2gaa.cif

ATOM   1896 C CB  . GLU A 1 266 ? 25.845 10.402 8.767   1.00 15.83 ? 266  GLU A CB  1 
ATOM   1897 C CG  . GLU A 1 266 ? 25.173 11.687 8.308   1.00 16.84 ? 266  GLU A CG  1 
ATOM   1898 C CD  . GLU A 1 266 ? 25.769 12.241 7.023   1.00 19.04 ? 266  GLU A CD  1 
ATOM   1899 O OE1 . GLU A 1 266 ? 26.743 11.656 6.501   1.00 18.35 ? 266  GLU A OE1 1 
ATOM   1900 O OE2 . GLU A 1 266 ? 25.256 13.270 6.536   1.00 21.30 ? 266  GLU A OE2 1 
ATOM   1901 N N   . GLY A 1 267 ? 29.154 10.690 8.681   1.00 13.72 ? 267  GLY A N   1 
ATOM   1902 C CA  . GLY A 1 267 ? 30.271 11.384 8.074   1.00 14.04 ? 267  GLY A CA  1 
ATOM   1903 C C   . GLY A 1 267 ? 31.388 10.467 7.638   1.00 14.30 ? 267  GLY A C   1 
ATOM   1904 O O   . GLY A 1 267 ? 31.326 9.252  7.810   1.00 15.39 ? 267  GLY A O   1 
ATOM   1905 N N   . LEU A 1 268 ? 32.429 11.068 7.083   1.00 15.93 ? 268  LEU A N   1 
ATOM   1906 C CA  . LEU A 1 268 ? 33.579 10.332 6.581   1.00 15.52 ? 268  LEU A CA  1 
ATOM   1907 C C   . LEU A 1 268 ? 34.533 9.806  7.644   1.00 15.29 ? 268  LEU A C   1 
ATOM   1908 O O   . LEU A 1 268 ? 34.964 8.648  7.589   1.00 13.27 ? 268  LEU A O   1 
ATOM   1909 C CB  . LEU A 1 268 ? 34.380 11.229 5.635   1.00 15.74 ? 268  LEU A CB  1 
ATOM   1910 C CG  . LEU A 1 268 ? 33.743 11.734 4.339   1.00 17.71 ? 268  LEU A CG  1 
ATOM   1911 C CD1 . LEU A 1 268 ? 34.524 12.939 3.851   1.00 16.32 ? 268  LEU A CD1 1 
ATOM   1912 C CD2 . LEU A 1 268 ? 33.722 10.622 3.281   1.00 15.85 ? 268  LEU A CD2 1 
ATOM   1913 N N   . TYR A 1 269 ? 34.840 10.655 8.622   1.00 15.98 ? 269  TYR A N   1 
ATOM   1914 C CA  . TYR A 1 269 ? 35.830 10.324 9.636   1.00 15.61 ? 269  TYR A CA  1 
ATOM   1915 C C   . TYR A 1 269 ? 35.398 10.098 11.089  1.00 16.76 ? 269  TYR A C   1 
ATOM   1916 O O   . TYR A 1 269 ? 36.191 10.306 12.008  1.00 17.40 ? 269  TYR A O   1 
ATOM   1917 C CB  . TYR A 1 269 ? 36.911 11.410 9.572   1.00 17.52 ? 269  TYR A CB  1 
ATOM   1918 C CG  . TYR A 1 269 ? 37.364 11.704 8.146   1.00 17.70 ? 269  TYR A CG  1 
ATOM   1919 C CD1 . TYR A 1 269 ? 37.960 10.713 7.366   1.00 19.09 ? 269  TYR A CD1 1 
ATOM   1920 C CD2 . TYR A 1 269 ? 37.161 12.958 7.569   1.00 17.86 ? 269  TYR A CD2 1 
ATOM   1921 C CE1 . TYR A 1 269 ? 38.344 10.966 6.038   1.00 20.79 ? 269  TYR A CE1 1 
ATOM   1922 C CE2 . TYR A 1 269 ? 37.539 13.220 6.245   1.00 18.69 ? 269  TYR A CE2 1 
ATOM   1923 C CZ  . TYR A 1 269 ? 38.129 12.218 5.488   1.00 19.74 ? 269  TYR A CZ  1 
ATOM   1924 O OH  . TYR A 1 269 ? 38.502 12.468 4.181   1.00 20.39 ? 269  TYR A OH  1 
ATOM   1925 N N   . LEU A 1 270 ? 34.171 9.647  11.312  1.00 14.66 ? 270  LEU A N   1 
ATOM   1926 C CA  . LEU A 1 270 ? 33.720 9.428  12.681  1.00 15.23 ? 270  LEU A CA  1 
ATOM   1927 C C   . LEU A 1 270 ? 34.446 8.255  13.342  1.00 16.68 ? 270  LEU A C   1 
ATOM   1928 O O   . LEU A 1 270 ? 34.443 8.128  14.570  1.00 15.65 ? 270  LEU A O   1 
ATOM   1929 C CB  . LEU A 1 270 ? 32.205 9.196  12.706  1.00 15.33 ? 270  LEU A CB  1 
ATOM   1930 C CG  . LEU A 1 270 ? 31.386 10.279 11.989  1.00 16.84 ? 270  LEU A CG  1 
ATOM   1931 C CD1 . LEU A 1 270 ? 29.891 10.027 12.204  1.00 16.59 ? 270  LEU A CD1 1 
ATOM   1932 C CD2 . LEU A 1 270 ? 31.777 11.655 12.514  1.00 16.67 ? 270  LEU A CD2 1 
ATOM   1933 N N   . LEU A 1 271 ? 35.078 7.411  12.520  1.00 16.88 ? 271  LEU A N   1 
ATOM   1934 C CA  . LEU A 1 271 ? 35.809 6.240  13.009  1.00 16.05 ? 271  LEU A CA  1 
ATOM   1935 C C   . LEU A 1 271 ? 37.267 6.259  12.531  1.00 17.96 ? 271  LEU A C   1 
ATOM   1936 O O   . LEU A 1 271 ? 37.896 5.206  12.384  1.00 19.68 ? 271  LEU A O   1 
ATOM   1937 C CB  . LEU A 1 271 ? 35.115 4.952  12.520  1.00 14.69 ? 271  LEU A CB  1 
ATOM   1938 C CG  . LEU A 1 271 ? 33.665 4.717  12.986  1.00 17.21 ? 271  LEU A CG  1 
ATOM   1939 C CD1 . LEU A 1 271 ? 33.054 3.540  12.244  1.00 17.08 ? 271  LEU A CD1 1 
ATOM   1940 C CD2 . LEU A 1 271 ? 33.635 4.466  14.494  1.00 14.18 ? 271  LEU A CD2 1 
ATOM   1941 N N   . TYR A 1 272 ? 37.798 7.462  12.306  1.00 17.02 ? 272  TYR A N   1 
ATOM   1942 C CA  . TYR A 1 272 ? 39.168 7.649  11.821  1.00 16.57 ? 272  TYR A CA  1 
ATOM   1943 C C   . TYR A 1 272 ? 40.150 7.644  12.996  1.00 19.20 ? 272  TYR A C   1 
ATOM   1944 O O   . TYR A 1 272 ? 40.005 8.428  13.944  1.00 17.22 ? 272  TYR A O   1 
ATOM   1945 C CB  . TYR A 1 272 ? 39.255 8.972  11.059  1.00 15.97 ? 272  TYR A CB  1 
ATOM   1946 C CG  . TYR A 1 272 ? 40.361 9.045  10.029  1.00 17.31 ? 272  TYR A CG  1 
ATOM   1947 C CD1 . TYR A 1 272 ? 40.233 8.414  8.796   1.00 15.80 ? 272  TYR A CD1 1 
ATOM   1948 C CD2 . TYR A 1 272 ? 41.523 9.775  10.275  1.00 17.06 ? 272  TYR A CD2 1 
ATOM   1949 C CE1 . TYR A 1 272 ? 41.233 8.514  7.824   1.00 18.32 ? 272  TYR A CE1 1 
ATOM   1950 C CE2 . TYR A 1 272 ? 42.529 9.877  9.309   1.00 19.13 ? 272  TYR A CE2 1 
ATOM   1951 C CZ  . TYR A 1 272 ? 42.371 9.245  8.089   1.00 16.14 ? 272  TYR A CZ  1 
ATOM   1952 O OH  . TYR A 1 272 ? 43.346 9.361  7.123   1.00 21.88 ? 272  TYR A OH  1 
ATOM   1953 N N   . ASP A 1 273 ? 41.159 6.777  12.922  1.00 20.92 ? 273  ASP A N   1 
ATOM   1954 C CA  . ASP A 1 273 ? 42.128 6.623  14.010  1.00 22.19 ? 273  ASP A CA  1 
ATOM   1955 C C   . ASP A 1 273 ? 43.197 7.697  14.192  1.00 22.10 ? 273  ASP A C   1 
ATOM   1956 O O   . ASP A 1 273 ? 44.250 7.423  14.767  1.00 22.40 ? 273  ASP A O   1 
ATOM   1957 C CB  . ASP A 1 273 ? 42.824 5.252  13.912  1.00 23.08 ? 273  ASP A CB  1 
ATOM   1958 C CG  . ASP A 1 273 ? 43.707 5.114  12.670  1.00 25.18 ? 273  ASP A CG  1 
ATOM   1959 O OD1 . ASP A 1 273 ? 44.074 6.137  12.056  1.00 23.53 ? 273  ASP A OD1 1 
ATOM   1960 O OD2 . ASP A 1 273 ? 44.047 3.966  12.313  1.00 25.87 ? 273  ASP A OD2 1 
ATOM   1961 N N   . GLN A 1 274 ? 42.928 8.916  13.738  1.00 20.56 ? 274  GLN A N   1 
ATOM   1962 C CA  . GLN A 1 274 ? 43.901 9.991  13.862  1.00 20.78 ? 274  GLN A CA  1 
ATOM   1963 C C   . GLN A 1 274 ? 43.399 11.220 14.613  1.00 20.46 ? 274  GLN A C   1 
ATOM   1964 O O   . GLN A 1 274 ? 42.205 11.530 14.615  1.00 20.35 ? 274  GLN A O   1 
ATOM   1965 C CB  . GLN A 1 274 ? 44.384 10.419 12.473  1.00 24.08 ? 274  GLN A CB  1 
ATOM   1966 C CG  . GLN A 1 274 ? 45.157 9.345  11.732  1.00 24.44 ? 274  GLN A CG  1 
ATOM   1967 C CD  . GLN A 1 274 ? 46.383 8.899  12.499  1.00 25.25 ? 274  GLN A CD  1 
ATOM   1968 O OE1 . GLN A 1 274 ? 47.266 9.707  12.808  1.00 28.50 ? 274  GLN A OE1 1 
ATOM   1969 N NE2 . GLN A 1 274 ? 46.445 7.612  12.817  1.00 24.82 ? 274  GLN A NE2 1 
ATOM   1970 N N   . GLU A 1 275 ? 44.340 11.913 15.241  1.00 19.38 ? 275  GLU A N   1 
ATOM   1971 C CA  . GLU A 1 275 ? 44.079 13.131 15.998  1.00 18.98 ? 275  GLU A CA  1 
ATOM   1972 C C   . GLU A 1 275 ? 42.746 13.182 16.753  1.00 18.16 ? 275  GLU A C   1 
ATOM   1973 O O   . GLU A 1 275 ? 42.431 12.290 17.542  1.00 16.33 ? 275  GLU A O   1 
ATOM   1974 C CB  . GLU A 1 275 ? 44.209 14.352 15.073  1.00 17.75 ? 275  GLU A CB  1 
ATOM   1975 C CG  . GLU A 1 275 ? 43.478 14.225 13.735  1.00 17.92 ? 275  GLU A CG  1 
ATOM   1976 C CD  . GLU A 1 275 ? 42.697 15.479 13.388  1.00 17.69 ? 275  GLU A CD  1 
ATOM   1977 O OE1 . GLU A 1 275 ? 42.033 16.023 14.297  1.00 16.36 ? 275  GLU A OE1 1 
ATOM   1978 O OE2 . GLU A 1 275 ? 42.731 15.916 12.217  1.00 15.59 ? 275  GLU A OE2 1 
ATOM   1979 N N   . ASN A 1 276 ? 41.962 14.228 16.512  1.00 16.00 ? 276  ASN A N   1 
ATOM   1980 C CA  . ASN A 1 276 ? 40.691 14.387 17.214  1.00 14.90 ? 276  ASN A CA  1 
ATOM   1981 C C   . ASN A 1 276 ? 39.629 13.371 16.800  1.00 14.91 ? 276  ASN A C   1 
ATOM   1982 O O   . ASN A 1 276 ? 38.740 13.049 17.589  1.00 15.54 ? 276  ASN A O   1 
ATOM   1983 C CB  . ASN A 1 276 ? 40.165 15.810 17.008  1.00 15.13 ? 276  ASN A CB  1 
ATOM   1984 C CG  . ASN A 1 276 ? 41.055 16.865 17.658  1.00 16.15 ? 276  ASN A CG  1 
ATOM   1985 O OD1 . ASN A 1 276 ? 41.205 17.980 17.141  1.00 15.75 ? 276  ASN A OD1 1 
ATOM   1986 N ND2 . ASN A 1 276 ? 41.634 16.524 18.800  1.00 13.57 ? 276  ASN A ND2 1 
ATOM   1987 N N   . TRP A 1 277 ? 39.714 12.865 15.572  1.00 15.54 ? 277  TRP A N   1 
ATOM   1988 C CA  . TRP A 1 277 ? 38.728 11.890 15.095  1.00 15.92 ? 277  TRP A CA  1 
ATOM   1989 C C   . TRP A 1 277 ? 38.712 10.635 15.952  1.00 17.28 ? 277  TRP A C   1 
ATOM   1990 O O   . TRP A 1 277 ? 37.655 10.078 16.242  1.00 19.22 ? 277  TRP A O   1 
ATOM   1991 C CB  . TRP A 1 277 ? 39.013 11.496 13.650  1.00 13.62 ? 277  TRP A CB  1 
ATOM   1992 C CG  . TRP A 1 277 ? 39.076 12.653 12.724  1.00 14.71 ? 277  TRP A CG  1 
ATOM   1993 C CD1 . TRP A 1 277 ? 40.177 13.108 12.053  1.00 14.20 ? 277  TRP A CD1 1 
ATOM   1994 C CD2 . TRP A 1 277 ? 37.993 13.513 12.358  1.00 14.21 ? 277  TRP A CD2 1 
ATOM   1995 N NE1 . TRP A 1 277 ? 39.842 14.203 11.289  1.00 17.01 ? 277  TRP A NE1 1 
ATOM   1996 C CE2 . TRP A 1 277 ? 38.507 14.470 11.456  1.00 15.17 ? 277  TRP A CE2 1 
ATOM   1997 C CE3 . TRP A 1 277 ? 36.633 13.568 12.703  1.00 14.88 ? 277  TRP A CE3 1 
ATOM   1998 C CZ2 . TRP A 1 277 ? 37.710 15.472 10.890  1.00 15.95 ? 277  TRP A CZ2 1 
ATOM   1999 C CZ3 . TRP A 1 277 ? 35.843 14.562 12.141  1.00 16.51 ? 277  TRP A CZ3 1 
ATOM   2000 C CH2 . TRP A 1 277 ? 36.385 15.500 11.243  1.00 16.70 ? 277  TRP A CH2 1 
ATOM   2001 N N   . LYS A 1 278 ? 39.893 10.196 16.357  1.00 19.68 ? 278  LYS A N   1 
ATOM   2002 C CA  . LYS A 1 278 ? 40.029 9.002  17.172  1.00 21.72 ? 278  LYS A CA  1 
ATOM   2003 C C   . LYS A 1 278 ? 39.286 9.119  18.495  1.00 21.83 ? 278  LYS A C   1 
ATOM   2004 O O   . LYS A 1 278 ? 38.771 8.133  19.008  1.00 24.14 ? 278  LYS A O   1 
ATOM   2005 C CB  . LYS A 1 278 ? 41.513 8.725  17.424  1.00 23.69 ? 278  LYS A CB  1 
ATOM   2006 C CG  . LYS A 1 278 ? 41.798 7.421  18.147  1.00 30.62 ? 278  LYS A CG  1 
ATOM   2007 C CD  . LYS A 1 278 ? 43.297 7.166  18.231  1.00 33.91 ? 278  LYS A CD  1 
ATOM   2008 C CE  . LYS A 1 278 ? 43.596 5.801  18.841  1.00 38.17 ? 278  LYS A CE  1 
ATOM   2009 N NZ  . LYS A 1 278 ? 45.059 5.485  18.805  1.00 39.94 ? 278  LYS A NZ  1 
ATOM   2010 N N   . LYS A 1 279 ? 39.213 10.328 19.041  1.00 20.94 ? 279  LYS A N   1 
ATOM   2011 C CA  . LYS A 1 279 ? 38.534 10.534 20.312  1.00 21.87 ? 279  LYS A CA  1 
ATOM   2012 C C   . LYS A 1 279 ? 37.009 10.539 20.211  1.00 22.15 ? 279  LYS A C   1 
ATOM   2013 O O   . LYS A 1 279 ? 36.317 10.453 21.230  1.00 19.37 ? 279  LYS A O   1 
ATOM   2014 C CB  . LYS A 1 279 ? 39.025 11.835 20.957  1.00 22.10 ? 279  LYS A CB  1 
ATOM   2015 C CG  . LYS A 1 279 ? 40.532 11.859 21.177  1.00 24.17 ? 279  LYS A CG  1 
ATOM   2016 C CD  . LYS A 1 279 ? 41.003 13.207 21.688  1.00 29.13 ? 279  LYS A CD  1 
ATOM   2017 C CE  . LYS A 1 279 ? 42.521 13.258 21.801  1.00 32.65 ? 279  LYS A CE  1 
ATOM   2018 N NZ  . LYS A 1 279 ? 43.000 14.602 22.227  1.00 33.03 ? 279  LYS A NZ  1 
ATOM   2019 N N   . ILE A 1 280 ? 36.486 10.626 18.989  1.00 23.46 ? 280  ILE A N   1 
ATOM   2020 C CA  . ILE A 1 280 ? 35.037 10.639 18.779  1.00 23.01 ? 280  ILE A CA  1 
ATOM   2021 C C   . ILE A 1 280 ? 34.340 9.370  19.240  1.00 24.23 ? 280  ILE A C   1 
ATOM   2022 O O   . ILE A 1 280 ? 33.372 9.431  19.996  1.00 23.30 ? 280  ILE A O   1 
ATOM   2023 C CB  . ILE A 1 280 ? 34.676 10.846 17.289  1.00 22.87 ? 280  ILE A CB  1 
ATOM   2024 C CG1 . ILE A 1 280 ? 35.001 12.276 16.874  1.00 16.52 ? 280  ILE A CG1 1 
ATOM   2025 C CG2 . ILE A 1 280 ? 33.195 10.551 17.057  1.00 22.29 ? 280  ILE A CG2 1 
ATOM   2026 C CD1 . ILE A 1 280 ? 34.786 12.524 15.397  1.00 21.53 ? 280  ILE A CD1 1 
ATOM   2027 N N   . TYR A 1 281 ? 34.816 8.224  18.759  1.00 24.28 ? 281  TYR A N   1 
ATOM   2028 C CA  . TYR A 1 281 ? 34.216 6.949  19.123  1.00 25.23 ? 281  TYR A CA  1 
ATOM   2029 C C   . TYR A 1 281 ? 34.188 6.762  20.632  1.00 24.14 ? 281  TYR A C   1 
ATOM   2030 O O   . TYR A 1 281 ? 33.132 6.512  21.211  1.00 24.15 ? 281  TYR A O   1 
ATOM   2031 C CB  . TYR A 1 281 ? 34.980 5.783  18.478  1.00 24.49 ? 281  TYR A CB  1 
ATOM   2032 C CG  . TYR A 1 281 ? 34.540 4.423  18.976  1.00 23.85 ? 281  TYR A CG  1 
ATOM   2033 C CD1 . TYR A 1 281 ? 33.344 3.849  18.545  1.00 23.26 ? 281  TYR A CD1 1 
ATOM   2034 C CD2 . TYR A 1 281 ? 35.298 3.731  19.919  1.00 24.58 ? 281  TYR A CD2 1 
ATOM   2035 C CE1 . TYR A 1 281 ? 32.909 2.613  19.049  1.00 24.01 ? 281  TYR A CE1 1 
ATOM   2036 C CE2 . TYR A 1 281 ? 34.873 2.502  20.430  1.00 25.42 ? 281  TYR A CE2 1 
ATOM   2037 C CZ  . TYR A 1 281 ? 33.678 1.951  19.993  1.00 26.71 ? 281  TYR A CZ  1 
ATOM   2038 O OH  . TYR A 1 281 ? 33.251 0.749  20.517  1.00 27.56 ? 281  TYR A OH  1 
ATOM   2039 N N   . LYS A 1 282 ? 35.349 6.875  21.268  1.00 24.91 ? 282  LYS A N   1 
ATOM   2040 C CA  . LYS A 1 282 ? 35.427 6.704  22.713  1.00 24.15 ? 282  LYS A CA  1 
ATOM   2041 C C   . LYS A 1 282 ? 34.506 7.660  23.461  1.00 21.00 ? 282  LYS A C   1 
ATOM   2042 O O   . LYS A 1 282 ? 33.857 7.271  24.430  1.00 21.43 ? 282  LYS A O   1 
ATOM   2043 C CB  . LYS A 1 282 ? 36.861 6.905  23.209  1.00 26.58 ? 282  LYS A CB  1 
ATOM   2044 C CG  . LYS A 1 282 ? 36.963 6.917  24.724  1.00 29.70 ? 282  LYS A CG  1 
ATOM   2045 C CD  . LYS A 1 282 ? 38.399 6.834  25.208  1.00 33.24 ? 282  LYS A CD  1 
ATOM   2046 C CE  . LYS A 1 282 ? 38.449 6.892  26.728  1.00 33.20 ? 282  LYS A CE  1 
ATOM   2047 N NZ  . LYS A 1 282 ? 37.561 5.867  27.334  1.00 34.26 ? 282  LYS A NZ  1 
ATOM   2048 N N   . THR A 1 283 ? 34.456 8.909  23.013  1.00 20.20 ? 283  THR A N   1 
ATOM   2049 C CA  . THR A 1 283 ? 33.616 9.906  23.663  1.00 20.69 ? 283  THR A CA  1 
ATOM   2050 C C   . THR A 1 283 ? 32.142 9.500  23.637  1.00 19.87 ? 283  THR A C   1 
ATOM   2051 O O   . THR A 1 283 ? 31.449 9.601  24.648  1.00 17.19 ? 283  THR A O   1 
ATOM   2052 C CB  . THR A 1 283 ? 33.792 11.281 22.999  1.00 22.81 ? 283  THR A CB  1 
ATOM   2053 O OG1 . THR A 1 283 ? 35.169 11.666 23.083  1.00 24.26 ? 283  THR A OG1 1 
ATOM   2054 C CG2 . THR A 1 283 ? 32.944 12.330 23.696  1.00 19.59 ? 283  THR A CG2 1 
ATOM   2055 N N   . LEU A 1 284 ? 31.665 9.028  22.488  1.00 19.53 ? 284  LEU A N   1 
ATOM   2056 C CA  . LEU A 1 284 ? 30.272 8.605  22.383  1.00 20.06 ? 284  LEU A CA  1 
ATOM   2057 C C   . LEU A 1 284 ? 30.085 7.189  22.929  1.00 20.37 ? 284  LEU A C   1 
ATOM   2058 O O   . LEU A 1 284 ? 29.066 6.884  23.553  1.00 19.72 ? 284  LEU A O   1 
ATOM   2059 C CB  . LEU A 1 284 ? 29.796 8.668  20.923  1.00 20.02 ? 284  LEU A CB  1 
ATOM   2060 C CG  . LEU A 1 284 ? 29.867 10.041 20.238  1.00 21.86 ? 284  LEU A CG  1 
ATOM   2061 C CD1 . LEU A 1 284 ? 29.272 9.939  18.833  1.00 17.72 ? 284  LEU A CD1 1 
ATOM   2062 C CD2 . LEU A 1 284 ? 29.115 11.081 21.059  1.00 19.13 ? 284  LEU A CD2 1 
ATOM   2063 N N   . ALA A 1 285 ? 31.068 6.323  22.695  1.00 20.87 ? 285  ALA A N   1 
ATOM   2064 C CA  . ALA A 1 285 ? 30.988 4.947  23.177  1.00 21.68 ? 285  ALA A CA  1 
ATOM   2065 C C   . ALA A 1 285 ? 30.857 4.912  24.699  1.00 22.58 ? 285  ALA A C   1 
ATOM   2066 O O   . ALA A 1 285 ? 30.036 4.165  25.242  1.00 21.40 ? 285  ALA A O   1 
ATOM   2067 C CB  . ALA A 1 285 ? 32.221 4.163  22.740  1.00 22.64 ? 285  ALA A CB  1 
ATOM   2068 N N   . ASP A 1 286 ? 31.646 5.739  25.383  1.00 20.83 ? 286  ASP A N   1 
ATOM   2069 C CA  . ASP A 1 286 ? 31.613 5.775  26.840  1.00 22.75 ? 286  ASP A CA  1 
ATOM   2070 C C   . ASP A 1 286 ? 30.258 6.121  27.453  1.00 22.56 ? 286  ASP A C   1 
ATOM   2071 O O   . ASP A 1 286 ? 30.066 5.951  28.660  1.00 22.23 ? 286  ASP A O   1 
ATOM   2072 C CB  . ASP A 1 286 ? 32.673 6.737  27.389  1.00 25.02 ? 286  ASP A CB  1 
ATOM   2073 C CG  . ASP A 1 286 ? 34.095 6.205  27.229  1.00 27.43 ? 286  ASP A CG  1 
ATOM   2074 O OD1 . ASP A 1 286 ? 34.271 4.979  27.063  1.00 27.28 ? 286  ASP A OD1 1 
ATOM   2075 O OD2 . ASP A 1 286 ? 35.041 7.017  27.286  1.00 28.81 ? 286  ASP A OD2 1 
ATOM   2076 N N   . THR A 1 287 ? 29.318 6.615  26.651  1.00 21.59 ? 287  THR A N   1 
ATOM   2077 C CA  . THR A 1 287 ? 28.000 6.933  27.195  1.00 20.05 ? 287  THR A CA  1 
ATOM   2078 C C   . THR A 1 287 ? 27.267 5.627  27.491  1.00 19.65 ? 287  THR A C   1 
ATOM   2079 O O   . THR A 1 287 ? 26.363 5.585  28.319  1.00 20.67 ? 287  THR A O   1 
ATOM   2080 C CB  . THR A 1 287 ? 27.123 7.747  26.204  1.00 19.57 ? 287  THR A CB  1 
ATOM   2081 O OG1 . THR A 1 287 ? 26.939 6.995  24.999  1.00 18.71 ? 287  THR A OG1 1 
ATOM   2082 C CG2 . THR A 1 287 ? 27.766 9.091  25.885  1.00 20.74 ? 287  THR A CG2 1 
ATOM   2083 N N   . GLY A 1 288 ? 27.663 4.563  26.800  1.00 21.16 ? 288  GLY A N   1 
ATOM   2084 C CA  . GLY A 1 288 ? 27.017 3.275  26.982  1.00 19.02 ? 288  GLY A CA  1 
ATOM   2085 C C   . GLY A 1 288 ? 25.754 3.185  26.140  1.00 19.94 ? 288  GLY A C   1 
ATOM   2086 O O   . GLY A 1 288 ? 24.959 2.256  26.279  1.00 19.83 ? 288  GLY A O   1 
ATOM   2087 N N   . ALA A 1 289 ? 25.567 4.155  25.253  1.00 17.14 ? 289  ALA A N   1 
ATOM   2088 C CA  . ALA A 1 289 ? 24.385 4.179  24.403  1.00 17.32 ? 289  ALA A CA  1 
ATOM   2089 C C   . ALA A 1 289 ? 24.777 4.588  22.986  1.00 17.08 ? 289  ALA A C   1 
ATOM   2090 O O   . ALA A 1 289 ? 24.365 5.640  22.493  1.00 17.55 ? 289  ALA A O   1 
ATOM   2091 C CB  . ALA A 1 289 ? 23.362 5.156  24.972  1.00 15.44 ? 289  ALA A CB  1 
ATOM   2092 N N   . LEU A 1 290 ? 25.577 3.743  22.342  1.00 16.94 ? 290  LEU A N   1 
ATOM   2093 C CA  . LEU A 1 290 ? 26.047 4.001  20.988  1.00 16.14 ? 290  LEU A CA  1 
ATOM   2094 C C   . LEU A 1 290 ? 25.915 2.796  20.062  1.00 15.43 ? 290  LEU A C   1 
ATOM   2095 O O   . LEU A 1 290 ? 26.231 1.673  20.440  1.00 15.55 ? 290  LEU A O   1 
ATOM   2096 C CB  . LEU A 1 290 ? 27.522 4.416  21.020  1.00 16.12 ? 290  LEU A CB  1 
ATOM   2097 C CG  . LEU A 1 290 ? 28.220 4.548  19.661  1.00 16.80 ? 290  LEU A CG  1 
ATOM   2098 C CD1 . LEU A 1 290 ? 27.714 5.790  18.950  1.00 14.65 ? 290  LEU A CD1 1 
ATOM   2099 C CD2 . LEU A 1 290 ? 29.726 4.626  19.849  1.00 17.71 ? 290  LEU A CD2 1 
ATOM   2100 N N   . LEU A 1 291 ? 25.427 3.039  18.853  1.00 15.67 ? 291  LEU A N   1 
ATOM   2101 C CA  . LEU A 1 291 ? 25.335 2.000  17.834  1.00 15.87 ? 291  LEU A CA  1 
ATOM   2102 C C   . LEU A 1 291 ? 26.277 2.540  16.764  1.00 17.96 ? 291  LEU A C   1 
ATOM   2103 O O   . LEU A 1 291 ? 26.305 3.747  16.520  1.00 16.77 ? 291  LEU A O   1 
ATOM   2104 C CB  . LEU A 1 291 ? 23.917 1.867  17.286  1.00 17.33 ? 291  LEU A CB  1 
ATOM   2105 C CG  . LEU A 1 291 ? 22.984 1.028  18.166  1.00 16.62 ? 291  LEU A CG  1 
ATOM   2106 C CD1 . LEU A 1 291 ? 21.590 1.017  17.582  1.00 16.60 ? 291  LEU A CD1 1 
ATOM   2107 C CD2 . LEU A 1 291 ? 23.535 -0.389 18.273  1.00 18.36 ? 291  LEU A CD2 1 
ATOM   2108 N N   . VAL A 1 292 ? 27.061 1.660  16.150  1.00 16.67 ? 292  VAL A N   1 
ATOM   2109 C CA  . VAL A 1 292 ? 28.031 2.077  15.142  1.00 16.17 ? 292  VAL A CA  1 
ATOM   2110 C C   . VAL A 1 292 ? 27.892 1.280  13.850  1.00 16.83 ? 292  VAL A C   1 
ATOM   2111 O O   . VAL A 1 292 ? 27.896 0.046  13.868  1.00 16.91 ? 292  VAL A O   1 
ATOM   2112 C CB  . VAL A 1 292 ? 29.472 1.907  15.671  1.00 14.22 ? 292  VAL A CB  1 
ATOM   2113 C CG1 . VAL A 1 292 ? 30.476 2.403  14.624  1.00 15.61 ? 292  VAL A CG1 1 
ATOM   2114 C CG2 . VAL A 1 292 ? 29.641 2.673  16.982  1.00 14.09 ? 292  VAL A CG2 1 
ATOM   2115 N N   . TYR A 1 293 ? 27.773 1.997  12.734  1.00 17.63 ? 293  TYR A N   1 
ATOM   2116 C CA  . TYR A 1 293 ? 27.639 1.372  11.421  1.00 18.50 ? 293  TYR A CA  1 
ATOM   2117 C C   . TYR A 1 293 ? 28.667 1.921  10.455  1.00 19.81 ? 293  TYR A C   1 
ATOM   2118 O O   . TYR A 1 293 ? 28.987 3.117  10.464  1.00 18.71 ? 293  TYR A O   1 
ATOM   2119 C CB  . TYR A 1 293 ? 26.251 1.623  10.843  1.00 18.37 ? 293  TYR A CB  1 
ATOM   2120 C CG  . TYR A 1 293 ? 25.145 1.089  11.711  1.00 19.33 ? 293  TYR A CG  1 
ATOM   2121 C CD1 . TYR A 1 293 ? 24.872 -0.279 11.769  1.00 18.17 ? 293  TYR A CD1 1 
ATOM   2122 C CD2 . TYR A 1 293 ? 24.387 1.949  12.502  1.00 18.97 ? 293  TYR A CD2 1 
ATOM   2123 C CE1 . TYR A 1 293 ? 23.869 -0.773 12.598  1.00 18.52 ? 293  TYR A CE1 1 
ATOM   2124 C CE2 . TYR A 1 293 ? 23.387 1.469  13.329  1.00 20.15 ? 293  TYR A CE2 1 
ATOM   2125 C CZ  . TYR A 1 293 ? 23.129 0.112  13.375  1.00 19.56 ? 293  TYR A CZ  1 
ATOM   2126 O OH  . TYR A 1 293 ? 22.120 -0.344 14.192  1.00 19.36 ? 293  TYR A OH  1 
ATOM   2127 N N   . LYS A 1 294 ? 29.182 1.031  9.619   1.00 20.14 ? 294  LYS A N   1 
ATOM   2128 C CA  . LYS A 1 294 ? 30.171 1.401  8.626   1.00 20.93 ? 294  LYS A CA  1 
ATOM   2129 C C   . LYS A 1 294 ? 29.702 0.781  7.315   1.00 21.63 ? 294  LYS A C   1 
ATOM   2130 O O   . LYS A 1 294 ? 29.479 -0.423 7.232   1.00 22.18 ? 294  LYS A O   1 
ATOM   2131 C CB  . LYS A 1 294 ? 31.546 0.867  9.046   1.00 23.28 ? 294  LYS A CB  1 
ATOM   2132 C CG  . LYS A 1 294 ? 32.732 1.506  8.333   1.00 23.97 ? 294  LYS A CG  1 
ATOM   2133 C CD  . LYS A 1 294 ? 32.864 0.986  6.924   1.00 26.30 ? 294  LYS A CD  1 
ATOM   2134 C CE  . LYS A 1 294 ? 34.095 1.561  6.236   1.00 26.51 ? 294  LYS A CE  1 
ATOM   2135 N NZ  . LYS A 1 294 ? 34.219 0.989  4.876   1.00 27.27 ? 294  LYS A NZ  1 
ATOM   2136 N N   . ILE A 1 295 ? 29.527 1.617  6.300   1.00 22.30 ? 295  ILE A N   1 
ATOM   2137 C CA  . ILE A 1 295 ? 29.067 1.154  4.997   1.00 24.87 ? 295  ILE A CA  1 
ATOM   2138 C C   . ILE A 1 295 ? 30.187 0.592  4.125   1.00 26.30 ? 295  ILE A C   1 
ATOM   2139 O O   . ILE A 1 295 ? 31.215 1.236  3.933   1.00 26.09 ? 295  ILE A O   1 
ATOM   2140 C CB  . ILE A 1 295 ? 28.393 2.301  4.210   1.00 23.54 ? 295  ILE A CB  1 
ATOM   2141 C CG1 . ILE A 1 295 ? 27.181 2.824  4.983   1.00 21.38 ? 295  ILE A CG1 1 
ATOM   2142 C CG2 . ILE A 1 295 ? 27.987 1.821  2.824   1.00 24.05 ? 295  ILE A CG2 1 
ATOM   2143 C CD1 . ILE A 1 295 ? 26.587 4.079  4.382   1.00 22.84 ? 295  ILE A CD1 1 
ATOM   2144 N N   . ASP A 1 296 ? 29.983 -0.613 3.603   1.00 28.15 ? 296  ASP A N   1 
ATOM   2145 C CA  . ASP A 1 296 ? 30.959 -1.227 2.712   1.00 30.99 ? 296  ASP A CA  1 
ATOM   2146 C C   . ASP A 1 296 ? 30.426 -0.954 1.316   1.00 30.61 ? 296  ASP A C   1 
ATOM   2147 O O   . ASP A 1 296 ? 29.292 -1.311 1.001   1.00 32.84 ? 296  ASP A O   1 
ATOM   2148 C CB  . ASP A 1 296 ? 31.070 -2.734 2.960   1.00 31.40 ? 296  ASP A CB  1 
ATOM   2149 C CG  . ASP A 1 296 ? 31.754 -3.061 4.278   1.00 34.22 ? 296  ASP A CG  1 
ATOM   2150 O OD1 . ASP A 1 296 ? 32.574 -2.241 4.753   1.00 31.09 ? 296  ASP A OD1 1 
ATOM   2151 O OD2 . ASP A 1 296 ? 31.485 -4.149 4.826   1.00 36.28 ? 296  ASP A OD2 1 
ATOM   2152 N N   . ILE A 1 297 ? 31.241 -0.320 0.482   1.00 31.43 ? 297  ILE A N   1 
ATOM   2153 C CA  . ILE A 1 297 ? 30.806 0.053  -0.860  1.00 32.94 ? 297  ILE A CA  1 
ATOM   2154 C C   . ILE A 1 297 ? 31.039 -0.932 -1.995  1.00 32.97 ? 297  ILE A C   1 
ATOM   2155 O O   . ILE A 1 297 ? 32.000 -1.700 -1.991  1.00 34.68 ? 297  ILE A O   1 
ATOM   2156 C CB  . ILE A 1 297 ? 31.463 1.380  -1.309  1.00 32.97 ? 297  ILE A CB  1 
ATOM   2157 C CG1 . ILE A 1 297 ? 32.972 1.174  -1.477  1.00 33.43 ? 297  ILE A CG1 1 
ATOM   2158 C CG2 . ILE A 1 297 ? 31.180 2.477  -0.298  1.00 33.07 ? 297  ILE A CG2 1 
ATOM   2159 C CD1 . ILE A 1 297 ? 33.686 2.339  -2.123  1.00 33.47 ? 297  ILE A CD1 1 
ATOM   2160 N N   . ASP A 1 298 ? 30.131 -0.891 -2.965  1.00 32.87 ? 298  ASP A N   1 
ATOM   2161 C CA  . ASP A 1 298 ? 30.239 -1.700 -4.170  1.00 34.04 ? 298  ASP A CA  1 
ATOM   2162 C C   . ASP A 1 298 ? 31.128 -0.784 -5.002  1.00 32.87 ? 298  ASP A C   1 
ATOM   2163 O O   . ASP A 1 298 ? 30.687 0.278  -5.452  1.00 30.66 ? 298  ASP A O   1 
ATOM   2164 C CB  . ASP A 1 298 ? 28.866 -1.868 -4.830  1.00 37.46 ? 298  ASP A CB  1 
ATOM   2165 C CG  . ASP A 1 298 ? 28.936 -2.628 -6.144  1.00 41.02 ? 298  ASP A CG  1 
ATOM   2166 O OD1 . ASP A 1 298 ? 29.542 -2.110 -7.108  1.00 42.98 ? 298  ASP A OD1 1 
ATOM   2167 O OD2 . ASP A 1 298 ? 28.387 -3.748 -6.213  1.00 43.88 ? 298  ASP A OD2 1 
ATOM   2168 N N   . TYR A 1 299 ? 32.385 -1.176 -5.175  1.00 31.16 ? 299  TYR A N   1 
ATOM   2169 C CA  . TYR A 1 299 ? 33.345 -0.359 -5.904  1.00 31.88 ? 299  TYR A CA  1 
ATOM   2170 C C   . TYR A 1 299 ? 32.870 0.233  -7.229  1.00 32.44 ? 299  TYR A C   1 
ATOM   2171 O O   . TYR A 1 299 ? 32.844 1.451  -7.391  1.00 29.76 ? 299  TYR A O   1 
ATOM   2172 C CB  . TYR A 1 299 ? 34.625 -1.147 -6.158  1.00 31.91 ? 299  TYR A CB  1 
ATOM   2173 C CG  . TYR A 1 299 ? 35.786 -0.266 -6.562  1.00 33.20 ? 299  TYR A CG  1 
ATOM   2174 C CD1 . TYR A 1 299 ? 36.590 0.338  -5.599  1.00 31.96 ? 299  TYR A CD1 1 
ATOM   2175 C CD2 . TYR A 1 299 ? 36.077 -0.030 -7.909  1.00 34.00 ? 299  TYR A CD2 1 
ATOM   2176 C CE1 . TYR A 1 299 ? 37.659 1.149  -5.958  1.00 31.65 ? 299  TYR A CE1 1 
ATOM   2177 C CE2 . TYR A 1 299 ? 37.148 0.786  -8.282  1.00 33.38 ? 299  TYR A CE2 1 
ATOM   2178 C CZ  . TYR A 1 299 ? 37.935 1.367  -7.298  1.00 34.27 ? 299  TYR A CZ  1 
ATOM   2179 O OH  . TYR A 1 299 ? 39.014 2.143  -7.647  1.00 34.38 ? 299  TYR A OH  1 
ATOM   2180 N N   . GLU A 1 300 ? 32.515 -0.625 -8.180  1.00 32.54 ? 300  GLU A N   1 
ATOM   2181 C CA  . GLU A 1 300 ? 32.073 -0.155 -9.488  1.00 34.01 ? 300  GLU A CA  1 
ATOM   2182 C C   . GLU A 1 300 ? 30.925 0.844  -9.415  1.00 32.09 ? 300  GLU A C   1 
ATOM   2183 O O   . GLU A 1 300 ? 31.004 1.933  -9.985  1.00 30.58 ? 300  GLU A O   1 
ATOM   2184 C CB  . GLU A 1 300 ? 31.673 -1.340 -10.372 1.00 37.18 ? 300  GLU A CB  1 
ATOM   2185 C CG  . GLU A 1 300 ? 32.850 -2.047 -11.025 1.00 44.12 ? 300  GLU A CG  1 
ATOM   2186 C CD  . GLU A 1 300 ? 33.540 -1.189 -12.075 1.00 48.27 ? 300  GLU A CD  1 
ATOM   2187 O OE1 . GLU A 1 300 ? 34.542 -1.651 -12.666 1.00 51.32 ? 300  GLU A OE1 1 
ATOM   2188 O OE2 . GLU A 1 300 ? 33.080 -0.053 -12.314 1.00 50.94 ? 300  GLU A OE2 1 
ATOM   2189 N N   . ALA A 1 301 ? 29.862 0.472  -8.711  1.00 29.84 ? 301  ALA A N   1 
ATOM   2190 C CA  . ALA A 1 301 ? 28.704 1.340  -8.580  1.00 28.81 ? 301  ALA A CA  1 
ATOM   2191 C C   . ALA A 1 301 ? 29.082 2.679  -7.958  1.00 28.13 ? 301  ALA A C   1 
ATOM   2192 O O   . ALA A 1 301 ? 28.596 3.726  -8.383  1.00 27.91 ? 301  ALA A O   1 
ATOM   2193 C CB  . ALA A 1 301 ? 27.625 0.655  -7.740  1.00 29.27 ? 301  ALA A CB  1 
ATOM   2194 N N   . THR A 1 302 ? 29.948 2.647  -6.951  1.00 26.57 ? 302  THR A N   1 
ATOM   2195 C CA  . THR A 1 302 ? 30.364 3.874  -6.282  1.00 25.01 ? 302  THR A CA  1 
ATOM   2196 C C   . THR A 1 302 ? 31.273 4.717  -7.164  1.00 24.91 ? 302  THR A C   1 
ATOM   2197 O O   . THR A 1 302 ? 31.176 5.945  -7.175  1.00 23.99 ? 302  THR A O   1 
ATOM   2198 C CB  . THR A 1 302 ? 31.096 3.568  -4.972  1.00 26.45 ? 302  THR A CB  1 
ATOM   2199 O OG1 . THR A 1 302 ? 30.248 2.774  -4.132  1.00 28.21 ? 302  THR A OG1 1 
ATOM   2200 C CG2 . THR A 1 302 ? 31.458 4.864  -4.250  1.00 23.15 ? 302  THR A CG2 1 
ATOM   2201 N N   . GLU A 1 303 ? 32.158 4.051  -7.900  1.00 24.18 ? 303  GLU A N   1 
ATOM   2202 C CA  . GLU A 1 303 ? 33.077 4.739  -8.801  1.00 25.78 ? 303  GLU A CA  1 
ATOM   2203 C C   . GLU A 1 303 ? 32.276 5.554  -9.817  1.00 26.25 ? 303  GLU A C   1 
ATOM   2204 O O   . GLU A 1 303 ? 32.547 6.736  -10.041 1.00 25.22 ? 303  GLU A O   1 
ATOM   2205 C CB  . GLU A 1 303 ? 33.945 3.725  -9.546  1.00 25.69 ? 303  GLU A CB  1 
ATOM   2206 C CG  . GLU A 1 303 ? 34.958 4.357  -10.488 1.00 28.61 ? 303  GLU A CG  1 
ATOM   2207 C CD  . GLU A 1 303 ? 35.636 3.333  -11.373 1.00 30.66 ? 303  GLU A CD  1 
ATOM   2208 O OE1 . GLU A 1 303 ? 34.996 2.850  -12.330 1.00 32.11 ? 303  GLU A OE1 1 
ATOM   2209 O OE2 . GLU A 1 303 ? 36.803 2.997  -11.103 1.00 32.44 ? 303  GLU A OE2 1 
ATOM   2210 N N   . GLU A 1 304 ? 31.294 4.904  -10.433 1.00 26.86 ? 304  GLU A N   1 
ATOM   2211 C CA  . GLU A 1 304 ? 30.448 5.555  -11.423 1.00 29.42 ? 304  GLU A CA  1 
ATOM   2212 C C   . GLU A 1 304 ? 29.717 6.733  -10.798 1.00 28.13 ? 304  GLU A C   1 
ATOM   2213 O O   . GLU A 1 304 ? 29.692 7.828  -11.355 1.00 28.94 ? 304  GLU A O   1 
ATOM   2214 C CB  . GLU A 1 304 ? 29.419 4.568  -11.977 1.00 31.47 ? 304  GLU A CB  1 
ATOM   2215 C CG  . GLU A 1 304 ? 28.506 5.173  -13.035 1.00 37.06 ? 304  GLU A CG  1 
ATOM   2216 C CD  . GLU A 1 304 ? 27.378 4.244  -13.438 1.00 41.11 ? 304  GLU A CD  1 
ATOM   2217 O OE1 . GLU A 1 304 ? 26.460 4.024  -12.616 1.00 44.92 ? 304  GLU A OE1 1 
ATOM   2218 O OE2 . GLU A 1 304 ? 27.410 3.731  -14.575 1.00 43.25 ? 304  GLU A OE2 1 
ATOM   2219 N N   . ARG A 1 305 ? 29.122 6.492  -9.636  1.00 28.21 ? 305  ARG A N   1 
ATOM   2220 C CA  . ARG A 1 305 ? 28.368 7.511  -8.921  1.00 28.04 ? 305  ARG A CA  1 
ATOM   2221 C C   . ARG A 1 305 ? 29.203 8.752  -8.630  1.00 25.91 ? 305  ARG A C   1 
ATOM   2222 O O   . ARG A 1 305 ? 28.770 9.876  -8.892  1.00 26.11 ? 305  ARG A O   1 
ATOM   2223 C CB  . ARG A 1 305 ? 27.813 6.926  -7.614  1.00 30.34 ? 305  ARG A CB  1 
ATOM   2224 C CG  . ARG A 1 305 ? 26.904 7.866  -6.842  1.00 34.61 ? 305  ARG A CG  1 
ATOM   2225 C CD  . ARG A 1 305 ? 26.235 7.178  -5.653  1.00 36.72 ? 305  ARG A CD  1 
ATOM   2226 N NE  . ARG A 1 305 ? 25.423 6.029  -6.053  1.00 40.93 ? 305  ARG A NE  1 
ATOM   2227 C CZ  . ARG A 1 305 ? 25.851 4.768  -6.052  1.00 44.00 ? 305  ARG A CZ  1 
ATOM   2228 N NH1 . ARG A 1 305 ? 27.088 4.483  -5.665  1.00 44.27 ? 305  ARG A NH1 1 
ATOM   2229 N NH2 . ARG A 1 305 ? 25.042 3.790  -6.441  1.00 46.15 ? 305  ARG A NH2 1 
ATOM   2230 N N   . VAL A 1 306 ? 30.398 8.553  -8.087  1.00 23.09 ? 306  VAL A N   1 
ATOM   2231 C CA  . VAL A 1 306 ? 31.274 9.672  -7.769  1.00 21.05 ? 306  VAL A CA  1 
ATOM   2232 C C   . VAL A 1 306 ? 31.808 10.332 -9.042  1.00 20.44 ? 306  VAL A C   1 
ATOM   2233 O O   . VAL A 1 306 ? 32.016 11.544 -9.079  1.00 20.13 ? 306  VAL A O   1 
ATOM   2234 C CB  . VAL A 1 306 ? 32.465 9.222  -6.893  1.00 22.02 ? 306  VAL A CB  1 
ATOM   2235 C CG1 . VAL A 1 306 ? 33.438 10.386 -6.694  1.00 25.01 ? 306  VAL A CG1 1 
ATOM   2236 C CG2 . VAL A 1 306 ? 31.962 8.743  -5.541  1.00 22.48 ? 306  VAL A CG2 1 
ATOM   2237 N N   . ALA A 1 307 ? 32.038 9.533  -10.079 1.00 19.74 ? 307  ALA A N   1 
ATOM   2238 C CA  . ALA A 1 307 ? 32.530 10.069 -11.347 1.00 20.28 ? 307  ALA A CA  1 
ATOM   2239 C C   . ALA A 1 307 ? 31.474 11.014 -11.920 1.00 22.00 ? 307  ALA A C   1 
ATOM   2240 O O   . ALA A 1 307 ? 31.786 12.119 -12.353 1.00 22.62 ? 307  ALA A O   1 
ATOM   2241 C CB  . ALA A 1 307 ? 32.811 8.935  -12.322 1.00 18.69 ? 307  ALA A CB  1 
ATOM   2242 N N   . LYS A 1 308 ? 30.218 10.577 -11.910 1.00 24.66 ? 308  LYS A N   1 
ATOM   2243 C CA  . LYS A 1 308 ? 29.128 11.404 -12.425 1.00 26.47 ? 308  LYS A CA  1 
ATOM   2244 C C   . LYS A 1 308 ? 28.974 12.687 -11.619 1.00 26.86 ? 308  LYS A C   1 
ATOM   2245 O O   . LYS A 1 308 ? 28.713 13.745 -12.185 1.00 26.60 ? 308  LYS A O   1 
ATOM   2246 C CB  . LYS A 1 308 ? 27.806 10.641 -12.399 1.00 27.86 ? 308  LYS A CB  1 
ATOM   2247 C CG  . LYS A 1 308 ? 27.716 9.478  -13.354 1.00 29.10 ? 308  LYS A CG  1 
ATOM   2248 C CD  . LYS A 1 308 ? 26.303 8.918  -13.330 1.00 33.15 ? 308  LYS A CD  1 
ATOM   2249 C CE  . LYS A 1 308 ? 26.137 7.740  -14.262 1.00 33.97 ? 308  LYS A CE  1 
ATOM   2250 N NZ  . LYS A 1 308 ? 24.743 7.217  -14.190 1.00 37.19 ? 308  LYS A NZ  1 
ATOM   2251 N N   . ARG A 1 309 ? 29.134 12.601 -10.300 1.00 27.95 ? 309  ARG A N   1 
ATOM   2252 C CA  . ARG A 1 309 ? 29.006 13.789 -9.457  1.00 29.01 ? 309  ARG A CA  1 
ATOM   2253 C C   . ARG A 1 309 ? 30.036 14.848 -9.822  1.00 27.88 ? 309  ARG A C   1 
ATOM   2254 O O   . ARG A 1 309 ? 29.715 16.032 -9.930  1.00 28.43 ? 309  ARG A O   1 
ATOM   2255 C CB  . ARG A 1 309 ? 29.158 13.430 -7.980  1.00 32.13 ? 309  ARG A CB  1 
ATOM   2256 C CG  . ARG A 1 309 ? 28.009 12.622 -7.421  1.00 35.64 ? 309  ARG A CG  1 
ATOM   2257 C CD  . ARG A 1 309 ? 28.184 12.429 -5.926  1.00 37.83 ? 309  ARG A CD  1 
ATOM   2258 N NE  . ARG A 1 309 ? 27.137 11.594 -5.344  1.00 38.79 ? 309  ARG A NE  1 
ATOM   2259 C CZ  . ARG A 1 309 ? 27.125 11.209 -4.071  1.00 37.54 ? 309  ARG A CZ  1 
ATOM   2260 N NH1 . ARG A 1 309 ? 28.104 11.590 -3.258  1.00 35.12 ? 309  ARG A NH1 1 
ATOM   2261 N NH2 . ARG A 1 309 ? 26.142 10.443 -3.615  1.00 37.06 ? 309  ARG A NH2 1 
ATOM   2262 N N   . HIS A 1 310 ? 31.277 14.418 -10.008 1.00 26.64 ? 310  HIS A N   1 
ATOM   2263 C CA  . HIS A 1 310 ? 32.348 15.329 -10.374 1.00 26.92 ? 310  HIS A CA  1 
ATOM   2264 C C   . HIS A 1 310 ? 32.106 15.932 -11.752 1.00 26.05 ? 310  HIS A C   1 
ATOM   2265 O O   . HIS A 1 310 ? 32.481 17.071 -12.009 1.00 23.86 ? 310  HIS A O   1 
ATOM   2266 C CB  . HIS A 1 310 ? 33.688 14.594 -10.347 1.00 30.74 ? 310  HIS A CB  1 
ATOM   2267 C CG  . HIS A 1 310 ? 34.166 14.268 -8.966  1.00 35.26 ? 310  HIS A CG  1 
ATOM   2268 N ND1 . HIS A 1 310 ? 33.326 13.799 -7.980  1.00 37.93 ? 310  HIS A ND1 1 
ATOM   2269 C CD2 . HIS A 1 310 ? 35.395 14.344 -8.407  1.00 37.04 ? 310  HIS A CD2 1 
ATOM   2270 C CE1 . HIS A 1 310 ? 34.017 13.603 -6.871  1.00 38.26 ? 310  HIS A CE1 1 
ATOM   2271 N NE2 . HIS A 1 310 ? 35.275 13.926 -7.104  1.00 39.58 ? 310  HIS A NE2 1 
ATOM   2272 N N   . LEU A 1 311 ? 31.486 15.162 -12.643 1.00 26.17 ? 311  LEU A N   1 
ATOM   2273 C CA  . LEU A 1 311 ? 31.198 15.650 -13.986 1.00 26.19 ? 311  LEU A CA  1 
ATOM   2274 C C   . LEU A 1 311 ? 30.113 16.718 -13.924 1.00 27.90 ? 311  LEU A C   1 
ATOM   2275 O O   . LEU A 1 311 ? 30.243 17.782 -14.523 1.00 29.36 ? 311  LEU A O   1 
ATOM   2276 C CB  . LEU A 1 311 ? 30.739 14.500 -14.891 1.00 24.71 ? 311  LEU A CB  1 
ATOM   2277 C CG  . LEU A 1 311 ? 30.375 14.892 -16.328 1.00 24.05 ? 311  LEU A CG  1 
ATOM   2278 C CD1 . LEU A 1 311 ? 31.601 15.460 -17.032 1.00 23.69 ? 311  LEU A CD1 1 
ATOM   2279 C CD2 . LEU A 1 311 ? 29.854 13.678 -17.081 1.00 21.80 ? 311  LEU A CD2 1 
ATOM   2280 N N   . GLN A 1 312 ? 29.047 16.429 -13.186 1.00 30.55 ? 312  GLN A N   1 
ATOM   2281 C CA  . GLN A 1 312 ? 27.930 17.355 -13.041 1.00 32.94 ? 312  GLN A CA  1 
ATOM   2282 C C   . GLN A 1 312 ? 28.367 18.624 -12.314 1.00 34.52 ? 312  GLN A C   1 
ATOM   2283 O O   . GLN A 1 312 ? 27.768 19.682 -12.486 1.00 33.80 ? 312  GLN A O   1 
ATOM   2284 C CB  . GLN A 1 312 ? 26.792 16.691 -12.260 1.00 34.69 ? 312  GLN A CB  1 
ATOM   2285 C CG  . GLN A 1 312 ? 26.412 15.305 -12.760 1.00 40.30 ? 312  GLN A CG  1 
ATOM   2286 C CD  . GLN A 1 312 ? 25.367 14.631 -11.884 1.00 44.00 ? 312  GLN A CD  1 
ATOM   2287 O OE1 . GLN A 1 312 ? 25.356 14.807 -10.662 1.00 46.29 ? 312  GLN A OE1 1 
ATOM   2288 N NE2 . GLN A 1 312 ? 24.496 13.837 -12.501 1.00 44.28 ? 312  GLN A NE2 1 
ATOM   2289 N N   . SER A 1 313 ? 29.412 18.513 -11.503 1.00 35.71 ? 313  SER A N   1 
ATOM   2290 C CA  . SER A 1 313 ? 29.916 19.651 -10.743 1.00 37.50 ? 313  SER A CA  1 
ATOM   2291 C C   . SER A 1 313 ? 30.960 20.450 -11.515 1.00 37.72 ? 313  SER A C   1 
ATOM   2292 O O   . SER A 1 313 ? 31.326 21.548 -11.113 1.00 38.89 ? 313  SER A O   1 
ATOM   2293 C CB  . SER A 1 313 ? 30.516 19.175 -9.418  1.00 39.12 ? 313  SER A CB  1 
ATOM   2294 O OG  . SER A 1 313 ? 29.578 18.408 -8.684  1.00 40.49 ? 313  SER A OG  1 
ATOM   2295 N N   . GLY A 1 314 ? 31.446 19.894 -12.618 1.00 38.22 ? 314  GLY A N   1 
ATOM   2296 C CA  . GLY A 1 314 ? 32.433 20.600 -13.416 1.00 37.29 ? 314  GLY A CA  1 
ATOM   2297 C C   . GLY A 1 314 ? 33.886 20.288 -13.113 1.00 37.21 ? 314  GLY A C   1 
ATOM   2298 O O   . GLY A 1 314 ? 34.777 20.783 -13.801 1.00 37.53 ? 314  GLY A O   1 
ATOM   2299 N N   . LEU A 1 315 ? 34.136 19.469 -12.095 1.00 37.57 ? 315  LEU A N   1 
ATOM   2300 C CA  . LEU A 1 315 ? 35.505 19.112 -11.724 1.00 37.60 ? 315  LEU A CA  1 
ATOM   2301 C C   . LEU A 1 315 ? 36.253 18.394 -12.844 1.00 36.48 ? 315  LEU A C   1 
ATOM   2302 O O   . LEU A 1 315 ? 37.476 18.484 -12.936 1.00 38.03 ? 315  LEU A O   1 
ATOM   2303 C CB  . LEU A 1 315 ? 35.506 18.234 -10.467 1.00 40.43 ? 315  LEU A CB  1 
ATOM   2304 C CG  . LEU A 1 315 ? 35.191 18.901 -9.123  1.00 42.85 ? 315  LEU A CG  1 
ATOM   2305 C CD1 . LEU A 1 315 ? 33.819 19.555 -9.157  1.00 44.53 ? 315  LEU A CD1 1 
ATOM   2306 C CD2 . LEU A 1 315 ? 35.252 17.855 -8.020  1.00 44.77 ? 315  LEU A CD2 1 
ATOM   2307 N N   . VAL A 1 316 ? 35.519 17.673 -13.685 1.00 34.14 ? 316  VAL A N   1 
ATOM   2308 C CA  . VAL A 1 316 ? 36.120 16.948 -14.801 1.00 31.17 ? 316  VAL A CA  1 
ATOM   2309 C C   . VAL A 1 316 ? 35.318 17.219 -16.071 1.00 29.05 ? 316  VAL A C   1 
ATOM   2310 O O   . VAL A 1 316 ? 34.168 17.639 -15.998 1.00 29.13 ? 316  VAL A O   1 
ATOM   2311 C CB  . VAL A 1 316 ? 36.157 15.426 -14.525 1.00 30.07 ? 316  VAL A CB  1 
ATOM   2312 C CG1 . VAL A 1 316 ? 37.021 15.145 -13.294 1.00 30.83 ? 316  VAL A CG1 1 
ATOM   2313 C CG2 . VAL A 1 316 ? 34.747 14.897 -14.314 1.00 24.93 ? 316  VAL A CG2 1 
ATOM   2314 N N   . THR A 1 317 ? 35.918 16.980 -17.233 1.00 29.00 ? 317  THR A N   1 
ATOM   2315 C CA  . THR A 1 317 ? 35.216 17.234 -18.489 1.00 28.05 ? 317  THR A CA  1 
ATOM   2316 C C   . THR A 1 317 ? 34.511 16.007 -19.060 1.00 25.86 ? 317  THR A C   1 
ATOM   2317 O O   . THR A 1 317 ? 33.619 16.139 -19.896 1.00 26.56 ? 317  THR A O   1 
ATOM   2318 C CB  . THR A 1 317 ? 36.171 17.794 -19.565 1.00 28.71 ? 317  THR A CB  1 
ATOM   2319 O OG1 . THR A 1 317 ? 37.036 16.753 -20.036 1.00 30.20 ? 317  THR A OG1 1 
ATOM   2320 C CG2 . THR A 1 317 ? 37.005 18.924 -18.987 1.00 26.77 ? 317  THR A CG2 1 
ATOM   2321 N N   . THR A 1 318 ? 34.913 14.822 -18.610 1.00 23.85 ? 318  THR A N   1 
ATOM   2322 C CA  . THR A 1 318 ? 34.311 13.574 -19.077 1.00 23.86 ? 318  THR A CA  1 
ATOM   2323 C C   . THR A 1 318 ? 34.192 12.595 -17.918 1.00 24.18 ? 318  THR A C   1 
ATOM   2324 O O   . THR A 1 318 ? 34.877 12.739 -16.902 1.00 25.40 ? 318  THR A O   1 
ATOM   2325 C CB  . THR A 1 318 ? 35.164 12.881 -20.152 1.00 23.88 ? 318  THR A CB  1 
ATOM   2326 O OG1 . THR A 1 318 ? 36.413 12.493 -19.570 1.00 21.71 ? 318  THR A OG1 1 
ATOM   2327 C CG2 . THR A 1 318 ? 35.413 13.804 -21.350 1.00 23.33 ? 318  THR A CG2 1 
ATOM   2328 N N   . ILE A 1 319 ? 33.341 11.589 -18.079 1.00 23.11 ? 319  ILE A N   1 
ATOM   2329 C CA  . ILE A 1 319 ? 33.150 10.582 -17.037 1.00 22.50 ? 319  ILE A CA  1 
ATOM   2330 C C   . ILE A 1 319 ? 34.448 9.778  -16.834 1.00 21.54 ? 319  ILE A C   1 
ATOM   2331 O O   . ILE A 1 319 ? 34.753 9.353  -15.717 1.00 19.78 ? 319  ILE A O   1 
ATOM   2332 C CB  . ILE A 1 319 ? 31.970 9.629  -17.404 1.00 22.97 ? 319  ILE A CB  1 
ATOM   2333 C CG1 . ILE A 1 319 ? 31.570 8.781  -16.196 1.00 23.10 ? 319  ILE A CG1 1 
ATOM   2334 C CG2 . ILE A 1 319 ? 32.353 8.740  -18.563 1.00 20.02 ? 319  ILE A CG2 1 
ATOM   2335 C CD1 . ILE A 1 319 ? 30.725 9.526  -15.191 1.00 27.95 ? 319  ILE A CD1 1 
ATOM   2336 N N   . ALA A 1 320 ? 35.213 9.583  -17.908 1.00 19.89 ? 320  ALA A N   1 
ATOM   2337 C CA  . ALA A 1 320 ? 36.477 8.847  -17.825 1.00 21.19 ? 320  ALA A CA  1 
ATOM   2338 C C   . ALA A 1 320 ? 37.446 9.540  -16.860 1.00 20.36 ? 320  ALA A C   1 
ATOM   2339 O O   . ALA A 1 320 ? 38.125 8.889  -16.064 1.00 21.03 ? 320  ALA A O   1 
ATOM   2340 C CB  . ALA A 1 320 ? 37.117 8.729  -19.208 1.00 21.10 ? 320  ALA A CB  1 
ATOM   2341 N N   . GLU A 1 321 ? 37.516 10.862 -16.940 1.00 21.61 ? 321  GLU A N   1 
ATOM   2342 C CA  . GLU A 1 321 ? 38.385 11.619 -16.052 1.00 22.10 ? 321  GLU A CA  1 
ATOM   2343 C C   . GLU A 1 321 ? 37.875 11.456 -14.620 1.00 22.18 ? 321  GLU A C   1 
ATOM   2344 O O   . GLU A 1 321 ? 38.658 11.297 -13.680 1.00 21.66 ? 321  GLU A O   1 
ATOM   2345 C CB  . GLU A 1 321 ? 38.387 13.089 -16.461 1.00 24.58 ? 321  GLU A CB  1 
ATOM   2346 C CG  . GLU A 1 321 ? 39.252 13.378 -17.683 1.00 28.50 ? 321  GLU A CG  1 
ATOM   2347 C CD  . GLU A 1 321 ? 38.868 14.665 -18.383 1.00 30.46 ? 321  GLU A CD  1 
ATOM   2348 O OE1 . GLU A 1 321 ? 38.536 15.647 -17.690 1.00 35.98 ? 321  GLU A OE1 1 
ATOM   2349 O OE2 . GLU A 1 321 ? 38.904 14.699 -19.628 1.00 35.83 ? 321  GLU A OE2 1 
ATOM   2350 N N   . GLY A 1 322 ? 36.554 11.480 -14.467 1.00 21.15 ? 322  GLY A N   1 
ATOM   2351 C CA  . GLY A 1 322 ? 35.957 11.319 -13.154 1.00 21.54 ? 322  GLY A CA  1 
ATOM   2352 C C   . GLY A 1 322 ? 36.335 9.989  -12.534 1.00 21.74 ? 322  GLY A C   1 
ATOM   2353 O O   . GLY A 1 322 ? 36.653 9.926  -11.349 1.00 21.58 ? 322  GLY A O   1 
ATOM   2354 N N   . ARG A 1 323 ? 36.305 8.925  -13.334 1.00 22.26 ? 323  ARG A N   1 
ATOM   2355 C CA  . ARG A 1 323 ? 36.646 7.586  -12.854 1.00 24.87 ? 323  ARG A CA  1 
ATOM   2356 C C   . ARG A 1 323 ? 38.109 7.473  -12.429 1.00 25.66 ? 323  ARG A C   1 
ATOM   2357 O O   . ARG A 1 323 ? 38.421 6.885  -11.395 1.00 25.81 ? 323  ARG A O   1 
ATOM   2358 C CB  . ARG A 1 323 ? 36.362 6.537  -13.940 1.00 24.98 ? 323  ARG A CB  1 
ATOM   2359 C CG  . ARG A 1 323 ? 34.892 6.358  -14.298 1.00 25.27 ? 323  ARG A CG  1 
ATOM   2360 C CD  . ARG A 1 323 ? 34.739 5.398  -15.482 1.00 29.80 ? 323  ARG A CD  1 
ATOM   2361 N NE  . ARG A 1 323 ? 33.343 5.136  -15.829 1.00 31.75 ? 323  ARG A NE  1 
ATOM   2362 C CZ  . ARG A 1 323 ? 32.495 4.449  -15.068 1.00 34.85 ? 323  ARG A CZ  1 
ATOM   2363 N NH1 . ARG A 1 323 ? 32.893 3.945  -13.905 1.00 34.79 ? 323  ARG A NH1 1 
ATOM   2364 N NH2 . ARG A 1 323 ? 31.244 4.263  -15.468 1.00 35.65 ? 323  ARG A NH2 1 
ATOM   2365 N N   . GLU A 1 324 ? 39.007 8.021  -13.238 1.00 29.32 ? 324  GLU A N   1 
ATOM   2366 C CA  . GLU A 1 324 ? 40.429 7.961  -12.928 1.00 31.84 ? 324  GLU A CA  1 
ATOM   2367 C C   . GLU A 1 324 ? 40.714 8.717  -11.643 1.00 32.61 ? 324  GLU A C   1 
ATOM   2368 O O   . GLU A 1 324 ? 41.543 8.296  -10.839 1.00 33.44 ? 324  GLU A O   1 
ATOM   2369 C CB  . GLU A 1 324 ? 41.254 8.554  -14.071 1.00 34.87 ? 324  GLU A CB  1 
ATOM   2370 C CG  . GLU A 1 324 ? 42.761 8.534  -13.815 1.00 42.41 ? 324  GLU A CG  1 
ATOM   2371 C CD  . GLU A 1 324 ? 43.275 7.149  -13.439 1.00 45.95 ? 324  GLU A CD  1 
ATOM   2372 O OE1 . GLU A 1 324 ? 43.108 6.208  -14.248 1.00 48.41 ? 324  GLU A OE1 1 
ATOM   2373 O OE2 . GLU A 1 324 ? 43.846 7.000  -12.336 1.00 46.13 ? 324  GLU A OE2 1 
ATOM   2374 N N   . LYS A 1 325 ? 40.017 9.834  -11.456 1.00 31.17 ? 325  LYS A N   1 
ATOM   2375 C CA  . LYS A 1 325 ? 40.177 10.654 -10.263 1.00 31.73 ? 325  LYS A CA  1 
ATOM   2376 C C   . LYS A 1 325 ? 39.776 9.849  -9.029  1.00 28.40 ? 325  LYS A C   1 
ATOM   2377 O O   . LYS A 1 325 ? 40.408 9.936  -7.979  1.00 28.63 ? 325  LYS A O   1 
ATOM   2378 C CB  . LYS A 1 325 ? 39.306 11.907 -10.380 1.00 34.40 ? 325  LYS A CB  1 
ATOM   2379 C CG  . LYS A 1 325 ? 39.343 12.810 -9.171  1.00 39.60 ? 325  LYS A CG  1 
ATOM   2380 C CD  . LYS A 1 325 ? 38.531 14.069 -9.404  1.00 44.01 ? 325  LYS A CD  1 
ATOM   2381 C CE  . LYS A 1 325 ? 38.565 14.974 -8.184  1.00 47.04 ? 325  LYS A CE  1 
ATOM   2382 N NZ  . LYS A 1 325 ? 37.748 16.199 -8.396  1.00 49.89 ? 325  LYS A NZ  1 
ATOM   2383 N N   . PHE A 1 326 ? 38.721 9.061  -9.173  1.00 26.38 ? 326  PHE A N   1 
ATOM   2384 C CA  . PHE A 1 326 ? 38.222 8.228  -8.088  1.00 25.84 ? 326  PHE A CA  1 
ATOM   2385 C C   . PHE A 1 326 ? 39.238 7.135  -7.766  1.00 26.90 ? 326  PHE A C   1 
ATOM   2386 O O   . PHE A 1 326 ? 39.586 6.912  -6.606  1.00 25.89 ? 326  PHE A O   1 
ATOM   2387 C CB  . PHE A 1 326 ? 36.899 7.590  -8.512  1.00 25.22 ? 326  PHE A CB  1 
ATOM   2388 C CG  . PHE A 1 326 ? 36.298 6.670  -7.484  1.00 26.36 ? 326  PHE A CG  1 
ATOM   2389 C CD1 . PHE A 1 326 ? 35.528 7.176  -6.439  1.00 25.43 ? 326  PHE A CD1 1 
ATOM   2390 C CD2 . PHE A 1 326 ? 36.474 5.289  -7.582  1.00 24.98 ? 326  PHE A CD2 1 
ATOM   2391 C CE1 . PHE A 1 326 ? 34.937 6.320  -5.511  1.00 24.68 ? 326  PHE A CE1 1 
ATOM   2392 C CE2 . PHE A 1 326 ? 35.889 4.428  -6.660  1.00 25.72 ? 326  PHE A CE2 1 
ATOM   2393 C CZ  . PHE A 1 326 ? 35.117 4.944  -5.622  1.00 24.55 ? 326  PHE A CZ  1 
ATOM   2394 N N   . ARG A 1 327 ? 39.717 6.463  -8.808  1.00 28.18 ? 327  ARG A N   1 
ATOM   2395 C CA  . ARG A 1 327 ? 40.672 5.371  -8.656  1.00 30.14 ? 327  ARG A CA  1 
ATOM   2396 C C   . ARG A 1 327 ? 42.018 5.769  -8.053  1.00 29.73 ? 327  ARG A C   1 
ATOM   2397 O O   . ARG A 1 327 ? 42.604 5.004  -7.284  1.00 29.47 ? 327  ARG A O   1 
ATOM   2398 C CB  . ARG A 1 327 ? 40.899 4.689  -10.011 1.00 31.33 ? 327  ARG A CB  1 
ATOM   2399 C CG  . ARG A 1 327 ? 39.647 4.026  -10.574 1.00 34.89 ? 327  ARG A CG  1 
ATOM   2400 C CD  . ARG A 1 327 ? 39.893 3.359  -11.925 1.00 38.12 ? 327  ARG A CD  1 
ATOM   2401 N NE  . ARG A 1 327 ? 40.377 4.301  -12.935 1.00 43.29 ? 327  ARG A NE  1 
ATOM   2402 C CZ  . ARG A 1 327 ? 40.516 4.011  -14.228 1.00 45.22 ? 327  ARG A CZ  1 
ATOM   2403 N NH1 . ARG A 1 327 ? 40.204 2.801  -14.677 1.00 46.69 ? 327  ARG A NH1 1 
ATOM   2404 N NH2 . ARG A 1 327 ? 40.976 4.928  -15.073 1.00 43.39 ? 327  ARG A NH2 1 
ATOM   2405 N N   . SER A 1 328 ? 42.504 6.960  -8.390  1.00 28.13 ? 328  SER A N   1 
ATOM   2406 C CA  . SER A 1 328 ? 43.793 7.406  -7.885  1.00 29.76 ? 328  SER A CA  1 
ATOM   2407 C C   . SER A 1 328 ? 43.743 8.223  -6.594  1.00 29.51 ? 328  SER A C   1 
ATOM   2408 O O   . SER A 1 328 ? 44.786 8.487  -5.998  1.00 29.98 ? 328  SER A O   1 
ATOM   2409 C CB  . SER A 1 328 ? 44.524 8.207  -8.964  1.00 31.92 ? 328  SER A CB  1 
ATOM   2410 O OG  . SER A 1 328 ? 43.827 9.398  -9.273  1.00 32.22 ? 328  SER A OG  1 
ATOM   2411 N N   . ASN A 1 329 ? 42.546 8.623  -6.166  1.00 28.26 ? 329  ASN A N   1 
ATOM   2412 C CA  . ASN A 1 329 ? 42.399 9.410  -4.942  1.00 26.37 ? 329  ASN A CA  1 
ATOM   2413 C C   . ASN A 1 329 ? 41.830 8.560  -3.804  1.00 26.34 ? 329  ASN A C   1 
ATOM   2414 O O   . ASN A 1 329 ? 40.622 8.328  -3.739  1.00 24.53 ? 329  ASN A O   1 
ATOM   2415 C CB  . ASN A 1 329 ? 41.476 10.605 -5.185  1.00 27.32 ? 329  ASN A CB  1 
ATOM   2416 C CG  . ASN A 1 329 ? 41.532 11.624 -4.057  1.00 29.06 ? 329  ASN A CG  1 
ATOM   2417 O OD1 . ASN A 1 329 ? 41.812 11.280 -2.909  1.00 27.99 ? 329  ASN A OD1 1 
ATOM   2418 N ND2 . ASN A 1 329 ? 41.252 12.880 -4.378  1.00 27.32 ? 329  ASN A ND2 1 
ATOM   2419 N N   . ASP A 1 330 ? 42.699 8.110  -2.902  1.00 26.20 ? 330  ASP A N   1 
ATOM   2420 C CA  . ASP A 1 330 ? 42.267 7.281  -1.782  1.00 28.61 ? 330  ASP A CA  1 
ATOM   2421 C C   . ASP A 1 330 ? 41.295 7.963  -0.827  1.00 29.63 ? 330  ASP A C   1 
ATOM   2422 O O   . ASP A 1 330 ? 40.776 7.325  0.088   1.00 30.04 ? 330  ASP A O   1 
ATOM   2423 C CB  . ASP A 1 330 ? 43.473 6.765  -0.994  1.00 28.75 ? 330  ASP A CB  1 
ATOM   2424 C CG  . ASP A 1 330 ? 44.249 5.703  -1.747  1.00 30.17 ? 330  ASP A CG  1 
ATOM   2425 O OD1 . ASP A 1 330 ? 43.688 5.105  -2.690  1.00 31.79 ? 330  ASP A OD1 1 
ATOM   2426 O OD2 . ASP A 1 330 ? 45.416 5.455  -1.387  1.00 31.17 ? 330  ASP A OD2 1 
ATOM   2427 N N   . LEU A 1 331 ? 41.060 9.257  -1.019  1.00 30.58 ? 331  LEU A N   1 
ATOM   2428 C CA  . LEU A 1 331 ? 40.115 9.974  -0.170  1.00 30.24 ? 331  LEU A CA  1 
ATOM   2429 C C   . LEU A 1 331 ? 38.727 9.776  -0.772  1.00 31.29 ? 331  LEU A C   1 
ATOM   2430 O O   . LEU A 1 331 ? 37.713 9.853  -0.077  1.00 31.33 ? 331  LEU A O   1 
ATOM   2431 C CB  . LEU A 1 331 ? 40.449 11.468 -0.122  1.00 32.14 ? 331  LEU A CB  1 
ATOM   2432 C CG  . LEU A 1 331 ? 41.706 11.911 0.630   1.00 32.09 ? 331  LEU A CG  1 
ATOM   2433 C CD1 . LEU A 1 331 ? 41.881 13.420 0.485   1.00 34.38 ? 331  LEU A CD1 1 
ATOM   2434 C CD2 . LEU A 1 331 ? 41.593 11.526 2.103   1.00 33.11 ? 331  LEU A CD2 1 
ATOM   2435 N N   . LEU A 1 332 ? 38.697 9.498  -2.073  1.00 29.09 ? 332  LEU A N   1 
ATOM   2436 C CA  . LEU A 1 332 ? 37.445 9.294  -2.787  1.00 27.91 ? 332  LEU A CA  1 
ATOM   2437 C C   . LEU A 1 332 ? 37.016 7.837  -2.874  1.00 26.44 ? 332  LEU A C   1 
ATOM   2438 O O   . LEU A 1 332 ? 35.833 7.531  -2.730  1.00 26.17 ? 332  LEU A O   1 
ATOM   2439 C CB  . LEU A 1 332 ? 37.545 9.859  -4.208  1.00 27.96 ? 332  LEU A CB  1 
ATOM   2440 C CG  . LEU A 1 332 ? 37.711 11.366 -4.406  1.00 28.26 ? 332  LEU A CG  1 
ATOM   2441 C CD1 . LEU A 1 332 ? 37.852 11.657 -5.900  1.00 27.72 ? 332  LEU A CD1 1 
ATOM   2442 C CD2 . LEU A 1 332 ? 36.509 12.109 -3.829  1.00 28.33 ? 332  LEU A CD2 1 
ATOM   2443 N N   . ASN A 1 333 ? 37.968 6.938  -3.121  1.00 25.78 ? 333  ASN A N   1 
ATOM   2444 C CA  . ASN A 1 333 ? 37.639 5.522  -3.247  1.00 26.06 ? 333  ASN A CA  1 
ATOM   2445 C C   . ASN A 1 333 ? 37.441 4.811  -1.911  1.00 24.96 ? 333  ASN A C   1 
ATOM   2446 O O   . ASN A 1 333 ? 37.096 3.632  -1.880  1.00 24.79 ? 333  ASN A O   1 
ATOM   2447 C CB  . ASN A 1 333 ? 38.693 4.781  -4.091  1.00 26.10 ? 333  ASN A CB  1 
ATOM   2448 C CG  . ASN A 1 333 ? 40.106 4.968  -3.574  1.00 26.14 ? 333  ASN A CG  1 
ATOM   2449 O OD1 . ASN A 1 333 ? 40.360 4.881  -2.372  1.00 25.49 ? 333  ASN A OD1 1 
ATOM   2450 N ND2 . ASN A 1 333 ? 41.037 5.212  -4.486  1.00 22.57 ? 333  ASN A ND2 1 
ATOM   2451 N N   . GLY A 1 334 ? 37.660 5.533  -0.817  1.00 25.84 ? 334  GLY A N   1 
ATOM   2452 C CA  . GLY A 1 334 ? 37.460 4.963  0.504   1.00 26.52 ? 334  GLY A CA  1 
ATOM   2453 C C   . GLY A 1 334 ? 38.623 4.225  1.140   1.00 27.30 ? 334  GLY A C   1 
ATOM   2454 O O   . GLY A 1 334 ? 38.534 3.815  2.301   1.00 26.06 ? 334  GLY A O   1 
ATOM   2455 N N   . ARG A 1 335 ? 39.714 4.051  0.402   1.00 26.93 ? 335  ARG A N   1 
ATOM   2456 C CA  . ARG A 1 335 ? 40.871 3.343  0.942   1.00 27.17 ? 335  ARG A CA  1 
ATOM   2457 C C   . ARG A 1 335 ? 41.452 3.988  2.195   1.00 24.58 ? 335  ARG A C   1 
ATOM   2458 O O   . ARG A 1 335 ? 41.838 3.293  3.131   1.00 23.83 ? 335  ARG A O   1 
ATOM   2459 C CB  . ARG A 1 335 ? 41.956 3.217  -0.128  1.00 29.72 ? 335  ARG A CB  1 
ATOM   2460 C CG  . ARG A 1 335 ? 41.525 2.331  -1.282  1.00 36.83 ? 335  ARG A CG  1 
ATOM   2461 C CD  . ARG A 1 335 ? 42.640 2.090  -2.282  1.00 39.74 ? 335  ARG A CD  1 
ATOM   2462 N NE  . ARG A 1 335 ? 42.165 1.264  -3.387  1.00 44.64 ? 335  ARG A NE  1 
ATOM   2463 C CZ  . ARG A 1 335 ? 42.945 0.761  -4.336  1.00 47.07 ? 335  ARG A CZ  1 
ATOM   2464 N NH1 . ARG A 1 335 ? 44.251 0.999  -4.319  1.00 46.94 ? 335  ARG A NH1 1 
ATOM   2465 N NH2 . ARG A 1 335 ? 42.416 0.015  -5.301  1.00 47.50 ? 335  ARG A NH2 1 
ATOM   2466 N N   . ASP A 1 336 ? 41.512 5.313  2.218   1.00 24.72 ? 336  ASP A N   1 
ATOM   2467 C CA  . ASP A 1 336 ? 42.057 6.011  3.374   1.00 23.60 ? 336  ASP A CA  1 
ATOM   2468 C C   . ASP A 1 336 ? 41.243 5.669  4.621   1.00 23.19 ? 336  ASP A C   1 
ATOM   2469 O O   . ASP A 1 336 ? 41.799 5.312  5.660   1.00 22.87 ? 336  ASP A O   1 
ATOM   2470 C CB  . ASP A 1 336 ? 42.043 7.516  3.135   1.00 28.86 ? 336  ASP A CB  1 
ATOM   2471 C CG  . ASP A 1 336 ? 42.853 8.273  4.165   1.00 33.40 ? 336  ASP A CG  1 
ATOM   2472 O OD1 . ASP A 1 336 ? 44.088 8.089  4.198   1.00 37.16 ? 336  ASP A OD1 1 
ATOM   2473 O OD2 . ASP A 1 336 ? 42.260 9.047  4.943   1.00 36.73 ? 336  ASP A OD2 1 
ATOM   2474 N N   . ILE A 1 337 ? 39.924 5.775  4.502   1.00 21.03 ? 337  ILE A N   1 
ATOM   2475 C CA  . ILE A 1 337 ? 39.007 5.468  5.597   1.00 21.06 ? 337  ILE A CA  1 
ATOM   2476 C C   . ILE A 1 337 ? 39.137 4.020  6.087   1.00 20.87 ? 337  ILE A C   1 
ATOM   2477 O O   . ILE A 1 337 ? 39.163 3.773  7.294   1.00 20.48 ? 337  ILE A O   1 
ATOM   2478 C CB  . ILE A 1 337 ? 37.543 5.738  5.166   1.00 19.99 ? 337  ILE A CB  1 
ATOM   2479 C CG1 . ILE A 1 337 ? 37.331 7.247  4.995   1.00 19.16 ? 337  ILE A CG1 1 
ATOM   2480 C CG2 . ILE A 1 337 ? 36.574 5.141  6.173   1.00 19.31 ? 337  ILE A CG2 1 
ATOM   2481 C CD1 . ILE A 1 337 ? 35.972 7.621  4.428   1.00 20.84 ? 337  ILE A CD1 1 
ATOM   2482 N N   . ASP A 1 338 ? 39.210 3.065  5.162   1.00 20.03 ? 338  ASP A N   1 
ATOM   2483 C CA  . ASP A 1 338 ? 39.345 1.662  5.554   1.00 22.10 ? 338  ASP A CA  1 
ATOM   2484 C C   . ASP A 1 338 ? 40.689 1.398  6.225   1.00 22.37 ? 338  ASP A C   1 
ATOM   2485 O O   . ASP A 1 338 ? 40.775 0.607  7.163   1.00 22.96 ? 338  ASP A O   1 
ATOM   2486 C CB  . ASP A 1 338 ? 39.197 0.727  4.344   1.00 24.90 ? 338  ASP A CB  1 
ATOM   2487 C CG  . ASP A 1 338 ? 37.771 0.665  3.819   1.00 28.30 ? 338  ASP A CG  1 
ATOM   2488 O OD1 . ASP A 1 338 ? 36.834 0.924  4.603   1.00 30.38 ? 338  ASP A OD1 1 
ATOM   2489 O OD2 . ASP A 1 338 ? 37.582 0.342  2.625   1.00 29.40 ? 338  ASP A OD2 1 
ATOM   2490 N N   . ASN A 1 339 ? 41.738 2.059  5.741   1.00 22.01 ? 339  ASN A N   1 
ATOM   2491 C CA  . ASN A 1 339 ? 43.071 1.884  6.303   1.00 24.46 ? 339  ASN A CA  1 
ATOM   2492 C C   . ASN A 1 339 ? 43.180 2.479  7.700   1.00 24.36 ? 339  ASN A C   1 
ATOM   2493 O O   . ASN A 1 339 ? 43.961 2.009  8.522   1.00 23.07 ? 339  ASN A O   1 
ATOM   2494 C CB  . ASN A 1 339 ? 44.138 2.534  5.409   1.00 25.94 ? 339  ASN A CB  1 
ATOM   2495 C CG  . ASN A 1 339 ? 44.270 1.855  4.055   1.00 27.49 ? 339  ASN A CG  1 
ATOM   2496 O OD1 . ASN A 1 339 ? 43.893 0.698  3.885   1.00 32.06 ? 339  ASN A OD1 1 
ATOM   2497 N ND2 . ASN A 1 339 ? 44.831 2.572  3.088   1.00 30.00 ? 339  ASN A ND2 1 
ATOM   2498 N N   . HIS A 1 340 ? 42.394 3.515  7.968   1.00 22.83 ? 340  HIS A N   1 
ATOM   2499 C CA  . HIS A 1 340 ? 42.439 4.173  9.270   1.00 21.16 ? 340  HIS A CA  1 
ATOM   2500 C C   . HIS A 1 340 ? 41.222 3.908  10.160  1.00 21.59 ? 340  HIS A C   1 
ATOM   2501 O O   . HIS A 1 340 ? 40.937 4.680  11.080  1.00 19.74 ? 340  HIS A O   1 
ATOM   2502 C CB  . HIS A 1 340 ? 42.619 5.674  9.068   1.00 20.59 ? 340  HIS A CB  1 
ATOM   2503 C CG  . HIS A 1 340 ? 43.987 6.059  8.600   1.00 21.32 ? 340  HIS A CG  1 
ATOM   2504 N ND1 . HIS A 1 340 ? 45.067 6.145  9.452   1.00 19.61 ? 340  HIS A ND1 1 
ATOM   2505 C CD2 . HIS A 1 340 ? 44.451 6.391  7.371   1.00 23.28 ? 340  HIS A CD2 1 
ATOM   2506 C CE1 . HIS A 1 340 ? 46.135 6.518  8.770   1.00 23.59 ? 340  HIS A CE1 1 
ATOM   2507 N NE2 . HIS A 1 340 ? 45.788 6.674  7.505   1.00 24.65 ? 340  HIS A NE2 1 
ATOM   2508 N N   . LEU A 1 341 ? 40.511 2.815  9.890   1.00 21.47 ? 341  LEU A N   1 
ATOM   2509 C CA  . LEU A 1 341 ? 39.338 2.463  10.681  1.00 23.62 ? 341  LEU A CA  1 
ATOM   2510 C C   . LEU A 1 341 ? 39.780 2.034  12.076  1.00 25.73 ? 341  LEU A C   1 
ATOM   2511 O O   . LEU A 1 341 ? 40.550 1.081  12.218  1.00 24.92 ? 341  LEU A O   1 
ATOM   2512 C CB  . LEU A 1 341 ? 38.572 1.321  10.011  1.00 23.21 ? 341  LEU A CB  1 
ATOM   2513 C CG  . LEU A 1 341 ? 37.135 1.115  10.492  1.00 24.76 ? 341  LEU A CG  1 
ATOM   2514 C CD1 . LEU A 1 341 ? 36.298 2.341  10.141  1.00 21.78 ? 341  LEU A CD1 1 
ATOM   2515 C CD2 . LEU A 1 341 ? 36.548 -0.131 9.837   1.00 25.16 ? 341  LEU A CD2 1 
ATOM   2516 N N   . ILE A 1 342 ? 39.300 2.731  13.105  1.00 25.80 ? 342  ILE A N   1 
ATOM   2517 C CA  . ILE A 1 342 ? 39.683 2.395  14.471  1.00 27.91 ? 342  ILE A CA  1 
ATOM   2518 C C   . ILE A 1 342 ? 39.401 0.928  14.768  1.00 29.92 ? 342  ILE A C   1 
ATOM   2519 O O   . ILE A 1 342 ? 38.402 0.374  14.311  1.00 27.10 ? 342  ILE A O   1 
ATOM   2520 C CB  . ILE A 1 342 ? 38.945 3.265  15.503  1.00 27.82 ? 342  ILE A CB  1 
ATOM   2521 C CG1 . ILE A 1 342 ? 37.438 3.073  15.369  1.00 27.28 ? 342  ILE A CG1 1 
ATOM   2522 C CG2 . ILE A 1 342 ? 39.321 4.719  15.311  1.00 26.43 ? 342  ILE A CG2 1 
ATOM   2523 C CD1 . ILE A 1 342 ? 36.652 3.777  16.442  1.00 28.91 ? 342  ILE A CD1 1 
ATOM   2524 N N   . LYS A 1 343 ? 40.288 0.310  15.541  1.00 33.49 ? 343  LYS A N   1 
ATOM   2525 C CA  . LYS A 1 343 ? 40.164 -1.103 15.879  1.00 37.14 ? 343  LYS A CA  1 
ATOM   2526 C C   . LYS A 1 343 ? 39.248 -1.365 17.065  1.00 37.99 ? 343  LYS A C   1 
ATOM   2527 O O   . LYS A 1 343 ? 39.707 -1.432 18.205  1.00 38.07 ? 343  LYS A O   1 
ATOM   2528 C CB  . LYS A 1 343 ? 41.543 -1.697 16.183  1.00 36.46 ? 343  LYS A CB  1 
ATOM   2529 C CG  . LYS A 1 343 ? 42.574 -1.540 15.077  1.00 40.51 ? 343  LYS A CG  1 
ATOM   2530 C CD  . LYS A 1 343 ? 42.236 -2.369 13.853  1.00 43.46 ? 343  LYS A CD  1 
ATOM   2531 C CE  . LYS A 1 343 ? 43.339 -2.259 12.808  1.00 46.73 ? 343  LYS A CE  1 
ATOM   2532 N NZ  . LYS A 1 343 ? 43.040 -3.046 11.575  1.00 48.38 ? 343  LYS A NZ  1 
ATOM   2533 N N   . VAL A 1 344 ? 37.956 -1.511 16.790  1.00 38.85 ? 344  VAL A N   1 
ATOM   2534 C CA  . VAL A 1 344 ? 36.972 -1.802 17.825  1.00 40.77 ? 344  VAL A CA  1 
ATOM   2535 C C   . VAL A 1 344 ? 36.014 -2.840 17.251  1.00 43.06 ? 344  VAL A C   1 
ATOM   2536 O O   . VAL A 1 344 ? 35.652 -2.782 16.077  1.00 44.20 ? 344  VAL A O   1 
ATOM   2537 C CB  . VAL A 1 344 ? 36.190 -0.537 18.265  1.00 40.27 ? 344  VAL A CB  1 
ATOM   2538 C CG1 . VAL A 1 344 ? 37.154 0.497  18.828  1.00 37.86 ? 344  VAL A CG1 1 
ATOM   2539 C CG2 . VAL A 1 344 ? 35.406 0.034  17.100  1.00 39.00 ? 344  VAL A CG2 1 
ATOM   2540 N N   . ASP A 1 345 ? 35.608 -3.789 18.085  1.00 45.82 ? 345  ASP A N   1 
ATOM   2541 C CA  . ASP A 1 345 ? 34.733 -4.875 17.659  1.00 48.16 ? 345  ASP A CA  1 
ATOM   2542 C C   . ASP A 1 345 ? 33.243 -4.570 17.577  1.00 47.99 ? 345  ASP A C   1 
ATOM   2543 O O   . ASP A 1 345 ? 32.452 -5.460 17.264  1.00 49.24 ? 345  ASP A O   1 
ATOM   2544 C CB  . ASP A 1 345 ? 34.934 -6.075 18.582  1.00 52.16 ? 345  ASP A CB  1 
ATOM   2545 C CG  . ASP A 1 345 ? 34.786 -5.710 20.045  1.00 55.75 ? 345  ASP A CG  1 
ATOM   2546 O OD1 . ASP A 1 345 ? 35.651 -4.968 20.559  1.00 58.36 ? 345  ASP A OD1 1 
ATOM   2547 O OD2 . ASP A 1 345 ? 33.803 -6.155 20.677  1.00 57.37 ? 345  ASP A OD2 1 
ATOM   2548 N N   . ASN A 1 346 ? 32.852 -3.331 17.849  1.00 46.61 ? 346  ASN A N   1 
ATOM   2549 C CA  . ASN A 1 346 ? 31.436 -2.980 17.809  1.00 45.02 ? 346  ASN A CA  1 
ATOM   2550 C C   . ASN A 1 346 ? 30.980 -2.313 16.514  1.00 41.47 ? 346  ASN A C   1 
ATOM   2551 O O   . ASN A 1 346 ? 29.850 -1.837 16.427  1.00 41.00 ? 346  ASN A O   1 
ATOM   2552 C CB  . ASN A 1 346 ? 31.093 -2.085 19.003  1.00 47.98 ? 346  ASN A CB  1 
ATOM   2553 C CG  . ASN A 1 346 ? 31.125 -2.838 20.322  1.00 52.10 ? 346  ASN A CG  1 
ATOM   2554 O OD1 . ASN A 1 346 ? 31.057 -2.239 21.396  1.00 53.16 ? 346  ASN A OD1 1 
ATOM   2555 N ND2 . ASN A 1 346 ? 31.220 -4.163 20.244  1.00 51.99 ? 346  ASN A ND2 1 
ATOM   2556 N N   . ILE A 1 347 ? 31.848 -2.285 15.508  1.00 37.82 ? 347  ILE A N   1 
ATOM   2557 C CA  . ILE A 1 347 ? 31.496 -1.670 14.229  1.00 34.02 ? 347  ILE A CA  1 
ATOM   2558 C C   . ILE A 1 347 ? 30.726 -2.640 13.331  1.00 32.10 ? 347  ILE A C   1 
ATOM   2559 O O   . ILE A 1 347 ? 31.278 -3.629 12.852  1.00 31.63 ? 347  ILE A O   1 
ATOM   2560 C CB  . ILE A 1 347 ? 32.754 -1.186 13.474  1.00 32.11 ? 347  ILE A CB  1 
ATOM   2561 C CG1 . ILE A 1 347 ? 33.529 -0.192 14.344  1.00 32.70 ? 347  ILE A CG1 1 
ATOM   2562 C CG2 . ILE A 1 347 ? 32.347 -0.522 12.161  1.00 30.66 ? 347  ILE A CG2 1 
ATOM   2563 C CD1 . ILE A 1 347 ? 34.830 0.295  13.728  1.00 31.80 ? 347  ILE A CD1 1 
ATOM   2564 N N   . VAL A 1 348 ? 29.446 -2.349 13.112  1.00 30.65 ? 348  VAL A N   1 
ATOM   2565 C CA  . VAL A 1 348 ? 28.589 -3.181 12.273  1.00 29.14 ? 348  VAL A CA  1 
ATOM   2566 C C   . VAL A 1 348 ? 28.679 -2.753 10.807  1.00 29.71 ? 348  VAL A C   1 
ATOM   2567 O O   . VAL A 1 348 ? 28.201 -1.680 10.432  1.00 29.24 ? 348  VAL A O   1 
ATOM   2568 C CB  . VAL A 1 348 ? 27.104 -3.087 12.719  1.00 29.04 ? 348  VAL A CB  1 
ATOM   2569 C CG1 . VAL A 1 348 ? 26.224 -3.889 11.775  1.00 26.62 ? 348  VAL A CG1 1 
ATOM   2570 C CG2 . VAL A 1 348 ? 26.950 -3.595 14.151  1.00 29.89 ? 348  VAL A CG2 1 
ATOM   2571 N N   . HIS A 1 349 ? 29.293 -3.594 9.979   1.00 29.41 ? 349  HIS A N   1 
ATOM   2572 C CA  . HIS A 1 349 ? 29.430 -3.290 8.558   1.00 28.61 ? 349  HIS A CA  1 
ATOM   2573 C C   . HIS A 1 349 ? 28.139 -3.574 7.813   1.00 28.38 ? 349  HIS A C   1 
ATOM   2574 O O   . HIS A 1 349 ? 27.577 -4.660 7.921   1.00 30.37 ? 349  HIS A O   1 
ATOM   2575 C CB  . HIS A 1 349 ? 30.565 -4.107 7.935   1.00 26.27 ? 349  HIS A CB  1 
ATOM   2576 C CG  . HIS A 1 349 ? 31.929 -3.654 8.348   1.00 27.90 ? 349  HIS A CG  1 
ATOM   2577 N ND1 . HIS A 1 349 ? 32.392 -3.767 9.640   1.00 27.93 ? 349  HIS A ND1 1 
ATOM   2578 C CD2 . HIS A 1 349 ? 32.921 -3.059 7.643   1.00 26.16 ? 349  HIS A CD2 1 
ATOM   2579 C CE1 . HIS A 1 349 ? 33.609 -3.259 9.715   1.00 28.29 ? 349  HIS A CE1 1 
ATOM   2580 N NE2 . HIS A 1 349 ? 33.953 -2.822 8.517   1.00 29.89 ? 349  HIS A NE2 1 
ATOM   2581 N N   . ILE A 1 350 ? 27.667 -2.587 7.059   1.00 27.77 ? 350  ILE A N   1 
ATOM   2582 C CA  . ILE A 1 350 ? 26.443 -2.747 6.289   1.00 27.15 ? 350  ILE A CA  1 
ATOM   2583 C C   . ILE A 1 350 ? 26.693 -2.444 4.818   1.00 28.35 ? 350  ILE A C   1 
ATOM   2584 O O   . ILE A 1 350 ? 27.656 -1.762 4.465   1.00 26.76 ? 350  ILE A O   1 
ATOM   2585 C CB  . ILE A 1 350 ? 25.317 -1.827 6.807   1.00 26.39 ? 350  ILE A CB  1 
ATOM   2586 C CG1 . ILE A 1 350 ? 25.794 -0.372 6.835   1.00 25.32 ? 350  ILE A CG1 1 
ATOM   2587 C CG2 . ILE A 1 350 ? 24.878 -2.275 8.199   1.00 27.46 ? 350  ILE A CG2 1 
ATOM   2588 C CD1 . ILE A 1 350 ? 24.714 0.613  7.235   1.00 22.97 ? 350  ILE A CD1 1 
ATOM   2589 N N   . ARG A 1 351 ? 25.825 -2.972 3.964   1.00 30.59 ? 351  ARG A N   1 
ATOM   2590 C CA  . ARG A 1 351 ? 25.946 -2.763 2.528   1.00 33.67 ? 351  ARG A CA  1 
ATOM   2591 C C   . ARG A 1 351 ? 24.846 -1.827 2.060   1.00 34.77 ? 351  ARG A C   1 
ATOM   2592 O O   . ARG A 1 351 ? 23.781 -1.747 2.670   1.00 35.78 ? 351  ARG A O   1 
ATOM   2593 C CB  . ARG A 1 351 ? 25.817 -4.095 1.778   1.00 33.39 ? 351  ARG A CB  1 
ATOM   2594 C CG  . ARG A 1 351 ? 26.821 -5.172 2.177   1.00 34.24 ? 351  ARG A CG  1 
ATOM   2595 C CD  . ARG A 1 351 ? 28.231 -4.878 1.665   1.00 32.01 ? 351  ARG A CD  1 
ATOM   2596 N NE  . ARG A 1 351 ? 28.253 -4.684 0.217   1.00 31.30 ? 351  ARG A NE  1 
ATOM   2597 C CZ  . ARG A 1 351 ? 29.360 -4.568 -0.512  1.00 29.34 ? 351  ARG A CZ  1 
ATOM   2598 N NH1 . ARG A 1 351 ? 30.557 -4.631 0.060   1.00 27.59 ? 351  ARG A NH1 1 
ATOM   2599 N NH2 . ARG A 1 351 ? 29.267 -4.376 -1.819  1.00 29.92 ? 351  ARG A NH2 1 
ATOM   2600 N N   . ASN A 1 352 ? 25.113 -1.110 0.979   1.00 36.78 ? 352  ASN A N   1 
ATOM   2601 C CA  . ASN A 1 352 ? 24.133 -0.202 0.407   1.00 41.35 ? 352  ASN A CA  1 
ATOM   2602 C C   . ASN A 1 352 ? 24.210 -0.355 -1.102  1.00 44.30 ? 352  ASN A C   1 
ATOM   2603 O O   . ASN A 1 352 ? 24.375 0.619  -1.832  1.00 44.18 ? 352  ASN A O   1 
ATOM   2604 C CB  . ASN A 1 352 ? 24.434 1.240  0.805   1.00 41.62 ? 352  ASN A CB  1 
ATOM   2605 C CG  . ASN A 1 352 ? 23.365 2.199  0.340   1.00 42.65 ? 352  ASN A CG  1 
ATOM   2606 O OD1 . ASN A 1 352 ? 22.172 1.954  0.531   1.00 43.17 ? 352  ASN A OD1 1 
ATOM   2607 N ND2 . ASN A 1 352 ? 23.782 3.301  -0.271  1.00 42.89 ? 352  ASN A ND2 1 
ATOM   2608 N N   . ASP A 1 353 ? 24.099 -1.598 -1.557  1.00 48.36 ? 353  ASP A N   1 
ATOM   2609 C CA  . ASP A 1 353 ? 24.168 -1.906 -2.978  1.00 52.91 ? 353  ASP A CA  1 
ATOM   2610 C C   . ASP A 1 353 ? 22.852 -1.601 -3.680  1.00 55.37 ? 353  ASP A C   1 
ATOM   2611 O O   . ASP A 1 353 ? 21.774 -1.872 -3.150  1.00 55.85 ? 353  ASP A O   1 
ATOM   2612 C CB  . ASP A 1 353 ? 24.533 -3.378 -3.176  1.00 52.97 ? 353  ASP A CB  1 
ATOM   2613 C CG  . ASP A 1 353 ? 25.808 -3.765 -2.447  1.00 53.86 ? 353  ASP A CG  1 
ATOM   2614 O OD1 . ASP A 1 353 ? 26.849 -3.106 -2.670  1.00 53.28 ? 353  ASP A OD1 1 
ATOM   2615 O OD2 . ASP A 1 353 ? 25.769 -4.729 -1.652  1.00 54.20 ? 353  ASP A OD2 1 
ATOM   2616 N N   . HIS A 1 354 ? 22.953 -1.031 -4.876  1.00 58.24 ? 354  HIS A N   1 
ATOM   2617 C CA  . HIS A 1 354 ? 21.782 -0.684 -5.671  1.00 60.49 ? 354  HIS A CA  1 
ATOM   2618 C C   . HIS A 1 354 ? 21.743 -1.500 -6.958  1.00 60.86 ? 354  HIS A C   1 
ATOM   2619 O O   . HIS A 1 354 ? 22.583 -2.415 -7.100  1.00 61.34 ? 354  HIS A O   1 
ATOM   2620 C CB  . HIS A 1 354 ? 21.795 0.809  -6.011  1.00 62.53 ? 354  HIS A CB  1 
ATOM   2621 C CG  . HIS A 1 354 ? 21.530 1.701  -4.838  1.00 64.41 ? 354  HIS A CG  1 
ATOM   2622 N ND1 . HIS A 1 354 ? 20.393 1.596  -4.065  1.00 65.20 ? 354  HIS A ND1 1 
ATOM   2623 C CD2 . HIS A 1 354 ? 22.245 2.727  -4.318  1.00 65.58 ? 354  HIS A CD2 1 
ATOM   2624 C CE1 . HIS A 1 354 ? 20.418 2.520  -3.121  1.00 65.92 ? 354  HIS A CE1 1 
ATOM   2625 N NE2 . HIS A 1 354 ? 21.531 3.220  -3.253  1.00 65.77 ? 354  HIS A NE2 1 
HETATM 2626 S S   . SO4 B 2 .   ? 27.463 10.102 0.324   1.00 36.92 ? 2847 SO4 A S   1 
HETATM 2627 O O1  . SO4 B 2 .   ? 28.565 10.772 -0.399  1.00 37.91 ? 2847 SO4 A O1  1 
HETATM 2628 O O2  . SO4 B 2 .   ? 28.024 9.083  1.231   1.00 32.91 ? 2847 SO4 A O2  1 
HETATM 2629 O O3  . SO4 B 2 .   ? 26.690 11.091 1.100   1.00 36.26 ? 2847 SO4 A O3  1 
HETATM 2630 O O4  . SO4 B 2 .   ? 26.585 9.455  -0.671  1.00 38.84 ? 2847 SO4 A O4  1 
HETATM 2631 O O   . HOH C 3 .   ? 22.674 9.149  33.077  1.00 38.66 ? 2848 HOH A O   1 
HETATM 2632 O O   . HOH C 3 .   ? 24.630 5.746  32.248  1.00 31.51 ? 2849 HOH A O   1 
HETATM 2633 O O   . HOH C 3 .   ? 29.323 2.241  29.816  1.00 50.43 ? 2850 HOH A O   1 
HETATM 2634 O O   . HOH C 3 .   ? 22.397 6.017  35.995  1.00 47.81 ? 2851 HOH A O   1 
HETATM 2635 O O   . HOH C 3 .   ? 16.189 8.308  28.623  1.00 20.03 ? 2852 HOH A O   1 
HETATM 2636 O O   . HOH C 3 .   ? 35.559 2.976  3.103   1.00 34.19 ? 2853 HOH A O   1 
HETATM 2637 O O   . HOH C 3 .   ? 32.482 3.227  2.980   1.00 29.98 ? 2854 HOH A O   1 
HETATM 2638 O O   . HOH C 3 .   ? 31.391 13.616 5.972   1.00 16.30 ? 2855 HOH A O   1 
HETATM 2639 O O   . HOH C 3 .   ? 31.893 15.155 3.533   1.00 36.16 ? 2856 HOH A O   1 
HETATM 2640 O O   . HOH C 3 .   ? 23.933 9.892  -0.068  1.00 34.93 ? 2857 HOH A O   1 
HETATM 2641 O O   . HOH C 3 .   ? 35.881 7.080  9.649   1.00 13.54 ? 2858 HOH A O   1 
HETATM 2642 O O   . HOH C 3 .   ? 12.446 8.805  -0.022  1.00 52.31 ? 2859 HOH A O   1 
HETATM 2643 O O   . HOH C 3 .   ? 11.248 13.612 10.374  1.00 32.77 ? 2860 HOH A O   1 
HETATM 2644 O O   . HOH C 3 .   ? 5.057  4.454  11.321  1.00 37.23 ? 2861 HOH A O   1 
HETATM 2645 O O   . HOH C 3 .   ? 4.319  3.655  15.694  1.00 29.00 ? 2862 HOH A O   1 
HETATM 2646 O O   . HOH C 3 .   ? 2.075  2.879  17.766  1.00 40.80 ? 2863 HOH A O   1 
HETATM 2647 O O   . HOH C 3 .   ? 21.118 37.550 20.819  1.00 50.94 ? 2864 HOH A O   1 
HETATM 2648 O O   . HOH C 3 .   ? 18.486 39.496 19.502  1.00 59.29 ? 2865 HOH A O   1 
HETATM 2649 O O   . HOH C 3 .   ? 26.038 15.074 32.557  1.00 23.39 ? 2866 HOH A O   1 
HETATM 2650 O O   . HOH C 3 .   ? 9.424  10.737 35.192  1.00 45.00 ? 2867 HOH A O   1 
HETATM 2651 O O   . HOH C 3 .   ? 7.481  10.053 41.603  1.00 59.06 ? 2868 HOH A O   1 
HETATM 2652 O O   . HOH C 3 .   ? 12.255 6.241  36.251  1.00 51.84 ? 2869 HOH A O   1 
HETATM 2653 O O   . HOH C 3 .   ? 11.085 10.279 38.695  1.00 56.16 ? 2870 HOH A O   1 
HETATM 2654 O O   . HOH C 3 .   ? 24.910 14.216 -1.624  1.00 57.73 ? 2871 HOH A O   1 
HETATM 2655 O O   . HOH C 3 .   ? 27.186 16.710 -3.147  1.00 43.32 ? 2872 HOH A O   1 
HETATM 2656 O O   . HOH C 3 .   ? 31.390 12.464 1.677   1.00 34.73 ? 2873 HOH A O   1 
HETATM 2657 O O   . HOH C 3 .   ? 26.091 14.427 4.584   1.00 35.79 ? 2874 HOH A O   1 
HETATM 2658 O O   . HOH C 3 .   ? 9.341  -1.790 10.713  1.00 44.15 ? 2875 HOH A O   1 
HETATM 2659 O O   . HOH C 3 .   ? 12.881 -2.538 18.514  1.00 25.11 ? 2876 HOH A O   1 
HETATM 2660 O O   . HOH C 3 .   ? 20.191 -2.587 19.505  1.00 21.79 ? 2877 HOH A O   1 
HETATM 2661 O O   . HOH C 3 .   ? 13.304 -2.392 29.645  1.00 38.62 ? 2878 HOH A O   1 
HETATM 2662 O O   . HOH C 3 .   ? 10.275 5.334  32.425  1.00 45.47 ? 2879 HOH A O   1 
HETATM 2663 O O   . HOH C 3 .   ? 19.807 19.356 23.031  1.00 17.61 ? 2880 HOH A O   1 
HETATM 2664 O O   . HOH C 3 .   ? 14.584 15.890 17.383  1.00 24.50 ? 2881 HOH A O   1 
HETATM 2665 O O   . HOH C 3 .   ? 32.344 10.506 26.928  1.00 25.30 ? 2882 HOH A O   1 
HETATM 2666 O O   . HOH C 3 .   ? 34.839 9.563  27.593  1.00 20.53 ? 2883 HOH A O   1 
HETATM 2667 O O   . HOH C 3 .   ? 36.419 7.497  16.513  1.00 22.59 ? 2884 HOH A O   1 
HETATM 2668 O O   . HOH C 3 .   ? 36.860 10.554 26.135  1.00 40.97 ? 2885 HOH A O   1 
HETATM 2669 O O   . HOH C 3 .   ? 38.764 7.182  1.949   1.00 21.88 ? 2886 HOH A O   1 
HETATM 2670 O O   . HOH C 3 .   ? 33.773 5.920  -2.107  1.00 29.05 ? 2887 HOH A O   1 
HETATM 2671 O O   . HOH C 3 .   ? 12.211 -4.749 11.275  1.00 41.94 ? 2888 HOH A O   1 
HETATM 2672 O O   . HOH C 3 .   ? -0.866 2.000  15.920  1.00 47.73 ? 2889 HOH A O   1 
HETATM 2673 O O   . HOH C 3 .   ? -2.693 10.771 26.222  1.00 21.62 ? 2890 HOH A O   1 
HETATM 2674 O O   . HOH C 3 .   ? 1.418  14.767 23.990  1.00 34.54 ? 2891 HOH A O   1 
HETATM 2675 O O   . HOH C 3 .   ? 12.368 19.322 38.951  1.00 28.64 ? 2892 HOH A O   1 
HETATM 2676 O O   . HOH C 3 .   ? 6.611  13.097 33.517  1.00 40.61 ? 2893 HOH A O   1 
HETATM 2677 O O   . HOH C 3 .   ? 20.137 19.917 36.201  1.00 33.90 ? 2894 HOH A O   1 
HETATM 2678 O O   . HOH C 3 .   ? 20.051 27.214 35.090  1.00 42.25 ? 2895 HOH A O   1 
HETATM 2679 O O   . HOH C 3 .   ? 36.166 20.181 26.403  1.00 24.51 ? 2896 HOH A O   1 
HETATM 2680 O O   . HOH C 3 .   ? 38.776 26.297 26.452  1.00 26.75 ? 2897 HOH A O   1 
HETATM 2681 O O   . HOH C 3 .   ? 41.191 27.495 25.709  1.00 34.24 ? 2898 HOH A O   1 
HETATM 2682 O O   . HOH C 3 .   ? 44.250 25.805 23.086  1.00 24.36 ? 2899 HOH A O   1 
HETATM 2683 O O   . HOH C 3 .   ? 41.771 27.676 23.108  1.00 18.91 ? 2900 HOH A O   1 
HETATM 2684 O O   . HOH C 3 .   ? 33.320 37.293 25.894  1.00 25.18 ? 2901 HOH A O   1 
HETATM 2685 O O   . HOH C 3 .   ? 30.339 43.487 13.554  1.00 52.61 ? 2902 HOH A O   1 
HETATM 2686 O O   . HOH C 3 .   ? 35.007 42.977 15.869  1.00 38.67 ? 2903 HOH A O   1 
HETATM 2687 O O   . HOH C 3 .   ? 35.286 31.399 7.807   1.00 23.49 ? 2904 HOH A O   1 
HETATM 2688 O O   . HOH C 3 .   ? 34.978 30.974 3.011   1.00 27.00 ? 2905 HOH A O   1 
HETATM 2689 O O   . HOH C 3 .   ? 48.587 28.042 9.044   1.00 41.13 ? 2906 HOH A O   1 
HETATM 2690 O O   . HOH C 3 .   ? 47.623 26.621 12.515  1.00 26.90 ? 2907 HOH A O   1 
HETATM 2691 O O   . HOH C 3 .   ? 44.737 33.529 16.264  1.00 42.77 ? 2908 HOH A O   1 
HETATM 2692 O O   . HOH C 3 .   ? 49.387 23.591 5.019   1.00 29.71 ? 2909 HOH A O   1 
HETATM 2693 O O   . HOH C 3 .   ? 47.151 20.864 7.504   1.00 31.60 ? 2910 HOH A O   1 
HETATM 2694 O O   . HOH C 3 .   ? 41.177 17.890 11.240  1.00 13.42 ? 2911 HOH A O   1 
HETATM 2695 O O   . HOH C 3 .   ? 41.888 17.892 21.222  1.00 41.81 ? 2912 HOH A O   1 
HETATM 2696 O O   . HOH C 3 .   ? 40.928 20.155 20.295  1.00 27.72 ? 2913 HOH A O   1 
HETATM 2697 O O   . HOH C 3 .   ? 23.595 -5.300 4.800   1.00 43.63 ? 2914 HOH A O   1 
HETATM 2698 O O   . HOH C 3 .   ? 29.374 37.937 18.284  1.00 49.74 ? 2915 HOH A O   1 
HETATM 2699 O O   . HOH C 3 .   ? 34.656 26.459 15.123  1.00 15.02 ? 2916 HOH A O   1 
HETATM 2700 O O   . HOH C 3 .   ? 35.967 27.249 8.998   1.00 19.55 ? 2917 HOH A O   1 
HETATM 2701 O O   . HOH C 3 .   ? 35.070 31.016 10.466  1.00 21.08 ? 2918 HOH A O   1 
HETATM 2702 O O   . HOH C 3 .   ? 27.647 28.266 12.565  1.00 34.01 ? 2919 HOH A O   1 
HETATM 2703 O O   . HOH C 3 .   ? 25.578 26.305 14.261  1.00 23.29 ? 2920 HOH A O   1 
HETATM 2704 O O   . HOH C 3 .   ? 13.016 31.812 27.553  1.00 40.08 ? 2921 HOH A O   1 
HETATM 2705 O O   . HOH C 3 .   ? 10.995 18.287 17.579  1.00 29.67 ? 2922 HOH A O   1 
HETATM 2706 O O   . HOH C 3 .   ? 34.597 23.404 -2.522  1.00 44.84 ? 2923 HOH A O   1 
HETATM 2707 O O   . HOH C 3 .   ? 47.915 22.229 2.869   1.00 36.72 ? 2924 HOH A O   1 
HETATM 2708 O O   . HOH C 3 .   ? 39.716 14.961 -2.337  1.00 49.77 ? 2925 HOH A O   1 
HETATM 2709 O O   . HOH C 3 .   ? 44.645 12.972 4.190   1.00 38.99 ? 2926 HOH A O   1 
HETATM 2710 O O   . HOH C 3 .   ? 42.003 13.792 -7.309  1.00 36.78 ? 2927 HOH A O   1 
HETATM 2711 O O   . HOH C 3 .   ? 31.528 14.832 27.704  1.00 20.37 ? 2928 HOH A O   1 
HETATM 2712 O O   . HOH C 3 .   ? 32.387 18.761 28.663  1.00 34.27 ? 2929 HOH A O   1 
HETATM 2713 O O   . HOH C 3 .   ? 6.059  2.606  37.703  1.00 57.04 ? 2930 HOH A O   1 
HETATM 2714 O O   . HOH C 3 .   ? 8.302  -4.290 30.357  1.00 32.98 ? 2931 HOH A O   1 
HETATM 2715 O O   . HOH C 3 .   ? 10.364 -3.077 29.097  1.00 43.96 ? 2932 HOH A O   1 
HETATM 2716 O O   . HOH C 3 .   ? 7.280  24.319 28.406  1.00 38.15 ? 2933 HOH A O   1 
HETATM 2717 O O   . HOH C 3 .   ? 15.645 22.042 24.435  1.00 21.02 ? 2934 HOH A O   1 
HETATM 2718 O O   . HOH C 3 .   ? 13.161 23.087 22.617  1.00 38.14 ? 2935 HOH A O   1 
HETATM 2719 O O   . HOH C 3 .   ? 19.490 28.109 5.739   1.00 44.01 ? 2936 HOH A O   1 
HETATM 2720 O O   . HOH C 3 .   ? 14.767 24.654 17.357  1.00 39.18 ? 2937 HOH A O   1 
HETATM 2721 O O   . HOH C 3 .   ? 38.185 5.740  9.243   1.00 19.50 ? 2938 HOH A O   1 
HETATM 2722 O O   . HOH C 3 .   ? 44.132 10.939 19.073  1.00 36.99 ? 2939 HOH A O   1 
HETATM 2723 O O   . HOH C 3 .   ? 45.996 2.679  18.034  1.00 50.06 ? 2940 HOH A O   1 
HETATM 2724 O O   . HOH C 3 .   ? 44.334 16.264 19.285  1.00 29.85 ? 2941 HOH A O   1 
HETATM 2725 O O   . HOH C 3 .   ? 46.994 15.513 11.975  1.00 39.69 ? 2942 HOH A O   1 
HETATM 2726 O O   . HOH C 3 .   ? 47.552 12.241 11.864  1.00 32.17 ? 2943 HOH A O   1 
HETATM 2727 O O   . HOH C 3 .   ? 47.143 11.802 15.329  1.00 39.38 ? 2944 HOH A O   1 
HETATM 2728 O O   . HOH C 3 .   ? 26.699 1.369  23.603  1.00 30.36 ? 2945 HOH A O   1 
HETATM 2729 O O   . HOH C 3 .   ? 29.116 1.900  24.094  1.00 28.78 ? 2946 HOH A O   1 
HETATM 2730 O O   . HOH C 3 .   ? 27.341 -0.880 17.301  1.00 21.84 ? 2947 HOH A O   1 
HETATM 2731 O O   . HOH C 3 .   ? 35.530 -2.107 21.574  1.00 51.75 ? 2948 HOH A O   1 
HETATM 2732 O O   . HOH C 3 .   ? 37.505 -1.533 -10.821 1.00 37.24 ? 2949 HOH A O   1 
HETATM 2733 O O   . HOH C 3 .   ? 39.455 -2.151 -12.344 1.00 37.45 ? 2950 HOH A O   1 
HETATM 2734 O O   . HOH C 3 .   ? 30.908 1.074  -13.148 1.00 55.27 ? 2951 HOH A O   1 
HETATM 2735 O O   . HOH C 3 .   ? 26.220 3.976  -9.621  1.00 32.16 ? 2952 HOH A O   1 
HETATM 2736 O O   . HOH C 3 .   ? 25.737 1.507  -11.133 1.00 52.40 ? 2953 HOH A O   1 
HETATM 2737 O O   . HOH C 3 .   ? 31.241 12.200 -19.903 1.00 15.94 ? 2954 HOH A O   1 
HETATM 2738 O O   . HOH C 3 .   ? 45.462 8.842  -3.081  1.00 30.28 ? 2955 HOH A O   1 
HETATM 2739 O O   . HOH C 3 .   ? 35.612 -3.079 11.738  1.00 32.20 ? 2956 HOH A O   1 
HETATM 2740 O O   . HOH C 3 .   ? 38.523 -4.036 14.512  1.00 39.80 ? 2957 HOH A O   1 
HETATM 2741 O O   . HOH C 3 .   ? 29.695 -6.476 10.884  1.00 29.98 ? 2958 HOH A O   1 
HETATM 2742 O O   . HOH C 3 .   ? 21.076 2.570  -8.213  1.00 49.93 ? 2959 HOH A O   1 
HETATM 2743 O O   . HOH C 3 .   ? 20.138 8.481  34.529  1.00 36.77 ? 2960 HOH A O   1 
HETATM 2744 O O   . HOH C 3 .   ? 28.678 14.371 6.582   1.00 21.82 ? 2961 HOH A O   1 
HETATM 2745 O O   . HOH C 3 .   ? 13.984 14.459 41.206  1.00 51.21 ? 2962 HOH A O   1 
HETATM 2746 O O   . HOH C 3 .   ? 23.680 16.086 3.646   1.00 40.29 ? 2963 HOH A O   1 
HETATM 2747 O O   . HOH C 3 .   ? 32.027 13.803 -3.846  1.00 48.35 ? 2964 HOH A O   1 
HETATM 2748 O O   . HOH C 3 .   ? 1.258  16.559 26.343  1.00 33.33 ? 2965 HOH A O   1 
HETATM 2749 O O   . HOH C 3 .   ? 20.307 17.817 35.040  1.00 41.98 ? 2966 HOH A O   1 
HETATM 2750 O O   . HOH C 3 .   ? 39.147 23.487 27.612  1.00 40.08 ? 2967 HOH A O   1 
HETATM 2751 O O   . HOH C 3 .   ? 42.982 26.005 27.020  1.00 42.85 ? 2968 HOH A O   1 
HETATM 2752 O O   . HOH C 3 .   ? 19.118 35.069 19.825  1.00 56.05 ? 2969 HOH A O   1 
HETATM 2753 O O   . HOH C 3 .   ? 37.147 13.600 0.189   1.00 45.28 ? 2970 HOH A O   1 
HETATM 2754 O O   . HOH C 3 .   ? 44.277 15.132 5.954   1.00 38.15 ? 2971 HOH A O   1 
HETATM 2755 O O   . HOH C 3 .   ? 16.693 29.824 16.937  1.00 42.04 ? 2972 HOH A O   1 
HETATM 2756 O O   . HOH C 3 .   ? 35.787 -1.475 5.962   1.00 42.72 ? 2973 HOH A O   1 
HETATM 2757 O O   . HOH C 3 .   ? 37.806 -1.882 12.656  1.00 35.22 ? 2974 HOH A O   1 
HETATM 2758 O O   . HOH C 3 .   ? 26.151 10.601 -9.069  1.00 30.31 ? 2975 HOH A O   1 
HETATM 2759 O O   . HOH C 3 .   ? 38.155 6.365  20.635  1.00 30.87 ? 2976 HOH A O   1 
HETATM 2760 O O   . HOH C 3 .   ? 41.264 5.637  23.400  1.00 49.68 ? 2977 HOH A O   1 
HETATM 2761 O O   . HOH C 3 .   ? 44.669 3.070  20.698  1.00 34.42 ? 2978 HOH A O   1 
HETATM 2762 O O   . HOH C 3 .   ? 24.586 8.606  24.181  1.00 28.76 ? 2979 HOH A O   1 
HETATM 2763 O O   . HOH C 3 .   ? 31.895 35.827 11.904  1.00 36.51 ? 2980 HOH A O   1 
HETATM 2764 O O   . HOH C 3 .   ? 30.699 30.203 5.852   1.00 33.67 ? 2981 HOH A O   1 
HETATM 2765 O O   . HOH C 3 .   ? 33.412 38.213 10.823  1.00 48.14 ? 2982 HOH A O   1 
HETATM 2766 O O   . HOH C 3 .   ? -3.551 2.710  20.868  1.00 37.23 ? 2983 HOH A O   1 
HETATM 2767 O O   . HOH C 3 .   ? 35.350 43.244 8.687   1.00 39.98 ? 2984 HOH A O   1 
HETATM 2768 O O   . HOH C 3 .   ? 0.523  12.253 15.635  1.00 41.52 ? 2985 HOH A O   1 
HETATM 2769 O O   . HOH C 3 .   ? 12.991 -5.439 17.886  1.00 39.49 ? 2986 HOH A O   1 
HETATM 2770 O O   . HOH C 3 .   ? 22.511 24.739 29.143  1.00 45.96 ? 2987 HOH A O   1 
HETATM 2771 O O   . HOH C 3 .   ? 14.776 16.725 14.741  1.00 56.56 ? 2988 HOH A O   1 
HETATM 2772 O O   . HOH C 3 .   ? 48.837 6.234  14.150  1.00 40.45 ? 2989 HOH A O   1 
HETATM 2773 O O   . HOH C 3 .   ? 48.750 8.579  15.664  1.00 43.37 ? 2990 HOH A O   1 
HETATM 2774 O O   . HOH C 3 .   ? 33.912 16.215 1.960   1.00 45.56 ? 2991 HOH A O   1 
HETATM 2775 O O   . HOH C 3 .   ? 23.720 -3.699 16.170  1.00 39.96 ? 2992 HOH A O   1 
HETATM 2776 O O   . HOH C 3 .   ? 25.915 -3.178 17.334  1.00 36.89 ? 2993 HOH A O   1 
HETATM 2777 O O   . HOH C 3 .   ? 21.993 -3.020 14.481  1.00 40.00 ? 2994 HOH A O   1 
HETATM 2778 O O   . HOH C 3 .   ? 23.822 -5.934 13.937  1.00 46.26 ? 2995 HOH A O   1 
HETATM 2779 O O   . HOH C 3 .   ? 34.896 14.871 0.069   1.00 45.54 ? 2996 HOH A O   1 
HETATM 2780 O O   . HOH C 3 .   ? 45.307 17.536 3.474   1.00 47.24 ? 2997 HOH A O   1 
HETATM 2781 O O   . HOH C 3 .   ? 42.602 30.366 23.207  1.00 46.46 ? 2998 HOH A O   1 
HETATM 2782 O O   . HOH C 3 .   ? 45.910 24.162 25.243  1.00 40.01 ? 2999 HOH A O   1 
HETATM 2783 O O   . HOH C 3 .   ? 47.404 24.745 20.784  1.00 40.85 ? 3000 HOH A O   1 
HETATM 2784 O O   . HOH C 3 .   ? 52.647 22.898 25.276  1.00 47.94 ? 3001 HOH A O   1 
HETATM 2785 O O   . HOH C 3 .   ? 25.640 -7.146 12.390  1.00 49.59 ? 3002 HOH A O   1 
HETATM 2786 O O   . HOH C 3 .   ? 42.167 1.939  17.111  1.00 46.58 ? 3003 HOH A O   1 
HETATM 2787 O O   . HOH C 3 .   ? 46.521 14.488 18.379  1.00 36.39 ? 3004 HOH A O   1 
HETATM 2788 O O   . HOH C 3 .   ? 28.608 12.928 0.757   1.00 44.46 ? 3005 HOH A O   1 
HETATM 2789 O O   . HOH C 3 .   ? 25.831 14.121 0.811   1.00 51.60 ? 3006 HOH A O   1 
HETATM 2790 O O   . HOH C 3 .   ? 23.570 17.317 -1.842  1.00 58.14 ? 3007 HOH A O   1 
HETATM 2791 O O   . HOH C 3 .   ? 32.305 19.404 -0.933  1.00 48.77 ? 3008 HOH A O   1 
HETATM 2792 O O   . HOH C 3 .   ? 17.667 2.322  -4.835  1.00 58.06 ? 3009 HOH A O   1 
HETATM 2793 O O   . HOH C 3 .   ? 14.400 0.851  -3.800  1.00 48.25 ? 3010 HOH A O   1 
HETATM 2794 O O   . HOH C 3 .   ? 11.903 1.912  -3.131  1.00 42.27 ? 3011 HOH A O   1 
HETATM 2795 O O   . HOH C 3 .   ? 18.188 41.450 17.018  1.00 44.00 ? 3012 HOH A O   1 
HETATM 2796 O O   . HOH C 3 .   ? -0.273 3.451  18.804  1.00 43.85 ? 3013 HOH A O   1 
HETATM 2797 O O   . HOH C 3 .   ? 11.766 -3.409 5.673   1.00 39.06 ? 3014 HOH A O   1 
HETATM 2798 O O   . HOH C 3 .   ? 16.332 -0.821 32.892  1.00 40.28 ? 3015 HOH A O   1 
HETATM 2799 O O   . HOH C 3 .   ? 35.086 5.606  30.246  1.00 36.46 ? 3016 HOH A O   1 
HETATM 2800 O O   . HOH C 3 .   ? 36.983 4.050  30.757  1.00 45.86 ? 3017 HOH A O   1 
HETATM 2801 O O   . HOH C 3 .   ? 51.472 31.355 7.206   1.00 48.50 ? 3018 HOH A O   1 
HETATM 2802 O O   . HOH C 3 .   ? 39.901 29.963 11.900  1.00 29.16 ? 3019 HOH A O   1 
HETATM 2803 O O   . HOH C 3 .   ? 10.299 27.440 24.625  1.00 44.71 ? 3020 HOH A O   1 
HETATM 2804 O O   . HOH C 3 .   ? 35.523 3.216  24.220  1.00 42.44 ? 3021 HOH A O   1 
HETATM 2805 O O   . HOH C 3 .   ? 38.839 -1.848 -15.408 1.00 37.84 ? 3022 HOH A O   1 
HETATM 2806 O O   . HOH C 3 .   ? 38.533 2.060  31.094  1.00 48.01 ? 3023 HOH A O   1 
HETATM 2807 O O   . HOH C 3 .   ? 33.045 2.498  29.667  1.00 53.14 ? 3024 HOH A O   1 
HETATM 2808 O O   . HOH C 3 .   ? 34.186 29.770 -6.817  1.00 52.75 ? 3025 HOH A O   1 
HETATM 2809 O O   . HOH C 3 .   ? 33.872 27.707 -8.214  1.00 47.39 ? 3026 HOH A O   1 
HETATM 2810 O O   . HOH C 3 .   ? 38.029 24.969 -2.225  1.00 44.89 ? 3027 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   VAL 2   2   2   VAL VAL A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   HIS 5   5   5   HIS HIS A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ALA 8   8   8   ALA ALA A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  GLU 20  20  20  GLU GLU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ASN 22  22  22  ASN ASN A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  CYS 26  26  26  CYS CYS A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  ILE 28  28  28  ILE ILE A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  CME 45  45  45  CME CYB A . n 
A 1 46  GLN 46  46  46  GLN GLN A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  ASN 49  49  49  ASN ASN A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  PHE 55  55  55  PHE PHE A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n