CNRS Nantes University UFIP UFIP
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***  3skp  ***

elNémo ID: 190903141325128677

Job options:

ID        	=	 190903141325128677
JOBID     	=	 3skp
USERID    	=	 mja
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3skp

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



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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.