C
ANISOU 1791  C   CYS A 577     8675   5700   9494   2858   3157   1924       C
ATOM   1792  O   CYS A 577     -40.033 -15.356 -32.453  1.00 58.85           O
ANISOU 1792  O   CYS A 577     8046   5211   9102   2717   3154   1776       O
ATOM   1793  CB  CYS A 577     -39.109 -17.848 -31.802  1.00 61.29           C
ANISOU 1793  CB  CYS A 577     8569   5238   9480   3019   3345   1970       C
ATOM   1794  SG  CYS A 577     -37.527 -17.180 -32.331  1.00 65.37           S
ANISOU 1794  SG  CYS A 577     8845   5935  10057   3128   3105   1867       S
ATOM   1795  N   HIS A 578     -40.786 -14.820 -30.400  1.00 58.56           N
ANISOU 1795  N   HIS A 578     8165   5277   8811   2875   3070   1979       N
ATOM   1796  CA  HIS A 578     -41.178 -13.468 -30.793  1.00 55.29           C
ANISOU 1796  CA  HIS A 578     7626   5009   8373   2730   2956   1866       C
ATOM   1797  C   HIS A 578     -40.601 -12.430 -29.831  1.00 55.43           C
ANISOU 1797  C   HIS A 578     7576   5237   8248   2888   2699   1904       C
ATOM   1798  O   HIS A 578     -40.159 -12.767 -28.730  1.00 57.89           O
ANISOU 1798  O   HIS A 578     7971   5576   8449   3101   2625   2029       O
ATOM   1799  CB  HIS A 578     -42.700 -13.351 -30.850  1.00 52.00           C
ANISOU 1799  CB  HIS A 578     7302   4515   7941   2543   3125   1858       C
ATOM   1800  CG  HIS A 578     -43.380 -13.736 -29.578  1.00 57.43           C
ANISOU 1800  CG  HIS A 578     8166   5156   8499   2644   3217   2018       C
ATOM   1801  ND1 HIS A 578     -43.975 -14.965 -29.395  1.00 62.18           N
ANISOU 1801  ND1 HIS A 578     8922   5558   9148   2628   3463   2097       N
ATOM   1802  CD2 HIS A 578     -43.550 -13.056 -28.419  1.00 60.72           C
ANISOU 1802  CD2 HIS A 578     8635   5701   8734   2765   3105   2108       C
ATOM   1803  CE1 HIS A 578     -44.488 -15.027 -28.178  1.00 65.42           C
ANISOU 1803  CE1 HIS A 578     9470   5975   9410   2735   3510   2236       C
ATOM   1804  NE2 HIS A 578     -44.247 -13.879 -27.567  1.00 66.93           N
ANISOU 1804  NE2 HIS A 578     9611   6368   9453   2822   3293   2245       N
ATOM   1805  N   LEU A 579     -40.595 -11.167 -30.243  1.00 51.79           N
ANISOU 1805  N   LEU A 579     6968   4924   7786   2788   2558   1789       N
ATOM   1806  CA  LEU A 579     -40.017 -10.124 -29.404  1.00 53.83           C
ANISOU 1806  CA  LEU A 579     7144   5380   7929   2923   2304   1797       C
ATOM   1807  C   LEU A 579     -41.028  -9.648 -28.366  1.00 55.17           C
ANISOU 1807  C   LEU A 579     7451   5593   7920   2944   2303   1880       C
ATOM   1808  O   LEU A 579     -40.676  -9.369 -27.216  1.00 53.94           O
ANISOU 1808  O   LEU A 579     7339   5543   7611   3129   2147   1958       O
ATOM   1809  CB  LEU A 579     -39.512  -8.957 -30.254  1.00 53.44           C
ANISOU 1809  CB  LEU A 579     6876   5466   7963   2815   2160   1637       C
ATOM   1810  CG  LEU A 579     -38.436  -9.281 -31.289  1.00 52.84           C
ANISOU 1810  CG  LEU A 579     6647   5373   8056   2798   2159   1545       C
ATOM   1811  CD1 LEU A 579     -37.874  -8.002 -31.897  1.00 50.74           C
ANISOU 1811  CD1 LEU A 579     6166   5263   7851   2715   2007   1406       C
ATOM   1812  CD2 LEU A 579     -37.326 -10.123 -30.666  1.00 54.06           C
ANISOU 1812  CD2 LEU A 579     6799   5516   8225   3034   2087   1627       C
ATOM   1813  N   ALA A 580     -42.287  -9.568 -28.785  1.00 52.62           N
ANISOU 1813  N   ALA A 580     7192   5189   7614   2756   2478   1855       N
ATOM   1814  CA  ALA A 580     -43.387  -9.199 -27.907  1.00 52.10           C
ANISOU 1814  CA  ALA A 580     7257   5140   7398   2756   2529   1930       C
ATOM   1815  C   ALA A 580     -44.709  -9.370 -28.638  1.00 54.71           C
ANISOU 1815  C   ALA A 580     7626   5341   7821   2528   2757   1881       C
ATOM   1816  O   ALA A 580     -44.741  -9.569 -29.850  1.00 57.07           O
ANISOU 1816  O   ALA A 580     7839   5566   8278   2366   2829   1768       O
ATOM   1817  CB  ALA A 580     -43.242  -7.754 -27.420  1.00 47.39           C
ANISOU 1817  CB  ALA A 580     6577   4748   6682   2801   2292   1879       C
ATOM   1818  N   ARG A 581     -45.798  -9.300 -27.883  1.00 56.92           N
ANISOU 1818  N   ARG A 581     8032   5595   7999   2522   2869   1959       N
ATOM   1819  CA  ARG A 581     -47.132  -9.217 -28.451  1.00 53.00           C
ANISOU 1819  CA  ARG A 581     7544   5006   7589   2312   3052   1898       C
ATOM   1820  C   ARG A 581     -47.381  -7.790 -28.920  1.00 53.32           C
ANISOU 1820  C   ARG A 581     7451   5193   7615   2211   2896   1768       C
ATOM   1821  O   ARG A 581     -46.921  -6.839 -28.291  1.00 58.48           O
ANISOU 1821  O   ARG A 581     8072   6014   8136   2329   2691   1775       O
ATOM   1822  CB  ARG A 581     -48.164  -9.574 -27.389  1.00 50.60           C
ANISOU 1822  CB  ARG A 581     7408   4636   7183   2358   3230   2028       C
ATOM   1823  CG  ARG A 581     -49.532  -9.855 -27.943  1.00 47.49           C
ANISOU 1823  CG  ARG A 581     7019   4098   6925   2145   3471   1971       C
ATOM   1824  CD  ARG A 581     -50.011 -11.171 -27.402  1.00 56.47           C
ANISOU 1824  CD  ARG A 581     8300   5061   8095   2172   3727   2076       C
ATOM   1825  NE  ARG A 581     -50.547 -12.041 -28.437  1.00 56.41           N
ANISOU 1825  NE  ARG A 581     8251   4866   8314   1975   3924   1973       N
ATOM   1826  CZ  ARG A 581     -50.802 -13.328 -28.244  1.00 59.28           C
ANISOU 1826  CZ  ARG A 581     8711   5052   8760   1977   4140   2021       C
ATOM   1827  NH1 ARG A 581     -51.303 -14.064 -29.226  1.00 63.99           N
ANISOU 1827  NH1 ARG A 581     9261   5486   9568   1790   4297   1896       N
ATOM   1828  NH2 ARG A 581     -50.552 -13.873 -27.061  1.00 54.28           N
ANISOU 1828  NH2 ARG A 581     8228   4405   7992   2171   4190   2187       N
ATOM   1829  N   ALA A 582     -48.110  -7.639 -30.020  1.00 49.67           N
ANISOU 1829  N   ALA A 582     6914   4671   7288   1996   2983   1638       N
ATOM   1830  CA  ALA A 582     -48.445  -6.315 -30.540  1.00 45.98           C
ANISOU 1830  CA  ALA A 582     6323   4341   6807   1888   2848   1503       C
ATOM   1831  C   ALA A 582     -49.960  -6.170 -30.601  1.00 42.72           C
ANISOU 1831  C   ALA A 582     5941   3871   6421   1745   3000   1467       C
ATOM   1832  O   ALA A 582     -50.633  -7.027 -31.167  1.00 39.87           O
ANISOU 1832  O   ALA A 582     5606   3348   6197   1609   3189   1435       O
ATOM   1833  CB  ALA A 582     -47.845  -6.128 -31.918  1.00 42.48           C
ANISOU 1833  CB  ALA A 582     5740   3920   6481   1758   2773   1349       C
ATOM   1834  N   PRO A 583     -50.506  -5.093 -30.012  1.00 38.46           N
ANISOU 1834  N   PRO A 583     5388   3466   5758   1772   2916   1459       N
ATOM   1835  CA  PRO A 583     -51.962  -4.931 -30.071  1.00 39.37           C
ANISOU 1835  CA  PRO A 583     5502   3559   5896   1620   3048   1409       C
ATOM   1836  C   PRO A 583     -52.379  -4.683 -31.508  1.00 41.19           C
ANISOU 1836  C   PRO A 583     5602   3801   6249   1375   2998   1215       C
ATOM   1837  O   PRO A 583     -51.665  -3.975 -32.236  1.00 35.61           O
ANISOU 1837  O   PRO A 583     4796   3202   5532   1350   2826   1117       O
ATOM   1838  CB  PRO A 583     -52.223  -3.667 -29.235  1.00 37.37           C
ANISOU 1838  CB  PRO A 583     5245   3497   5455   1692   2899   1417       C
ATOM   1839  CG  PRO A 583     -50.930  -3.364 -28.529  1.00 37.79           C
ANISOU 1839  CG  PRO A 583     5335   3638   5387   1911   2716   1498       C
ATOM   1840  CD  PRO A 583     -49.844  -3.947 -29.366  1.00 42.87           C
ANISOU 1840  CD  PRO A 583     5913   4214   6162   1914   2686   1467       C
ATOM   1841  N   ASN A 584     -53.508  -5.255 -31.914  1.00 42.69           N
ANISOU 1841  N   ASN A 584     5793   3877   6550   1201   3134   1155       N
ATOM   1842  CA  ASN A 584     -54.003  -5.067 -33.272  1.00 40.82           C
ANISOU 1842  CA  ASN A 584     5445   3654   6412    989   3070    958       C
ATOM   1843  C   ASN A 584     -54.089  -3.596 -33.654  1.00 36.49           C
ANISOU 1843  C   ASN A 584     4791   3317   5756    946   2853    852       C
ATOM   1844  O   ASN A 584     -54.342  -2.751 -32.799  1.00 37.50           O
ANISOU 1844  O   ASN A 584     4925   3563   5758   1021   2785    904       O
ATOM   1845  CB  ASN A 584     -55.371  -5.721 -33.429  1.00 37.10           C
ANISOU 1845  CB  ASN A 584     4972   3062   6060    828   3210    893       C
ATOM   1846  CG  ASN A 584     -55.311  -7.232 -33.310  1.00 47.95           C
ANISOU 1846  CG  ASN A 584     6448   4188   7584    837   3442    962       C
ATOM   1847  OD1 ASN A 584     -54.257  -7.806 -33.008  1.00 45.64           O
ANISOU 1847  OD1 ASN A 584     6241   3811   7289    987   3511   1087       O
ATOM   1848  ND2 ASN A 584     -56.448  -7.890 -33.536  1.00 40.27           N
ANISOU 1848  ND2 ASN A 584     5460   3092   6750    685   3567    876       N
ATOM   1849  N   HIS A 585     -53.858  -3.292 -34.930  1.00 33.18           N
ANISOU 1849  N   HIS A 585     4289   2939   5379    839   2759    709       N
ATOM   1850  CA  HIS A 585     -54.141  -1.952 -35.452  1.00 31.61           C
ANISOU 1850  CA  HIS A 585     4001   2913   5096    778   2585    601       C
ATOM   1851  C   HIS A 585     -55.607  -1.632 -35.188  1.00 47.66           C
ANISOU 1851  C   HIS A 585     6003   4986   7118    689   2601    555       C
ATOM   1852  O   HIS A 585     -56.433  -2.542 -35.113  1.00 32.89           O
ANISOU 1852  O   HIS A 585     4148   3000   5349    611   2741    545       O
ATOM   1853  CB  HIS A 585     -53.929  -1.885 -36.956  1.00 30.98           C
ANISOU 1853  CB  HIS A 585     3861   2842   5069    664   2532    455       C
ATOM   1854  CG  HIS A 585     -52.517  -2.126 -37.392  1.00 30.96           C
ANISOU 1854  CG  HIS A 585     3868   2811   5085    731   2511    477       C
ATOM   1855  ND1 HIS A 585     -52.038  -1.679 -38.599  1.00 30.44           N
ANISOU 1855  ND1 HIS A 585     3755   2799   5013    671   2433    372       N
ATOM   1856  CD2 HIS A 585     -51.491  -2.774 -36.789  1.00 31.78           C
ANISOU 1856  CD2 HIS A 585     4018   2843   5213    861   2563    595       C
ATOM   1857  CE1 HIS A 585     -50.771  -2.037 -38.728  1.00 33.14           C
ANISOU 1857  CE1 HIS A 585     4103   3103   5385    747   2439    418       C
ATOM   1858  NE2 HIS A 585     -50.418  -2.710 -37.652  1.00 31.52           N
ANISOU 1858  NE2 HIS A 585     3947   2825   5204    865   2509    548       N
ATOM   1859  N   ALA A 586     -55.932  -0.346 -35.085  1.00 30.59           N
ANISOU 1859  N   ALA A 586     3789   2982   4851    699   2465    517       N
ATOM   1860  CA  ALA A 586     -57.293   0.073 -34.766  1.00 30.75           C
ANISOU 1860  CA  ALA A 586     3768   3061   4855    639   2471    476       C
ATOM   1861  C   ALA A 586     -57.670   1.372 -35.491  1.00 32.48           C
ANISOU 1861  C   ALA A 586     3898   3430   5011    596   2318    361       C
ATOM   1862  O   ALA A 586     -56.813   2.173 -35.855  1.00 32.49           O
ANISOU 1862  O   ALA A 586     3896   3501   4947    646   2204    350       O
ATOM   1863  CB  ALA A 586     -57.461   0.233 -33.257  1.00 31.38           C
ANISOU 1863  CB  ALA A 586     3920   3158   4843    763   2516    612       C
ATOM   1864  N   VAL A 587     -58.959   1.546 -35.732  1.00 30.96           N
ANISOU 1864  N   VAL A 587     3629   3280   4854    507   2330    273       N
ATOM   1865  CA  VAL A 587     -59.476   2.791 -36.272  1.00 28.89           C
ANISOU 1865  CA  VAL A 587     3288   3159   4530    496   2205    179       C
ATOM   1866  C   VAL A 587     -59.587   3.760 -35.111  1.00 28.59           C
ANISOU 1866  C   VAL A 587     3282   3206   4373    612   2152    257       C
ATOM   1867  O   VAL A 587     -60.125   3.404 -34.070  1.00 29.51           O
ANISOU 1867  O   VAL A 587     3429   3298   4485    642   2240    328       O
ATOM   1868  CB  VAL A 587     -60.885   2.578 -36.849  1.00 33.47           C
ANISOU 1868  CB  VAL A 587     3753   3759   5203    377   2246     55       C
ATOM   1869  CG1 VAL A 587     -61.532   3.924 -37.249  1.00 29.02           C
ANISOU 1869  CG1 VAL A 587     3106   3347   4572    402   2125    -28       C
ATOM   1870  CG2 VAL A 587     -60.840   1.591 -38.021  1.00 32.57           C
ANISOU 1870  CG2 VAL A 587     3608   3558   5210    257   2306    -51       C
ATOM   1871  N   VAL A 588     -59.068   4.972 -35.277  1.00 33.56           N
ANISOU 1871  N   VAL A 588     3915   3927   4908    683   2023    244       N
ATOM   1872  CA  VAL A 588     -59.271   6.029 -34.289  1.00 31.78           C
ANISOU 1872  CA  VAL A 588     3717   3785   4570    794   1965    286       C
ATOM   1873  C   VAL A 588     -60.073   7.186 -34.873  1.00 30.00           C
ANISOU 1873  C   VAL A 588     3419   3661   4320    786   1877    187       C
ATOM   1874  O   VAL A 588     -60.171   7.331 -36.088  1.00 31.36           O
ANISOU 1874  O   VAL A 588     3537   3847   4532    715   1826     99       O
ATOM   1875  CB  VAL A 588     -57.941   6.584 -33.760  1.00 26.73           C
ANISOU 1875  CB  VAL A 588     3155   3157   3844    916   1893    358       C
ATOM   1876  CG1 VAL A 588     -57.061   5.454 -33.239  1.00 32.64           C
ANISOU 1876  CG1 VAL A 588     3968   3814   4619    955   1976    459       C
ATOM   1877  CG2 VAL A 588     -57.251   7.369 -34.843  1.00 25.73           C
ANISOU 1877  CG2 VAL A 588     3004   3057   3713    879   1755    292       C
ATOM   1878  N   THR A 589     -60.638   8.009 -33.992  1.00 36.51           N
ANISOU 1878  N   THR A 589     4256   4554   5064    873   1850    203       N
ATOM   1879  CA  THR A 589     -61.459   9.160 -34.373  1.00 34.33           C
ANISOU 1879  CA  THR A 589     3922   4368   4755    893   1756    120       C
ATOM   1880  C   THR A 589     -61.619  10.063 -33.149  1.00 28.68           C
ANISOU 1880  C   THR A 589     3269   3703   3925   1024   1726    162       C
ATOM   1881  O   THR A 589     -61.124   9.726 -32.073  1.00 29.75           O
ANISOU 1881  O   THR A 589     3491   3811   4002   1093   1782    249       O
ATOM   1882  CB  THR A 589     -62.862   8.726 -34.861  1.00 36.40           C
ANISOU 1882  CB  THR A 589     4048   4660   5121    810   1832     35       C
ATOM   1883  OG1 THR A 589     -63.575   9.867 -35.358  1.00 37.22           O
ANISOU 1883  OG1 THR A 589     4097   4856   5189    843   1702    -48       O
ATOM   1884  CG2 THR A 589     -63.659   8.099 -33.723  1.00 33.90           C
ANISOU 1884  CG2 THR A 589     3724   4332   4826    803   1950     83       C
ATOM   1885  N   ARG A 590     -62.300  11.199 -33.313  1.00 26.94           N
ANISOU 1885  N   ARG A 590     3019   3554   3662   1066   1628     96       N
ATOM   1886  CA  ARG A 590     -62.591  12.093 -32.193  1.00 37.86           C
ANISOU 1886  CA  ARG A 590     4463   4984   4939   1195   1607    114       C
ATOM   1887  C   ARG A 590     -63.742  11.530 -31.366  1.00 38.37           C
ANISOU 1887  C   ARG A 590     4477   5073   5028   1196   1754    129       C
ATOM   1888  O   ARG A 590     -64.566  10.779 -31.885  1.00 33.06           O
ANISOU 1888  O   ARG A 590     3688   4399   4473   1090   1831     90       O
ATOM   1889  CB  ARG A 590     -62.995  13.487 -32.682  1.00 32.73           C
ANISOU 1889  CB  ARG A 590     3803   4385   4248   1241   1456     36       C
ATOM   1890  CG  ARG A 590     -61.910  14.280 -33.388  1.00 28.34           C
ANISOU 1890  CG  ARG A 590     3319   3791   3656   1227   1292     26       C
ATOM   1891  CD  ARG A 590     -62.466  15.627 -33.855  1.00 26.14           C
ANISOU 1891  CD  ARG A 590     3044   3546   3343   1283   1169    -39       C
ATOM   1892  NE  ARG A 590     -63.684  15.491 -34.659  1.00 30.15           N
ANISOU 1892  NE  ARG A 590     3428   4112   3915   1256   1185   -101       N
ATOM   1893  CZ  ARG A 590     -63.701  15.270 -35.969  1.00 29.42           C
ANISOU 1893  CZ  ARG A 590     3289   4021   3869   1175   1135   -138       C
ATOM   1894  NH1 ARG A 590     -62.559  15.159 -36.643  1.00 28.27           N
ANISOU 1894  NH1 ARG A 590     3211   3814   3715   1111   1090   -110       N
ATOM   1895  NH2 ARG A 590     -64.862  15.162 -36.613  1.00 32.49           N
ANISOU 1895  NH2 ARG A 590     3556   4478   4310   1165   1128   -210       N
ATOM   1896  N   LYS A 591     -63.799  11.900 -30.090  1.00 29.28           N
ANISOU 1896  N   LYS A 591     3419   3941   3764   1302   1775    176       N
ATOM   1897  CA  LYS A 591     -64.908  11.499 -29.222  1.00 41.89           C
ANISOU 1897  CA  LYS A 591     4987   5559   5370   1300   1904    194       C
ATOM   1898  C   LYS A 591     -66.282  11.872 -29.793  1.00 39.32           C
ANISOU 1898  C   LYS A 591     4499   5303   5140   1259   1910     93       C
ATOM   1899  O   LYS A 591     -67.210  11.068 -29.748  1.00 46.93           O
ANISOU 1899  O   LYS A 591     5357   6269   6207   1173   2032     83       O
ATOM   1900  CB  LYS A 591     -64.731  12.069 -27.805  1.00 42.98           C
ANISOU 1900  CB  LYS A 591     5269   5719   5342   1447   1911    248       C
ATOM   1901  CG  LYS A 591     -63.885  11.171 -26.906  1.00 53.11           C
ANISOU 1901  CG  LYS A 591     6685   6944   6549   1488   1990    371       C
ATOM   1902  CD  LYS A 591     -63.428  11.851 -25.616  1.00 55.48           C
ANISOU 1902  CD  LYS A 591     7152   7279   6647   1665   1954    409       C
ATOM   1903  CE  LYS A 591     -61.923  11.657 -25.401  1.00 56.90           C
ANISOU 1903  CE  LYS A 591     7448   7432   6739   1746   1882    466       C
ATOM   1904  NZ  LYS A 591     -61.576  11.065 -24.071  1.00 58.34           N
ANISOU 1904  NZ  LYS A 591     7788   7609   6772   1873   1969    580       N
ATOM   1905  N   ASP A 592     -66.401  13.072 -30.356  1.00 32.48           N
ANISOU 1905  N   ASP A 592     3608   4488   4245   1328   1779     17       N
ATOM   1906  CA  ASP A 592     -67.687  13.573 -30.854  1.00 34.01           C
ANISOU 1906  CA  ASP A 592     3648   4760   4517   1334   1766    -79       C
ATOM   1907  C   ASP A 592     -68.214  12.813 -32.076  1.00 40.35           C
ANISOU 1907  C   ASP A 592     4276   5577   5478   1210   1789   -145       C
ATOM   1908  O   ASP A 592     -69.366  12.997 -32.478  1.00 41.04           O
ANISOU 1908  O   ASP A 592     4199   5740   5654   1209   1794   -231       O
ATOM   1909  CB  ASP A 592     -67.579  15.069 -31.179  1.00 33.11           C
ANISOU 1909  CB  ASP A 592     3579   4679   4322   1463   1608   -130       C
ATOM   1910  CG  ASP A 592     -66.308  15.397 -31.957  1.00 47.96           C
ANISOU 1910  CG  ASP A 592     5556   6507   6158   1460   1481   -112       C
ATOM   1911  OD1 ASP A 592     -65.235  15.544 -31.318  1.00 53.98           O
ANISOU 1911  OD1 ASP A 592     6465   7217   6827   1494   1450    -55       O
ATOM   1912  OD2 ASP A 592     -66.377  15.481 -33.205  1.00 46.44           O
ANISOU 1912  OD2 ASP A 592     5299   6320   6025   1393   1382   -162       O
ATOM   1913  N   LYS A 593     -67.378  11.969 -32.675  1.00 37.72           N
ANISOU 1913  N   LYS A 593     3972   5176   5185   1114   1800   -116       N
ATOM   1914  CA  LYS A 593     -67.792  11.226 -33.863  1.00 40.35           C
ANISOU 1914  CA  LYS A 593     4157   5512   5663    993   1818   -193       C
ATOM   1915  C   LYS A 593     -67.740   9.717 -33.667  1.00 42.64           C
ANISOU 1915  C   LYS A 593     4435   5721   6046    851   1955   -155       C
ATOM   1916  O   LYS A 593     -68.063   8.967 -34.590  1.00 45.16           O
ANISOU 1916  O   LYS A 593     4640   6024   6494    733   1978   -230       O
ATOM   1917  CB  LYS A 593     -66.932  11.602 -35.082  1.00 43.09           C
ANISOU 1917  CB  LYS A 593     4560   5841   5971    972   1650   -224       C
ATOM   1918  CG  LYS A 593     -67.447  12.790 -35.880  1.00 49.69           C
ANISOU 1918  CG  LYS A 593     5357   6759   6765   1039   1467   -305       C
ATOM   1919  CD  LYS A 593     -67.733  12.394 -37.324  1.00 52.08           C
ANISOU 1919  CD  LYS A 593     5566   7087   7135    943   1378   -403       C
ATOM   1920  CE  LYS A 593     -68.086  13.603 -38.178  1.00 51.88           C
ANISOU 1920  CE  LYS A 593     5542   7135   7035   1033   1182   -461       C
ATOM   1921  NZ  LYS A 593     -68.266  13.237 -39.620  1.00 49.97           N
ANISOU 1921  NZ  LYS A 593     5242   6925   6818    958   1078   -554       N
ATOM   1922  N   GLU A 594     -67.341   9.269 -32.477  1.00 36.90           N
ANISOU 1922  N   GLU A 594     3833   4933   5255    870   2044    -43       N
ATOM   1923  CA  GLU A 594     -67.089   7.844 -32.271  1.00 32.53           C
ANISOU 1923  CA  GLU A 594     3312   4271   4778    761   2174     20       C
ATOM   1924  C   GLU A 594     -68.314   6.956 -32.523  1.00 34.21           C
ANISOU 1924  C   GLU A 594     3362   4476   5162    632   2291    -45       C
ATOM   1925  O   GLU A 594     -68.203   5.948 -33.206  1.00 34.49           O
ANISOU 1925  O   GLU A 594     3358   4430   5316    509   2338    -75       O
ATOM   1926  CB  GLU A 594     -66.443   7.558 -30.909  1.00 42.86           C
ANISOU 1926  CB  GLU A 594     4793   5515   5977    839   2252    163       C
ATOM   1927  CG  GLU A 594     -67.286   7.920 -29.712  1.00 57.05           C
ANISOU 1927  CG  GLU A 594     6603   7359   7714    914   2333    198       C
ATOM   1928  CD  GLU A 594     -66.609   7.577 -28.401  1.00 65.75           C
ANISOU 1928  CD  GLU A 594     7892   8397   8693   1007   2415    342       C
ATOM   1929  OE1 GLU A 594     -66.772   8.352 -27.433  1.00 68.56           O
ANISOU 1929  OE1 GLU A 594     8322   8809   8917   1130   2410    370       O
ATOM   1930  OE2 GLU A 594     -65.919   6.533 -28.339  1.00 66.68           O
ANISOU 1930  OE2 GLU A 594     8087   8407   8842    970   2484    425       O
ATOM   1931  N   ALA A 595     -69.476   7.342 -32.010  1.00 40.61           N
ANISOU 1931  N   ALA A 595     4070   5366   5996    658   2337    -78       N
ATOM   1932  CA  ALA A 595     -70.684   6.550 -32.215  1.00 46.08           C
ANISOU 1932  CA  ALA A 595     4585   6056   6868    533   2449   -145       C
ATOM   1933  C   ALA A 595     -71.016   6.442 -33.706  1.00 45.48           C
ANISOU 1933  C   ALA A 595     4337   6016   6926    437   2356   -297       C
ATOM   1934  O   ALA A 595     -71.327   5.356 -34.215  1.00 45.91           O
ANISOU 1934  O   ALA A 595     4308   5995   7143    286   2431   -353       O
ATOM   1935  CB  ALA A 595     -71.847   7.153 -31.444  1.00 38.83           C
ANISOU 1935  CB  ALA A 595     3572   5238   5945    597   2501   -161       C
ATOM   1936  N   CYS A 596     -70.923   7.576 -34.396  1.00 41.08           N
ANISOU 1936  N   CYS A 596     3740   5564   6303    531   2194   -370       N
ATOM   1937  CA  CYS A 596     -71.195   7.652 -35.825  1.00 36.23           C
ANISOU 1937  CA  CYS A 596     2974   5002   5790    474   2083   -525       C
ATOM   1938  C   CYS A 596     -70.249   6.772 -36.649  1.00 41.26           C
ANISOU 1938  C   CYS A 596     3683   5531   6462    366   2085   -542       C
ATOM   1939  O   CYS A 596     -70.699   5.909 -37.410  1.00 36.56           O
ANISOU 1939  O   CYS A 596     2960   4907   6022    224   2112   -660       O
ATOM   1940  CB  CYS A 596     -71.099   9.105 -36.292  1.00 47.71           C
ANISOU 1940  CB  CYS A 596     4422   6564   7141    630   1917   -573       C
ATOM   1941  SG  CYS A 596     -71.771   9.400 -37.943  1.00 98.78           S
ANISOU 1941  SG  CYS A 596    10727  13141  13663    592   1685   -765       S
ATOM   1942  N   VAL A 597     -68.943   6.996 -36.499  1.00 37.60           N
ANISOU 1942  N   VAL A 597     3417   5008   5860    433   2055   -437       N
ATOM   1943  CA  VAL A 597     -67.938   6.210 -37.218  1.00 40.54           C
ANISOU 1943  CA  VAL A 597     3874   5278   6251    352   2064   -439       C
ATOM   1944  C   VAL A 597     -68.133   4.717 -36.950  1.00 45.85           C
ANISOU 1944  C   VAL A 597     4539   5822   7059    210   2219   -422       C
ATOM   1945  O   VAL A 597     -68.055   3.890 -37.863  1.00 42.84           O
ANISOU 1945  O   VAL A 597     4111   5378   6789     90   2241   -520       O
ATOM   1946  CB  VAL A 597     -66.505   6.618 -36.814  1.00 35.69           C
ANISOU 1946  CB  VAL A 597     3470   4615   5478    451   2024   -304       C
ATOM   1947  CG1 VAL A 597     -65.468   5.687 -37.460  1.00 37.69           C
ANISOU 1947  CG1 VAL A 597     3805   4756   5760    372   2054   -295       C
ATOM   1948  CG2 VAL A 597     -66.238   8.075 -37.189  1.00 30.22           C
ANISOU 1948  CG2 VAL A 597     2823   4018   4641    567   1828   -317       C
ATOM   1949  N   HIS A 598     -68.407   4.398 -35.687  1.00 46.11           N
ANISOU 1949  N   HIS A 598     4628   5810   7083    229   2334   -305       N
ATOM   1950  CA  HIS A 598     -68.666   3.034 -35.239  1.00 42.69           C
ANISOU 1950  CA  HIS A 598     4206   5234   6780    115   2506   -266       C
ATOM   1951  C   HIS A 598     -69.759   2.387 -36.068  1.00 44.61           C
ANISOU 1951  C   HIS A 598     4244   5472   7234    -46   2544   -435       C
ATOM   1952  O   HIS A 598     -69.571   1.323 -36.657  1.00 43.42           O
ANISOU 1952  O   HIS A 598     4090   5198   7209   -171   2609   -495       O
ATOM   1953  CB  HIS A 598     -69.112   3.054 -33.777  1.00 37.62           C
ANISOU 1953  CB  HIS A 598     3620   4582   6091    179   2621   -139       C
ATOM   1954  CG  HIS A 598     -69.158   1.706 -33.142  1.00 40.35           C
ANISOU 1954  CG  HIS A 598     4037   4755   6541    100   2814    -56       C
ATOM   1955  ND1 HIS A 598     -70.264   0.886 -33.217  1.00 44.03           N
ANISOU 1955  ND1 HIS A 598     4366   5161   7203    -40   2944   -128       N
ATOM   1956  CD2 HIS A 598     -68.232   1.027 -32.422  1.00 41.60           C
ANISOU 1956  CD2 HIS A 598     4386   4777   6643    148   2904     92       C
ATOM   1957  CE1 HIS A 598     -70.018  -0.239 -32.571  1.00 48.28           C
ANISOU 1957  CE1 HIS A 598     5023   5520   7800    -75   3116    -24       C
ATOM   1958  NE2 HIS A 598     -68.793  -0.180 -32.079  1.00 43.98           N
ANISOU 1958  NE2 HIS A 598     4680   4930   7102     46   3094    114       N
ATOM   1959  N   LYS A 599     -70.907   3.046 -36.112  1.00 39.28           N
ANISOU 1959  N   LYS A 599     3391   4931   6604    -37   2498   -524       N
ATOM   1960  CA  LYS A 599     -72.039   2.519 -36.837  1.00 42.40           C
ANISOU 1960  CA  LYS A 599     3557   5344   7210   -185   2512   -702       C
ATOM   1961  C   LYS A 599     -71.728   2.430 -38.325  1.00 42.01           C
ANISOU 1961  C   LYS A 599     3432   5320   7211   -254   2386   -879       C
ATOM   1962  O   LYS A 599     -71.921   1.385 -38.939  1.00 42.08           O
ANISOU 1962  O   LYS A 599     3370   5235   7384   -413   2442   -997       O
ATOM   1963  CB  LYS A 599     -73.290   3.370 -36.583  1.00 42.36           C
ANISOU 1963  CB  LYS A 599     3364   5499   7233   -131   2463   -762       C
ATOM   1964  CG  LYS A 599     -74.560   2.794 -37.206  1.00 51.98           C
ANISOU 1964  CG  LYS A 599     4318   6741   8690   -287   2472   -951       C
ATOM   1965  CD  LYS A 599     -75.796   3.584 -36.782  1.00 54.62           C
ANISOU 1965  CD  LYS A 599     4470   7227   9055   -219   2444   -984       C
ATOM   1966  CE  LYS A 599     -77.093   2.956 -37.296  1.00 59.20           C
ANISOU 1966  CE  LYS A 599     4774   7829   9890   -379   2454  -1170       C
ATOM   1967  NZ  LYS A 599     -77.513   1.723 -36.560  1.00 58.57           N
ANISOU 1967  NZ  LYS A 599     4703   7581   9970   -527   2688  -1115       N
ATOM   1968  N   ILE A 600     -71.239   3.518 -38.909  1.00 39.13           N
ANISOU 1968  N   ILE A 600     3088   5077   6703   -133   2223   -908       N
ATOM   1969  CA  ILE A 600     -70.975   3.514 -40.351  1.00 38.89           C
ANISOU 1969  CA  ILE A 600     3030   5089   6659   -177   2054  -1069       C
ATOM   1970  C   ILE A 600     -69.978   2.435 -40.787  1.00 43.15           C
ANISOU 1970  C   ILE A 600     3713   5466   7218   -273   2129  -1059       C
ATOM   1971  O   ILE A 600     -70.193   1.746 -41.781  1.00 48.61           O
ANISOU 1971  O   ILE A 600     4341   6132   7999   -396   2076  -1224       O
ATOM   1972  CB  ILE A 600     -70.539   4.892 -40.858  1.00 37.29           C
ANISOU 1972  CB  ILE A 600     2928   5015   6227    -13   1813  -1045       C
ATOM   1973  CG1 ILE A 600     -71.728   5.852 -40.806  1.00 42.65           C
ANISOU 1973  CG1 ILE A 600     3429   5860   6917     69   1699  -1119       C
ATOM   1974  CG2 ILE A 600     -69.991   4.783 -42.272  1.00 36.98           C
ANISOU 1974  CG2 ILE A 600     2964   4984   6102    -46   1640  -1150       C
ATOM   1975  CD1 ILE A 600     -71.431   7.265 -41.274  1.00 40.86           C
ANISOU 1975  CD1 ILE A 600     3301   5746   6477    240   1471  -1092       C
ATOM   1976  N   LEU A 601     -68.905   2.263 -40.026  1.00 41.46           N
ANISOU 1976  N   LEU A 601     3687   5143   6923   -211   2250   -875       N
ATOM   1977  CA  LEU A 601     -67.894   1.274 -40.380  1.00 41.63           C
ANISOU 1977  CA  LEU A 601     3847   5007   6961   -274   2328   -852       C
ATOM   1978  C   LEU A 601     -68.381  -0.177 -40.289  1.00 47.42           C
ANISOU 1978  C   LEU A 601     4518   5580   7918   -446   2511   -912       C
ATOM   1979  O   LEU A 601     -67.952  -1.025 -41.076  1.00 48.61           O
ANISOU 1979  O   LEU A 601     4701   5628   8140   -541   2544  -1005       O
ATOM   1980  CB  LEU A 601     -66.627   1.461 -39.546  1.00 45.30           C
ANISOU 1980  CB  LEU A 601     4527   5405   7279   -148   2372   -635       C
ATOM   1981  CG  LEU A 601     -65.796   2.715 -39.830  1.00 46.52           C
ANISOU 1981  CG  LEU A 601     4781   5667   7228     -6   2196   -584       C
ATOM   1982  CD1 LEU A 601     -64.430   2.588 -39.165  1.00 43.11           C
ANISOU 1982  CD1 LEU A 601     4534   5144   6702     81   2248   -409       C
ATOM   1983  CD2 LEU A 601     -65.644   2.956 -41.321  1.00 52.68           C
ANISOU 1983  CD2 LEU A 601     5559   6506   7948    -39   2014   -727       C
ATOM   1984  N   ARG A 602     -69.270  -0.468 -39.341  1.00 43.30           N
ANISOU 1984  N   ARG A 602     3941   5025   7488   -479   2608   -854       N
ATOM   1985  CA  ARG A 602     -69.813  -1.821 -39.212  1.00 48.30           C
ANISOU 1985  CA  ARG A 602     4533   5485   8335   -642   2773   -905       C
ATOM   1986  C   ARG A 602     -70.688  -2.200 -40.408  1.00 52.59           C
ANISOU 1986  C   ARG A 602     4847   6066   9068   -814   2720  -1183       C
ATOM   1987  O   ARG A 602     -70.656  -3.337 -40.875  1.00 52.39           O
ANISOU 1987  O   ARG A 602     4819   5885   9201   -960   2814  -1287       O
ATOM   1988  CB  ARG A 602     -70.606  -1.976 -37.911  1.00 53.09           C
ANISOU 1988  CB  ARG A 602     5131   6054   8986   -629   2900   -780       C
ATOM   1989  CG  ARG A 602     -69.788  -1.695 -36.668  1.00 58.35           C
ANISOU 1989  CG  ARG A 602     6017   6685   9469   -466   2952   -530       C
ATOM   1990  CD  ARG A 602     -69.373  -2.951 -35.944  1.00 63.77           C
ANISOU 1990  CD  ARG A 602     6861   7144  10226   -494   3149   -405       C
ATOM   1991  NE  ARG A 602     -70.391  -3.390 -34.998  1.00 67.00           N
ANISOU 1991  NE  ARG A 602     7223   7494  10741   -537   3308   -356       N
ATOM   1992  CZ  ARG A 602     -71.287  -4.332 -35.258  1.00 71.09           C
ANISOU 1992  CZ  ARG A 602     7620   7900  11492   -705   3430   -472       C
ATOM   1993  NH1 ARG A 602     -72.180  -4.675 -34.339  1.00 74.25           N
ANISOU 1993  NH1 ARG A 602     7983   8248  11979   -733   3587   -413       N
ATOM   1994  NH2 ARG A 602     -71.288  -4.933 -36.440  1.00 74.49           N
ANISOU 1994  NH2 ARG A 602     7965   8269  12069   -845   3400   -658       N
ATOM   1995  N   GLN A 603     -71.474  -1.253 -40.905  1.00 53.86           N
ANISOU 1995  N   GLN A 603     4813   6435   9218   -791   2559  -1318       N
ATOM   1996  CA  GLN A 603     -72.306  -1.531 -42.067  1.00 53.38           C
ANISOU 1996  CA  GLN A 603     4512   6447   9324   -939   2459  -1607       C
ATOM   1997  C   GLN A 603     -71.468  -1.563 -43.351  1.00 53.93           C
ANISOU 1997  C   GLN A 603     4726   6525   9240   -921   2260  -1706       C
ATOM   1998  O   GLN A 603     -71.807  -2.262 -44.304  1.00 57.15           O
ANISOU 1998  O   GLN A 603     5056   6902   9755  -1058   2193  -1922       O
ATOM   1999  CB  GLN A 603     -73.446  -0.521 -42.185  1.00 60.54           C
ANISOU 1999  CB  GLN A 603     5193   7578  10233   -884   2290  -1708       C
ATOM   2000  CG  GLN A 603     -73.045   0.812 -42.782  1.00 72.09           C
ANISOU 2000  CG  GLN A 603     6750   9223  11418   -692   2010  -1689       C
ATOM   2001  CD  GLN A 603     -73.733   1.089 -44.107  1.00 80.07           C
ANISOU 2001  CD  GLN A 603     7615  10389  12419   -715   1733  -1935       C
ATOM   2002  OE1 GLN A 603     -73.542   2.148 -44.708  1.00 84.12           O
ANISOU 2002  OE1 GLN A 603     8196  11049  12715   -562   1502  -1934       O
ATOM   2003  NE2 GLN A 603     -74.539   0.137 -44.568  1.00 79.88           N
ANISOU 2003  NE2 GLN A 603     7395  10328  12627   -903   1754  -2149       N
ATOM   2004  N   GLN A 604     -70.369  -0.817 -43.373  1.00 50.28           N
ANISOU 2004  N   GLN A 604     4475   6101   8529   -756   2175  -1556       N
ATOM   2005  CA  GLN A 604     -69.512  -0.803 -44.552  1.00 54.63           C
ANISOU 2005  CA  GLN A 604     5175   6659   8923   -728   2019  -1628       C
ATOM   2006  C   GLN A 604     -68.807  -2.143 -44.750  1.00 57.60           C
ANISOU 2006  C   GLN A 604     5666   6818   9403   -841   2183  -1648       C
ATOM   2007  O   GLN A 604     -68.747  -2.663 -45.868  1.00 60.71           O
ANISOU 2007  O   GLN A 604     6075   7190   9803   -920   2095  -1832       O
ATOM   2008  CB  GLN A 604     -68.500   0.341 -44.480  1.00 50.42           C
ANISOU 2008  CB  GLN A 604     4823   6207   8127   -536   1913  -1457       C
ATOM   2009  CG  GLN A 604     -69.117   1.709 -44.734  1.00 50.13           C
ANISOU 2009  CG  GLN A 604     4709   6382   7957   -418   1695  -1484       C
ATOM   2010  CD  GLN A 604     -69.642   1.854 -46.148  1.00 48.89           C
ANISOU 2010  CD  GLN A 604     4485   6344   7745   -443   1466  -1704       C
ATOM   2011  OE1 GLN A 604     -68.899   1.691 -47.115  1.00 48.57           O
ANISOU 2011  OE1 GLN A 604     4590   6284   7583   -437   1390  -1753       O
ATOM   2012  NE2 GLN A 604     -70.927   2.152 -46.277  1.00 50.97           N
ANISOU 2012  NE2 GLN A 604     4529   6740   8097   -462   1355  -1841       N
ATOM   2013  N   GLN A 605     -68.287  -2.705 -43.660  1.00 54.89           N
ANISOU 2013  N   GLN A 605     5412   6312   9133   -836   2421  -1461       N
ATOM   2014  CA  GLN A 605     -67.575  -3.978 -43.726  1.00 54.95           C
ANISOU 2014  CA  GLN A 605     5542   6093   9243   -918   2598  -1451       C
ATOM   2015  C   GLN A 605     -68.557  -5.106 -43.960  1.00 57.08           C
ANISOU 2015  C   GLN A 605     5659   6240   9787  -1131   2707  -1642       C
ATOM   2016  O   GLN A 605     -68.190  -6.178 -44.432  1.00 62.12           O
ANISOU 2016  O   GLN A 605     6372   6702  10527  -1231   2798  -1728       O
ATOM   2017  CB  GLN A 605     -66.793  -4.243 -42.444  1.00 53.60           C
ANISOU 2017  CB  GLN A 605     5511   5787   9066   -830   2812  -1188       C
ATOM   2018  CG  GLN A 605     -67.659  -4.303 -41.209  1.00 55.92           C
ANISOU 2018  CG  GLN A 605     5733   6055   9458   -842   2934  -1078       C
ATOM   2019  CD  GLN A 605     -66.949  -4.943 -40.039  1.00 57.01           C
ANISOU 2019  CD  GLN A 605     6082   6013   9565   -756   3082   -837       C
ATOM   2020  OE1 GLN A 605     -65.831  -5.451 -40.173  1.00 50.73           O
ANISOU 2020  OE1 GLN A 605     5445   5099   8731   -708   3134   -768       O
ATOM   2021  NE2 GLN A 605     -67.596  -4.923 -38.878  1.00 60.21           N
ANISOU 2021  NE2 GLN A 605     6486   6405   9987   -725   3155   -713       N
ATOM   2022  N   HIS A 606     -69.817  -4.875 -43.625  1.00 51.33           N
ANISOU 2022  N   HIS A 606     4709   5599   9194  -1206   2706  -1717       N
ATOM   2023  CA  HIS A 606     -70.811  -5.867 -43.958  1.00 55.27           C
ANISOU 2023  CA  HIS A 606     5027   5999   9973  -1428   2783  -1933       C
ATOM   2024  C   HIS A 606     -71.052  -5.856 -45.469  1.00 56.66           C
ANISOU 2024  C   HIS A 606     5145   6278  10106  -1489   2523  -2220       C
ATOM   2025  O   HIS A 606     -71.299  -6.898 -46.066  1.00 58.37           O
ANISOU 2025  O   HIS A 606     5322   6359  10499  -1661   2565  -2417       O
ATOM   2026  CB  HIS A 606     -72.103  -5.674 -43.165  1.00 58.57           C
ANISOU 2026  CB  HIS A 606     5244   6475  10533  -1471   2834  -1925       C
ATOM   2027  CG  HIS A 606     -72.864  -6.944 -42.969  1.00 69.08           C
ANISOU 2027  CG  HIS A 606     6522   7608  12116  -1644   2982  -2015       C
ATOM   2028  ND1 HIS A 606     -73.808  -7.393 -43.869  1.00 75.69           N
ANISOU 2028  ND1 HIS A 606     7143   8471  13144  -1821   2884  -2314       N
ATOM   2029  CD2 HIS A 606     -72.786  -7.890 -42.002  1.00 71.65           C
ANISOU 2029  CD2 HIS A 606     6990   7703  12531  -1656   3216  -1852       C
ATOM   2030  CE1 HIS A 606     -74.295  -8.548 -43.452  1.00 80.47           C
ANISOU 2030  CE1 HIS A 606     7756   8866  13953  -1939   3067  -2327       C
ATOM   2031  NE2 HIS A 606     -73.690  -8.872 -42.324  1.00 79.88           N
ANISOU 2031  NE2 HIS A 606     7898   8631  13821  -1841   3278  -2047       N
ATOM   2032  N   LEU A 607     -70.950  -4.682 -46.089  1.00 56.00           N
ANISOU 2032  N   LEU A 607     5075   6424   9777  -1342   2256  -2241       N
ATOM   2033  CA  LEU A 607     -71.085  -4.572 -47.542  1.00 54.00           C
ANISOU 2033  CA  LEU A 607     4810   6286   9421  -1359   1995  -2488       C
ATOM   2034  C   LEU A 607     -69.842  -5.047 -48.299  1.00 56.82           C
ANISOU 2034  C   LEU A 607     5422   6533   9634  -1326   1998  -2491       C
ATOM   2035  O   LEU A 607     -69.947  -5.800 -49.276  1.00 57.67           O
ANISOU 2035  O   LEU A 607     5534   6583   9794  -1437   1938  -2723       O
ATOM   2036  CB  LEU A 607     -71.410  -3.137 -47.947  1.00 55.03           C
ANISOU 2036  CB  LEU A 607     4890   6690   9329  -1196   1722  -2491       C
ATOM   2037  CG  LEU A 607     -72.730  -2.569 -47.420  1.00 62.37           C
ANISOU 2037  CG  LEU A 607     5545   7766  10387  -1207   1671  -2533       C
ATOM   2038  CD1 LEU A 607     -72.985  -1.164 -47.963  1.00 64.34           C
ANISOU 2038  CD1 LEU A 607     5774   8272  10400  -1024   1383  -2544       C
ATOM   2039  CD2 LEU A 607     -73.883  -3.495 -47.761  1.00 65.37           C
ANISOU 2039  CD2 LEU A 607     5669   8110  11059  -1426   1676  -2805       C
ATOM   2040  N   PHE A 608     -68.668  -4.618 -47.844  1.00 54.93           N
ANISOU 2040  N   PHE A 608     5386   6264   9222  -1172   2069  -2245       N
ATOM   2041  CA  PHE A 608     -67.441  -4.823 -48.605  1.00 54.78           C
ANISOU 2041  CA  PHE A 608     5595   6184   9036  -1105   2052  -2234       C
ATOM   2042  C   PHE A 608     -66.340  -5.552 -47.839  1.00 54.48           C
ANISOU 2042  C   PHE A 608     5720   5925   9054  -1081   2305  -2035       C
ATOM   2043  O   PHE A 608     -65.180  -5.538 -48.251  1.00 52.83           O
ANISOU 2043  O   PHE A 608     5694   5682   8698   -987   2309  -1968       O
ATOM   2044  CB  PHE A 608     -66.904  -3.478 -49.092  1.00 51.01           C
ANISOU 2044  CB  PHE A 608     5217   5906   8258   -920   1851  -2149       C
ATOM   2045  CG  PHE A 608     -67.960  -2.573 -49.653  1.00 52.76           C
ANISOU 2045  CG  PHE A 608     5291   6356   8401   -893   1601  -2286       C
ATOM   2046  CD1 PHE A 608     -68.607  -2.894 -50.835  1.00 53.91           C
ANISOU 2046  CD1 PHE A 608     5372   6571   8542   -971   1430  -2563       C
ATOM   2047  CD2 PHE A 608     -68.302  -1.397 -49.005  1.00 48.98           C
ANISOU 2047  CD2 PHE A 608     4744   6022   7845   -776   1527  -2146       C
ATOM   2048  CE1 PHE A 608     -69.586  -2.065 -51.357  1.00 53.32           C
ANISOU 2048  CE1 PHE A 608     5157   6716   8388   -924   1180  -2689       C
ATOM   2049  CE2 PHE A 608     -69.277  -0.561 -49.525  1.00 49.55           C
ANISOU 2049  CE2 PHE A 608     4680   6299   7847   -730   1295  -2267       C
ATOM   2050  CZ  PHE A 608     -69.921  -0.901 -50.708  1.00 48.02           C
ANISOU 2050  CZ  PHE A 608     4414   6182   7649   -799   1116  -2536       C
ATOM   2051  N   GLY A 609     -66.692  -6.194 -46.732  1.00 51.94           N
ANISOU 2051  N   GLY A 609     5334   5456   8945  -1157   2521  -1938       N
ATOM   2052  CA  GLY A 609     -65.696  -6.872 -45.921  1.00 52.97           C
ANISOU 2052  CA  GLY A 609     5623   5382   9122  -1109   2753  -1733       C
ATOM   2053  C   GLY A 609     -65.194  -8.174 -46.514  1.00 59.66           C
ANISOU 2053  C   GLY A 609     6578   6005  10083  -1200   2876  -1846       C
ATOM   2054  O   GLY A 609     -65.317  -8.420 -47.713  1.00 61.24           O
ANISOU 2054  O   GLY A 609     6781   6229  10260  -1269   2754  -2078       O
ATOM   2055  N   SER A 610     -64.631  -9.022 -45.663  1.00 63.81           N
ANISOU 2055  N   SER A 610     7207   6309  10729  -1190   3120  -1682       N
ATOM   2056  CA  SER A 610     -63.983 -10.236 -46.139  1.00 69.21           C
ANISOU 2056  CA  SER A 610     8025   6758  11513  -1241   3255  -1755       C
ATOM   2057  C   SER A 610     -64.988 -11.339 -46.476  1.00 72.53           C
ANISOU 2057  C   SER A 610     8344   7009  12206  -1473   3349  -1987       C
ATOM   2058  O   SER A 610     -64.611 -12.502 -46.628  1.00 72.41           O
ANISOU 2058  O   SER A 610     8435   6742  12335  -1538   3517  -2035       O
ATOM   2059  CB  SER A 610     -62.931 -10.731 -45.137  1.00 67.70           C
ANISOU 2059  CB  SER A 610     7996   6388  11339  -1115   3469  -1486       C
ATOM   2060  OG  SER A 610     -63.532 -11.260 -43.969  1.00 65.17           O
ANISOU 2060  OG  SER A 610     7632   5923  11205  -1177   3679  -1359       O
ATOM   2061  N   ASN A 611     -66.261 -10.971 -46.596  1.00 71.96           N
ANISOU 2061  N   ASN A 611     8059   7068  12215  -1597   3241  -2139       N
ATOM   2062  CA  ASN A 611     -67.264 -11.904 -47.092  1.00 79.10           C
ANISOU 2062  CA  ASN A 611     8830   7846  13380  -1834   3280  -2412       C
ATOM   2063  C   ASN A 611     -67.695 -11.603 -48.526  1.00 80.98           C
ANISOU 2063  C   ASN A 611     8991   8256  13520  -1891   2996  -2728       C
ATOM   2064  O   ASN A 611     -68.689 -12.141 -49.014  1.00 83.46           O
ANISOU 2064  O   ASN A 611     9147   8535  14030  -2086   2954  -2994       O
ATOM   2065  CB  ASN A 611     -68.470 -11.977 -46.160  1.00 84.58           C
ANISOU 2065  CB  ASN A 611     9320   8528  14289  -1951   3394  -2378       C
ATOM   2066  CG  ASN A 611     -68.608 -13.336 -45.501  1.00 91.91           C
ANISOU 2066  CG  ASN A 611    10333   9201  15389  -1977   3632  -2302       C
ATOM   2067  OD1 ASN A 611     -69.093 -14.291 -46.113  1.00 97.05           O
ANISOU 2067  OD1 ASN A 611    10937   9742  16197  -2118   3648  -2517       O
ATOM   2068  ND2 ASN A 611     -68.175 -13.434 -44.249  1.00 91.62           N
ANISOU 2068  ND2 ASN A 611    10426   9075  15310  -1832   3808  -1999       N
ATOM   2069  N   VAL A 612     -66.937 -10.740 -49.194  1.00 78.26           N
ANISOU 2069  N   VAL A 612     8765   8098  12874  -1718   2804  -2697       N
ATOM   2070  CA  VAL A 612     -67.107 -10.516 -50.623  1.00 80.56           C
ANISOU 2070  CA  VAL A 612     9056   8534  13018  -1732   2551  -2971       C
ATOM   2071  C   VAL A 612     -66.366 -11.623 -51.375  1.00 88.37           C
ANISOU 2071  C   VAL A 612    10227   9311  14039  -1777   2646  -3108       C
ATOM   2072  O   VAL A 612     -65.375 -12.162 -50.880  1.00 91.71           O
ANISOU 2072  O   VAL A 612    10815   9542  14490  -1709   2858  -2927       O
ATOM   2073  CB  VAL A 612     -66.573  -9.125 -51.039  1.00 75.72           C
ANISOU 2073  CB  VAL A 612     8518   8191  12062  -1523   2335  -2864       C
ATOM   2074  CG1 VAL A 612     -66.711  -8.900 -52.539  1.00 74.35           C
ANISOU 2074  CG1 VAL A 612     8380   8166  11703  -1515   2084  -3129       C
ATOM   2075  CG2 VAL A 612     -67.310  -8.039 -50.282  1.00 74.14           C
ANISOU 2075  CG2 VAL A 612     8148   8183  11838  -1470   2247  -2736       C
ATOM   2076  N   THR A 613     -66.866 -11.979 -52.555  1.00 90.46           N
ANISOU 2076  N   THR A 613    10461   9609  14302  -1883   2487  -3436       N
ATOM   2077  CA  THR A 613     -66.210 -12.961 -53.410  1.00 90.47           C
ANISOU 2077  CA  THR A 613    10644   9429  14303  -1917   2551  -3607       C
ATOM   2078  C   THR A 613     -65.254 -12.280 -54.394  1.00 90.57           C
ANISOU 2078  C   THR A 613    10846   9606  13959  -1725   2401  -3601       C
ATOM   2079  O   THR A 613     -64.337 -11.574 -53.977  1.00 90.24           O
ANISOU 2079  O   THR A 613    10907   9633  13748  -1546   2446  -3328       O
ATOM   2080  CB  THR A 613     -67.247 -13.786 -54.182  1.00 92.81           C
ANISOU 2080  CB  THR A 613    10815   9676  14772  -2127   2454  -3970       C
ATOM   2081  OG1 THR A 613     -68.145 -12.898 -54.860  1.00 95.88           O
ANISOU 2081  OG1 THR A 613    11048  10346  15037  -2140   2145  -4172       O
ATOM   2082  CG2 THR A 613     -68.045 -14.659 -53.225  1.00 90.00           C
ANISOU 2082  CG2 THR A 613    10292   9155  14749  -2283   2646  -3903       C
ATOM   2083  N   ASP A 614     -65.492 -12.514 -55.685  1.00 92.51           N
ANISOU 2083  N   ASP A 614    11138   9912  14100  -1770   2231  -3909       N
ATOM   2084  CA  ASP A 614     -64.750 -11.938 -56.824  1.00 91.78           C
ANISOU 2084  CA  ASP A 614    11232   9982  13657  -1606   2082  -3959       C
ATOM   2085  C   ASP A 614     -63.513 -11.075 -56.529  1.00 86.17           C
ANISOU 2085  C   ASP A 614    10670   9351  12719  -1385   2151  -3636       C
ATOM   2086  O   ASP A 614     -62.380 -11.499 -56.782  1.00 87.97           O
ANISOU 2086  O   ASP A 614    11088   9455  12881  -1299   2301  -3574       O
ATOM   2087  CB  ASP A 614     -65.711 -11.149 -57.723  1.00 93.67           C
ANISOU 2087  CB  ASP A 614    11368  10505  13716  -1605   1749  -4176       C
ATOM   2088  CG  ASP A 614     -65.312 -11.194 -59.186  1.00 94.78           C
ANISOU 2088  CG  ASP A 614    11706  10730  13578  -1530   1606  -4397       C
ATOM   2089  OD1 ASP A 614     -64.096 -11.232 -59.477  1.00 95.93           O
ANISOU 2089  OD1 ASP A 614    12075  10814  13560  -1399   1737  -4277       O
ATOM   2090  OD2 ASP A 614     -66.218 -11.197 -60.047  1.00 95.50           O
ANISOU 2090  OD2 ASP A 614    11723  10952  13611  -1596   1363  -4697       O
ATOM   2091  N   CYS A 615     -63.760  -9.867 -56.022  1.00 78.69           N
ANISOU 2091  N   CYS A 615     9625   8610  11665  -1295   2037  -3448       N
ATOM   2092  CA  CYS A 615     -62.723  -8.879 -55.698  1.00 78.18           C
ANISOU 2092  CA  CYS A 615     9665   8643  11396  -1101   2069  -3152       C
ATOM   2093  C   CYS A 615     -62.115  -8.172 -56.911  1.00 79.70           C
ANISOU 2093  C   CYS A 615    10025   9003  11252   -960   1932  -3198       C
ATOM   2094  O   CYS A 615     -61.379  -7.194 -56.765  1.00 74.53           O
ANISOU 2094  O   CYS A 615     9440   8457  10421   -811   1928  -2975       O
ATOM   2095  CB  CYS A 615     -61.625  -9.467 -54.804  1.00 78.56           C
ANISOU 2095  CB  CYS A 615     9802   8473  11574  -1054   2345  -2922       C
ATOM   2096  SG  CYS A 615     -61.844  -9.126 -53.050  1.00 94.35           S
ANISOU 2096  SG  CYS A 615    11658  10439  13754  -1049   2459  -2624       S
ATOM   2097  N   SER A 616     -62.420  -8.664 -58.106  1.00 85.92           N
ANISOU 2097  N   SER A 616    10886   9807  11952  -1008   1826  -3489       N
ATOM   2098  CA  SER A 616     -62.011  -7.980 -59.326  1.00 85.59           C
ANISOU 2098  CA  SER A 616    11013   9942  11566   -873   1684  -3550       C
ATOM   2099  C   SER A 616     -63.167  -7.108 -59.797  1.00 85.42           C
ANISOU 2099  C   SER A 616    10882  10169  11403   -864   1382  -3673       C
ATOM   2100  O   SER A 616     -63.009  -5.904 -60.009  1.00 86.71           O
ANISOU 2100  O   SER A 616    11094  10521  11329   -720   1265  -3530       O
ATOM   2101  CB  SER A 616     -61.610  -8.984 -60.408  1.00 85.24           C
ANISOU 2101  CB  SER A 616    11144   9784  11460   -899   1739  -3799       C
ATOM   2102  N   GLY A 617     -64.336  -7.723 -59.942  1.00 84.33           N
ANISOU 2102  N   GLY A 617    10589  10023  11430  -1019   1260  -3939       N
ATOM   2103  CA  GLY A 617     -65.537  -6.995 -60.293  1.00 87.71           C
ANISOU 2103  CA  GLY A 617    10867  10684  11775  -1017    965  -4073       C
ATOM   2104  C   GLY A 617     -66.069  -6.233 -59.097  1.00 90.19           C
ANISOU 2104  C   GLY A 617    10973  11065  12231  -1015    961  -3856       C
ATOM   2105  O   GLY A 617     -66.399  -5.050 -59.196  1.00 95.11           O
ANISOU 2105  O   GLY A 617    11564  11900  12673   -890    781  -3765       O
ATOM   2106  N   ASN A 618     -66.148  -6.915 -57.959  1.00 86.86           N
ANISOU 2106  N   ASN A 618    10424  10451  12126  -1142   1171  -3767       N
ATOM   2107  CA  ASN A 618     -66.639  -6.300 -56.732  1.00 81.62           C
ANISOU 2107  CA  ASN A 618     9574   9830  11609  -1144   1204  -3562       C
ATOM   2108  C   ASN A 618     -65.539  -5.539 -55.982  1.00 78.19           C
ANISOU 2108  C   ASN A 618     9260   9385  11065   -991   1346  -3208       C
ATOM   2109  O   ASN A 618     -64.353  -5.816 -56.163  1.00 76.54           O
ANISOU 2109  O   ASN A 618     9243   9067  10771   -927   1492  -3111       O
ATOM   2110  CB  ASN A 618     -67.268  -7.364 -55.830  1.00 81.80           C
ANISOU 2110  CB  ASN A 618     9416   9654  12012  -1347   1377  -3620       C
ATOM   2111  N   PHE A 619     -65.935  -4.577 -55.149  1.00 75.98           N
ANISOU 2111  N   PHE A 619     8857   9219  10793   -929   1299  -3029       N
ATOM   2112  CA  PHE A 619     -64.980  -3.836 -54.320  1.00 67.36           C
ANISOU 2112  CA  PHE A 619     7855   8115   9624   -798   1419  -2710       C
ATOM   2113  C   PHE A 619     -64.796  -4.495 -52.958  1.00 62.33           C
ANISOU 2113  C   PHE A 619     7151   7288   9245   -871   1664  -2552       C
ATOM   2114  O   PHE A 619     -65.767  -4.776 -52.253  1.00 63.20           O
ANISOU 2114  O   PHE A 619     7075   7373   9565   -978   1693  -2590       O
ATOM   2115  CB  PHE A 619     -65.411  -2.379 -54.135  1.00 61.46           C
ANISOU 2115  CB  PHE A 619     7045   7582   8724   -673   1242  -2593       C
ATOM   2116  CG  PHE A 619     -64.661  -1.657 -53.046  1.00 56.93           C
ANISOU 2116  CG  PHE A 619     6512   6985   8135   -572   1362  -2289       C
ATOM   2117  CD1 PHE A 619     -63.361  -1.226 -53.251  1.00 51.89           C
ANISOU 2117  CD1 PHE A 619     6065   6326   7326   -456   1425  -2128       C
ATOM   2118  CD2 PHE A 619     -65.257  -1.408 -51.817  1.00 55.56           C
ANISOU 2118  CD2 PHE A 619     6180   6811   8118   -592   1413  -2175       C
ATOM   2119  CE1 PHE A 619     -62.670  -0.563 -52.255  1.00 51.49           C
ANISOU 2119  CE1 PHE A 619     6037   6256   7270   -371   1515  -1874       C
ATOM   2120  CE2 PHE A 619     -64.568  -0.742 -50.814  1.00 51.93           C
ANISOU 2120  CE2 PHE A 619     5768   6335   7629   -494   1507  -1916       C
ATOM   2121  CZ  PHE A 619     -63.274  -0.317 -51.036  1.00 51.11           C
ANISOU 2121  CZ  PHE A 619     5846   6211   7362   -386   1546  -1772       C
ATOM   2122  N   CYS A 620     -63.544  -4.739 -52.593  1.00 59.35           N
ANISOU 2122  N   CYS A 620     6924   6779   8847   -805   1843  -2372       N
ATOM   2123  CA  CYS A 620     -63.240  -5.353 -51.309  1.00 54.80           C
ANISOU 2123  CA  CYS A 620     6320   6023   8478   -839   2071  -2200       C
ATOM   2124  C   CYS A 620     -62.486  -4.375 -50.419  1.00 46.48           C
ANISOU 2124  C   CYS A 620     5310   5029   7321   -690   2101  -1914       C
ATOM   2125  O   CYS A 620     -61.415  -3.894 -50.779  1.00 41.09           O
ANISOU 2125  O   CYS A 620     4764   4380   6470   -574   2092  -1815       O
ATOM   2126  CB  CYS A 620     -62.442  -6.639 -51.507  1.00 54.61           C
ANISOU 2126  CB  CYS A 620     6422   5768   8560   -886   2264  -2241       C
ATOM   2127  SG  CYS A 620     -63.336  -7.878 -52.461  1.00 79.58           S
ANISOU 2127  SG  CYS A 620     9536   8823  11877  -1082   2243  -2599       S
ATOM   2128  N   LEU A 621     -63.063  -4.079 -49.257  1.00 41.64           N
ANISOU 2128  N   LEU A 621     4577   4430   6813   -697   2140  -1791       N
ATOM   2129  CA  LEU A 621     -62.476  -3.112 -48.345  1.00 39.86           C
ANISOU 2129  CA  LEU A 621     4383   4270   6492   -560   2147  -1544       C
ATOM   2130  C   LEU A 621     -61.138  -3.580 -47.762  1.00 43.07           C
ANISOU 2130  C   LEU A 621     4920   4528   6918   -487   2322  -1363       C
ATOM   2131  O   LEU A 621     -60.268  -2.761 -47.471  1.00 38.14           O
ANISOU 2131  O   LEU A 621     4362   3966   6163   -361   2292  -1201       O
ATOM   2132  CB  LEU A 621     -63.459  -2.776 -47.226  1.00 39.66           C
ANISOU 2132  CB  LEU A 621     4207   4288   6573   -581   2163  -1473       C
ATOM   2133  CG  LEU A 621     -63.048  -1.637 -46.296  1.00 36.36           C
ANISOU 2133  CG  LEU A 621     3813   3963   6039   -439   2134  -1252       C
ATOM   2134  CD1 LEU A 621     -62.634  -0.405 -47.097  1.00 37.82           C
ANISOU 2134  CD1 LEU A 621     4065   4309   5995   -331   1942  -1247       C
ATOM   2135  CD2 LEU A 621     -64.177  -1.306 -45.331  1.00 36.66           C
ANISOU 2135  CD2 LEU A 621     3699   4059   6172   -460   2146  -1220       C
ATOM   2136  N   PHE A 622     -60.963  -4.890 -47.601  1.00 41.83           N
ANISOU 2136  N   PHE A 622     4794   4169   6929   -563   2499  -1396       N
ATOM   2137  CA  PHE A 622     -59.778  -5.388 -46.911  1.00 39.22           C
ANISOU 2137  CA  PHE A 622     4572   3694   6636   -476   2666  -1213       C
ATOM   2138  C   PHE A 622     -58.767  -6.078 -47.830  1.00 47.40           C
ANISOU 2138  C   PHE A 622     5735   4626   7649   -456   2729  -1283       C
ATOM   2139  O   PHE A 622     -57.994  -6.936 -47.394  1.00 44.65           O
ANISOU 2139  O   PHE A 622     5462   4105   7400   -418   2897  -1193       O
ATOM   2140  CB  PHE A 622     -60.185  -6.285 -45.747  1.00 39.43           C
ANISOU 2140  CB  PHE A 622     4565   3551   6866   -529   2854  -1125       C
ATOM   2141  CG  PHE A 622     -61.103  -5.610 -44.770  1.00 38.83           C
ANISOU 2141  CG  PHE A 622     4373   3575   6805   -532   2823  -1040       C
ATOM   2142  CD1 PHE A 622     -60.836  -4.324 -44.329  1.00 38.28           C
ANISOU 2142  CD1 PHE A 622     4298   3677   6569   -407   2699   -907       C
ATOM   2143  CD2 PHE A 622     -62.248  -6.249 -44.317  1.00 44.43           C
ANISOU 2143  CD2 PHE A 622     4976   4203   7703   -666   2928  -1103       C
ATOM   2144  CE1 PHE A 622     -61.684  -3.693 -43.439  1.00 39.11           C
ANISOU 2144  CE1 PHE A 622     4306   3873   6680   -398   2677   -839       C
ATOM   2145  CE2 PHE A 622     -63.095  -5.622 -43.422  1.00 43.78           C
ANISOU 2145  CE2 PHE A 622     4783   4217   7634   -660   2919  -1025       C
ATOM   2146  CZ  PHE A 622     -62.812  -4.339 -42.989  1.00 43.41           C
ANISOU 2146  CZ  PHE A 622     4744   4347   7404   -518   2791   -896       C
ATOM   2147  N   ARG A 623     -58.770  -5.687 -49.100  1.00 51.86           N
ANISOU 2147  N   ARG A 623     6332   5300   8073   -466   2597  -1440       N
ATOM   2148  CA  ARG A 623     -57.748  -6.144 -50.035  1.00 54.82           C
ANISOU 2148  CA  ARG A 623     6837   5608   8383   -423   2654  -1500       C
ATOM   2149  C   ARG A 623     -57.132  -4.959 -50.777  1.00 58.34           C
ANISOU 2149  C   ARG A 623     7340   6234   8592   -321   2524  -1465       C
ATOM   2150  O   ARG A 623     -57.795  -3.944 -50.985  1.00 61.97           O
ANISOU 2150  O   ARG A 623     7749   6866   8932   -318   2356  -1486       O
ATOM   2151  CB  ARG A 623     -58.322  -7.171 -51.014  1.00 56.97           C
ANISOU 2151  CB  ARG A 623     7134   5784   8728   -550   2673  -1764       C
ATOM   2152  CG  ARG A 623     -58.799  -8.483 -50.368  1.00 63.91           C
ANISOU 2152  CG  ARG A 623     7979   6434   9869   -665   2842  -1804       C
ATOM   2153  CD  ARG A 623     -57.664  -9.283 -49.699  1.00 69.80           C
ANISOU 2153  CD  ARG A 623     8823   6977  10720   -578   3058  -1636       C
ATOM   2154  NE  ARG A 623     -56.332  -8.889 -50.163  1.00 74.30           N
ANISOU 2154  NE  ARG A 623     9494   7598  11137   -430   3061  -1553       N
ATOM   2155  CZ  ARG A 623     -55.193  -9.451 -49.765  1.00 73.67           C
ANISOU 2155  CZ  ARG A 623     9490   7388  11113   -328   3203  -1408       C
ATOM   2156  NH1 ARG A 623     -54.036  -9.008 -50.248  1.00 72.61           N
ANISOU 2156  NH1 ARG A 623     9412   7345  10831   -218   3150  -1317       N
ATOM   2157  NH2 ARG A 623     -55.208 -10.455 -48.894  1.00 68.20           N
ANISOU 2157  NH2 ARG A 623     8808   6499  10606   -347   3349  -1315       N
ATOM   2158  N   SER A 624     -55.866  -5.089 -51.168  1.00 59.51           N
ANISOU 2158  N   SER A 624     7592   6335   8683   -233   2614  -1407       N
ATOM   2159  CA  SER A 624     -55.134  -3.980 -51.783  1.00 57.85           C
ANISOU 2159  CA  SER A 624     7439   6270   8272   -137   2536  -1343       C
ATOM   2160  C   SER A 624     -53.822  -4.441 -52.416  1.00 65.04           C
ANISOU 2160  C   SER A 624     8456   7100   9155    -67   2676  -1335       C
ATOM   2161  O   SER A 624     -52.834  -3.691 -52.432  1.00 67.05           O
ANISOU 2161  O   SER A 624     8732   7421   9325     25   2680  -1194       O
ATOM   2162  CB  SER A 624     -54.815  -2.916 -50.730  1.00 48.45           C
ANISOU 2162  CB  SER A 624     6183   5164   7063    -59   2487  -1123       C
ATOM   2163  OG  SER A 624     -53.524  -3.119 -50.161  1.00 42.13           O
ANISOU 2163  OG  SER A 624     5401   4282   6326     31   2613   -967       O
ATOM   2164  N   GLU A 625     -53.831  -5.657 -52.958  1.00 64.36           N
ANISOU 2164  N   GLU A 625     8432   6873   9147   -116   2783  -1489       N
ATOM   2165  CA  GLU A 625     -52.605  -6.378 -53.325  1.00 69.31           C
ANISOU 2165  CA  GLU A 625     9138   7404   9791    -60   2881  -1429       C
ATOM   2166  C   GLU A 625     -51.789  -6.684 -52.059  1.00 69.26           C
ANISOU 2166  C   GLU A 625     9074   7310   9932      2   2942  -1192       C
ATOM   2167  O   GLU A 625     -52.191  -7.499 -51.219  1.00 73.58           O
ANISOU 2167  O   GLU A 625     9589   7721  10646    -37   3011  -1169       O
ATOM   2168  CB  GLU A 625     -51.738  -5.629 -54.367  1.00 67.56           C
ANISOU 2168  CB  GLU A 625     8996   7305   9366     17   2850  -1409       C
ATOM   2169  CG  GLU A 625     -52.491  -4.769 -55.405  1.00 72.61           C
ANISOU 2169  CG  GLU A 625     9700   8097   9791      0   2749  -1569       C
ATOM   2170  CD  GLU A 625     -53.112  -5.572 -56.543  1.00 83.68           C
ANISOU 2170  CD  GLU A 625    11203   9463  11129    -64   2743  -1842       C
ATOM   2171  OE1 GLU A 625     -53.128  -6.819 -56.464  1.00 86.60           O
ANISOU 2171  OE1 GLU A 625    11579   9675  11651   -117   2823  -1920       O
ATOM   2172  OE2 GLU A 625     -53.582  -4.952 -57.524  1.00 86.77           O
ANISOU 2172  OE2 GLU A 625    11674   9988  11308    -58   2638  -1970       O
ATOM   2173  N   THR A 626     -50.656  -6.005 -51.915  1.00 59.18           N
ANISOU 2173  N   THR A 626     7786   6108   8591     99   2913  -1022       N
ATOM   2174  CA  THR A 626     -49.714  -6.307 -50.848  1.00 50.68           C
ANISOU 2174  CA  THR A 626     6665   4961   7630    176   2947   -823       C
ATOM   2175  C   THR A 626     -49.350  -5.074 -50.036  1.00 50.30           C
ANISOU 2175  C   THR A 626     6538   5040   7533    237   2837   -654       C
ATOM   2176  O   THR A 626     -48.458  -5.135 -49.187  1.00 52.53           O
ANISOU 2176  O   THR A 626     6779   5296   7883    316   2836   -498       O
ATOM   2177  CB  THR A 626     -48.401  -6.869 -51.442  1.00 52.23           C
ANISOU 2177  CB  THR A 626     6906   5104   7834    245   3027   -796       C
ATOM   2178  OG1 THR A 626     -47.753  -5.851 -52.223  1.00 47.38           O
ANISOU 2178  OG1 THR A 626     6298   4628   7075    281   2978   -781       O
ATOM   2179  CG2 THR A 626     -48.688  -8.088 -52.322  1.00 49.09           C
ANISOU 2179  CG2 THR A 626     6601   4579   7473    191   3134   -973       C
ATOM   2180  N   LYS A 627     -50.030  -3.958 -50.299  1.00 46.18           N
ANISOU 2180  N   LYS A 627     5998   4655   6892    207   2741   -694       N
ATOM   2181  CA  LYS A 627     -49.620  -2.666 -49.745  1.00 44.88           C
ANISOU 2181  CA  LYS A 627     5774   4614   6665    259   2637   -555       C
ATOM   2182  C   LYS A 627     -50.328  -2.237 -48.450  1.00 45.42           C
ANISOU 2182  C   LYS A 627     5772   4710   6774    261   2562   -469       C
ATOM   2183  O   LYS A 627     -49.969  -1.211 -47.869  1.00 44.56           O
ANISOU 2183  O   LYS A 627     5616   4690   6624    307   2474   -359       O
ATOM   2184  CB  LYS A 627     -49.765  -1.566 -50.801  1.00 47.67           C
ANISOU 2184  CB  LYS A 627     6166   5098   6850    247   2586   -620       C
ATOM   2185  CG  LYS A 627     -48.635  -1.507 -51.825  1.00 48.34           C
ANISOU 2185  CG  LYS A 627     6307   5191   6870    282   2646   -619       C
ATOM   2186  CD  LYS A 627     -49.083  -0.779 -53.089  1.00 55.34           C
ANISOU 2186  CD  LYS A 627     7284   6175   7566    263   2634   -726       C
ATOM   2187  CE  LYS A 627     -47.897  -0.452 -53.989  1.00 59.65           C
ANISOU 2187  CE  LYS A 627     7882   6746   8038    304   2699   -683       C
ATOM   2188  NZ  LYS A 627     -46.972  -1.616 -54.155  1.00 61.72           N
ANISOU 2188  NZ  LYS A 627     8146   6900   8403    327   2803   -686       N
ATOM   2189  N   ASP A 628     -51.319  -3.011 -48.006  1.00 38.08           N
ANISOU 2189  N   ASP A 628     4837   3701   5932    207   2608   -525       N
ATOM   2190  CA  ASP A 628     -52.046  -2.696 -46.774  1.00 40.34           C
ANISOU 2190  CA  ASP A 628     5062   4009   6255    210   2561   -442       C
ATOM   2191  C   ASP A 628     -52.670  -1.310 -46.842  1.00 39.66           C
ANISOU 2191  C   ASP A 628     4934   4083   6051    204   2441   -455       C
ATOM   2192  O   ASP A 628     -52.575  -0.536 -45.892  1.00 39.30           O
ANISOU 2192  O   ASP A 628     4849   4101   5984    256   2362   -334       O
ATOM   2193  CB  ASP A 628     -51.129  -2.786 -45.546  1.00 37.92           C
ANISOU 2193  CB  ASP A 628     4741   3665   6001    308   2551   -256       C
ATOM   2194  CG  ASP A 628     -50.649  -4.199 -45.275  1.00 43.37           C
ANISOU 2194  CG  ASP A 628     5475   4184   6818    333   2681   -223       C
ATOM   2195  OD1 ASP A 628     -51.427  -5.150 -45.514  1.00 46.14           O
ANISOU 2195  OD1 ASP A 628     5857   4420   7254    257   2787   -320       O
ATOM   2196  OD2 ASP A 628     -49.495  -4.358 -44.815  1.00 45.48           O
ANISOU 2196  OD2 ASP A 628     5741   4428   7111    431   2684   -106       O
ATOM   2197  N   LEU A 629     -53.292  -1.004 -47.977  1.00 31.32           N
ANISOU 2197  N   LEU A 629     3898   3090   4912    151   2431   -611       N
ATOM   2198  CA  LEU A 629     -53.905   0.288 -48.195  1.00 36.52           C
ANISOU 2198  CA  LEU A 629     4537   3899   5442    150   2289   -621       C
ATOM   2199  C   LEU A 629     -55.155   0.413 -47.333  1.00 36.56           C
ANISOU 2199  C   LEU A 629     4463   3935   5492    112   2221   -623       C
ATOM   2200  O   LEU A 629     -56.017  -0.459 -47.363  1.00 33.65           O
ANISOU 2200  O   LEU A 629     4065   3508   5212     32   2262   -726       O
ATOM   2201  CB  LEU A 629     -54.247   0.459 -49.677  1.00 35.08           C
ANISOU 2201  CB  LEU A 629     4423   3778   5127    110   2233   -773       C
ATOM   2202  CG  LEU A 629     -53.075   0.304 -50.658  1.00 38.16           C
ANISOU 2202  CG  LEU A 629     4906   4139   5456    147   2327   -785       C
ATOM   2203  CD1 LEU A 629     -53.551   0.410 -52.102  1.00 36.17           C
ANISOU 2203  CD1 LEU A 629     4745   3953   5044    116   2269   -945       C
ATOM   2204  CD2 LEU A 629     -51.974   1.331 -50.375  1.00 33.67           C
ANISOU 2204  CD2 LEU A 629     4332   3615   4846    223   2328   -625       C
ATOM   2205  N   LEU A 630     -55.223   1.502 -46.573  1.00 39.21           N
ANISOU 2205  N   LEU A 630     4763   4359   5776    167   2129   -513       N
ATOM   2206  CA  LEU A 630     -56.285   1.786 -45.599  1.00 38.67           C
ANISOU 2206  CA  LEU A 630     4621   4332   5741    158   2077   -487       C
ATOM   2207  C   LEU A 630     -56.318   0.824 -44.400  1.00 37.67           C
ANISOU 2207  C   LEU A 630     4467   4092   5753    162   2207   -409       C
ATOM   2208  O   LEU A 630     -56.319   1.263 -43.249  1.00 36.47           O
ANISOU 2208  O   LEU A 630     4294   3963   5598    225   2194   -290       O
ATOM   2209  CB  LEU A 630     -57.661   1.887 -46.268  1.00 35.66           C
ANISOU 2209  CB  LEU A 630     4191   4025   5334     82   1987   -640       C
ATOM   2210  CG  LEU A 630     -57.742   2.836 -47.470  1.00 34.94           C
ANISOU 2210  CG  LEU A 630     4147   4049   5079    100   1849   -712       C
ATOM   2211  CD1 LEU A 630     -59.117   2.729 -48.130  1.00 35.71           C
ANISOU 2211  CD1 LEU A 630     4183   4220   5164     35   1749   -882       C
ATOM   2212  CD2 LEU A 630     -57.449   4.272 -47.064  1.00 28.42           C
ANISOU 2212  CD2 LEU A 630     3337   3310   4150    188   1749   -590       C
ATOM   2213  N   PHE A 631     -56.353  -0.478 -44.673  1.00 34.29           N
ANISOU 2213  N   PHE A 631     4054   3536   5438    100   2336   -476       N
ATOM   2214  CA  PHE A 631     -56.312  -1.494 -43.626  1.00 36.04           C
ANISOU 2214  CA  PHE A 631     4286   3622   5784    105   2457   -384       C
ATOM   2215  C   PHE A 631     -55.289  -2.559 -43.974  1.00 41.58           C
ANISOU 2215  C   PHE A 631     5065   4182   6550    119   2554   -371       C
ATOM   2216  O   PHE A 631     -54.910  -2.697 -45.136  1.00 44.99           O
ANISOU 2216  O   PHE A 631     5527   4611   6955     94   2564   -481       O
ATOM   2217  CB  PHE A 631     -57.674  -2.167 -43.477  1.00 32.17           C
ANISOU 2217  CB  PHE A 631     3726   3080   5416     -5   2546   -484       C
ATOM   2218  CG  PHE A 631     -58.789  -1.214 -43.222  1.00 33.17           C
ANISOU 2218  CG  PHE A 631     3763   3350   5491    -26   2429   -512       C
ATOM   2219  CD1 PHE A 631     -59.078  -0.804 -41.932  1.00 31.33           C
ANISOU 2219  CD1 PHE A 631     3508   3145   5249     34   2437   -377       C
ATOM   2220  CD2 PHE A 631     -59.553  -0.724 -44.273  1.00 32.03           C
ANISOU 2220  CD2 PHE A 631     3565   3314   5291    -92   2296   -674       C
ATOM   2221  CE1 PHE A 631     -60.116   0.079 -41.690  1.00 39.29           C
ANISOU 2221  CE1 PHE A 631     4426   4283   6219     28   2353   -409       C
ATOM   2222  CE2 PHE A 631     -60.582   0.156 -44.040  1.00 33.07           C
ANISOU 2222  CE2 PHE A 631     3604   3578   5382    -93   2185   -699       C
ATOM   2223  CZ  PHE A 631     -60.871   0.556 -42.748  1.00 37.10           C
ANISOU 2223  CZ  PHE A 631     4081   4110   5905    -35   2221   -569       C
ATOM   2224  N   ARG A 632     -54.848  -3.313 -42.969  1.00 36.22           N
ANISOU 2224  N   ARG A 632     4429   3385   5948    173   2633   -237       N
ATOM   2225  CA  ARG A 632     -53.950  -4.428 -43.214  1.00 39.89           C
ANISOU 2225  CA  ARG A 632     4964   3698   6496    198   2744   -220       C
ATOM   2226  C   ARG A 632     -54.655  -5.443 -44.113  1.00 40.81           C
ANISOU 2226  C   ARG A 632     5088   3694   6725     73   2872   -402       C
ATOM   2227  O   ARG A 632     -55.852  -5.664 -43.977  1.00 37.37           O
ANISOU 2227  O   ARG A 632     4598   3235   6365    -26   2925   -486       O
ATOM   2228  CB  ARG A 632     -53.498  -5.061 -41.896  1.00 41.20           C
ANISOU 2228  CB  ARG A 632     5178   3755   6723    295   2822    -41       C
ATOM   2229  CG  ARG A 632     -52.245  -4.419 -41.293  1.00 33.94           C
ANISOU 2229  CG  ARG A 632     4263   2916   5716    440   2722    106       C
ATOM   2230  CD  ARG A 632     -51.920  -4.963 -39.911  1.00 33.38           C
ANISOU 2230  CD  ARG A 632     4241   2762   5680    557   2793    280       C
ATOM   2231  NE  ARG A 632     -51.988  -6.423 -39.845  1.00 35.08           N
ANISOU 2231  NE  ARG A 632     4529   2768   6033    546   2983    297       N
ATOM   2232  CZ  ARG A 632     -51.413  -7.152 -38.897  1.00 36.11           C
ANISOU 2232  CZ  ARG A 632     4727   2793   6202    671   3078    454       C
ATOM   2233  NH1 ARG A 632     -50.691  -6.566 -37.948  1.00 36.63           N
ANISOU 2233  NH1 ARG A 632     4789   2958   6173    823   2986    594       N
ATOM   2234  NH2 ARG A 632     -51.550  -8.469 -38.907  1.00 39.58           N
ANISOU 2234  NH2 ARG A 632     5241   3025   6772    651   3268    467       N
ATOM   2235  N   ASP A 633     -53.917  -6.040 -45.043  1.00 40.54           N
ANISOU 2235  N   ASP A 633     5110   3586   6706     72   2922   -476       N
ATOM   2236  CA  ASP A 633     -54.528  -6.952 -46.015  1.00 46.34           C
ANISOU 2236  CA  ASP A 633     5863   4210   7534    -46   3030   -686       C
ATOM   2237  C   ASP A 633     -55.044  -8.243 -45.388  1.00 43.18           C
ANISOU 2237  C   ASP A 633     5483   3592   7330   -105   3214   -686       C
ATOM   2238  O   ASP A 633     -55.917  -8.909 -45.946  1.00 46.37           O
ANISOU 2238  O   ASP A 633     5871   3900   7847   -235   3303   -881       O
ATOM   2239  CB  ASP A 633     -53.557  -7.265 -47.160  1.00 48.18           C
ANISOU 2239  CB  ASP A 633     6170   4422   7715    -20   3035   -761       C
ATOM   2240  CG  ASP A 633     -53.345  -6.074 -48.082  1.00 49.00           C
ANISOU 2240  CG  ASP A 633     6263   4719   7635     -1   2896   -821       C
ATOM   2241  OD1 ASP A 633     -54.324  -5.328 -48.337  1.00 46.73           O
ANISOU 2241  OD1 ASP A 633     5921   4549   7283    -55   2820   -923       O
ATOM   2242  OD2 ASP A 633     -52.199  -5.879 -48.543  1.00 44.07           O
ANISOU 2242  OD2 ASP A 633     5682   4127   6937     74   2874   -762       O
ATOM   2243  N   ASP A 634     -54.503  -8.595 -44.229  1.00 43.74           N
ANISOU 2243  N   ASP A 634     5597   3577   7444     -8   3274   -474       N
ATOM   2244  CA  ASP A 634     -54.960  -9.780 -43.514  1.00 46.02           C
ANISOU 2244  CA  ASP A 634     5927   3644   7915    -46   3474   -433       C
ATOM   2245  C   ASP A 634     -56.059  -9.461 -42.494  1.00 47.37           C
ANISOU 2245  C   ASP A 634     6035   3843   8119    -89   3499   -368       C
ATOM   2246  O   ASP A 634     -56.350 -10.277 -41.611  1.00 46.22           O
ANISOU 2246  O   ASP A 634     5937   3526   8099    -88   3667   -267       O
ATOM   2247  CB  ASP A 634     -53.782 -10.516 -42.859  1.00 40.79           C
ANISOU 2247  CB  ASP A 634     5366   2854   7281     94   3556   -239       C
ATOM   2248  CG  ASP A 634     -52.924  -9.611 -41.990  1.00 47.56           C
ANISOU 2248  CG  ASP A 634     6216   3861   7994    259   3416    -36       C
ATOM   2249  OD1 ASP A 634     -53.300  -8.439 -41.753  1.00 45.01           O
ANISOU 2249  OD1 ASP A 634     5824   3721   7557    261   3268    -27       O
ATOM   2250  OD2 ASP A 634     -51.862 -10.084 -41.534  1.00 51.52           O
ANISOU 2250  OD2 ASP A 634     6774   4302   8498    389   3450    107       O
ATOM   2251  N   THR A 635     -56.671  -8.281 -42.628  1.00 40.21           N
ANISOU 2251  N   THR A 635     5029   3151   7097   -122   3334   -419       N
ATOM   2252  CA  THR A 635     -57.838  -7.925 -41.811  1.00 38.81           C
ANISOU 2252  CA  THR A 635     4774   3027   6943   -180   3330   -384       C
ATOM   2253  C   THR A 635     -59.045  -8.787 -42.155  1.00 43.52           C
ANISOU 2253  C   THR A 635     5298   3498   7740   -373   3481   -556       C
ATOM   2254  O   THR A 635     -59.466  -8.851 -43.308  1.00 46.43           O
ANISOU 2254  O   THR A 635     5612   3898   8133   -492   3411   -777       O
ATOM   2255  CB  THR A 635     -58.255  -6.453 -41.992  1.00 37.11           C
ANISOU 2255  CB  THR A 635     4463   3070   6568   -171   3119   -419       C
ATOM   2256  OG1 THR A 635     -57.178  -5.590 -41.607  1.00 36.28           O
ANISOU 2256  OG1 THR A 635     4412   3076   6297    -13   2982   -267       O
ATOM   2257  CG2 THR A 635     -59.475  -6.134 -41.135  1.00 37.41           C
ANISOU 2257  CG2 THR A 635     4419   3159   6636   -221   3117   -386       C
ATOM   2258  N   VAL A 636     -59.605  -9.438 -41.143  1.00 42.07           N
ANISOU 2258  N   VAL A 636     5139   3173   7671   -397   3612   -452       N
ATOM   2259  CA  VAL A 636     -60.760 -10.307 -41.323  1.00 45.82           C
ANISOU 2259  CA  VAL A 636     5543   3508   8358   -589   3747   -600       C
ATOM   2260  C   VAL A 636     -62.041  -9.498 -41.140  1.00 46.78           C
ANISOU 2260  C   VAL A 636     5504   3805   8464   -675   3633   -668       C
ATOM   2261  O   VAL A 636     -63.019  -9.697 -41.861  1.00 49.37           O
ANISOU 2261  O   VAL A 636     5692   4142   8926   -858   3634   -885       O
ATOM   2262  CB  VAL A 636     -60.716 -11.496 -40.338  1.00 46.15           C
ANISOU 2262  CB  VAL A 636     5709   3299   8526   -544   3950   -460       C
ATOM   2263  CG1 VAL A 636     -62.012 -12.315 -40.389  1.00 48.64           C
ANISOU 2263  CG1 VAL A 636     5938   3495   9046   -729   4063   -609       C
ATOM   2264  CG2 VAL A 636     -59.519 -12.374 -40.640  1.00 46.65           C
ANISOU 2264  CG2 VAL A 636     5915   3179   8632   -463   4076   -419       C
ATOM   2265  N   CYS A 637     -62.014  -8.573 -40.181  1.00 43.18           N
ANISOU 2265  N   CYS A 637     5062   3493   7851   -539   3529   -493       N
ATOM   2266  CA  CYS A 637     -63.124  -7.662 -39.929  1.00 42.40           C
ANISOU 2266  CA  CYS A 637     4820   3577   7713   -582   3419   -534       C
ATOM   2267  C   CYS A 637     -62.686  -6.613 -38.929  1.00 40.61           C
ANISOU 2267  C   CYS A 637     4656   3495   7279   -399   3306   -329       C
ATOM   2268  O   CYS A 637     -61.625  -6.724 -38.315  1.00 41.47           O
ANISOU 2268  O   CYS A 637     4910   3548   7300   -254   3325   -157       O
ATOM   2269  CB  CYS A 637     -64.322  -8.404 -39.334  1.00 46.54           C
ANISOU 2269  CB  CYS A 637     5282   3983   8418   -696   3558   -560       C
ATOM   2270  SG  CYS A 637     -64.162  -8.716 -37.538  1.00 50.71           S
ANISOU 2270  SG  CYS A 637     5969   4406   8894   -538   3690   -270       S
ATOM   2271  N   LEU A 638     -63.518  -5.595 -38.771  1.00 45.03           N
ANISOU 2271  N   LEU A 638     5097   4241   7770   -406   3188   -361       N
ATOM   2272  CA  LEU A 638     -63.358  -4.618 -37.707  1.00 38.76           C
ANISOU 2272  CA  LEU A 638     4351   3575   6803   -255   3103   -190       C
ATOM   2273  C   LEU A 638     -64.228  -5.061 -36.533  1.00 48.42           C
ANISOU 2273  C   LEU A 638     5579   4722   8097   -265   3240    -98       C
ATOM   2274  O   LEU A 638     -65.387  -5.429 -36.713  1.00 42.02           O
ANISOU 2274  O   LEU A 638     4642   3884   7438   -404   3309   -214       O
ATOM   2275  CB  LEU A 638     -63.762  -3.237 -38.206  1.00 37.37           C
ANISOU 2275  CB  LEU A 638     4053   3633   6512   -240   2914   -279       C
ATOM   2276  CG  LEU A 638     -62.981  -2.786 -39.444  1.00 44.76           C
ANISOU 2276  CG  LEU A 638     4988   4644   7376   -229   2793   -381       C
ATOM   2277  CD1 LEU A 638     -63.663  -1.595 -40.099  1.00 48.24           C
ANISOU 2277  CD1 LEU A 638     5289   5289   7751   -237   2641   -508       C
ATOM   2278  CD2 LEU A 638     -61.536  -2.449 -39.071  1.00 37.13           C
ANISOU 2278  CD2 LEU A 638     4172   3676   6259    -74   2735   -222       C
ATOM   2279  N   ALA A 639     -63.659  -5.039 -35.336  1.00 46.59           N
ANISOU 2279  N   ALA A 639     5488   4455   7757   -117   3285    105       N
ATOM   2280  CA  ALA A 639     -64.310  -5.632 -34.186  1.00 42.08           C
ANISOU 2280  CA  ALA A 639     4965   3779   7244   -106   3453    213       C
ATOM   2281  C   ALA A 639     -64.551  -4.615 -33.080  1.00 47.50           C
ANISOU 2281  C   ALA A 639     5672   4616   7760     19   3394    333       C
ATOM   2282  O   ALA A 639     -63.813  -3.642 -32.941  1.00 39.63           O
ANISOU 2282  O   ALA A 639     4716   3755   6585    142   3245    387       O
ATOM   2283  CB  ALA A 639     -63.477  -6.770 -33.672  1.00 43.13           C
ANISOU 2283  CB  ALA A 639     5273   3697   7419    -29   3612    349       C
ATOM   2284  N   LYS A 640     -65.592  -4.859 -32.292  1.00 49.66           N
ANISOU 2284  N   LYS A 640     5916   4857   8095    -14   3522    366       N
ATOM   2285  CA  LYS A 640     -65.947  -4.010 -31.159  1.00 46.15           C
ANISOU 2285  CA  LYS A 640     5499   4537   7500    101   3507    474       C
ATOM   2286  C   LYS A 640     -64.866  -4.010 -30.076  1.00 48.74           C
ANISOU 2286  C   LYS A 640     6035   4828   7657    300   3532    678       C
ATOM   2287  O   LYS A 640     -64.195  -5.028 -29.845  1.00 43.76           O
ANISOU 2287  O   LYS A 640     5535   4021   7071    345   3652    773       O
ATOM   2288  CB  LYS A 640     -67.289  -4.459 -30.569  1.00 48.43           C
ANISOU 2288  CB  LYS A 640     5715   4773   7915     15   3677    466       C
ATOM   2289  CG  LYS A 640     -68.436  -4.403 -31.559  1.00 51.29           C
ANISOU 2289  CG  LYS A 640     5846   5193   8451   -172   3646    258       C
ATOM   2290  CD  LYS A 640     -69.774  -4.670 -30.889  1.00 62.43           C
ANISOU 2290  CD  LYS A 640     7162   6582   9979   -245   3805    254       C
ATOM   2291  CE  LYS A 640     -70.180  -6.135 -30.984  1.00 72.81           C
ANISOU 2291  CE  LYS A 640     8477   7660  11527   -382   4016    224       C
ATOM   2292  NZ  LYS A 640     -69.496  -7.042 -30.005  1.00 77.10           N
ANISOU 2292  NZ  LYS A 640     9252   8005  12037   -276   4198    419       N
ATOM   2293  N   LEU A 641     -64.712  -2.864 -29.415  1.00 41.75           N
ANISOU 2293  N   LEU A 641     5178   4108   6578    429   3421    737       N
ATOM   2294  CA  LEU A 641     -63.670  -2.661 -28.412  1.00 49.61           C
ANISOU 2294  CA  LEU A 641     6354   5108   7387    632   3410    909       C
ATOM   2295  C   LEU A 641     -64.186  -2.873 -26.997  1.00 52.20           C
ANISOU 2295  C   LEU A 641     6792   5397   7643    731   3568   1050       C
ATOM   2296  O   LEU A 641     -63.406  -3.080 -26.062  1.00 56.70           O
ANISOU 2296  O   LEU A 641     7539   5924   8080    907   3616   1211       O
ATOM   2297  CB  LEU A 641     -63.137  -1.236 -28.505  1.00 49.30           C
ANISOU 2297  CB  LEU A 641     6292   5270   7171    723   3193    876       C
ATOM   2298  CG  LEU A 641     -62.494  -0.792 -29.811  1.00 48.63           C
ANISOU 2298  CG  LEU A 641     6118   5248   7110    662   3021    753       C
ATOM   2299  CD1 LEU A 641     -62.023   0.609 -29.620  1.00 46.28           C
ANISOU 2299  CD1 LEU A 641     5824   5125   6635    775   2842    745       C
ATOM   2300  CD2 LEU A 641     -61.338  -1.697 -30.159  1.00 48.05           C
ANISOU 2300  CD2 LEU A 641     6132   5041   7085    690   3058    810       C
ATOM   2301  N   HIS A 642     -65.503  -2.787 -26.850  1.00 50.78           N
ANISOU 2301  N   HIS A 642     6504   5244   7546    628   3648    986       N
ATOM   2302  CA  HIS A 642     -66.164  -2.916 -25.555  1.00 52.79           C
ANISOU 2302  CA  HIS A 642     6844   5473   7741    706   3811   1103       C
ATOM   2303  C   HIS A 642     -65.635  -1.905 -24.540  1.00 54.69           C
ANISOU 2303  C   HIS A 642     7212   5851   7717    914   3722   1204       C
ATOM   2304  O   HIS A 642     -65.827  -0.702 -24.703  1.00 49.64           O
ANISOU 2304  O   HIS A 642     6487   5387   6985    927   3568   1118       O
ATOM   2305  CB  HIS A 642     -66.062  -4.350 -25.054  1.00 51.43           C
ANISOU 2305  CB  HIS A 642     6804   5070   7667    719   4040   1224       C
ATOM   2306  CG  HIS A 642     -66.571  -5.354 -26.039  1.00 61.24           C
ANISOU 2306  CG  HIS A 642     7929   6165   9175    515   4132   1107       C
ATOM   2307  ND1 HIS A 642     -65.746  -6.246 -26.692  1.00 65.93           N
ANISOU 2307  ND1 HIS A 642     8577   6609   9864    494   4151   1104       N
ATOM   2308  CD2 HIS A 642     -67.822  -5.591 -26.503  1.00 67.18           C
ANISOU 2308  CD2 HIS A 642     8505   6901  10120    326   4209    976       C
ATOM   2309  CE1 HIS A 642     -66.468  -6.998 -27.503  1.00 70.24           C
ANISOU 2309  CE1 HIS A 642     8999   7046  10645    298   4237    970       C
ATOM   2310  NE2 HIS A 642     -67.732  -6.623 -27.405  1.00 71.94           N
ANISOU 2310  NE2 HIS A 642     9067   7341  10925    192   4270    890       N
ATOM   2311  N   ASP A 643     -64.954  -2.387 -23.510  1.00 61.47           N
ANISOU 2311  N   ASP A 643     8278   6627   8450   1087   3817   1380       N
ATOM   2312  CA  ASP A 643     -64.434  -1.496 -22.480  1.00 66.05           C
ANISOU 2312  CA  ASP A 643     8997   7334   8767   1300   3736   1472       C
ATOM   2313  C   ASP A 643     -63.209  -0.713 -22.923  1.00 63.54           C
ANISOU 2313  C   ASP A 643     8691   7128   8322   1390   3510   1443       C
ATOM   2314  O   ASP A 643     -62.884   0.328 -22.348  1.00 62.35           O
ANISOU 2314  O   ASP A 643     8598   7122   7968   1529   3389   1452       O
ATOM   2315  CB  ASP A 643     -64.120  -2.281 -21.210  1.00 73.87           C
ANISOU 2315  CB  ASP A 643    10213   8211   9645   1481   3907   1668       C
ATOM   2316  CG  ASP A 643     -65.274  -2.276 -20.243  1.00 81.57           C
ANISOU 2316  CG  ASP A 643    11217   9181  10593   1490   4078   1713       C
ATOM   2317  OD1 ASP A 643     -66.377  -1.856 -20.658  1.00 80.12           O
ANISOU 2317  OD1 ASP A 643    10855   9061  10527   1330   4086   1588       O
ATOM   2318  OD2 ASP A 643     -65.080  -2.687 -19.079  1.00 88.32           O
ANISOU 2318  OD2 ASP A 643    12271   9979  11309   1665   4204   1870       O
ATOM   2319  N   ARG A 644     -62.540  -1.218 -23.953  1.00 63.49           N
ANISOU 2319  N   ARG A 644     8630   7053   8442   1308   3459   1399       N
ATOM   2320  CA  ARG A 644     -61.275  -0.653 -24.403  1.00 60.32           C
ANISOU 2320  CA  ARG A 644     8239   6734   7945   1391   3275   1383       C
ATOM   2321  C   ARG A 644     -61.468   0.443 -25.455  1.00 53.59           C
ANISOU 2321  C   ARG A 644     7210   6022   7129   1272   3086   1203       C
ATOM   2322  O   ARG A 644     -61.039   0.293 -26.601  1.00 49.31           O
ANISOU 2322  O   ARG A 644     6576   5458   6702   1169   3010   1116       O
ATOM   2323  CB  ARG A 644     -60.368  -1.775 -24.924  1.00 57.46           C
ANISOU 2323  CB  ARG A 644     7921   6220   7691   1389   3333   1439       C
ATOM   2324  CG  ARG A 644     -60.008  -2.797 -23.847  1.00 60.36           C
ANISOU 2324  CG  ARG A 644     8486   6451   7996   1556   3508   1632       C
ATOM   2325  CD  ARG A 644     -59.994  -4.236 -24.364  1.00 64.97           C
ANISOU 2325  CD  ARG A 644     9078   6813   8793   1466   3673   1652       C
ATOM   2326  NE  ARG A 644     -58.917  -4.488 -25.318  1.00 66.78           N
ANISOU 2326  NE  ARG A 644     9271   7011   9091   1456   3592   1620       N
ATOM   2327  CZ  ARG A 644     -59.105  -4.769 -26.606  1.00 66.54           C
ANISOU 2327  CZ  ARG A 644     9103   6924   9257   1257   3570   1473       C
ATOM   2328  NH1 ARG A 644     -60.336  -4.845 -27.103  1.00 69.06           N
ANISOU 2328  NH1 ARG A 644     9299   7219   9720   1056   3614   1343       N
ATOM   2329  NH2 ARG A 644     -58.059  -4.982 -27.395  1.00 59.35           N
ANISOU 2329  NH2 ARG A 644     8173   5987   8391   1269   3507   1453       N
ATOM   2330  N   ASN A 645     -62.115   1.538 -25.053  1.00 51.16           N
ANISOU 2330  N   ASN A 645     6867   5853   6719   1299   3017   1148       N
ATOM   2331  CA  ASN A 645     -62.339   2.685 -25.938  1.00 47.10           C
ANISOU 2331  CA  ASN A 645     6204   5472   6218   1221   2841    988       C
ATOM   2332  C   ASN A 645     -61.419   3.855 -25.577  1.00 40.36           C
ANISOU 2332  C   ASN A 645     5419   4746   5169   1382   2671    988       C
ATOM   2333  O   ASN A 645     -61.739   5.023 -25.793  1.00 36.39           O
ANISOU 2333  O   ASN A 645     4849   4359   4619   1382   2548    885       O
ATOM   2334  CB  ASN A 645     -63.802   3.126 -25.899  1.00 45.49           C
ANISOU 2334  CB  ASN A 645     5884   5330   6068   1132   2883    901       C
ATOM   2335  CG  ASN A 645     -64.245   3.507 -24.515  1.00 55.89           C
ANISOU 2335  CG  ASN A 645     7311   6693   7231   1268   2960    985       C
ATOM   2336  OD1 ASN A 645     -63.633   3.101 -23.524  1.00 57.31           O
ANISOU 2336  OD1 ASN A 645     7667   6824   7283   1413   3028   1127       O
ATOM   2337  ND2 ASN A 645     -65.318   4.286 -24.428  1.00 62.67           N
ANISOU 2337  ND2 ASN A 645     8071   7648   8091   1237   2951    898       N
ATOM   2338  N   THR A 646     -60.266   3.510 -25.031  1.00 40.32           N
ANISOU 2338  N   THR A 646     5550   4713   5057   1530   2669   1101       N
ATOM   2339  CA  THR A 646     -59.261   4.472 -24.632  1.00 42.14           C
ANISOU 2339  CA  THR A 646     5850   5057   5104   1700   2513   1099       C
ATOM   2340  C   THR A 646     -57.901   3.901 -25.061  1.00 36.91           C
ANISOU 2340  C   THR A 646     5204   4346   4472   1752   2477   1145       C
ATOM   2341  O   THR A 646     -57.715   2.688 -25.029  1.00 36.06           O
ANISOU 2341  O   THR A 646     5145   4116   4441   1744   2612   1245       O
ATOM   2342  CB  THR A 646     -59.344   4.664 -23.119  1.00 49.74           C
ANISOU 2342  CB  THR A 646     6988   6068   5844   1898   2562   1203       C
ATOM   2343  OG1 THR A 646     -59.990   5.914 -22.839  1.00 59.36           O
ANISOU 2343  OG1 THR A 646     8182   7401   6971   1917   2472   1104       O
ATOM   2344  CG2 THR A 646     -57.976   4.610 -22.464  1.00 46.34           C
ANISOU 2344  CG2 THR A 646     6700   5677   5231   2122   2496   1290       C
ATOM   2345  N   TYR A 647     -56.965   4.750 -25.484  1.00 33.84           N
ANISOU 2345  N   TYR A 647     4770   4036   4051   1789   2270   1063       N
ATOM   2346  CA  TYR A 647     -55.672   4.237 -25.947  1.00 36.84           C
ANISOU 2346  CA  TYR A 647     5137   4366   4496   1801   2175   1085       C
ATOM   2347  C   TYR A 647     -54.977   3.403 -24.871  1.00 37.04           C
ANISOU 2347  C   TYR A 647     5316   4350   4409   1985   2220   1243       C
ATOM   2348  O   TYR A 647     -54.469   2.343 -25.175  1.00 35.71           O
ANISOU 2348  O   TYR A 647     5154   4075   4338   1983   2304   1314       O
ATOM   2349  CB  TYR A 647     -54.759   5.337 -26.517  1.00 32.16           C
ANISOU 2349  CB  TYR A 647     4461   3853   3903   1780   1913    968       C
ATOM   2350  CG  TYR A 647     -54.007   6.152 -25.490  1.00 32.77           C
ANISOU 2350  CG  TYR A 647     4622   4027   3801   1944   1717    970       C
ATOM   2351  CD1 TYR A 647     -54.608   7.236 -24.858  1.00 40.36           C
ANISOU 2351  CD1 TYR A 647     5631   5078   4627   1992   1648    911       C
ATOM   2352  CD2 TYR A 647     -52.697   5.844 -25.155  1.00 33.93           C
ANISOU 2352  CD2 TYR A 647     4795   4176   3919   2055   1594   1016       C
ATOM   2353  CE1 TYR A 647     -53.924   7.982 -23.925  1.00 38.15           C
ANISOU 2353  CE1 TYR A 647     5433   4881   4181   2137   1458    889       C
ATOM   2354  CE2 TYR A 647     -52.003   6.581 -24.214  1.00 35.88           C
ANISOU 2354  CE2 TYR A 647     5108   4519   4006   2203   1392    996       C
ATOM   2355  CZ  TYR A 647     -52.622   7.649 -23.608  1.00 40.33           C
ANISOU 2355  CZ  TYR A 647     5728   5164   4431   2237   1324    927       C
ATOM   2356  OH  TYR A 647     -51.938   8.390 -22.677  1.00 48.95           O
ANISOU 2356  OH  TYR A 647     6891   6347   5362   2379   1113    884       O
ATOM   2357  N   GLU A 648     -54.996   3.853 -23.616  1.00 42.22           N
ANISOU 2357  N   GLU A 648     6106   5085   4849   2156   2172   1297       N
ATOM   2358  CA  GLU A 648     -54.440   3.052 -22.513  1.00 45.90           C
ANISOU 2358  CA  GLU A 648     6747   5521   5172   2359   2220   1460       C
ATOM   2359  C   GLU A 648     -55.149   1.707 -22.360  1.00 49.47           C
ANISOU 2359  C   GLU A 648     7278   5824   5694   2339   2535   1607       C
ATOM   2360  O   GLU A 648     -54.506   0.655 -22.327  1.00 40.72           O
ANISOU 2360  O   GLU A 648     6231   4610   4631   2405   2601   1720       O
ATOM   2361  CB  GLU A 648     -54.517   3.800 -21.178  1.00 45.02           C
ANISOU 2361  CB  GLU A 648     6787   5529   4789   2548   2129   1482       C
ATOM   2362  CG  GLU A 648     -53.636   5.039 -21.079  1.00 56.35           C
ANISOU 2362  CG  GLU A 648     8179   7096   6136   2602   1804   1348       C
ATOM   2363  CD  GLU A 648     -54.449   6.320 -20.983  1.00 64.24           C
ANISOU 2363  CD  GLU A 648     9156   8185   7068   2552   1749   1218       C
ATOM   2364  OE1 GLU A 648     -55.495   6.413 -21.665  1.00 61.05           O
ANISOU 2364  OE1 GLU A 648     8659   7746   6791   2395   1895   1174       O
ATOM   2365  OE2 GLU A 648     -54.048   7.228 -20.221  1.00 66.59           O
ANISOU 2365  OE2 GLU A 648     9527   8586   7187   2676   1552   1154       O
ATOM   2366  N   LYS A 649     -56.473   1.739 -22.256  1.00 45.41           N
ANISOU 2366  N   LYS A 649     6758   5293   5203   2250   2737   1604       N
ATOM   2367  CA  LYS A 649     -57.231   0.505 -22.073  1.00 49.81           C
ANISOU 2367  CA  LYS A 649     7369   5676   5879   2178   2973   1711       C
ATOM   2368  C   LYS A 649     -57.075  -0.422 -23.274  1.00 48.17           C
ANISOU 2368  C   LYS A 649     7048   5323   5932   2005   3041   1677       C
ATOM   2369  O   LYS A 649     -56.949  -1.632 -23.108  1.00 47.87           O
ANISOU 2369  O   LYS A 649     7095   5124   5970   2032   3197   1791       O
ATOM   2370  CB  LYS A 649     -58.710   0.801 -21.780  1.00 53.98           C
ANISOU 2370  CB  LYS A 649     7858   6202   6451   2057   3050   1655       C
ATOM   2371  CG  LYS A 649     -58.919   1.597 -20.493  1.00 60.31           C
ANISOU 2371  CG  LYS A 649     8797   7125   6995   2240   3012   1694       C
ATOM   2372  CD  LYS A 649     -60.375   1.996 -20.258  1.00 64.43           C
ANISOU 2372  CD  LYS A 649     9255   7659   7567   2124   3090   1628       C
ATOM   2373  CE  LYS A 649     -61.149   0.908 -19.525  1.00 73.59           C
ANISOU 2373  CE  LYS A 649    10506   8674   8781   2124   3330   1749       C
ATOM   2374  NZ  LYS A 649     -62.454   1.406 -18.987  1.00 76.62           N
ANISOU 2374  NZ  LYS A 649    10858   9103   9153   2074   3412   1707       N
ATOM   2375  N   TYR A 650     -57.058   0.148 -24.479  1.00 48.33           N
ANISOU 2375  N   TYR A 650     6888   5392   6082   1840   2916   1513       N
ATOM   2376  CA  TYR A 650     -56.947  -0.654 -25.699  1.00 44.25           C
ANISOU 2376  CA  TYR A 650     6266   4749   5798   1668   2959   1451       C
ATOM   2377  C   TYR A 650     -55.581  -1.295 -25.886  1.00 38.38           C
ANISOU 2377  C   TYR A 650     5567   3950   5064   1791   2964   1530       C
ATOM   2378  O   TYR A 650     -55.470  -2.507 -26.068  1.00 39.46           O
ANISOU 2378  O   TYR A 650     5753   3918   5324   1769   3115   1604       O
ATOM   2379  CB  TYR A 650     -57.281   0.162 -26.950  1.00 36.18           C
ANISOU 2379  CB  TYR A 650     5059   3805   4883   1478   2811   1255       C
ATOM   2380  CG  TYR A 650     -57.122  -0.658 -28.213  1.00 43.64           C
ANISOU 2380  CG  TYR A 650     5917   4631   6034   1318   2844   1181       C
ATOM   2381  CD1 TYR A 650     -58.099  -1.572 -28.593  1.00 44.36           C
ANISOU 2381  CD1 TYR A 650     5977   4587   6290   1160   2985   1145       C
ATOM   2382  CD2 TYR A 650     -55.985  -0.540 -29.010  1.00 43.92           C
ANISOU 2382  CD2 TYR A 650     5901   4686   6102   1333   2738   1136       C
ATOM   2383  CE1 TYR A 650     -57.956  -2.333 -29.735  1.00 46.25           C
ANISOU 2383  CE1 TYR A 650     6153   4716   6703   1025   3017   1062       C
ATOM   2384  CE2 TYR A 650     -55.829  -1.299 -30.158  1.00 41.11           C
ANISOU 2384  CE2 TYR A 650     5483   4220   5916   1198   2774   1063       C
ATOM   2385  CZ  TYR A 650     -56.820  -2.192 -30.514  1.00 43.87           C
ANISOU 2385  CZ  TYR A 650     5820   4439   6410   1048   2913   1025       C
ATOM   2386  OH  TYR A 650     -56.687  -2.945 -31.647  1.00 36.93           O
ANISOU 2386  OH  TYR A 650     4891   3451   5688    922   2952    935       O
ATOM   2387  N   LEU A 651     -54.540  -0.476 -25.876  1.00 41.01           N
ANISOU 2387  N   LEU A 651     5874   4409   5299   1894   2724   1487       N
ATOM   2388  CA  LEU A 651     -53.193  -0.983 -26.082  1.00 37.67           C
ANISOU 2388  CA  LEU A 651     5459   3943   4911   1989   2627   1528       C
ATOM   2389  C   LEU A 651     -52.807  -1.922 -24.943  1.00 44.56           C
ANISOU 2389  C   LEU A 651     6520   4735   5677   2201   2730   1728       C
ATOM   2390  O   LEU A 651     -52.186  -2.969 -25.165  1.00 40.85           O
ANISOU 2390  O   LEU A 651     6086   4133   5304   2249   2809   1805       O
ATOM   2391  CB  LEU A 651     -52.205   0.175 -26.194  1.00 36.52           C
ANISOU 2391  CB  LEU A 651     5230   3953   4691   2042   2330   1432       C
ATOM   2392  CG  LEU A 651     -52.424   1.131 -27.373  1.00 34.43           C
ANISOU 2392  CG  LEU A 651     4799   3757   4525   1852   2223   1252       C
ATOM   2393  CD1 LEU A 651     -51.462   2.287 -27.273  1.00 33.75           C
ANISOU 2393  CD1 LEU A 651     4655   3806   4361   1914   1953   1178       C
ATOM   2394  CD2 LEU A 651     -52.269   0.419 -28.720  1.00 33.77           C
ANISOU 2394  CD2 LEU A 651     4617   3565   4648   1701   2310   1191       C
ATOM   2395  N   GLY A 652     -53.207  -1.554 -23.726  1.00 48.74           N
ANISOU 2395  N   GLY A 652     7184   5338   5997   2338   2739   1813       N
ATOM   2396  CA  GLY A 652     -52.928  -2.356 -22.550  1.00 53.44           C
ANISOU 2396  CA  GLY A 652     7991   5869   6444   2563   2838   2016       C
ATOM   2397  C   GLY A 652     -51.670  -1.928 -21.815  1.00 56.99           C
ANISOU 2397  C   GLY A 652     8500   6446   6708   2801   2568   2048       C
ATOM   2398  O   GLY A 652     -50.768  -1.314 -22.397  1.00 59.31           O
ANISOU 2398  O   GLY A 652     8647   6830   7059   2778   2327   1924       O
ATOM   2399  N   GLU A 653     -51.615  -2.277 -20.533  1.00 53.66           N
ANISOU 2399  N   GLU A 653     8290   6033   6066   3026   2611   2209       N
ATOM   2400  CA  GLU A 653     -50.542  -1.875 -19.625  1.00 50.67           C
ANISOU 2400  CA  GLU A 653     7968   5815   5468   3240   2336   2203       C
ATOM   2401  C   GLU A 653     -49.122  -2.165 -20.122  1.00 53.59           C
ANISOU 2401  C   GLU A 653     8214   6205   5941   3274   2131   2154       C
ATOM   2402  O   GLU A 653     -48.251  -1.298 -20.057  1.00 57.32           O
ANISOU 2402  O   GLU A 653     8595   6822   6361   3339   1838   2052       O
ATOM   2403  CB  GLU A 653     -50.750  -2.540 -18.258  1.00 52.10           C
ANISOU 2403  CB  GLU A 653     8372   5999   5425   3416   2453   2333       C
ATOM   2404  N   GLU A 654     -48.890  -3.385 -20.599  1.00 52.32           N
ANISOU 2404  N   GLU A 654     8046   5897   5936   3227   2289   2218       N
ATOM   2405  CA  GLU A 654     -47.557  -3.789 -21.022  1.00 57.42           C
ANISOU 2405  CA  GLU A 654     8584   6552   6680   3271   2125   2187       C
ATOM   2406  C   GLU A 654     -47.027  -2.896 -22.141  1.00 56.88           C
ANISOU 2406  C   GLU A 654     8282   6545   6783   3142   1942   2020       C
ATOM   2407  O   GLU A 654     -45.921  -2.365 -22.051  1.00 58.46           O
ANISOU 2407  O   GLU A 654     8379   6870   6963   3227   1676   1947       O
ATOM   2408  CB  GLU A 654     -47.548  -5.256 -21.465  1.00 58.74           C
ANISOU 2408  CB  GLU A 654     8787   6529   7003   3222   2360   2274       C
ATOM   2409  N   TYR A 655     -47.825  -2.717 -23.187  1.00 52.56           N
ANISOU 2409  N   TYR A 655     7645   5913   6412   2934   2088   1949       N
ATOM   2410  CA  TYR A 655     -47.360  -1.977 -24.351  1.00 51.35           C
ANISOU 2410  CA  TYR A 655     7275   5804   6430   2796   1956   1786       C
ATOM   2411  C   TYR A 655     -47.243  -0.469 -24.078  1.00 52.88           C
ANISOU 2411  C   TYR A 655     7395   6179   6516   2805   1714   1667       C
ATOM   2412  O   TYR A 655     -46.320   0.179 -24.565  1.00 54.54           O
ANISOU 2412  O   TYR A 655     7443   6476   6803   2775   1514   1552       O
ATOM   2413  CB  TYR A 655     -48.221  -2.281 -25.584  1.00 48.92           C
ANISOU 2413  CB  TYR A 655     6895   5363   6329   2565   2172   1721       C
ATOM   2414  CG  TYR A 655     -47.698  -1.636 -26.846  1.00 48.28           C
ANISOU 2414  CG  TYR A 655     6606   5335   6404   2402   2053   1550       C
ATOM   2415  CD1 TYR A 655     -46.478  -2.017 -27.383  1.00 43.81           C
ANISOU 2415  CD1 TYR A 655     5938   4758   5948   2430   1971   1526       C
ATOM   2416  CD2 TYR A 655     -48.417  -0.633 -27.492  1.00 45.90           C
ANISOU 2416  CD2 TYR A 655     6213   5105   6122   2205   2017   1408       C
ATOM   2417  CE1 TYR A 655     -45.982  -1.422 -28.532  1.00 44.11           C
ANISOU 2417  CE1 TYR A 655     5798   4837   6126   2296   1892   1384       C
ATOM   2418  CE2 TYR A 655     -47.932  -0.035 -28.644  1.00 44.12           C
ANISOU 2418  CE2 TYR A 655     5822   4920   6020   2067   1922   1269       C
ATOM   2419  CZ  TYR A 655     -46.710  -0.435 -29.163  1.00 42.47           C
ANISOU 2419  CZ  TYR A 655     5522   4686   5927   2115   1873   1261       C
ATOM   2420  OH  TYR A 655     -46.212   0.160 -30.308  1.00 37.93           O
ANISOU 2420  OH  TYR A 655     4792   4149   5470   1980   1806   1132       O
ATOM   2421  N   VAL A 656     -48.162   0.077 -23.283  1.00 51.47           N
ANISOU 2421  N   VAL A 656     7334   6061   6160   2822   1735   1681       N
ATOM   2422  CA  VAL A 656     -48.101   1.482 -22.873  1.00 47.45           C
ANISOU 2422  CA  VAL A 656     6786   5721   5521   2826   1504   1559       C
ATOM   2423  C   VAL A 656     -46.798   1.836 -22.153  1.00 49.08           C
ANISOU 2423  C   VAL A 656     6978   6048   5622   3027   1221   1546       C
ATOM   2424  O   VAL A 656     -46.196   2.881 -22.418  1.00 46.95           O
ANISOU 2424  O   VAL A 656     6566   5884   5389   2968    996   1396       O
ATOM   2425  CB  VAL A 656     -49.289   1.858 -21.964  1.00 50.65           C
ANISOU 2425  CB  VAL A 656     7353   6164   5729   2860   1599   1598       C
ATOM   2426  CG1 VAL A 656     -49.097   3.244 -21.378  1.00 47.01           C
ANISOU 2426  CG1 VAL A 656     6883   5868   5110   2909   1346   1475       C
ATOM   2427  CG2 VAL A 656     -50.586   1.793 -22.742  1.00 55.93           C
ANISOU 2427  CG2 VAL A 656     7978   6750   6525   2638   1828   1561       C
ATOM   2428  N   LYS A 657     -46.367   0.968 -21.238  1.00 53.50           N
ANISOU 2428  N   LYS A 657     7684   6588   6056   3265   1230   1701       N
ATOM   2429  CA  LYS A 657     -45.121   1.192 -20.514  1.00 57.92           C
ANISOU 2429  CA  LYS A 657     8217   7279   6511   3432    943   1665       C
ATOM   2430  C   LYS A 657     -43.916   0.997 -21.432  1.00 60.91           C
ANISOU 2430  C   LYS A 657     8371   7648   7126   3377    833   1594       C
ATOM   2431  O   LYS A 657     -42.934   1.739 -21.346  1.00 66.40           O
ANISOU 2431  O   LYS A 657     8925   8463   7840   3426    564   1482       O
ATOM   2432  CB  LYS A 657     -45.011   0.268 -19.294  1.00 61.41           C
ANISOU 2432  CB  LYS A 657     8869   7723   6740   3629    982   1809       C
ATOM   2433  CG  LYS A 657     -43.778   0.541 -18.426  1.00 61.04           C
ANISOU 2433  CG  LYS A 657     8803   7827   6561   3818    663   1758       C
ATOM   2434  CD  LYS A 657     -43.525  -0.564 -17.409  1.00 59.87           C
ANISOU 2434  CD  LYS A 657     8844   7660   6245   4012    718   1904       C
ATOM   2435  CE  LYS A 657     -42.112  -0.451 -16.821  1.00 65.55           C
ANISOU 2435  CE  LYS A 657     9485   8511   6910   4182    391   1842       C
ATOM   2436  NZ  LYS A 657     -41.661  -1.674 -16.077  1.00 67.62           N
ANISOU 2436  NZ  LYS A 657     9890   8734   7069   4369    440   1986       N
ATOM   2437  N   ALA A 658     -43.996  -0.005 -22.304  1.00 54.61           N
ANISOU 2437  N   ALA A 658     7536   6702   6511   3274   1047   1651       N
ATOM   2438  CA  ALA A 658     -42.945  -0.258 -23.287  1.00 52.53           C
ANISOU 2438  CA  ALA A 658     7066   6413   6481   3209    993   1584       C
ATOM   2439  C   ALA A 658     -42.731   0.927 -24.239  1.00 42.81           C
ANISOU 2439  C   ALA A 658     5622   5241   5401   3059    887   1421       C
ATOM   2440  O   ALA A 658     -41.596   1.232 -24.608  1.00 52.08           O
ANISOU 2440  O   ALA A 658     6607   6478   6703   3068    724   1337       O
ATOM   2441  CB  ALA A 658     -43.235  -1.528 -24.069  1.00 52.10           C
ANISOU 2441  CB  ALA A 658     7041   6180   6576   3112   1263   1660       C
ATOM   2442  N   VAL A 659     -43.817   1.591 -24.628  1.00 47.06           N
ANISOU 2442  N   VAL A 659     6186   5768   5926   2879    981   1357       N
ATOM   2443  CA  VAL A 659     -43.714   2.783 -25.470  1.00 46.42           C
ANISOU 2443  CA  VAL A 659     5935   5749   5952   2674    878   1185       C
ATOM   2444  C   VAL A 659     -43.249   3.964 -24.623  1.00 47.29           C
ANISOU 2444  C   VAL A 659     6020   6013   5937   2747    597   1090       C
ATOM   2445  O   VAL A 659     -42.388   4.741 -25.043  1.00 44.34           O
ANISOU 2445  O   VAL A 659     5466   5703   5680   2674    429    965       O
ATOM   2446  CB  VAL A 659     -45.049   3.126 -26.168  1.00 40.93           C
ANISOU 2446  CB  VAL A 659     5279   4997   5276   2460   1051   1140       C
ATOM   2447  CG1 VAL A 659     -44.941   4.451 -26.900  1.00 41.97           C
ANISOU 2447  CG1 VAL A 659     5270   5195   5483   2283    928    978       C
ATOM   2448  CG2 VAL A 659     -45.449   2.024 -27.136  1.00 36.54           C
ANISOU 2448  CG2 VAL A 659     4723   4293   4869   2360   1303   1192       C
ATOM   2449  N   GLY A 660     -43.819   4.081 -23.425  1.00 49.13           N
ANISOU 2449  N   GLY A 660     6437   6298   5934   2888    558   1146       N
ATOM   2450  CA  GLY A 660     -43.420   5.106 -22.480  1.00 52.62           C
ANISOU 2450  CA  GLY A 660     6889   6881   6222   2987    288   1053       C
ATOM   2451  C   GLY A 660     -41.928   5.044 -22.205  1.00 56.64           C
ANISOU 2451  C   GLY A 660     7259   7472   6790   3124     47   1016       C
ATOM   2452  O   GLY A 660     -41.262   6.078 -22.112  1.00 55.14           O
ANISOU 2452  O   GLY A 660     6938   7380   6633   3085   -191    863       O
ATOM   2453  N   ASN A 661     -41.396   3.827 -22.110  1.00 59.11           N
ANISOU 2453  N   ASN A 661     7588   7736   7134   3281    113   1150       N
ATOM   2454  CA  ASN A 661     -39.971   3.622 -21.847  1.00 62.71           C
ANISOU 2454  CA  ASN A 661     7896   8271   7658   3441   -109   1127       C
ATOM   2455  C   ASN A 661     -39.102   4.209 -22.952  1.00 58.22           C
ANISOU 2455  C   ASN A 661     7035   7715   7371   3252   -183    977       C
ATOM   2456  O   ASN A 661     -37.907   4.434 -22.773  1.00 59.24           O
ANISOU 2456  O   ASN A 661     6984   7938   7587   3333   -408    899       O
ATOM   2457  CB  ASN A 661     -39.661   2.134 -21.671  1.00 67.19           C
ANISOU 2457  CB  ASN A 661     8547   8753   8230   3547     20   1279       C
ATOM   2458  CG  ASN A 661     -38.305   1.891 -21.022  1.00 71.23           C
ANISOU 2458  CG  ASN A 661     8961   9364   8740   3717   -232   1255       C
ATOM   2459  OD1 ASN A 661     -37.279   1.806 -21.707  1.00 67.73           O
ANISOU 2459  OD1 ASN A 661     8282   8926   8528   3684   -301   1192       O
ATOM   2460  ND2 ASN A 661     -38.295   1.779 -19.694  1.00 72.88           N
ANISOU 2460  ND2 ASN A 661     9348   9655   8689   3900   -365   1301       N
ATOM   2461  N   LEU A 662     -39.727   4.474 -24.090  1.00 56.27           N
ANISOU 2461  N   LEU A 662     6742   7376   7263   3001      9    935       N
ATOM   2462  CA  LEU A 662     -39.034   5.020 -25.245  1.00 54.35           C
ANISOU 2462  CA  LEU A 662     6253   7125   7273   2806     -5    812       C
ATOM   2463  C   LEU A 662     -39.353   6.505 -25.442  1.00 55.58           C
ANISOU 2463  C   LEU A 662     6361   7325   7431   2615   -107    657       C
ATOM   2464  O   LEU A 662     -39.023   7.076 -26.485  1.00 53.14           O
ANISOU 2464  O   LEU A 662     5889   6987   7315   2420    -73    565       O
ATOM   2465  CB  LEU A 662     -39.429   4.225 -26.488  1.00 51.44           C
ANISOU 2465  CB  LEU A 662     5875   6615   7056   2673    286    874       C
ATOM   2466  CG  LEU A 662     -38.346   3.906 -27.510  1.00 46.82           C
ANISOU 2466  CG  LEU A 662     5064   5999   6725   2617    327    836       C
ATOM   2467  CD1 LEU A 662     -37.117   3.363 -26.818  1.00 47.74           C
ANISOU 2467  CD1 LEU A 662     5075   6187   6877   2850    160    869       C
ATOM   2468  CD2 LEU A 662     -38.884   2.902 -28.515  1.00 40.38           C
ANISOU 2468  CD2 LEU A 662     4309   5037   5996   2538    620    914       C
ATOM   2469  N   ARG A 663     -39.988   7.120 -24.439  1.00 58.25           N
ANISOU 2469  N   ARG A 663     6857   7726   7549   2680   -220    633       N
ATOM   2470  CA  ARG A 663     -40.378   8.535 -24.496  1.00 56.82           C
ANISOU 2470  CA  ARG A 663     6666   7575   7349   2524   -317    489       C
ATOM   2471  C   ARG A 663     -39.190   9.456 -24.768  1.00 57.48           C
ANISOU 2471  C   ARG A 663     6511   7712   7616   2433   -526    329       C
ATOM   2472  O   ARG A 663     -39.232  10.265 -25.687  1.00 57.71           O
ANISOU 2472  O   ARG A 663     6443   7690   7795   2219   -476    242       O
ATOM   2473  CB  ARG A 663     -41.110   8.971 -23.224  1.00 57.42           C
ANISOU 2473  CB  ARG A 663     6952   7718   7146   2654   -421    483       C
ATOM   2474  N   LYS A 664     -38.137   9.348 -23.965  1.00 59.13           N
ANISOU 2474  N   LYS A 664     6627   8022   7816   2597   -760    289       N
ATOM   2475  CA  LYS A 664     -36.858   9.927 -24.354  1.00 57.65           C
ANISOU 2475  CA  LYS A 664     6161   7876   7868   2510   -922    152       C
ATOM   2476  C   LYS A 664     -36.452   9.079 -25.548  1.00 66.00           C
ANISOU 2476  C   LYS A 664     7080   8851   9147   2437   -703    234       C
ATOM   2477  O   LYS A 664     -36.738   7.888 -25.540  1.00 76.66           O
ANISOU 2477  O   LYS A 664     8534  10161  10434   2564   -553    384       O
ATOM   2478  CB  LYS A 664     -35.836   9.794 -23.223  1.00 53.32           C
ANISOU 2478  CB  LYS A 664     5533   7465   7262   2732  -1223    100       C
ATOM   2479  N   CYS A 665     -35.802   9.693 -26.543  1.00 59.97           N
ANISOU 2479  N   CYS A 665     6096   8054   8635   2238   -674    137       N
ATOM   2480  CA  CYS A 665     -35.460   9.104 -27.860  1.00 57.25           C
ANISOU 2480  CA  CYS A 665     5623   7624   8506   2128   -439    191       C
ATOM   2481  C   CYS A 665     -36.448   9.520 -28.932  1.00 54.43           C
ANISOU 2481  C   CYS A 665     5368   7157   8157   1912   -211    203       C
ATOM   2482  O   CYS A 665     -36.097   9.564 -30.111  1.00 56.13           O
ANISOU 2482  O   CYS A 665     5460   7308   8558   1763    -56    191       O
ATOM   2483  CB  CYS A 665     -35.357   7.568 -27.893  1.00 58.15           C
ANISOU 2483  CB  CYS A 665     5780   7710   8605   2306   -303    341       C
ATOM   2484  SG  CYS A 665     -34.041   6.814 -26.914  1.00 74.55           S
ANISOU 2484  SG  CYS A 665     7708   9903  10715   2591   -531    358       S
ATOM   2485  N   SER A 666     -37.685   9.799 -28.529  1.00 50.04           N
ANISOU 2485  N   SER A 666     5039   6582   7391   1909   -187    229       N
ATOM   2486  CA  SER A 666     -38.738  10.076 -29.502  1.00 46.18           C
ANISOU 2486  CA  SER A 666     4658   5999   6887   1737     21    250       C
ATOM   2487  C   SER A 666     -38.406  11.245 -30.412  1.00 46.41           C
ANISOU 2487  C   SER A 666     4565   5990   7079   1521     28    145       C
ATOM   2488  O   SER A 666     -38.059  12.336 -29.958  1.00 43.99           O
ANISOU 2488  O   SER A 666     4202   5716   6797   1473   -151     34       O
ATOM   2489  CB  SER A 666     -40.092  10.318 -28.836  1.00 43.07           C
ANISOU 2489  CB  SER A 666     4498   5607   6258   1774     25    278       C
ATOM   2490  OG  SER A 666     -41.066  10.637 -29.825  1.00 40.41           O
ANISOU 2490  OG  SER A 666     4237   5191   5926   1612    202    284       O
ATOM   2491  N   THR A 667     -38.538  10.988 -31.705  1.00 49.60           N
ANISOU 2491  N   THR A 667     4945   6314   7586   1394    245    182       N
ATOM   2492  CA  THR A 667     -38.248  11.956 -32.743  1.00 51.43           C
ANISOU 2492  CA  THR A 667     5086   6490   7966   1194    308    116       C
ATOM   2493  C   THR A 667     -39.538  12.663 -33.198  1.00 46.11           C
ANISOU 2493  C   THR A 667     4594   5758   7167   1086    389    117       C
ATOM   2494  O   THR A 667     -39.485  13.675 -33.889  1.00 46.14           O
ANISOU 2494  O   THR A 667     4574   5709   7249    935    416     66       O
ATOM   2495  CB  THR A 667     -37.578  11.228 -33.928  1.00 57.19           C
ANISOU 2495  CB  THR A 667     5691   7174   8864   1141    506    158       C
ATOM   2496  OG1 THR A 667     -37.240  12.160 -34.961  1.00 61.56           O
ANISOU 2496  OG1 THR A 667     6166   7670   9555    952    591    107       O
ATOM   2497  CG2 THR A 667     -38.507  10.150 -34.481  1.00 53.34           C
ANISOU 2497  CG2 THR A 667     5359   6638   8271   1176    704    255       C
ATOM   2498  N   SER A 668     -40.689  12.143 -32.763  1.00 46.16           N
ANISOU 2498  N   SER A 668     4779   5772   6987   1173    426    179       N
ATOM   2499  CA  SER A 668     -42.006  12.551 -33.277  1.00 41.02           C
ANISOU 2499  CA  SER A 668     4285   5076   6224   1094    525    191       C
ATOM   2500  C   SER A 668     -42.425  13.972 -32.901  1.00 36.19           C
ANISOU 2500  C   SER A 668     3736   4461   5555   1038    398    111       C
ATOM   2501  O   SER A 668     -42.645  14.278 -31.736  1.00 37.00           O
ANISOU 2501  O   SER A 668     3898   4613   5545   1134    249     78       O
ATOM   2502  CB  SER A 668     -43.085  11.566 -32.812  1.00 38.94           C
ANISOU 2502  CB  SER A 668     4167   4825   5803   1202    602    271       C
ATOM   2503  OG  SER A 668     -44.387  12.033 -33.136  1.00 34.04           O
ANISOU 2503  OG  SER A 668     3675   4179   5078   1141    664    266       O
ATOM   2504  N   SER A 669     -42.544  14.833 -33.901  1.00 37.29           N
ANISOU 2504  N   SER A 669     3876   4533   5762    891    464     82       N
ATOM   2505  CA  SER A 669     -42.923  16.219 -33.657  1.00 40.42           C
ANISOU 2505  CA  SER A 669     4338   4897   6122    834    361      9       C
ATOM   2506  C   SER A 669     -44.395  16.341 -33.264  1.00 41.26           C
ANISOU 2506  C   SER A 669     4623   5018   6036    899    368     27       C
ATOM   2507  O   SER A 669     -44.780  17.266 -32.550  1.00 42.07           O
ANISOU 2507  O   SER A 669     4799   5121   6063    923    247    -37       O
ATOM   2508  CB  SER A 669     -42.626  17.075 -34.885  1.00 41.46           C
ANISOU 2508  CB  SER A 669     4437   4936   6379    670    452     -6       C
ATOM   2509  OG  SER A 669     -43.509  16.741 -35.938  1.00 44.02           O
ANISOU 2509  OG  SER A 669     4859   5231   6636    636    619     61       O
ATOM   2510  N   LEU A 670     -45.222  15.411 -33.729  1.00 28.31           N
ANISOU 2510  N   LEU A 670     3044   3387   4326    925    512    103       N
ATOM   2511  CA  LEU A 670     -46.617  15.403 -33.304  1.00 30.67           C
ANISOU 2511  CA  LEU A 670     3480   3710   4464    989    530    118       C
ATOM   2512  C   LEU A 670     -46.732  15.021 -31.831  1.00 39.17           C
ANISOU 2512  C   LEU A 670     4602   4855   5424   1138    435    123       C
ATOM   2513  O   LEU A 670     -47.544  15.591 -31.102  1.00 43.89           O
ANISOU 2513  O   LEU A 670     5302   5476   5898   1197    378     94       O
ATOM   2514  CB  LEU A 670     -47.458  14.461 -34.164  1.00 29.21           C
ANISOU 2514  CB  LEU A 670     3329   3515   4256    967    704    182       C
ATOM   2515  CG  LEU A 670     -48.955  14.413 -33.836  1.00 26.08           C
ANISOU 2515  CG  LEU A 670     3039   3145   3725   1017    741    192       C
ATOM   2516  CD1 LEU A 670     -49.583  15.782 -33.993  1.00 25.59           C
ANISOU 2516  CD1 LEU A 670     3040   3064   3619    986    674    136       C
ATOM   2517  CD2 LEU A 670     -49.664  13.383 -34.716  1.00 25.04           C
ANISOU 2517  CD2 LEU A 670     2911   3002   3603    979    902    235       C
ATOM   2518  N   LEU A 671     -45.920  14.057 -31.393  1.00 41.59           N
ANISOU 2518  N   LEU A 671     4843   5195   5764   1213    424    164       N
ATOM   2519  CA  LEU A 671     -45.931  13.645 -29.989  1.00 42.99           C
ANISOU 2519  CA  LEU A 671     5082   5440   5812   1376    332    184       C
ATOM   2520  C   LEU A 671     -45.577  14.819 -29.082  1.00 30.98           C
ANISOU 2520  C   LEU A 671     3578   3953   4239   1411    123     79       C
ATOM   2521  O   LEU A 671     -46.244  15.030 -28.082  1.00 31.47           O
ANISOU 2521  O   LEU A 671     3763   4059   4136   1518     68     67       O
ATOM   2522  CB  LEU A 671     -44.983  12.471 -29.713  1.00 43.69           C
ANISOU 2522  CB  LEU A 671     5094   5553   5951   1467    336    248       C
ATOM   2523  CG  LEU A 671     -45.468  11.353 -28.771  1.00 43.83           C
ANISOU 2523  CG  LEU A 671     5223   5604   5828   1632    391    348       C
ATOM   2524  CD1 LEU A 671     -44.300  10.666 -28.101  1.00 45.85           C
ANISOU 2524  CD1 LEU A 671     5414   5902   6103   1768    290    382       C
ATOM   2525  CD2 LEU A 671     -46.486  11.807 -27.723  1.00 45.48           C
ANISOU 2525  CD2 LEU A 671     5589   5856   5836   1721    352    341       C
ATOM   2526  N   GLU A 672     -44.546  15.589 -29.423  1.00 31.67           N
ANISOU 2526  N   GLU A 672     3545   4015   4472   1318     17     -5       N
ATOM   2527  CA  GLU A 672     -44.210  16.733 -28.582  1.00 42.25           C
ANISOU 2527  CA  GLU A 672     4899   5372   5781   1334   -188   -128       C
ATOM   2528  C   GLU A 672     -45.331  17.761 -28.565  1.00 35.92           C
ANISOU 2528  C   GLU A 672     4237   4529   4883   1303   -177   -174       C
ATOM   2529  O   GLU A 672     -45.707  18.253 -27.494  1.00 35.21           O
ANISOU 2529  O   GLU A 672     4253   4478   4646   1403   -294   -236       O
ATOM   2530  CB  GLU A 672     -42.856  17.358 -28.925  1.00 47.86           C
ANISOU 2530  CB  GLU A 672     5432   6052   6698   1224   -299   -220       C
ATOM   2531  CG  GLU A 672     -42.791  18.097 -30.231  1.00 56.38           C
ANISOU 2531  CG  GLU A 672     6460   7024   7939   1033   -190   -233       C
ATOM   2532  CD  GLU A 672     -41.573  18.998 -30.309  1.00 60.86           C
ANISOU 2532  CD  GLU A 672     6874   7548   8702    918   -313   -347       C
ATOM   2533  OE1 GLU A 672     -41.101  19.276 -31.439  1.00 61.37           O
ANISOU 2533  OE1 GLU A 672     6844   7531   8942    767   -196   -333       O
ATOM   2534  OE2 GLU A 672     -41.098  19.430 -29.232  1.00 56.34           O
ANISOU 2534  OE2 GLU A 672     6278   7023   8106    979   -523   -456       O
ATOM   2535  N   ALA A 673     -45.893  18.055 -29.736  1.00 37.05           N
ANISOU 2535  N   ALA A 673     4387   4596   5093   1182    -36   -143       N
ATOM   2536  CA  ALA A 673     -47.047  18.940 -29.817  1.00 30.30           C
ANISOU 2536  CA  ALA A 673     3662   3703   4150   1172    -11   -172       C
ATOM   2537  C   ALA A 673     -48.186  18.486 -28.893  1.00 37.50           C
ANISOU 2537  C   ALA A 673     4702   4686   4862   1320     21   -136       C
ATOM   2538  O   ALA A 673     -48.677  19.271 -28.082  1.00 34.70           O
ANISOU 2538  O   ALA A 673     4450   4342   4394   1390    -66   -207       O
ATOM   2539  CB  ALA A 673     -47.546  19.059 -31.267  1.00 29.53           C
ANISOU 2539  CB  ALA A 673     3558   3533   4131   1052    144   -120       C
ATOM   2540  N   CYS A 674     -48.599  17.223 -29.003  1.00 36.70           N
ANISOU 2540  N   CYS A 674     4598   4624   4721   1366    158    -30       N
ATOM   2541  CA  CYS A 674     -49.742  16.732 -28.220  1.00 39.02           C
ANISOU 2541  CA  CYS A 674     5005   4972   4847   1488    233     18       C
ATOM   2542  C   CYS A 674     -49.447  16.586 -26.730  1.00 41.40           C
ANISOU 2542  C   CYS A 674     5383   5347   4998   1649    120      4       C
ATOM   2543  O   CYS A 674     -50.356  16.410 -25.917  1.00 36.49           O
ANISOU 2543  O   CYS A 674     4877   4770   4217   1762    175     31       O
ATOM   2544  CB  CYS A 674     -50.240  15.396 -28.770  1.00 37.00           C
ANISOU 2544  CB  CYS A 674     4724   4718   4616   1476    423    131       C
ATOM   2545  SG  CYS A 674     -50.955  15.545 -30.409  1.00 38.73           S
ANISOU 2545  SG  CYS A 674     4893   4876   4945   1322    554    136       S
ATOM   2546  N   THR A 675     -48.171  16.667 -26.386  1.00 35.98           N
ANISOU 2546  N   THR A 675     4628   4678   4363   1663    -37    -43       N
ATOM   2547  CA  THR A 675     -47.722  16.405 -25.037  1.00 40.39           C
ANISOU 2547  CA  THR A 675     5252   5320   4776   1829   -168    -55       C
ATOM   2548  C   THR A 675     -47.381  17.737 -24.343  1.00 47.29           C
ANISOU 2548  C   THR A 675     6165   6202   5600   1846   -384   -215       C
ATOM   2549  O   THR A 675     -46.897  17.770 -23.211  1.00 46.15           O
ANISOU 2549  O   THR A 675     6075   6132   5328   1980   -546   -268       O
ATOM   2550  CB  THR A 675     -46.542  15.376 -25.062  1.00 41.66           C
ANISOU 2550  CB  THR A 675     5300   5509   5022   1865   -203      6       C
ATOM   2551  OG1 THR A 675     -46.576  14.558 -23.892  1.00 59.28           O
ANISOU 2551  OG1 THR A 675     7638   7817   7069   2063   -224     78       O
ATOM   2552  CG2 THR A 675     -45.191  16.044 -25.196  1.00 39.19           C
ANISOU 2552  CG2 THR A 675     4839   5193   4858   1796   -400   -110       C
ATOM   2553  N   PHE A 676     -47.699  18.837 -25.020  1.00 46.28           N
ANISOU 2553  N   PHE A 676     6028   5994   5564   1717   -382   -294       N
ATOM   2554  CA  PHE A 676     -47.343  20.185 -24.560  1.00 41.47           C
ANISOU 2554  CA  PHE A 676     5448   5353   4956   1696   -571   -459       C
ATOM   2555  C   PHE A 676     -48.062  20.616 -23.269  1.00 51.06           C
ANISOU 2555  C   PHE A 676     6846   6624   5930   1861   -643   -524       C
ATOM   2556  O   PHE A 676     -47.482  21.307 -22.428  1.00 49.80           O
ANISOU 2556  O   PHE A 676     6722   6484   5714   1911   -848   -663       O
ATOM   2557  CB  PHE A 676     -47.584  21.196 -25.695  1.00 37.84           C
ANISOU 2557  CB  PHE A 676     4955   4768   4656   1525   -516   -500       C
ATOM   2558  CG  PHE A 676     -47.029  22.561 -25.424  1.00 35.84           C
ANISOU 2558  CG  PHE A 676     4707   4442   4468   1463   -693   -667       C
ATOM   2559  CD1 PHE A 676     -45.667  22.743 -25.231  1.00 37.71           C
ANISOU 2559  CD1 PHE A 676     4815   4678   4836   1404   -861   -760       C
ATOM   2560  CD2 PHE A 676     -47.866  23.661 -25.364  1.00 35.89           C
ANISOU 2560  CD2 PHE A 676     4841   4374   4423   1464   -691   -739       C
ATOM   2561  CE1 PHE A 676     -45.150  23.996 -24.976  1.00 41.39           C
ANISOU 2561  CE1 PHE A 676     5278   5063   5386   1328  -1024   -929       C
ATOM   2562  CE2 PHE A 676     -47.354  24.925 -25.098  1.00 39.75           C
ANISOU 2562  CE2 PHE A 676     5348   4772   4984   1402   -849   -902       C
ATOM   2563  CZ  PHE A 676     -45.992  25.090 -24.908  1.00 41.37           C
ANISOU 2563  CZ  PHE A 676     5422   4968   5327   1324  -1015  -1000       C
ATOM   2564  N   ARG A 677     -49.324  20.220 -23.118  1.00 52.34           N
ANISOU 2564  N   ARG A 677     7119   6811   5954   1942   -471   -435       N
ATOM   2565  CA  ARG A 677     -50.054  20.493 -21.882  1.00 58.55           C
ANISOU 2565  CA  ARG A 677     8086   7661   6500   2114   -496   -477       C
ATOM   2566  C   ARG A 677     -50.028  19.292 -20.938  1.00 60.94           C
ANISOU 2566  C   ARG A 677     8462   8073   6622   2285   -457   -369       C
ATOM   2567  O   ARG A 677     -49.523  19.383 -19.817  1.00 64.43           O
ANISOU 2567  O   ARG A 677     8992   8587   6900   2426   -619   -434       O
ATOM   2568  CB  ARG A 677     -51.502  20.922 -22.166  1.00 60.65           C
ANISOU 2568  CB  ARG A 677     8431   7892   6722   2116   -327   -458       C
ATOM   2569  CG  ARG A 677     -51.646  22.318 -22.787  1.00 63.14           C
ANISOU 2569  CG  ARG A 677     8739   8097   7153   2007   -390   -578       C
ATOM   2570  CD  ARG A 677     -53.061  22.873 -22.632  1.00 65.64           C
ANISOU 2570  CD  ARG A 677     9168   8404   7369   2082   -274   -590       C
ATOM   2571  NE  ARG A 677     -53.888  22.591 -23.802  1.00 70.02           N
ANISOU 2571  NE  ARG A 677     9641   8923   8039   1993    -96   -491       N
ATOM   2572  CZ  ARG A 677     -55.215  22.680 -23.826  1.00 69.24           C
ANISOU 2572  CZ  ARG A 677     9587   8841   7879   2056     46   -462       C
ATOM   2573  NH1 ARG A 677     -55.876  22.396 -24.948  1.00 66.80           N
ANISOU 2573  NH1 ARG A 677     9185   8509   7685   1970    176   -386       N
ATOM   2574  NH2 ARG A 677     -55.880  23.043 -22.729  1.00 66.29           N
ANISOU 2574  NH2 ARG A 677     9344   8514   7327   2211     56   -517       N
END



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